data_2PMV
# 
_entry.id   2PMV 
# 
_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   2PMV         
RCSB  RCSB042552   
WWPDB D_1000042552 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2PMV 
_pdbx_database_status.recvd_initial_deposition_date   2007-04-23 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Mathews, F.S.'     1 
'Gordon, M.M.'      2 
'Chen, Z.'          3 
'Rajashankar, K.R.' 4 
'Ealick, S.E.'      5 
'Alpers, D.H.'      6 
'Sukumar, N.'       7 
# 
_citation.id                        primary 
_citation.title                     'Crystal structure of human intrinsic factor: Cobalamin complex at 2.6-A resolution' 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            104 
_citation.page_first                17311 
_citation.page_last                 17316 
_citation.year                      2007 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   17954916 
_citation.pdbx_database_id_DOI      10.1073/pnas.0703228104 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Mathews, F.S.'     1 
primary 'Gordon, M.M.'      2 
primary 'Chen, Z.'          3 
primary 'Rajashankar, K.R.' 4 
primary 'Ealick, S.E.'      5 
primary 'Alpers, D.H.'      6 
primary 'Sukumar, N.'       7 
# 
_cell.entry_id           2PMV 
_cell.length_a           90.100 
_cell.length_b           67.300 
_cell.length_c           147.700 
_cell.angle_alpha        90.00 
_cell.angle_beta         96.80 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2PMV 
_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 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Gastric intrinsic factor' 43448.379 4   ? ? ? ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE     221.208   4   ? ? ? ? 
3 non-polymer syn COBALAMIN                  1330.356  2   ? ? ? ? 
4 water       nat water                      18.015    459 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Intrinsic factor, IF, INF' 
# 
_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       
;STQTQSSCSVPSAQEPLVNGIQVLMENSVTSSAYPNPSILIAMNLAGAYNLKAQKLLTYQLMSSDNNDLTIGHLGLTIMA
LTSSCRDPGDKVSILQRQMENWAPSSPNAEASAFYGPSLAILALCQKNSEATLPIAVRFAKTLLANSSPFNVDTGAMATL
ALTCMYNKIPVGSEEGYRSLFGQVLKDIVEKISMKIKDNGIIGDIYSTGLAMQALSVTPEPSKKEWNCKKTTDMILNEIK
QGKFHNPMSIAQILPSLKGKTYLDVPQVTCSPDHEVQPTLPSNPGPGPTSASNITVIYTINNQLRGVELLFNETINVSVK
SGSVLLVVLEEAQRKNPMFKFETTMTSWGLVVSSINNIAENVNHKTYWQFLSGVTPLNEGVADYIPFNHEHITANFTQY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;STQTQSSCSVPSAQEPLVNGIQVLMENSVTSSAYPNPSILIAMNLAGAYNLKAQKLLTYQLMSSDNNDLTIGHLGLTIMA
LTSSCRDPGDKVSILQRQMENWAPSSPNAEASAFYGPSLAILALCQKNSEATLPIAVRFAKTLLANSSPFNVDTGAMATL
ALTCMYNKIPVGSEEGYRSLFGQVLKDIVEKISMKIKDNGIIGDIYSTGLAMQALSVTPEPSKKEWNCKKTTDMILNEIK
QGKFHNPMSIAQILPSLKGKTYLDVPQVTCSPDHEVQPTLPSNPGPGPTSASNITVIYTINNQLRGVELLFNETINVSVK
SGSVLLVVLEEAQRKNPMFKFETTMTSWGLVVSSINNIAENVNHKTYWQFLSGVTPLNEGVADYIPFNHEHITANFTQY
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   THR n 
1 3   GLN n 
1 4   THR n 
1 5   GLN n 
1 6   SER n 
1 7   SER n 
1 8   CYS n 
1 9   SER n 
1 10  VAL n 
1 11  PRO n 
1 12  SER n 
1 13  ALA n 
1 14  GLN n 
1 15  GLU n 
1 16  PRO n 
1 17  LEU n 
1 18  VAL n 
1 19  ASN n 
1 20  GLY n 
1 21  ILE n 
1 22  GLN n 
1 23  VAL n 
1 24  LEU n 
1 25  MET n 
1 26  GLU n 
1 27  ASN n 
1 28  SER n 
1 29  VAL n 
1 30  THR n 
1 31  SER n 
1 32  SER n 
1 33  ALA n 
1 34  TYR n 
1 35  PRO n 
1 36  ASN n 
1 37  PRO n 
1 38  SER n 
1 39  ILE n 
1 40  LEU n 
1 41  ILE n 
1 42  ALA n 
1 43  MET n 
1 44  ASN n 
1 45  LEU n 
1 46  ALA n 
1 47  GLY n 
1 48  ALA n 
1 49  TYR n 
1 50  ASN n 
1 51  LEU n 
1 52  LYS n 
1 53  ALA n 
1 54  GLN n 
1 55  LYS n 
1 56  LEU n 
1 57  LEU n 
1 58  THR n 
1 59  TYR n 
1 60  GLN n 
1 61  LEU n 
1 62  MET n 
1 63  SER n 
1 64  SER n 
1 65  ASP n 
1 66  ASN n 
1 67  ASN n 
1 68  ASP n 
1 69  LEU n 
1 70  THR n 
1 71  ILE n 
1 72  GLY n 
1 73  HIS n 
1 74  LEU n 
1 75  GLY n 
1 76  LEU n 
1 77  THR n 
1 78  ILE n 
1 79  MET n 
1 80  ALA n 
1 81  LEU n 
1 82  THR n 
1 83  SER n 
1 84  SER n 
1 85  CYS n 
1 86  ARG n 
1 87  ASP n 
1 88  PRO n 
1 89  GLY n 
1 90  ASP n 
1 91  LYS n 
1 92  VAL n 
1 93  SER n 
1 94  ILE n 
1 95  LEU n 
1 96  GLN n 
1 97  ARG n 
1 98  GLN n 
1 99  MET n 
1 100 GLU n 
1 101 ASN n 
1 102 TRP n 
1 103 ALA n 
1 104 PRO n 
1 105 SER n 
1 106 SER n 
1 107 PRO n 
1 108 ASN n 
1 109 ALA n 
1 110 GLU n 
1 111 ALA n 
1 112 SER n 
1 113 ALA n 
1 114 PHE n 
1 115 TYR n 
1 116 GLY n 
1 117 PRO n 
1 118 SER n 
1 119 LEU n 
1 120 ALA n 
1 121 ILE n 
1 122 LEU n 
1 123 ALA n 
1 124 LEU n 
1 125 CYS n 
1 126 GLN n 
1 127 LYS n 
1 128 ASN n 
1 129 SER n 
1 130 GLU n 
1 131 ALA n 
1 132 THR n 
1 133 LEU n 
1 134 PRO n 
1 135 ILE n 
1 136 ALA n 
1 137 VAL n 
1 138 ARG n 
1 139 PHE n 
1 140 ALA n 
1 141 LYS n 
1 142 THR n 
1 143 LEU n 
1 144 LEU n 
1 145 ALA n 
1 146 ASN n 
1 147 SER n 
1 148 SER n 
1 149 PRO n 
1 150 PHE n 
1 151 ASN n 
1 152 VAL n 
1 153 ASP n 
1 154 THR n 
1 155 GLY n 
1 156 ALA n 
1 157 MET n 
1 158 ALA n 
1 159 THR n 
1 160 LEU n 
1 161 ALA n 
1 162 LEU n 
1 163 THR n 
1 164 CYS n 
1 165 MET n 
1 166 TYR n 
1 167 ASN n 
1 168 LYS n 
1 169 ILE n 
1 170 PRO n 
1 171 VAL n 
1 172 GLY n 
1 173 SER n 
1 174 GLU n 
1 175 GLU n 
1 176 GLY n 
1 177 TYR n 
1 178 ARG n 
1 179 SER n 
1 180 LEU n 
1 181 PHE n 
1 182 GLY n 
1 183 GLN n 
1 184 VAL n 
1 185 LEU n 
1 186 LYS n 
1 187 ASP n 
1 188 ILE n 
1 189 VAL n 
1 190 GLU n 
1 191 LYS n 
1 192 ILE n 
1 193 SER n 
1 194 MET n 
1 195 LYS n 
1 196 ILE n 
1 197 LYS n 
1 198 ASP n 
1 199 ASN n 
1 200 GLY n 
1 201 ILE n 
1 202 ILE n 
1 203 GLY n 
1 204 ASP n 
1 205 ILE n 
1 206 TYR n 
1 207 SER n 
1 208 THR n 
1 209 GLY n 
1 210 LEU n 
1 211 ALA n 
1 212 MET n 
1 213 GLN n 
1 214 ALA n 
1 215 LEU n 
1 216 SER n 
1 217 VAL n 
1 218 THR n 
1 219 PRO n 
1 220 GLU n 
1 221 PRO n 
1 222 SER n 
1 223 LYS n 
1 224 LYS n 
1 225 GLU n 
1 226 TRP n 
1 227 ASN n 
1 228 CYS n 
1 229 LYS n 
1 230 LYS n 
1 231 THR n 
1 232 THR n 
1 233 ASP n 
1 234 MET n 
1 235 ILE n 
1 236 LEU n 
1 237 ASN n 
1 238 GLU n 
1 239 ILE n 
1 240 LYS n 
1 241 GLN n 
1 242 GLY n 
1 243 LYS n 
1 244 PHE n 
1 245 HIS n 
1 246 ASN n 
1 247 PRO n 
1 248 MET n 
1 249 SER n 
1 250 ILE n 
1 251 ALA n 
1 252 GLN n 
1 253 ILE n 
1 254 LEU n 
1 255 PRO n 
1 256 SER n 
1 257 LEU n 
1 258 LYS n 
1 259 GLY n 
1 260 LYS n 
1 261 THR n 
1 262 TYR n 
1 263 LEU n 
1 264 ASP n 
1 265 VAL n 
1 266 PRO n 
1 267 GLN n 
1 268 VAL n 
1 269 THR n 
1 270 CYS n 
1 271 SER n 
1 272 PRO n 
1 273 ASP n 
1 274 HIS n 
1 275 GLU n 
1 276 VAL n 
1 277 GLN n 
1 278 PRO n 
1 279 THR n 
1 280 LEU n 
1 281 PRO n 
1 282 SER n 
1 283 ASN n 
1 284 PRO n 
1 285 GLY n 
1 286 PRO n 
1 287 GLY n 
1 288 PRO n 
1 289 THR n 
1 290 SER n 
1 291 ALA n 
1 292 SER n 
1 293 ASN n 
1 294 ILE n 
1 295 THR n 
1 296 VAL n 
1 297 ILE n 
1 298 TYR n 
1 299 THR n 
1 300 ILE n 
1 301 ASN n 
1 302 ASN n 
1 303 GLN n 
1 304 LEU n 
1 305 ARG n 
1 306 GLY n 
1 307 VAL n 
1 308 GLU n 
1 309 LEU n 
1 310 LEU n 
1 311 PHE n 
1 312 ASN n 
1 313 GLU n 
1 314 THR n 
1 315 ILE n 
1 316 ASN n 
1 317 VAL n 
1 318 SER n 
1 319 VAL n 
1 320 LYS n 
1 321 SER n 
1 322 GLY n 
1 323 SER n 
1 324 VAL n 
1 325 LEU n 
1 326 LEU n 
1 327 VAL n 
1 328 VAL n 
1 329 LEU n 
1 330 GLU n 
1 331 GLU n 
1 332 ALA n 
1 333 GLN n 
1 334 ARG n 
1 335 LYS n 
1 336 ASN n 
1 337 PRO n 
1 338 MET n 
1 339 PHE n 
1 340 LYS n 
1 341 PHE n 
1 342 GLU n 
1 343 THR n 
1 344 THR n 
1 345 MET n 
1 346 THR n 
1 347 SER n 
1 348 TRP n 
1 349 GLY n 
1 350 LEU n 
1 351 VAL n 
1 352 VAL n 
1 353 SER n 
1 354 SER n 
1 355 ILE n 
1 356 ASN n 
1 357 ASN n 
1 358 ILE n 
1 359 ALA n 
1 360 GLU n 
1 361 ASN n 
1 362 VAL n 
1 363 ASN n 
1 364 HIS n 
1 365 LYS n 
1 366 THR n 
1 367 TYR n 
1 368 TRP n 
1 369 GLN n 
1 370 PHE n 
1 371 LEU n 
1 372 SER n 
1 373 GLY n 
1 374 VAL n 
1 375 THR n 
1 376 PRO n 
1 377 LEU n 
1 378 ASN n 
1 379 GLU n 
1 380 GLY n 
1 381 VAL n 
1 382 ALA n 
1 383 ASP n 
1 384 TYR n 
1 385 ILE n 
1 386 PRO n 
1 387 PHE n 
1 388 ASN n 
1 389 HIS n 
1 390 GLU n 
1 391 HIS n 
1 392 ILE n 
1 393 THR n 
1 394 ALA n 
1 395 ASN n 
1 396 PHE n 
1 397 THR n 
1 398 GLN n 
1 399 TYR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Pichia pastoris' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4922 
_entity_src_gen.host_org_genus                     Pichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    IF_HUMAN 
_struct_ref.pdbx_db_accession          P27352 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;STQTQSSCSVPSAQEPLVNGIQVLMENSVTSSAYPNPSILIAMNLAGAYNLKAQKLLTYQLMSSDNNDLTIGQLGLTIMA
LTSSCRDPGDKVSILQRQMENWAPSSPNAEASAFYGPSLAILALCQKNSEATLPIAVRFAKTLLANSSPFNVDTGAMATL
ALTCMYNKIPVGSEEGYRSLFGQVLKDIVEKISMKIKDNGIIGDIYSTGLAMQALSVTPEPSKKEWNCKKTTDMILNEIK
QGKFHNPMSIAQILPSLKGKTYLDVPQVTCSPDHEVQPTLPSNPGPGPTSASNITVIYTINNQLRGVELLFNETINVSVK
SGSVLLVVLEEAQRKNPMFKFETTMTSWGLVVSSINNIAENVNHKTYWQFLSGVTPLNEGVADYIPFNHEHITANFTQY
;
_struct_ref.pdbx_align_begin           19 
_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 2PMV A 1 ? 399 ? P27352 19 ? 417 ? 1 399 
2 1 2PMV B 1 ? 399 ? P27352 19 ? 417 ? 1 399 
3 1 2PMV C 1 ? 399 ? P27352 19 ? 417 ? 1 399 
4 1 2PMV D 1 ? 399 ? P27352 19 ? 417 ? 1 399 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2PMV HIS A 73 ? UNP P27352 GLN 91 CONFLICT 73 1 
2 2PMV HIS B 73 ? UNP P27352 GLN 91 CONFLICT 73 2 
3 2PMV HIS C 73 ? UNP P27352 GLN 91 CONFLICT 73 3 
4 2PMV HIS D 73 ? UNP P27352 GLN 91 CONFLICT 73 4 
# 
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  
B12 non-polymer         . COBALAMIN              ? 'C62 H89 Co N13 O14 P 2' 1330.356 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'           121.158  
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'           146.144  
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'             147.129  
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'             75.067   
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1'         156.162  
HOH non-polymer         . WATER                  ? 'H2 O'                   18.015   
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'            131.173  
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'            131.173  
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1'         147.195  
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'          149.211  
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'            221.208  
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          2PMV 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.56 
_exptl_crystal.density_percent_sol   51.90 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            295 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.0 
_exptl_crystal_grow.pdbx_details    
'10% PEG20000, 100mM MES, 20mM CaCL2 and 9mM BaCL2, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_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 315' 
_diffrn_detector.pdbx_collection_date   ? 
_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   1.6059 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 8-BM' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   8-BM 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.6059 
# 
_reflns.entry_id                     2PMV 
_reflns.observed_criterion_sigma_F   -3 
_reflns.observed_criterion_sigma_I   -3 
_reflns.d_resolution_high            2.5 
_reflns.d_resolution_low             50 
_reflns.number_all                   61149 
_reflns.number_obs                   55707 
_reflns.percent_possible_obs         91.1 
_reflns.pdbx_Rmerge_I_obs            0.070 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.5 
_reflns.B_iso_Wilson_estimate        36.5 
_reflns.pdbx_redundancy              3.5 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.5 
_reflns_shell.d_res_low              2.6 
_reflns_shell.percent_possible_all   54.7 
_reflns_shell.Rmerge_I_obs           0.491 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.2 
_reflns_shell.pdbx_redundancy        3.2 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2PMV 
_refine.ls_number_reflns_obs                     50885 
_refine.ls_number_reflns_all                     54502 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               491016.14 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             37.53 
_refine.ls_d_res_high                            2.60 
_refine.ls_percent_reflns_obs                    93.4 
_refine.ls_R_factor_obs                          0.213 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.213 
_refine.ls_R_factor_R_free                       0.249 
_refine.ls_R_factor_R_free_error                 0.006 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.0 
_refine.ls_number_reflns_R_free                  1529 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               56.0 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        2PMV 
_refine_analyze.Luzzati_coordinate_error_obs    0.32 
_refine_analyze.Luzzati_sigma_a_obs             0.35 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.40 
_refine_analyze.Luzzati_sigma_a_free            0.43 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        9760 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         238 
_refine_hist.number_atoms_solvent             459 
_refine_hist.number_atoms_total               10457 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        37.53 
# 
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 
c_bond_d           0.013 ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        1.9   ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d 22.2  ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d 1.14  ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       2.60 
_refine_ls_shell.d_res_low                        2.76 
_refine_ls_shell.number_reflns_R_work             7090 
_refine_ls_shell.R_factor_R_work                  0.31 
_refine_ls_shell.percent_reflns_obs               81.8 
_refine_ls_shell.R_factor_R_free                  0.349 
_refine_ls_shell.R_factor_R_free_error            0.023 
_refine_ls_shell.percent_reflns_R_free            3.2 
_refine_ls_shell.number_reflns_R_free             238 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2PMV 
_struct.title                     'Crystal Structure of Human Intrinsic Factor- Cobalamin Complex at 2.6 A Resolution' 
_struct.pdbx_descriptor           'Gastric intrinsic factor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2PMV 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
_struct_keywords.text            'Cobalamin transport protein Alpha6-Alpha6 motif two domain protein, TRANSPORT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 2 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
# 
loop_
_struct_biol.id 
_struct_biol.details 
1 'The biological assembly is a monomer.' 
2 ?                                       
3 ?                                       
4 ?                                       
# 
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 14  ? ASN A 27  ? GLN A 14  ASN A 27  1 ? 14 
HELX_P HELX_P2  2  ASN A 36  ? GLY A 47  ? ASN A 36  GLY A 47  1 ? 12 
HELX_P HELX_P3  3  ASN A 50  ? SER A 63  ? ASN A 50  SER A 63  1 ? 14 
HELX_P HELX_P4  4  ASP A 65  ? LEU A 69  ? ASP A 65  LEU A 69  5 ? 5  
HELX_P HELX_P5  5  THR A 70  ? SER A 84  ? THR A 70  SER A 84  1 ? 15 
HELX_P HELX_P6  6  GLY A 89  ? ASN A 101 ? GLY A 89  ASN A 101 1 ? 13 
HELX_P HELX_P7  7  GLU A 110 ? ALA A 113 ? GLU A 110 ALA A 113 5 ? 4  
HELX_P HELX_P8  8  PHE A 114 ? ASN A 128 ? PHE A 114 ASN A 128 1 ? 15 
HELX_P HELX_P9  9  ASN A 128 ? ASN A 146 ? ASN A 128 ASN A 146 1 ? 19 
HELX_P HELX_P10 10 ASN A 151 ? ASN A 167 ? ASN A 151 ASN A 167 1 ? 17 
HELX_P HELX_P11 11 GLY A 176 ? SER A 193 ? GLY A 176 SER A 193 1 ? 18 
HELX_P HELX_P12 12 ASP A 204 ? THR A 218 ? ASP A 204 THR A 218 1 ? 15 
HELX_P HELX_P13 13 ASN A 227 ? LYS A 240 ? ASN A 227 LYS A 240 1 ? 14 
HELX_P HELX_P14 14 ASN A 246 ? LYS A 258 ? ASN A 246 LYS A 258 1 ? 13 
HELX_P HELX_P15 15 THR A 261 ? VAL A 268 ? THR A 261 VAL A 268 5 ? 8  
HELX_P HELX_P16 16 VAL A 324 ? LYS A 335 ? VAL A 324 LYS A 335 1 ? 12 
HELX_P HELX_P17 17 ASN A 361 ? HIS A 364 ? ASN A 361 HIS A 364 5 ? 4  
HELX_P HELX_P18 18 GLN B 14  ? SER B 28  ? GLN B 14  SER B 28  1 ? 15 
HELX_P HELX_P19 19 ASN B 36  ? GLY B 47  ? ASN B 36  GLY B 47  1 ? 12 
HELX_P HELX_P20 20 ASN B 50  ? MET B 62  ? ASN B 50  MET B 62  1 ? 13 
HELX_P HELX_P21 21 THR B 70  ? SER B 84  ? THR B 70  SER B 84  1 ? 15 
HELX_P HELX_P22 22 GLY B 89  ? ASN B 101 ? GLY B 89  ASN B 101 1 ? 13 
HELX_P HELX_P23 23 GLU B 110 ? ALA B 113 ? GLU B 110 ALA B 113 5 ? 4  
HELX_P HELX_P24 24 PHE B 114 ? ASN B 128 ? PHE B 114 ASN B 128 1 ? 15 
HELX_P HELX_P25 25 ASN B 128 ? ASN B 146 ? ASN B 128 ASN B 146 1 ? 19 
HELX_P HELX_P26 26 ASN B 151 ? ASN B 167 ? ASN B 151 ASN B 167 1 ? 17 
HELX_P HELX_P27 27 GLY B 176 ? SER B 193 ? GLY B 176 SER B 193 1 ? 18 
HELX_P HELX_P28 28 ASP B 204 ? TYR B 206 ? ASP B 204 TYR B 206 5 ? 3  
HELX_P HELX_P29 29 SER B 207 ? THR B 218 ? SER B 207 THR B 218 1 ? 12 
HELX_P HELX_P30 30 ASN B 227 ? GLN B 241 ? ASN B 227 GLN B 241 1 ? 15 
HELX_P HELX_P31 31 ASN B 246 ? GLN B 252 ? ASN B 246 GLN B 252 1 ? 7  
HELX_P HELX_P32 32 ILE B 253 ? LYS B 258 ? ILE B 253 LYS B 258 1 ? 6  
HELX_P HELX_P33 33 THR B 261 ? VAL B 268 ? THR B 261 VAL B 268 5 ? 8  
HELX_P HELX_P34 34 GLN C 14  ? ASN C 27  ? GLN C 14  ASN C 27  1 ? 14 
HELX_P HELX_P35 35 ASN C 36  ? GLY C 47  ? ASN C 36  GLY C 47  1 ? 12 
HELX_P HELX_P36 36 ASN C 50  ? SER C 63  ? ASN C 50  SER C 63  1 ? 14 
HELX_P HELX_P37 37 ASP C 65  ? LEU C 69  ? ASP C 65  LEU C 69  5 ? 5  
HELX_P HELX_P38 38 THR C 70  ? SER C 84  ? THR C 70  SER C 84  1 ? 15 
HELX_P HELX_P39 39 GLY C 89  ? GLU C 100 ? GLY C 89  GLU C 100 1 ? 12 
HELX_P HELX_P40 40 GLU C 110 ? ALA C 113 ? GLU C 110 ALA C 113 5 ? 4  
HELX_P HELX_P41 41 PHE C 114 ? ASN C 146 ? PHE C 114 ASN C 146 1 ? 33 
HELX_P HELX_P42 42 ASN C 151 ? ASN C 167 ? ASN C 151 ASN C 167 1 ? 17 
HELX_P HELX_P43 43 GLY C 176 ? SER C 193 ? GLY C 176 SER C 193 1 ? 18 
HELX_P HELX_P44 44 ASP C 204 ? THR C 218 ? ASP C 204 THR C 218 1 ? 15 
HELX_P HELX_P45 45 ASN C 227 ? GLN C 241 ? ASN C 227 GLN C 241 1 ? 15 
HELX_P HELX_P46 46 ASN C 246 ? LYS C 258 ? ASN C 246 LYS C 258 1 ? 13 
HELX_P HELX_P47 47 THR C 261 ? VAL C 268 ? THR C 261 VAL C 268 5 ? 8  
HELX_P HELX_P48 48 VAL C 324 ? LYS C 335 ? VAL C 324 LYS C 335 1 ? 12 
HELX_P HELX_P49 49 ASN C 361 ? HIS C 364 ? ASN C 361 HIS C 364 5 ? 4  
HELX_P HELX_P50 50 GLN D 14  ? SER D 28  ? GLN D 14  SER D 28  1 ? 15 
HELX_P HELX_P51 51 ASN D 36  ? GLY D 47  ? ASN D 36  GLY D 47  1 ? 12 
HELX_P HELX_P52 52 ASN D 50  ? MET D 62  ? ASN D 50  MET D 62  1 ? 13 
HELX_P HELX_P53 53 THR D 70  ? SER D 83  ? THR D 70  SER D 83  1 ? 14 
HELX_P HELX_P54 54 GLY D 89  ? ASN D 101 ? GLY D 89  ASN D 101 1 ? 13 
HELX_P HELX_P55 55 GLU D 110 ? ALA D 113 ? GLU D 110 ALA D 113 5 ? 4  
HELX_P HELX_P56 56 PHE D 114 ? ASN D 128 ? PHE D 114 ASN D 128 1 ? 15 
HELX_P HELX_P57 57 ASN D 128 ? ASN D 146 ? ASN D 128 ASN D 146 1 ? 19 
HELX_P HELX_P58 58 ASN D 151 ? ASN D 167 ? ASN D 151 ASN D 167 1 ? 17 
HELX_P HELX_P59 59 GLY D 176 ? SER D 193 ? GLY D 176 SER D 193 1 ? 18 
HELX_P HELX_P60 60 SER D 207 ? THR D 218 ? SER D 207 THR D 218 1 ? 12 
HELX_P HELX_P61 61 ASN D 227 ? GLN D 241 ? ASN D 227 GLN D 241 1 ? 15 
HELX_P HELX_P62 62 ASN D 246 ? GLN D 252 ? ASN D 246 GLN D 252 1 ? 7  
HELX_P HELX_P63 63 ILE D 253 ? LYS D 258 ? ILE D 253 LYS D 258 1 ? 6  
HELX_P HELX_P64 64 THR D 261 ? VAL D 268 ? THR D 261 VAL D 268 5 ? 8  
# 
_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 
disulf1  disulf ? ? A CYS 8   SG ? ? ? 1_555 A CYS 228 SG  ? ? A CYS 8   A CYS 228 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf2  disulf ? ? A CYS 85  SG ? ? ? 1_555 A CYS 270 SG  ? ? A CYS 85  A CYS 270 1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf3  disulf ? ? A CYS 125 SG ? ? ? 1_555 A CYS 164 SG  ? ? A CYS 125 A CYS 164 1_555 ? ? ? ? ? ? ? 2.077 ? 
disulf4  disulf ? ? B CYS 8   SG ? ? ? 1_555 B CYS 228 SG  ? ? B CYS 8   B CYS 228 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf5  disulf ? ? B CYS 85  SG ? ? ? 1_555 B CYS 270 SG  ? ? B CYS 85  B CYS 270 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf6  disulf ? ? B CYS 125 SG ? ? ? 1_555 B CYS 164 SG  ? ? B CYS 125 B CYS 164 1_555 ? ? ? ? ? ? ? 2.081 ? 
disulf7  disulf ? ? C CYS 8   SG ? ? ? 1_555 C CYS 228 SG  ? ? C CYS 8   C CYS 228 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf8  disulf ? ? C CYS 85  SG ? ? ? 1_555 C CYS 270 SG  ? ? C CYS 85  C CYS 270 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf9  disulf ? ? C CYS 125 SG ? ? ? 1_555 C CYS 164 SG  ? ? C CYS 125 C CYS 164 1_555 ? ? ? ? ? ? ? 2.073 ? 
disulf10 disulf ? ? D CYS 8   SG ? ? ? 1_555 D CYS 228 SG  ? ? D CYS 8   D CYS 228 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf11 disulf ? ? D CYS 85  SG ? ? ? 1_555 D CYS 270 SG  ? ? D CYS 85  D CYS 270 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf12 disulf ? ? D CYS 125 SG ? ? ? 1_555 D CYS 164 SG  ? ? D CYS 125 D CYS 164 1_555 ? ? ? ? ? ? ? 2.093 ? 
covale1  covale ? ? H NAG .   C1 ? ? ? 1_555 C ASN 395 ND2 ? ? C NAG 901 C ASN 395 1_555 ? ? ? ? ? ? ? 1.372 ? 
covale2  covale ? ? E NAG .   C1 ? ? ? 1_555 A ASN 395 ND2 ? ? A NAG 901 A ASN 395 1_555 ? ? ? ? ? ? ? 1.372 ? 
covale3  covale ? ? H NAG .   O4 ? ? ? 1_555 I NAG .   C1  ? ? C NAG 901 C NAG 902 1_555 ? ? ? ? ? ? ? 1.491 ? 
covale4  covale ? ? E NAG .   O4 ? ? ? 1_555 F NAG .   C1  ? ? A NAG 901 A NAG 902 1_555 ? ? ? ? ? ? ? 1.492 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 3 ? 
B ? 5 ? 
C ? 2 ? 
D ? 3 ? 
E ? 5 ? 
F ? 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 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? parallel      
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
C 1 2 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? parallel      
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
F 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 
A 1 PHE A 311 ? ASN A 312 ? PHE A 311 ASN A 312 
A 2 ILE A 294 ? ASN A 301 ? ILE A 294 ASN A 301 
A 3 ILE A 315 ? SER A 318 ? ILE A 315 SER A 318 
B 1 PHE A 311 ? ASN A 312 ? PHE A 311 ASN A 312 
B 2 ILE A 294 ? ASN A 301 ? ILE A 294 ASN A 301 
B 3 HIS A 391 ? GLN A 398 ? HIS A 391 GLN A 398 
B 4 THR A 366 ? SER A 372 ? THR A 366 SER A 372 
B 5 THR A 375 ? PRO A 376 ? THR A 375 PRO A 376 
C 1 PHE A 341 ? THR A 346 ? PHE A 341 THR A 346 
C 2 GLY A 349 ? ILE A 355 ? GLY A 349 ILE A 355 
D 1 PHE C 311 ? ASN C 312 ? PHE C 311 ASN C 312 
D 2 ILE C 294 ? ASN C 301 ? ILE C 294 ASN C 301 
D 3 ILE C 315 ? SER C 318 ? ILE C 315 SER C 318 
E 1 PHE C 311 ? ASN C 312 ? PHE C 311 ASN C 312 
E 2 ILE C 294 ? ASN C 301 ? ILE C 294 ASN C 301 
E 3 HIS C 391 ? GLN C 398 ? HIS C 391 GLN C 398 
E 4 THR C 366 ? SER C 372 ? THR C 366 SER C 372 
E 5 THR C 375 ? PRO C 376 ? THR C 375 PRO C 376 
F 1 PHE C 341 ? THR C 346 ? PHE C 341 THR C 346 
F 2 GLY C 349 ? ILE C 355 ? GLY C 349 ILE C 355 
# 
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 
A 1 2 O ASN A 312 ? O ASN A 312 N ILE A 300 ? N ILE A 300 
A 2 3 N VAL A 296 ? N VAL A 296 O ASN A 316 ? O ASN A 316 
B 1 2 O ASN A 312 ? O ASN A 312 N ILE A 300 ? N ILE A 300 
B 2 3 N ILE A 297 ? N ILE A 297 O ILE A 392 ? O ILE A 392 
B 3 4 O ASN A 395 ? O ASN A 395 N GLN A 369 ? N GLN A 369 
B 4 5 N SER A 372 ? N SER A 372 O THR A 375 ? O THR A 375 
C 1 2 N THR A 344 ? N THR A 344 O VAL A 351 ? O VAL A 351 
D 1 2 O ASN C 312 ? O ASN C 312 N ILE C 300 ? N ILE C 300 
D 2 3 N VAL C 296 ? N VAL C 296 O ASN C 316 ? O ASN C 316 
E 1 2 O ASN C 312 ? O ASN C 312 N ILE C 300 ? N ILE C 300 
E 2 3 N ILE C 297 ? N ILE C 297 O ILE C 392 ? O ILE C 392 
E 3 4 O ASN C 395 ? O ASN C 395 N GLN C 369 ? N GLN C 369 
E 4 5 N SER C 372 ? N SER C 372 O THR C 375 ? O THR C 375 
F 1 2 N THR C 344 ? N THR C 344 O VAL C 351 ? O VAL C 351 
# 
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 NAG A 901'  
AC2 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG A 902'  
AC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG C 901'  
AC4 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG C 902'  
AC5 Software ? ? ? ? 30 'BINDING SITE FOR RESIDUE B12 A 1001' 
AC6 Software ? ? ? ? 35 'BINDING SITE FOR RESIDUE B12 C 1002' 
# 
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  GLN A 303 ? GLN A 303  . ? 1_555 ? 
2  AC1 4  ASN A 395 ? ASN A 395  . ? 1_555 ? 
3  AC1 4  THR A 397 ? THR A 397  . ? 1_555 ? 
4  AC1 4  NAG F .   ? NAG A 902  . ? 1_555 ? 
5  AC2 1  NAG E .   ? NAG A 901  . ? 1_555 ? 
6  AC3 5  GLN C 303 ? GLN C 303  . ? 1_555 ? 
7  AC3 5  ASN C 395 ? ASN C 395  . ? 1_555 ? 
8  AC3 5  THR C 397 ? THR C 397  . ? 1_555 ? 
9  AC3 5  NAG I .   ? NAG C 902  . ? 1_555 ? 
10 AC3 5  HOH M .   ? HOH C 1216 . ? 1_555 ? 
11 AC4 1  NAG H .   ? NAG C 901  . ? 1_555 ? 
12 AC5 30 THR A 70  ? THR A 70   . ? 1_555 ? 
13 AC5 30 GLY A 72  ? GLY A 72   . ? 1_555 ? 
14 AC5 30 HIS A 73  ? HIS A 73   . ? 1_555 ? 
15 AC5 30 TYR A 115 ? TYR A 115  . ? 1_555 ? 
16 AC5 30 ASP A 153 ? ASP A 153  . ? 1_555 ? 
17 AC5 30 ASP A 204 ? ASP A 204  . ? 1_555 ? 
18 AC5 30 TYR A 206 ? TYR A 206  . ? 1_555 ? 
19 AC5 30 SER A 207 ? SER A 207  . ? 1_555 ? 
20 AC5 30 GLN A 252 ? GLN A 252  . ? 1_555 ? 
21 AC5 30 THR A 346 ? THR A 346  . ? 1_555 ? 
22 AC5 30 SER A 347 ? SER A 347  . ? 1_555 ? 
23 AC5 30 TRP A 348 ? TRP A 348  . ? 1_555 ? 
24 AC5 30 GLY A 349 ? GLY A 349  . ? 1_555 ? 
25 AC5 30 LEU A 350 ? LEU A 350  . ? 1_555 ? 
26 AC5 30 VAL A 351 ? VAL A 351  . ? 1_555 ? 
27 AC5 30 VAL A 352 ? VAL A 352  . ? 1_555 ? 
28 AC5 30 TYR A 367 ? TYR A 367  . ? 1_555 ? 
29 AC5 30 TRP A 368 ? TRP A 368  . ? 1_555 ? 
30 AC5 30 GLN A 369 ? GLN A 369  . ? 1_555 ? 
31 AC5 30 PHE A 370 ? PHE A 370  . ? 1_555 ? 
32 AC5 30 LEU A 377 ? LEU A 377  . ? 1_555 ? 
33 AC5 30 ASN A 378 ? ASN A 378  . ? 1_555 ? 
34 AC5 30 GLU A 379 ? GLU A 379  . ? 1_555 ? 
35 AC5 30 GLY A 380 ? GLY A 380  . ? 1_555 ? 
36 AC5 30 TYR A 399 ? TYR A 399  . ? 1_555 ? 
37 AC5 30 HOH K .   ? HOH A 1020 . ? 1_555 ? 
38 AC5 30 HOH K .   ? HOH A 1032 . ? 1_555 ? 
39 AC5 30 HOH K .   ? HOH A 1033 . ? 1_555 ? 
40 AC5 30 HOH K .   ? HOH A 1035 . ? 1_555 ? 
41 AC5 30 HOH K .   ? HOH A 1079 . ? 1_555 ? 
42 AC6 35 THR C 70  ? THR C 70   . ? 1_555 ? 
43 AC6 35 GLY C 72  ? GLY C 72   . ? 1_555 ? 
44 AC6 35 HIS C 73  ? HIS C 73   . ? 1_555 ? 
45 AC6 35 TYR C 115 ? TYR C 115  . ? 1_555 ? 
46 AC6 35 ASP C 153 ? ASP C 153  . ? 1_555 ? 
47 AC6 35 ASP C 204 ? ASP C 204  . ? 1_555 ? 
48 AC6 35 TYR C 206 ? TYR C 206  . ? 1_555 ? 
49 AC6 35 SER C 207 ? SER C 207  . ? 1_555 ? 
50 AC6 35 LEU C 210 ? LEU C 210  . ? 1_555 ? 
51 AC6 35 GLN C 252 ? GLN C 252  . ? 1_555 ? 
52 AC6 35 THR C 346 ? THR C 346  . ? 1_555 ? 
53 AC6 35 SER C 347 ? SER C 347  . ? 1_555 ? 
54 AC6 35 TRP C 348 ? TRP C 348  . ? 1_555 ? 
55 AC6 35 GLY C 349 ? GLY C 349  . ? 1_555 ? 
56 AC6 35 LEU C 350 ? LEU C 350  . ? 1_555 ? 
57 AC6 35 VAL C 351 ? VAL C 351  . ? 1_555 ? 
58 AC6 35 VAL C 352 ? VAL C 352  . ? 1_555 ? 
59 AC6 35 VAL C 362 ? VAL C 362  . ? 1_555 ? 
60 AC6 35 TYR C 367 ? TYR C 367  . ? 1_555 ? 
61 AC6 35 TRP C 368 ? TRP C 368  . ? 1_555 ? 
62 AC6 35 GLN C 369 ? GLN C 369  . ? 1_555 ? 
63 AC6 35 PHE C 370 ? PHE C 370  . ? 1_555 ? 
64 AC6 35 PRO C 376 ? PRO C 376  . ? 1_555 ? 
65 AC6 35 LEU C 377 ? LEU C 377  . ? 1_555 ? 
66 AC6 35 ASN C 378 ? ASN C 378  . ? 1_555 ? 
67 AC6 35 GLU C 379 ? GLU C 379  . ? 1_555 ? 
68 AC6 35 GLY C 380 ? GLY C 380  . ? 1_555 ? 
69 AC6 35 TYR C 399 ? TYR C 399  . ? 1_555 ? 
70 AC6 35 HOH M .   ? HOH C 1099 . ? 1_555 ? 
71 AC6 35 HOH M .   ? HOH C 1109 . ? 1_555 ? 
72 AC6 35 HOH M .   ? HOH C 1113 . ? 1_555 ? 
73 AC6 35 HOH M .   ? HOH C 1115 . ? 1_555 ? 
74 AC6 35 HOH M .   ? HOH C 1122 . ? 1_555 ? 
75 AC6 35 HOH M .   ? HOH C 1166 . ? 1_555 ? 
76 AC6 35 HOH M .   ? HOH C 1175 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2PMV 
_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                    2PMV 
_atom_sites.fract_transf_matrix[1][1]   0.011099 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001323 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014859 
_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]   0.006818 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CO 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . SER A 1 7   ? -3.980  47.944  106.385 1.00 95.45 ? 7    SER A N   1 
ATOM   2     C  CA  . SER A 1 7   ? -4.068  47.707  104.908 1.00 97.42 ? 7    SER A CA  1 
ATOM   3     C  C   . SER A 1 7   ? -3.266  48.767  104.157 1.00 96.80 ? 7    SER A C   1 
ATOM   4     O  O   . SER A 1 7   ? -2.965  48.624  102.965 1.00 96.86 ? 7    SER A O   1 
ATOM   5     C  CB  . SER A 1 7   ? -5.535  47.772  104.431 1.00 99.44 ? 7    SER A CB  1 
ATOM   6     O  OG  . SER A 1 7   ? -6.323  46.690  104.909 1.00 99.45 ? 7    SER A OG  1 
ATOM   7     N  N   . CYS A 1 8   ? -2.926  49.834  104.868 1.00 94.59 ? 8    CYS A N   1 
ATOM   8     C  CA  . CYS A 1 8   ? -2.203  50.944  104.268 1.00 90.70 ? 8    CYS A CA  1 
ATOM   9     C  C   . CYS A 1 8   ? -1.432  51.724  105.313 1.00 86.91 ? 8    CYS A C   1 
ATOM   10    O  O   . CYS A 1 8   ? -1.574  52.947  105.431 1.00 85.07 ? 8    CYS A O   1 
ATOM   11    C  CB  . CYS A 1 8   ? -3.199  51.858  103.571 1.00 91.42 ? 8    CYS A CB  1 
ATOM   12    S  SG  . CYS A 1 8   ? -4.787  51.939  104.471 1.00 94.97 ? 8    CYS A SG  1 
ATOM   13    N  N   . SER A 1 9   ? -0.626  51.000  106.078 1.00 82.84 ? 9    SER A N   1 
ATOM   14    C  CA  . SER A 1 9   ? 0.192   51.614  107.108 1.00 78.96 ? 9    SER A CA  1 
ATOM   15    C  C   . SER A 1 9   ? 1.349   52.288  106.366 1.00 75.22 ? 9    SER A C   1 
ATOM   16    O  O   . SER A 1 9   ? 1.496   52.111  105.152 1.00 72.17 ? 9    SER A O   1 
ATOM   17    C  CB  . SER A 1 9   ? 0.724   50.533  108.059 1.00 78.64 ? 9    SER A CB  1 
ATOM   18    O  OG  . SER A 1 9   ? -0.273  49.562  108.335 1.00 78.05 ? 9    SER A OG  1 
ATOM   19    N  N   . VAL A 1 10  ? 2.157   53.067  107.079 1.00 71.19 ? 10   VAL A N   1 
ATOM   20    C  CA  . VAL A 1 10  ? 3.288   53.699  106.434 1.00 68.92 ? 10   VAL A CA  1 
ATOM   21    C  C   . VAL A 1 10  ? 4.397   52.656  106.370 1.00 67.04 ? 10   VAL A C   1 
ATOM   22    O  O   . VAL A 1 10  ? 4.746   52.046  107.381 1.00 69.29 ? 10   VAL A O   1 
ATOM   23    C  CB  . VAL A 1 10  ? 3.773   54.924  107.205 1.00 67.89 ? 10   VAL A CB  1 
ATOM   24    C  CG1 . VAL A 1 10  ? 4.959   55.539  106.495 1.00 68.45 ? 10   VAL A CG1 1 
ATOM   25    C  CG2 . VAL A 1 10  ? 2.653   55.938  107.304 1.00 70.26 ? 10   VAL A CG2 1 
ATOM   26    N  N   . PRO A 1 11  ? 4.942   52.422  105.170 1.00 63.38 ? 11   PRO A N   1 
ATOM   27    C  CA  . PRO A 1 11  ? 6.010   51.455  104.924 1.00 62.73 ? 11   PRO A CA  1 
ATOM   28    C  C   . PRO A 1 11  ? 7.216   51.702  105.821 1.00 63.66 ? 11   PRO A C   1 
ATOM   29    O  O   . PRO A 1 11  ? 7.783   52.807  105.837 1.00 62.41 ? 11   PRO A O   1 
ATOM   30    C  CB  . PRO A 1 11  ? 6.349   51.681  103.451 1.00 62.47 ? 11   PRO A CB  1 
ATOM   31    C  CG  . PRO A 1 11  ? 5.083   52.218  102.879 1.00 62.44 ? 11   PRO A CG  1 
ATOM   32    C  CD  . PRO A 1 11  ? 4.620   53.165  103.943 1.00 63.24 ? 11   PRO A CD  1 
ATOM   33    N  N   . SER A 1 12  ? 7.595   50.677  106.577 1.00 64.24 ? 12   SER A N   1 
ATOM   34    C  CA  . SER A 1 12  ? 8.751   50.778  107.458 1.00 67.99 ? 12   SER A CA  1 
ATOM   35    C  C   . SER A 1 12  ? 9.926   50.938  106.529 1.00 66.64 ? 12   SER A C   1 
ATOM   36    O  O   . SER A 1 12  ? 10.525  49.961  106.103 1.00 71.64 ? 12   SER A O   1 
ATOM   37    C  CB  . SER A 1 12  ? 8.911   49.500  108.293 1.00 72.31 ? 12   SER A CB  1 
ATOM   38    O  OG  . SER A 1 12  ? 7.837   49.352  109.226 1.00 78.98 ? 12   SER A OG  1 
ATOM   39    N  N   . ALA A 1 13  ? 10.236  52.178  106.200 1.00 63.29 ? 13   ALA A N   1 
ATOM   40    C  CA  . ALA A 1 13  ? 11.315  52.492  105.281 1.00 60.40 ? 13   ALA A CA  1 
ATOM   41    C  C   . ALA A 1 13  ? 11.083  53.960  105.063 1.00 59.12 ? 13   ALA A C   1 
ATOM   42    O  O   . ALA A 1 13  ? 11.986  54.716  104.718 1.00 59.10 ? 13   ALA A O   1 
ATOM   43    C  CB  . ALA A 1 13  ? 11.141  51.732  103.981 1.00 58.43 ? 13   ALA A CB  1 
ATOM   44    N  N   . GLN A 1 14  ? 9.837   54.348  105.299 1.00 56.97 ? 14   GLN A N   1 
ATOM   45    C  CA  . GLN A 1 14  ? 9.420   55.729  105.180 1.00 56.65 ? 14   GLN A CA  1 
ATOM   46    C  C   . GLN A 1 14  ? 9.191   56.254  106.601 1.00 52.36 ? 14   GLN A C   1 
ATOM   47    O  O   . GLN A 1 14  ? 8.982   57.444  106.832 1.00 49.40 ? 14   GLN A O   1 
ATOM   48    C  CB  . GLN A 1 14  ? 8.136   55.805  104.348 1.00 62.31 ? 14   GLN A CB  1 
ATOM   49    C  CG  . GLN A 1 14  ? 8.307   55.412  102.883 1.00 67.03 ? 14   GLN A CG  1 
ATOM   50    C  CD  . GLN A 1 14  ? 9.024   56.482  102.071 1.00 70.89 ? 14   GLN A CD  1 
ATOM   51    O  OE1 . GLN A 1 14  ? 8.704   56.702  100.903 1.00 75.88 ? 14   GLN A OE1 1 
ATOM   52    N  NE2 . GLN A 1 14  ? 9.996   57.149  102.681 1.00 69.60 ? 14   GLN A NE2 1 
ATOM   53    N  N   . GLU A 1 15  ? 9.238   55.348  107.566 1.00 50.28 ? 15   GLU A N   1 
ATOM   54    C  CA  . GLU A 1 15  ? 9.042   55.744  108.949 1.00 48.78 ? 15   GLU A CA  1 
ATOM   55    C  C   . GLU A 1 15  ? 9.971   56.860  109.402 1.00 46.25 ? 15   GLU A C   1 
ATOM   56    O  O   . GLU A 1 15  ? 9.554   57.761  110.131 1.00 46.02 ? 15   GLU A O   1 
ATOM   57    C  CB  . GLU A 1 15  ? 9.167   54.538  109.864 1.00 51.00 ? 15   GLU A CB  1 
ATOM   58    C  CG  . GLU A 1 15  ? 7.875   53.750  109.910 1.00 55.24 ? 15   GLU A CG  1 
ATOM   59    C  CD  . GLU A 1 15  ? 7.883   52.641  110.945 1.00 60.81 ? 15   GLU A CD  1 
ATOM   60    O  OE1 . GLU A 1 15  ? 8.387   52.878  112.068 1.00 65.04 ? 15   GLU A OE1 1 
ATOM   61    O  OE2 . GLU A 1 15  ? 7.365   51.540  110.642 1.00 61.80 ? 15   GLU A OE2 1 
ATOM   62    N  N   . PRO A 1 16  ? 11.247  56.812  108.999 1.00 43.87 ? 16   PRO A N   1 
ATOM   63    C  CA  . PRO A 1 16  ? 12.149  57.891  109.417 1.00 43.70 ? 16   PRO A CA  1 
ATOM   64    C  C   . PRO A 1 16  ? 11.542  59.245  109.046 1.00 44.75 ? 16   PRO A C   1 
ATOM   65    O  O   . PRO A 1 16  ? 11.653  60.203  109.795 1.00 45.39 ? 16   PRO A O   1 
ATOM   66    C  CB  . PRO A 1 16  ? 13.436  57.598  108.632 1.00 41.73 ? 16   PRO A CB  1 
ATOM   67    C  CG  . PRO A 1 16  ? 13.432  56.105  108.543 1.00 40.95 ? 16   PRO A CG  1 
ATOM   68    C  CD  . PRO A 1 16  ? 11.972  55.776  108.235 1.00 44.52 ? 16   PRO A CD  1 
ATOM   69    N  N   . LEU A 1 17  ? 10.900  59.303  107.881 1.00 46.59 ? 17   LEU A N   1 
ATOM   70    C  CA  . LEU A 1 17  ? 10.272  60.522  107.386 1.00 47.75 ? 17   LEU A CA  1 
ATOM   71    C  C   . LEU A 1 17  ? 9.199   60.950  108.380 1.00 44.14 ? 17   LEU A C   1 
ATOM   72    O  O   . LEU A 1 17  ? 9.155   62.091  108.828 1.00 45.18 ? 17   LEU A O   1 
ATOM   73    C  CB  . LEU A 1 17  ? 9.654   60.239  106.012 1.00 52.32 ? 17   LEU A CB  1 
ATOM   74    C  CG  . LEU A 1 17  ? 9.451   61.349  104.990 1.00 56.53 ? 17   LEU A CG  1 
ATOM   75    C  CD1 . LEU A 1 17  ? 10.544  62.404  105.110 1.00 54.70 ? 17   LEU A CD1 1 
ATOM   76    C  CD2 . LEU A 1 17  ? 9.432   60.682  103.600 1.00 57.07 ? 17   LEU A CD2 1 
ATOM   77    N  N   . VAL A 1 18  ? 8.333   60.027  108.742 1.00 40.59 ? 18   VAL A N   1 
ATOM   78    C  CA  . VAL A 1 18  ? 7.283   60.390  109.677 1.00 39.68 ? 18   VAL A CA  1 
ATOM   79    C  C   . VAL A 1 18  ? 7.906   60.852  110.985 1.00 37.15 ? 18   VAL A C   1 
ATOM   80    O  O   . VAL A 1 18  ? 7.509   61.886  111.544 1.00 36.48 ? 18   VAL A O   1 
ATOM   81    C  CB  . VAL A 1 18  ? 6.330   59.207  109.928 1.00 38.11 ? 18   VAL A CB  1 
ATOM   82    C  CG1 . VAL A 1 18  ? 5.201   59.650  110.793 1.00 31.58 ? 18   VAL A CG1 1 
ATOM   83    C  CG2 . VAL A 1 18  ? 5.820   58.642  108.581 1.00 38.20 ? 18   VAL A CG2 1 
ATOM   84    N  N   . ASN A 1 19  ? 8.887   60.099  111.471 1.00 35.60 ? 19   ASN A N   1 
ATOM   85    C  CA  . ASN A 1 19  ? 9.538   60.463  112.720 1.00 38.02 ? 19   ASN A CA  1 
ATOM   86    C  C   . ASN A 1 19  ? 10.043  61.900  112.675 1.00 39.91 ? 19   ASN A C   1 
ATOM   87    O  O   . ASN A 1 19  ? 9.870   62.662  113.648 1.00 38.28 ? 19   ASN A O   1 
ATOM   88    C  CB  . ASN A 1 19  ? 10.719  59.556  113.013 1.00 43.61 ? 19   ASN A CB  1 
ATOM   89    C  CG  . ASN A 1 19  ? 10.333  58.094  113.177 1.00 46.04 ? 19   ASN A CG  1 
ATOM   90    O  OD1 . ASN A 1 19  ? 9.215   57.752  113.598 1.00 42.83 ? 19   ASN A OD1 1 
ATOM   91    N  ND2 . ASN A 1 19  ? 11.292  57.211  112.864 1.00 51.96 ? 19   ASN A ND2 1 
ATOM   92    N  N   . GLY A 1 20  ? 10.669  62.262  111.544 1.00 41.79 ? 20   GLY A N   1 
ATOM   93    C  CA  . GLY A 1 20  ? 11.197  63.608  111.361 1.00 38.53 ? 20   GLY A CA  1 
ATOM   94    C  C   . GLY A 1 20  ? 10.157  64.707  111.542 1.00 39.63 ? 20   GLY A C   1 
ATOM   95    O  O   . GLY A 1 20  ? 10.371  65.646  112.323 1.00 38.08 ? 20   GLY A O   1 
ATOM   96    N  N   . ILE A 1 21  ? 9.026   64.613  110.839 1.00 38.94 ? 21   ILE A N   1 
ATOM   97    C  CA  . ILE A 1 21  ? 8.022   65.665  110.986 1.00 38.88 ? 21   ILE A CA  1 
ATOM   98    C  C   . ILE A 1 21  ? 7.463   65.689  112.389 1.00 35.40 ? 21   ILE A C   1 
ATOM   99    O  O   . ILE A 1 21  ? 7.164   66.756  112.905 1.00 35.90 ? 21   ILE A O   1 
ATOM   100   C  CB  . ILE A 1 21  ? 6.898   65.554  109.926 1.00 39.40 ? 21   ILE A CB  1 
ATOM   101   C  CG1 . ILE A 1 21  ? 6.098   64.248  110.061 1.00 41.96 ? 21   ILE A CG1 1 
ATOM   102   C  CG2 . ILE A 1 21  ? 7.544   65.614  108.561 1.00 39.37 ? 21   ILE A CG2 1 
ATOM   103   C  CD1 . ILE A 1 21  ? 5.018   64.102  108.972 1.00 39.10 ? 21   ILE A CD1 1 
ATOM   104   N  N   . GLN A 1 22  ? 7.349   64.520  113.020 1.00 34.38 ? 22   GLN A N   1 
ATOM   105   C  CA  . GLN A 1 22  ? 6.846   64.479  114.387 1.00 31.68 ? 22   GLN A CA  1 
ATOM   106   C  C   . GLN A 1 22  ? 7.743   65.363  115.240 1.00 31.10 ? 22   GLN A C   1 
ATOM   107   O  O   . GLN A 1 22  ? 7.256   66.178  116.015 1.00 28.56 ? 22   GLN A O   1 
ATOM   108   C  CB  . GLN A 1 22  ? 6.859   63.062  114.965 1.00 29.03 ? 22   GLN A CB  1 
ATOM   109   C  CG  . GLN A 1 22  ? 6.228   63.071  116.351 1.00 32.80 ? 22   GLN A CG  1 
ATOM   110   C  CD  . GLN A 1 22  ? 6.102   61.699  116.989 1.00 37.23 ? 22   GLN A CD  1 
ATOM   111   O  OE1 . GLN A 1 22  ? 5.979   60.684  116.281 1.00 36.41 ? 22   GLN A OE1 1 
ATOM   112   N  NE2 . GLN A 1 22  ? 6.109   61.655  118.345 1.00 36.13 ? 22   GLN A NE2 1 
ATOM   113   N  N   . VAL A 1 23  ? 9.059   65.182  115.090 1.00 31.53 ? 23   VAL A N   1 
ATOM   114   C  CA  . VAL A 1 23  ? 10.019  65.979  115.834 1.00 32.20 ? 23   VAL A CA  1 
ATOM   115   C  C   . VAL A 1 23  ? 9.881   67.425  115.433 1.00 34.03 ? 23   VAL A C   1 
ATOM   116   O  O   . VAL A 1 23  ? 9.877   68.276  116.308 1.00 34.55 ? 23   VAL A O   1 
ATOM   117   C  CB  . VAL A 1 23  ? 11.475  65.511  115.589 1.00 36.29 ? 23   VAL A CB  1 
ATOM   118   C  CG1 . VAL A 1 23  ? 12.480  66.532  116.157 1.00 29.33 ? 23   VAL A CG1 1 
ATOM   119   C  CG2 . VAL A 1 23  ? 11.677  64.133  116.222 1.00 31.84 ? 23   VAL A CG2 1 
ATOM   120   N  N   . LEU A 1 24  ? 9.745   67.717  114.134 1.00 33.81 ? 24   LEU A N   1 
ATOM   121   C  CA  . LEU A 1 24  ? 9.589   69.120  113.724 1.00 37.31 ? 24   LEU A CA  1 
ATOM   122   C  C   . LEU A 1 24  ? 8.381   69.732  114.470 1.00 40.13 ? 24   LEU A C   1 
ATOM   123   O  O   . LEU A 1 24  ? 8.461   70.835  115.035 1.00 41.85 ? 24   LEU A O   1 
ATOM   124   C  CB  . LEU A 1 24  ? 9.357   69.238  112.203 1.00 40.51 ? 24   LEU A CB  1 
ATOM   125   C  CG  . LEU A 1 24  ? 9.995   70.372  111.386 1.00 38.64 ? 24   LEU A CG  1 
ATOM   126   C  CD1 . LEU A 1 24  ? 9.053   70.744  110.259 1.00 38.61 ? 24   LEU A CD1 1 
ATOM   127   C  CD2 . LEU A 1 24  ? 10.285  71.560  112.232 1.00 40.02 ? 24   LEU A CD2 1 
ATOM   128   N  N   . MET A 1 25  ? 7.268   69.003  114.488 1.00 37.89 ? 25   MET A N   1 
ATOM   129   C  CA  . MET A 1 25  ? 6.063   69.486  115.135 1.00 37.15 ? 25   MET A CA  1 
ATOM   130   C  C   . MET A 1 25  ? 6.186   69.668  116.654 1.00 38.41 ? 25   MET A C   1 
ATOM   131   O  O   . MET A 1 25  ? 5.706   70.676  117.209 1.00 37.15 ? 25   MET A O   1 
ATOM   132   C  CB  . MET A 1 25  ? 4.892   68.546  114.817 1.00 39.36 ? 25   MET A CB  1 
ATOM   133   C  CG  . MET A 1 25  ? 3.590   68.897  115.542 1.00 35.84 ? 25   MET A CG  1 
ATOM   134   S  SD  . MET A 1 25  ? 2.437   67.522  115.516 1.00 40.11 ? 25   MET A SD  1 
ATOM   135   C  CE  . MET A 1 25  ? 3.073   66.382  116.794 1.00 29.30 ? 25   MET A CE  1 
ATOM   136   N  N   . GLU A 1 26  ? 6.787   68.694  117.335 1.00 37.60 ? 26   GLU A N   1 
ATOM   137   C  CA  . GLU A 1 26  ? 6.954   68.793  118.786 1.00 39.13 ? 26   GLU A CA  1 
ATOM   138   C  C   . GLU A 1 26  ? 7.898   69.925  119.104 1.00 41.25 ? 26   GLU A C   1 
ATOM   139   O  O   . GLU A 1 26  ? 7.691   70.661  120.054 1.00 38.62 ? 26   GLU A O   1 
ATOM   140   C  CB  . GLU A 1 26  ? 7.542   67.509  119.367 1.00 37.23 ? 26   GLU A CB  1 
ATOM   141   C  CG  . GLU A 1 26  ? 6.605   66.339  119.333 1.00 37.29 ? 26   GLU A CG  1 
ATOM   142   C  CD  . GLU A 1 26  ? 7.176   65.106  120.017 1.00 37.86 ? 26   GLU A CD  1 
ATOM   143   O  OE1 . GLU A 1 26  ? 8.242   65.217  120.641 1.00 37.87 ? 26   GLU A OE1 1 
ATOM   144   O  OE2 . GLU A 1 26  ? 6.554   64.022  119.940 1.00 39.02 ? 26   GLU A OE2 1 
ATOM   145   N  N   . ASN A 1 27  ? 8.933   70.061  118.281 1.00 44.86 ? 27   ASN A N   1 
ATOM   146   C  CA  . ASN A 1 27  ? 9.938   71.085  118.487 1.00 46.29 ? 27   ASN A CA  1 
ATOM   147   C  C   . ASN A 1 27  ? 9.430   72.508  118.413 1.00 46.62 ? 27   ASN A C   1 
ATOM   148   O  O   . ASN A 1 27  ? 10.144  73.445  118.796 1.00 47.91 ? 27   ASN A O   1 
ATOM   149   C  CB  . ASN A 1 27  ? 11.089  70.905  117.486 1.00 53.15 ? 27   ASN A CB  1 
ATOM   150   C  CG  . ASN A 1 27  ? 12.249  70.109  118.081 1.00 57.26 ? 27   ASN A CG  1 
ATOM   151   O  OD1 . ASN A 1 27  ? 12.537  70.232  119.277 1.00 57.91 ? 27   ASN A OD1 1 
ATOM   152   N  ND2 . ASN A 1 27  ? 12.918  69.290  117.257 1.00 62.20 ? 27   ASN A ND2 1 
ATOM   153   N  N   . SER A 1 28  ? 8.210   72.689  117.918 1.00 44.90 ? 28   SER A N   1 
ATOM   154   C  CA  . SER A 1 28  ? 7.665   74.032  117.772 1.00 40.49 ? 28   SER A CA  1 
ATOM   155   C  C   . SER A 1 28  ? 7.055   74.542  119.055 1.00 38.65 ? 28   SER A C   1 
ATOM   156   O  O   . SER A 1 28  ? 6.708   75.719  119.152 1.00 38.62 ? 28   SER A O   1 
ATOM   157   C  CB  . SER A 1 28  ? 6.619   74.071  116.652 1.00 40.14 ? 28   SER A CB  1 
ATOM   158   O  OG  . SER A 1 28  ? 5.423   73.420  117.033 1.00 40.81 ? 28   SER A OG  1 
ATOM   159   N  N   . VAL A 1 29  ? 6.923   73.662  120.039 1.00 36.82 ? 29   VAL A N   1 
ATOM   160   C  CA  . VAL A 1 29  ? 6.323   74.046  121.322 1.00 41.27 ? 29   VAL A CA  1 
ATOM   161   C  C   . VAL A 1 29  ? 7.312   74.852  122.182 1.00 44.39 ? 29   VAL A C   1 
ATOM   162   O  O   . VAL A 1 29  ? 8.399   74.373  122.522 1.00 45.23 ? 29   VAL A O   1 
ATOM   163   C  CB  . VAL A 1 29  ? 5.854   72.790  122.117 1.00 42.00 ? 29   VAL A CB  1 
ATOM   164   C  CG1 . VAL A 1 29  ? 5.142   73.211  123.424 1.00 39.38 ? 29   VAL A CG1 1 
ATOM   165   C  CG2 . VAL A 1 29  ? 4.954   71.929  121.238 1.00 31.02 ? 29   VAL A CG2 1 
ATOM   166   N  N   . THR A 1 30  ? 6.949   76.084  122.516 1.00 45.55 ? 30   THR A N   1 
ATOM   167   C  CA  . THR A 1 30  ? 7.833   76.927  123.315 1.00 47.06 ? 30   THR A CA  1 
ATOM   168   C  C   . THR A 1 30  ? 6.996   77.795  124.225 1.00 52.18 ? 30   THR A C   1 
ATOM   169   O  O   . THR A 1 30  ? 5.764   77.806  124.134 1.00 56.15 ? 30   THR A O   1 
ATOM   170   C  CB  . THR A 1 30  ? 8.724   77.849  122.438 1.00 46.69 ? 30   THR A CB  1 
ATOM   171   O  OG1 . THR A 1 30  ? 7.904   78.822  121.761 1.00 45.36 ? 30   THR A OG1 1 
ATOM   172   C  CG2 . THR A 1 30  ? 9.528   77.018  121.408 1.00 40.82 ? 30   THR A CG2 1 
ATOM   173   N  N   . SER A 1 31  ? 7.655   78.534  125.105 1.00 54.94 ? 31   SER A N   1 
ATOM   174   C  CA  . SER A 1 31  ? 6.933   79.383  126.048 1.00 58.14 ? 31   SER A CA  1 
ATOM   175   C  C   . SER A 1 31  ? 6.142   80.512  125.403 1.00 57.73 ? 31   SER A C   1 
ATOM   176   O  O   . SER A 1 31  ? 5.139   80.965  125.952 1.00 59.02 ? 31   SER A O   1 
ATOM   177   C  CB  . SER A 1 31  ? 7.904   79.959  127.063 1.00 60.58 ? 31   SER A CB  1 
ATOM   178   O  OG  . SER A 1 31  ? 8.608   78.922  127.722 1.00 66.87 ? 31   SER A OG  1 
ATOM   179   N  N   . SER A 1 32  ? 6.593   80.960  124.238 1.00 57.68 ? 32   SER A N   1 
ATOM   180   C  CA  . SER A 1 32  ? 5.916   82.033  123.515 1.00 56.08 ? 32   SER A CA  1 
ATOM   181   C  C   . SER A 1 32  ? 5.040   81.488  122.384 1.00 52.66 ? 32   SER A C   1 
ATOM   182   O  O   . SER A 1 32  ? 4.142   82.170  121.907 1.00 53.20 ? 32   SER A O   1 
ATOM   183   C  CB  . SER A 1 32  ? 6.957   83.012  122.954 1.00 56.93 ? 32   SER A CB  1 
ATOM   184   O  OG  . SER A 1 32  ? 7.993   82.313  122.279 1.00 57.83 ? 32   SER A OG  1 
ATOM   185   N  N   . ALA A 1 33  ? 5.301   80.256  121.960 1.00 51.33 ? 33   ALA A N   1 
ATOM   186   C  CA  . ALA A 1 33  ? 4.520   79.653  120.891 1.00 51.06 ? 33   ALA A CA  1 
ATOM   187   C  C   . ALA A 1 33  ? 3.034   79.642  121.287 1.00 52.05 ? 33   ALA A C   1 
ATOM   188   O  O   . ALA A 1 33  ? 2.703   79.615  122.477 1.00 55.11 ? 33   ALA A O   1 
ATOM   189   C  CB  . ALA A 1 33  ? 5.025   78.230  120.611 1.00 44.59 ? 33   ALA A CB  1 
ATOM   190   N  N   . TYR A 1 34  ? 2.150   79.700  120.293 1.00 49.73 ? 34   TYR A N   1 
ATOM   191   C  CA  . TYR A 1 34  ? 0.709   79.668  120.538 1.00 50.17 ? 34   TYR A CA  1 
ATOM   192   C  C   . TYR A 1 34  ? 0.392   78.223  120.976 1.00 47.95 ? 34   TYR A C   1 
ATOM   193   O  O   . TYR A 1 34  ? 0.721   77.282  120.257 1.00 48.46 ? 34   TYR A O   1 
ATOM   194   C  CB  . TYR A 1 34  ? -0.038  80.052  119.239 1.00 47.37 ? 34   TYR A CB  1 
ATOM   195   C  CG  . TYR A 1 34  ? -1.538  79.913  119.302 1.00 46.86 ? 34   TYR A CG  1 
ATOM   196   C  CD1 . TYR A 1 34  ? -2.151  78.656  119.229 1.00 47.10 ? 34   TYR A CD1 1 
ATOM   197   C  CD2 . TYR A 1 34  ? -2.352  81.033  119.438 1.00 46.93 ? 34   TYR A CD2 1 
ATOM   198   C  CE1 . TYR A 1 34  ? -3.541  78.522  119.294 1.00 48.02 ? 34   TYR A CE1 1 
ATOM   199   C  CE2 . TYR A 1 34  ? -3.753  80.910  119.506 1.00 49.66 ? 34   TYR A CE2 1 
ATOM   200   C  CZ  . TYR A 1 34  ? -4.335  79.654  119.438 1.00 49.68 ? 34   TYR A CZ  1 
ATOM   201   O  OH  . TYR A 1 34  ? -5.702  79.525  119.565 1.00 54.52 ? 34   TYR A OH  1 
ATOM   202   N  N   . PRO A 1 35  ? -0.208  78.031  122.173 1.00 45.35 ? 35   PRO A N   1 
ATOM   203   C  CA  . PRO A 1 35  ? -0.540  76.686  122.669 1.00 42.09 ? 35   PRO A CA  1 
ATOM   204   C  C   . PRO A 1 35  ? -1.516  75.986  121.735 1.00 41.38 ? 35   PRO A C   1 
ATOM   205   O  O   . PRO A 1 35  ? -2.720  76.293  121.711 1.00 41.26 ? 35   PRO A O   1 
ATOM   206   C  CB  . PRO A 1 35  ? -1.147  76.961  124.040 1.00 41.87 ? 35   PRO A CB  1 
ATOM   207   C  CG  . PRO A 1 35  ? -0.457  78.230  124.451 1.00 42.73 ? 35   PRO A CG  1 
ATOM   208   C  CD  . PRO A 1 35  ? -0.527  79.044  123.191 1.00 42.03 ? 35   PRO A CD  1 
ATOM   209   N  N   . ASN A 1 36  ? -0.991  75.051  120.955 1.00 36.27 ? 36   ASN A N   1 
ATOM   210   C  CA  . ASN A 1 36  ? -1.815  74.342  120.011 1.00 35.53 ? 36   ASN A CA  1 
ATOM   211   C  C   . ASN A 1 36  ? -2.305  72.973  120.516 1.00 35.15 ? 36   ASN A C   1 
ATOM   212   O  O   . ASN A 1 36  ? -1.545  72.002  120.544 1.00 34.86 ? 36   ASN A O   1 
ATOM   213   C  CB  . ASN A 1 36  ? -1.050  74.170  118.700 1.00 33.49 ? 36   ASN A CB  1 
ATOM   214   C  CG  . ASN A 1 36  ? -1.948  73.649  117.558 1.00 38.35 ? 36   ASN A CG  1 
ATOM   215   O  OD1 . ASN A 1 36  ? -3.010  73.066  117.800 1.00 38.09 ? 36   ASN A OD1 1 
ATOM   216   N  ND2 . ASN A 1 36  ? -1.508  73.844  116.314 1.00 33.17 ? 36   ASN A ND2 1 
ATOM   217   N  N   . PRO A 1 37  ? -3.595  72.872  120.894 1.00 34.19 ? 37   PRO A N   1 
ATOM   218   C  CA  . PRO A 1 37  ? -4.119  71.581  121.379 1.00 34.10 ? 37   PRO A CA  1 
ATOM   219   C  C   . PRO A 1 37  ? -4.016  70.417  120.346 1.00 37.69 ? 37   PRO A C   1 
ATOM   220   O  O   . PRO A 1 37  ? -3.871  69.235  120.728 1.00 36.88 ? 37   PRO A O   1 
ATOM   221   C  CB  . PRO A 1 37  ? -5.560  71.919  121.786 1.00 29.02 ? 37   PRO A CB  1 
ATOM   222   C  CG  . PRO A 1 37  ? -5.905  73.068  120.904 1.00 29.29 ? 37   PRO A CG  1 
ATOM   223   C  CD  . PRO A 1 37  ? -4.645  73.906  120.883 1.00 28.40 ? 37   PRO A CD  1 
ATOM   224   N  N   . SER A 1 38  ? -4.051  70.735  119.050 1.00 37.05 ? 38   SER A N   1 
ATOM   225   C  CA  . SER A 1 38  ? -3.960  69.671  118.053 1.00 37.14 ? 38   SER A CA  1 
ATOM   226   C  C   . SER A 1 38  ? -2.571  69.087  118.077 1.00 37.41 ? 38   SER A C   1 
ATOM   227   O  O   . SER A 1 38  ? -2.398  67.877  117.863 1.00 38.73 ? 38   SER A O   1 
ATOM   228   C  CB  . SER A 1 38  ? -4.266  70.178  116.648 1.00 36.67 ? 38   SER A CB  1 
ATOM   229   O  OG  . SER A 1 38  ? -5.560  70.748  116.607 1.00 43.44 ? 38   SER A OG  1 
ATOM   230   N  N   . ILE A 1 39  ? -1.569  69.914  118.359 1.00 32.10 ? 39   ILE A N   1 
ATOM   231   C  CA  . ILE A 1 39  ? -0.240  69.347  118.373 1.00 29.59 ? 39   ILE A CA  1 
ATOM   232   C  C   . ILE A 1 39  ? -0.087  68.386  119.536 1.00 30.67 ? 39   ILE A C   1 
ATOM   233   O  O   . ILE A 1 39  ? 0.552   67.353  119.395 1.00 32.59 ? 39   ILE A O   1 
ATOM   234   C  CB  . ILE A 1 39  ? 0.846   70.428  118.434 1.00 30.96 ? 39   ILE A CB  1 
ATOM   235   C  CG1 . ILE A 1 39  ? 0.955   71.115  117.064 1.00 28.01 ? 39   ILE A CG1 1 
ATOM   236   C  CG2 . ILE A 1 39  ? 2.205   69.784  118.784 1.00 30.76 ? 39   ILE A CG2 1 
ATOM   237   C  CD1 . ILE A 1 39  ? 1.923   72.263  117.012 1.00 21.28 ? 39   ILE A CD1 1 
ATOM   238   N  N   . LEU A 1 40  ? -0.684  68.729  120.676 1.00 31.31 ? 40   LEU A N   1 
ATOM   239   C  CA  . LEU A 1 40  ? -0.616  67.899  121.873 1.00 32.70 ? 40   LEU A CA  1 
ATOM   240   C  C   . LEU A 1 40  ? -1.319  66.578  121.595 1.00 33.95 ? 40   LEU A C   1 
ATOM   241   O  O   . LEU A 1 40  ? -0.792  65.514  121.942 1.00 32.63 ? 40   LEU A O   1 
ATOM   242   C  CB  . LEU A 1 40  ? -1.270  68.612  123.090 1.00 32.59 ? 40   LEU A CB  1 
ATOM   243   C  CG  . LEU A 1 40  ? -1.175  67.799  124.385 1.00 35.36 ? 40   LEU A CG  1 
ATOM   244   C  CD1 . LEU A 1 40  ? 0.277   67.464  124.661 1.00 34.48 ? 40   LEU A CD1 1 
ATOM   245   C  CD2 . LEU A 1 40  ? -1.739  68.555  125.565 1.00 38.43 ? 40   LEU A CD2 1 
ATOM   246   N  N   . ILE A 1 41  ? -2.494  66.653  120.954 1.00 32.00 ? 41   ILE A N   1 
ATOM   247   C  CA  . ILE A 1 41  ? -3.253  65.459  120.617 1.00 30.79 ? 41   ILE A CA  1 
ATOM   248   C  C   . ILE A 1 41  ? -2.440  64.553  119.716 1.00 32.60 ? 41   ILE A C   1 
ATOM   249   O  O   . ILE A 1 41  ? -2.379  63.324  119.922 1.00 35.30 ? 41   ILE A O   1 
ATOM   250   C  CB  . ILE A 1 41  ? -4.560  65.791  119.892 1.00 33.35 ? 41   ILE A CB  1 
ATOM   251   C  CG1 . ILE A 1 41  ? -5.488  66.563  120.827 1.00 30.33 ? 41   ILE A CG1 1 
ATOM   252   C  CG2 . ILE A 1 41  ? -5.232  64.495  119.402 1.00 32.55 ? 41   ILE A CG2 1 
ATOM   253   C  CD1 . ILE A 1 41  ? -6.790  66.953  120.188 1.00 25.70 ? 41   ILE A CD1 1 
ATOM   254   N  N   . ALA A 1 42  ? -1.816  65.164  118.714 1.00 32.80 ? 42   ALA A N   1 
ATOM   255   C  CA  . ALA A 1 42  ? -0.999  64.424  117.768 1.00 34.11 ? 42   ALA A CA  1 
ATOM   256   C  C   . ALA A 1 42  ? 0.196   63.761  118.450 1.00 33.64 ? 42   ALA A C   1 
ATOM   257   O  O   . ALA A 1 42  ? 0.398   62.551  118.317 1.00 32.50 ? 42   ALA A O   1 
ATOM   258   C  CB  . ALA A 1 42  ? -0.529  65.342  116.639 1.00 34.10 ? 42   ALA A CB  1 
ATOM   259   N  N   . MET A 1 43  ? 0.989   64.518  119.195 1.00 33.21 ? 43   MET A N   1 
ATOM   260   C  CA  . MET A 1 43  ? 2.123   63.850  119.805 1.00 35.78 ? 43   MET A CA  1 
ATOM   261   C  C   . MET A 1 43  ? 1.651   62.791  120.780 1.00 34.13 ? 43   MET A C   1 
ATOM   262   O  O   . MET A 1 43  ? 2.229   61.701  120.842 1.00 32.81 ? 43   MET A O   1 
ATOM   263   C  CB  . MET A 1 43  ? 3.105   64.840  120.460 1.00 35.26 ? 43   MET A CB  1 
ATOM   264   C  CG  . MET A 1 43  ? 2.610   65.602  121.674 1.00 40.54 ? 43   MET A CG  1 
ATOM   265   S  SD  . MET A 1 43  ? 3.743   66.934  122.074 1.00 44.27 ? 43   MET A SD  1 
ATOM   266   C  CE  . MET A 1 43  ? 5.231   66.060  122.367 1.00 40.73 ? 43   MET A CE  1 
ATOM   267   N  N   . ASN A 1 44  ? 0.578   63.063  121.511 1.00 33.37 ? 44   ASN A N   1 
ATOM   268   C  CA  . ASN A 1 44  ? 0.140   62.037  122.441 1.00 33.10 ? 44   ASN A CA  1 
ATOM   269   C  C   . ASN A 1 44  ? -0.352  60.778  121.734 1.00 33.51 ? 44   ASN A C   1 
ATOM   270   O  O   . ASN A 1 44  ? -0.099  59.694  122.220 1.00 38.09 ? 44   ASN A O   1 
ATOM   271   C  CB  . ASN A 1 44  ? -0.908  62.575  123.409 1.00 32.04 ? 44   ASN A CB  1 
ATOM   272   C  CG  . ASN A 1 44  ? -0.296  63.479  124.474 1.00 35.18 ? 44   ASN A CG  1 
ATOM   273   O  OD1 . ASN A 1 44  ? 0.913   63.417  124.717 1.00 31.84 ? 44   ASN A OD1 1 
ATOM   274   N  ND2 . ASN A 1 44  ? -1.127  64.315  125.122 1.00 31.42 ? 44   ASN A ND2 1 
ATOM   275   N  N   . LEU A 1 45  ? -1.034  60.891  120.594 1.00 32.68 ? 45   LEU A N   1 
ATOM   276   C  CA  . LEU A 1 45  ? -1.503  59.685  119.895 1.00 31.43 ? 45   LEU A CA  1 
ATOM   277   C  C   . LEU A 1 45  ? -0.330  58.924  119.248 1.00 32.50 ? 45   LEU A C   1 
ATOM   278   O  O   . LEU A 1 45  ? -0.366  57.700  119.068 1.00 29.83 ? 45   LEU A O   1 
ATOM   279   C  CB  . LEU A 1 45  ? -2.500  60.058  118.809 1.00 31.71 ? 45   LEU A CB  1 
ATOM   280   C  CG  . LEU A 1 45  ? -3.892  60.500  119.226 1.00 34.42 ? 45   LEU A CG  1 
ATOM   281   C  CD1 . LEU A 1 45  ? -4.645  61.001  117.987 1.00 30.14 ? 45   LEU A CD1 1 
ATOM   282   C  CD2 . LEU A 1 45  ? -4.618  59.328  119.883 1.00 29.32 ? 45   LEU A CD2 1 
ATOM   283   N  N   . ALA A 1 46  ? 0.705   59.665  118.885 1.00 30.05 ? 46   ALA A N   1 
ATOM   284   C  CA  . ALA A 1 46  ? 1.868   59.076  118.276 1.00 29.64 ? 46   ALA A CA  1 
ATOM   285   C  C   . ALA A 1 46  ? 2.805   58.478  119.296 1.00 31.63 ? 46   ALA A C   1 
ATOM   286   O  O   . ALA A 1 46  ? 3.491   57.512  118.998 1.00 33.45 ? 46   ALA A O   1 
ATOM   287   C  CB  . ALA A 1 46  ? 2.619   60.127  117.486 1.00 30.09 ? 46   ALA A CB  1 
ATOM   288   N  N   . GLY A 1 47  ? 2.821   59.041  120.496 1.00 31.23 ? 47   GLY A N   1 
ATOM   289   C  CA  . GLY A 1 47  ? 3.765   58.599  121.510 1.00 33.84 ? 47   GLY A CA  1 
ATOM   290   C  C   . GLY A 1 47  ? 4.817   59.700  121.456 1.00 33.66 ? 47   GLY A C   1 
ATOM   291   O  O   . GLY A 1 47  ? 5.656   59.709  120.563 1.00 36.60 ? 47   GLY A O   1 
ATOM   292   N  N   . ALA A 1 48  ? 4.740   60.645  122.381 1.00 32.55 ? 48   ALA A N   1 
ATOM   293   C  CA  . ALA A 1 48  ? 5.635   61.795  122.412 1.00 36.82 ? 48   ALA A CA  1 
ATOM   294   C  C   . ALA A 1 48  ? 7.142   61.496  122.503 1.00 37.95 ? 48   ALA A C   1 
ATOM   295   O  O   . ALA A 1 48  ? 7.538   60.559  123.180 1.00 38.77 ? 48   ALA A O   1 
ATOM   296   C  CB  . ALA A 1 48  ? 5.223   62.710  123.564 1.00 32.44 ? 48   ALA A CB  1 
ATOM   297   N  N   . TYR A 1 49  ? 7.971   62.289  121.821 1.00 36.24 ? 49   TYR A N   1 
ATOM   298   C  CA  . TYR A 1 49  ? 9.418   62.094  121.887 1.00 36.01 ? 49   TYR A CA  1 
ATOM   299   C  C   . TYR A 1 49  ? 9.969   63.036  122.940 1.00 37.36 ? 49   TYR A C   1 
ATOM   300   O  O   . TYR A 1 49  ? 10.610  62.622  123.889 1.00 38.07 ? 49   TYR A O   1 
ATOM   301   C  CB  . TYR A 1 49  ? 10.104  62.437  120.574 1.00 31.06 ? 49   TYR A CB  1 
ATOM   302   C  CG  . TYR A 1 49  ? 9.819   61.487  119.452 1.00 34.63 ? 49   TYR A CG  1 
ATOM   303   C  CD1 . TYR A 1 49  ? 9.885   60.105  119.663 1.00 29.32 ? 49   TYR A CD1 1 
ATOM   304   C  CD2 . TYR A 1 49  ? 9.538   61.961  118.144 1.00 30.34 ? 49   TYR A CD2 1 
ATOM   305   C  CE1 . TYR A 1 49  ? 9.688   59.210  118.616 1.00 29.76 ? 49   TYR A CE1 1 
ATOM   306   C  CE2 . TYR A 1 49  ? 9.342   61.054  117.079 1.00 29.80 ? 49   TYR A CE2 1 
ATOM   307   C  CZ  . TYR A 1 49  ? 9.422   59.684  117.333 1.00 29.90 ? 49   TYR A CZ  1 
ATOM   308   O  OH  . TYR A 1 49  ? 9.280   58.764  116.323 1.00 37.27 ? 49   TYR A OH  1 
ATOM   309   N  N   . ASN A 1 50  ? 9.689   64.310  122.756 1.00 39.37 ? 50   ASN A N   1 
ATOM   310   C  CA  . ASN A 1 50  ? 10.169  65.350  123.643 1.00 42.40 ? 50   ASN A CA  1 
ATOM   311   C  C   . ASN A 1 50  ? 9.263   65.540  124.861 1.00 43.63 ? 50   ASN A C   1 
ATOM   312   O  O   . ASN A 1 50  ? 8.269   66.305  124.823 1.00 41.92 ? 50   ASN A O   1 
ATOM   313   C  CB  . ASN A 1 50  ? 10.287  66.647  122.841 1.00 43.56 ? 50   ASN A CB  1 
ATOM   314   C  CG  . ASN A 1 50  ? 10.697  67.814  123.676 1.00 44.62 ? 50   ASN A CG  1 
ATOM   315   O  OD1 . ASN A 1 50  ? 10.974  68.884  123.134 1.00 48.60 ? 50   ASN A OD1 1 
ATOM   316   N  ND2 . ASN A 1 50  ? 10.739  67.636  125.003 1.00 45.05 ? 50   ASN A ND2 1 
ATOM   317   N  N   . LEU A 1 51  ? 9.631   64.883  125.959 1.00 41.62 ? 51   LEU A N   1 
ATOM   318   C  CA  . LEU A 1 51  ? 8.818   64.980  127.160 1.00 40.89 ? 51   LEU A CA  1 
ATOM   319   C  C   . LEU A 1 51  ? 8.744   66.376  127.751 1.00 39.82 ? 51   LEU A C   1 
ATOM   320   O  O   . LEU A 1 51  ? 7.751   66.714  128.410 1.00 39.98 ? 51   LEU A O   1 
ATOM   321   C  CB  . LEU A 1 51  ? 9.293   63.958  128.189 1.00 43.35 ? 51   LEU A CB  1 
ATOM   322   C  CG  . LEU A 1 51  ? 9.252   62.532  127.607 1.00 45.09 ? 51   LEU A CG  1 
ATOM   323   C  CD1 . LEU A 1 51  ? 9.832   61.531  128.597 1.00 47.17 ? 51   LEU A CD1 1 
ATOM   324   C  CD2 . LEU A 1 51  ? 7.801   62.166  127.275 1.00 45.23 ? 51   LEU A CD2 1 
ATOM   325   N  N   . LYS A 1 52  ? 9.739   67.238  127.492 1.00 40.74 ? 52   LYS A N   1 
ATOM   326   C  CA  . LYS A 1 52  ? 9.633   68.604  128.028 1.00 41.83 ? 52   LYS A CA  1 
ATOM   327   C  C   . LYS A 1 52  ? 8.618   69.338  127.191 1.00 39.77 ? 52   LYS A C   1 
ATOM   328   O  O   . LYS A 1 52  ? 7.824   70.119  127.789 1.00 37.22 ? 52   LYS A O   1 
ATOM   329   C  CB  . LYS A 1 52  ? 10.871  69.429  127.846 1.00 45.70 ? 52   LYS A CB  1 
ATOM   330   C  CG  . LYS A 1 52  ? 11.393  70.052  129.169 1.00 54.37 ? 52   LYS A CG  1 
ATOM   331   C  CD  . LYS A 1 52  ? 12.818  69.894  129.023 1.00 61.40 ? 52   LYS A CD  1 
ATOM   332   C  CE  . LYS A 1 52  ? 12.908  68.333  128.853 1.00 64.84 ? 52   LYS A CE  1 
ATOM   333   N  NZ  . LYS A 1 52  ? 14.092  68.650  128.207 1.00 70.33 ? 52   LYS A NZ  1 
ATOM   334   N  N   . ALA A 1 53  ? 8.670   69.210  125.911 1.00 36.49 ? 53   ALA A N   1 
ATOM   335   C  CA  . ALA A 1 53  ? 7.691   69.935  125.101 1.00 36.26 ? 53   ALA A CA  1 
ATOM   336   C  C   . ALA A 1 53  ? 6.299   69.413  125.475 1.00 37.18 ? 53   ALA A C   1 
ATOM   337   O  O   . ALA A 1 53  ? 5.343   70.182  125.641 1.00 36.73 ? 53   ALA A O   1 
ATOM   338   C  CB  . ALA A 1 53  ? 7.963   69.713  123.648 1.00 33.80 ? 53   ALA A CB  1 
ATOM   339   N  N   . GLN A 1 54  ? 6.200   68.099  125.662 1.00 37.72 ? 54   GLN A N   1 
ATOM   340   C  CA  . GLN A 1 54  ? 4.922   67.507  126.037 1.00 40.03 ? 54   GLN A CA  1 
ATOM   341   C  C   . GLN A 1 54  ? 4.347   68.127  127.306 1.00 41.05 ? 54   GLN A C   1 
ATOM   342   O  O   . GLN A 1 54  ? 3.179   68.515  127.347 1.00 39.43 ? 54   GLN A O   1 
ATOM   343   C  CB  . GLN A 1 54  ? 5.059   66.010  126.248 1.00 35.20 ? 54   GLN A CB  1 
ATOM   344   C  CG  . GLN A 1 54  ? 3.762   65.369  126.696 1.00 33.01 ? 54   GLN A CG  1 
ATOM   345   C  CD  . GLN A 1 54  ? 3.937   63.879  126.952 1.00 38.33 ? 54   GLN A CD  1 
ATOM   346   O  OE1 . GLN A 1 54  ? 3.175   63.057  126.447 1.00 41.76 ? 54   GLN A OE1 1 
ATOM   347   N  NE2 . GLN A 1 54  ? 4.955   63.523  127.728 1.00 39.42 ? 54   GLN A NE2 1 
ATOM   348   N  N   . LYS A 1 55  ? 5.179   68.213  128.339 1.00 42.45 ? 55   LYS A N   1 
ATOM   349   C  CA  . LYS A 1 55  ? 4.767   68.768  129.624 1.00 43.84 ? 55   LYS A CA  1 
ATOM   350   C  C   . LYS A 1 55  ? 4.436   70.260  129.531 1.00 43.71 ? 55   LYS A C   1 
ATOM   351   O  O   . LYS A 1 55  ? 3.433   70.725  130.079 1.00 44.07 ? 55   LYS A O   1 
ATOM   352   C  CB  . LYS A 1 55  ? 5.885   68.524  130.639 1.00 49.65 ? 55   LYS A CB  1 
ATOM   353   C  CG  . LYS A 1 55  ? 5.647   69.064  132.030 1.00 56.96 ? 55   LYS A CG  1 
ATOM   354   C  CD  . LYS A 1 55  ? 6.841   68.692  132.909 1.00 63.43 ? 55   LYS A CD  1 
ATOM   355   C  CE  . LYS A 1 55  ? 6.798   69.361  134.280 1.00 64.43 ? 55   LYS A CE  1 
ATOM   356   N  NZ  . LYS A 1 55  ? 8.020   68.980  135.026 1.00 62.56 ? 55   LYS A NZ  1 
ATOM   357   N  N   . LEU A 1 56  ? 5.275   71.012  128.827 1.00 42.30 ? 56   LEU A N   1 
ATOM   358   C  CA  . LEU A 1 56  ? 5.048   72.432  128.698 1.00 40.13 ? 56   LEU A CA  1 
ATOM   359   C  C   . LEU A 1 56  ? 3.672   72.731  128.093 1.00 39.56 ? 56   LEU A C   1 
ATOM   360   O  O   . LEU A 1 56  ? 2.895   73.492  128.666 1.00 40.67 ? 56   LEU A O   1 
ATOM   361   C  CB  . LEU A 1 56  ? 6.173   73.060  127.870 1.00 38.10 ? 56   LEU A CB  1 
ATOM   362   C  CG  . LEU A 1 56  ? 5.923   74.508  127.461 1.00 38.55 ? 56   LEU A CG  1 
ATOM   363   C  CD1 . LEU A 1 56  ? 5.611   75.344  128.679 1.00 34.41 ? 56   LEU A CD1 1 
ATOM   364   C  CD2 . LEU A 1 56  ? 7.128   75.037  126.712 1.00 39.28 ? 56   LEU A CD2 1 
ATOM   365   N  N   . LEU A 1 57  ? 3.367   72.112  126.952 1.00 40.49 ? 57   LEU A N   1 
ATOM   366   C  CA  . LEU A 1 57  ? 2.085   72.315  126.255 1.00 38.76 ? 57   LEU A CA  1 
ATOM   367   C  C   . LEU A 1 57  ? 0.926   71.924  127.135 1.00 40.00 ? 57   LEU A C   1 
ATOM   368   O  O   . LEU A 1 57  ? -0.066  72.653  127.245 1.00 42.61 ? 57   LEU A O   1 
ATOM   369   C  CB  . LEU A 1 57  ? 2.045   71.481  124.976 1.00 37.57 ? 57   LEU A CB  1 
ATOM   370   C  CG  . LEU A 1 57  ? 0.917   71.681  123.960 1.00 37.33 ? 57   LEU A CG  1 
ATOM   371   C  CD1 . LEU A 1 57  ? 0.523   73.150  123.856 1.00 27.36 ? 57   LEU A CD1 1 
ATOM   372   C  CD2 . LEU A 1 57  ? 1.387   71.123  122.579 1.00 33.22 ? 57   LEU A CD2 1 
ATOM   373   N  N   . THR A 1 58  ? 1.054   70.767  127.775 1.00 40.00 ? 58   THR A N   1 
ATOM   374   C  CA  . THR A 1 58  ? 0.012   70.294  128.660 1.00 37.80 ? 58   THR A CA  1 
ATOM   375   C  C   . THR A 1 58  ? -0.274  71.319  129.728 1.00 37.86 ? 58   THR A C   1 
ATOM   376   O  O   . THR A 1 58  ? -1.432  71.527  130.065 1.00 39.30 ? 58   THR A O   1 
ATOM   377   C  CB  . THR A 1 58  ? 0.401   68.960  129.309 1.00 36.36 ? 58   THR A CB  1 
ATOM   378   O  OG1 . THR A 1 58  ? 0.485   67.959  128.278 1.00 41.07 ? 58   THR A OG1 1 
ATOM   379   C  CG2 . THR A 1 58  ? -0.640  68.533  130.338 1.00 30.10 ? 58   THR A CG2 1 
ATOM   380   N  N   . TYR A 1 59  ? 0.766   71.978  130.242 1.00 39.49 ? 59   TYR A N   1 
ATOM   381   C  CA  . TYR A 1 59  ? 0.567   72.976  131.295 1.00 42.08 ? 59   TYR A CA  1 
ATOM   382   C  C   . TYR A 1 59  ? -0.066  74.241  130.753 1.00 40.43 ? 59   TYR A C   1 
ATOM   383   O  O   . TYR A 1 59  ? -0.932  74.835  131.422 1.00 39.29 ? 59   TYR A O   1 
ATOM   384   C  CB  . TYR A 1 59  ? 1.886   73.309  132.036 1.00 47.70 ? 59   TYR A CB  1 
ATOM   385   C  CG  . TYR A 1 59  ? 2.314   72.266  133.064 1.00 55.76 ? 59   TYR A CG  1 
ATOM   386   C  CD1 . TYR A 1 59  ? 1.378   71.408  133.653 1.00 59.92 ? 59   TYR A CD1 1 
ATOM   387   C  CD2 . TYR A 1 59  ? 3.645   72.146  133.459 1.00 59.96 ? 59   TYR A CD2 1 
ATOM   388   C  CE1 . TYR A 1 59  ? 1.756   70.455  134.605 1.00 61.08 ? 59   TYR A CE1 1 
ATOM   389   C  CE2 . TYR A 1 59  ? 4.040   71.195  134.417 1.00 62.08 ? 59   TYR A CE2 1 
ATOM   390   C  CZ  . TYR A 1 59  ? 3.089   70.350  134.986 1.00 63.17 ? 59   TYR A CZ  1 
ATOM   391   O  OH  . TYR A 1 59  ? 3.474   69.398  135.924 1.00 57.95 ? 59   TYR A OH  1 
ATOM   392   N  N   . GLN A 1 60  ? 0.353   74.647  129.554 1.00 36.69 ? 60   GLN A N   1 
ATOM   393   C  CA  . GLN A 1 60  ? -0.216  75.831  128.933 1.00 38.65 ? 60   GLN A CA  1 
ATOM   394   C  C   . GLN A 1 60  ? -1.715  75.628  128.689 1.00 43.13 ? 60   GLN A C   1 
ATOM   395   O  O   . GLN A 1 60  ? -2.505  76.559  128.842 1.00 45.96 ? 60   GLN A O   1 
ATOM   396   C  CB  . GLN A 1 60  ? 0.482   76.136  127.604 1.00 37.86 ? 60   GLN A CB  1 
ATOM   397   C  CG  . GLN A 1 60  ? 1.979   76.310  127.750 1.00 41.98 ? 60   GLN A CG  1 
ATOM   398   C  CD  . GLN A 1 60  ? 2.722   76.505  126.426 1.00 44.46 ? 60   GLN A CD  1 
ATOM   399   O  OE1 . GLN A 1 60  ? 2.558   75.727  125.482 1.00 45.19 ? 60   GLN A OE1 1 
ATOM   400   N  NE2 . GLN A 1 60  ? 3.563   77.534  126.366 1.00 42.77 ? 60   GLN A NE2 1 
ATOM   401   N  N   . LEU A 1 61  ? -2.126  74.423  128.304 1.00 42.93 ? 61   LEU A N   1 
ATOM   402   C  CA  . LEU A 1 61  ? -3.546  74.213  128.072 1.00 44.03 ? 61   LEU A CA  1 
ATOM   403   C  C   . LEU A 1 61  ? -4.314  74.085  129.377 1.00 46.23 ? 61   LEU A C   1 
ATOM   404   O  O   . LEU A 1 61  ? -5.446  74.563  129.460 1.00 46.96 ? 61   LEU A O   1 
ATOM   405   C  CB  . LEU A 1 61  ? -3.782  72.969  127.205 1.00 41.88 ? 61   LEU A CB  1 
ATOM   406   C  CG  . LEU A 1 61  ? -3.058  73.053  125.876 1.00 41.76 ? 61   LEU A CG  1 
ATOM   407   C  CD1 . LEU A 1 61  ? -3.128  71.728  125.198 1.00 39.31 ? 61   LEU A CD1 1 
ATOM   408   C  CD2 . LEU A 1 61  ? -3.651  74.166  125.027 1.00 39.07 ? 61   LEU A CD2 1 
ATOM   409   N  N   . MET A 1 62  ? -3.721  73.439  130.386 1.00 47.47 ? 62   MET A N   1 
ATOM   410   C  CA  . MET A 1 62  ? -4.414  73.263  131.673 1.00 50.43 ? 62   MET A CA  1 
ATOM   411   C  C   . MET A 1 62  ? -4.765  74.609  132.241 1.00 52.56 ? 62   MET A C   1 
ATOM   412   O  O   . MET A 1 62  ? -5.774  74.780  132.934 1.00 56.23 ? 62   MET A O   1 
ATOM   413   C  CB  . MET A 1 62  ? -3.545  72.547  132.692 1.00 46.08 ? 62   MET A CB  1 
ATOM   414   C  CG  . MET A 1 62  ? -3.432  71.077  132.502 1.00 44.62 ? 62   MET A CG  1 
ATOM   415   S  SD  . MET A 1 62  ? -2.077  70.477  133.518 1.00 48.13 ? 62   MET A SD  1 
ATOM   416   C  CE  . MET A 1 62  ? -2.645  70.967  135.095 1.00 43.49 ? 62   MET A CE  1 
ATOM   417   N  N   . SER A 1 63  ? -3.923  75.578  131.933 1.00 53.73 ? 63   SER A N   1 
ATOM   418   C  CA  . SER A 1 63  ? -4.142  76.917  132.437 1.00 54.49 ? 63   SER A CA  1 
ATOM   419   C  C   . SER A 1 63  ? -4.798  77.882  131.439 1.00 54.04 ? 63   SER A C   1 
ATOM   420   O  O   . SER A 1 63  ? -4.890  79.068  131.715 1.00 53.19 ? 63   SER A O   1 
ATOM   421   C  CB  . SER A 1 63  ? -2.811  77.487  132.916 1.00 51.98 ? 63   SER A CB  1 
ATOM   422   O  OG  . SER A 1 63  ? -2.048  77.915  131.802 1.00 51.62 ? 63   SER A OG  1 
ATOM   423   N  N   . SER A 1 64  ? -5.233  77.393  130.281 1.00 56.23 ? 64   SER A N   1 
ATOM   424   C  CA  . SER A 1 64  ? -5.896  78.271  129.321 1.00 57.01 ? 64   SER A CA  1 
ATOM   425   C  C   . SER A 1 64  ? -7.181  78.730  130.001 1.00 58.99 ? 64   SER A C   1 
ATOM   426   O  O   . SER A 1 64  ? -7.751  78.004  130.825 1.00 59.27 ? 64   SER A O   1 
ATOM   427   C  CB  . SER A 1 64  ? -6.210  77.526  128.017 1.00 56.96 ? 64   SER A CB  1 
ATOM   428   O  OG  . SER A 1 64  ? -6.939  76.333  128.257 1.00 57.86 ? 64   SER A OG  1 
ATOM   429   N  N   . ASP A 1 65  ? -7.624  79.940  129.674 1.00 60.60 ? 65   ASP A N   1 
ATOM   430   C  CA  . ASP A 1 65  ? -8.831  80.513  130.273 1.00 60.50 ? 65   ASP A CA  1 
ATOM   431   C  C   . ASP A 1 65  ? -10.076 80.072  129.516 1.00 57.07 ? 65   ASP A C   1 
ATOM   432   O  O   . ASP A 1 65  ? -10.187 80.300  128.315 1.00 57.31 ? 65   ASP A O   1 
ATOM   433   C  CB  . ASP A 1 65  ? -8.728  82.046  130.262 1.00 64.36 ? 65   ASP A CB  1 
ATOM   434   C  CG  . ASP A 1 65  ? -9.920  82.718  130.913 1.00 69.08 ? 65   ASP A CG  1 
ATOM   435   O  OD1 . ASP A 1 65  ? -11.073 82.332  130.611 1.00 70.40 ? 65   ASP A OD1 1 
ATOM   436   O  OD2 . ASP A 1 65  ? -9.700  83.645  131.722 1.00 75.11 ? 65   ASP A OD2 1 
ATOM   437   N  N   . ASN A 1 66  ? -11.028 79.467  130.215 1.00 54.83 ? 66   ASN A N   1 
ATOM   438   C  CA  . ASN A 1 66  ? -12.238 78.999  129.543 1.00 54.45 ? 66   ASN A CA  1 
ATOM   439   C  C   . ASN A 1 66  ? -12.969 80.065  128.726 1.00 53.98 ? 66   ASN A C   1 
ATOM   440   O  O   . ASN A 1 66  ? -13.609 79.741  127.734 1.00 54.45 ? 66   ASN A O   1 
ATOM   441   C  CB  . ASN A 1 66  ? -13.195 78.373  130.551 1.00 52.28 ? 66   ASN A CB  1 
ATOM   442   C  CG  . ASN A 1 66  ? -12.518 77.322  131.414 1.00 54.81 ? 66   ASN A CG  1 
ATOM   443   O  OD1 . ASN A 1 66  ? -11.660 76.569  130.935 1.00 54.13 ? 66   ASN A OD1 1 
ATOM   444   N  ND2 . ASN A 1 66  ? -12.905 77.259  132.692 1.00 55.65 ? 66   ASN A ND2 1 
ATOM   445   N  N   . ASN A 1 67  ? -12.859 81.329  129.123 1.00 54.88 ? 67   ASN A N   1 
ATOM   446   C  CA  . ASN A 1 67  ? -13.540 82.411  128.418 1.00 57.54 ? 67   ASN A CA  1 
ATOM   447   C  C   . ASN A 1 67  ? -12.816 82.897  127.172 1.00 59.82 ? 67   ASN A C   1 
ATOM   448   O  O   . ASN A 1 67  ? -13.304 83.778  126.452 1.00 59.35 ? 67   ASN A O   1 
ATOM   449   C  CB  . ASN A 1 67  ? -13.772 83.584  129.356 1.00 57.48 ? 67   ASN A CB  1 
ATOM   450   C  CG  . ASN A 1 67  ? -14.884 83.323  130.318 1.00 58.93 ? 67   ASN A CG  1 
ATOM   451   O  OD1 . ASN A 1 67  ? -14.793 83.689  131.480 1.00 59.41 ? 67   ASN A OD1 1 
ATOM   452   N  ND2 . ASN A 1 67  ? -15.952 82.681  129.842 1.00 60.33 ? 67   ASN A ND2 1 
ATOM   453   N  N   . ASP A 1 68  ? -11.647 82.327  126.923 1.00 59.57 ? 68   ASP A N   1 
ATOM   454   C  CA  . ASP A 1 68  ? -10.875 82.690  125.750 1.00 60.08 ? 68   ASP A CA  1 
ATOM   455   C  C   . ASP A 1 68  ? -11.071 81.660  124.646 1.00 57.33 ? 68   ASP A C   1 
ATOM   456   O  O   . ASP A 1 68  ? -10.673 81.874  123.510 1.00 60.12 ? 68   ASP A O   1 
ATOM   457   C  CB  . ASP A 1 68  ? -9.380  82.750  126.084 1.00 64.27 ? 68   ASP A CB  1 
ATOM   458   C  CG  . ASP A 1 68  ? -8.980  84.036  126.780 1.00 67.82 ? 68   ASP A CG  1 
ATOM   459   O  OD1 . ASP A 1 68  ? -9.820  84.962  126.839 1.00 72.43 ? 68   ASP A OD1 1 
ATOM   460   O  OD2 . ASP A 1 68  ? -7.819  84.119  127.251 1.00 68.56 ? 68   ASP A OD2 1 
ATOM   461   N  N   . LEU A 1 69  ? -11.690 80.543  124.983 1.00 53.43 ? 69   LEU A N   1 
ATOM   462   C  CA  . LEU A 1 69  ? -11.856 79.480  124.020 1.00 50.44 ? 69   LEU A CA  1 
ATOM   463   C  C   . LEU A 1 69  ? -13.210 79.404  123.371 1.00 49.03 ? 69   LEU A C   1 
ATOM   464   O  O   . LEU A 1 69  ? -14.231 79.598  124.028 1.00 48.71 ? 69   LEU A O   1 
ATOM   465   C  CB  . LEU A 1 69  ? -11.567 78.156  124.703 1.00 48.85 ? 69   LEU A CB  1 
ATOM   466   C  CG  . LEU A 1 69  ? -10.196 78.111  125.370 1.00 48.51 ? 69   LEU A CG  1 
ATOM   467   C  CD1 . LEU A 1 69  ? -10.088 76.884  126.284 1.00 44.06 ? 69   LEU A CD1 1 
ATOM   468   C  CD2 . LEU A 1 69  ? -9.128  78.098  124.275 1.00 42.23 ? 69   LEU A CD2 1 
ATOM   469   N  N   . THR A 1 70  ? -13.196 79.099  122.075 1.00 46.70 ? 70   THR A N   1 
ATOM   470   C  CA  . THR A 1 70  ? -14.407 78.928  121.289 1.00 43.00 ? 70   THR A CA  1 
ATOM   471   C  C   . THR A 1 70  ? -14.880 77.496  121.453 1.00 42.17 ? 70   THR A C   1 
ATOM   472   O  O   . THR A 1 70  ? -14.167 76.643  121.972 1.00 38.77 ? 70   THR A O   1 
ATOM   473   C  CB  . THR A 1 70  ? -14.150 79.125  119.821 1.00 41.66 ? 70   THR A CB  1 
ATOM   474   O  OG1 . THR A 1 70  ? -13.227 78.123  119.372 1.00 40.04 ? 70   THR A OG1 1 
ATOM   475   C  CG2 . THR A 1 70  ? -13.572 80.488  119.581 1.00 39.88 ? 70   THR A CG2 1 
ATOM   476   N  N   . ILE A 1 71  ? -16.098 77.239  121.002 1.00 45.01 ? 71   ILE A N   1 
ATOM   477   C  CA  . ILE A 1 71  ? -16.678 75.911  121.082 1.00 44.47 ? 71   ILE A CA  1 
ATOM   478   C  C   . ILE A 1 71  ? -15.665 74.864  120.602 1.00 44.78 ? 71   ILE A C   1 
ATOM   479   O  O   . ILE A 1 71  ? -15.434 73.857  121.268 1.00 46.88 ? 71   ILE A O   1 
ATOM   480   C  CB  . ILE A 1 71  ? -17.954 75.880  120.248 1.00 47.25 ? 71   ILE A CB  1 
ATOM   481   C  CG1 . ILE A 1 71  ? -19.106 76.445  121.083 1.00 54.01 ? 71   ILE A CG1 1 
ATOM   482   C  CG2 . ILE A 1 71  ? -18.250 74.486  119.758 1.00 50.91 ? 71   ILE A CG2 1 
ATOM   483   C  CD1 . ILE A 1 71  ? -20.469 76.444  120.339 1.00 59.18 ? 71   ILE A CD1 1 
ATOM   484   N  N   . GLY A 1 72  ? -15.041 75.119  119.461 1.00 42.51 ? 72   GLY A N   1 
ATOM   485   C  CA  . GLY A 1 72  ? -14.065 74.196  118.930 1.00 39.78 ? 72   GLY A CA  1 
ATOM   486   C  C   . GLY A 1 72  ? -12.769 74.150  119.706 1.00 41.21 ? 72   GLY A C   1 
ATOM   487   O  O   . GLY A 1 72  ? -12.188 73.083  119.839 1.00 44.87 ? 72   GLY A O   1 
ATOM   488   N  N   . HIS A 1 73  ? -12.285 75.295  120.182 1.00 44.35 ? 73   HIS A N   1 
ATOM   489   C  CA  . HIS A 1 73  ? -11.046 75.350  120.978 1.00 44.38 ? 73   HIS A CA  1 
ATOM   490   C  C   . HIS A 1 73  ? -11.298 74.390  122.135 1.00 43.46 ? 73   HIS A C   1 
ATOM   491   O  O   . HIS A 1 73  ? -10.544 73.461  122.395 1.00 43.35 ? 73   HIS A O   1 
ATOM   492   C  CB  . HIS A 1 73  ? -10.862 76.717  121.639 1.00 48.70 ? 73   HIS A CB  1 
ATOM   493   C  CG  . HIS A 1 73  ? -10.388 77.804  120.736 1.00 51.70 ? 73   HIS A CG  1 
ATOM   494   N  ND1 . HIS A 1 73  ? -10.627 79.139  121.008 1.00 52.34 ? 73   HIS A ND1 1 
ATOM   495   C  CD2 . HIS A 1 73  ? -9.590  77.778  119.645 1.00 52.53 ? 73   HIS A CD2 1 
ATOM   496   C  CE1 . HIS A 1 73  ? -9.992  79.886  120.124 1.00 52.94 ? 73   HIS A CE1 1 
ATOM   497   N  NE2 . HIS A 1 73  ? -9.353  79.086  119.287 1.00 54.66 ? 73   HIS A NE2 1 
ATOM   498   N  N   . LEU A 1 74  ? -12.376 74.687  122.846 1.00 39.95 ? 74   LEU A N   1 
ATOM   499   C  CA  . LEU A 1 74  ? -12.808 73.928  123.991 1.00 40.39 ? 74   LEU A CA  1 
ATOM   500   C  C   . LEU A 1 74  ? -12.751 72.442  123.692 1.00 39.28 ? 74   LEU A C   1 
ATOM   501   O  O   . LEU A 1 74  ? -12.090 71.691  124.415 1.00 42.36 ? 74   LEU A O   1 
ATOM   502   C  CB  . LEU A 1 74  ? -14.231 74.363  124.372 1.00 42.87 ? 74   LEU A CB  1 
ATOM   503   C  CG  . LEU A 1 74  ? -14.553 74.836  125.799 1.00 46.19 ? 74   LEU A CG  1 
ATOM   504   C  CD1 . LEU A 1 74  ? -13.319 75.385  126.495 1.00 47.64 ? 74   LEU A CD1 1 
ATOM   505   C  CD2 . LEU A 1 74  ? -15.643 75.915  125.725 1.00 49.28 ? 74   LEU A CD2 1 
ATOM   506   N  N   . GLY A 1 75  ? -13.430 72.016  122.629 1.00 36.84 ? 75   GLY A N   1 
ATOM   507   C  CA  . GLY A 1 75  ? -13.429 70.605  122.286 1.00 34.15 ? 75   GLY A CA  1 
ATOM   508   C  C   . GLY A 1 75  ? -12.011 70.069  122.132 1.00 35.51 ? 75   GLY A C   1 
ATOM   509   O  O   . GLY A 1 75  ? -11.645 69.030  122.694 1.00 36.44 ? 75   GLY A O   1 
ATOM   510   N  N   . LEU A 1 76  ? -11.201 70.787  121.364 1.00 32.03 ? 76   LEU A N   1 
ATOM   511   C  CA  . LEU A 1 76  ? -9.832  70.387  121.124 1.00 30.96 ? 76   LEU A CA  1 
ATOM   512   C  C   . LEU A 1 76  ? -9.030  70.314  122.428 1.00 32.36 ? 76   LEU A C   1 
ATOM   513   O  O   . LEU A 1 76  ? -8.258  69.371  122.668 1.00 29.40 ? 76   LEU A O   1 
ATOM   514   C  CB  . LEU A 1 76  ? -9.193  71.375  120.148 1.00 35.02 ? 76   LEU A CB  1 
ATOM   515   C  CG  . LEU A 1 76  ? -8.851  70.995  118.680 1.00 38.77 ? 76   LEU A CG  1 
ATOM   516   C  CD1 . LEU A 1 76  ? -9.420  69.684  118.253 1.00 34.90 ? 76   LEU A CD1 1 
ATOM   517   C  CD2 . LEU A 1 76  ? -9.349  72.096  117.776 1.00 36.38 ? 76   LEU A CD2 1 
ATOM   518   N  N   . THR A 1 77  ? -9.222  71.302  123.286 1.00 32.29 ? 77   THR A N   1 
ATOM   519   C  CA  . THR A 1 77  ? -8.500  71.348  124.540 1.00 33.64 ? 77   THR A CA  1 
ATOM   520   C  C   . THR A 1 77  ? -8.899  70.232  125.513 1.00 35.20 ? 77   THR A C   1 
ATOM   521   O  O   . THR A 1 77  ? -8.054  69.728  126.273 1.00 32.54 ? 77   THR A O   1 
ATOM   522   C  CB  . THR A 1 77  ? -8.719  72.687  125.193 1.00 35.25 ? 77   THR A CB  1 
ATOM   523   O  OG1 . THR A 1 77  ? -8.387  73.698  124.236 1.00 39.18 ? 77   THR A OG1 1 
ATOM   524   C  CG2 . THR A 1 77  ? -7.847  72.836  126.500 1.00 33.77 ? 77   THR A CG2 1 
ATOM   525   N  N   . ILE A 1 78  ? -10.181 69.868  125.513 1.00 34.16 ? 78   ILE A N   1 
ATOM   526   C  CA  . ILE A 1 78  ? -10.650 68.789  126.362 1.00 35.62 ? 78   ILE A CA  1 
ATOM   527   C  C   . ILE A 1 78  ? -9.976  67.478  125.889 1.00 41.24 ? 78   ILE A C   1 
ATOM   528   O  O   . ILE A 1 78  ? -9.440  66.677  126.704 1.00 44.39 ? 78   ILE A O   1 
ATOM   529   C  CB  . ILE A 1 78  ? -12.176 68.701  126.288 1.00 36.48 ? 78   ILE A CB  1 
ATOM   530   C  CG1 . ILE A 1 78  ? -12.763 69.886  127.083 1.00 33.62 ? 78   ILE A CG1 1 
ATOM   531   C  CG2 . ILE A 1 78  ? -12.668 67.330  126.775 1.00 29.92 ? 78   ILE A CG2 1 
ATOM   532   C  CD1 . ILE A 1 78  ? -14.259 70.098  126.911 1.00 28.62 ? 78   ILE A CD1 1 
ATOM   533   N  N   . MET A 1 79  ? -9.951  67.271  124.579 1.00 37.52 ? 79   MET A N   1 
ATOM   534   C  CA  . MET A 1 79  ? -9.307  66.074  124.074 1.00 39.77 ? 79   MET A CA  1 
ATOM   535   C  C   . MET A 1 79  ? -7.794  66.091  124.320 1.00 37.25 ? 79   MET A C   1 
ATOM   536   O  O   . MET A 1 79  ? -7.201  65.062  124.605 1.00 38.31 ? 79   MET A O   1 
ATOM   537   C  CB  . MET A 1 79  ? -9.603  65.894  122.575 1.00 38.65 ? 79   MET A CB  1 
ATOM   538   C  CG  . MET A 1 79  ? -11.055 65.471  122.297 1.00 37.29 ? 79   MET A CG  1 
ATOM   539   S  SD  . MET A 1 79  ? -11.265 65.019  120.587 1.00 39.53 ? 79   MET A SD  1 
ATOM   540   C  CE  . MET A 1 79  ? -11.241 66.655  119.828 1.00 32.87 ? 79   MET A CE  1 
ATOM   541   N  N   . ALA A 1 80  ? -7.167  67.254  124.210 1.00 36.40 ? 80   ALA A N   1 
ATOM   542   C  CA  . ALA A 1 80  ? -5.727  67.311  124.406 1.00 35.30 ? 80   ALA A CA  1 
ATOM   543   C  C   . ALA A 1 80  ? -5.396  66.936  125.839 1.00 33.31 ? 80   ALA A C   1 
ATOM   544   O  O   . ALA A 1 80  ? -4.510  66.113  126.069 1.00 30.40 ? 80   ALA A O   1 
ATOM   545   C  CB  . ALA A 1 80  ? -5.188  68.706  124.083 1.00 33.52 ? 80   ALA A CB  1 
ATOM   546   N  N   . LEU A 1 81  ? -6.106  67.544  126.795 1.00 31.90 ? 81   LEU A N   1 
ATOM   547   C  CA  . LEU A 1 81  ? -5.870  67.242  128.200 1.00 33.03 ? 81   LEU A CA  1 
ATOM   548   C  C   . LEU A 1 81  ? -6.094  65.749  128.412 1.00 32.20 ? 81   LEU A C   1 
ATOM   549   O  O   . LEU A 1 81  ? -5.213  65.042  128.909 1.00 30.82 ? 81   LEU A O   1 
ATOM   550   C  CB  . LEU A 1 81  ? -6.776  68.087  129.105 1.00 31.97 ? 81   LEU A CB  1 
ATOM   551   C  CG  . LEU A 1 81  ? -6.379  69.570  129.051 1.00 29.99 ? 81   LEU A CG  1 
ATOM   552   C  CD1 . LEU A 1 81  ? -7.159  70.403  130.028 1.00 29.30 ? 81   LEU A CD1 1 
ATOM   553   C  CD2 . LEU A 1 81  ? -4.927  69.685  129.387 1.00 32.55 ? 81   LEU A CD2 1 
ATOM   554   N  N   . THR A 1 82  ? -7.250  65.250  128.004 1.00 32.42 ? 82   THR A N   1 
ATOM   555   C  CA  . THR A 1 82  ? -7.500  63.826  128.157 1.00 33.69 ? 82   THR A CA  1 
ATOM   556   C  C   . THR A 1 82  ? -6.345  62.944  127.627 1.00 33.94 ? 82   THR A C   1 
ATOM   557   O  O   . THR A 1 82  ? -5.945  61.976  128.288 1.00 31.30 ? 82   THR A O   1 
ATOM   558   C  CB  . THR A 1 82  ? -8.807  63.482  127.477 1.00 33.30 ? 82   THR A CB  1 
ATOM   559   O  OG1 . THR A 1 82  ? -9.834  64.257  128.111 1.00 40.05 ? 82   THR A OG1 1 
ATOM   560   C  CG2 . THR A 1 82  ? -9.138  62.015  127.623 1.00 32.40 ? 82   THR A CG2 1 
ATOM   561   N  N   . SER A 1 83  ? -5.798  63.290  126.459 1.00 32.68 ? 83   SER A N   1 
ATOM   562   C  CA  . SER A 1 83  ? -4.701  62.525  125.860 1.00 33.82 ? 83   SER A CA  1 
ATOM   563   C  C   . SER A 1 83  ? -3.437  62.627  126.706 1.00 34.88 ? 83   SER A C   1 
ATOM   564   O  O   . SER A 1 83  ? -2.486  61.875  126.500 1.00 34.02 ? 83   SER A O   1 
ATOM   565   C  CB  . SER A 1 83  ? -4.392  63.017  124.436 1.00 32.66 ? 83   SER A CB  1 
ATOM   566   O  OG  . SER A 1 83  ? -3.574  64.184  124.444 1.00 36.28 ? 83   SER A OG  1 
ATOM   567   N  N   . SER A 1 84  ? -3.418  63.584  127.631 1.00 36.51 ? 84   SER A N   1 
ATOM   568   C  CA  . SER A 1 84  ? -2.278  63.748  128.531 1.00 38.20 ? 84   SER A CA  1 
ATOM   569   C  C   . SER A 1 84  ? -2.641  63.197  129.898 1.00 39.22 ? 84   SER A C   1 
ATOM   570   O  O   . SER A 1 84  ? -1.886  63.377  130.849 1.00 40.97 ? 84   SER A O   1 
ATOM   571   C  CB  . SER A 1 84  ? -1.886  65.217  128.670 1.00 37.08 ? 84   SER A CB  1 
ATOM   572   O  OG  . SER A 1 84  ? -1.029  65.633  127.621 1.00 42.37 ? 84   SER A OG  1 
ATOM   573   N  N   . CYS A 1 85  ? -3.784  62.510  129.967 1.00 37.12 ? 85   CYS A N   1 
ATOM   574   C  CA  . CYS A 1 85  ? -4.300  61.929  131.191 1.00 39.68 ? 85   CYS A CA  1 
ATOM   575   C  C   . CYS A 1 85  ? -4.490  62.964  132.286 1.00 43.73 ? 85   CYS A C   1 
ATOM   576   O  O   . CYS A 1 85  ? -4.133  62.736  133.454 1.00 43.63 ? 85   CYS A O   1 
ATOM   577   C  CB  . CYS A 1 85  ? -3.389  60.816  131.688 1.00 41.88 ? 85   CYS A CB  1 
ATOM   578   S  SG  . CYS A 1 85  ? -3.214  59.428  130.529 1.00 47.46 ? 85   CYS A SG  1 
ATOM   579   N  N   . ARG A 1 86  ? -5.062  64.101  131.897 1.00 44.84 ? 86   ARG A N   1 
ATOM   580   C  CA  . ARG A 1 86  ? -5.343  65.205  132.805 1.00 43.62 ? 86   ARG A CA  1 
ATOM   581   C  C   . ARG A 1 86  ? -6.837  65.487  132.845 1.00 44.19 ? 86   ARG A C   1 
ATOM   582   O  O   . ARG A 1 86  ? -7.511  65.464  131.820 1.00 48.26 ? 86   ARG A O   1 
ATOM   583   C  CB  . ARG A 1 86  ? -4.611  66.439  132.319 1.00 44.83 ? 86   ARG A CB  1 
ATOM   584   C  CG  . ARG A 1 86  ? -3.157  66.434  132.642 1.00 45.99 ? 86   ARG A CG  1 
ATOM   585   C  CD  . ARG A 1 86  ? -2.984  66.908  134.056 1.00 47.34 ? 86   ARG A CD  1 
ATOM   586   N  NE  . ARG A 1 86  ? -1.588  66.888  134.438 1.00 51.40 ? 86   ARG A NE  1 
ATOM   587   C  CZ  . ARG A 1 86  ? -1.156  67.237  135.641 1.00 53.00 ? 86   ARG A CZ  1 
ATOM   588   N  NH1 . ARG A 1 86  ? -2.034  67.636  136.550 1.00 52.98 ? 86   ARG A NH1 1 
ATOM   589   N  NH2 . ARG A 1 86  ? 0.140   67.164  135.939 1.00 47.94 ? 86   ARG A NH2 1 
ATOM   590   N  N   . ASP A 1 87  ? -7.357  65.764  134.027 1.00 46.38 ? 87   ASP A N   1 
ATOM   591   C  CA  . ASP A 1 87  ? -8.773  66.056  134.175 1.00 45.87 ? 87   ASP A CA  1 
ATOM   592   C  C   . ASP A 1 87  ? -8.983  67.401  133.505 1.00 45.12 ? 87   ASP A C   1 
ATOM   593   O  O   . ASP A 1 87  ? -8.189  68.315  133.692 1.00 45.53 ? 87   ASP A O   1 
ATOM   594   C  CB  . ASP A 1 87  ? -9.131  66.132  135.656 1.00 47.38 ? 87   ASP A CB  1 
ATOM   595   C  CG  . ASP A 1 87  ? -10.629 66.219  135.911 1.00 51.51 ? 87   ASP A CG  1 
ATOM   596   O  OD1 . ASP A 1 87  ? -11.425 66.406  134.971 1.00 55.49 ? 87   ASP A OD1 1 
ATOM   597   O  OD2 . ASP A 1 87  ? -11.011 66.111  137.090 1.00 53.46 ? 87   ASP A OD2 1 
ATOM   598   N  N   . PRO A 1 88  ? -10.020 67.511  132.667 1.00 46.35 ? 88   PRO A N   1 
ATOM   599   C  CA  . PRO A 1 88  ? -10.387 68.725  131.932 1.00 46.78 ? 88   PRO A CA  1 
ATOM   600   C  C   . PRO A 1 88  ? -11.287 69.546  132.821 1.00 48.42 ? 88   PRO A C   1 
ATOM   601   O  O   . PRO A 1 88  ? -11.441 70.751  132.653 1.00 49.36 ? 88   PRO A O   1 
ATOM   602   C  CB  . PRO A 1 88  ? -11.160 68.193  130.741 1.00 46.27 ? 88   PRO A CB  1 
ATOM   603   C  CG  . PRO A 1 88  ? -10.776 66.732  130.670 1.00 49.15 ? 88   PRO A CG  1 
ATOM   604   C  CD  . PRO A 1 88  ? -10.706 66.345  132.093 1.00 47.57 ? 88   PRO A CD  1 
ATOM   605   N  N   . GLY A 1 89  ? -11.885 68.858  133.779 1.00 50.08 ? 89   GLY A N   1 
ATOM   606   C  CA  . GLY A 1 89  ? -12.794 69.492  134.706 1.00 50.23 ? 89   GLY A CA  1 
ATOM   607   C  C   . GLY A 1 89  ? -13.710 70.531  134.104 1.00 50.22 ? 89   GLY A C   1 
ATOM   608   O  O   . GLY A 1 89  ? -14.478 70.306  133.169 1.00 54.23 ? 89   GLY A O   1 
ATOM   609   N  N   . ASP A 1 90  ? -13.623 71.689  134.710 1.00 49.60 ? 90   ASP A N   1 
ATOM   610   C  CA  . ASP A 1 90  ? -14.362 72.879  134.362 1.00 48.74 ? 90   ASP A CA  1 
ATOM   611   C  C   . ASP A 1 90  ? -14.845 72.996  132.906 1.00 48.27 ? 90   ASP A C   1 
ATOM   612   O  O   . ASP A 1 90  ? -16.027 73.249  132.628 1.00 46.94 ? 90   ASP A O   1 
ATOM   613   C  CB  . ASP A 1 90  ? -13.430 74.033  134.691 1.00 53.38 ? 90   ASP A CB  1 
ATOM   614   C  CG  . ASP A 1 90  ? -14.145 75.247  135.108 1.00 57.01 ? 90   ASP A CG  1 
ATOM   615   O  OD1 . ASP A 1 90  ? -15.216 75.105  135.740 1.00 61.37 ? 90   ASP A OD1 1 
ATOM   616   O  OD2 . ASP A 1 90  ? -13.617 76.342  134.818 1.00 60.84 ? 90   ASP A OD2 1 
ATOM   617   N  N   . LYS A 1 91  ? -13.905 72.836  131.981 1.00 47.19 ? 91   LYS A N   1 
ATOM   618   C  CA  . LYS A 1 91  ? -14.174 72.969  130.553 1.00 42.69 ? 91   LYS A CA  1 
ATOM   619   C  C   . LYS A 1 91  ? -15.280 72.105  129.976 1.00 41.68 ? 91   LYS A C   1 
ATOM   620   O  O   . LYS A 1 91  ? -15.983 72.548  129.065 1.00 41.05 ? 91   LYS A O   1 
ATOM   621   C  CB  . LYS A 1 91  ? -12.898 72.732  129.764 1.00 38.76 ? 91   LYS A CB  1 
ATOM   622   C  CG  . LYS A 1 91  ? -11.683 73.125  130.521 1.00 40.90 ? 91   LYS A CG  1 
ATOM   623   C  CD  . LYS A 1 91  ? -10.632 73.755  129.646 1.00 39.79 ? 91   LYS A CD  1 
ATOM   624   C  CE  . LYS A 1 91  ? -9.474  74.225  130.516 1.00 42.68 ? 91   LYS A CE  1 
ATOM   625   N  NZ  . LYS A 1 91  ? -8.832  75.391  129.927 1.00 42.61 ? 91   LYS A NZ  1 
ATOM   626   N  N   . VAL A 1 92  ? -15.451 70.886  130.474 1.00 39.83 ? 92   VAL A N   1 
ATOM   627   C  CA  . VAL A 1 92  ? -16.502 70.043  129.927 1.00 39.47 ? 92   VAL A CA  1 
ATOM   628   C  C   . VAL A 1 92  ? -17.899 70.578  130.268 1.00 42.92 ? 92   VAL A C   1 
ATOM   629   O  O   . VAL A 1 92  ? -18.810 70.554  129.409 1.00 41.76 ? 92   VAL A O   1 
ATOM   630   C  CB  . VAL A 1 92  ? -16.341 68.631  130.408 1.00 39.77 ? 92   VAL A CB  1 
ATOM   631   C  CG1 . VAL A 1 92  ? -17.479 67.771  129.891 1.00 41.93 ? 92   VAL A CG1 1 
ATOM   632   C  CG2 . VAL A 1 92  ? -15.005 68.108  129.941 1.00 40.95 ? 92   VAL A CG2 1 
ATOM   633   N  N   . SER A 1 93  ? -18.061 71.076  131.500 1.00 43.70 ? 93   SER A N   1 
ATOM   634   C  CA  . SER A 1 93  ? -19.342 71.654  131.955 1.00 45.52 ? 93   SER A CA  1 
ATOM   635   C  C   . SER A 1 93  ? -19.651 72.881  131.109 1.00 43.96 ? 93   SER A C   1 
ATOM   636   O  O   . SER A 1 93  ? -20.739 73.049  130.582 1.00 39.63 ? 93   SER A O   1 
ATOM   637   C  CB  . SER A 1 93  ? -19.250 72.103  133.418 1.00 48.70 ? 93   SER A CB  1 
ATOM   638   O  OG  . SER A 1 93  ? -19.121 70.996  134.305 1.00 58.25 ? 93   SER A OG  1 
ATOM   639   N  N   . ILE A 1 94  ? -18.655 73.737  130.990 1.00 43.55 ? 94   ILE A N   1 
ATOM   640   C  CA  . ILE A 1 94  ? -18.792 74.947  130.234 1.00 44.92 ? 94   ILE A CA  1 
ATOM   641   C  C   . ILE A 1 94  ? -19.155 74.605  128.795 1.00 47.83 ? 94   ILE A C   1 
ATOM   642   O  O   . ILE A 1 94  ? -20.091 75.186  128.234 1.00 47.64 ? 94   ILE A O   1 
ATOM   643   C  CB  . ILE A 1 94  ? -17.484 75.746  130.337 1.00 46.89 ? 94   ILE A CB  1 
ATOM   644   C  CG1 . ILE A 1 94  ? -17.245 76.066  131.816 1.00 47.96 ? 94   ILE A CG1 1 
ATOM   645   C  CG2 . ILE A 1 94  ? -17.548 77.026  129.501 1.00 44.20 ? 94   ILE A CG2 1 
ATOM   646   C  CD1 . ILE A 1 94  ? -15.928 76.747  132.130 1.00 53.52 ? 94   ILE A CD1 1 
ATOM   647   N  N   . LEU A 1 95  ? -18.450 73.638  128.200 1.00 47.97 ? 95   LEU A N   1 
ATOM   648   C  CA  . LEU A 1 95  ? -18.729 73.253  126.806 1.00 45.41 ? 95   LEU A CA  1 
ATOM   649   C  C   . LEU A 1 95  ? -20.136 72.683  126.637 1.00 43.39 ? 95   LEU A C   1 
ATOM   650   O  O   . LEU A 1 95  ? -20.843 73.052  125.707 1.00 40.77 ? 95   LEU A O   1 
ATOM   651   C  CB  . LEU A 1 95  ? -17.695 72.235  126.299 1.00 41.73 ? 95   LEU A CB  1 
ATOM   652   C  CG  . LEU A 1 95  ? -17.868 71.683  124.868 1.00 40.12 ? 95   LEU A CG  1 
ATOM   653   C  CD1 . LEU A 1 95  ? -17.882 72.817  123.844 1.00 38.33 ? 95   LEU A CD1 1 
ATOM   654   C  CD2 . LEU A 1 95  ? -16.736 70.735  124.561 1.00 37.41 ? 95   LEU A CD2 1 
ATOM   655   N  N   . GLN A 1 96  ? -20.526 71.782  127.532 1.00 43.31 ? 96   GLN A N   1 
ATOM   656   C  CA  . GLN A 1 96  ? -21.849 71.168  127.485 1.00 47.35 ? 96   GLN A CA  1 
ATOM   657   C  C   . GLN A 1 96  ? -22.973 72.236  127.435 1.00 49.31 ? 96   GLN A C   1 
ATOM   658   O  O   . GLN A 1 96  ? -23.900 72.162  126.605 1.00 47.21 ? 96   GLN A O   1 
ATOM   659   C  CB  . GLN A 1 96  ? -22.016 70.243  128.709 1.00 48.47 ? 96   GLN A CB  1 
ATOM   660   C  CG  . GLN A 1 96  ? -23.333 69.465  128.812 1.00 60.31 ? 96   GLN A CG  1 
ATOM   661   C  CD  . GLN A 1 96  ? -23.592 68.439  127.668 1.00 67.41 ? 96   GLN A CD  1 
ATOM   662   O  OE1 . GLN A 1 96  ? -22.746 67.578  127.354 1.00 68.76 ? 96   GLN A OE1 1 
ATOM   663   N  NE2 . GLN A 1 96  ? -24.782 68.523  127.067 1.00 65.98 ? 96   GLN A NE2 1 
ATOM   664   N  N   . ARG A 1 97  ? -22.887 73.250  128.293 1.00 50.42 ? 97   ARG A N   1 
ATOM   665   C  CA  . ARG A 1 97  ? -23.925 74.266  128.293 1.00 50.20 ? 97   ARG A CA  1 
ATOM   666   C  C   . ARG A 1 97  ? -23.807 75.198  127.086 1.00 46.16 ? 97   ARG A C   1 
ATOM   667   O  O   . ARG A 1 97  ? -24.800 75.714  126.580 1.00 46.18 ? 97   ARG A O   1 
ATOM   668   C  CB  . ARG A 1 97  ? -23.952 75.040  129.636 1.00 55.17 ? 97   ARG A CB  1 
ATOM   669   C  CG  . ARG A 1 97  ? -23.061 76.264  129.770 1.00 63.30 ? 97   ARG A CG  1 
ATOM   670   C  CD  . ARG A 1 97  ? -23.336 76.974  131.119 1.00 70.91 ? 97   ARG A CD  1 
ATOM   671   N  NE  . ARG A 1 97  ? -22.754 76.275  132.269 1.00 74.32 ? 97   ARG A NE  1 
ATOM   672   C  CZ  . ARG A 1 97  ? -21.568 76.569  132.808 1.00 74.38 ? 97   ARG A CZ  1 
ATOM   673   N  NH1 . ARG A 1 97  ? -20.836 77.558  132.311 1.00 74.57 ? 97   ARG A NH1 1 
ATOM   674   N  NH2 . ARG A 1 97  ? -21.096 75.853  133.824 1.00 74.72 ? 97   ARG A NH2 1 
ATOM   675   N  N   . GLN A 1 98  ? -22.615 75.419  126.581 1.00 43.11 ? 98   GLN A N   1 
ATOM   676   C  CA  . GLN A 1 98  ? -22.571 76.287  125.418 1.00 46.14 ? 98   GLN A CA  1 
ATOM   677   C  C   . GLN A 1 98  ? -23.205 75.569  124.240 1.00 48.80 ? 98   GLN A C   1 
ATOM   678   O  O   . GLN A 1 98  ? -23.869 76.198  123.419 1.00 48.19 ? 98   GLN A O   1 
ATOM   679   C  CB  . GLN A 1 98  ? -21.141 76.685  125.061 1.00 43.17 ? 98   GLN A CB  1 
ATOM   680   C  CG  . GLN A 1 98  ? -20.574 77.662  126.009 1.00 39.69 ? 98   GLN A CG  1 
ATOM   681   C  CD  . GLN A 1 98  ? -19.171 78.046  125.661 1.00 44.39 ? 98   GLN A CD  1 
ATOM   682   O  OE1 . GLN A 1 98  ? -18.475 78.665  126.468 1.00 43.89 ? 98   GLN A OE1 1 
ATOM   683   N  NE2 . GLN A 1 98  ? -18.738 77.694  124.451 1.00 43.88 ? 98   GLN A NE2 1 
ATOM   684   N  N   . MET A 1 99  ? -22.988 74.253  124.162 1.00 49.65 ? 99   MET A N   1 
ATOM   685   C  CA  . MET A 1 99  ? -23.533 73.443  123.085 1.00 52.18 ? 99   MET A CA  1 
ATOM   686   C  C   . MET A 1 99  ? -25.044 73.287  123.138 1.00 55.29 ? 99   MET A C   1 
ATOM   687   O  O   . MET A 1 99  ? -25.700 73.203  122.102 1.00 56.31 ? 99   MET A O   1 
ATOM   688   C  CB  . MET A 1 99  ? -22.895 72.054  123.074 1.00 49.96 ? 99   MET A CB  1 
ATOM   689   C  CG  . MET A 1 99  ? -21.507 72.017  122.488 1.00 50.20 ? 99   MET A CG  1 
ATOM   690   S  SD  . MET A 1 99  ? -21.442 72.810  120.868 1.00 52.76 ? 99   MET A SD  1 
ATOM   691   C  CE  . MET A 1 99  ? -22.662 71.845  119.972 1.00 43.98 ? 99   MET A CE  1 
ATOM   692   N  N   . GLU A 1 100 ? -25.613 73.229  124.332 1.00 58.76 ? 100  GLU A N   1 
ATOM   693   C  CA  . GLU A 1 100 ? -27.059 73.079  124.409 1.00 62.36 ? 100  GLU A CA  1 
ATOM   694   C  C   . GLU A 1 100 ? -27.664 74.364  123.893 1.00 62.41 ? 100  GLU A C   1 
ATOM   695   O  O   . GLU A 1 100 ? -28.846 74.417  123.567 1.00 64.90 ? 100  GLU A O   1 
ATOM   696   C  CB  . GLU A 1 100 ? -27.484 72.801  125.853 1.00 61.23 ? 100  GLU A CB  1 
ATOM   697   C  CG  . GLU A 1 100 ? -26.840 71.520  126.370 1.00 67.59 ? 100  GLU A CG  1 
ATOM   698   C  CD  . GLU A 1 100 ? -27.098 71.228  127.848 1.00 71.14 ? 100  GLU A CD  1 
ATOM   699   O  OE1 . GLU A 1 100 ? -27.093 72.180  128.669 1.00 73.83 ? 100  GLU A OE1 1 
ATOM   700   O  OE2 . GLU A 1 100 ? -27.277 70.033  128.189 1.00 69.20 ? 100  GLU A OE2 1 
ATOM   701   N  N   . ASN A 1 101 ? -26.812 75.376  123.766 1.00 61.60 ? 101  ASN A N   1 
ATOM   702   C  CA  . ASN A 1 101 ? -27.200 76.714  123.336 1.00 61.95 ? 101  ASN A CA  1 
ATOM   703   C  C   . ASN A 1 101 ? -26.761 77.035  121.932 1.00 61.27 ? 101  ASN A C   1 
ATOM   704   O  O   . ASN A 1 101 ? -26.945 78.150  121.453 1.00 62.70 ? 101  ASN A O   1 
ATOM   705   C  CB  . ASN A 1 101 ? -26.567 77.732  124.280 1.00 66.00 ? 101  ASN A CB  1 
ATOM   706   C  CG  . ASN A 1 101 ? -27.572 78.622  124.914 1.00 69.15 ? 101  ASN A CG  1 
ATOM   707   O  OD1 . ASN A 1 101 ? -27.955 79.649  124.346 1.00 77.43 ? 101  ASN A OD1 1 
ATOM   708   N  ND2 . ASN A 1 101 ? -28.038 78.232  126.095 1.00 67.52 ? 101  ASN A ND2 1 
ATOM   709   N  N   . TRP A 1 102 ? -26.150 76.066  121.275 1.00 60.32 ? 102  TRP A N   1 
ATOM   710   C  CA  . TRP A 1 102 ? -25.666 76.292  119.931 1.00 56.28 ? 102  TRP A CA  1 
ATOM   711   C  C   . TRP A 1 102 ? -26.663 75.940  118.830 1.00 57.26 ? 102  TRP A C   1 
ATOM   712   O  O   . TRP A 1 102 ? -27.485 75.031  118.966 1.00 58.92 ? 102  TRP A O   1 
ATOM   713   C  CB  . TRP A 1 102 ? -24.378 75.506  119.708 1.00 49.64 ? 102  TRP A CB  1 
ATOM   714   C  CG  . TRP A 1 102 ? -23.913 75.599  118.295 1.00 45.20 ? 102  TRP A CG  1 
ATOM   715   C  CD1 . TRP A 1 102 ? -23.102 76.554  117.765 1.00 43.43 ? 102  TRP A CD1 1 
ATOM   716   C  CD2 . TRP A 1 102 ? -24.294 74.744  117.207 1.00 41.17 ? 102  TRP A CD2 1 
ATOM   717   N  NE1 . TRP A 1 102 ? -22.953 76.352  116.412 1.00 41.71 ? 102  TRP A NE1 1 
ATOM   718   C  CE2 . TRP A 1 102 ? -23.673 75.250  116.041 1.00 40.24 ? 102  TRP A CE2 1 
ATOM   719   C  CE3 . TRP A 1 102 ? -25.104 73.608  117.103 1.00 40.95 ? 102  TRP A CE3 1 
ATOM   720   C  CZ2 . TRP A 1 102 ? -23.829 74.658  114.779 1.00 37.68 ? 102  TRP A CZ2 1 
ATOM   721   C  CZ3 . TRP A 1 102 ? -25.264 73.007  115.829 1.00 41.13 ? 102  TRP A CZ3 1 
ATOM   722   C  CH2 . TRP A 1 102 ? -24.623 73.544  114.690 1.00 35.72 ? 102  TRP A CH2 1 
ATOM   723   N  N   . ALA A 1 103 ? -26.561 76.673  117.730 1.00 57.55 ? 103  ALA A N   1 
ATOM   724   C  CA  . ALA A 1 103 ? -27.398 76.467  116.559 1.00 57.23 ? 103  ALA A CA  1 
ATOM   725   C  C   . ALA A 1 103 ? -26.719 77.248  115.452 1.00 56.89 ? 103  ALA A C   1 
ATOM   726   O  O   . ALA A 1 103 ? -26.025 78.232  115.712 1.00 58.28 ? 103  ALA A O   1 
ATOM   727   C  CB  . ALA A 1 103 ? -28.793 77.006  116.799 1.00 56.22 ? 103  ALA A CB  1 
ATOM   728   N  N   . PRO A 1 104 ? -26.879 76.811  114.201 1.00 57.23 ? 104  PRO A N   1 
ATOM   729   C  CA  . PRO A 1 104 ? -26.226 77.565  113.122 1.00 58.14 ? 104  PRO A CA  1 
ATOM   730   C  C   . PRO A 1 104 ? -26.928 78.898  112.874 1.00 60.57 ? 104  PRO A C   1 
ATOM   731   O  O   . PRO A 1 104 ? -28.096 79.076  113.259 1.00 60.25 ? 104  PRO A O   1 
ATOM   732   C  CB  . PRO A 1 104 ? -26.308 76.609  111.934 1.00 54.62 ? 104  PRO A CB  1 
ATOM   733   C  CG  . PRO A 1 104 ? -27.523 75.799  112.226 1.00 52.20 ? 104  PRO A CG  1 
ATOM   734   C  CD  . PRO A 1 104 ? -27.489 75.566  113.704 1.00 54.25 ? 104  PRO A CD  1 
ATOM   735   N  N   . SER A 1 105 ? -26.219 79.836  112.250 1.00 63.47 ? 105  SER A N   1 
ATOM   736   C  CA  . SER A 1 105 ? -26.799 81.155  111.965 1.00 65.13 ? 105  SER A CA  1 
ATOM   737   C  C   . SER A 1 105 ? -28.066 81.063  111.085 1.00 62.61 ? 105  SER A C   1 
ATOM   738   O  O   . SER A 1 105 ? -29.011 81.841  111.235 1.00 60.05 ? 105  SER A O   1 
ATOM   739   C  CB  . SER A 1 105 ? -25.738 82.080  111.325 1.00 65.90 ? 105  SER A CB  1 
ATOM   740   O  OG  . SER A 1 105 ? -24.972 81.425  110.319 1.00 71.75 ? 105  SER A OG  1 
ATOM   741   N  N   . SER A 1 106 ? -28.100 80.092  110.188 1.00 60.44 ? 106  SER A N   1 
ATOM   742   C  CA  . SER A 1 106 ? -29.260 79.925  109.326 1.00 60.60 ? 106  SER A CA  1 
ATOM   743   C  C   . SER A 1 106 ? -29.148 78.557  108.657 1.00 61.96 ? 106  SER A C   1 
ATOM   744   O  O   . SER A 1 106 ? -28.139 77.866  108.815 1.00 63.00 ? 106  SER A O   1 
ATOM   745   C  CB  . SER A 1 106 ? -29.290 81.016  108.261 1.00 60.40 ? 106  SER A CB  1 
ATOM   746   O  OG  . SER A 1 106 ? -28.479 80.663  107.151 1.00 57.31 ? 106  SER A OG  1 
ATOM   747   N  N   . PRO A 1 107 ? -30.184 78.135  107.913 1.00 62.29 ? 107  PRO A N   1 
ATOM   748   C  CA  . PRO A 1 107 ? -30.135 76.825  107.241 1.00 61.53 ? 107  PRO A CA  1 
ATOM   749   C  C   . PRO A 1 107 ? -29.287 76.813  105.974 1.00 63.40 ? 107  PRO A C   1 
ATOM   750   O  O   . PRO A 1 107 ? -29.102 75.764  105.354 1.00 63.62 ? 107  PRO A O   1 
ATOM   751   C  CB  . PRO A 1 107 ? -31.602 76.513  106.971 1.00 58.84 ? 107  PRO A CB  1 
ATOM   752   C  CG  . PRO A 1 107 ? -32.218 77.859  106.845 1.00 61.24 ? 107  PRO A CG  1 
ATOM   753   C  CD  . PRO A 1 107 ? -31.553 78.672  107.916 1.00 61.01 ? 107  PRO A CD  1 
ATOM   754   N  N   . ASN A 1 108 ? -28.765 77.982  105.604 1.00 65.07 ? 108  ASN A N   1 
ATOM   755   C  CA  . ASN A 1 108 ? -27.921 78.116  104.415 1.00 63.84 ? 108  ASN A CA  1 
ATOM   756   C  C   . ASN A 1 108 ? -26.497 78.477  104.810 1.00 61.58 ? 108  ASN A C   1 
ATOM   757   O  O   . ASN A 1 108 ? -25.673 78.834  103.956 1.00 60.63 ? 108  ASN A O   1 
ATOM   758   C  CB  . ASN A 1 108 ? -28.491 79.200  103.497 1.00 66.82 ? 108  ASN A CB  1 
ATOM   759   C  CG  . ASN A 1 108 ? -29.833 78.815  102.926 1.00 69.74 ? 108  ASN A CG  1 
ATOM   760   O  OD1 . ASN A 1 108 ? -30.782 79.619  102.927 1.00 73.65 ? 108  ASN A OD1 1 
ATOM   761   N  ND2 . ASN A 1 108 ? -29.928 77.573  102.431 1.00 64.16 ? 108  ASN A ND2 1 
ATOM   762   N  N   . ALA A 1 109 ? -26.223 78.394  106.112 1.00 58.82 ? 109  ALA A N   1 
ATOM   763   C  CA  . ALA A 1 109 ? -24.906 78.703  106.652 1.00 55.19 ? 109  ALA A CA  1 
ATOM   764   C  C   . ALA A 1 109 ? -23.869 77.791  105.992 1.00 52.09 ? 109  ALA A C   1 
ATOM   765   O  O   . ALA A 1 109 ? -24.160 76.613  105.691 1.00 47.06 ? 109  ALA A O   1 
ATOM   766   C  CB  . ALA A 1 109 ? -24.910 78.501  108.163 1.00 57.13 ? 109  ALA A CB  1 
ATOM   767   N  N   . GLU A 1 110 ? -22.674 78.344  105.776 1.00 47.89 ? 110  GLU A N   1 
ATOM   768   C  CA  . GLU A 1 110 ? -21.555 77.640  105.141 1.00 47.44 ? 110  GLU A CA  1 
ATOM   769   C  C   . GLU A 1 110 ? -21.214 76.332  105.856 1.00 46.73 ? 110  GLU A C   1 
ATOM   770   O  O   . GLU A 1 110 ? -21.334 76.232  107.087 1.00 48.06 ? 110  GLU A O   1 
ATOM   771   C  CB  . GLU A 1 110 ? -20.315 78.554  105.108 1.00 50.03 ? 110  GLU A CB  1 
ATOM   772   C  CG  . GLU A 1 110 ? -19.574 78.730  106.444 1.00 55.40 ? 110  GLU A CG  1 
ATOM   773   C  CD  . GLU A 1 110 ? -20.309 79.594  107.464 1.00 58.05 ? 110  GLU A CD  1 
ATOM   774   O  OE1 . GLU A 1 110 ? -21.525 79.858  107.306 1.00 59.05 ? 110  GLU A OE1 1 
ATOM   775   O  OE2 . GLU A 1 110 ? -19.658 79.999  108.452 1.00 61.58 ? 110  GLU A OE2 1 
ATOM   776   N  N   . ALA A 1 111 ? -20.774 75.336  105.095 1.00 43.31 ? 111  ALA A N   1 
ATOM   777   C  CA  . ALA A 1 111 ? -20.433 74.031  105.672 1.00 42.84 ? 111  ALA A CA  1 
ATOM   778   C  C   . ALA A 1 111 ? -19.466 74.083  106.868 1.00 41.63 ? 111  ALA A C   1 
ATOM   779   O  O   . ALA A 1 111 ? -19.691 73.398  107.872 1.00 39.98 ? 111  ALA A O   1 
ATOM   780   C  CB  . ALA A 1 111 ? -19.859 73.108  104.594 1.00 42.44 ? 111  ALA A CB  1 
ATOM   781   N  N   . SER A 1 112 ? -18.410 74.893  106.773 1.00 37.33 ? 112  SER A N   1 
ATOM   782   C  CA  . SER A 1 112 ? -17.437 74.982  107.862 1.00 38.62 ? 112  SER A CA  1 
ATOM   783   C  C   . SER A 1 112 ? -18.011 75.529  109.163 1.00 38.10 ? 112  SER A C   1 
ATOM   784   O  O   . SER A 1 112 ? -17.317 75.592  110.170 1.00 38.89 ? 112  SER A O   1 
ATOM   785   C  CB  . SER A 1 112 ? -16.240 75.841  107.457 1.00 38.24 ? 112  SER A CB  1 
ATOM   786   O  OG  . SER A 1 112 ? -16.657 77.174  107.226 1.00 45.88 ? 112  SER A OG  1 
ATOM   787   N  N   . ALA A 1 113 ? -19.265 75.949  109.151 1.00 36.43 ? 113  ALA A N   1 
ATOM   788   C  CA  . ALA A 1 113 ? -19.853 76.459  110.371 1.00 35.39 ? 113  ALA A CA  1 
ATOM   789   C  C   . ALA A 1 113 ? -19.977 75.308  111.342 1.00 38.09 ? 113  ALA A C   1 
ATOM   790   O  O   . ALA A 1 113 ? -20.037 75.492  112.556 1.00 41.41 ? 113  ALA A O   1 
ATOM   791   C  CB  . ALA A 1 113 ? -21.222 77.012  110.085 1.00 33.44 ? 113  ALA A CB  1 
ATOM   792   N  N   . PHE A 1 114 ? -20.015 74.110  110.786 1.00 38.74 ? 114  PHE A N   1 
ATOM   793   C  CA  . PHE A 1 114 ? -20.213 72.921  111.568 1.00 37.40 ? 114  PHE A CA  1 
ATOM   794   C  C   . PHE A 1 114 ? -18.942 72.319  112.142 1.00 39.53 ? 114  PHE A C   1 
ATOM   795   O  O   . PHE A 1 114 ? -18.997 71.456  113.040 1.00 40.38 ? 114  PHE A O   1 
ATOM   796   C  CB  . PHE A 1 114 ? -20.967 71.911  110.703 1.00 36.53 ? 114  PHE A CB  1 
ATOM   797   C  CG  . PHE A 1 114 ? -22.402 72.252  110.501 1.00 39.77 ? 114  PHE A CG  1 
ATOM   798   C  CD1 . PHE A 1 114 ? -23.359 71.884  111.438 1.00 44.23 ? 114  PHE A CD1 1 
ATOM   799   C  CD2 . PHE A 1 114 ? -22.800 72.986  109.400 1.00 44.79 ? 114  PHE A CD2 1 
ATOM   800   C  CE1 . PHE A 1 114 ? -24.691 72.249  111.275 1.00 48.14 ? 114  PHE A CE1 1 
ATOM   801   C  CE2 . PHE A 1 114 ? -24.130 73.359  109.231 1.00 43.45 ? 114  PHE A CE2 1 
ATOM   802   C  CZ  . PHE A 1 114 ? -25.074 72.990  110.165 1.00 45.48 ? 114  PHE A CZ  1 
ATOM   803   N  N   . TYR A 1 115 ? -17.798 72.786  111.653 1.00 39.55 ? 115  TYR A N   1 
ATOM   804   C  CA  . TYR A 1 115 ? -16.512 72.262  112.111 1.00 39.47 ? 115  TYR A CA  1 
ATOM   805   C  C   . TYR A 1 115 ? -16.328 72.316  113.647 1.00 39.49 ? 115  TYR A C   1 
ATOM   806   O  O   . TYR A 1 115 ? -16.182 71.264  114.293 1.00 39.01 ? 115  TYR A O   1 
ATOM   807   C  CB  . TYR A 1 115 ? -15.389 72.990  111.378 1.00 35.20 ? 115  TYR A CB  1 
ATOM   808   C  CG  . TYR A 1 115 ? -14.002 72.383  111.531 1.00 37.52 ? 115  TYR A CG  1 
ATOM   809   C  CD1 . TYR A 1 115 ? -13.236 72.600  112.692 1.00 33.62 ? 115  TYR A CD1 1 
ATOM   810   C  CD2 . TYR A 1 115 ? -13.422 71.664  110.482 1.00 35.01 ? 115  TYR A CD2 1 
ATOM   811   C  CE1 . TYR A 1 115 ? -11.939 72.141  112.799 1.00 30.52 ? 115  TYR A CE1 1 
ATOM   812   C  CE2 . TYR A 1 115 ? -12.123 71.192  110.571 1.00 33.98 ? 115  TYR A CE2 1 
ATOM   813   C  CZ  . TYR A 1 115 ? -11.379 71.438  111.732 1.00 38.68 ? 115  TYR A CZ  1 
ATOM   814   O  OH  . TYR A 1 115 ? -10.067 71.005  111.805 1.00 36.00 ? 115  TYR A OH  1 
ATOM   815   N  N   . GLY A 1 116 ? -16.356 73.518  114.229 1.00 41.69 ? 116  GLY A N   1 
ATOM   816   C  CA  . GLY A 1 116 ? -16.212 73.668  115.688 1.00 40.01 ? 116  GLY A CA  1 
ATOM   817   C  C   . GLY A 1 116 ? -17.176 72.783  116.466 1.00 37.45 ? 116  GLY A C   1 
ATOM   818   O  O   . GLY A 1 116 ? -16.751 72.023  117.358 1.00 35.33 ? 116  GLY A O   1 
ATOM   819   N  N   . PRO A 1 117 ? -18.486 72.867  116.155 1.00 35.18 ? 117  PRO A N   1 
ATOM   820   C  CA  . PRO A 1 117 ? -19.499 72.059  116.819 1.00 32.76 ? 117  PRO A CA  1 
ATOM   821   C  C   . PRO A 1 117 ? -19.155 70.554  116.744 1.00 33.06 ? 117  PRO A C   1 
ATOM   822   O  O   . PRO A 1 117 ? -19.383 69.819  117.707 1.00 34.36 ? 117  PRO A O   1 
ATOM   823   C  CB  . PRO A 1 117 ? -20.767 72.416  116.039 1.00 38.28 ? 117  PRO A CB  1 
ATOM   824   C  CG  . PRO A 1 117 ? -20.571 73.823  115.714 1.00 35.92 ? 117  PRO A CG  1 
ATOM   825   C  CD  . PRO A 1 117 ? -19.120 73.855  115.264 1.00 33.75 ? 117  PRO A CD  1 
ATOM   826   N  N   . SER A 1 118 ? -18.621 70.099  115.605 1.00 32.03 ? 118  SER A N   1 
ATOM   827   C  CA  . SER A 1 118 ? -18.239 68.689  115.439 1.00 30.40 ? 118  SER A CA  1 
ATOM   828   C  C   . SER A 1 118 ? -17.179 68.335  116.463 1.00 31.67 ? 118  SER A C   1 
ATOM   829   O  O   . SER A 1 118 ? -17.209 67.266  117.074 1.00 28.35 ? 118  SER A O   1 
ATOM   830   C  CB  . SER A 1 118 ? -17.638 68.429  114.055 1.00 30.94 ? 118  SER A CB  1 
ATOM   831   O  OG  . SER A 1 118 ? -18.589 68.615  113.029 1.00 36.96 ? 118  SER A OG  1 
ATOM   832   N  N   . LEU A 1 119 ? -16.216 69.232  116.613 1.00 32.70 ? 119  LEU A N   1 
ATOM   833   C  CA  . LEU A 1 119 ? -15.132 69.021  117.556 1.00 36.66 ? 119  LEU A CA  1 
ATOM   834   C  C   . LEU A 1 119 ? -15.677 68.931  118.974 1.00 39.84 ? 119  LEU A C   1 
ATOM   835   O  O   . LEU A 1 119 ? -15.213 68.123  119.793 1.00 40.48 ? 119  LEU A O   1 
ATOM   836   C  CB  . LEU A 1 119 ? -14.165 70.186  117.484 1.00 36.34 ? 119  LEU A CB  1 
ATOM   837   C  CG  . LEU A 1 119 ? -12.751 69.974  116.961 1.00 40.58 ? 119  LEU A CG  1 
ATOM   838   C  CD1 . LEU A 1 119 ? -12.625 68.693  116.165 1.00 38.43 ? 119  LEU A CD1 1 
ATOM   839   C  CD2 . LEU A 1 119 ? -12.383 71.208  116.142 1.00 38.75 ? 119  LEU A CD2 1 
ATOM   840   N  N   . ALA A 1 120 ? -16.658 69.776  119.257 1.00 36.39 ? 120  ALA A N   1 
ATOM   841   C  CA  . ALA A 1 120 ? -17.225 69.814  120.573 1.00 34.71 ? 120  ALA A CA  1 
ATOM   842   C  C   . ALA A 1 120 ? -17.992 68.546  120.861 1.00 36.26 ? 120  ALA A C   1 
ATOM   843   O  O   . ALA A 1 120 ? -17.852 67.952  121.932 1.00 37.93 ? 120  ALA A O   1 
ATOM   844   C  CB  . ALA A 1 120 ? -18.138 71.025  120.701 1.00 35.85 ? 120  ALA A CB  1 
ATOM   845   N  N   . ILE A 1 121 ? -18.807 68.116  119.911 1.00 34.64 ? 121  ILE A N   1 
ATOM   846   C  CA  . ILE A 1 121 ? -19.601 66.935  120.156 1.00 33.91 ? 121  ILE A CA  1 
ATOM   847   C  C   . ILE A 1 121 ? -18.692 65.746  120.325 1.00 34.14 ? 121  ILE A C   1 
ATOM   848   O  O   . ILE A 1 121 ? -18.945 64.871  121.150 1.00 36.07 ? 121  ILE A O   1 
ATOM   849   C  CB  . ILE A 1 121 ? -20.644 66.745  119.030 1.00 36.13 ? 121  ILE A CB  1 
ATOM   850   C  CG1 . ILE A 1 121 ? -21.878 67.596  119.360 1.00 38.77 ? 121  ILE A CG1 1 
ATOM   851   C  CG2 . ILE A 1 121 ? -21.025 65.270  118.875 1.00 32.89 ? 121  ILE A CG2 1 
ATOM   852   C  CD1 . ILE A 1 121 ? -22.586 68.157  118.136 1.00 42.19 ? 121  ILE A CD1 1 
ATOM   853   N  N   . LEU A 1 122 ? -17.609 65.708  119.570 1.00 33.98 ? 122  LEU A N   1 
ATOM   854   C  CA  . LEU A 1 122 ? -16.703 64.593  119.717 1.00 34.29 ? 122  LEU A CA  1 
ATOM   855   C  C   . LEU A 1 122 ? -16.174 64.586  121.152 1.00 36.97 ? 122  LEU A C   1 
ATOM   856   O  O   . LEU A 1 122 ? -16.223 63.551  121.845 1.00 39.24 ? 122  LEU A O   1 
ATOM   857   C  CB  . LEU A 1 122 ? -15.556 64.698  118.721 1.00 35.01 ? 122  LEU A CB  1 
ATOM   858   C  CG  . LEU A 1 122 ? -14.504 63.586  118.803 1.00 36.89 ? 122  LEU A CG  1 
ATOM   859   C  CD1 . LEU A 1 122 ? -15.164 62.198  118.808 1.00 26.89 ? 122  LEU A CD1 1 
ATOM   860   C  CD2 . LEU A 1 122 ? -13.561 63.743  117.630 1.00 30.35 ? 122  LEU A CD2 1 
ATOM   861   N  N   . ALA A 1 123 ? -15.706 65.741  121.620 1.00 35.42 ? 123  ALA A N   1 
ATOM   862   C  CA  . ALA A 1 123 ? -15.168 65.818  122.981 1.00 36.86 ? 123  ALA A CA  1 
ATOM   863   C  C   . ALA A 1 123 ? -16.188 65.347  124.029 1.00 37.27 ? 123  ALA A C   1 
ATOM   864   O  O   . ALA A 1 123 ? -15.897 64.474  124.869 1.00 36.20 ? 123  ALA A O   1 
ATOM   865   C  CB  . ALA A 1 123 ? -14.715 67.245  123.291 1.00 34.95 ? 123  ALA A CB  1 
ATOM   866   N  N   . LEU A 1 124 ? -17.374 65.951  123.969 1.00 34.97 ? 124  LEU A N   1 
ATOM   867   C  CA  . LEU A 1 124 ? -18.468 65.649  124.868 1.00 32.04 ? 124  LEU A CA  1 
ATOM   868   C  C   . LEU A 1 124 ? -18.852 64.183  124.740 1.00 33.48 ? 124  LEU A C   1 
ATOM   869   O  O   . LEU A 1 124 ? -19.147 63.519  125.734 1.00 31.22 ? 124  LEU A O   1 
ATOM   870   C  CB  . LEU A 1 124 ? -19.653 66.549  124.536 1.00 33.11 ? 124  LEU A CB  1 
ATOM   871   C  CG  . LEU A 1 124 ? -19.809 67.856  125.345 1.00 34.40 ? 124  LEU A CG  1 
ATOM   872   C  CD1 . LEU A 1 124 ? -18.481 68.326  125.822 1.00 28.42 ? 124  LEU A CD1 1 
ATOM   873   C  CD2 . LEU A 1 124 ? -20.539 68.930  124.505 1.00 31.39 ? 124  LEU A CD2 1 
ATOM   874   N  N   . CYS A 1 125 ? -18.818 63.657  123.523 1.00 33.50 ? 125  CYS A N   1 
ATOM   875   C  CA  . CYS A 1 125 ? -19.166 62.262  123.339 1.00 35.04 ? 125  CYS A CA  1 
ATOM   876   C  C   . CYS A 1 125 ? -18.157 61.370  124.102 1.00 34.86 ? 125  CYS A C   1 
ATOM   877   O  O   . CYS A 1 125 ? -18.526 60.377  124.761 1.00 31.99 ? 125  CYS A O   1 
ATOM   878   C  CB  . CYS A 1 125 ? -19.198 61.936  121.841 1.00 34.75 ? 125  CYS A CB  1 
ATOM   879   S  SG  . CYS A 1 125 ? -19.485 60.172  121.517 1.00 42.25 ? 125  CYS A SG  1 
ATOM   880   N  N   . GLN A 1 126 ? -16.882 61.733  124.030 1.00 35.84 ? 126  GLN A N   1 
ATOM   881   C  CA  . GLN A 1 126 ? -15.872 60.963  124.730 1.00 36.32 ? 126  GLN A CA  1 
ATOM   882   C  C   . GLN A 1 126 ? -16.030 61.021  126.257 1.00 39.66 ? 126  GLN A C   1 
ATOM   883   O  O   . GLN A 1 126 ? -15.792 60.017  126.950 1.00 40.70 ? 126  GLN A O   1 
ATOM   884   C  CB  . GLN A 1 126 ? -14.494 61.414  124.306 1.00 31.08 ? 126  GLN A CB  1 
ATOM   885   C  CG  . GLN A 1 126 ? -14.116 60.895  122.967 1.00 35.66 ? 126  GLN A CG  1 
ATOM   886   C  CD  . GLN A 1 126 ? -12.870 61.561  122.397 1.00 39.85 ? 126  GLN A CD  1 
ATOM   887   O  OE1 . GLN A 1 126 ? -12.316 61.110  121.389 1.00 44.06 ? 126  GLN A OE1 1 
ATOM   888   N  NE2 . GLN A 1 126 ? -12.435 62.642  123.027 1.00 38.17 ? 126  GLN A NE2 1 
ATOM   889   N  N   . LYS A 1 127 ? -16.459 62.160  126.792 1.00 40.03 ? 127  LYS A N   1 
ATOM   890   C  CA  . LYS A 1 127 ? -16.640 62.248  128.245 1.00 42.06 ? 127  LYS A CA  1 
ATOM   891   C  C   . LYS A 1 127 ? -17.925 61.613  128.759 1.00 40.71 ? 127  LYS A C   1 
ATOM   892   O  O   . LYS A 1 127 ? -17.937 61.036  129.839 1.00 42.66 ? 127  LYS A O   1 
ATOM   893   C  CB  . LYS A 1 127 ? -16.597 63.715  128.723 1.00 46.54 ? 127  LYS A CB  1 
ATOM   894   C  CG  . LYS A 1 127 ? -15.209 64.285  128.739 1.00 52.70 ? 127  LYS A CG  1 
ATOM   895   C  CD  . LYS A 1 127 ? -14.346 63.419  129.670 1.00 59.24 ? 127  LYS A CD  1 
ATOM   896   C  CE  . LYS A 1 127 ? -12.863 63.651  129.463 1.00 59.72 ? 127  LYS A CE  1 
ATOM   897   N  NZ  . LYS A 1 127 ? -12.527 63.413  128.043 1.00 65.18 ? 127  LYS A NZ  1 
ATOM   898   N  N   . ASN A 1 128 ? -19.012 61.713  127.999 1.00 38.79 ? 128  ASN A N   1 
ATOM   899   C  CA  . ASN A 1 128 ? -20.277 61.167  128.468 1.00 37.35 ? 128  ASN A CA  1 
ATOM   900   C  C   . ASN A 1 128 ? -21.231 61.070  127.303 1.00 37.64 ? 128  ASN A C   1 
ATOM   901   O  O   . ASN A 1 128 ? -22.035 61.976  127.042 1.00 39.55 ? 128  ASN A O   1 
ATOM   902   C  CB  . ASN A 1 128 ? -20.841 62.075  129.572 1.00 35.63 ? 128  ASN A CB  1 
ATOM   903   C  CG  . ASN A 1 128 ? -22.109 61.531  130.190 1.00 37.51 ? 128  ASN A CG  1 
ATOM   904   O  OD1 . ASN A 1 128 ? -22.513 61.967  131.268 1.00 39.69 ? 128  ASN A OD1 1 
ATOM   905   N  ND2 . ASN A 1 128 ? -22.752 60.585  129.511 1.00 38.19 ? 128  ASN A ND2 1 
ATOM   906   N  N   . SER A 1 129 ? -21.150 59.946  126.608 1.00 36.90 ? 129  SER A N   1 
ATOM   907   C  CA  . SER A 1 129 ? -21.970 59.756  125.445 1.00 34.47 ? 129  SER A CA  1 
ATOM   908   C  C   . SER A 1 129 ? -23.460 59.997  125.672 1.00 33.05 ? 129  SER A C   1 
ATOM   909   O  O   . SER A 1 129 ? -24.059 60.779  124.959 1.00 34.14 ? 129  SER A O   1 
ATOM   910   C  CB  . SER A 1 129 ? -21.719 58.363  124.847 1.00 34.79 ? 129  SER A CB  1 
ATOM   911   O  OG  . SER A 1 129 ? -22.058 57.305  125.734 1.00 36.25 ? 129  SER A OG  1 
ATOM   912   N  N   . GLU A 1 130 ? -24.055 59.363  126.670 1.00 34.47 ? 130  GLU A N   1 
ATOM   913   C  CA  . GLU A 1 130 ? -25.492 59.500  126.885 1.00 35.60 ? 130  GLU A CA  1 
ATOM   914   C  C   . GLU A 1 130 ? -25.926 60.931  127.173 1.00 36.44 ? 130  GLU A C   1 
ATOM   915   O  O   . GLU A 1 130 ? -27.005 61.381  126.718 1.00 35.76 ? 130  GLU A O   1 
ATOM   916   C  CB  . GLU A 1 130 ? -25.968 58.549  127.998 1.00 35.92 ? 130  GLU A CB  1 
ATOM   917   C  CG  . GLU A 1 130 ? -27.467 58.654  128.318 1.00 42.76 ? 130  GLU A CG  1 
ATOM   918   C  CD  . GLU A 1 130 ? -28.017 57.492  129.168 1.00 50.26 ? 130  GLU A CD  1 
ATOM   919   O  OE1 . GLU A 1 130 ? -27.261 56.859  129.944 1.00 53.82 ? 130  GLU A OE1 1 
ATOM   920   O  OE2 . GLU A 1 130 ? -29.232 57.219  129.070 1.00 56.56 ? 130  GLU A OE2 1 
ATOM   921   N  N   . ALA A 1 131 ? -25.103 61.665  127.910 1.00 31.81 ? 131  ALA A N   1 
ATOM   922   C  CA  . ALA A 1 131 ? -25.466 63.053  128.205 1.00 33.28 ? 131  ALA A CA  1 
ATOM   923   C  C   . ALA A 1 131 ? -25.398 63.923  126.973 1.00 33.28 ? 131  ALA A C   1 
ATOM   924   O  O   . ALA A 1 131 ? -25.901 65.041  126.987 1.00 39.14 ? 131  ALA A O   1 
ATOM   925   C  CB  . ALA A 1 131 ? -24.556 63.628  129.236 1.00 28.48 ? 131  ALA A CB  1 
ATOM   926   N  N   . THR A 1 132 ? -24.768 63.409  125.924 1.00 30.56 ? 132  THR A N   1 
ATOM   927   C  CA  . THR A 1 132 ? -24.571 64.117  124.677 1.00 32.32 ? 132  THR A CA  1 
ATOM   928   C  C   . THR A 1 132 ? -25.583 63.787  123.585 1.00 32.56 ? 132  THR A C   1 
ATOM   929   O  O   . THR A 1 132 ? -25.623 64.475  122.575 1.00 33.45 ? 132  THR A O   1 
ATOM   930   C  CB  . THR A 1 132 ? -23.130 63.806  124.158 1.00 35.82 ? 132  THR A CB  1 
ATOM   931   O  OG1 . THR A 1 132 ? -22.199 64.095  125.203 1.00 37.51 ? 132  THR A OG1 1 
ATOM   932   C  CG2 . THR A 1 132 ? -22.759 64.630  122.924 1.00 30.08 ? 132  THR A CG2 1 
ATOM   933   N  N   . LEU A 1 133 ? -26.396 62.749  123.767 1.00 34.79 ? 133  LEU A N   1 
ATOM   934   C  CA  . LEU A 1 133 ? -27.362 62.381  122.727 1.00 37.20 ? 133  LEU A CA  1 
ATOM   935   C  C   . LEU A 1 133 ? -28.201 63.539  122.237 1.00 39.10 ? 133  LEU A C   1 
ATOM   936   O  O   . LEU A 1 133 ? -28.199 63.845  121.034 1.00 40.17 ? 133  LEU A O   1 
ATOM   937   C  CB  . LEU A 1 133 ? -28.300 61.281  123.203 1.00 38.95 ? 133  LEU A CB  1 
ATOM   938   C  CG  . LEU A 1 133 ? -27.787 59.886  122.940 1.00 38.43 ? 133  LEU A CG  1 
ATOM   939   C  CD1 . LEU A 1 133 ? -28.721 58.887  123.617 1.00 36.56 ? 133  LEU A CD1 1 
ATOM   940   C  CD2 . LEU A 1 133 ? -27.682 59.671  121.432 1.00 35.99 ? 133  LEU A CD2 1 
ATOM   941   N  N   . PRO A 1 134 ? -28.916 64.209  123.165 1.00 37.94 ? 134  PRO A N   1 
ATOM   942   C  CA  . PRO A 1 134 ? -29.769 65.344  122.784 1.00 38.84 ? 134  PRO A CA  1 
ATOM   943   C  C   . PRO A 1 134 ? -29.083 66.259  121.781 1.00 39.35 ? 134  PRO A C   1 
ATOM   944   O  O   . PRO A 1 134 ? -29.580 66.489  120.678 1.00 43.45 ? 134  PRO A O   1 
ATOM   945   C  CB  . PRO A 1 134 ? -30.047 66.040  124.122 1.00 37.73 ? 134  PRO A CB  1 
ATOM   946   C  CG  . PRO A 1 134 ? -29.998 64.891  125.101 1.00 34.62 ? 134  PRO A CG  1 
ATOM   947   C  CD  . PRO A 1 134 ? -28.805 64.102  124.632 1.00 32.11 ? 134  PRO A CD  1 
ATOM   948   N  N   . ILE A 1 135 ? -27.927 66.764  122.170 1.00 40.54 ? 135  ILE A N   1 
ATOM   949   C  CA  . ILE A 1 135 ? -27.167 67.670  121.331 1.00 40.62 ? 135  ILE A CA  1 
ATOM   950   C  C   . ILE A 1 135 ? -26.764 67.045  120.004 1.00 39.90 ? 135  ILE A C   1 
ATOM   951   O  O   . ILE A 1 135 ? -26.801 67.698  118.946 1.00 42.75 ? 135  ILE A O   1 
ATOM   952   C  CB  . ILE A 1 135 ? -25.901 68.146  122.074 1.00 41.37 ? 135  ILE A CB  1 
ATOM   953   C  CG1 . ILE A 1 135 ? -26.295 69.048  123.229 1.00 45.54 ? 135  ILE A CG1 1 
ATOM   954   C  CG2 . ILE A 1 135 ? -25.011 68.933  121.157 1.00 43.16 ? 135  ILE A CG2 1 
ATOM   955   C  CD1 . ILE A 1 135 ? -25.114 69.487  124.043 1.00 50.00 ? 135  ILE A CD1 1 
ATOM   956   N  N   . ALA A 1 136 ? -26.387 65.776  120.059 1.00 38.41 ? 136  ALA A N   1 
ATOM   957   C  CA  . ALA A 1 136 ? -25.937 65.081  118.870 1.00 36.58 ? 136  ALA A CA  1 
ATOM   958   C  C   . ALA A 1 136 ? -27.083 64.806  117.902 1.00 35.74 ? 136  ALA A C   1 
ATOM   959   O  O   . ALA A 1 136 ? -26.893 64.856  116.690 1.00 36.22 ? 136  ALA A O   1 
ATOM   960   C  CB  . ALA A 1 136 ? -25.224 63.800  119.270 1.00 30.94 ? 136  ALA A CB  1 
ATOM   961   N  N   . VAL A 1 137 ? -28.270 64.511  118.426 1.00 35.87 ? 137  VAL A N   1 
ATOM   962   C  CA  . VAL A 1 137 ? -29.424 64.259  117.563 1.00 35.95 ? 137  VAL A CA  1 
ATOM   963   C  C   . VAL A 1 137 ? -29.742 65.545  116.810 1.00 38.38 ? 137  VAL A C   1 
ATOM   964   O  O   . VAL A 1 137 ? -29.888 65.560  115.562 1.00 36.29 ? 137  VAL A O   1 
ATOM   965   C  CB  . VAL A 1 137 ? -30.653 63.851  118.377 1.00 37.65 ? 137  VAL A CB  1 
ATOM   966   C  CG1 . VAL A 1 137 ? -31.916 63.960  117.532 1.00 30.29 ? 137  VAL A CG1 1 
ATOM   967   C  CG2 . VAL A 1 137 ? -30.492 62.406  118.834 1.00 38.54 ? 137  VAL A CG2 1 
ATOM   968   N  N   . ARG A 1 138 ? -29.821 66.621  117.594 1.00 36.12 ? 138  ARG A N   1 
ATOM   969   C  CA  . ARG A 1 138 ? -30.091 67.946  117.090 1.00 34.11 ? 138  ARG A CA  1 
ATOM   970   C  C   . ARG A 1 138 ? -29.020 68.302  116.059 1.00 35.42 ? 138  ARG A C   1 
ATOM   971   O  O   . ARG A 1 138 ? -29.330 68.851  114.991 1.00 35.12 ? 138  ARG A O   1 
ATOM   972   C  CB  . ARG A 1 138 ? -30.103 68.923  118.275 1.00 38.60 ? 138  ARG A CB  1 
ATOM   973   C  CG  . ARG A 1 138 ? -30.207 70.399  117.928 1.00 46.86 ? 138  ARG A CG  1 
ATOM   974   C  CD  . ARG A 1 138 ? -31.193 71.107  118.858 1.00 53.01 ? 138  ARG A CD  1 
ATOM   975   N  NE  . ARG A 1 138 ? -31.126 70.640  120.242 1.00 56.74 ? 138  ARG A NE  1 
ATOM   976   C  CZ  . ARG A 1 138 ? -30.243 71.060  121.147 1.00 58.76 ? 138  ARG A CZ  1 
ATOM   977   N  NH1 . ARG A 1 138 ? -29.320 71.970  120.830 1.00 60.30 ? 138  ARG A NH1 1 
ATOM   978   N  NH2 . ARG A 1 138 ? -30.303 70.577  122.383 1.00 58.71 ? 138  ARG A NH2 1 
ATOM   979   N  N   . PHE A 1 139 ? -27.766 67.958  116.364 1.00 35.41 ? 139  PHE A N   1 
ATOM   980   C  CA  . PHE A 1 139 ? -26.646 68.268  115.465 1.00 35.60 ? 139  PHE A CA  1 
ATOM   981   C  C   . PHE A 1 139 ? -26.768 67.513  114.145 1.00 36.10 ? 139  PHE A C   1 
ATOM   982   O  O   . PHE A 1 139 ? -26.548 68.081  113.065 1.00 37.56 ? 139  PHE A O   1 
ATOM   983   C  CB  . PHE A 1 139 ? -25.314 67.924  116.133 1.00 31.84 ? 139  PHE A CB  1 
ATOM   984   C  CG  . PHE A 1 139 ? -24.112 68.181  115.269 1.00 30.94 ? 139  PHE A CG  1 
ATOM   985   C  CD1 . PHE A 1 139 ? -23.641 69.478  115.062 1.00 31.47 ? 139  PHE A CD1 1 
ATOM   986   C  CD2 . PHE A 1 139 ? -23.411 67.109  114.705 1.00 31.94 ? 139  PHE A CD2 1 
ATOM   987   C  CE1 . PHE A 1 139 ? -22.468 69.715  114.308 1.00 30.51 ? 139  PHE A CE1 1 
ATOM   988   C  CE2 . PHE A 1 139 ? -22.249 67.318  113.952 1.00 31.80 ? 139  PHE A CE2 1 
ATOM   989   C  CZ  . PHE A 1 139 ? -21.768 68.644  113.753 1.00 32.79 ? 139  PHE A CZ  1 
ATOM   990   N  N   . ALA A 1 140 ? -27.128 66.238  114.236 1.00 34.03 ? 140  ALA A N   1 
ATOM   991   C  CA  . ALA A 1 140 ? -27.287 65.418  113.040 1.00 38.61 ? 140  ALA A CA  1 
ATOM   992   C  C   . ALA A 1 140 ? -28.408 65.959  112.146 1.00 38.75 ? 140  ALA A C   1 
ATOM   993   O  O   . ALA A 1 140 ? -28.296 65.944  110.929 1.00 37.54 ? 140  ALA A O   1 
ATOM   994   C  CB  . ALA A 1 140 ? -27.585 63.967  113.430 1.00 37.05 ? 140  ALA A CB  1 
ATOM   995   N  N   . LYS A 1 141 ? -29.488 66.430  112.761 1.00 39.42 ? 141  LYS A N   1 
ATOM   996   C  CA  . LYS A 1 141 ? -30.614 66.961  112.005 1.00 40.30 ? 141  LYS A CA  1 
ATOM   997   C  C   . LYS A 1 141 ? -30.271 68.284  111.352 1.00 39.27 ? 141  LYS A C   1 
ATOM   998   O  O   . LYS A 1 141 ? -30.670 68.560  110.222 1.00 40.02 ? 141  LYS A O   1 
ATOM   999   C  CB  . LYS A 1 141 ? -31.800 67.166  112.921 1.00 38.48 ? 141  LYS A CB  1 
ATOM   1000  C  CG  . LYS A 1 141 ? -32.370 65.894  113.450 1.00 37.79 ? 141  LYS A CG  1 
ATOM   1001  C  CD  . LYS A 1 141 ? -33.416 66.192  114.504 1.00 31.94 ? 141  LYS A CD  1 
ATOM   1002  C  CE  . LYS A 1 141 ? -34.221 64.931  114.791 1.00 35.99 ? 141  LYS A CE  1 
ATOM   1003  N  NZ  . LYS A 1 141 ? -35.038 65.080  116.011 1.00 33.12 ? 141  LYS A NZ  1 
ATOM   1004  N  N   . THR A 1 142 ? -29.531 69.109  112.069 1.00 38.02 ? 142  THR A N   1 
ATOM   1005  C  CA  . THR A 1 142 ? -29.153 70.387  111.518 1.00 38.18 ? 142  THR A CA  1 
ATOM   1006  C  C   . THR A 1 142 ? -28.258 70.161  110.322 1.00 39.13 ? 142  THR A C   1 
ATOM   1007  O  O   . THR A 1 142 ? -28.331 70.895  109.334 1.00 38.29 ? 142  THR A O   1 
ATOM   1008  C  CB  . THR A 1 142 ? -28.418 71.221  112.559 1.00 37.04 ? 142  THR A CB  1 
ATOM   1009  O  OG1 . THR A 1 142 ? -29.330 71.536  113.620 1.00 41.80 ? 142  THR A OG1 1 
ATOM   1010  C  CG2 . THR A 1 142 ? -27.885 72.506  111.948 1.00 35.28 ? 142  THR A CG2 1 
ATOM   1011  N  N   . LEU A 1 143 ? -27.427 69.124  110.410 1.00 39.69 ? 143  LEU A N   1 
ATOM   1012  C  CA  . LEU A 1 143 ? -26.469 68.815  109.348 1.00 40.08 ? 143  LEU A CA  1 
ATOM   1013  C  C   . LEU A 1 143 ? -27.214 68.229  108.146 1.00 40.48 ? 143  LEU A C   1 
ATOM   1014  O  O   . LEU A 1 143 ? -26.937 68.538  106.959 1.00 41.33 ? 143  LEU A O   1 
ATOM   1015  C  CB  . LEU A 1 143 ? -25.404 67.848  109.886 1.00 40.75 ? 143  LEU A CB  1 
ATOM   1016  C  CG  . LEU A 1 143 ? -23.983 67.905  109.320 1.00 42.67 ? 143  LEU A CG  1 
ATOM   1017  C  CD1 . LEU A 1 143 ? -23.401 69.308  109.334 1.00 41.63 ? 143  LEU A CD1 1 
ATOM   1018  C  CD2 . LEU A 1 143 ? -23.142 66.983  110.155 1.00 41.53 ? 143  LEU A CD2 1 
ATOM   1019  N  N   . LEU A 1 144 ? -28.188 67.390  108.452 1.00 38.54 ? 144  LEU A N   1 
ATOM   1020  C  CA  . LEU A 1 144 ? -29.005 66.794  107.407 1.00 39.19 ? 144  LEU A CA  1 
ATOM   1021  C  C   . LEU A 1 144 ? -29.785 67.858  106.628 1.00 40.19 ? 144  LEU A C   1 
ATOM   1022  O  O   . LEU A 1 144 ? -30.028 67.738  105.422 1.00 40.47 ? 144  LEU A O   1 
ATOM   1023  C  CB  . LEU A 1 144 ? -30.019 65.836  108.001 1.00 36.87 ? 144  LEU A CB  1 
ATOM   1024  C  CG  . LEU A 1 144 ? -30.723 64.969  106.945 1.00 39.49 ? 144  LEU A CG  1 
ATOM   1025  C  CD1 . LEU A 1 144 ? -29.717 64.134  106.111 1.00 45.33 ? 144  LEU A CD1 1 
ATOM   1026  C  CD2 . LEU A 1 144 ? -31.630 64.043  107.666 1.00 43.38 ? 144  LEU A CD2 1 
ATOM   1027  N  N   . ALA A 1 145 ? -30.205 68.888  107.338 1.00 39.50 ? 145  ALA A N   1 
ATOM   1028  C  CA  . ALA A 1 145 ? -30.943 69.973  106.736 1.00 40.09 ? 145  ALA A CA  1 
ATOM   1029  C  C   . ALA A 1 145 ? -30.123 71.029  105.992 1.00 41.38 ? 145  ALA A C   1 
ATOM   1030  O  O   . ALA A 1 145 ? -30.701 71.780  105.221 1.00 45.27 ? 145  ALA A O   1 
ATOM   1031  C  CB  . ALA A 1 145 ? -31.781 70.645  107.798 1.00 36.63 ? 145  ALA A CB  1 
ATOM   1032  N  N   . ASN A 1 146 ? -28.807 71.102  106.206 1.00 41.81 ? 146  ASN A N   1 
ATOM   1033  C  CA  . ASN A 1 146 ? -27.980 72.129  105.547 1.00 43.59 ? 146  ASN A CA  1 
ATOM   1034  C  C   . ASN A 1 146 ? -27.728 71.812  104.060 1.00 45.69 ? 146  ASN A C   1 
ATOM   1035  O  O   . ASN A 1 146 ? -27.631 70.638  103.691 1.00 48.41 ? 146  ASN A O   1 
ATOM   1036  C  CB  . ASN A 1 146 ? -26.654 72.252  106.313 1.00 37.28 ? 146  ASN A CB  1 
ATOM   1037  C  CG  . ASN A 1 146 ? -25.714 73.224  105.695 1.00 36.14 ? 146  ASN A CG  1 
ATOM   1038  O  OD1 . ASN A 1 146 ? -25.767 74.443  105.966 1.00 41.55 ? 146  ASN A OD1 1 
ATOM   1039  N  ND2 . ASN A 1 146 ? -24.828 72.709  104.847 1.00 34.82 ? 146  ASN A ND2 1 
ATOM   1040  N  N   . SER A 1 147 ? -27.624 72.844  103.214 1.00 48.23 ? 147  SER A N   1 
ATOM   1041  C  CA  . SER A 1 147 ? -27.372 72.629  101.781 1.00 50.41 ? 147  SER A CA  1 
ATOM   1042  C  C   . SER A 1 147 ? -26.063 73.204  101.223 1.00 52.03 ? 147  SER A C   1 
ATOM   1043  O  O   . SER A 1 147 ? -25.673 72.883  100.106 1.00 57.58 ? 147  SER A O   1 
ATOM   1044  C  CB  . SER A 1 147 ? -28.529 73.182  100.961 1.00 48.90 ? 147  SER A CB  1 
ATOM   1045  O  OG  . SER A 1 147 ? -29.759 72.822  101.555 1.00 54.59 ? 147  SER A OG  1 
ATOM   1046  N  N   . SER A 1 148 ? -25.378 74.043  101.979 1.00 50.54 ? 148  SER A N   1 
ATOM   1047  C  CA  . SER A 1 148 ? -24.139 74.620  101.498 1.00 50.28 ? 148  SER A CA  1 
ATOM   1048  C  C   . SER A 1 148 ? -23.144 73.694  100.752 1.00 47.60 ? 148  SER A C   1 
ATOM   1049  O  O   . SER A 1 148 ? -23.174 72.466  100.880 1.00 41.70 ? 148  SER A O   1 
ATOM   1050  C  CB  . SER A 1 148 ? -23.457 75.268  102.682 1.00 54.79 ? 148  SER A CB  1 
ATOM   1051  O  OG  . SER A 1 148 ? -24.377 76.132  103.335 1.00 65.49 ? 148  SER A OG  1 
ATOM   1052  N  N   . PRO A 1 149 ? -22.275 74.282  99.911  1.00 44.82 ? 149  PRO A N   1 
ATOM   1053  C  CA  . PRO A 1 149 ? -21.297 73.450  99.197  1.00 43.52 ? 149  PRO A CA  1 
ATOM   1054  C  C   . PRO A 1 149 ? -20.392 72.759  100.233 1.00 41.80 ? 149  PRO A C   1 
ATOM   1055  O  O   . PRO A 1 149 ? -19.940 73.381  101.202 1.00 38.90 ? 149  PRO A O   1 
ATOM   1056  C  CB  . PRO A 1 149 ? -20.542 74.458  98.328  1.00 41.18 ? 149  PRO A CB  1 
ATOM   1057  C  CG  . PRO A 1 149 ? -20.699 75.759  99.084  1.00 44.46 ? 149  PRO A CG  1 
ATOM   1058  C  CD  . PRO A 1 149 ? -22.141 75.696  99.536  1.00 43.25 ? 149  PRO A CD  1 
ATOM   1059  N  N   . PHE A 1 150 ? -20.146 71.473  100.009 1.00 39.77 ? 150  PHE A N   1 
ATOM   1060  C  CA  . PHE A 1 150 ? -19.349 70.619  100.884 1.00 38.09 ? 150  PHE A CA  1 
ATOM   1061  C  C   . PHE A 1 150 ? -17.896 70.980  101.212 1.00 41.29 ? 150  PHE A C   1 
ATOM   1062  O  O   . PHE A 1 150 ? -17.095 71.322  100.337 1.00 43.60 ? 150  PHE A O   1 
ATOM   1063  C  CB  . PHE A 1 150 ? -19.358 69.210  100.316 1.00 35.94 ? 150  PHE A CB  1 
ATOM   1064  C  CG  . PHE A 1 150 ? -18.879 68.157  101.282 1.00 42.48 ? 150  PHE A CG  1 
ATOM   1065  C  CD1 . PHE A 1 150 ? -19.546 67.960  102.498 1.00 39.30 ? 150  PHE A CD1 1 
ATOM   1066  C  CD2 . PHE A 1 150 ? -17.821 67.307  100.946 1.00 37.20 ? 150  PHE A CD2 1 
ATOM   1067  C  CE1 . PHE A 1 150 ? -19.179 66.942  103.344 1.00 38.86 ? 150  PHE A CE1 1 
ATOM   1068  C  CE2 . PHE A 1 150 ? -17.449 66.284  101.789 1.00 39.45 ? 150  PHE A CE2 1 
ATOM   1069  C  CZ  . PHE A 1 150 ? -18.132 66.096  102.995 1.00 42.99 ? 150  PHE A CZ  1 
ATOM   1070  N  N   . ASN A 1 151 ? -17.567 70.870  102.493 1.00 42.53 ? 151  ASN A N   1 
ATOM   1071  C  CA  . ASN A 1 151 ? -16.219 71.108  102.978 1.00 41.66 ? 151  ASN A CA  1 
ATOM   1072  C  C   . ASN A 1 151 ? -15.676 69.767  103.541 1.00 40.13 ? 151  ASN A C   1 
ATOM   1073  O  O   . ASN A 1 151 ? -16.211 69.222  104.504 1.00 40.94 ? 151  ASN A O   1 
ATOM   1074  C  CB  . ASN A 1 151 ? -16.226 72.178  104.075 1.00 43.23 ? 151  ASN A CB  1 
ATOM   1075  C  CG  . ASN A 1 151 ? -14.852 72.395  104.657 1.00 47.14 ? 151  ASN A CG  1 
ATOM   1076  O  OD1 . ASN A 1 151 ? -13.947 72.857  103.967 1.00 45.49 ? 151  ASN A OD1 1 
ATOM   1077  N  ND2 . ASN A 1 151 ? -14.676 72.024  105.924 1.00 49.23 ? 151  ASN A ND2 1 
ATOM   1078  N  N   . VAL A 1 152 ? -14.615 69.243  102.947 1.00 38.38 ? 152  VAL A N   1 
ATOM   1079  C  CA  . VAL A 1 152 ? -14.065 67.986  103.405 1.00 37.30 ? 152  VAL A CA  1 
ATOM   1080  C  C   . VAL A 1 152 ? -13.563 68.038  104.835 1.00 37.93 ? 152  VAL A C   1 
ATOM   1081  O  O   . VAL A 1 152 ? -13.843 67.128  105.619 1.00 36.94 ? 152  VAL A O   1 
ATOM   1082  C  CB  . VAL A 1 152 ? -12.945 67.516  102.499 1.00 35.73 ? 152  VAL A CB  1 
ATOM   1083  C  CG1 . VAL A 1 152 ? -12.369 66.236  103.027 1.00 30.67 ? 152  VAL A CG1 1 
ATOM   1084  C  CG2 . VAL A 1 152 ? -13.481 67.319  101.107 1.00 31.17 ? 152  VAL A CG2 1 
ATOM   1085  N  N   . ASP A 1 153 ? -12.837 69.096  105.190 1.00 38.25 ? 153  ASP A N   1 
ATOM   1086  C  CA  . ASP A 1 153 ? -12.324 69.217  106.560 1.00 39.19 ? 153  ASP A CA  1 
ATOM   1087  C  C   . ASP A 1 153 ? -13.497 69.029  107.544 1.00 39.19 ? 153  ASP A C   1 
ATOM   1088  O  O   . ASP A 1 153 ? -13.463 68.176  108.438 1.00 39.96 ? 153  ASP A O   1 
ATOM   1089  C  CB  . ASP A 1 153 ? -11.660 70.587  106.781 1.00 40.71 ? 153  ASP A CB  1 
ATOM   1090  C  CG  . ASP A 1 153 ? -10.686 70.988  105.648 1.00 47.83 ? 153  ASP A CG  1 
ATOM   1091  O  OD1 . ASP A 1 153 ? -11.133 71.099  104.482 1.00 51.47 ? 153  ASP A OD1 1 
ATOM   1092  O  OD2 . ASP A 1 153 ? -9.472  71.213  105.914 1.00 46.76 ? 153  ASP A OD2 1 
ATOM   1093  N  N   . THR A 1 154 ? -14.554 69.810  107.351 1.00 40.02 ? 154  THR A N   1 
ATOM   1094  C  CA  . THR A 1 154 ? -15.724 69.729  108.223 1.00 38.51 ? 154  THR A CA  1 
ATOM   1095  C  C   . THR A 1 154 ? -16.394 68.363  108.173 1.00 36.97 ? 154  THR A C   1 
ATOM   1096  O  O   . THR A 1 154 ? -16.770 67.803  109.205 1.00 35.53 ? 154  THR A O   1 
ATOM   1097  C  CB  . THR A 1 154 ? -16.755 70.803  107.852 1.00 39.76 ? 154  THR A CB  1 
ATOM   1098  O  OG1 . THR A 1 154 ? -16.147 72.091  107.976 1.00 45.08 ? 154  THR A OG1 1 
ATOM   1099  C  CG2 . THR A 1 154 ? -17.951 70.749  108.786 1.00 38.85 ? 154  THR A CG2 1 
ATOM   1100  N  N   . GLY A 1 155 ? -16.546 67.831  106.966 1.00 35.43 ? 155  GLY A N   1 
ATOM   1101  C  CA  . GLY A 1 155 ? -17.173 66.538  106.816 1.00 30.86 ? 155  GLY A CA  1 
ATOM   1102  C  C   . GLY A 1 155 ? -16.453 65.507  107.666 1.00 30.46 ? 155  GLY A C   1 
ATOM   1103  O  O   . GLY A 1 155 ? -17.089 64.707  108.374 1.00 26.18 ? 155  GLY A O   1 
ATOM   1104  N  N   . ALA A 1 156 ? -15.122 65.558  107.598 1.00 28.93 ? 156  ALA A N   1 
ATOM   1105  C  CA  . ALA A 1 156 ? -14.254 64.645  108.322 1.00 29.82 ? 156  ALA A CA  1 
ATOM   1106  C  C   . ALA A 1 156 ? -14.527 64.759  109.809 1.00 31.89 ? 156  ALA A C   1 
ATOM   1107  O  O   . ALA A 1 156 ? -14.804 63.754  110.478 1.00 30.98 ? 156  ALA A O   1 
ATOM   1108  C  CB  . ALA A 1 156 ? -12.802 64.981  108.025 1.00 29.63 ? 156  ALA A CB  1 
ATOM   1109  N  N   . MET A 1 157 ? -14.457 65.984  110.326 1.00 29.21 ? 157  MET A N   1 
ATOM   1110  C  CA  . MET A 1 157 ? -14.705 66.162  111.726 1.00 33.04 ? 157  MET A CA  1 
ATOM   1111  C  C   . MET A 1 157 ? -16.076 65.661  112.075 1.00 35.47 ? 157  MET A C   1 
ATOM   1112  O  O   . MET A 1 157 ? -16.243 64.981  113.075 1.00 40.04 ? 157  MET A O   1 
ATOM   1113  C  CB  . MET A 1 157 ? -14.601 67.627  112.135 1.00 38.17 ? 157  MET A CB  1 
ATOM   1114  C  CG  . MET A 1 157 ? -13.191 68.143  112.164 1.00 45.56 ? 157  MET A CG  1 
ATOM   1115  S  SD  . MET A 1 157 ? -12.167 67.089  113.215 1.00 52.25 ? 157  MET A SD  1 
ATOM   1116  C  CE  . MET A 1 157 ? -10.676 68.079  113.279 1.00 52.37 ? 157  MET A CE  1 
ATOM   1117  N  N   . ALA A 1 158 ? -17.066 65.988  111.253 1.00 35.06 ? 158  ALA A N   1 
ATOM   1118  C  CA  . ALA A 1 158 ? -18.424 65.591  111.560 1.00 33.06 ? 158  ALA A CA  1 
ATOM   1119  C  C   . ALA A 1 158 ? -18.614 64.096  111.614 1.00 34.18 ? 158  ALA A C   1 
ATOM   1120  O  O   . ALA A 1 158 ? -19.371 63.619  112.471 1.00 34.10 ? 158  ALA A O   1 
ATOM   1121  C  CB  . ALA A 1 158 ? -19.392 66.203  110.571 1.00 29.36 ? 158  ALA A CB  1 
ATOM   1122  N  N   . THR A 1 159 ? -17.954 63.346  110.723 1.00 34.54 ? 159  THR A N   1 
ATOM   1123  C  CA  . THR A 1 159 ? -18.141 61.894  110.764 1.00 35.98 ? 159  THR A CA  1 
ATOM   1124  C  C   . THR A 1 159 ? -17.490 61.284  112.027 1.00 35.08 ? 159  THR A C   1 
ATOM   1125  O  O   . THR A 1 159 ? -18.026 60.335  112.608 1.00 35.14 ? 159  THR A O   1 
ATOM   1126  C  CB  . THR A 1 159 ? -17.683 61.177  109.427 1.00 33.99 ? 159  THR A CB  1 
ATOM   1127  O  OG1 . THR A 1 159 ? -16.641 60.224  109.694 1.00 34.53 ? 159  THR A OG1 1 
ATOM   1128  C  CG2 . THR A 1 159 ? -17.247 62.171  108.419 1.00 29.77 ? 159  THR A CG2 1 
ATOM   1129  N  N   . LEU A 1 160 ? -16.373 61.847  112.473 1.00 32.38 ? 160  LEU A N   1 
ATOM   1130  C  CA  . LEU A 1 160 ? -15.745 61.365  113.694 1.00 35.05 ? 160  LEU A CA  1 
ATOM   1131  C  C   . LEU A 1 160 ? -16.730 61.516  114.862 1.00 34.82 ? 160  LEU A C   1 
ATOM   1132  O  O   . LEU A 1 160 ? -17.018 60.570  115.600 1.00 37.94 ? 160  LEU A O   1 
ATOM   1133  C  CB  . LEU A 1 160 ? -14.490 62.178  114.007 1.00 36.16 ? 160  LEU A CB  1 
ATOM   1134  C  CG  . LEU A 1 160 ? -13.260 61.968  113.122 1.00 38.07 ? 160  LEU A CG  1 
ATOM   1135  C  CD1 . LEU A 1 160 ? -12.134 62.920  113.578 1.00 33.77 ? 160  LEU A CD1 1 
ATOM   1136  C  CD2 . LEU A 1 160 ? -12.813 60.501  113.209 1.00 37.86 ? 160  LEU A CD2 1 
ATOM   1137  N  N   . ALA A 1 161 ? -17.241 62.722  115.033 1.00 32.96 ? 161  ALA A N   1 
ATOM   1138  C  CA  . ALA A 1 161 ? -18.169 62.982  116.107 1.00 34.93 ? 161  ALA A CA  1 
ATOM   1139  C  C   . ALA A 1 161 ? -19.392 62.065  116.019 1.00 35.32 ? 161  ALA A C   1 
ATOM   1140  O  O   . ALA A 1 161 ? -19.780 61.456  117.001 1.00 37.01 ? 161  ALA A O   1 
ATOM   1141  C  CB  . ALA A 1 161 ? -18.589 64.456  116.080 1.00 33.41 ? 161  ALA A CB  1 
ATOM   1142  N  N   . LEU A 1 162 ? -19.982 61.941  114.834 1.00 36.37 ? 162  LEU A N   1 
ATOM   1143  C  CA  . LEU A 1 162 ? -21.156 61.106  114.699 1.00 36.23 ? 162  LEU A CA  1 
ATOM   1144  C  C   . LEU A 1 162 ? -20.834 59.640  114.867 1.00 35.97 ? 162  LEU A C   1 
ATOM   1145  O  O   . LEU A 1 162 ? -21.686 58.882  115.350 1.00 33.94 ? 162  LEU A O   1 
ATOM   1146  C  CB  . LEU A 1 162 ? -21.854 61.348  113.347 1.00 37.13 ? 162  LEU A CB  1 
ATOM   1147  C  CG  . LEU A 1 162 ? -23.105 62.237  113.388 1.00 37.63 ? 162  LEU A CG  1 
ATOM   1148  C  CD1 . LEU A 1 162 ? -23.231 62.976  114.736 1.00 37.91 ? 162  LEU A CD1 1 
ATOM   1149  C  CD2 . LEU A 1 162 ? -23.023 63.208  112.262 1.00 34.41 ? 162  LEU A CD2 1 
ATOM   1150  N  N   . THR A 1 163 ? -19.626 59.230  114.467 1.00 33.37 ? 163  THR A N   1 
ATOM   1151  C  CA  . THR A 1 163 ? -19.248 57.825  114.618 1.00 33.81 ? 163  THR A CA  1 
ATOM   1152  C  C   . THR A 1 163 ? -19.099 57.521  116.102 1.00 34.47 ? 163  THR A C   1 
ATOM   1153  O  O   . THR A 1 163 ? -19.435 56.431  116.562 1.00 31.61 ? 163  THR A O   1 
ATOM   1154  C  CB  . THR A 1 163 ? -17.936 57.498  113.901 1.00 33.93 ? 163  THR A CB  1 
ATOM   1155  O  OG1 . THR A 1 163 ? -18.125 57.622  112.487 1.00 38.31 ? 163  THR A OG1 1 
ATOM   1156  C  CG2 . THR A 1 163 ? -17.500 56.069  114.204 1.00 29.71 ? 163  THR A CG2 1 
ATOM   1157  N  N   . CYS A 1 164 ? -18.607 58.505  116.850 1.00 33.85 ? 164  CYS A N   1 
ATOM   1158  C  CA  . CYS A 1 164 ? -18.454 58.340  118.278 1.00 34.37 ? 164  CYS A CA  1 
ATOM   1159  C  C   . CYS A 1 164 ? -19.823 58.031  118.849 1.00 33.79 ? 164  CYS A C   1 
ATOM   1160  O  O   . CYS A 1 164 ? -19.990 57.054  119.575 1.00 35.74 ? 164  CYS A O   1 
ATOM   1161  C  CB  . CYS A 1 164 ? -17.888 59.614  118.925 1.00 36.42 ? 164  CYS A CB  1 
ATOM   1162  S  SG  . CYS A 1 164 ? -17.682 59.490  120.744 1.00 43.70 ? 164  CYS A SG  1 
ATOM   1163  N  N   . MET A 1 165 ? -20.805 58.867  118.539 1.00 32.85 ? 165  MET A N   1 
ATOM   1164  C  CA  . MET A 1 165 ? -22.158 58.652  119.041 1.00 33.89 ? 165  MET A CA  1 
ATOM   1165  C  C   . MET A 1 165 ? -22.791 57.344  118.559 1.00 35.91 ? 165  MET A C   1 
ATOM   1166  O  O   . MET A 1 165 ? -23.386 56.571  119.343 1.00 32.61 ? 165  MET A O   1 
ATOM   1167  C  CB  . MET A 1 165 ? -23.020 59.801  118.610 1.00 38.92 ? 165  MET A CB  1 
ATOM   1168  C  CG  . MET A 1 165 ? -22.579 61.096  119.223 1.00 44.56 ? 165  MET A CG  1 
ATOM   1169  S  SD  . MET A 1 165 ? -22.696 61.016  121.023 1.00 51.91 ? 165  MET A SD  1 
ATOM   1170  C  CE  . MET A 1 165 ? -24.223 60.177  121.266 1.00 42.92 ? 165  MET A CE  1 
ATOM   1171  N  N   . TYR A 1 166 ? -22.657 57.115  117.257 1.00 33.51 ? 166  TYR A N   1 
ATOM   1172  C  CA  . TYR A 1 166 ? -23.175 55.930  116.606 1.00 33.72 ? 166  TYR A CA  1 
ATOM   1173  C  C   . TYR A 1 166 ? -22.812 54.655  117.341 1.00 35.30 ? 166  TYR A C   1 
ATOM   1174  O  O   . TYR A 1 166 ? -23.614 53.736  117.401 1.00 36.97 ? 166  TYR A O   1 
ATOM   1175  C  CB  . TYR A 1 166 ? -22.633 55.857  115.187 1.00 34.25 ? 166  TYR A CB  1 
ATOM   1176  C  CG  . TYR A 1 166 ? -23.078 54.644  114.393 1.00 35.67 ? 166  TYR A CG  1 
ATOM   1177  C  CD1 . TYR A 1 166 ? -24.290 54.645  113.689 1.00 38.71 ? 166  TYR A CD1 1 
ATOM   1178  C  CD2 . TYR A 1 166 ? -22.260 53.516  114.296 1.00 37.54 ? 166  TYR A CD2 1 
ATOM   1179  C  CE1 . TYR A 1 166 ? -24.668 53.541  112.893 1.00 37.68 ? 166  TYR A CE1 1 
ATOM   1180  C  CE2 . TYR A 1 166 ? -22.622 52.417  113.513 1.00 39.55 ? 166  TYR A CE2 1 
ATOM   1181  C  CZ  . TYR A 1 166 ? -23.823 52.437  112.806 1.00 39.62 ? 166  TYR A CZ  1 
ATOM   1182  O  OH  . TYR A 1 166 ? -24.133 51.386  111.969 1.00 35.20 ? 166  TYR A OH  1 
ATOM   1183  N  N   . ASN A 1 167 ? -21.602 54.601  117.891 1.00 35.40 ? 167  ASN A N   1 
ATOM   1184  C  CA  . ASN A 1 167 ? -21.150 53.418  118.598 1.00 39.63 ? 167  ASN A CA  1 
ATOM   1185  C  C   . ASN A 1 167 ? -21.531 53.369  120.074 1.00 41.79 ? 167  ASN A C   1 
ATOM   1186  O  O   . ASN A 1 167 ? -21.292 52.360  120.740 1.00 42.09 ? 167  ASN A O   1 
ATOM   1187  C  CB  . ASN A 1 167 ? -19.634 53.281  118.476 1.00 41.18 ? 167  ASN A CB  1 
ATOM   1188  C  CG  . ASN A 1 167 ? -19.202 52.914  117.085 1.00 44.11 ? 167  ASN A CG  1 
ATOM   1189  O  OD1 . ASN A 1 167 ? -19.745 51.972  116.474 1.00 44.06 ? 167  ASN A OD1 1 
ATOM   1190  N  ND2 . ASN A 1 167 ? -18.217 53.647  116.564 1.00 42.55 ? 167  ASN A ND2 1 
ATOM   1191  N  N   . LYS A 1 168 ? -22.115 54.447  120.589 1.00 40.91 ? 168  LYS A N   1 
ATOM   1192  C  CA  . LYS A 1 168 ? -22.469 54.454  121.989 1.00 39.94 ? 168  LYS A CA  1 
ATOM   1193  C  C   . LYS A 1 168 ? -23.959 54.640  122.214 1.00 39.74 ? 168  LYS A C   1 
ATOM   1194  O  O   . LYS A 1 168 ? -24.388 55.384  123.087 1.00 39.72 ? 168  LYS A O   1 
ATOM   1195  C  CB  . LYS A 1 168 ? -21.659 55.525  122.732 1.00 39.99 ? 168  LYS A CB  1 
ATOM   1196  C  CG  . LYS A 1 168 ? -20.151 55.328  122.696 1.00 40.65 ? 168  LYS A CG  1 
ATOM   1197  C  CD  . LYS A 1 168 ? -19.684 54.146  123.534 1.00 40.83 ? 168  LYS A CD  1 
ATOM   1198  C  CE  . LYS A 1 168 ? -18.162 54.061  123.635 1.00 39.20 ? 168  LYS A CE  1 
ATOM   1199  N  NZ  . LYS A 1 168 ? -17.735 52.851  124.397 1.00 40.02 ? 168  LYS A NZ  1 
ATOM   1200  N  N   . ILE A 1 169 ? -24.764 53.936  121.433 1.00 42.78 ? 169  ILE A N   1 
ATOM   1201  C  CA  . ILE A 1 169 ? -26.207 54.032  121.595 1.00 38.62 ? 169  ILE A CA  1 
ATOM   1202  C  C   . ILE A 1 169 ? -26.642 53.283  122.870 1.00 40.17 ? 169  ILE A C   1 
ATOM   1203  O  O   . ILE A 1 169 ? -26.573 52.052  122.957 1.00 38.52 ? 169  ILE A O   1 
ATOM   1204  C  CB  . ILE A 1 169 ? -26.945 53.408  120.407 1.00 41.25 ? 169  ILE A CB  1 
ATOM   1205  C  CG1 . ILE A 1 169 ? -26.595 54.148  119.102 1.00 37.73 ? 169  ILE A CG1 1 
ATOM   1206  C  CG2 . ILE A 1 169 ? -28.441 53.368  120.725 1.00 38.16 ? 169  ILE A CG2 1 
ATOM   1207  C  CD1 . ILE A 1 169 ? -26.937 55.620  119.110 1.00 36.81 ? 169  ILE A CD1 1 
ATOM   1208  N  N   . PRO A 1 170 ? -27.129 54.021  123.869 1.00 39.78 ? 170  PRO A N   1 
ATOM   1209  C  CA  . PRO A 1 170 ? -27.565 53.407  125.126 1.00 39.65 ? 170  PRO A CA  1 
ATOM   1210  C  C   . PRO A 1 170 ? -28.440 52.155  124.983 1.00 42.04 ? 170  PRO A C   1 
ATOM   1211  O  O   . PRO A 1 170 ? -29.444 52.174  124.274 1.00 41.20 ? 170  PRO A O   1 
ATOM   1212  C  CB  . PRO A 1 170 ? -28.320 54.539  125.821 1.00 36.22 ? 170  PRO A CB  1 
ATOM   1213  C  CG  . PRO A 1 170 ? -27.704 55.808  125.238 1.00 37.30 ? 170  PRO A CG  1 
ATOM   1214  C  CD  . PRO A 1 170 ? -27.480 55.456  123.807 1.00 39.46 ? 170  PRO A CD  1 
ATOM   1215  N  N   . VAL A 1 171 ? -28.064 51.076  125.671 1.00 44.44 ? 171  VAL A N   1 
ATOM   1216  C  CA  . VAL A 1 171 ? -28.850 49.853  125.638 1.00 46.87 ? 171  VAL A CA  1 
ATOM   1217  C  C   . VAL A 1 171 ? -30.252 50.186  126.142 1.00 50.35 ? 171  VAL A C   1 
ATOM   1218  O  O   . VAL A 1 171 ? -30.407 50.906  127.137 1.00 48.55 ? 171  VAL A O   1 
ATOM   1219  C  CB  . VAL A 1 171 ? -28.242 48.766  126.545 1.00 46.13 ? 171  VAL A CB  1 
ATOM   1220  C  CG1 . VAL A 1 171 ? -29.268 47.654  126.795 1.00 44.60 ? 171  VAL A CG1 1 
ATOM   1221  C  CG2 . VAL A 1 171 ? -26.986 48.188  125.877 1.00 46.71 ? 171  VAL A CG2 1 
ATOM   1222  N  N   . GLY A 1 172 ? -31.273 49.703  125.437 1.00 53.50 ? 172  GLY A N   1 
ATOM   1223  C  CA  . GLY A 1 172 ? -32.639 49.946  125.872 1.00 59.91 ? 172  GLY A CA  1 
ATOM   1224  C  C   . GLY A 1 172 ? -33.249 51.181  125.227 1.00 65.78 ? 172  GLY A C   1 
ATOM   1225  O  O   . GLY A 1 172 ? -34.424 51.225  124.871 1.00 66.31 ? 172  GLY A O   1 
ATOM   1226  N  N   . SER A 1 173 ? -32.421 52.213  125.120 1.00 74.12 ? 173  SER A N   1 
ATOM   1227  C  CA  . SER A 1 173 ? -32.781 53.482  124.514 1.00 79.44 ? 173  SER A CA  1 
ATOM   1228  C  C   . SER A 1 173 ? -32.591 53.162  123.057 1.00 80.31 ? 173  SER A C   1 
ATOM   1229  O  O   . SER A 1 173 ? -31.667 53.631  122.419 1.00 78.65 ? 173  SER A O   1 
ATOM   1230  C  CB  . SER A 1 173 ? -31.813 54.595  124.969 1.00 83.08 ? 173  SER A CB  1 
ATOM   1231  O  OG  . SER A 1 173 ? -32.092 55.867  124.410 1.00 84.88 ? 173  SER A OG  1 
ATOM   1232  N  N   . GLU A 1 174 ? -33.503 52.398  122.453 1.00 84.18 ? 174  GLU A N   1 
ATOM   1233  C  CA  . GLU A 1 174 ? -33.414 51.960  121.021 1.00 88.21 ? 174  GLU A CA  1 
ATOM   1234  C  C   . GLU A 1 174 ? -34.346 52.771  119.993 1.00 89.64 ? 174  GLU A C   1 
ATOM   1235  O  O   . GLU A 1 174 ? -34.799 52.274  118.997 1.00 86.95 ? 174  GLU A O   1 
ATOM   1236  C  CB  . GLU A 1 174 ? -33.864 50.506  121.057 1.00 94.19 ? 174  GLU A CB  1 
ATOM   1237  C  CG  . GLU A 1 174 ? -33.349 49.726  122.235 1.00 98.98 ? 174  GLU A CG  1 
ATOM   1238  C  CD  . GLU A 1 174 ? -31.846 49.478  122.112 1.00 99.45 ? 174  GLU A CD  1 
ATOM   1239  O  OE1 . GLU A 1 174 ? -31.055 49.780  123.059 1.00 98.99 ? 174  GLU A OE1 1 
ATOM   1240  O  OE2 . GLU A 1 174 ? -31.456 48.974  121.036 1.00 99.44 ? 174  GLU A OE2 1 
ATOM   1241  N  N   . GLU A 1 175 ? -34.368 54.064  119.889 1.00 89.73 ? 175  GLU A N   1 
ATOM   1242  C  CA  . GLU A 1 175 ? -35.334 54.845  119.081 1.00 89.55 ? 175  GLU A CA  1 
ATOM   1243  C  C   . GLU A 1 175 ? -34.783 55.613  117.878 1.00 86.31 ? 175  GLU A C   1 
ATOM   1244  O  O   . GLU A 1 175 ? -34.804 56.856  117.811 1.00 86.88 ? 175  GLU A O   1 
ATOM   1245  C  CB  . GLU A 1 175 ? -35.605 55.642  120.313 1.00 92.83 ? 175  GLU A CB  1 
ATOM   1246  C  CG  . GLU A 1 175 ? -36.351 56.723  120.620 1.00 96.32 ? 175  GLU A CG  1 
ATOM   1247  C  CD  . GLU A 1 175 ? -35.356 57.430  121.553 1.00 98.65 ? 175  GLU A CD  1 
ATOM   1248  O  OE1 . GLU A 1 175 ? -34.243 57.497  121.000 1.00 99.45 ? 175  GLU A OE1 1 
ATOM   1249  O  OE2 . GLU A 1 175 ? -35.551 57.800  122.768 1.00 99.13 ? 175  GLU A OE2 1 
ATOM   1250  N  N   . GLY A 1 176 ? -34.331 54.883  116.865 1.00 80.30 ? 176  GLY A N   1 
ATOM   1251  C  CA  . GLY A 1 176 ? -33.736 55.401  115.582 1.00 73.81 ? 176  GLY A CA  1 
ATOM   1252  C  C   . GLY A 1 176 ? -32.574 56.386  115.666 1.00 67.65 ? 176  GLY A C   1 
ATOM   1253  O  O   . GLY A 1 176 ? -32.208 56.980  114.677 1.00 70.51 ? 176  GLY A O   1 
ATOM   1254  N  N   . TYR A 1 177 ? -31.989 56.545  116.846 1.00 63.03 ? 177  TYR A N   1 
ATOM   1255  C  CA  . TYR A 1 177 ? -30.822 57.431  117.003 1.00 60.00 ? 177  TYR A CA  1 
ATOM   1256  C  C   . TYR A 1 177 ? -29.762 56.860  116.074 1.00 54.74 ? 177  TYR A C   1 
ATOM   1257  O  O   . TYR A 1 177 ? -29.106 57.581  115.333 1.00 51.25 ? 177  TYR A O   1 
ATOM   1258  C  CB  . TYR A 1 177 ? -30.278 57.305  118.401 1.00 66.70 ? 177  TYR A CB  1 
ATOM   1259  C  CG  . TYR A 1 177 ? -30.999 58.069  119.439 1.00 73.27 ? 177  TYR A CG  1 
ATOM   1260  C  CD1 . TYR A 1 177 ? -32.390 58.194  119.420 1.00 78.59 ? 177  TYR A CD1 1 
ATOM   1261  C  CD2 . TYR A 1 177 ? -30.282 58.610  120.507 1.00 77.44 ? 177  TYR A CD2 1 
ATOM   1262  C  CE1 . TYR A 1 177 ? -33.042 58.852  120.454 1.00 83.10 ? 177  TYR A CE1 1 
ATOM   1263  C  CE2 . TYR A 1 177 ? -30.925 59.251  121.568 1.00 81.50 ? 177  TYR A CE2 1 
ATOM   1264  C  CZ  . TYR A 1 177 ? -32.303 59.364  121.538 1.00 85.15 ? 177  TYR A CZ  1 
ATOM   1265  O  OH  . TYR A 1 177 ? -32.940 59.971  122.596 1.00 89.74 ? 177  TYR A OH  1 
ATOM   1266  N  N   . ARG A 1 178 ? -29.617 55.542  116.133 1.00 48.16 ? 178  ARG A N   1 
ATOM   1267  C  CA  . ARG A 1 178 ? -28.639 54.861  115.315 1.00 49.30 ? 178  ARG A CA  1 
ATOM   1268  C  C   . ARG A 1 178 ? -28.965 55.109  113.844 1.00 50.00 ? 178  ARG A C   1 
ATOM   1269  O  O   . ARG A 1 178 ? -28.080 55.323  113.011 1.00 50.82 ? 178  ARG A O   1 
ATOM   1270  C  CB  . ARG A 1 178 ? -28.672 53.372  115.631 1.00 50.39 ? 178  ARG A CB  1 
ATOM   1271  C  CG  . ARG A 1 178 ? -27.593 52.547  114.954 1.00 58.77 ? 178  ARG A CG  1 
ATOM   1272  C  CD  . ARG A 1 178 ? -27.791 51.064  115.295 1.00 66.76 ? 178  ARG A CD  1 
ATOM   1273  N  NE  . ARG A 1 178 ? -26.973 50.164  114.488 1.00 69.76 ? 178  ARG A NE  1 
ATOM   1274  C  CZ  . ARG A 1 178 ? -25.649 50.103  114.571 1.00 73.12 ? 178  ARG A CZ  1 
ATOM   1275  N  NH1 . ARG A 1 178 ? -25.004 50.899  115.428 1.00 70.70 ? 178  ARG A NH1 1 
ATOM   1276  N  NH2 . ARG A 1 178 ? -24.973 49.242  113.811 1.00 70.10 ? 178  ARG A NH2 1 
ATOM   1277  N  N   . SER A 1 179 ? -30.255 55.078  113.535 1.00 47.95 ? 179  SER A N   1 
ATOM   1278  C  CA  . SER A 1 179 ? -30.732 55.280  112.176 1.00 44.74 ? 179  SER A CA  1 
ATOM   1279  C  C   . SER A 1 179 ? -30.357 56.680  111.668 1.00 41.91 ? 179  SER A C   1 
ATOM   1280  O  O   . SER A 1 179 ? -29.829 56.821  110.561 1.00 36.82 ? 179  SER A O   1 
ATOM   1281  C  CB  . SER A 1 179 ? -32.247 55.094  112.143 1.00 48.77 ? 179  SER A CB  1 
ATOM   1282  O  OG  . SER A 1 179 ? -32.786 55.603  110.935 1.00 55.22 ? 179  SER A OG  1 
ATOM   1283  N  N   . LEU A 1 180 ? -30.654 57.699  112.476 1.00 36.79 ? 180  LEU A N   1 
ATOM   1284  C  CA  . LEU A 1 180 ? -30.338 59.083  112.168 1.00 36.64 ? 180  LEU A CA  1 
ATOM   1285  C  C   . LEU A 1 180 ? -28.821 59.259  111.951 1.00 39.98 ? 180  LEU A C   1 
ATOM   1286  O  O   . LEU A 1 180 ? -28.373 59.702  110.877 1.00 41.43 ? 180  LEU A O   1 
ATOM   1287  C  CB  . LEU A 1 180 ? -30.754 59.977  113.332 1.00 35.43 ? 180  LEU A CB  1 
ATOM   1288  C  CG  . LEU A 1 180 ? -31.295 61.406  113.124 1.00 36.47 ? 180  LEU A CG  1 
ATOM   1289  C  CD1 . LEU A 1 180 ? -30.911 62.253  114.328 1.00 28.56 ? 180  LEU A CD1 1 
ATOM   1290  C  CD2 . LEU A 1 180 ? -30.782 62.021  111.863 1.00 26.44 ? 180  LEU A CD2 1 
ATOM   1291  N  N   . PHE A 1 181 ? -28.017 58.908  112.954 1.00 40.29 ? 181  PHE A N   1 
ATOM   1292  C  CA  . PHE A 1 181 ? -26.568 59.095  112.815 1.00 38.32 ? 181  PHE A CA  1 
ATOM   1293  C  C   . PHE A 1 181 ? -26.020 58.302  111.649 1.00 38.48 ? 181  PHE A C   1 
ATOM   1294  O  O   . PHE A 1 181 ? -25.226 58.821  110.879 1.00 39.11 ? 181  PHE A O   1 
ATOM   1295  C  CB  . PHE A 1 181 ? -25.806 58.686  114.083 1.00 36.50 ? 181  PHE A CB  1 
ATOM   1296  C  CG  . PHE A 1 181 ? -26.263 59.373  115.337 1.00 33.19 ? 181  PHE A CG  1 
ATOM   1297  C  CD1 . PHE A 1 181 ? -26.561 60.726  115.333 1.00 30.91 ? 181  PHE A CD1 1 
ATOM   1298  C  CD2 . PHE A 1 181 ? -26.339 58.668  116.540 1.00 31.56 ? 181  PHE A CD2 1 
ATOM   1299  C  CE1 . PHE A 1 181 ? -26.930 61.379  116.508 1.00 33.46 ? 181  PHE A CE1 1 
ATOM   1300  C  CE2 . PHE A 1 181 ? -26.711 59.321  117.733 1.00 34.20 ? 181  PHE A CE2 1 
ATOM   1301  C  CZ  . PHE A 1 181 ? -27.005 60.670  117.714 1.00 31.27 ? 181  PHE A CZ  1 
ATOM   1302  N  N   . GLY A 1 182 ? -26.443 57.049  111.514 1.00 39.47 ? 182  GLY A N   1 
ATOM   1303  C  CA  . GLY A 1 182 ? -25.947 56.221  110.423 1.00 41.37 ? 182  GLY A CA  1 
ATOM   1304  C  C   . GLY A 1 182 ? -26.233 56.809  109.055 1.00 43.84 ? 182  GLY A C   1 
ATOM   1305  O  O   . GLY A 1 182 ? -25.398 56.787  108.140 1.00 44.33 ? 182  GLY A O   1 
ATOM   1306  N  N   . GLN A 1 183 ? -27.438 57.351  108.929 1.00 46.26 ? 183  GLN A N   1 
ATOM   1307  C  CA  . GLN A 1 183 ? -27.880 57.939  107.693 1.00 46.81 ? 183  GLN A CA  1 
ATOM   1308  C  C   . GLN A 1 183 ? -27.054 59.185  107.365 1.00 45.99 ? 183  GLN A C   1 
ATOM   1309  O  O   . GLN A 1 183 ? -26.534 59.313  106.267 1.00 46.00 ? 183  GLN A O   1 
ATOM   1310  C  CB  . GLN A 1 183 ? -29.362 58.257  107.795 1.00 50.39 ? 183  GLN A CB  1 
ATOM   1311  C  CG  . GLN A 1 183 ? -29.984 58.537  106.464 1.00 63.53 ? 183  GLN A CG  1 
ATOM   1312  C  CD  . GLN A 1 183 ? -29.588 57.501  105.391 1.00 73.97 ? 183  GLN A CD  1 
ATOM   1313  O  OE1 . GLN A 1 183 ? -29.841 56.291  105.543 1.00 79.49 ? 183  GLN A OE1 1 
ATOM   1314  N  NE2 . GLN A 1 183 ? -28.965 57.978  104.302 1.00 72.93 ? 183  GLN A NE2 1 
ATOM   1315  N  N   . VAL A 1 184 ? -26.914 60.094  108.320 1.00 43.41 ? 184  VAL A N   1 
ATOM   1316  C  CA  . VAL A 1 184 ? -26.119 61.292  108.085 1.00 41.15 ? 184  VAL A CA  1 
ATOM   1317  C  C   . VAL A 1 184 ? -24.658 60.913  107.783 1.00 40.59 ? 184  VAL A C   1 
ATOM   1318  O  O   . VAL A 1 184 ? -23.994 61.559  106.975 1.00 38.28 ? 184  VAL A O   1 
ATOM   1319  C  CB  . VAL A 1 184 ? -26.196 62.225  109.313 1.00 43.18 ? 184  VAL A CB  1 
ATOM   1320  C  CG1 . VAL A 1 184 ? -25.221 63.392  109.181 1.00 38.08 ? 184  VAL A CG1 1 
ATOM   1321  C  CG2 . VAL A 1 184 ? -27.627 62.723  109.458 1.00 40.74 ? 184  VAL A CG2 1 
ATOM   1322  N  N   . LEU A 1 185 ? -24.157 59.864  108.427 1.00 37.94 ? 185  LEU A N   1 
ATOM   1323  C  CA  . LEU A 1 185 ? -22.787 59.431  108.177 1.00 40.54 ? 185  LEU A CA  1 
ATOM   1324  C  C   . LEU A 1 185 ? -22.647 58.925  106.747 1.00 43.14 ? 185  LEU A C   1 
ATOM   1325  O  O   . LEU A 1 185 ? -21.671 59.244  106.074 1.00 44.60 ? 185  LEU A O   1 
ATOM   1326  C  CB  . LEU A 1 185 ? -22.362 58.311  109.142 1.00 35.92 ? 185  LEU A CB  1 
ATOM   1327  C  CG  . LEU A 1 185 ? -22.045 58.756  110.567 1.00 36.82 ? 185  LEU A CG  1 
ATOM   1328  C  CD1 . LEU A 1 185 ? -22.235 57.570  111.550 1.00 30.15 ? 185  LEU A CD1 1 
ATOM   1329  C  CD2 . LEU A 1 185 ? -20.618 59.349  110.595 1.00 30.75 ? 185  LEU A CD2 1 
ATOM   1330  N  N   . LYS A 1 186 ? -23.614 58.125  106.300 1.00 44.87 ? 186  LYS A N   1 
ATOM   1331  C  CA  . LYS A 1 186 ? -23.608 57.562  104.949 1.00 48.28 ? 186  LYS A CA  1 
ATOM   1332  C  C   . LYS A 1 186 ? -23.550 58.703  103.924 1.00 47.63 ? 186  LYS A C   1 
ATOM   1333  O  O   . LYS A 1 186 ? -22.826 58.650  102.915 1.00 47.61 ? 186  LYS A O   1 
ATOM   1334  C  CB  . LYS A 1 186 ? -24.886 56.730  104.730 1.00 51.03 ? 186  LYS A CB  1 
ATOM   1335  C  CG  . LYS A 1 186 ? -24.685 55.454  103.925 1.00 52.19 ? 186  LYS A CG  1 
ATOM   1336  C  CD  . LYS A 1 186 ? -24.036 55.756  102.594 1.00 58.48 ? 186  LYS A CD  1 
ATOM   1337  C  CE  . LYS A 1 186 ? -23.745 54.490  101.803 1.00 59.77 ? 186  LYS A CE  1 
ATOM   1338  N  NZ  . LYS A 1 186 ? -23.367 54.812  100.372 1.00 64.95 ? 186  LYS A NZ  1 
ATOM   1339  N  N   . ASP A 1 187 ? -24.346 59.720  104.235 1.00 47.28 ? 187  ASP A N   1 
ATOM   1340  C  CA  . ASP A 1 187 ? -24.515 60.951  103.495 1.00 46.20 ? 187  ASP A CA  1 
ATOM   1341  C  C   . ASP A 1 187 ? -23.163 61.625  103.291 1.00 44.81 ? 187  ASP A C   1 
ATOM   1342  O  O   . ASP A 1 187 ? -22.730 61.865  102.156 1.00 41.56 ? 187  ASP A O   1 
ATOM   1343  C  CB  . ASP A 1 187 ? -25.431 61.831  104.324 1.00 57.73 ? 187  ASP A CB  1 
ATOM   1344  C  CG  . ASP A 1 187 ? -26.138 62.865  103.508 1.00 68.48 ? 187  ASP A CG  1 
ATOM   1345  O  OD1 . ASP A 1 187 ? -26.689 62.461  102.448 1.00 73.81 ? 187  ASP A OD1 1 
ATOM   1346  O  OD2 . ASP A 1 187 ? -26.156 64.067  103.927 1.00 77.05 ? 187  ASP A OD2 1 
ATOM   1347  N  N   . ILE A 1 188 ? -22.494 61.909  104.411 1.00 42.41 ? 188  ILE A N   1 
ATOM   1348  C  CA  . ILE A 1 188 ? -21.185 62.552  104.417 1.00 38.95 ? 188  ILE A CA  1 
ATOM   1349  C  C   . ILE A 1 188 ? -20.106 61.703  103.739 1.00 39.75 ? 188  ILE A C   1 
ATOM   1350  O  O   . ILE A 1 188 ? -19.245 62.218  103.017 1.00 40.92 ? 188  ILE A O   1 
ATOM   1351  C  CB  . ILE A 1 188 ? -20.766 62.877  105.869 1.00 37.66 ? 188  ILE A CB  1 
ATOM   1352  C  CG1 . ILE A 1 188 ? -21.713 63.924  106.443 1.00 36.14 ? 188  ILE A CG1 1 
ATOM   1353  C  CG2 . ILE A 1 188 ? -19.332 63.397  105.921 1.00 34.83 ? 188  ILE A CG2 1 
ATOM   1354  C  CD1 . ILE A 1 188 ? -21.576 64.069  107.932 1.00 38.17 ? 188  ILE A CD1 1 
ATOM   1355  N  N   . VAL A 1 189 ? -20.152 60.396  103.932 1.00 38.96 ? 189  VAL A N   1 
ATOM   1356  C  CA  . VAL A 1 189 ? -19.127 59.572  103.326 1.00 42.81 ? 189  VAL A CA  1 
ATOM   1357  C  C   . VAL A 1 189 ? -19.222 59.663  101.816 1.00 45.81 ? 189  VAL A C   1 
ATOM   1358  O  O   . VAL A 1 189 ? -18.204 59.665  101.112 1.00 50.13 ? 189  VAL A O   1 
ATOM   1359  C  CB  . VAL A 1 189 ? -19.252 58.119  103.747 1.00 43.96 ? 189  VAL A CB  1 
ATOM   1360  C  CG1 . VAL A 1 189 ? -18.062 57.362  103.250 1.00 41.81 ? 189  VAL A CG1 1 
ATOM   1361  C  CG2 . VAL A 1 189 ? -19.334 58.032  105.264 1.00 53.21 ? 189  VAL A CG2 1 
ATOM   1362  N  N   . GLU A 1 190 ? -20.448 59.721  101.319 1.00 44.37 ? 190  GLU A N   1 
ATOM   1363  C  CA  . GLU A 1 190 ? -20.665 59.846  99.897  1.00 43.06 ? 190  GLU A CA  1 
ATOM   1364  C  C   . GLU A 1 190 ? -20.045 61.149  99.410  1.00 40.59 ? 190  GLU A C   1 
ATOM   1365  O  O   . GLU A 1 190 ? -19.427 61.177  98.368  1.00 39.09 ? 190  GLU A O   1 
ATOM   1366  C  CB  . GLU A 1 190 ? -22.167 59.844  99.576  1.00 48.90 ? 190  GLU A CB  1 
ATOM   1367  C  CG  . GLU A 1 190 ? -22.753 58.471  99.401  1.00 53.22 ? 190  GLU A CG  1 
ATOM   1368  C  CD  . GLU A 1 190 ? -21.835 57.571  98.574  1.00 61.63 ? 190  GLU A CD  1 
ATOM   1369  O  OE1 . GLU A 1 190 ? -21.178 58.083  97.629  1.00 63.35 ? 190  GLU A OE1 1 
ATOM   1370  O  OE2 . GLU A 1 190 ? -21.771 56.348  98.861  1.00 62.20 ? 190  GLU A OE2 1 
ATOM   1371  N  N   . LYS A 1 191 ? -20.231 62.231  100.152 1.00 39.81 ? 191  LYS A N   1 
ATOM   1372  C  CA  . LYS A 1 191 ? -19.662 63.501  99.749  1.00 42.49 ? 191  LYS A CA  1 
ATOM   1373  C  C   . LYS A 1 191 ? -18.133 63.530  99.945  1.00 45.69 ? 191  LYS A C   1 
ATOM   1374  O  O   . LYS A 1 191 ? -17.412 64.231  99.206  1.00 42.86 ? 191  LYS A O   1 
ATOM   1375  C  CB  . LYS A 1 191 ? -20.326 64.633  100.523 1.00 39.83 ? 191  LYS A CB  1 
ATOM   1376  C  CG  . LYS A 1 191 ? -21.811 64.690  100.306 1.00 39.12 ? 191  LYS A CG  1 
ATOM   1377  C  CD  . LYS A 1 191 ? -22.353 65.944  100.946 1.00 42.66 ? 191  LYS A CD  1 
ATOM   1378  C  CE  . LYS A 1 191 ? -23.851 66.078  100.797 1.00 41.98 ? 191  LYS A CE  1 
ATOM   1379  N  NZ  . LYS A 1 191 ? -24.448 66.798  101.980 1.00 48.62 ? 191  LYS A NZ  1 
ATOM   1380  N  N   . ILE A 1 192 ? -17.623 62.791  100.933 1.00 45.45 ? 192  ILE A N   1 
ATOM   1381  C  CA  . ILE A 1 192 ? -16.175 62.785  101.111 1.00 46.18 ? 192  ILE A CA  1 
ATOM   1382  C  C   . ILE A 1 192 ? -15.612 62.020  99.909  1.00 47.71 ? 192  ILE A C   1 
ATOM   1383  O  O   . ILE A 1 192 ? -14.684 62.481  99.212  1.00 42.68 ? 192  ILE A O   1 
ATOM   1384  C  CB  . ILE A 1 192 ? -15.744 62.119  102.444 1.00 40.80 ? 192  ILE A CB  1 
ATOM   1385  C  CG1 . ILE A 1 192 ? -15.811 63.150  103.568 1.00 41.27 ? 192  ILE A CG1 1 
ATOM   1386  C  CG2 . ILE A 1 192 ? -14.322 61.588  102.330 1.00 36.00 ? 192  ILE A CG2 1 
ATOM   1387  C  CD1 . ILE A 1 192 ? -15.717 62.546  104.947 1.00 44.58 ? 192  ILE A CD1 1 
ATOM   1388  N  N   . SER A 1 193 ? -16.170 60.842  99.666  1.00 49.62 ? 193  SER A N   1 
ATOM   1389  C  CA  . SER A 1 193 ? -15.738 60.076  98.512  1.00 54.17 ? 193  SER A CA  1 
ATOM   1390  C  C   . SER A 1 193 ? -16.127 61.028  97.406  1.00 54.92 ? 193  SER A C   1 
ATOM   1391  O  O   . SER A 1 193 ? -16.921 61.938  97.645  1.00 61.86 ? 193  SER A O   1 
ATOM   1392  C  CB  . SER A 1 193 ? -16.545 58.792  98.395  1.00 54.87 ? 193  SER A CB  1 
ATOM   1393  O  OG  . SER A 1 193 ? -16.225 58.127  97.187  1.00 60.26 ? 193  SER A OG  1 
ATOM   1394  N  N   . MET A 1 194 ? -15.593 60.875  96.215  1.00 50.87 ? 194  MET A N   1 
ATOM   1395  C  CA  . MET A 1 194 ? -15.982 61.811  95.162  1.00 54.56 ? 194  MET A CA  1 
ATOM   1396  C  C   . MET A 1 194 ? -15.422 63.209  95.344  1.00 52.48 ? 194  MET A C   1 
ATOM   1397  O  O   . MET A 1 194 ? -15.797 64.128  94.635  1.00 56.70 ? 194  MET A O   1 
ATOM   1398  C  CB  . MET A 1 194 ? -17.511 61.878  94.998  1.00 57.66 ? 194  MET A CB  1 
ATOM   1399  C  CG  . MET A 1 194 ? -18.213 63.068  95.584  1.00 61.74 ? 194  MET A CG  1 
ATOM   1400  S  SD  . MET A 1 194 ? -19.975 62.907  95.212  1.00 75.58 ? 194  MET A SD  1 
ATOM   1401  C  CE  . MET A 1 194 ? -20.505 64.663  95.182  1.00 71.47 ? 194  MET A CE  1 
ATOM   1402  N  N   . LYS A 1 195 ? -14.546 63.367  96.324  1.00 50.79 ? 195  LYS A N   1 
ATOM   1403  C  CA  . LYS A 1 195 ? -13.822 64.612  96.537  1.00 45.23 ? 195  LYS A CA  1 
ATOM   1404  C  C   . LYS A 1 195 ? -12.414 64.035  96.502  1.00 45.08 ? 195  LYS A C   1 
ATOM   1405  O  O   . LYS A 1 195 ? -11.426 64.750  96.611  1.00 44.74 ? 195  LYS A O   1 
ATOM   1406  C  CB  . LYS A 1 195 ? -14.104 65.206  97.897  1.00 46.97 ? 195  LYS A CB  1 
ATOM   1407  C  CG  . LYS A 1 195 ? -15.170 66.244  97.877  1.00 51.14 ? 195  LYS A CG  1 
ATOM   1408  C  CD  . LYS A 1 195 ? -14.745 67.433  97.048  1.00 53.95 ? 195  LYS A CD  1 
ATOM   1409  C  CE  . LYS A 1 195 ? -15.814 68.511  97.084  1.00 58.17 ? 195  LYS A CE  1 
ATOM   1410  N  NZ  . LYS A 1 195 ? -15.311 69.800  96.547  1.00 60.11 ? 195  LYS A NZ  1 
ATOM   1411  N  N   . ILE A 1 196 ? -12.380 62.708  96.337  1.00 43.00 ? 196  ILE A N   1 
ATOM   1412  C  CA  . ILE A 1 196 ? -11.187 61.894  96.265  1.00 42.94 ? 196  ILE A CA  1 
ATOM   1413  C  C   . ILE A 1 196 ? -10.602 61.889  94.847  1.00 47.35 ? 196  ILE A C   1 
ATOM   1414  O  O   . ILE A 1 196 ? -11.157 61.252  93.945  1.00 46.29 ? 196  ILE A O   1 
ATOM   1415  C  CB  . ILE A 1 196 ? -11.505 60.421  96.643  1.00 40.54 ? 196  ILE A CB  1 
ATOM   1416  C  CG1 . ILE A 1 196 ? -11.949 60.330  98.096  1.00 43.01 ? 196  ILE A CG1 1 
ATOM   1417  C  CG2 . ILE A 1 196 ? -10.278 59.533  96.433  1.00 40.25 ? 196  ILE A CG2 1 
ATOM   1418  C  CD1 . ILE A 1 196 ? -12.221 58.902  98.575  1.00 37.73 ? 196  ILE A CD1 1 
ATOM   1419  N  N   . LYS A 1 197 ? -9.476  62.588  94.669  1.00 49.61 ? 197  LYS A N   1 
ATOM   1420  C  CA  . LYS A 1 197 ? -8.762  62.664  93.396  1.00 48.08 ? 197  LYS A CA  1 
ATOM   1421  C  C   . LYS A 1 197 ? -8.161  61.310  93.013  1.00 51.50 ? 197  LYS A C   1 
ATOM   1422  O  O   . LYS A 1 197 ? -8.072  60.378  93.823  1.00 48.78 ? 197  LYS A O   1 
ATOM   1423  C  CB  . LYS A 1 197 ? -7.622  63.669  93.489  1.00 48.98 ? 197  LYS A CB  1 
ATOM   1424  C  CG  . LYS A 1 197 ? -7.946  65.070  93.060  1.00 47.70 ? 197  LYS A CG  1 
ATOM   1425  C  CD  . LYS A 1 197 ? -8.920  65.752  93.958  1.00 51.07 ? 197  LYS A CD  1 
ATOM   1426  C  CE  . LYS A 1 197 ? -9.092  67.184  93.476  1.00 53.29 ? 197  LYS A CE  1 
ATOM   1427  N  NZ  . LYS A 1 197 ? -7.757  67.835  93.327  1.00 52.82 ? 197  LYS A NZ  1 
ATOM   1428  N  N   . ASP A 1 198 ? -7.730  61.206  91.764  1.00 55.81 ? 198  ASP A N   1 
ATOM   1429  C  CA  . ASP A 1 198 ? -7.140  59.960  91.300  1.00 58.61 ? 198  ASP A CA  1 
ATOM   1430  C  C   . ASP A 1 198 ? -5.736  59.832  91.848  1.00 56.47 ? 198  ASP A C   1 
ATOM   1431  O  O   . ASP A 1 198 ? -5.243  58.717  92.063  1.00 55.17 ? 198  ASP A O   1 
ATOM   1432  C  CB  . ASP A 1 198 ? -7.144  59.920  89.779  1.00 63.79 ? 198  ASP A CB  1 
ATOM   1433  C  CG  . ASP A 1 198 ? -8.556  59.975  89.212  1.00 72.45 ? 198  ASP A CG  1 
ATOM   1434  O  OD1 . ASP A 1 198 ? -9.512  60.144  90.013  1.00 72.45 ? 198  ASP A OD1 1 
ATOM   1435  O  OD2 . ASP A 1 198 ? -8.715  59.856  87.972  1.00 75.92 ? 198  ASP A OD2 1 
ATOM   1436  N  N   . ASN A 1 199 ? -5.110  60.984  92.094  1.00 54.59 ? 199  ASN A N   1 
ATOM   1437  C  CA  . ASN A 1 199 ? -3.765  61.017  92.646  1.00 52.91 ? 199  ASN A CA  1 
ATOM   1438  C  C   . ASN A 1 199 ? -3.747  60.579  94.115  1.00 52.76 ? 199  ASN A C   1 
ATOM   1439  O  O   . ASN A 1 199 ? -2.678  60.336  94.667  1.00 55.27 ? 199  ASN A O   1 
ATOM   1440  C  CB  . ASN A 1 199 ? -3.142  62.416  92.515  1.00 51.59 ? 199  ASN A CB  1 
ATOM   1441  C  CG  . ASN A 1 199 ? -3.983  63.511  93.160  1.00 57.45 ? 199  ASN A CG  1 
ATOM   1442  O  OD1 . ASN A 1 199 ? -4.832  63.257  94.029  1.00 55.64 ? 199  ASN A OD1 1 
ATOM   1443  N  ND2 . ASN A 1 199 ? -3.730  64.752  92.747  1.00 56.85 ? 199  ASN A ND2 1 
ATOM   1444  N  N   . GLY A 1 200 ? -4.921  60.475  94.741  1.00 48.75 ? 200  GLY A N   1 
ATOM   1445  C  CA  . GLY A 1 200 ? -4.975  60.058  96.133  1.00 46.43 ? 200  GLY A CA  1 
ATOM   1446  C  C   . GLY A 1 200 ? -5.371  61.141  97.130  1.00 44.20 ? 200  GLY A C   1 
ATOM   1447  O  O   . GLY A 1 200 ? -5.699  60.839  98.273  1.00 43.89 ? 200  GLY A O   1 
ATOM   1448  N  N   . ILE A 1 201 ? -5.308  62.396  96.705  1.00 41.38 ? 201  ILE A N   1 
ATOM   1449  C  CA  . ILE A 1 201 ? -5.677  63.519  97.544  1.00 42.52 ? 201  ILE A CA  1 
ATOM   1450  C  C   . ILE A 1 201 ? -7.157  63.398  97.842  1.00 45.07 ? 201  ILE A C   1 
ATOM   1451  O  O   . ILE A 1 201 ? -7.890  62.794  97.053  1.00 46.71 ? 201  ILE A O   1 
ATOM   1452  C  CB  . ILE A 1 201 ? -5.439  64.849  96.800  1.00 41.83 ? 201  ILE A CB  1 
ATOM   1453  C  CG1 . ILE A 1 201 ? -3.961  65.195  96.836  1.00 40.72 ? 201  ILE A CG1 1 
ATOM   1454  C  CG2 . ILE A 1 201 ? -6.270  65.963  97.401  1.00 39.88 ? 201  ILE A CG2 1 
ATOM   1455  C  CD1 . ILE A 1 201 ? -3.667  66.599  96.346  1.00 46.31 ? 201  ILE A CD1 1 
ATOM   1456  N  N   . ILE A 1 202 ? -7.591  63.938  98.985  1.00 44.46 ? 202  ILE A N   1 
ATOM   1457  C  CA  . ILE A 1 202 ? -9.010  63.927  99.347  1.00 41.60 ? 202  ILE A CA  1 
ATOM   1458  C  C   . ILE A 1 202 ? -9.431  65.346  99.696  1.00 44.40 ? 202  ILE A C   1 
ATOM   1459  O  O   . ILE A 1 202 ? -9.217  65.814  100.814 1.00 44.87 ? 202  ILE A O   1 
ATOM   1460  C  CB  . ILE A 1 202 ? -9.275  63.014  100.513 1.00 37.63 ? 202  ILE A CB  1 
ATOM   1461  C  CG1 . ILE A 1 202 ? -8.665  61.641  100.226 1.00 35.29 ? 202  ILE A CG1 1 
ATOM   1462  C  CG2 . ILE A 1 202 ? -10.781 62.863  100.702 1.00 40.67 ? 202  ILE A CG2 1 
ATOM   1463  C  CD1 . ILE A 1 202 ? -8.926  60.599  101.295 1.00 35.77 ? 202  ILE A CD1 1 
ATOM   1464  N  N   . GLY A 1 203 ? -10.035 66.027  98.726  1.00 46.44 ? 203  GLY A N   1 
ATOM   1465  C  CA  . GLY A 1 203 ? -10.412 67.413  98.926  1.00 49.02 ? 203  GLY A CA  1 
ATOM   1466  C  C   . GLY A 1 203 ? -9.156  68.103  98.431  1.00 50.75 ? 203  GLY A C   1 
ATOM   1467  O  O   . GLY A 1 203 ? -9.007  68.330  97.227  1.00 53.49 ? 203  GLY A O   1 
ATOM   1468  N  N   . ASP A 1 204 ? -8.244  68.411  99.353  1.00 50.46 ? 204  ASP A N   1 
ATOM   1469  C  CA  . ASP A 1 204 ? -6.955  69.026  99.023  1.00 48.86 ? 204  ASP A CA  1 
ATOM   1470  C  C   . ASP A 1 204 ? -5.907  68.410  99.962  1.00 48.51 ? 204  ASP A C   1 
ATOM   1471  O  O   . ASP A 1 204 ? -6.259  67.631  100.846 1.00 49.46 ? 204  ASP A O   1 
ATOM   1472  C  CB  . ASP A 1 204 ? -7.032  70.552  99.173  1.00 50.50 ? 204  ASP A CB  1 
ATOM   1473  C  CG  . ASP A 1 204 ? -7.392  71.000  100.582 1.00 56.94 ? 204  ASP A CG  1 
ATOM   1474  O  OD1 . ASP A 1 204 ? -6.604  70.734  101.517 1.00 59.34 ? 204  ASP A OD1 1 
ATOM   1475  O  OD2 . ASP A 1 204 ? -8.462  71.634  100.750 1.00 60.54 ? 204  ASP A OD2 1 
ATOM   1476  N  N   . ILE A 1 205 ? -4.628  68.731  99.802  1.00 48.41 ? 205  ILE A N   1 
ATOM   1477  C  CA  . ILE A 1 205 ? -3.650  68.115  100.698 1.00 47.79 ? 205  ILE A CA  1 
ATOM   1478  C  C   . ILE A 1 205 ? -3.846  68.419  102.162 1.00 45.24 ? 205  ILE A C   1 
ATOM   1479  O  O   . ILE A 1 205 ? -3.700  67.537  103.016 1.00 43.68 ? 205  ILE A O   1 
ATOM   1480  C  CB  . ILE A 1 205 ? -2.226  68.515  100.405 1.00 48.61 ? 205  ILE A CB  1 
ATOM   1481  C  CG1 . ILE A 1 205 ? -2.188  69.964  99.982  1.00 49.12 ? 205  ILE A CG1 1 
ATOM   1482  C  CG2 . ILE A 1 205 ? -1.613  67.532  99.457  1.00 49.36 ? 205  ILE A CG2 1 
ATOM   1483  C  CD1 . ILE A 1 205 ? -0.806  70.532  100.104 1.00 53.71 ? 205  ILE A CD1 1 
ATOM   1484  N  N   . TYR A 1 206 ? -4.149  69.670  102.471 1.00 41.17 ? 206  TYR A N   1 
ATOM   1485  C  CA  . TYR A 1 206 ? -4.327  70.018  103.870 1.00 37.52 ? 206  TYR A CA  1 
ATOM   1486  C  C   . TYR A 1 206 ? -5.620  69.571  104.516 1.00 35.97 ? 206  TYR A C   1 
ATOM   1487  O  O   . TYR A 1 206 ? -5.849  69.847  105.692 1.00 38.21 ? 206  TYR A O   1 
ATOM   1488  C  CB  . TYR A 1 206 ? -4.093  71.510  104.056 1.00 33.17 ? 206  TYR A CB  1 
ATOM   1489  C  CG  . TYR A 1 206 ? -2.694  71.840  103.634 1.00 33.53 ? 206  TYR A CG  1 
ATOM   1490  C  CD1 . TYR A 1 206 ? -1.612  71.133  104.168 1.00 34.26 ? 206  TYR A CD1 1 
ATOM   1491  C  CD2 . TYR A 1 206 ? -2.445  72.796  102.666 1.00 27.59 ? 206  TYR A CD2 1 
ATOM   1492  C  CE1 . TYR A 1 206 ? -0.318  71.370  103.743 1.00 34.79 ? 206  TYR A CE1 1 
ATOM   1493  C  CE2 . TYR A 1 206 ? -1.179  73.040  102.236 1.00 32.99 ? 206  TYR A CE2 1 
ATOM   1494  C  CZ  . TYR A 1 206 ? -0.108  72.325  102.772 1.00 36.77 ? 206  TYR A CZ  1 
ATOM   1495  O  OH  . TYR A 1 206 ? 1.166   72.553  102.324 1.00 35.39 ? 206  TYR A OH  1 
ATOM   1496  N  N   . SER A 1 207 ? -6.455  68.865  103.763 1.00 33.18 ? 207  SER A N   1 
ATOM   1497  C  CA  . SER A 1 207 ? -7.705  68.362  104.316 1.00 32.27 ? 207  SER A CA  1 
ATOM   1498  C  C   . SER A 1 207 ? -7.654  66.844  104.245 1.00 31.48 ? 207  SER A C   1 
ATOM   1499  O  O   . SER A 1 207 ? -8.517  66.164  104.778 1.00 32.75 ? 207  SER A O   1 
ATOM   1500  C  CB  . SER A 1 207 ? -8.929  68.893  103.518 1.00 36.71 ? 207  SER A CB  1 
ATOM   1501  O  OG  . SER A 1 207 ? -9.093  68.282  102.226 1.00 38.27 ? 207  SER A OG  1 
ATOM   1502  N  N   . THR A 1 208 ? -6.630  66.310  103.593 1.00 27.68 ? 208  THR A N   1 
ATOM   1503  C  CA  . THR A 1 208 ? -6.531  64.878  103.427 1.00 29.02 ? 208  THR A CA  1 
ATOM   1504  C  C   . THR A 1 208 ? -6.329  64.066  104.711 1.00 30.17 ? 208  THR A C   1 
ATOM   1505  O  O   . THR A 1 208 ? -6.885  62.972  104.863 1.00 32.11 ? 208  THR A O   1 
ATOM   1506  C  CB  . THR A 1 208 ? -5.435  64.565  102.402 1.00 31.23 ? 208  THR A CB  1 
ATOM   1507  O  OG1 . THR A 1 208 ? -5.667  65.368  101.230 1.00 32.16 ? 208  THR A OG1 1 
ATOM   1508  C  CG2 . THR A 1 208 ? -5.468  63.079  102.003 1.00 27.07 ? 208  THR A CG2 1 
ATOM   1509  N  N   . GLY A 1 209 ? -5.552  64.601  105.644 1.00 30.46 ? 209  GLY A N   1 
ATOM   1510  C  CA  . GLY A 1 209 ? -5.317  63.900  106.897 1.00 28.64 ? 209  GLY A CA  1 
ATOM   1511  C  C   . GLY A 1 209 ? -6.612  63.646  107.627 1.00 33.18 ? 209  GLY A C   1 
ATOM   1512  O  O   . GLY A 1 209 ? -6.914  62.495  108.011 1.00 32.10 ? 209  GLY A O   1 
ATOM   1513  N  N   . LEU A 1 210 ? -7.389  64.716  107.828 1.00 30.82 ? 210  LEU A N   1 
ATOM   1514  C  CA  . LEU A 1 210 ? -8.647  64.554  108.508 1.00 31.92 ? 210  LEU A CA  1 
ATOM   1515  C  C   . LEU A 1 210 ? -9.538  63.586  107.750 1.00 31.71 ? 210  LEU A C   1 
ATOM   1516  O  O   . LEU A 1 210 ? -10.197 62.744  108.351 1.00 33.01 ? 210  LEU A O   1 
ATOM   1517  C  CB  . LEU A 1 210 ? -9.355  65.889  108.673 1.00 33.35 ? 210  LEU A CB  1 
ATOM   1518  C  CG  . LEU A 1 210 ? -8.598  66.867  109.558 1.00 38.61 ? 210  LEU A CG  1 
ATOM   1519  C  CD1 . LEU A 1 210 ? -9.367  68.193  109.579 1.00 35.00 ? 210  LEU A CD1 1 
ATOM   1520  C  CD2 . LEU A 1 210 ? -8.421  66.285  110.965 1.00 34.94 ? 210  LEU A CD2 1 
ATOM   1521  N  N   . ALA A 1 211 ? -9.542  63.673  106.431 1.00 30.92 ? 211  ALA A N   1 
ATOM   1522  C  CA  . ALA A 1 211 ? -10.395 62.782  105.655 1.00 34.55 ? 211  ALA A CA  1 
ATOM   1523  C  C   . ALA A 1 211 ? -9.985  61.309  105.856 1.00 36.68 ? 211  ALA A C   1 
ATOM   1524  O  O   . ALA A 1 211 ? -10.831 60.398  105.886 1.00 38.53 ? 211  ALA A O   1 
ATOM   1525  C  CB  . ALA A 1 211 ? -10.345 63.164  104.177 1.00 33.75 ? 211  ALA A CB  1 
ATOM   1526  N  N   . MET A 1 212 ? -8.691  61.069  106.000 1.00 36.41 ? 212  MET A N   1 
ATOM   1527  C  CA  . MET A 1 212 ? -8.231  59.703  106.221 1.00 39.10 ? 212  MET A CA  1 
ATOM   1528  C  C   . MET A 1 212 ? -8.768  59.166  107.555 1.00 38.86 ? 212  MET A C   1 
ATOM   1529  O  O   . MET A 1 212 ? -9.097  57.986  107.683 1.00 36.63 ? 212  MET A O   1 
ATOM   1530  C  CB  . MET A 1 212 ? -6.702  59.651  106.227 1.00 39.67 ? 212  MET A CB  1 
ATOM   1531  C  CG  . MET A 1 212 ? -6.074  60.109  104.916 1.00 44.41 ? 212  MET A CG  1 
ATOM   1532  S  SD  . MET A 1 212 ? -4.277  60.073  104.996 1.00 45.19 ? 212  MET A SD  1 
ATOM   1533  C  CE  . MET A 1 212 ? -4.050  58.299  104.963 1.00 41.91 ? 212  MET A CE  1 
ATOM   1534  N  N   . GLN A 1 213 ? -8.846  60.021  108.562 1.00 37.02 ? 213  GLN A N   1 
ATOM   1535  C  CA  . GLN A 1 213 ? -9.361  59.541  109.823 1.00 38.19 ? 213  GLN A CA  1 
ATOM   1536  C  C   . GLN A 1 213 ? -10.814 59.159  109.652 1.00 38.47 ? 213  GLN A C   1 
ATOM   1537  O  O   . GLN A 1 213 ? -11.241 58.075  110.060 1.00 40.59 ? 213  GLN A O   1 
ATOM   1538  C  CB  . GLN A 1 213 ? -9.248  60.599  110.909 1.00 37.19 ? 213  GLN A CB  1 
ATOM   1539  C  CG  . GLN A 1 213 ? -7.856  60.853  111.384 1.00 35.03 ? 213  GLN A CG  1 
ATOM   1540  C  CD  . GLN A 1 213 ? -7.878  61.709  112.608 1.00 34.18 ? 213  GLN A CD  1 
ATOM   1541  O  OE1 . GLN A 1 213 ? -7.095  62.643  112.745 1.00 39.17 ? 213  GLN A OE1 1 
ATOM   1542  N  NE2 . GLN A 1 213 ? -8.789  61.403  113.516 1.00 33.53 ? 213  GLN A NE2 1 
ATOM   1543  N  N   . ALA A 1 214 ? -11.579 60.057  109.047 1.00 36.36 ? 214  ALA A N   1 
ATOM   1544  C  CA  . ALA A 1 214 ? -12.990 59.802  108.845 1.00 33.73 ? 214  ALA A CA  1 
ATOM   1545  C  C   . ALA A 1 214 ? -13.216 58.512  108.046 1.00 33.59 ? 214  ALA A C   1 
ATOM   1546  O  O   . ALA A 1 214 ? -14.007 57.655  108.446 1.00 32.21 ? 214  ALA A O   1 
ATOM   1547  C  CB  . ALA A 1 214 ? -13.647 61.012  108.143 1.00 33.27 ? 214  ALA A CB  1 
ATOM   1548  N  N   . LEU A 1 215 ? -12.514 58.347  106.934 1.00 31.79 ? 215  LEU A N   1 
ATOM   1549  C  CA  . LEU A 1 215 ? -12.741 57.144  106.127 1.00 35.34 ? 215  LEU A CA  1 
ATOM   1550  C  C   . LEU A 1 215 ? -12.415 55.832  106.823 1.00 37.59 ? 215  LEU A C   1 
ATOM   1551  O  O   . LEU A 1 215 ? -13.070 54.817  106.578 1.00 39.44 ? 215  LEU A O   1 
ATOM   1552  C  CB  . LEU A 1 215 ? -11.984 57.211  104.783 1.00 30.14 ? 215  LEU A CB  1 
ATOM   1553  C  CG  . LEU A 1 215 ? -12.484 58.314  103.849 1.00 31.91 ? 215  LEU A CG  1 
ATOM   1554  C  CD1 . LEU A 1 215 ? -11.566 58.458  102.651 1.00 30.39 ? 215  LEU A CD1 1 
ATOM   1555  C  CD2 . LEU A 1 215 ? -13.904 58.006  103.440 1.00 26.01 ? 215  LEU A CD2 1 
ATOM   1556  N  N   . SER A 1 216 ? -11.427 55.833  107.704 1.00 38.48 ? 216  SER A N   1 
ATOM   1557  C  CA  . SER A 1 216 ? -11.059 54.590  108.367 1.00 38.98 ? 216  SER A CA  1 
ATOM   1558  C  C   . SER A 1 216 ? -11.980 54.231  109.507 1.00 38.42 ? 216  SER A C   1 
ATOM   1559  O  O   . SER A 1 216 ? -11.933 53.135  110.048 1.00 39.83 ? 216  SER A O   1 
ATOM   1560  C  CB  . SER A 1 216 ? -9.602  54.668  108.857 1.00 39.90 ? 216  SER A CB  1 
ATOM   1561  O  OG  . SER A 1 216 ? -9.191  56.000  109.121 1.00 50.02 ? 216  SER A OG  1 
ATOM   1562  N  N   . VAL A 1 217 ? -12.883 55.137  109.814 1.00 39.36 ? 217  VAL A N   1 
ATOM   1563  C  CA  . VAL A 1 217 ? -13.751 54.976  110.955 1.00 35.89 ? 217  VAL A CA  1 
ATOM   1564  C  C   . VAL A 1 217 ? -15.282 54.985  110.730 1.00 38.32 ? 217  VAL A C   1 
ATOM   1565  O  O   . VAL A 1 217 ? -16.024 54.529  111.608 1.00 37.45 ? 217  VAL A O   1 
ATOM   1566  C  CB  . VAL A 1 217 ? -13.303 56.072  111.956 1.00 36.95 ? 217  VAL A CB  1 
ATOM   1567  C  CG1 . VAL A 1 217 ? -14.468 56.795  112.554 1.00 34.75 ? 217  VAL A CG1 1 
ATOM   1568  C  CG2 . VAL A 1 217 ? -12.392 55.462  112.972 1.00 37.16 ? 217  VAL A CG2 1 
ATOM   1569  N  N   . THR A 1 218 ? -15.779 55.490  109.594 1.00 38.50 ? 218  THR A N   1 
ATOM   1570  C  CA  . THR A 1 218 ? -17.235 55.486  109.412 1.00 42.64 ? 218  THR A CA  1 
ATOM   1571  C  C   . THR A 1 218 ? -17.723 54.073  109.353 1.00 43.66 ? 218  THR A C   1 
ATOM   1572  O  O   . THR A 1 218 ? -17.093 53.213  108.738 1.00 44.60 ? 218  THR A O   1 
ATOM   1573  C  CB  . THR A 1 218 ? -17.746 56.153  108.108 1.00 45.93 ? 218  THR A CB  1 
ATOM   1574  O  OG1 . THR A 1 218 ? -16.807 55.934  107.048 1.00 47.29 ? 218  THR A OG1 1 
ATOM   1575  C  CG2 . THR A 1 218 ? -18.032 57.625  108.319 1.00 46.31 ? 218  THR A CG2 1 
ATOM   1576  N  N   . PRO A 1 219 ? -18.881 53.819  109.966 1.00 46.42 ? 219  PRO A N   1 
ATOM   1577  C  CA  . PRO A 1 219 ? -19.479 52.481  109.996 1.00 49.03 ? 219  PRO A CA  1 
ATOM   1578  C  C   . PRO A 1 219 ? -19.857 51.911  108.636 1.00 51.62 ? 219  PRO A C   1 
ATOM   1579  O  O   . PRO A 1 219 ? -19.862 50.688  108.442 1.00 52.48 ? 219  PRO A O   1 
ATOM   1580  C  CB  . PRO A 1 219 ? -20.684 52.660  110.935 1.00 45.80 ? 219  PRO A CB  1 
ATOM   1581  C  CG  . PRO A 1 219 ? -21.024 54.092  110.811 1.00 44.64 ? 219  PRO A CG  1 
ATOM   1582  C  CD  . PRO A 1 219 ? -19.691 54.787  110.728 1.00 43.60 ? 219  PRO A CD  1 
ATOM   1583  N  N   . GLU A 1 220 ? -20.147 52.803  107.694 1.00 56.48 ? 220  GLU A N   1 
ATOM   1584  C  CA  . GLU A 1 220 ? -20.557 52.401  106.350 1.00 63.08 ? 220  GLU A CA  1 
ATOM   1585  C  C   . GLU A 1 220 ? -19.786 53.106  105.219 1.00 62.53 ? 220  GLU A C   1 
ATOM   1586  O  O   . GLU A 1 220 ? -19.931 54.310  104.990 1.00 61.34 ? 220  GLU A O   1 
ATOM   1587  C  CB  . GLU A 1 220 ? -22.077 52.637  106.211 1.00 69.02 ? 220  GLU A CB  1 
ATOM   1588  C  CG  . GLU A 1 220 ? -22.656 52.482  104.814 1.00 74.70 ? 220  GLU A CG  1 
ATOM   1589  C  CD  . GLU A 1 220 ? -22.680 51.051  104.346 1.00 79.11 ? 220  GLU A CD  1 
ATOM   1590  O  OE1 . GLU A 1 220 ? -21.607 50.400  104.358 1.00 80.65 ? 220  GLU A OE1 1 
ATOM   1591  O  OE2 . GLU A 1 220 ? -23.774 50.583  103.959 1.00 81.41 ? 220  GLU A OE2 1 
ATOM   1592  N  N   . PRO A 1 221 ? -18.950 52.350  104.487 1.00 65.30 ? 221  PRO A N   1 
ATOM   1593  C  CA  . PRO A 1 221 ? -18.175 52.938  103.382 1.00 65.90 ? 221  PRO A CA  1 
ATOM   1594  C  C   . PRO A 1 221 ? -19.084 53.446  102.274 1.00 68.38 ? 221  PRO A C   1 
ATOM   1595  O  O   . PRO A 1 221 ? -20.299 53.250  102.321 1.00 68.74 ? 221  PRO A O   1 
ATOM   1596  C  CB  . PRO A 1 221 ? -17.299 51.779  102.914 1.00 63.70 ? 221  PRO A CB  1 
ATOM   1597  C  CG  . PRO A 1 221 ? -18.144 50.566  103.220 1.00 62.27 ? 221  PRO A CG  1 
ATOM   1598  C  CD  . PRO A 1 221 ? -18.695 50.899  104.598 1.00 64.76 ? 221  PRO A CD  1 
ATOM   1599  N  N   . SER A 1 222 ? -18.499 54.103  101.280 1.00 71.24 ? 222  SER A N   1 
ATOM   1600  C  CA  . SER A 1 222 ? -19.284 54.625  100.167 1.00 73.18 ? 222  SER A CA  1 
ATOM   1601  C  C   . SER A 1 222 ? -19.264 53.598  99.044  1.00 75.62 ? 222  SER A C   1 
ATOM   1602  O  O   . SER A 1 222 ? -18.408 52.712  99.037  1.00 74.96 ? 222  SER A O   1 
ATOM   1603  C  CB  . SER A 1 222 ? -18.691 55.938  99.673  1.00 73.23 ? 222  SER A CB  1 
ATOM   1604  O  OG  . SER A 1 222 ? -17.376 55.734  99.185  1.00 75.98 ? 222  SER A OG  1 
ATOM   1605  N  N   . LYS A 1 223 ? -20.207 53.715  98.104  1.00 79.00 ? 223  LYS A N   1 
ATOM   1606  C  CA  . LYS A 1 223 ? -20.289 52.788  96.971  1.00 79.78 ? 223  LYS A CA  1 
ATOM   1607  C  C   . LYS A 1 223 ? -18.936 52.665  96.267  1.00 80.17 ? 223  LYS A C   1 
ATOM   1608  O  O   . LYS A 1 223 ? -18.407 51.560  96.108  1.00 79.46 ? 223  LYS A O   1 
ATOM   1609  C  CB  . LYS A 1 223 ? -21.366 53.246  95.976  1.00 80.85 ? 223  LYS A CB  1 
ATOM   1610  C  CG  . LYS A 1 223 ? -22.659 52.430  96.045  1.00 84.46 ? 223  LYS A CG  1 
ATOM   1611  C  CD  . LYS A 1 223 ? -22.398 50.944  95.729  1.00 87.26 ? 223  LYS A CD  1 
ATOM   1612  C  CE  . LYS A 1 223 ? -23.664 50.097  95.853  1.00 87.37 ? 223  LYS A CE  1 
ATOM   1613  N  NZ  . LYS A 1 223 ? -24.779 50.550  94.966  1.00 88.01 ? 223  LYS A NZ  1 
ATOM   1614  N  N   . LYS A 1 224 ? -18.377 53.797  95.849  1.00 79.51 ? 224  LYS A N   1 
ATOM   1615  C  CA  . LYS A 1 224 ? -17.080 53.781  95.191  1.00 79.41 ? 224  LYS A CA  1 
ATOM   1616  C  C   . LYS A 1 224 ? -16.005 53.513  96.253  1.00 80.05 ? 224  LYS A C   1 
ATOM   1617  O  O   . LYS A 1 224 ? -15.894 54.234  97.255  1.00 78.84 ? 224  LYS A O   1 
ATOM   1618  C  CB  . LYS A 1 224 ? -16.812 55.116  94.485  1.00 79.69 ? 224  LYS A CB  1 
ATOM   1619  C  CG  . LYS A 1 224 ? -15.555 55.113  93.602  1.00 78.89 ? 224  LYS A CG  1 
ATOM   1620  C  CD  . LYS A 1 224 ? -15.194 56.514  93.102  1.00 78.37 ? 224  LYS A CD  1 
ATOM   1621  C  CE  . LYS A 1 224 ? -13.841 56.526  92.404  1.00 77.17 ? 224  LYS A CE  1 
ATOM   1622  N  NZ  . LYS A 1 224 ? -13.332 57.912  92.167  1.00 79.33 ? 224  LYS A NZ  1 
ATOM   1623  N  N   . GLU A 1 225 ? -15.230 52.457  96.026  1.00 79.29 ? 225  GLU A N   1 
ATOM   1624  C  CA  . GLU A 1 225 ? -14.167 52.053  96.933  1.00 77.91 ? 225  GLU A CA  1 
ATOM   1625  C  C   . GLU A 1 225 ? -13.030 53.074  97.020  1.00 76.27 ? 225  GLU A C   1 
ATOM   1626  O  O   . GLU A 1 225 ? -12.706 53.771  96.044  1.00 75.98 ? 225  GLU A O   1 
ATOM   1627  C  CB  . GLU A 1 225 ? -13.626 50.703  96.489  1.00 80.58 ? 225  GLU A CB  1 
ATOM   1628  C  CG  . GLU A 1 225 ? -12.476 50.193  97.302  1.00 85.37 ? 225  GLU A CG  1 
ATOM   1629  C  CD  . GLU A 1 225 ? -12.086 48.803  96.880  1.00 88.83 ? 225  GLU A CD  1 
ATOM   1630  O  OE1 . GLU A 1 225 ? -11.956 48.576  95.653  1.00 89.15 ? 225  GLU A OE1 1 
ATOM   1631  O  OE2 . GLU A 1 225 ? -11.912 47.943  97.772  1.00 90.73 ? 225  GLU A OE2 1 
ATOM   1632  N  N   . TRP A 1 226 ? -12.422 53.156  98.197  1.00 72.23 ? 226  TRP A N   1 
ATOM   1633  C  CA  . TRP A 1 226 ? -11.348 54.102  98.414  1.00 67.88 ? 226  TRP A CA  1 
ATOM   1634  C  C   . TRP A 1 226 ? -10.014 53.433  98.552  1.00 67.63 ? 226  TRP A C   1 
ATOM   1635  O  O   . TRP A 1 226 ? -9.789  52.656  99.485  1.00 67.82 ? 226  TRP A O   1 
ATOM   1636  C  CB  . TRP A 1 226 ? -11.609 54.928  99.667  1.00 63.74 ? 226  TRP A CB  1 
ATOM   1637  C  CG  . TRP A 1 226 ? -10.379 55.634  100.208 1.00 59.96 ? 226  TRP A CG  1 
ATOM   1638  C  CD1 . TRP A 1 226 ? -9.590  56.553  99.548  1.00 60.43 ? 226  TRP A CD1 1 
ATOM   1639  C  CD2 . TRP A 1 226 ? -9.859  55.555  101.547 1.00 54.65 ? 226  TRP A CD2 1 
ATOM   1640  N  NE1 . TRP A 1 226 ? -8.625  57.053  100.402 1.00 56.33 ? 226  TRP A NE1 1 
ATOM   1641  C  CE2 . TRP A 1 226 ? -8.772  56.465  101.632 1.00 52.69 ? 226  TRP A CE2 1 
ATOM   1642  C  CE3 . TRP A 1 226 ? -10.211 54.813  102.684 1.00 49.27 ? 226  TRP A CE3 1 
ATOM   1643  C  CZ2 . TRP A 1 226 ? -8.043  56.650  102.805 1.00 49.17 ? 226  TRP A CZ2 1 
ATOM   1644  C  CZ3 . TRP A 1 226 ? -9.482  55.000  103.853 1.00 46.59 ? 226  TRP A CZ3 1 
ATOM   1645  C  CH2 . TRP A 1 226 ? -8.411  55.915  103.903 1.00 45.30 ? 226  TRP A CH2 1 
ATOM   1646  N  N   . ASN A 1 227 ? -9.121  53.760  97.627  1.00 66.77 ? 227  ASN A N   1 
ATOM   1647  C  CA  . ASN A 1 227 ? -7.775  53.221  97.653  1.00 66.02 ? 227  ASN A CA  1 
ATOM   1648  C  C   . ASN A 1 227 ? -7.015  53.958  98.752  1.00 65.71 ? 227  ASN A C   1 
ATOM   1649  O  O   . ASN A 1 227 ? -6.575  55.095  98.574  1.00 67.09 ? 227  ASN A O   1 
ATOM   1650  C  CB  . ASN A 1 227 ? -7.091  53.444  96.312  1.00 65.30 ? 227  ASN A CB  1 
ATOM   1651  C  CG  . ASN A 1 227 ? -5.823  52.632  96.173  1.00 67.55 ? 227  ASN A CG  1 
ATOM   1652  O  OD1 . ASN A 1 227 ? -5.044  52.488  97.131  1.00 68.13 ? 227  ASN A OD1 1 
ATOM   1653  N  ND2 . ASN A 1 227 ? -5.600  52.092  94.975  1.00 66.62 ? 227  ASN A ND2 1 
ATOM   1654  N  N   . CYS A 1 228 ? -6.876  53.306  99.893  1.00 65.66 ? 228  CYS A N   1 
ATOM   1655  C  CA  . CYS A 1 228 ? -6.197  53.894  101.019 1.00 65.59 ? 228  CYS A CA  1 
ATOM   1656  C  C   . CYS A 1 228 ? -4.694  54.042  100.781 1.00 63.84 ? 228  CYS A C   1 
ATOM   1657  O  O   . CYS A 1 228 ? -4.123  55.108  101.006 1.00 63.64 ? 228  CYS A O   1 
ATOM   1658  C  CB  . CYS A 1 228 ? -6.486  53.048  102.252 1.00 70.38 ? 228  CYS A CB  1 
ATOM   1659  S  SG  . CYS A 1 228 ? -5.652  53.633  103.756 1.00 89.61 ? 228  CYS A SG  1 
ATOM   1660  N  N   . LYS A 1 229 ? -4.053  52.974  100.318 1.00 62.56 ? 229  LYS A N   1 
ATOM   1661  C  CA  . LYS A 1 229 ? -2.621  53.005  100.063 1.00 58.68 ? 229  LYS A CA  1 
ATOM   1662  C  C   . LYS A 1 229 ? -2.247  54.138  99.095  1.00 56.82 ? 229  LYS A C   1 
ATOM   1663  O  O   . LYS A 1 229 ? -1.257  54.858  99.287  1.00 51.44 ? 229  LYS A O   1 
ATOM   1664  C  CB  . LYS A 1 229 ? -2.169  51.666  99.496  1.00 61.06 ? 229  LYS A CB  1 
ATOM   1665  C  CG  . LYS A 1 229 ? -0.739  51.688  99.008  1.00 64.71 ? 229  LYS A CG  1 
ATOM   1666  C  CD  . LYS A 1 229 ? -0.396  50.469  98.164  1.00 71.42 ? 229  LYS A CD  1 
ATOM   1667  C  CE  . LYS A 1 229 ? 1.046   50.552  97.652  1.00 72.28 ? 229  LYS A CE  1 
ATOM   1668  N  NZ  . LYS A 1 229 ? 2.042   50.635  98.775  1.00 74.41 ? 229  LYS A NZ  1 
ATOM   1669  N  N   . LYS A 1 230 ? -3.043  54.299  98.049  1.00 54.22 ? 230  LYS A N   1 
ATOM   1670  C  CA  . LYS A 1 230 ? -2.779  55.351  97.086  1.00 54.07 ? 230  LYS A CA  1 
ATOM   1671  C  C   . LYS A 1 230 ? -2.680  56.707  97.783  1.00 52.45 ? 230  LYS A C   1 
ATOM   1672  O  O   . LYS A 1 230 ? -1.813  57.514  97.448  1.00 53.34 ? 230  LYS A O   1 
ATOM   1673  C  CB  . LYS A 1 230 ? -3.878  55.364  96.014  1.00 55.96 ? 230  LYS A CB  1 
ATOM   1674  C  CG  . LYS A 1 230 ? -3.821  56.533  95.042  1.00 64.11 ? 230  LYS A CG  1 
ATOM   1675  C  CD  . LYS A 1 230 ? -2.598  56.504  94.149  1.00 71.40 ? 230  LYS A CD  1 
ATOM   1676  C  CE  . LYS A 1 230 ? -2.620  57.688  93.172  1.00 76.13 ? 230  LYS A CE  1 
ATOM   1677  N  NZ  . LYS A 1 230 ? -1.402  57.785  92.302  1.00 75.24 ? 230  LYS A NZ  1 
ATOM   1678  N  N   . THR A 1 231 ? -3.555  56.944  98.762  1.00 48.67 ? 231  THR A N   1 
ATOM   1679  C  CA  . THR A 1 231 ? -3.566  58.208  99.488  1.00 47.06 ? 231  THR A CA  1 
ATOM   1680  C  C   . THR A 1 231 ? -2.387  58.344  100.448 1.00 46.39 ? 231  THR A C   1 
ATOM   1681  O  O   . THR A 1 231 ? -1.755  59.396  100.511 1.00 44.94 ? 231  THR A O   1 
ATOM   1682  C  CB  . THR A 1 231 ? -4.891  58.401  100.291 1.00 49.45 ? 231  THR A CB  1 
ATOM   1683  O  OG1 . THR A 1 231 ? -5.980  58.595  99.383  1.00 54.66 ? 231  THR A OG1 1 
ATOM   1684  C  CG2 . THR A 1 231 ? -4.815  59.621  101.196 1.00 46.84 ? 231  THR A CG2 1 
ATOM   1685  N  N   . THR A 1 232 ? -2.080  57.294  101.204 1.00 47.40 ? 232  THR A N   1 
ATOM   1686  C  CA  . THR A 1 232 ? -0.973  57.401  102.144 1.00 45.88 ? 232  THR A CA  1 
ATOM   1687  C  C   . THR A 1 232 ? 0.348   57.601  101.395 1.00 45.82 ? 232  THR A C   1 
ATOM   1688  O  O   . THR A 1 232 ? 1.193   58.401  101.820 1.00 41.02 ? 232  THR A O   1 
ATOM   1689  C  CB  . THR A 1 232 ? -0.963  56.195  103.140 1.00 46.84 ? 232  THR A CB  1 
ATOM   1690  O  OG1 . THR A 1 232 ? 0.370   55.936  103.580 1.00 48.07 ? 232  THR A OG1 1 
ATOM   1691  C  CG2 . THR A 1 232 ? -1.564  54.962  102.513 1.00 51.46 ? 232  THR A CG2 1 
ATOM   1692  N  N   . ASP A 1 233 ? 0.496   56.932  100.247 1.00 49.38 ? 233  ASP A N   1 
ATOM   1693  C  CA  . ASP A 1 233 ? 1.697   57.086  99.415  1.00 49.82 ? 233  ASP A CA  1 
ATOM   1694  C  C   . ASP A 1 233 ? 1.772   58.505  98.870  1.00 49.45 ? 233  ASP A C   1 
ATOM   1695  O  O   . ASP A 1 233 ? 2.853   59.112  98.830  1.00 55.24 ? 233  ASP A O   1 
ATOM   1696  C  CB  . ASP A 1 233 ? 1.708   56.097  98.252  1.00 50.74 ? 233  ASP A CB  1 
ATOM   1697  C  CG  . ASP A 1 233 ? 2.044   54.675  98.691  1.00 58.85 ? 233  ASP A CG  1 
ATOM   1698  O  OD1 . ASP A 1 233 ? 2.398   54.458  99.889  1.00 61.51 ? 233  ASP A OD1 1 
ATOM   1699  O  OD2 . ASP A 1 233 ? 1.957   53.766  97.830  1.00 60.45 ? 233  ASP A OD2 1 
ATOM   1700  N  N   . MET A 1 234 ? 0.642   59.047  98.445  1.00 45.02 ? 234  MET A N   1 
ATOM   1701  C  CA  . MET A 1 234 ? 0.659   60.411  97.956  1.00 44.47 ? 234  MET A CA  1 
ATOM   1702  C  C   . MET A 1 234 ? 1.101   61.353  99.091  1.00 43.90 ? 234  MET A C   1 
ATOM   1703  O  O   . MET A 1 234 ? 1.846   62.313  98.868  1.00 42.71 ? 234  MET A O   1 
ATOM   1704  C  CB  . MET A 1 234 ? -0.721  60.801  97.440  1.00 43.00 ? 234  MET A CB  1 
ATOM   1705  C  CG  . MET A 1 234 ? -0.808  62.223  96.936  1.00 48.90 ? 234  MET A CG  1 
ATOM   1706  S  SD  . MET A 1 234 ? -1.020  63.435  98.284  1.00 63.65 ? 234  MET A SD  1 
ATOM   1707  C  CE  . MET A 1 234 ? -2.636  62.985  98.923  1.00 56.69 ? 234  MET A CE  1 
ATOM   1708  N  N   . ILE A 1 235 ? 0.650   61.072  100.311 1.00 42.66 ? 235  ILE A N   1 
ATOM   1709  C  CA  . ILE A 1 235 ? 1.012   61.894  101.447 1.00 43.21 ? 235  ILE A CA  1 
ATOM   1710  C  C   . ILE A 1 235 ? 2.522   61.854  101.703 1.00 45.78 ? 235  ILE A C   1 
ATOM   1711  O  O   . ILE A 1 235 ? 3.161   62.915  101.855 1.00 44.03 ? 235  ILE A O   1 
ATOM   1712  C  CB  . ILE A 1 235 ? 0.233   61.451  102.704 1.00 44.22 ? 235  ILE A CB  1 
ATOM   1713  C  CG1 . ILE A 1 235 ? -1.202  61.961  102.609 1.00 45.54 ? 235  ILE A CG1 1 
ATOM   1714  C  CG2 . ILE A 1 235 ? 0.877   62.017  103.977 1.00 48.33 ? 235  ILE A CG2 1 
ATOM   1715  C  CD1 . ILE A 1 235 ? -1.309  63.499  102.579 1.00 39.86 ? 235  ILE A CD1 1 
ATOM   1716  N  N   . LEU A 1 236 ? 3.095   60.648  101.735 1.00 44.62 ? 236  LEU A N   1 
ATOM   1717  C  CA  . LEU A 1 236 ? 4.526   60.516  101.972 1.00 43.98 ? 236  LEU A CA  1 
ATOM   1718  C  C   . LEU A 1 236 ? 5.310   61.352  100.955 1.00 44.84 ? 236  LEU A C   1 
ATOM   1719  O  O   . LEU A 1 236 ? 6.217   62.108  101.309 1.00 46.25 ? 236  LEU A O   1 
ATOM   1720  C  CB  . LEU A 1 236 ? 4.930   59.042  101.908 1.00 45.55 ? 236  LEU A CB  1 
ATOM   1721  C  CG  . LEU A 1 236 ? 4.192   58.176  102.943 1.00 47.78 ? 236  LEU A CG  1 
ATOM   1722  C  CD1 . LEU A 1 236 ? 4.618   56.711  102.858 1.00 43.42 ? 236  LEU A CD1 1 
ATOM   1723  C  CD2 . LEU A 1 236 ? 4.473   58.726  104.332 1.00 47.42 ? 236  LEU A CD2 1 
ATOM   1724  N  N   . ASN A 1 237 ? 4.950   61.243  99.689  1.00 44.15 ? 237  ASN A N   1 
ATOM   1725  C  CA  . ASN A 1 237 ? 5.635   62.024  98.675  1.00 44.56 ? 237  ASN A CA  1 
ATOM   1726  C  C   . ASN A 1 237 ? 5.475   63.516  98.879  1.00 46.10 ? 237  ASN A C   1 
ATOM   1727  O  O   . ASN A 1 237 ? 6.395   64.304  98.612  1.00 48.57 ? 237  ASN A O   1 
ATOM   1728  C  CB  . ASN A 1 237 ? 5.121   61.667  97.291  1.00 42.38 ? 237  ASN A CB  1 
ATOM   1729  C  CG  . ASN A 1 237 ? 5.498   60.281  96.900  1.00 46.47 ? 237  ASN A CG  1 
ATOM   1730  O  OD1 . ASN A 1 237 ? 6.562   59.769  97.296  1.00 53.41 ? 237  ASN A OD1 1 
ATOM   1731  N  ND2 . ASN A 1 237 ? 4.652   59.651  96.117  1.00 45.86 ? 237  ASN A ND2 1 
ATOM   1732  N  N   . GLU A 1 238 ? 4.301   63.917  99.341  1.00 44.82 ? 238  GLU A N   1 
ATOM   1733  C  CA  . GLU A 1 238 ? 4.080   65.324  99.548  1.00 45.86 ? 238  GLU A CA  1 
ATOM   1734  C  C   . GLU A 1 238 ? 5.008   65.818  100.658 1.00 43.83 ? 238  GLU A C   1 
ATOM   1735  O  O   . GLU A 1 238 ? 5.532   66.940  100.575 1.00 40.11 ? 238  GLU A O   1 
ATOM   1736  C  CB  . GLU A 1 238 ? 2.608   65.569  99.883  1.00 50.43 ? 238  GLU A CB  1 
ATOM   1737  C  CG  . GLU A 1 238 ? 1.979   66.662  99.039  1.00 52.97 ? 238  GLU A CG  1 
ATOM   1738  C  CD  . GLU A 1 238 ? 2.403   66.576  97.596  1.00 55.47 ? 238  GLU A CD  1 
ATOM   1739  O  OE1 . GLU A 1 238 ? 2.388   65.467  97.051  1.00 58.73 ? 238  GLU A OE1 1 
ATOM   1740  O  OE2 . GLU A 1 238 ? 2.755   67.607  96.997  1.00 61.02 ? 238  GLU A OE2 1 
ATOM   1741  N  N   . ILE A 1 239 ? 5.216   64.983  101.683 1.00 41.00 ? 239  ILE A N   1 
ATOM   1742  C  CA  . ILE A 1 239 ? 6.108   65.359  102.775 1.00 39.60 ? 239  ILE A CA  1 
ATOM   1743  C  C   . ILE A 1 239 ? 7.482   65.577  102.152 1.00 39.45 ? 239  ILE A C   1 
ATOM   1744  O  O   . ILE A 1 239 ? 8.117   66.615  102.412 1.00 33.88 ? 239  ILE A O   1 
ATOM   1745  C  CB  . ILE A 1 239 ? 6.208   64.248  103.886 1.00 41.70 ? 239  ILE A CB  1 
ATOM   1746  C  CG1 . ILE A 1 239 ? 4.840   64.054  104.554 1.00 40.79 ? 239  ILE A CG1 1 
ATOM   1747  C  CG2 . ILE A 1 239 ? 7.261   64.648  104.957 1.00 33.47 ? 239  ILE A CG2 1 
ATOM   1748  C  CD1 . ILE A 1 239 ? 4.720   62.735  105.293 1.00 40.44 ? 239  ILE A CD1 1 
ATOM   1749  N  N   . LYS A 1 240 ? 7.907   64.614  101.311 1.00 35.68 ? 240  LYS A N   1 
ATOM   1750  C  CA  . LYS A 1 240 ? 9.214   64.673  100.640 1.00 38.36 ? 240  LYS A CA  1 
ATOM   1751  C  C   . LYS A 1 240 ? 9.379   65.890  99.698  1.00 38.46 ? 240  LYS A C   1 
ATOM   1752  O  O   . LYS A 1 240 ? 10.475  66.182  99.200  1.00 38.20 ? 240  LYS A O   1 
ATOM   1753  C  CB  . LYS A 1 240 ? 9.496   63.367  99.873  1.00 34.03 ? 240  LYS A CB  1 
ATOM   1754  C  CG  . LYS A 1 240 ? 9.458   62.097  100.735 1.00 33.25 ? 240  LYS A CG  1 
ATOM   1755  C  CD  . LYS A 1 240 ? 9.898   60.863  99.972  1.00 32.27 ? 240  LYS A CD  1 
ATOM   1756  C  CE  . LYS A 1 240 ? 11.420  60.597  100.124 1.00 48.54 ? 240  LYS A CE  1 
ATOM   1757  N  NZ  . LYS A 1 240 ? 12.379  61.721  99.794  1.00 45.69 ? 240  LYS A NZ  1 
ATOM   1758  N  N   . GLN A 1 241 ? 8.288   66.602  99.462  1.00 36.00 ? 241  GLN A N   1 
ATOM   1759  C  CA  . GLN A 1 241 ? 8.351   67.783  98.615  1.00 36.56 ? 241  GLN A CA  1 
ATOM   1760  C  C   . GLN A 1 241 ? 8.238   69.028  99.455  1.00 38.53 ? 241  GLN A C   1 
ATOM   1761  O  O   . GLN A 1 241 ? 8.014   70.112  98.912  1.00 43.03 ? 241  GLN A O   1 
ATOM   1762  C  CB  . GLN A 1 241 ? 7.224   67.811  97.587  1.00 34.60 ? 241  GLN A CB  1 
ATOM   1763  C  CG  . GLN A 1 241 ? 7.272   66.685  96.574  1.00 35.42 ? 241  GLN A CG  1 
ATOM   1764  C  CD  . GLN A 1 241 ? 8.473   66.789  95.683  1.00 37.91 ? 241  GLN A CD  1 
ATOM   1765  O  OE1 . GLN A 1 241 ? 8.726   67.845  95.103  1.00 40.28 ? 241  GLN A OE1 1 
ATOM   1766  N  NE2 . GLN A 1 241 ? 9.232   65.695  95.563  1.00 40.37 ? 241  GLN A NE2 1 
ATOM   1767  N  N   . GLY A 1 242 ? 8.361   68.880  100.773 1.00 36.51 ? 242  GLY A N   1 
ATOM   1768  C  CA  . GLY A 1 242 ? 8.294   70.036  101.651 1.00 33.63 ? 242  GLY A CA  1 
ATOM   1769  C  C   . GLY A 1 242 ? 6.932   70.661  101.908 1.00 34.79 ? 242  GLY A C   1 
ATOM   1770  O  O   . GLY A 1 242 ? 6.844   71.798  102.412 1.00 33.73 ? 242  GLY A O   1 
ATOM   1771  N  N   . LYS A 1 243 ? 5.868   69.924  101.607 1.00 36.94 ? 243  LYS A N   1 
ATOM   1772  C  CA  . LYS A 1 243 ? 4.510   70.445  101.796 1.00 39.18 ? 243  LYS A CA  1 
ATOM   1773  C  C   . LYS A 1 243 ? 4.035   70.511  103.239 1.00 40.11 ? 243  LYS A C   1 
ATOM   1774  O  O   . LYS A 1 243 ? 3.143   71.305  103.565 1.00 37.17 ? 243  LYS A O   1 
ATOM   1775  C  CB  . LYS A 1 243 ? 3.514   69.613  100.993 1.00 41.22 ? 243  LYS A CB  1 
ATOM   1776  C  CG  . LYS A 1 243 ? 3.730   69.691  99.498  1.00 45.57 ? 243  LYS A CG  1 
ATOM   1777  C  CD  . LYS A 1 243 ? 3.440   71.085  98.965  1.00 45.87 ? 243  LYS A CD  1 
ATOM   1778  C  CE  . LYS A 1 243 ? 3.768   71.182  97.483  1.00 52.01 ? 243  LYS A CE  1 
ATOM   1779  N  NZ  . LYS A 1 243 ? 3.019   70.244  96.559  1.00 50.37 ? 243  LYS A NZ  1 
ATOM   1780  N  N   . PHE A 1 244 ? 4.631   69.696  104.111 1.00 40.81 ? 244  PHE A N   1 
ATOM   1781  C  CA  . PHE A 1 244 ? 4.202   69.681  105.499 1.00 41.22 ? 244  PHE A CA  1 
ATOM   1782  C  C   . PHE A 1 244 ? 5.162   70.289  106.505 1.00 42.41 ? 244  PHE A C   1 
ATOM   1783  O  O   . PHE A 1 244 ? 5.508   69.667  107.511 1.00 46.04 ? 244  PHE A O   1 
ATOM   1784  C  CB  . PHE A 1 244 ? 3.834   68.249  105.884 1.00 39.37 ? 244  PHE A CB  1 
ATOM   1785  C  CG  . PHE A 1 244 ? 2.615   67.734  105.170 1.00 39.88 ? 244  PHE A CG  1 
ATOM   1786  C  CD1 . PHE A 1 244 ? 1.348   68.209  105.504 1.00 38.50 ? 244  PHE A CD1 1 
ATOM   1787  C  CD2 . PHE A 1 244 ? 2.732   66.808  104.141 1.00 41.12 ? 244  PHE A CD2 1 
ATOM   1788  C  CE1 . PHE A 1 244 ? 0.219   67.779  104.832 1.00 38.54 ? 244  PHE A CE1 1 
ATOM   1789  C  CE2 . PHE A 1 244 ? 1.602   66.364  103.456 1.00 41.67 ? 244  PHE A CE2 1 
ATOM   1790  C  CZ  . PHE A 1 244 ? 0.336   66.854  103.807 1.00 39.84 ? 244  PHE A CZ  1 
ATOM   1791  N  N   . HIS A 1 245 ? 5.588   71.516  106.254 1.00 38.59 ? 245  HIS A N   1 
ATOM   1792  C  CA  . HIS A 1 245 ? 6.480   72.149  107.195 1.00 40.01 ? 245  HIS A CA  1 
ATOM   1793  C  C   . HIS A 1 245 ? 5.693   72.853  108.333 1.00 42.02 ? 245  HIS A C   1 
ATOM   1794  O  O   . HIS A 1 245 ? 6.213   73.080  109.434 1.00 43.19 ? 245  HIS A O   1 
ATOM   1795  C  CB  . HIS A 1 245 ? 7.436   73.104  106.454 1.00 41.17 ? 245  HIS A CB  1 
ATOM   1796  C  CG  . HIS A 1 245 ? 6.750   74.159  105.641 1.00 43.46 ? 245  HIS A CG  1 
ATOM   1797  N  ND1 . HIS A 1 245 ? 6.448   75.407  106.148 1.00 43.62 ? 245  HIS A ND1 1 
ATOM   1798  C  CD2 . HIS A 1 245 ? 6.240   74.128  104.385 1.00 42.13 ? 245  HIS A CD2 1 
ATOM   1799  C  CE1 . HIS A 1 245 ? 5.776   76.095  105.243 1.00 41.33 ? 245  HIS A CE1 1 
ATOM   1800  N  NE2 . HIS A 1 245 ? 5.636   75.342  104.165 1.00 41.87 ? 245  HIS A NE2 1 
ATOM   1801  N  N   . ASN A 1 246 ? 4.433   73.181  108.090 1.00 39.22 ? 246  ASN A N   1 
ATOM   1802  C  CA  . ASN A 1 246 ? 3.651   73.817  109.131 1.00 40.07 ? 246  ASN A CA  1 
ATOM   1803  C  C   . ASN A 1 246 ? 3.345   72.794  110.243 1.00 40.13 ? 246  ASN A C   1 
ATOM   1804  O  O   . ASN A 1 246 ? 2.804   71.718  109.986 1.00 38.41 ? 246  ASN A O   1 
ATOM   1805  C  CB  . ASN A 1 246 ? 2.351   74.362  108.543 1.00 44.17 ? 246  ASN A CB  1 
ATOM   1806  C  CG  . ASN A 1 246 ? 1.660   75.335  109.483 1.00 47.35 ? 246  ASN A CG  1 
ATOM   1807  O  OD1 . ASN A 1 246 ? 1.377   75.009  110.647 1.00 49.87 ? 246  ASN A OD1 1 
ATOM   1808  N  ND2 . ASN A 1 246 ? 1.391   76.539  108.988 1.00 45.39 ? 246  ASN A ND2 1 
ATOM   1809  N  N   . PRO A 1 247 ? 3.699   73.113  111.499 1.00 41.41 ? 247  PRO A N   1 
ATOM   1810  C  CA  . PRO A 1 247 ? 3.418   72.150  112.567 1.00 37.78 ? 247  PRO A CA  1 
ATOM   1811  C  C   . PRO A 1 247 ? 1.957   71.759  112.640 1.00 35.74 ? 247  PRO A C   1 
ATOM   1812  O  O   . PRO A 1 247 ? 1.640   70.597  112.836 1.00 35.04 ? 247  PRO A O   1 
ATOM   1813  C  CB  . PRO A 1 247 ? 3.940   72.846  113.824 1.00 40.11 ? 247  PRO A CB  1 
ATOM   1814  C  CG  . PRO A 1 247 ? 3.990   74.301  113.451 1.00 46.42 ? 247  PRO A CG  1 
ATOM   1815  C  CD  . PRO A 1 247 ? 4.446   74.268  112.017 1.00 41.93 ? 247  PRO A CD  1 
ATOM   1816  N  N   . MET A 1 248 ? 1.062   72.717  112.459 1.00 37.48 ? 248  MET A N   1 
ATOM   1817  C  CA  . MET A 1 248 ? -0.370  72.400  112.482 1.00 36.92 ? 248  MET A CA  1 
ATOM   1818  C  C   . MET A 1 248 ? -0.689  71.429  111.335 1.00 35.82 ? 248  MET A C   1 
ATOM   1819  O  O   . MET A 1 248 ? -1.571  70.583  111.472 1.00 34.89 ? 248  MET A O   1 
ATOM   1820  C  CB  . MET A 1 248 ? -1.241  73.659  112.300 1.00 37.64 ? 248  MET A CB  1 
ATOM   1821  C  CG  . MET A 1 248 ? -2.745  73.351  112.239 1.00 36.01 ? 248  MET A CG  1 
ATOM   1822  S  SD  . MET A 1 248 ? -3.298  72.565  113.775 1.00 37.24 ? 248  MET A SD  1 
ATOM   1823  C  CE  . MET A 1 248 ? -5.047  72.760  113.751 1.00 39.52 ? 248  MET A CE  1 
ATOM   1824  N  N   . SER A 1 249 ? 0.001   71.557  110.202 1.00 31.02 ? 249  SER A N   1 
ATOM   1825  C  CA  . SER A 1 249 ? -0.286  70.632  109.112 1.00 33.30 ? 249  SER A CA  1 
ATOM   1826  C  C   . SER A 1 249 ? 0.240   69.243  109.486 1.00 31.41 ? 249  SER A C   1 
ATOM   1827  O  O   . SER A 1 249 ? -0.329  68.223  109.117 1.00 31.32 ? 249  SER A O   1 
ATOM   1828  C  CB  . SER A 1 249 ? 0.313   71.135  107.787 1.00 31.84 ? 249  SER A CB  1 
ATOM   1829  O  OG  . SER A 1 249 ? 1.706   70.930  107.697 1.00 42.47 ? 249  SER A OG  1 
ATOM   1830  N  N   . ILE A 1 250 ? 1.310   69.195  110.263 1.00 32.21 ? 250  ILE A N   1 
ATOM   1831  C  CA  . ILE A 1 250 ? 1.832   67.898  110.674 1.00 33.34 ? 250  ILE A CA  1 
ATOM   1832  C  C   . ILE A 1 250 ? 0.850   67.241  111.655 1.00 33.89 ? 250  ILE A C   1 
ATOM   1833  O  O   . ILE A 1 250 ? 0.599   66.024  111.598 1.00 33.23 ? 250  ILE A O   1 
ATOM   1834  C  CB  . ILE A 1 250 ? 3.234   68.047  111.328 1.00 29.94 ? 250  ILE A CB  1 
ATOM   1835  C  CG1 . ILE A 1 250 ? 4.202   68.636  110.297 1.00 31.87 ? 250  ILE A CG1 1 
ATOM   1836  C  CG2 . ILE A 1 250 ? 3.732   66.691  111.811 1.00 26.84 ? 250  ILE A CG2 1 
ATOM   1837  C  CD1 . ILE A 1 250 ? 5.530   69.111  110.845 1.00 32.45 ? 250  ILE A CD1 1 
ATOM   1838  N  N   . ALA A 1 251 ? 0.285   68.076  112.523 1.00 30.76 ? 251  ALA A N   1 
ATOM   1839  C  CA  . ALA A 1 251 ? -0.648  67.646  113.535 1.00 31.10 ? 251  ALA A CA  1 
ATOM   1840  C  C   . ALA A 1 251 ? -1.868  66.981  112.905 1.00 34.08 ? 251  ALA A C   1 
ATOM   1841  O  O   . ALA A 1 251 ? -2.443  66.054  113.486 1.00 33.25 ? 251  ALA A O   1 
ATOM   1842  C  CB  . ALA A 1 251 ? -1.076  68.849  114.394 1.00 28.57 ? 251  ALA A CB  1 
ATOM   1843  N  N   . GLN A 1 252 ? -2.267  67.429  111.716 1.00 34.94 ? 252  GLN A N   1 
ATOM   1844  C  CA  . GLN A 1 252 ? -3.449  66.824  111.107 1.00 35.76 ? 252  GLN A CA  1 
ATOM   1845  C  C   . GLN A 1 252 ? -3.206  65.577  110.250 1.00 34.26 ? 252  GLN A C   1 
ATOM   1846  O  O   . GLN A 1 252 ? -4.159  64.931  109.842 1.00 35.39 ? 252  GLN A O   1 
ATOM   1847  C  CB  . GLN A 1 252 ? -4.287  67.882  110.360 1.00 32.56 ? 252  GLN A CB  1 
ATOM   1848  C  CG  . GLN A 1 252 ? -4.821  68.924  111.333 1.00 34.22 ? 252  GLN A CG  1 
ATOM   1849  C  CD  . GLN A 1 252 ? -5.873  69.882  110.744 1.00 36.48 ? 252  GLN A CD  1 
ATOM   1850  O  OE1 . GLN A 1 252 ? -5.843  70.213  109.558 1.00 40.96 ? 252  GLN A OE1 1 
ATOM   1851  N  NE2 . GLN A 1 252 ? -6.789  70.352  111.595 1.00 31.89 ? 252  GLN A NE2 1 
ATOM   1852  N  N   . ILE A 1 253 ? -1.954  65.217  109.986 1.00 33.16 ? 253  ILE A N   1 
ATOM   1853  C  CA  . ILE A 1 253 ? -1.700  63.976  109.234 1.00 34.22 ? 253  ILE A CA  1 
ATOM   1854  C  C   . ILE A 1 253 ? -0.994  62.916  110.089 1.00 35.10 ? 253  ILE A C   1 
ATOM   1855  O  O   . ILE A 1 253 ? -1.107  61.718  109.812 1.00 32.15 ? 253  ILE A O   1 
ATOM   1856  C  CB  . ILE A 1 253 ? -0.807  64.193  108.001 1.00 33.23 ? 253  ILE A CB  1 
ATOM   1857  C  CG1 . ILE A 1 253 ? 0.383   65.079  108.386 1.00 36.24 ? 253  ILE A CG1 1 
ATOM   1858  C  CG2 . ILE A 1 253 ? -1.611  64.751  106.885 1.00 31.98 ? 253  ILE A CG2 1 
ATOM   1859  C  CD1 . ILE A 1 253 ? 1.467   65.110  107.371 1.00 37.76 ? 253  ILE A CD1 1 
ATOM   1860  N  N   . LEU A 1 254 ? -0.260  63.368  111.117 1.00 36.59 ? 254  LEU A N   1 
ATOM   1861  C  CA  . LEU A 1 254 ? 0.498   62.468  111.990 1.00 34.41 ? 254  LEU A CA  1 
ATOM   1862  C  C   . LEU A 1 254 ? -0.370  61.329  112.516 1.00 34.47 ? 254  LEU A C   1 
ATOM   1863  O  O   . LEU A 1 254 ? 0.024   60.160  112.453 1.00 35.87 ? 254  LEU A O   1 
ATOM   1864  C  CB  . LEU A 1 254 ? 1.098   63.233  113.174 1.00 35.05 ? 254  LEU A CB  1 
ATOM   1865  C  CG  . LEU A 1 254 ? 2.552   62.922  113.579 1.00 33.71 ? 254  LEU A CG  1 
ATOM   1866  C  CD1 . LEU A 1 254 ? 2.668   63.049  115.081 1.00 30.67 ? 254  LEU A CD1 1 
ATOM   1867  C  CD2 . LEU A 1 254 ? 2.973   61.541  113.158 1.00 31.33 ? 254  LEU A CD2 1 
ATOM   1868  N  N   . PRO A 1 255 ? -1.565  61.656  113.047 1.00 32.10 ? 255  PRO A N   1 
ATOM   1869  C  CA  . PRO A 1 255 ? -2.430  60.594  113.564 1.00 32.45 ? 255  PRO A CA  1 
ATOM   1870  C  C   . PRO A 1 255 ? -2.639  59.487  112.539 1.00 34.16 ? 255  PRO A C   1 
ATOM   1871  O  O   . PRO A 1 255 ? -2.487  58.288  112.836 1.00 33.54 ? 255  PRO A O   1 
ATOM   1872  C  CB  . PRO A 1 255 ? -3.723  61.334  113.905 1.00 29.68 ? 255  PRO A CB  1 
ATOM   1873  C  CG  . PRO A 1 255 ? -3.202  62.645  114.367 1.00 28.76 ? 255  PRO A CG  1 
ATOM   1874  C  CD  . PRO A 1 255 ? -2.163  62.979  113.292 1.00 27.00 ? 255  PRO A CD  1 
ATOM   1875  N  N   . SER A 1 256 ? -2.965  59.889  111.318 1.00 34.70 ? 256  SER A N   1 
ATOM   1876  C  CA  . SER A 1 256 ? -3.210  58.908  110.267 1.00 35.69 ? 256  SER A CA  1 
ATOM   1877  C  C   . SER A 1 256 ? -1.981  58.093  109.934 1.00 34.89 ? 256  SER A C   1 
ATOM   1878  O  O   . SER A 1 256 ? -2.067  56.878  109.738 1.00 33.33 ? 256  SER A O   1 
ATOM   1879  C  CB  . SER A 1 256 ? -3.755  59.598  109.026 1.00 35.02 ? 256  SER A CB  1 
ATOM   1880  O  OG  . SER A 1 256 ? -5.121  59.913  109.243 1.00 41.38 ? 256  SER A OG  1 
ATOM   1881  N  N   . LEU A 1 257 ? -0.833  58.765  109.897 1.00 34.46 ? 257  LEU A N   1 
ATOM   1882  C  CA  . LEU A 1 257 ? 0.418   58.103  109.598 1.00 35.12 ? 257  LEU A CA  1 
ATOM   1883  C  C   . LEU A 1 257 ? 0.809   57.111  110.685 1.00 37.30 ? 257  LEU A C   1 
ATOM   1884  O  O   . LEU A 1 257 ? 1.595   56.206  110.443 1.00 38.35 ? 257  LEU A O   1 
ATOM   1885  C  CB  . LEU A 1 257 ? 1.516   59.142  109.390 1.00 35.08 ? 257  LEU A CB  1 
ATOM   1886  C  CG  . LEU A 1 257 ? 1.198   60.013  108.162 1.00 41.01 ? 257  LEU A CG  1 
ATOM   1887  C  CD1 . LEU A 1 257 ? 2.265   61.077  107.966 1.00 39.56 ? 257  LEU A CD1 1 
ATOM   1888  C  CD2 . LEU A 1 257 ? 1.098   59.146  106.919 1.00 38.44 ? 257  LEU A CD2 1 
ATOM   1889  N  N   . LYS A 1 258 ? 0.258   57.268  111.881 1.00 36.87 ? 258  LYS A N   1 
ATOM   1890  C  CA  . LYS A 1 258 ? 0.579   56.362  112.966 1.00 37.59 ? 258  LYS A CA  1 
ATOM   1891  C  C   . LYS A 1 258 ? -0.559  55.349  113.167 1.00 39.62 ? 258  LYS A C   1 
ATOM   1892  O  O   . LYS A 1 258 ? -0.568  54.582  114.126 1.00 40.26 ? 258  LYS A O   1 
ATOM   1893  C  CB  . LYS A 1 258 ? 0.838   57.165  114.254 1.00 36.70 ? 258  LYS A CB  1 
ATOM   1894  C  CG  . LYS A 1 258 ? 2.226   57.850  114.306 1.00 37.46 ? 258  LYS A CG  1 
ATOM   1895  C  CD  . LYS A 1 258 ? 3.333   56.821  114.348 1.00 38.16 ? 258  LYS A CD  1 
ATOM   1896  C  CE  . LYS A 1 258 ? 4.582   57.286  115.053 1.00 45.99 ? 258  LYS A CE  1 
ATOM   1897  N  NZ  . LYS A 1 258 ? 5.510   58.183  114.247 1.00 51.02 ? 258  LYS A NZ  1 
ATOM   1898  N  N   . GLY A 1 259 ? -1.515  55.353  112.247 1.00 40.34 ? 259  GLY A N   1 
ATOM   1899  C  CA  . GLY A 1 259 ? -2.642  54.445  112.344 1.00 39.94 ? 259  GLY A CA  1 
ATOM   1900  C  C   . GLY A 1 259 ? -3.622  54.741  113.460 1.00 40.63 ? 259  GLY A C   1 
ATOM   1901  O  O   . GLY A 1 259 ? -4.253  53.814  113.976 1.00 44.90 ? 259  GLY A O   1 
ATOM   1902  N  N   . LYS A 1 260 ? -3.777  56.013  113.826 1.00 38.93 ? 260  LYS A N   1 
ATOM   1903  C  CA  . LYS A 1 260 ? -4.689  56.400  114.916 1.00 37.03 ? 260  LYS A CA  1 
ATOM   1904  C  C   . LYS A 1 260 ? -5.656  57.488  114.442 1.00 34.24 ? 260  LYS A C   1 
ATOM   1905  O  O   . LYS A 1 260 ? -5.504  58.039  113.345 1.00 35.40 ? 260  LYS A O   1 
ATOM   1906  C  CB  . LYS A 1 260 ? -3.870  56.971  116.082 1.00 39.02 ? 260  LYS A CB  1 
ATOM   1907  C  CG  . LYS A 1 260 ? -2.755  56.080  116.597 1.00 44.10 ? 260  LYS A CG  1 
ATOM   1908  C  CD  . LYS A 1 260 ? -3.295  55.035  117.550 1.00 47.63 ? 260  LYS A CD  1 
ATOM   1909  C  CE  . LYS A 1 260 ? -2.191  54.347  118.321 1.00 50.17 ? 260  LYS A CE  1 
ATOM   1910  N  NZ  . LYS A 1 260 ? -2.750  53.318  119.269 1.00 54.63 ? 260  LYS A NZ  1 
ATOM   1911  N  N   . THR A 1 261 ? -6.647  57.808  115.258 1.00 28.37 ? 261  THR A N   1 
ATOM   1912  C  CA  . THR A 1 261 ? -7.558  58.893  114.912 1.00 29.85 ? 261  THR A CA  1 
ATOM   1913  C  C   . THR A 1 261 ? -7.928  59.529  116.215 1.00 30.97 ? 261  THR A C   1 
ATOM   1914  O  O   . THR A 1 261 ? -7.560  59.015  117.286 1.00 31.75 ? 261  THR A O   1 
ATOM   1915  C  CB  . THR A 1 261 ? -8.880  58.433  114.232 1.00 30.89 ? 261  THR A CB  1 
ATOM   1916  O  OG1 . THR A 1 261 ? -9.765  57.878  115.216 1.00 30.95 ? 261  THR A OG1 1 
ATOM   1917  C  CG2 . THR A 1 261 ? -8.603  57.427  113.101 1.00 25.60 ? 261  THR A CG2 1 
ATOM   1918  N  N   . TYR A 1 262 ? -8.661  60.634  116.148 1.00 28.79 ? 262  TYR A N   1 
ATOM   1919  C  CA  . TYR A 1 262 ? -9.078  61.293  117.383 1.00 30.65 ? 262  TYR A CA  1 
ATOM   1920  C  C   . TYR A 1 262 ? -9.966  60.390  118.266 1.00 31.29 ? 262  TYR A C   1 
ATOM   1921  O  O   . TYR A 1 262 ? -10.194 60.679  119.439 1.00 32.41 ? 262  TYR A O   1 
ATOM   1922  C  CB  . TYR A 1 262 ? -9.822  62.584  117.068 1.00 29.90 ? 262  TYR A CB  1 
ATOM   1923  C  CG  . TYR A 1 262 ? -8.948  63.666  116.473 1.00 32.00 ? 262  TYR A CG  1 
ATOM   1924  C  CD1 . TYR A 1 262 ? -7.556  63.572  116.508 1.00 27.22 ? 262  TYR A CD1 1 
ATOM   1925  C  CD2 . TYR A 1 262 ? -9.517  64.816  115.953 1.00 33.41 ? 262  TYR A CD2 1 
ATOM   1926  C  CE1 . TYR A 1 262 ? -6.752  64.608  116.048 1.00 33.46 ? 262  TYR A CE1 1 
ATOM   1927  C  CE2 . TYR A 1 262 ? -8.733  65.861  115.491 1.00 36.87 ? 262  TYR A CE2 1 
ATOM   1928  C  CZ  . TYR A 1 262 ? -7.356  65.764  115.543 1.00 37.36 ? 262  TYR A CZ  1 
ATOM   1929  O  OH  . TYR A 1 262 ? -6.611  66.856  115.126 1.00 31.02 ? 262  TYR A OH  1 
ATOM   1930  N  N   . LEU A 1 263 ? -10.467 59.298  117.708 1.00 32.84 ? 263  LEU A N   1 
ATOM   1931  C  CA  . LEU A 1 263 ? -11.315 58.414  118.487 1.00 33.07 ? 263  LEU A CA  1 
ATOM   1932  C  C   . LEU A 1 263 ? -10.467 57.576  119.415 1.00 33.46 ? 263  LEU A C   1 
ATOM   1933  O  O   . LEU A 1 263 ? -10.990 56.953  120.340 1.00 34.85 ? 263  LEU A O   1 
ATOM   1934  C  CB  . LEU A 1 263 ? -12.144 57.500  117.590 1.00 28.74 ? 263  LEU A CB  1 
ATOM   1935  C  CG  . LEU A 1 263 ? -13.145 58.176  116.650 1.00 31.95 ? 263  LEU A CG  1 
ATOM   1936  C  CD1 . LEU A 1 263 ? -14.077 57.107  116.064 1.00 25.78 ? 263  LEU A CD1 1 
ATOM   1937  C  CD2 . LEU A 1 263 ? -13.954 59.221  117.389 1.00 27.03 ? 263  LEU A CD2 1 
ATOM   1938  N  N   . ASP A 1 264 ? -9.158  57.566  119.180 1.00 32.22 ? 264  ASP A N   1 
ATOM   1939  C  CA  . ASP A 1 264 ? -8.267  56.779  120.025 1.00 32.25 ? 264  ASP A CA  1 
ATOM   1940  C  C   . ASP A 1 264 ? -7.813  57.530  121.283 1.00 32.81 ? 264  ASP A C   1 
ATOM   1941  O  O   . ASP A 1 264 ? -7.280  56.930  122.206 1.00 32.06 ? 264  ASP A O   1 
ATOM   1942  C  CB  . ASP A 1 264 ? -7.064  56.311  119.197 1.00 30.36 ? 264  ASP A CB  1 
ATOM   1943  C  CG  . ASP A 1 264 ? -7.490  55.444  118.016 1.00 36.44 ? 264  ASP A CG  1 
ATOM   1944  O  OD1 . ASP A 1 264 ? -8.347  54.558  118.229 1.00 34.83 ? 264  ASP A OD1 1 
ATOM   1945  O  OD2 . ASP A 1 264 ? -6.985  55.635  116.879 1.00 45.57 ? 264  ASP A OD2 1 
ATOM   1946  N  N   . VAL A 1 265 ? -8.070  58.839  121.306 1.00 34.03 ? 265  VAL A N   1 
ATOM   1947  C  CA  . VAL A 1 265 ? -7.681  59.721  122.398 1.00 35.59 ? 265  VAL A CA  1 
ATOM   1948  C  C   . VAL A 1 265 ? -8.002  59.167  123.786 1.00 37.06 ? 265  VAL A C   1 
ATOM   1949  O  O   . VAL A 1 265 ? -7.161  59.191  124.693 1.00 38.56 ? 265  VAL A O   1 
ATOM   1950  C  CB  . VAL A 1 265 ? -8.351  61.137  122.241 1.00 33.49 ? 265  VAL A CB  1 
ATOM   1951  C  CG1 . VAL A 1 265 ? -8.261  61.915  123.517 1.00 33.10 ? 265  VAL A CG1 1 
ATOM   1952  C  CG2 . VAL A 1 265 ? -7.652  61.928  121.164 1.00 32.23 ? 265  VAL A CG2 1 
ATOM   1953  N  N   . PRO A 1 266 ? -9.224  58.670  123.974 1.00 36.22 ? 266  PRO A N   1 
ATOM   1954  C  CA  . PRO A 1 266 ? -9.562  58.142  125.300 1.00 35.77 ? 266  PRO A CA  1 
ATOM   1955  C  C   . PRO A 1 266 ? -8.727  56.963  125.732 1.00 34.15 ? 266  PRO A C   1 
ATOM   1956  O  O   . PRO A 1 266 ? -8.634  56.669  126.913 1.00 35.92 ? 266  PRO A O   1 
ATOM   1957  C  CB  . PRO A 1 266 ? -11.039 57.773  125.156 1.00 32.01 ? 266  PRO A CB  1 
ATOM   1958  C  CG  . PRO A 1 266 ? -11.517 58.805  124.189 1.00 32.15 ? 266  PRO A CG  1 
ATOM   1959  C  CD  . PRO A 1 266 ? -10.430 58.809  123.141 1.00 32.34 ? 266  PRO A CD  1 
ATOM   1960  N  N   . GLN A 1 267 ? -8.118  56.292  124.768 1.00 36.56 ? 267  GLN A N   1 
ATOM   1961  C  CA  . GLN A 1 267 ? -7.324  55.103  125.058 1.00 37.65 ? 267  GLN A CA  1 
ATOM   1962  C  C   . GLN A 1 267 ? -5.835  55.364  125.151 1.00 37.01 ? 267  GLN A C   1 
ATOM   1963  O  O   . GLN A 1 267 ? -5.046  54.432  125.231 1.00 36.92 ? 267  GLN A O   1 
ATOM   1964  C  CB  . GLN A 1 267 ? -7.576  54.019  123.998 1.00 42.25 ? 267  GLN A CB  1 
ATOM   1965  C  CG  . GLN A 1 267 ? -8.950  53.321  124.054 1.00 47.90 ? 267  GLN A CG  1 
ATOM   1966  C  CD  . GLN A 1 267 ? -10.074 54.209  123.532 1.00 58.68 ? 267  GLN A CD  1 
ATOM   1967  O  OE1 . GLN A 1 267 ? -10.170 54.504  122.328 1.00 56.05 ? 267  GLN A OE1 1 
ATOM   1968  N  NE2 . GLN A 1 267 ? -10.931 54.657  124.449 1.00 63.08 ? 267  GLN A NE2 1 
ATOM   1969  N  N   . VAL A 1 268 ? -5.439  56.626  125.149 1.00 37.75 ? 268  VAL A N   1 
ATOM   1970  C  CA  . VAL A 1 268 ? -4.019  56.923  125.223 1.00 42.26 ? 268  VAL A CA  1 
ATOM   1971  C  C   . VAL A 1 268 ? -3.376  56.506  126.537 1.00 42.44 ? 268  VAL A C   1 
ATOM   1972  O  O   . VAL A 1 268 ? -3.910  56.790  127.611 1.00 45.09 ? 268  VAL A O   1 
ATOM   1973  C  CB  . VAL A 1 268 ? -3.770  58.415  124.979 1.00 44.56 ? 268  VAL A CB  1 
ATOM   1974  C  CG1 . VAL A 1 268 ? -2.390  58.795  125.419 1.00 44.93 ? 268  VAL A CG1 1 
ATOM   1975  C  CG2 . VAL A 1 268 ? -3.925  58.716  123.485 1.00 46.05 ? 268  VAL A CG2 1 
ATOM   1976  N  N   . THR A 1 269 ? -2.233  55.826  126.428 1.00 41.14 ? 269  THR A N   1 
ATOM   1977  C  CA  . THR A 1 269 ? -1.442  55.368  127.572 1.00 40.27 ? 269  THR A CA  1 
ATOM   1978  C  C   . THR A 1 269 ? -0.448  56.475  127.904 1.00 41.93 ? 269  THR A C   1 
ATOM   1979  O  O   . THR A 1 269 ? 0.288   56.903  127.037 1.00 41.03 ? 269  THR A O   1 
ATOM   1980  C  CB  . THR A 1 269 ? -0.611  54.129  127.211 1.00 39.94 ? 269  THR A CB  1 
ATOM   1981  O  OG1 . THR A 1 269 ? -1.458  52.989  127.082 1.00 37.71 ? 269  THR A OG1 1 
ATOM   1982  C  CG2 . THR A 1 269 ? 0.424   53.852  128.273 1.00 44.25 ? 269  THR A CG2 1 
ATOM   1983  N  N   . CYS A 1 270 ? -0.413  56.930  129.147 1.00 47.15 ? 270  CYS A N   1 
ATOM   1984  C  CA  . CYS A 1 270 ? 0.535   57.968  129.534 1.00 55.37 ? 270  CYS A CA  1 
ATOM   1985  C  C   . CYS A 1 270 ? 1.765   57.420  130.264 1.00 61.15 ? 270  CYS A C   1 
ATOM   1986  O  O   . CYS A 1 270 ? 1.675   56.497  131.094 1.00 61.96 ? 270  CYS A O   1 
ATOM   1987  C  CB  . CYS A 1 270 ? -0.149  59.022  130.399 1.00 54.72 ? 270  CYS A CB  1 
ATOM   1988  S  SG  . CYS A 1 270 ? -1.488  59.866  129.515 1.00 59.04 ? 270  CYS A SG  1 
ATOM   1989  N  N   . SER A 1 271 ? 2.907   58.036  129.956 1.00 69.35 ? 271  SER A N   1 
ATOM   1990  C  CA  . SER A 1 271 ? 4.231   57.674  130.494 1.00 75.20 ? 271  SER A CA  1 
ATOM   1991  C  C   . SER A 1 271 ? 4.539   56.244  130.056 1.00 79.58 ? 271  SER A C   1 
ATOM   1992  O  O   . SER A 1 271 ? 4.804   55.372  130.893 1.00 78.07 ? 271  SER A O   1 
ATOM   1993  C  CB  . SER A 1 271 ? 4.274   57.786  132.027 1.00 74.58 ? 271  SER A CB  1 
ATOM   1994  O  OG  . SER A 1 271 ? 5.600   58.008  132.477 1.00 71.36 ? 271  SER A OG  1 
ATOM   1995  N  N   . PRO A 1 272 ? 4.507   55.997  128.720 1.00 84.55 ? 272  PRO A N   1 
ATOM   1996  C  CA  . PRO A 1 272 ? 4.753   54.728  128.008 1.00 88.31 ? 272  PRO A CA  1 
ATOM   1997  C  C   . PRO A 1 272 ? 6.033   53.954  128.353 1.00 91.69 ? 272  PRO A C   1 
ATOM   1998  O  O   . PRO A 1 272 ? 7.117   54.530  128.507 1.00 92.67 ? 272  PRO A O   1 
ATOM   1999  C  CB  . PRO A 1 272 ? 4.720   55.145  126.533 1.00 87.92 ? 272  PRO A CB  1 
ATOM   2000  C  CG  . PRO A 1 272 ? 3.748   56.279  126.531 1.00 87.64 ? 272  PRO A CG  1 
ATOM   2001  C  CD  . PRO A 1 272 ? 4.202   57.066  127.746 1.00 84.44 ? 272  PRO A CD  1 
ATOM   2002  N  N   . ASP A 1 273 ? 5.893   52.633  128.447 1.00 94.60 ? 273  ASP A N   1 
ATOM   2003  C  CA  . ASP A 1 273 ? 7.014   51.760  128.770 1.00 96.59 ? 273  ASP A CA  1 
ATOM   2004  C  C   . ASP A 1 273 ? 7.864   51.530  127.531 1.00 97.23 ? 273  ASP A C   1 
ATOM   2005  O  O   . ASP A 1 273 ? 7.953   50.406  127.042 1.00 99.11 ? 273  ASP A O   1 
ATOM   2006  C  CB  . ASP A 1 273 ? 6.509   50.413  129.304 1.00 96.91 ? 273  ASP A CB  1 
ATOM   2007  C  CG  . ASP A 1 273 ? 7.074   50.076  130.684 1.00 99.45 ? 273  ASP A CG  1 
ATOM   2008  O  OD1 . ASP A 1 273 ? 8.319   50.116  130.850 1.00 99.45 ? 273  ASP A OD1 1 
ATOM   2009  O  OD2 . ASP A 1 273 ? 6.268   49.765  131.599 1.00 99.45 ? 273  ASP A OD2 1 
ATOM   2010  N  N   . THR A 1 289 ? 15.562  98.368  104.251 1.00 99.45 ? 289  THR A N   1 
ATOM   2011  C  CA  . THR A 1 289 ? 15.105  96.995  104.554 1.00 99.45 ? 289  THR A CA  1 
ATOM   2012  C  C   . THR A 1 289 ? 14.697  96.238  103.295 1.00 99.45 ? 289  THR A C   1 
ATOM   2013  O  O   . THR A 1 289 ? 13.891  95.290  103.367 1.00 99.35 ? 289  THR A O   1 
ATOM   2014  C  CB  . THR A 1 289 ? 13.777  97.057  105.460 1.00 99.45 ? 289  THR A CB  1 
ATOM   2015  O  OG1 . THR A 1 289 ? 14.053  97.608  106.781 1.00 99.45 ? 289  THR A OG1 1 
ATOM   2016  C  CG2 . THR A 1 289 ? 13.163  95.601  105.600 1.00 99.45 ? 289  THR A CG2 1 
ATOM   2017  N  N   . SER A 1 290 ? 15.266  96.556  102.149 1.00 99.17 ? 290  SER A N   1 
ATOM   2018  C  CA  . SER A 1 290 ? 14.566  95.972  101.031 1.00 99.17 ? 290  SER A CA  1 
ATOM   2019  C  C   . SER A 1 290 ? 14.844  95.005  99.905  1.00 99.17 ? 290  SER A C   1 
ATOM   2020  O  O   . SER A 1 290 ? 15.248  93.900  100.167 1.00 99.17 ? 290  SER A O   1 
ATOM   2021  C  CB  . SER A 1 290 ? 13.865  97.142  100.383 1.00 99.17 ? 290  SER A CB  1 
ATOM   2022  O  OG  . SER A 1 290 ? 12.812  96.640  99.571  1.00 99.17 ? 290  SER A OG  1 
ATOM   2023  N  N   . ALA A 1 291 ? 14.465  95.533  98.707  1.00 99.17 ? 291  ALA A N   1 
ATOM   2024  C  CA  . ALA A 1 291 ? 14.498  94.972  97.349  1.00 99.10 ? 291  ALA A CA  1 
ATOM   2025  C  C   . ALA A 1 291 ? 15.305  93.712  97.162  1.00 98.98 ? 291  ALA A C   1 
ATOM   2026  O  O   . ALA A 1 291 ? 16.096  93.352  98.035  1.00 99.17 ? 291  ALA A O   1 
ATOM   2027  C  CB  . ALA A 1 291 ? 14.958  96.010  96.312  1.00 98.52 ? 291  ALA A CB  1 
ATOM   2028  N  N   . SER A 1 292 ? 15.132  93.035  96.017  1.00 98.96 ? 292  SER A N   1 
ATOM   2029  C  CA  . SER A 1 292 ? 15.901  91.807  95.810  1.00 98.93 ? 292  SER A CA  1 
ATOM   2030  C  C   . SER A 1 292 ? 15.999  91.138  94.426  1.00 98.76 ? 292  SER A C   1 
ATOM   2031  O  O   . SER A 1 292 ? 16.995  91.375  93.728  1.00 99.17 ? 292  SER A O   1 
ATOM   2032  C  CB  . SER A 1 292 ? 15.496  90.796  96.845  1.00 99.17 ? 292  SER A CB  1 
ATOM   2033  O  OG  . SER A 1 292 ? 14.486  91.316  97.709  1.00 99.17 ? 292  SER A OG  1 
ATOM   2034  N  N   . ASN A 1 293 ? 15.040  90.312  93.994  1.00 96.82 ? 293  ASN A N   1 
ATOM   2035  C  CA  . ASN A 1 293 ? 15.137  89.646  92.674  1.00 97.58 ? 293  ASN A CA  1 
ATOM   2036  C  C   . ASN A 1 293 ? 13.804  89.297  92.070  1.00 98.15 ? 293  ASN A C   1 
ATOM   2037  O  O   . ASN A 1 293 ? 13.721  88.839  90.920  1.00 98.56 ? 293  ASN A O   1 
ATOM   2038  C  CB  . ASN A 1 293 ? 15.830  88.275  92.715  1.00 97.28 ? 293  ASN A CB  1 
ATOM   2039  C  CG  . ASN A 1 293 ? 17.174  88.293  93.366  1.00 96.94 ? 293  ASN A CG  1 
ATOM   2040  O  OD1 . ASN A 1 293 ? 17.929  89.248  93.239  1.00 96.75 ? 293  ASN A OD1 1 
ATOM   2041  N  ND2 . ASN A 1 293 ? 17.502  87.200  94.056  1.00 97.94 ? 293  ASN A ND2 1 
ATOM   2042  N  N   . ILE A 1 294 ? 12.765  89.416  92.867  1.00 97.39 ? 294  ILE A N   1 
ATOM   2043  C  CA  . ILE A 1 294 ? 11.461  89.032  92.398  1.00 95.57 ? 294  ILE A CA  1 
ATOM   2044  C  C   . ILE A 1 294 ? 10.560  90.219  92.624  1.00 94.13 ? 294  ILE A C   1 
ATOM   2045  O  O   . ILE A 1 294 ? 10.780  91.008  93.546  1.00 92.44 ? 294  ILE A O   1 
ATOM   2046  C  CB  . ILE A 1 294 ? 11.010  87.755  93.186  1.00 96.91 ? 294  ILE A CB  1 
ATOM   2047  C  CG1 . ILE A 1 294 ? 11.181  86.517  92.296  1.00 98.24 ? 294  ILE A CG1 1 
ATOM   2048  C  CG2 . ILE A 1 294 ? 9.607   87.920  93.747  1.00 95.04 ? 294  ILE A CG2 1 
ATOM   2049  C  CD1 . ILE A 1 294 ? 9.885   85.904  91.816  1.00 99.45 ? 294  ILE A CD1 1 
ATOM   2050  N  N   . THR A 1 295 ? 9.576   90.384  91.756  1.00 92.41 ? 295  THR A N   1 
ATOM   2051  C  CA  . THR A 1 295 ? 8.673   91.494  91.936  1.00 92.05 ? 295  THR A CA  1 
ATOM   2052  C  C   . THR A 1 295 ? 7.275   90.921  91.878  1.00 90.88 ? 295  THR A C   1 
ATOM   2053  O  O   . THR A 1 295 ? 6.940   90.137  90.977  1.00 90.41 ? 295  THR A O   1 
ATOM   2054  C  CB  . THR A 1 295 ? 8.872   92.591  90.847  1.00 93.93 ? 295  THR A CB  1 
ATOM   2055  O  OG1 . THR A 1 295 ? 8.004   92.344  89.730  1.00 94.93 ? 295  THR A OG1 1 
ATOM   2056  C  CG2 . THR A 1 295 ? 10.319  92.600  90.365  1.00 94.51 ? 295  THR A CG2 1 
ATOM   2057  N  N   . VAL A 1 296 ? 6.469   91.294  92.864  1.00 89.96 ? 296  VAL A N   1 
ATOM   2058  C  CA  . VAL A 1 296 ? 5.102   90.810  92.937  1.00 89.99 ? 296  VAL A CA  1 
ATOM   2059  C  C   . VAL A 1 296 ? 4.132   91.979  92.878  1.00 87.97 ? 296  VAL A C   1 
ATOM   2060  O  O   . VAL A 1 296 ? 4.418   93.080  93.356  1.00 86.08 ? 296  VAL A O   1 
ATOM   2061  C  CB  . VAL A 1 296 ? 4.851   89.989  94.243  1.00 91.13 ? 296  VAL A CB  1 
ATOM   2062  C  CG1 . VAL A 1 296 ? 3.977   88.762  93.931  1.00 89.96 ? 296  VAL A CG1 1 
ATOM   2063  C  CG2 . VAL A 1 296 ? 6.192   89.568  94.875  1.00 91.16 ? 296  VAL A CG2 1 
ATOM   2064  N  N   . ILE A 1 297 ? 2.978   91.711  92.290  1.00 87.07 ? 297  ILE A N   1 
ATOM   2065  C  CA  . ILE A 1 297 ? 1.932   92.703  92.122  1.00 87.78 ? 297  ILE A CA  1 
ATOM   2066  C  C   . ILE A 1 297 ? 0.821   92.426  93.143  1.00 85.72 ? 297  ILE A C   1 
ATOM   2067  O  O   . ILE A 1 297 ? 0.096   91.426  93.038  1.00 85.11 ? 297  ILE A O   1 
ATOM   2068  C  CB  . ILE A 1 297 ? 1.398   92.598  90.708  1.00 91.74 ? 297  ILE A CB  1 
ATOM   2069  C  CG1 . ILE A 1 297 ? 2.314   91.658  89.895  1.00 94.08 ? 297  ILE A CG1 1 
ATOM   2070  C  CG2 . ILE A 1 297 ? 1.347   93.980  90.084  1.00 92.57 ? 297  ILE A CG2 1 
ATOM   2071  C  CD1 . ILE A 1 297 ? 1.580   90.884  88.787  1.00 96.92 ? 297  ILE A CD1 1 
ATOM   2072  N  N   . TYR A 1 298 ? 0.692   93.322  94.118  1.00 81.41 ? 298  TYR A N   1 
ATOM   2073  C  CA  . TYR A 1 298 ? -0.270  93.150  95.192  1.00 79.37 ? 298  TYR A CA  1 
ATOM   2074  C  C   . TYR A 1 298 ? -1.424  94.151  95.229  1.00 79.29 ? 298  TYR A C   1 
ATOM   2075  O  O   . TYR A 1 298 ? -1.233  95.336  95.471  1.00 78.51 ? 298  TYR A O   1 
ATOM   2076  C  CB  . TYR A 1 298 ? 0.506   93.156  96.520  1.00 76.96 ? 298  TYR A CB  1 
ATOM   2077  C  CG  . TYR A 1 298 ? -0.298  92.973  97.791  1.00 71.90 ? 298  TYR A CG  1 
ATOM   2078  C  CD1 . TYR A 1 298 ? -1.382  92.096  97.849  1.00 72.05 ? 298  TYR A CD1 1 
ATOM   2079  C  CD2 . TYR A 1 298 ? 0.071   93.638  98.956  1.00 70.77 ? 298  TYR A CD2 1 
ATOM   2080  C  CE1 . TYR A 1 298 ? -2.081  91.889  99.047  1.00 71.59 ? 298  TYR A CE1 1 
ATOM   2081  C  CE2 . TYR A 1 298 ? -0.610  93.439  100.155 1.00 70.56 ? 298  TYR A CE2 1 
ATOM   2082  C  CZ  . TYR A 1 298 ? -1.684  92.565  100.197 1.00 70.86 ? 298  TYR A CZ  1 
ATOM   2083  O  OH  . TYR A 1 298 ? -2.345  92.382  101.391 1.00 68.70 ? 298  TYR A OH  1 
ATOM   2084  N  N   . THR A 1 299 ? -2.624  93.625  95.013  1.00 80.19 ? 299  THR A N   1 
ATOM   2085  C  CA  . THR A 1 299 ? -3.874  94.373  95.019  1.00 82.38 ? 299  THR A CA  1 
ATOM   2086  C  C   . THR A 1 299 ? -4.619  94.171  96.347  1.00 83.47 ? 299  THR A C   1 
ATOM   2087  O  O   . THR A 1 299 ? -4.650  93.061  96.880  1.00 84.46 ? 299  THR A O   1 
ATOM   2088  C  CB  . THR A 1 299 ? -4.821  93.838  93.942  1.00 83.15 ? 299  THR A CB  1 
ATOM   2089  O  OG1 . THR A 1 299 ? -4.160  92.825  93.182  1.00 87.46 ? 299  THR A OG1 1 
ATOM   2090  C  CG2 . THR A 1 299 ? -5.228  94.895  93.030  1.00 84.46 ? 299  THR A CG2 1 
ATOM   2091  N  N   . ILE A 1 300 ? -5.229  95.229  96.873  1.00 84.11 ? 300  ILE A N   1 
ATOM   2092  C  CA  . ILE A 1 300 ? -6.025  95.111  98.094  1.00 83.56 ? 300  ILE A CA  1 
ATOM   2093  C  C   . ILE A 1 300 ? -7.399  95.676  97.724  1.00 85.15 ? 300  ILE A C   1 
ATOM   2094  O  O   . ILE A 1 300 ? -7.491  96.742  97.132  1.00 85.46 ? 300  ILE A O   1 
ATOM   2095  C  CB  . ILE A 1 300 ? -5.385  95.871  99.279  1.00 81.44 ? 300  ILE A CB  1 
ATOM   2096  C  CG1 . ILE A 1 300 ? -5.645  97.368  99.185  1.00 79.56 ? 300  ILE A CG1 1 
ATOM   2097  C  CG2 . ILE A 1 300 ? -3.892  95.628  99.280  1.00 81.65 ? 300  ILE A CG2 1 
ATOM   2098  C  CD1 . ILE A 1 300 ? -5.065  98.144  100.359 1.00 76.67 ? 300  ILE A CD1 1 
ATOM   2099  N  N   . ASN A 1 301 ? -8.465  94.957  98.069  1.00 88.40 ? 301  ASN A N   1 
ATOM   2100  C  CA  . ASN A 1 301 ? -9.819  95.357  97.685  1.00 89.80 ? 301  ASN A CA  1 
ATOM   2101  C  C   . ASN A 1 301 ? -10.850 95.459  98.812  1.00 91.14 ? 301  ASN A C   1 
ATOM   2102  O  O   . ASN A 1 301 ? -10.569 95.121  99.951  1.00 93.14 ? 301  ASN A O   1 
ATOM   2103  C  CB  . ASN A 1 301 ? -10.320 94.366  96.639  1.00 90.36 ? 301  ASN A CB  1 
ATOM   2104  C  CG  . ASN A 1 301 ? -11.349 94.961  95.732  1.00 92.77 ? 301  ASN A CG  1 
ATOM   2105  O  OD1 . ASN A 1 301 ? -11.672 96.153  95.845  1.00 93.21 ? 301  ASN A OD1 1 
ATOM   2106  N  ND2 . ASN A 1 301 ? -11.874 94.147  94.808  1.00 92.56 ? 301  ASN A ND2 1 
ATOM   2107  N  N   . ASN A 1 302 ? -12.052 95.917  98.470  1.00 92.70 ? 302  ASN A N   1 
ATOM   2108  C  CA  . ASN A 1 302 ? -13.159 96.061  99.421  1.00 92.83 ? 302  ASN A CA  1 
ATOM   2109  C  C   . ASN A 1 302 ? -14.391 96.564  98.650  1.00 93.13 ? 302  ASN A C   1 
ATOM   2110  O  O   . ASN A 1 302 ? -14.242 97.262  97.651  1.00 92.96 ? 302  ASN A O   1 
ATOM   2111  C  CB  . ASN A 1 302 ? -12.778 97.052  100.537 1.00 94.03 ? 302  ASN A CB  1 
ATOM   2112  C  CG  . ASN A 1 302 ? -13.866 97.205  101.575 1.00 96.14 ? 302  ASN A CG  1 
ATOM   2113  O  OD1 . ASN A 1 302 ? -14.277 96.250  102.189 1.00 96.32 ? 302  ASN A OD1 1 
ATOM   2114  N  ND2 . ASN A 1 302 ? -14.336 98.410  101.772 1.00 96.27 ? 302  ASN A ND2 1 
ATOM   2115  N  N   . GLN A 1 303 ? -15.595 96.201  99.093  1.00 93.45 ? 303  GLN A N   1 
ATOM   2116  C  CA  . GLN A 1 303 ? -16.844 96.635  98.433  1.00 93.81 ? 303  GLN A CA  1 
ATOM   2117  C  C   . GLN A 1 303 ? -17.933 96.632  99.495  1.00 95.98 ? 303  GLN A C   1 
ATOM   2118  O  O   . GLN A 1 303 ? -18.303 95.509  99.872  1.00 96.17 ? 303  GLN A O   1 
ATOM   2119  C  CB  . GLN A 1 303 ? -17.209 95.641  97.335  1.00 90.32 ? 303  GLN A CB  1 
ATOM   2120  C  CG  . GLN A 1 303 ? -16.409 95.854  96.097  1.00 88.91 ? 303  GLN A CG  1 
ATOM   2121  C  CD  . GLN A 1 303 ? -15.826 94.585  95.575  1.00 90.97 ? 303  GLN A CD  1 
ATOM   2122  O  OE1 . GLN A 1 303 ? -15.505 94.483  94.401  1.00 92.14 ? 303  GLN A OE1 1 
ATOM   2123  N  NE2 . GLN A 1 303 ? -15.673 93.598  96.447  1.00 95.11 ? 303  GLN A NE2 1 
ATOM   2124  N  N   . LEU A 1 304 ? -18.465 97.794  99.978  1.00 99.06 ? 304  LEU A N   1 
ATOM   2125  C  CA  . LEU A 1 304 ? -19.465 97.662  101.069 1.00 99.30 ? 304  LEU A CA  1 
ATOM   2126  C  C   . LEU A 1 304 ? -20.647 98.448  101.760 1.00 99.45 ? 304  LEU A C   1 
ATOM   2127  O  O   . LEU A 1 304 ? -21.325 99.335  101.185 1.00 99.45 ? 304  LEU A O   1 
ATOM   2128  C  CB  . LEU A 1 304 ? -18.692 97.031  102.222 1.00 99.30 ? 304  LEU A CB  1 
ATOM   2129  C  CG  . LEU A 1 304 ? -19.410 95.678  102.109 1.00 99.45 ? 304  LEU A CG  1 
ATOM   2130  C  CD1 . LEU A 1 304 ? -19.934 95.539  103.486 1.00 99.44 ? 304  LEU A CD1 1 
ATOM   2131  C  CD2 . LEU A 1 304 ? -20.617 95.559  100.980 1.00 99.45 ? 304  LEU A CD2 1 
ATOM   2132  N  N   . ARG A 1 305 ? -20.916 97.900  102.973 1.00 99.45 ? 305  ARG A N   1 
ATOM   2133  C  CA  . ARG A 1 305 ? -21.905 98.242  104.026 1.00 99.45 ? 305  ARG A CA  1 
ATOM   2134  C  C   . ARG A 1 305 ? -21.189 99.420  104.636 1.00 99.45 ? 305  ARG A C   1 
ATOM   2135  O  O   . ARG A 1 305 ? -21.064 100.427 103.933 1.00 99.45 ? 305  ARG A O   1 
ATOM   2136  C  CB  . ARG A 1 305 ? -22.021 97.118  105.112 1.00 99.45 ? 305  ARG A CB  1 
ATOM   2137  C  CG  . ARG A 1 305 ? -22.324 95.636  104.669 1.00 99.45 ? 305  ARG A CG  1 
ATOM   2138  C  CD  . ARG A 1 305 ? -21.678 94.609  105.658 1.00 99.45 ? 305  ARG A CD  1 
ATOM   2139  N  NE  . ARG A 1 305 ? -22.589 93.518  105.994 1.00 99.45 ? 305  ARG A NE  1 
ATOM   2140  C  CZ  . ARG A 1 305 ? -22.466 92.736  107.065 1.00 99.45 ? 305  ARG A CZ  1 
ATOM   2141  N  NH1 . ARG A 1 305 ? -21.458 92.917  107.914 1.00 99.45 ? 305  ARG A NH1 1 
ATOM   2142  N  NH2 . ARG A 1 305 ? -23.372 91.792  107.302 1.00 99.45 ? 305  ARG A NH2 1 
ATOM   2143  N  N   . GLY A 1 306 ? -20.713 99.302  105.889 1.00 99.45 ? 306  GLY A N   1 
ATOM   2144  C  CA  . GLY A 1 306 ? -19.972 100.395 106.515 1.00 98.52 ? 306  GLY A CA  1 
ATOM   2145  C  C   . GLY A 1 306 ? -19.062 101.199 105.573 1.00 98.87 ? 306  GLY A C   1 
ATOM   2146  O  O   . GLY A 1 306 ? -18.039 101.739 106.008 1.00 97.16 ? 306  GLY A O   1 
ATOM   2147  N  N   . VAL A 1 307 ? -19.471 101.291 104.299 1.00 99.45 ? 307  VAL A N   1 
ATOM   2148  C  CA  . VAL A 1 307 ? -18.813 101.993 103.181 1.00 99.45 ? 307  VAL A CA  1 
ATOM   2149  C  C   . VAL A 1 307 ? -17.300 101.871 103.287 1.00 99.45 ? 307  VAL A C   1 
ATOM   2150  O  O   . VAL A 1 307 ? -16.797 100.805 103.683 1.00 99.45 ? 307  VAL A O   1 
ATOM   2151  C  CB  . VAL A 1 307 ? -19.251 103.519 103.085 1.00 99.45 ? 307  VAL A CB  1 
ATOM   2152  C  CG1 . VAL A 1 307 ? -20.760 103.624 102.795 1.00 99.45 ? 307  VAL A CG1 1 
ATOM   2153  C  CG2 . VAL A 1 307 ? -18.906 104.271 104.372 1.00 98.56 ? 307  VAL A CG2 1 
ATOM   2154  N  N   . GLU A 1 308 ? -16.570 102.926 102.919 1.00 99.45 ? 308  GLU A N   1 
ATOM   2155  C  CA  . GLU A 1 308 ? -15.110 102.885 103.030 1.00 97.84 ? 308  GLU A CA  1 
ATOM   2156  C  C   . GLU A 1 308 ? -14.500 101.919 101.992 1.00 96.59 ? 308  GLU A C   1 
ATOM   2157  O  O   . GLU A 1 308 ? -13.716 101.033 102.343 1.00 96.17 ? 308  GLU A O   1 
ATOM   2158  C  CB  . GLU A 1 308 ? -14.792 102.456 104.477 1.00 95.63 ? 308  GLU A CB  1 
ATOM   2159  C  CG  . GLU A 1 308 ? -13.392 102.566 104.985 1.00 97.19 ? 308  GLU A CG  1 
ATOM   2160  C  CD  . GLU A 1 308 ? -12.676 103.794 104.491 1.00 99.45 ? 308  GLU A CD  1 
ATOM   2161  O  OE1 . GLU A 1 308 ? -12.627 103.952 103.324 1.00 97.06 ? 308  GLU A OE1 1 
ATOM   2162  O  OE2 . GLU A 1 308 ? -12.126 104.627 105.191 1.00 99.45 ? 308  GLU A OE2 1 
ATOM   2163  N  N   . LEU A 1 309 ? -14.849 102.096 100.717 1.00 94.78 ? 309  LEU A N   1 
ATOM   2164  C  CA  . LEU A 1 309 ? -14.338 101.203 99.679  1.00 93.07 ? 309  LEU A CA  1 
ATOM   2165  C  C   . LEU A 1 309 ? -12.900 101.503 99.286  1.00 93.35 ? 309  LEU A C   1 
ATOM   2166  O  O   . LEU A 1 309 ? -12.455 102.649 99.310  1.00 93.70 ? 309  LEU A O   1 
ATOM   2167  C  CB  . LEU A 1 309 ? -15.240 101.233 98.437  1.00 91.24 ? 309  LEU A CB  1 
ATOM   2168  C  CG  . LEU A 1 309 ? -16.739 101.131 98.735  1.00 89.42 ? 309  LEU A CG  1 
ATOM   2169  C  CD1 . LEU A 1 309 ? -17.513 100.882 97.458  1.00 89.50 ? 309  LEU A CD1 1 
ATOM   2170  C  CD2 . LEU A 1 309 ? -16.984 100.020 99.715  1.00 87.69 ? 309  LEU A CD2 1 
ATOM   2171  N  N   . LEU A 1 310 ? -12.177 100.444 98.938  1.00 93.24 ? 310  LEU A N   1 
ATOM   2172  C  CA  . LEU A 1 310 ? -10.780 100.536 98.540  1.00 91.77 ? 310  LEU A CA  1 
ATOM   2173  C  C   . LEU A 1 310 ? -10.627 99.825  97.210  1.00 90.78 ? 310  LEU A C   1 
ATOM   2174  O  O   . LEU A 1 310 ? -11.595 99.284  96.662  1.00 90.14 ? 310  LEU A O   1 
ATOM   2175  C  CB  . LEU A 1 310 ? -9.880  99.834  99.565  1.00 92.51 ? 310  LEU A CB  1 
ATOM   2176  C  CG  . LEU A 1 310 ? -9.765  100.387 100.983 1.00 92.93 ? 310  LEU A CG  1 
ATOM   2177  C  CD1 . LEU A 1 310 ? -9.680  99.259  101.997 1.00 92.27 ? 310  LEU A CD1 1 
ATOM   2178  C  CD2 . LEU A 1 310 ? -8.534  101.248 101.062 1.00 93.30 ? 310  LEU A CD2 1 
ATOM   2179  N  N   . PHE A 1 311 ? -9.392  99.827  96.720  1.00 88.60 ? 311  PHE A N   1 
ATOM   2180  C  CA  . PHE A 1 311 ? -8.999  99.185  95.471  1.00 87.94 ? 311  PHE A CA  1 
ATOM   2181  C  C   . PHE A 1 311 ? -7.717  99.899  95.079  1.00 88.39 ? 311  PHE A C   1 
ATOM   2182  O  O   . PHE A 1 311 ? -7.756  100.930 94.406  1.00 91.37 ? 311  PHE A O   1 
ATOM   2183  C  CB  . PHE A 1 311 ? -10.060 99.370  94.382  1.00 85.10 ? 311  PHE A CB  1 
ATOM   2184  C  CG  . PHE A 1 311 ? -9.910  98.431  93.209  1.00 83.41 ? 311  PHE A CG  1 
ATOM   2185  C  CD1 . PHE A 1 311 ? -8.651  98.136  92.682  1.00 81.49 ? 311  PHE A CD1 1 
ATOM   2186  C  CD2 . PHE A 1 311 ? -11.043 97.883  92.591  1.00 82.99 ? 311  PHE A CD2 1 
ATOM   2187  C  CE1 . PHE A 1 311 ? -8.530  97.309  91.549  1.00 84.55 ? 311  PHE A CE1 1 
ATOM   2188  C  CE2 . PHE A 1 311 ? -10.931 97.057  91.458  1.00 82.58 ? 311  PHE A CE2 1 
ATOM   2189  C  CZ  . PHE A 1 311 ? -9.677  96.772  90.940  1.00 82.85 ? 311  PHE A CZ  1 
ATOM   2190  N  N   . ASN A 1 312 ? -6.585  99.361  95.540  1.00 87.43 ? 312  ASN A N   1 
ATOM   2191  C  CA  . ASN A 1 312 ? -5.255  99.924  95.264  1.00 86.42 ? 312  ASN A CA  1 
ATOM   2192  C  C   . ASN A 1 312 ? -4.168  98.859  95.038  1.00 85.89 ? 312  ASN A C   1 
ATOM   2193  O  O   . ASN A 1 312 ? -3.945  98.001  95.898  1.00 87.88 ? 312  ASN A O   1 
ATOM   2194  C  CB  . ASN A 1 312 ? -4.819  100.860 96.411  1.00 84.58 ? 312  ASN A CB  1 
ATOM   2195  C  CG  . ASN A 1 312 ? -5.115  102.321 96.116  0.00 85.32 ? 312  ASN A CG  1 
ATOM   2196  O  OD1 . ASN A 1 312 ? -5.127  102.742 94.957  0.00 86.07 ? 312  ASN A OD1 1 
ATOM   2197  N  ND2 . ASN A 1 312 ? -5.337  103.104 97.164  0.00 86.07 ? 312  ASN A ND2 1 
ATOM   2198  N  N   . GLU A 1 313 ? -3.500  98.932  93.881  1.00 85.76 ? 313  GLU A N   1 
ATOM   2199  C  CA  . GLU A 1 313 ? -2.429  98.001  93.518  1.00 84.67 ? 313  GLU A CA  1 
ATOM   2200  C  C   . GLU A 1 313 ? -1.059  98.514  93.958  1.00 84.19 ? 313  GLU A C   1 
ATOM   2201  O  O   . GLU A 1 313 ? -0.943  99.533  94.635  1.00 83.56 ? 313  GLU A O   1 
ATOM   2202  C  CB  . GLU A 1 313 ? -2.401  97.757  92.003  1.00 85.41 ? 313  GLU A CB  1 
ATOM   2203  C  CG  . GLU A 1 313 ? -3.367  96.698  91.488  1.00 89.17 ? 313  GLU A CG  1 
ATOM   2204  C  CD  . GLU A 1 313 ? -4.838  97.137  91.525  1.00 95.37 ? 313  GLU A CD  1 
ATOM   2205  O  OE1 . GLU A 1 313 ? -5.273  97.708  92.560  1.00 95.25 ? 313  GLU A OE1 1 
ATOM   2206  O  OE2 . GLU A 1 313 ? -5.568  96.884  90.528  1.00 99.44 ? 313  GLU A OE2 1 
ATOM   2207  N  N   . THR A 1 314 ? -0.024  97.784  93.561  1.00 84.90 ? 314  THR A N   1 
ATOM   2208  C  CA  . THR A 1 314 ? 1.360   98.116  93.880  1.00 85.06 ? 314  THR A CA  1 
ATOM   2209  C  C   . THR A 1 314 ? 2.228   96.980  93.349  1.00 86.42 ? 314  THR A C   1 
ATOM   2210  O  O   . THR A 1 314 ? 1.729   95.895  93.032  1.00 88.64 ? 314  THR A O   1 
ATOM   2211  C  CB  . THR A 1 314 ? 1.546   98.264  95.392  1.00 81.15 ? 314  THR A CB  1 
ATOM   2212  N  N   . ILE A 1 315 ? 3.521   97.237  93.218  1.00 86.87 ? 315  ILE A N   1 
ATOM   2213  C  CA  . ILE A 1 315 ? 4.450   96.218  92.741  1.00 87.93 ? 315  ILE A CA  1 
ATOM   2214  C  C   . ILE A 1 315 ? 5.544   96.151  93.804  1.00 88.25 ? 315  ILE A C   1 
ATOM   2215  O  O   . ILE A 1 315 ? 6.124   97.174  94.149  1.00 89.05 ? 315  ILE A O   1 
ATOM   2216  C  CB  . ILE A 1 315 ? 5.022   96.621  91.382  1.00 84.76 ? 315  ILE A CB  1 
ATOM   2217  N  N   . ASN A 1 316 ? 5.823   94.966  94.339  1.00 88.35 ? 316  ASN A N   1 
ATOM   2218  C  CA  . ASN A 1 316 ? 6.827   94.860  95.393  1.00 88.22 ? 316  ASN A CA  1 
ATOM   2219  C  C   . ASN A 1 316 ? 8.090   94.106  94.999  1.00 88.90 ? 316  ASN A C   1 
ATOM   2220  O  O   . ASN A 1 316 ? 8.049   93.182  94.183  1.00 89.82 ? 316  ASN A O   1 
ATOM   2221  C  CB  . ASN A 1 316 ? 6.198   94.228  96.627  1.00 87.48 ? 316  ASN A CB  1 
ATOM   2222  N  N   . VAL A 1 317 ? 9.210   94.505  95.596  1.00 89.38 ? 317  VAL A N   1 
ATOM   2223  C  CA  . VAL A 1 317 ? 10.501  93.885  95.322  1.00 91.47 ? 317  VAL A CA  1 
ATOM   2224  C  C   . VAL A 1 317 ? 10.891  92.971  96.472  1.00 93.33 ? 317  VAL A C   1 
ATOM   2225  O  O   . VAL A 1 317 ? 11.472  93.422  97.455  1.00 95.93 ? 317  VAL A O   1 
ATOM   2226  C  CB  . VAL A 1 317 ? 11.562  94.954  95.138  1.00 89.62 ? 317  VAL A CB  1 
ATOM   2227  N  N   . SER A 1 318 ? 10.585  91.685  96.352  1.00 95.08 ? 318  SER A N   1 
ATOM   2228  C  CA  . SER A 1 318 ? 10.910  90.715  97.403  1.00 96.34 ? 318  SER A CA  1 
ATOM   2229  C  C   . SER A 1 318 ? 12.104  89.854  97.006  1.00 96.80 ? 318  SER A C   1 
ATOM   2230  O  O   . SER A 1 318 ? 12.346  89.612  95.828  1.00 96.06 ? 318  SER A O   1 
ATOM   2231  C  CB  . SER A 1 318 ? 9.694   89.824  97.666  1.00 96.62 ? 318  SER A CB  1 
ATOM   2232  O  OG  . SER A 1 318 ? 8.590   90.590  98.118  1.00 96.74 ? 318  SER A OG  1 
ATOM   2233  N  N   . VAL A 1 319 ? 12.835  89.366  98.006  1.00 97.62 ? 319  VAL A N   1 
ATOM   2234  C  CA  . VAL A 1 319 ? 14.011  88.531  97.728  1.00 98.41 ? 319  VAL A CA  1 
ATOM   2235  C  C   . VAL A 1 319 ? 13.713  87.299  96.847  1.00 99.45 ? 319  VAL A C   1 
ATOM   2236  O  O   . VAL A 1 319 ? 12.607  87.031  96.447  1.00 99.45 ? 319  VAL A O   1 
ATOM   2237  C  CB  . VAL A 1 319 ? 14.737  88.113  99.024  1.00 98.91 ? 319  VAL A CB  1 
ATOM   2238  C  CG1 . VAL A 1 319 ? 14.817  89.259  100.046 1.00 97.82 ? 319  VAL A CG1 1 
ATOM   2239  C  CG2 . VAL A 1 319 ? 14.022  86.891  99.637  1.00 99.45 ? 319  VAL A CG2 1 
ATOM   2240  N  N   . LYS A 1 320 ? 14.799  86.619  96.563  1.00 99.08 ? 320  LYS A N   1 
ATOM   2241  C  CA  . LYS A 1 320 ? 14.910  85.413  95.777  1.00 99.17 ? 320  LYS A CA  1 
ATOM   2242  C  C   . LYS A 1 320 ? 13.694  84.683  95.188  1.00 99.17 ? 320  LYS A C   1 
ATOM   2243  O  O   . LYS A 1 320 ? 13.586  84.435  94.001  1.00 99.17 ? 320  LYS A O   1 
ATOM   2244  C  CB  . LYS A 1 320 ? 15.663  84.394  96.595  1.00 99.17 ? 320  LYS A CB  1 
ATOM   2245  N  N   . SER A 1 321 ? 12.792  84.355  96.066  1.00 99.14 ? 321  SER A N   1 
ATOM   2246  C  CA  . SER A 1 321 ? 11.578  83.623  95.895  1.00 98.93 ? 321  SER A CA  1 
ATOM   2247  C  C   . SER A 1 321 ? 11.945  83.244  97.282  1.00 99.06 ? 321  SER A C   1 
ATOM   2248  O  O   . SER A 1 321 ? 13.061  83.531  97.731  1.00 99.17 ? 321  SER A O   1 
ATOM   2249  C  CB  . SER A 1 321 ? 11.605  82.435  94.899  1.00 98.25 ? 321  SER A CB  1 
ATOM   2250  N  N   . GLY A 1 322 ? 11.068  82.628  98.031  1.00 98.57 ? 322  GLY A N   1 
ATOM   2251  C  CA  . GLY A 1 322 ? 11.470  82.383  99.425  1.00 97.72 ? 322  GLY A CA  1 
ATOM   2252  C  C   . GLY A 1 322 ? 10.685  83.496  100.073 1.00 97.04 ? 322  GLY A C   1 
ATOM   2253  O  O   . GLY A 1 322 ? 9.462   83.393  100.042 1.00 97.51 ? 322  GLY A O   1 
ATOM   2254  N  N   . SER A 1 323 ? 11.322  84.540  100.618 1.00 96.86 ? 323  SER A N   1 
ATOM   2255  C  CA  . SER A 1 323 ? 10.593  85.643  101.258 1.00 95.16 ? 323  SER A CA  1 
ATOM   2256  C  C   . SER A 1 323 ? 9.125   85.316  101.042 1.00 94.00 ? 323  SER A C   1 
ATOM   2257  O  O   . SER A 1 323 ? 8.553   85.636  99.989  1.00 95.21 ? 323  SER A O   1 
ATOM   2258  C  CB  . SER A 1 323 ? 10.940  86.967  100.593 1.00 95.14 ? 323  SER A CB  1 
ATOM   2259  O  OG  . SER A 1 323 ? 11.964  87.672  101.282 1.00 93.76 ? 323  SER A OG  1 
ATOM   2260  N  N   . VAL A 1 324 ? 8.563   84.585  102.004 1.00 90.70 ? 324  VAL A N   1 
ATOM   2261  C  CA  . VAL A 1 324 ? 7.179   84.150  101.968 1.00 85.89 ? 324  VAL A CA  1 
ATOM   2262  C  C   . VAL A 1 324 ? 6.311   85.296  101.461 1.00 83.81 ? 324  VAL A C   1 
ATOM   2263  O  O   . VAL A 1 324 ? 6.764   86.437  101.377 1.00 84.00 ? 324  VAL A O   1 
ATOM   2264  C  CB  . VAL A 1 324 ? 6.734   83.765  103.379 1.00 84.51 ? 324  VAL A CB  1 
ATOM   2265  C  CG1 . VAL A 1 324 ? 7.489   82.535  103.854 1.00 85.17 ? 324  VAL A CG1 1 
ATOM   2266  C  CG2 . VAL A 1 324 ? 7.018   84.911  104.324 1.00 81.36 ? 324  VAL A CG2 1 
ATOM   2267  N  N   . LEU A 1 325 ? 5.065   85.011  101.122 1.00 79.27 ? 325  LEU A N   1 
ATOM   2268  C  CA  . LEU A 1 325 ? 4.210   86.077  100.657 1.00 73.78 ? 325  LEU A CA  1 
ATOM   2269  C  C   . LEU A 1 325 ? 4.056   87.184  101.719 1.00 72.70 ? 325  LEU A C   1 
ATOM   2270  O  O   . LEU A 1 325 ? 3.592   88.277  101.402 1.00 71.31 ? 325  LEU A O   1 
ATOM   2271  C  CB  . LEU A 1 325 ? 2.852   85.497  100.270 1.00 73.76 ? 325  LEU A CB  1 
ATOM   2272  C  CG  . LEU A 1 325 ? 1.801   86.421  99.645  1.00 74.14 ? 325  LEU A CG  1 
ATOM   2273  C  CD1 . LEU A 1 325 ? 0.960   87.077  100.731 1.00 71.93 ? 325  LEU A CD1 1 
ATOM   2274  C  CD2 . LEU A 1 325 ? 2.495   87.451  98.754  1.00 70.91 ? 325  LEU A CD2 1 
ATOM   2275  N  N   . LEU A 1 326 ? 4.463   86.913  102.964 1.00 70.51 ? 326  LEU A N   1 
ATOM   2276  C  CA  . LEU A 1 326 ? 4.347   87.888  104.054 1.00 70.20 ? 326  LEU A CA  1 
ATOM   2277  C  C   . LEU A 1 326 ? 5.379   89.002  103.971 1.00 72.87 ? 326  LEU A C   1 
ATOM   2278  O  O   . LEU A 1 326 ? 5.190   90.078  104.545 1.00 73.18 ? 326  LEU A O   1 
ATOM   2279  C  CB  . LEU A 1 326 ? 4.481   87.212  105.427 1.00 68.25 ? 326  LEU A CB  1 
ATOM   2280  C  CG  . LEU A 1 326 ? 4.513   88.174  106.636 1.00 67.65 ? 326  LEU A CG  1 
ATOM   2281  C  CD1 . LEU A 1 326 ? 3.152   88.812  106.852 1.00 65.01 ? 326  LEU A CD1 1 
ATOM   2282  C  CD2 . LEU A 1 326 ? 4.910   87.430  107.877 1.00 68.98 ? 326  LEU A CD2 1 
ATOM   2283  N  N   . VAL A 1 327 ? 6.490   88.742  103.292 1.00 74.99 ? 327  VAL A N   1 
ATOM   2284  C  CA  . VAL A 1 327 ? 7.515   89.769  103.157 1.00 77.58 ? 327  VAL A CA  1 
ATOM   2285  C  C   . VAL A 1 327 ? 6.936   90.852  102.238 1.00 78.00 ? 327  VAL A C   1 
ATOM   2286  O  O   . VAL A 1 327 ? 7.126   92.050  102.467 1.00 76.93 ? 327  VAL A O   1 
ATOM   2287  C  CB  . VAL A 1 327 ? 8.835   89.176  102.568 1.00 77.75 ? 327  VAL A CB  1 
ATOM   2288  C  CG1 . VAL A 1 327 ? 9.801   90.291  102.188 1.00 74.21 ? 327  VAL A CG1 1 
ATOM   2289  C  CG2 . VAL A 1 327 ? 9.492   88.271  103.607 1.00 77.80 ? 327  VAL A CG2 1 
ATOM   2290  N  N   . VAL A 1 328 ? 6.204   90.405  101.218 1.00 78.43 ? 328  VAL A N   1 
ATOM   2291  C  CA  . VAL A 1 328 ? 5.561   91.286  100.252 1.00 76.97 ? 328  VAL A CA  1 
ATOM   2292  C  C   . VAL A 1 328 ? 4.660   92.285  100.963 1.00 77.40 ? 328  VAL A C   1 
ATOM   2293  O  O   . VAL A 1 328 ? 4.736   93.477  100.710 1.00 78.05 ? 328  VAL A O   1 
ATOM   2294  C  CB  . VAL A 1 328 ? 4.696   90.484  99.273  1.00 76.66 ? 328  VAL A CB  1 
ATOM   2295  C  CG1 . VAL A 1 328 ? 4.104   91.412  98.219  1.00 73.22 ? 328  VAL A CG1 1 
ATOM   2296  C  CG2 . VAL A 1 328 ? 5.525   89.373  98.652  1.00 74.71 ? 328  VAL A CG2 1 
ATOM   2297  N  N   . LEU A 1 329 ? 3.804   91.789  101.850 1.00 78.55 ? 329  LEU A N   1 
ATOM   2298  C  CA  . LEU A 1 329 ? 2.896   92.653  102.590 1.00 79.56 ? 329  LEU A CA  1 
ATOM   2299  C  C   . LEU A 1 329 ? 3.650   93.589  103.522 1.00 81.42 ? 329  LEU A C   1 
ATOM   2300  O  O   . LEU A 1 329 ? 3.204   94.715  103.755 1.00 82.05 ? 329  LEU A O   1 
ATOM   2301  C  CB  . LEU A 1 329 ? 1.914   91.842  103.446 1.00 77.58 ? 329  LEU A CB  1 
ATOM   2302  C  CG  . LEU A 1 329 ? 1.263   90.556  102.946 1.00 76.55 ? 329  LEU A CG  1 
ATOM   2303  C  CD1 . LEU A 1 329 ? 0.171   90.187  103.931 1.00 75.19 ? 329  LEU A CD1 1 
ATOM   2304  C  CD2 . LEU A 1 329 ? 0.699   90.719  101.551 1.00 72.60 ? 329  LEU A CD2 1 
ATOM   2305  N  N   . GLU A 1 330 ? 4.774   93.126  104.074 1.00 83.24 ? 330  GLU A N   1 
ATOM   2306  C  CA  . GLU A 1 330 ? 5.555   93.950  105.001 1.00 85.65 ? 330  GLU A CA  1 
ATOM   2307  C  C   . GLU A 1 330 ? 6.206   95.128  104.294 1.00 86.60 ? 330  GLU A C   1 
ATOM   2308  O  O   . GLU A 1 330 ? 6.169   96.262  104.791 1.00 84.81 ? 330  GLU A O   1 
ATOM   2309  C  CB  . GLU A 1 330 ? 6.621   93.113  105.717 1.00 85.54 ? 330  GLU A CB  1 
ATOM   2310  C  CG  . GLU A 1 330 ? 6.050   92.120  106.705 1.00 87.58 ? 330  GLU A CG  1 
ATOM   2311  C  CD  . GLU A 1 330 ? 7.122   91.344  107.426 1.00 90.05 ? 330  GLU A CD  1 
ATOM   2312  O  OE1 . GLU A 1 330 ? 8.244   91.257  106.882 1.00 91.61 ? 330  GLU A OE1 1 
ATOM   2313  O  OE2 . GLU A 1 330 ? 6.844   90.811  108.524 1.00 90.18 ? 330  GLU A OE2 1 
ATOM   2314  N  N   . GLU A 1 331 ? 6.795   94.855  103.131 1.00 87.69 ? 331  GLU A N   1 
ATOM   2315  C  CA  . GLU A 1 331 ? 7.444   95.891  102.333 1.00 88.38 ? 331  GLU A CA  1 
ATOM   2316  C  C   . GLU A 1 331 ? 6.416   96.865  101.796 1.00 88.29 ? 331  GLU A C   1 
ATOM   2317  O  O   . GLU A 1 331 ? 6.671   98.065  101.734 1.00 88.49 ? 331  GLU A O   1 
ATOM   2318  C  CB  . GLU A 1 331 ? 8.229   95.270  101.179 1.00 88.25 ? 331  GLU A CB  1 
ATOM   2319  C  CG  . GLU A 1 331 ? 9.580   94.737  101.613 1.00 88.83 ? 331  GLU A CG  1 
ATOM   2320  C  CD  . GLU A 1 331 ? 10.492  95.836  102.130 1.00 89.24 ? 331  GLU A CD  1 
ATOM   2321  O  OE1 . GLU A 1 331 ? 10.296  96.322  103.264 1.00 89.70 ? 331  GLU A OE1 1 
ATOM   2322  O  OE2 . GLU A 1 331 ? 11.403  96.228  101.388 1.00 91.72 ? 331  GLU A OE2 1 
ATOM   2323  N  N   . ALA A 1 332 ? 5.253   96.349  101.412 1.00 88.49 ? 332  ALA A N   1 
ATOM   2324  C  CA  . ALA A 1 332 ? 4.184   97.195  100.903 1.00 88.96 ? 332  ALA A CA  1 
ATOM   2325  C  C   . ALA A 1 332 ? 3.762   98.165  102.008 1.00 89.33 ? 332  ALA A C   1 
ATOM   2326  O  O   . ALA A 1 332 ? 3.349   99.287  101.740 1.00 89.64 ? 332  ALA A O   1 
ATOM   2327  C  CB  . ALA A 1 332 ? 3.003   96.342  100.461 1.00 86.83 ? 332  ALA A CB  1 
ATOM   2328  N  N   . GLN A 1 333 ? 3.870   97.735  103.256 1.00 89.81 ? 333  GLN A N   1 
ATOM   2329  C  CA  . GLN A 1 333 ? 3.510   98.605  104.365 1.00 92.37 ? 333  GLN A CA  1 
ATOM   2330  C  C   . GLN A 1 333 ? 4.653   99.591  104.631 1.00 94.41 ? 333  GLN A C   1 
ATOM   2331  O  O   . GLN A 1 333 ? 4.450   100.647 105.241 1.00 94.97 ? 333  GLN A O   1 
ATOM   2332  C  CB  . GLN A 1 333 ? 3.230   97.775  105.623 1.00 92.81 ? 333  GLN A CB  1 
ATOM   2333  C  CG  . GLN A 1 333 ? 2.947   98.604  106.868 1.00 93.65 ? 333  GLN A CG  1 
ATOM   2334  C  CD  . GLN A 1 333 ? 2.830   97.755  108.117 1.00 94.80 ? 333  GLN A CD  1 
ATOM   2335  O  OE1 . GLN A 1 333 ? 3.657   96.876  108.353 1.00 96.26 ? 333  GLN A OE1 1 
ATOM   2336  N  NE2 . GLN A 1 333 ? 1.809   98.018  108.933 1.00 94.30 ? 333  GLN A NE2 1 
ATOM   2337  N  N   . ARG A 1 334 ? 5.854   99.236  104.171 1.00 95.69 ? 334  ARG A N   1 
ATOM   2338  C  CA  . ARG A 1 334 ? 7.042   100.074 104.351 1.00 95.59 ? 334  ARG A CA  1 
ATOM   2339  C  C   . ARG A 1 334 ? 6.908   101.321 103.474 1.00 95.42 ? 334  ARG A C   1 
ATOM   2340  O  O   . ARG A 1 334 ? 7.096   102.446 103.955 1.00 94.18 ? 334  ARG A O   1 
ATOM   2341  C  CB  . ARG A 1 334 ? 8.313   99.287  103.977 1.00 96.13 ? 334  ARG A CB  1 
ATOM   2342  C  CG  . ARG A 1 334 ? 9.621   99.947  104.400 1.00 95.62 ? 334  ARG A CG  1 
ATOM   2343  C  CD  . ARG A 1 334 ? 9.667   100.134 105.908 1.00 95.05 ? 334  ARG A CD  1 
ATOM   2344  N  NE  . ARG A 1 334 ? 10.909  100.759 106.352 1.00 97.39 ? 334  ARG A NE  1 
ATOM   2345  C  CZ  . ARG A 1 334 ? 11.199  102.051 106.214 1.00 99.45 ? 334  ARG A CZ  1 
ATOM   2346  N  NH1 . ARG A 1 334 ? 10.328  102.881 105.643 1.00 99.45 ? 334  ARG A NH1 1 
ATOM   2347  N  NH2 . ARG A 1 334 ? 12.371  102.513 106.639 1.00 99.45 ? 334  ARG A NH2 1 
ATOM   2348  N  N   . LYS A 1 335 ? 6.579   101.111 102.196 1.00 94.07 ? 335  LYS A N   1 
ATOM   2349  C  CA  . LYS A 1 335 ? 6.389   102.207 101.249 1.00 95.43 ? 335  LYS A CA  1 
ATOM   2350  C  C   . LYS A 1 335 ? 5.397   103.180 101.863 1.00 97.22 ? 335  LYS A C   1 
ATOM   2351  O  O   . LYS A 1 335 ? 5.212   104.299 101.379 1.00 97.97 ? 335  LYS A O   1 
ATOM   2352  C  CB  . LYS A 1 335 ? 5.821   101.693 99.929  1.00 94.89 ? 335  LYS A CB  1 
ATOM   2353  C  CG  . LYS A 1 335 ? 6.734   100.756 99.179  1.00 94.32 ? 335  LYS A CG  1 
ATOM   2354  C  CD  . LYS A 1 335 ? 6.020   100.247 97.949  1.00 96.73 ? 335  LYS A CD  1 
ATOM   2355  C  CE  . LYS A 1 335 ? 6.864   99.251  97.185  1.00 97.34 ? 335  LYS A CE  1 
ATOM   2356  N  NZ  . LYS A 1 335 ? 6.028   98.566  96.160  1.00 98.70 ? 335  LYS A NZ  1 
ATOM   2357  N  N   . ASN A 1 336 ? 4.740   102.706 102.918 1.00 98.32 ? 336  ASN A N   1 
ATOM   2358  C  CA  . ASN A 1 336 ? 3.762   103.462 103.685 1.00 98.93 ? 336  ASN A CA  1 
ATOM   2359  C  C   . ASN A 1 336 ? 2.544   104.050 102.950 1.00 99.45 ? 336  ASN A C   1 
ATOM   2360  O  O   . ASN A 1 336 ? 1.985   105.055 103.411 1.00 99.45 ? 336  ASN A O   1 
ATOM   2361  C  CB  . ASN A 1 336 ? 4.484   104.571 104.475 1.00 98.88 ? 336  ASN A CB  1 
ATOM   2362  N  N   . PRO A 1 337 ? 2.111   103.453 101.809 1.00 99.27 ? 337  PRO A N   1 
ATOM   2363  C  CA  . PRO A 1 337 ? 0.937   104.038 101.142 1.00 98.76 ? 337  PRO A CA  1 
ATOM   2364  C  C   . PRO A 1 337 ? -0.285  103.898 102.070 1.00 99.45 ? 337  PRO A C   1 
ATOM   2365  O  O   . PRO A 1 337 ? -1.413  103.625 101.632 1.00 99.45 ? 337  PRO A O   1 
ATOM   2366  C  CB  . PRO A 1 337 ? 0.815   103.206 99.864  1.00 97.45 ? 337  PRO A CB  1 
ATOM   2367  C  CG  . PRO A 1 337 ? 2.238   102.814 99.588  1.00 98.45 ? 337  PRO A CG  1 
ATOM   2368  C  CD  . PRO A 1 337 ? 2.711   102.409 100.960 1.00 98.48 ? 337  PRO A CD  1 
ATOM   2369  N  N   . MET A 1 338 ? -0.016  104.079 103.364 1.00 99.32 ? 338  MET A N   1 
ATOM   2370  C  CA  . MET A 1 338 ? -0.991  104.003 104.443 1.00 98.97 ? 338  MET A CA  1 
ATOM   2371  C  C   . MET A 1 338 ? -1.715  102.666 104.503 1.00 98.80 ? 338  MET A C   1 
ATOM   2372  O  O   . MET A 1 338 ? -2.414  102.379 105.491 1.00 99.45 ? 338  MET A O   1 
ATOM   2373  C  CB  . MET A 1 338 ? -2.016  105.142 104.341 1.00 99.45 ? 338  MET A CB  1 
ATOM   2374  C  CG  . MET A 1 338 ? -2.885  105.275 105.593 1.00 99.43 ? 338  MET A CG  1 
ATOM   2375  S  SD  . MET A 1 338 ? -4.181  106.519 105.490 1.00 99.45 ? 338  MET A SD  1 
ATOM   2376  C  CE  . MET A 1 338 ? -5.599  105.509 104.862 1.00 96.85 ? 338  MET A CE  1 
ATOM   2377  N  N   . PHE A 1 339 ? -1.569  101.851 103.457 1.00 96.35 ? 339  PHE A N   1 
ATOM   2378  C  CA  . PHE A 1 339 ? -2.213  100.550 103.466 1.00 92.88 ? 339  PHE A CA  1 
ATOM   2379  C  C   . PHE A 1 339 ? -1.317  99.549  104.211 1.00 90.73 ? 339  PHE A C   1 
ATOM   2380  O  O   . PHE A 1 339 ? -0.630  98.701  103.636 1.00 89.41 ? 339  PHE A O   1 
ATOM   2381  C  CB  . PHE A 1 339 ? -2.595  100.105 102.032 1.00 94.41 ? 339  PHE A CB  1 
ATOM   2382  C  CG  . PHE A 1 339 ? -1.492  99.439  101.251 1.00 94.29 ? 339  PHE A CG  1 
ATOM   2383  C  CD1 . PHE A 1 339 ? -0.241  100.022 101.137 1.00 95.28 ? 339  PHE A CD1 1 
ATOM   2384  C  CD2 . PHE A 1 339 ? -1.736  98.243  100.581 1.00 93.31 ? 339  PHE A CD2 1 
ATOM   2385  C  CE1 . PHE A 1 339 ? 0.744   99.422  100.370 1.00 96.78 ? 339  PHE A CE1 1 
ATOM   2386  C  CE2 . PHE A 1 339 ? -0.761  97.640  99.815  1.00 93.23 ? 339  PHE A CE2 1 
ATOM   2387  C  CZ  . PHE A 1 339 ? 0.480   98.227  99.705  1.00 96.14 ? 339  PHE A CZ  1 
ATOM   2388  N  N   . LYS A 1 340 ? -1.324  99.711  105.530 1.00 88.53 ? 340  LYS A N   1 
ATOM   2389  C  CA  . LYS A 1 340 ? -0.579  98.868  106.440 1.00 86.47 ? 340  LYS A CA  1 
ATOM   2390  C  C   . LYS A 1 340 ? -1.538  97.761  106.851 1.00 86.76 ? 340  LYS A C   1 
ATOM   2391  O  O   . LYS A 1 340 ? -2.641  97.653  106.311 1.00 87.58 ? 340  LYS A O   1 
ATOM   2392  C  CB  . LYS A 1 340 ? -0.162  99.665  107.672 1.00 86.51 ? 340  LYS A CB  1 
ATOM   2393  C  CG  . LYS A 1 340 ? -1.259  99.862  108.714 1.00 84.73 ? 340  LYS A CG  1 
ATOM   2394  C  CD  . LYS A 1 340 ? -2.333  100.831 108.266 1.00 83.95 ? 340  LYS A CD  1 
ATOM   2395  C  CE  . LYS A 1 340 ? -3.313  101.073 109.401 1.00 84.33 ? 340  LYS A CE  1 
ATOM   2396  N  NZ  . LYS A 1 340 ? -4.388  102.007 109.016 1.00 86.31 ? 340  LYS A NZ  1 
ATOM   2397  N  N   . PHE A 1 341 ? -1.139  96.941  107.813 1.00 85.42 ? 341  PHE A N   1 
ATOM   2398  C  CA  . PHE A 1 341 ? -2.011  95.864  108.237 1.00 82.67 ? 341  PHE A CA  1 
ATOM   2399  C  C   . PHE A 1 341 ? -1.677  95.340  109.622 1.00 82.40 ? 341  PHE A C   1 
ATOM   2400  O  O   . PHE A 1 341 ? -0.691  95.742  110.248 1.00 82.63 ? 341  PHE A O   1 
ATOM   2401  C  CB  . PHE A 1 341 ? -1.953  94.718  107.228 1.00 80.99 ? 341  PHE A CB  1 
ATOM   2402  C  CG  . PHE A 1 341 ? -0.633  94.016  107.187 1.00 81.30 ? 341  PHE A CG  1 
ATOM   2403  C  CD1 . PHE A 1 341 ? 0.537   94.722  106.931 1.00 82.07 ? 341  PHE A CD1 1 
ATOM   2404  C  CD2 . PHE A 1 341 ? -0.557  92.640  107.383 1.00 82.88 ? 341  PHE A CD2 1 
ATOM   2405  C  CE1 . PHE A 1 341 ? 1.770   94.070  106.869 1.00 82.70 ? 341  PHE A CE1 1 
ATOM   2406  C  CE2 . PHE A 1 341 ? 0.671   91.973  107.324 1.00 83.20 ? 341  PHE A CE2 1 
ATOM   2407  C  CZ  . PHE A 1 341 ? 1.837   92.690  107.064 1.00 83.09 ? 341  PHE A CZ  1 
ATOM   2408  N  N   . GLU A 1 342 ? -2.528  94.437  110.090 1.00 81.16 ? 342  GLU A N   1 
ATOM   2409  C  CA  . GLU A 1 342 ? -2.376  93.816  111.386 1.00 78.77 ? 342  GLU A CA  1 
ATOM   2410  C  C   . GLU A 1 342 ? -2.447  92.310  111.182 1.00 78.81 ? 342  GLU A C   1 
ATOM   2411  O  O   . GLU A 1 342 ? -3.104  91.817  110.250 1.00 79.06 ? 342  GLU A O   1 
ATOM   2412  C  CB  . GLU A 1 342 ? -3.485  94.286  112.315 1.00 80.70 ? 342  GLU A CB  1 
ATOM   2413  C  CG  . GLU A 1 342 ? -3.425  95.773  112.620 1.00 86.72 ? 342  GLU A CG  1 
ATOM   2414  C  CD  . GLU A 1 342 ? -4.611  96.248  113.450 1.00 91.85 ? 342  GLU A CD  1 
ATOM   2415  O  OE1 . GLU A 1 342 ? -5.330  95.389  114.011 1.00 94.58 ? 342  GLU A OE1 1 
ATOM   2416  O  OE2 . GLU A 1 342 ? -4.825  97.480  113.552 1.00 94.17 ? 342  GLU A OE2 1 
ATOM   2417  N  N   . THR A 1 343 ? -1.763  91.573  112.045 1.00 76.21 ? 343  THR A N   1 
ATOM   2418  C  CA  . THR A 1 343 ? -1.752  90.134  111.918 1.00 72.65 ? 343  THR A CA  1 
ATOM   2419  C  C   . THR A 1 343 ? -2.116  89.525  113.251 1.00 71.19 ? 343  THR A C   1 
ATOM   2420  O  O   . THR A 1 343 ? -1.729  90.044  114.292 1.00 71.71 ? 343  THR A O   1 
ATOM   2421  C  CB  . THR A 1 343 ? -0.367  89.662  111.463 1.00 72.52 ? 343  THR A CB  1 
ATOM   2422  O  OG1 . THR A 1 343 ? -0.501  88.424  110.770 1.00 76.07 ? 343  THR A OG1 1 
ATOM   2423  C  CG2 . THR A 1 343 ? 0.569   89.481  112.648 1.00 72.69 ? 343  THR A CG2 1 
ATOM   2424  N  N   . THR A 1 344 ? -2.879  88.436  113.226 1.00 69.79 ? 344  THR A N   1 
ATOM   2425  C  CA  . THR A 1 344 ? -3.289  87.769  114.464 1.00 66.37 ? 344  THR A CA  1 
ATOM   2426  C  C   . THR A 1 344 ? -2.860  86.293  114.475 1.00 63.95 ? 344  THR A C   1 
ATOM   2427  O  O   . THR A 1 344 ? -3.014  85.582  113.480 1.00 62.17 ? 344  THR A O   1 
ATOM   2428  C  CB  . THR A 1 344 ? -4.827  87.901  114.692 1.00 65.64 ? 344  THR A CB  1 
ATOM   2429  O  OG1 . THR A 1 344 ? -5.225  87.079  115.797 1.00 63.58 ? 344  THR A OG1 1 
ATOM   2430  C  CG2 . THR A 1 344 ? -5.592  87.483  113.457 1.00 68.35 ? 344  THR A CG2 1 
ATOM   2431  N  N   . MET A 1 345 ? -2.312  85.855  115.613 1.00 61.58 ? 345  MET A N   1 
ATOM   2432  C  CA  . MET A 1 345 ? -1.807  84.490  115.802 1.00 59.37 ? 345  MET A CA  1 
ATOM   2433  C  C   . MET A 1 345 ? -2.848  83.411  116.055 1.00 57.64 ? 345  MET A C   1 
ATOM   2434  O  O   . MET A 1 345 ? -3.758  83.582  116.860 1.00 57.04 ? 345  MET A O   1 
ATOM   2435  C  CB  . MET A 1 345 ? -0.822  84.450  116.965 1.00 58.57 ? 345  MET A CB  1 
ATOM   2436  C  CG  . MET A 1 345 ? 0.603   84.179  116.578 1.00 62.89 ? 345  MET A CG  1 
ATOM   2437  S  SD  . MET A 1 345 ? 0.788   82.667  115.651 1.00 62.78 ? 345  MET A SD  1 
ATOM   2438  C  CE  . MET A 1 345 ? 2.413   82.899  114.963 1.00 60.68 ? 345  MET A CE  1 
ATOM   2439  N  N   . THR A 1 346 ? -2.675  82.275  115.388 1.00 55.58 ? 346  THR A N   1 
ATOM   2440  C  CA  . THR A 1 346 ? -3.595  81.146  115.540 1.00 52.90 ? 346  THR A CA  1 
ATOM   2441  C  C   . THR A 1 346 ? -2.871  79.789  115.448 1.00 49.48 ? 346  THR A C   1 
ATOM   2442  O  O   . THR A 1 346 ? -1.668  79.717  115.206 1.00 46.39 ? 346  THR A O   1 
ATOM   2443  C  CB  . THR A 1 346 ? -4.667  81.180  114.441 1.00 51.12 ? 346  THR A CB  1 
ATOM   2444  O  OG1 . THR A 1 346 ? -4.034  80.944  113.183 1.00 52.18 ? 346  THR A OG1 1 
ATOM   2445  C  CG2 . THR A 1 346 ? -5.354  82.544  114.392 1.00 51.05 ? 346  THR A CG2 1 
ATOM   2446  N  N   . SER A 1 347 ? -3.618  78.708  115.630 1.00 49.88 ? 347  SER A N   1 
ATOM   2447  C  CA  . SER A 1 347 ? -3.052  77.363  115.547 1.00 48.31 ? 347  SER A CA  1 
ATOM   2448  C  C   . SER A 1 347 ? -2.366  77.059  114.204 1.00 47.39 ? 347  SER A C   1 
ATOM   2449  O  O   . SER A 1 347 ? -1.549  76.162  114.143 1.00 48.06 ? 347  SER A O   1 
ATOM   2450  C  CB  . SER A 1 347 ? -4.139  76.318  115.785 1.00 49.68 ? 347  SER A CB  1 
ATOM   2451  O  OG  . SER A 1 347 ? -5.104  76.327  114.736 1.00 47.21 ? 347  SER A OG  1 
ATOM   2452  N  N   . TRP A 1 348 ? -2.698  77.791  113.140 1.00 46.15 ? 348  TRP A N   1 
ATOM   2453  C  CA  . TRP A 1 348 ? -2.096  77.570  111.818 1.00 43.78 ? 348  TRP A CA  1 
ATOM   2454  C  C   . TRP A 1 348 ? -1.016  78.624  111.509 1.00 44.73 ? 348  TRP A C   1 
ATOM   2455  O  O   . TRP A 1 348 ? -0.299  78.533  110.496 1.00 42.02 ? 348  TRP A O   1 
ATOM   2456  C  CB  . TRP A 1 348 ? -3.176  77.613  110.712 1.00 42.71 ? 348  TRP A CB  1 
ATOM   2457  C  CG  . TRP A 1 348 ? -3.854  76.299  110.382 1.00 40.03 ? 348  TRP A CG  1 
ATOM   2458  C  CD1 . TRP A 1 348 ? -5.033  75.807  110.903 1.00 39.15 ? 348  TRP A CD1 1 
ATOM   2459  C  CD2 . TRP A 1 348 ? -3.350  75.280  109.513 1.00 38.06 ? 348  TRP A CD2 1 
ATOM   2460  N  NE1 . TRP A 1 348 ? -5.276  74.545  110.413 1.00 33.94 ? 348  TRP A NE1 1 
ATOM   2461  C  CE2 . TRP A 1 348 ? -4.254  74.198  109.563 1.00 36.61 ? 348  TRP A CE2 1 
ATOM   2462  C  CE3 . TRP A 1 348 ? -2.210  75.168  108.705 1.00 37.09 ? 348  TRP A CE3 1 
ATOM   2463  C  CZ2 . TRP A 1 348 ? -4.044  73.018  108.836 1.00 34.95 ? 348  TRP A CZ2 1 
ATOM   2464  C  CZ3 . TRP A 1 348 ? -2.011  73.987  107.982 1.00 31.25 ? 348  TRP A CZ3 1 
ATOM   2465  C  CH2 . TRP A 1 348 ? -2.918  72.937  108.056 1.00 28.68 ? 348  TRP A CH2 1 
ATOM   2466  N  N   . GLY A 1 349 ? -0.914  79.636  112.370 1.00 44.25 ? 349  GLY A N   1 
ATOM   2467  C  CA  . GLY A 1 349 ? 0.082   80.667  112.157 1.00 43.22 ? 349  GLY A CA  1 
ATOM   2468  C  C   . GLY A 1 349 ? -0.488  82.063  112.054 1.00 46.17 ? 349  GLY A C   1 
ATOM   2469  O  O   . GLY A 1 349 ? -1.575  82.336  112.588 1.00 45.06 ? 349  GLY A O   1 
ATOM   2470  N  N   . LEU A 1 350 ? 0.251   82.950  111.375 1.00 47.52 ? 350  LEU A N   1 
ATOM   2471  C  CA  . LEU A 1 350 ? -0.172  84.344  111.200 1.00 50.97 ? 350  LEU A CA  1 
ATOM   2472  C  C   . LEU A 1 350 ? -1.339  84.534  110.228 1.00 51.48 ? 350  LEU A C   1 
ATOM   2473  O  O   . LEU A 1 350 ? -1.275  84.152  109.057 1.00 52.05 ? 350  LEU A O   1 
ATOM   2474  C  CB  . LEU A 1 350 ? 0.993   85.226  110.725 1.00 51.77 ? 350  LEU A CB  1 
ATOM   2475  C  CG  . LEU A 1 350 ? 2.003   85.764  111.736 1.00 52.42 ? 350  LEU A CG  1 
ATOM   2476  C  CD1 . LEU A 1 350 ? 1.246   86.172  113.029 1.00 51.41 ? 350  LEU A CD1 1 
ATOM   2477  C  CD2 . LEU A 1 350 ? 3.060   84.717  112.011 1.00 53.52 ? 350  LEU A CD2 1 
ATOM   2478  N  N   . VAL A 1 351 ? -2.404  85.131  110.734 1.00 51.93 ? 351  VAL A N   1 
ATOM   2479  C  CA  . VAL A 1 351 ? -3.585  85.422  109.931 1.00 52.76 ? 351  VAL A CA  1 
ATOM   2480  C  C   . VAL A 1 351 ? -3.625  86.926  109.687 1.00 53.62 ? 351  VAL A C   1 
ATOM   2481  O  O   . VAL A 1 351 ? -3.503  87.717  110.637 1.00 51.55 ? 351  VAL A O   1 
ATOM   2482  C  CB  . VAL A 1 351 ? -4.886  85.067  110.680 1.00 50.25 ? 351  VAL A CB  1 
ATOM   2483  C  CG1 . VAL A 1 351 ? -6.065  85.796  110.059 1.00 47.10 ? 351  VAL A CG1 1 
ATOM   2484  C  CG2 . VAL A 1 351 ? -5.110  83.615  110.635 1.00 48.15 ? 351  VAL A CG2 1 
ATOM   2485  N  N   . VAL A 1 352 ? -3.804  87.323  108.433 1.00 54.26 ? 352  VAL A N   1 
ATOM   2486  C  CA  . VAL A 1 352 ? -3.904  88.743  108.142 1.00 54.85 ? 352  VAL A CA  1 
ATOM   2487  C  C   . VAL A 1 352 ? -5.328  89.120  108.547 1.00 56.03 ? 352  VAL A C   1 
ATOM   2488  O  O   . VAL A 1 352 ? -6.299  88.824  107.827 1.00 53.62 ? 352  VAL A O   1 
ATOM   2489  C  CB  . VAL A 1 352 ? -3.723  89.039  106.666 1.00 55.45 ? 352  VAL A CB  1 
ATOM   2490  C  CG1 . VAL A 1 352 ? -3.827  90.539  106.449 1.00 56.50 ? 352  VAL A CG1 1 
ATOM   2491  C  CG2 . VAL A 1 352 ? -2.392  88.511  106.188 1.00 54.28 ? 352  VAL A CG2 1 
ATOM   2492  N  N   . SER A 1 353 ? -5.441  89.766  109.706 1.00 56.77 ? 353  SER A N   1 
ATOM   2493  C  CA  . SER A 1 353 ? -6.730  90.159  110.265 1.00 57.83 ? 353  SER A CA  1 
ATOM   2494  C  C   . SER A 1 353 ? -7.205  91.571  109.922 1.00 61.67 ? 353  SER A C   1 
ATOM   2495  O  O   . SER A 1 353 ? -8.379  91.900  110.112 1.00 63.34 ? 353  SER A O   1 
ATOM   2496  C  CB  . SER A 1 353 ? -6.686  89.988  111.785 1.00 55.20 ? 353  SER A CB  1 
ATOM   2497  O  OG  . SER A 1 353 ? -5.443  90.422  112.329 1.00 53.15 ? 353  SER A OG  1 
ATOM   2498  N  N   . SER A 1 354 ? -6.306  92.412  109.432 1.00 64.58 ? 354  SER A N   1 
ATOM   2499  C  CA  . SER A 1 354 ? -6.701  93.763  109.079 1.00 70.46 ? 354  SER A CA  1 
ATOM   2500  C  C   . SER A 1 354 ? -5.823  94.359  107.982 1.00 74.41 ? 354  SER A C   1 
ATOM   2501  O  O   . SER A 1 354 ? -4.607  94.139  107.949 1.00 74.28 ? 354  SER A O   1 
ATOM   2502  C  CB  . SER A 1 354 ? -6.655  94.652  110.321 1.00 70.68 ? 354  SER A CB  1 
ATOM   2503  O  OG  . SER A 1 354 ? -7.031  95.983  110.022 1.00 73.69 ? 354  SER A OG  1 
ATOM   2504  N  N   . ILE A 1 355 ? -6.453  95.100  107.073 1.00 76.65 ? 355  ILE A N   1 
ATOM   2505  C  CA  . ILE A 1 355 ? -5.732  95.765  105.996 1.00 78.05 ? 355  ILE A CA  1 
ATOM   2506  C  C   . ILE A 1 355 ? -6.297  97.165  105.828 1.00 81.11 ? 355  ILE A C   1 
ATOM   2507  O  O   . ILE A 1 355 ? -7.499  97.339  105.646 1.00 82.14 ? 355  ILE A O   1 
ATOM   2508  C  CB  . ILE A 1 355 ? -5.868  95.038  104.660 1.00 74.91 ? 355  ILE A CB  1 
ATOM   2509  C  CG1 . ILE A 1 355 ? -5.262  93.638  104.757 1.00 72.09 ? 355  ILE A CG1 1 
ATOM   2510  C  CG2 . ILE A 1 355 ? -5.189  95.856  103.575 1.00 74.09 ? 355  ILE A CG2 1 
ATOM   2511  C  CD1 . ILE A 1 355 ? -5.285  92.877  103.445 1.00 68.38 ? 355  ILE A CD1 1 
ATOM   2512  N  N   . ASN A 1 356 ? -5.418  98.158  105.892 1.00 83.33 ? 356  ASN A N   1 
ATOM   2513  C  CA  . ASN A 1 356 ? -5.806  99.554  105.751 1.00 84.93 ? 356  ASN A CA  1 
ATOM   2514  C  C   . ASN A 1 356 ? -6.961  99.911  106.677 1.00 85.40 ? 356  ASN A C   1 
ATOM   2515  O  O   . ASN A 1 356 ? -8.012  100.388 106.244 1.00 84.61 ? 356  ASN A O   1 
ATOM   2516  C  CB  . ASN A 1 356 ? -6.169  99.866  104.297 1.00 86.67 ? 356  ASN A CB  1 
ATOM   2517  C  CG  . ASN A 1 356 ? -6.139  101.348 104.005 1.00 88.81 ? 356  ASN A CG  1 
ATOM   2518  O  OD1 . ASN A 1 356 ? -5.197  102.048 104.389 1.00 91.37 ? 356  ASN A OD1 1 
ATOM   2519  N  ND2 . ASN A 1 356 ? -7.162  101.837 103.325 1.00 88.42 ? 356  ASN A ND2 1 
ATOM   2520  N  N   . ASN A 1 357 ? -6.742  99.642  107.961 1.00 86.68 ? 357  ASN A N   1 
ATOM   2521  C  CA  . ASN A 1 357 ? -7.689  99.929  109.029 1.00 86.43 ? 357  ASN A CA  1 
ATOM   2522  C  C   . ASN A 1 357 ? -9.094  99.325  108.949 1.00 86.15 ? 357  ASN A C   1 
ATOM   2523  O  O   . ASN A 1 357 ? -10.078 99.969  109.318 1.00 87.09 ? 357  ASN A O   1 
ATOM   2524  C  CB  . ASN A 1 357 ? -7.780  101.442 109.218 1.00 87.96 ? 357  ASN A CB  1 
ATOM   2525  C  CG  . ASN A 1 357 ? -7.342  101.874 110.605 1.00 90.30 ? 357  ASN A CG  1 
ATOM   2526  O  OD1 . ASN A 1 357 ? -8.028  101.593 111.593 1.00 92.31 ? 357  ASN A OD1 1 
ATOM   2527  N  ND2 . ASN A 1 357 ? -6.193  102.542 110.693 1.00 88.79 ? 357  ASN A ND2 1 
ATOM   2528  N  N   . ILE A 1 358 ? -9.186  98.083  108.484 1.00 84.67 ? 358  ILE A N   1 
ATOM   2529  C  CA  . ILE A 1 358 ? -10.466 97.383  108.396 1.00 81.61 ? 358  ILE A CA  1 
ATOM   2530  C  C   . ILE A 1 358 ? -10.258 95.902  108.743 1.00 79.59 ? 358  ILE A C   1 
ATOM   2531  O  O   . ILE A 1 358 ? -9.704  95.121  107.965 1.00 77.68 ? 358  ILE A O   1 
ATOM   2532  C  CB  . ILE A 1 358 ? -11.109 97.551  106.994 1.00 81.29 ? 358  ILE A CB  1 
ATOM   2533  C  CG1 . ILE A 1 358 ? -11.837 96.263  106.593 1.00 81.87 ? 358  ILE A CG1 1 
ATOM   2534  C  CG2 . ILE A 1 358 ? -10.065 98.002  105.996 1.00 79.28 ? 358  ILE A CG2 1 
ATOM   2535  C  CD1 . ILE A 1 358 ? -12.385 96.269  105.184 1.00 82.84 ? 358  ILE A CD1 1 
ATOM   2536  N  N   . ALA A 1 359 ? -10.711 95.540  109.937 1.00 77.98 ? 359  ALA A N   1 
ATOM   2537  C  CA  . ALA A 1 359 ? -10.567 94.190  110.473 1.00 77.11 ? 359  ALA A CA  1 
ATOM   2538  C  C   . ALA A 1 359 ? -11.595 93.160  110.005 1.00 75.73 ? 359  ALA A C   1 
ATOM   2539  O  O   . ALA A 1 359 ? -12.661 93.502  109.483 1.00 73.25 ? 359  ALA A O   1 
ATOM   2540  C  CB  . ALA A 1 359 ? -10.563 94.252  111.999 1.00 76.99 ? 359  ALA A CB  1 
ATOM   2541  N  N   . GLU A 1 360 ? -11.263 91.890  110.232 1.00 74.99 ? 360  GLU A N   1 
ATOM   2542  C  CA  . GLU A 1 360 ? -12.118 90.785  109.834 1.00 75.14 ? 360  GLU A CA  1 
ATOM   2543  C  C   . GLU A 1 360 ? -13.502 90.727  110.493 1.00 73.97 ? 360  GLU A C   1 
ATOM   2544  O  O   . GLU A 1 360 ? -14.510 90.657  109.793 1.00 75.30 ? 360  GLU A O   1 
ATOM   2545  C  CB  . GLU A 1 360 ? -11.379 89.456  110.036 1.00 74.15 ? 360  GLU A CB  1 
ATOM   2546  C  CG  . GLU A 1 360 ? -10.707 89.316  111.389 1.00 76.25 ? 360  GLU A CG  1 
ATOM   2547  C  CD  . GLU A 1 360 ? -9.799  88.089  111.476 1.00 79.08 ? 360  GLU A CD  1 
ATOM   2548  O  OE1 . GLU A 1 360 ? -9.543  87.460  110.419 1.00 76.99 ? 360  GLU A OE1 1 
ATOM   2549  O  OE2 . GLU A 1 360 ? -9.332  87.765  112.601 1.00 78.97 ? 360  GLU A OE2 1 
ATOM   2550  N  N   . ASN A 1 361 ? -13.569 90.769  111.816 1.00 70.95 ? 361  ASN A N   1 
ATOM   2551  C  CA  . ASN A 1 361 ? -14.861 90.677  112.509 1.00 72.17 ? 361  ASN A CA  1 
ATOM   2552  C  C   . ASN A 1 361 ? -15.724 89.461  112.084 1.00 70.92 ? 361  ASN A C   1 
ATOM   2553  O  O   . ASN A 1 361 ? -16.449 89.482  111.080 1.00 67.76 ? 361  ASN A O   1 
ATOM   2554  C  CB  . ASN A 1 361 ? -15.667 91.969  112.336 1.00 73.55 ? 361  ASN A CB  1 
ATOM   2555  C  CG  . ASN A 1 361 ? -16.950 91.970  113.160 1.00 73.13 ? 361  ASN A CG  1 
ATOM   2556  O  OD1 . ASN A 1 361 ? -17.717 92.929  113.132 1.00 77.83 ? 361  ASN A OD1 1 
ATOM   2557  N  ND2 . ASN A 1 361 ? -17.183 90.893  113.897 1.00 71.41 ? 361  ASN A ND2 1 
ATOM   2558  N  N   . VAL A 1 362 ? -15.655 88.411  112.892 1.00 71.73 ? 362  VAL A N   1 
ATOM   2559  C  CA  . VAL A 1 362 ? -16.377 87.170  112.634 1.00 73.67 ? 362  VAL A CA  1 
ATOM   2560  C  C   . VAL A 1 362 ? -17.898 87.297  112.813 1.00 74.67 ? 362  VAL A C   1 
ATOM   2561  O  O   . VAL A 1 362 ? -18.660 86.427  112.391 1.00 73.80 ? 362  VAL A O   1 
ATOM   2562  C  CB  . VAL A 1 362 ? -15.833 86.040  113.551 1.00 73.46 ? 362  VAL A CB  1 
ATOM   2563  C  CG1 . VAL A 1 362 ? -16.467 86.146  114.932 1.00 73.37 ? 362  VAL A CG1 1 
ATOM   2564  C  CG2 . VAL A 1 362 ? -16.075 84.676  112.921 1.00 74.05 ? 362  VAL A CG2 1 
ATOM   2565  N  N   . ASN A 1 363 ? -18.342 88.373  113.448 1.00 76.20 ? 363  ASN A N   1 
ATOM   2566  C  CA  . ASN A 1 363 ? -19.776 88.579  113.634 1.00 77.67 ? 363  ASN A CA  1 
ATOM   2567  C  C   . ASN A 1 363 ? -20.422 88.815  112.276 1.00 77.01 ? 363  ASN A C   1 
ATOM   2568  O  O   . ASN A 1 363 ? -21.554 88.413  112.041 1.00 76.20 ? 363  ASN A O   1 
ATOM   2569  C  CB  . ASN A 1 363 ? -20.031 89.784  114.544 1.00 80.94 ? 363  ASN A CB  1 
ATOM   2570  C  CG  . ASN A 1 363 ? -19.751 89.478  116.009 1.00 82.52 ? 363  ASN A CG  1 
ATOM   2571  O  OD1 . ASN A 1 363 ? -19.270 90.338  116.763 1.00 83.85 ? 363  ASN A OD1 1 
ATOM   2572  N  ND2 . ASN A 1 363 ? -20.062 88.251  116.423 1.00 79.91 ? 363  ASN A ND2 1 
ATOM   2573  N  N   . HIS A 1 364 ? -19.680 89.455  111.382 1.00 76.75 ? 364  HIS A N   1 
ATOM   2574  C  CA  . HIS A 1 364 ? -20.177 89.756  110.050 1.00 77.52 ? 364  HIS A CA  1 
ATOM   2575  C  C   . HIS A 1 364 ? -19.753 88.708  109.037 1.00 75.56 ? 364  HIS A C   1 
ATOM   2576  O  O   . HIS A 1 364 ? -19.883 88.933  107.830 1.00 73.23 ? 364  HIS A O   1 
ATOM   2577  C  CB  . HIS A 1 364 ? -19.673 91.137  109.618 1.00 82.37 ? 364  HIS A CB  1 
ATOM   2578  C  CG  . HIS A 1 364 ? -20.115 92.248  110.523 1.00 86.38 ? 364  HIS A CG  1 
ATOM   2579  N  ND1 . HIS A 1 364 ? -19.561 93.510  110.478 1.00 88.23 ? 364  HIS A ND1 1 
ATOM   2580  C  CD2 . HIS A 1 364 ? -21.056 92.282  111.498 1.00 87.09 ? 364  HIS A CD2 1 
ATOM   2581  C  CE1 . HIS A 1 364 ? -20.142 94.274  111.390 1.00 88.71 ? 364  HIS A CE1 1 
ATOM   2582  N  NE2 . HIS A 1 364 ? -21.051 93.553  112.022 1.00 87.98 ? 364  HIS A NE2 1 
ATOM   2583  N  N   . LYS A 1 365 ? -19.263 87.567  109.540 1.00 74.22 ? 365  LYS A N   1 
ATOM   2584  C  CA  . LYS A 1 365 ? -18.797 86.452  108.702 1.00 69.90 ? 365  LYS A CA  1 
ATOM   2585  C  C   . LYS A 1 365 ? -17.937 87.048  107.610 1.00 67.02 ? 365  LYS A C   1 
ATOM   2586  O  O   . LYS A 1 365 ? -18.009 86.636  106.452 1.00 65.09 ? 365  LYS A O   1 
ATOM   2587  C  CB  . LYS A 1 365 ? -19.977 85.714  108.052 1.00 71.33 ? 365  LYS A CB  1 
ATOM   2588  C  CG  . LYS A 1 365 ? -20.190 84.256  108.477 1.00 72.86 ? 365  LYS A CG  1 
ATOM   2589  C  CD  . LYS A 1 365 ? -20.851 84.139  109.837 1.00 78.97 ? 365  LYS A CD  1 
ATOM   2590  C  CE  . LYS A 1 365 ? -21.093 82.675  110.238 1.00 82.00 ? 365  LYS A CE  1 
ATOM   2591  N  NZ  . LYS A 1 365 ? -22.121 81.963  109.400 1.00 82.73 ? 365  LYS A NZ  1 
ATOM   2592  N  N   . THR A 1 366 ? -17.111 88.016  107.983 1.00 66.24 ? 366  THR A N   1 
ATOM   2593  C  CA  . THR A 1 366 ? -16.293 88.686  106.995 1.00 66.14 ? 366  THR A CA  1 
ATOM   2594  C  C   . THR A 1 366 ? -14.787 88.599  107.269 1.00 63.63 ? 366  THR A C   1 
ATOM   2595  O  O   . THR A 1 366 ? -14.357 88.654  108.413 1.00 64.04 ? 366  THR A O   1 
ATOM   2596  C  CB  . THR A 1 366 ? -16.782 90.156  106.876 1.00 65.51 ? 366  THR A CB  1 
ATOM   2597  O  OG1 . THR A 1 366 ? -16.243 90.749  105.695 1.00 72.80 ? 366  THR A OG1 1 
ATOM   2598  C  CG2 . THR A 1 366 ? -16.371 90.959  108.075 1.00 61.19 ? 366  THR A CG2 1 
ATOM   2599  N  N   . TYR A 1 367 ? -13.992 88.442  106.209 1.00 61.83 ? 367  TYR A N   1 
ATOM   2600  C  CA  . TYR A 1 367 ? -12.528 88.336  106.334 1.00 59.09 ? 367  TYR A CA  1 
ATOM   2601  C  C   . TYR A 1 367 ? -11.784 88.707  105.036 1.00 58.66 ? 367  TYR A C   1 
ATOM   2602  O  O   . TYR A 1 367 ? -12.394 89.022  104.006 1.00 57.00 ? 367  TYR A O   1 
ATOM   2603  C  CB  . TYR A 1 367 ? -12.139 86.901  106.679 1.00 55.72 ? 367  TYR A CB  1 
ATOM   2604  C  CG  . TYR A 1 367 ? -12.273 85.982  105.479 1.00 54.32 ? 367  TYR A CG  1 
ATOM   2605  C  CD1 . TYR A 1 367 ? -13.515 85.797  104.842 1.00 53.41 ? 367  TYR A CD1 1 
ATOM   2606  C  CD2 . TYR A 1 367 ? -11.157 85.319  104.953 1.00 51.59 ? 367  TYR A CD2 1 
ATOM   2607  C  CE1 . TYR A 1 367 ? -13.640 84.964  103.705 1.00 49.87 ? 367  TYR A CE1 1 
ATOM   2608  C  CE2 . TYR A 1 367 ? -11.270 84.490  103.814 1.00 50.08 ? 367  TYR A CE2 1 
ATOM   2609  C  CZ  . TYR A 1 367 ? -12.512 84.317  103.201 1.00 50.03 ? 367  TYR A CZ  1 
ATOM   2610  O  OH  . TYR A 1 367 ? -12.613 83.493  102.089 1.00 49.10 ? 367  TYR A OH  1 
ATOM   2611  N  N   . TRP A 1 368 ? -10.459 88.642  105.096 1.00 56.33 ? 368  TRP A N   1 
ATOM   2612  C  CA  . TRP A 1 368 ? -9.637  88.929  103.936 1.00 58.47 ? 368  TRP A CA  1 
ATOM   2613  C  C   . TRP A 1 368 ? -9.216  87.640  103.218 1.00 57.86 ? 368  TRP A C   1 
ATOM   2614  O  O   . TRP A 1 368 ? -8.461  86.838  103.773 1.00 57.79 ? 368  TRP A O   1 
ATOM   2615  C  CB  . TRP A 1 368 ? -8.382  89.703  104.351 1.00 59.80 ? 368  TRP A CB  1 
ATOM   2616  C  CG  . TRP A 1 368 ? -8.646  91.085  104.797 1.00 64.32 ? 368  TRP A CG  1 
ATOM   2617  C  CD1 . TRP A 1 368 ? -8.810  91.523  106.084 1.00 66.38 ? 368  TRP A CD1 1 
ATOM   2618  C  CD2 . TRP A 1 368 ? -8.792  92.233  103.957 1.00 66.57 ? 368  TRP A CD2 1 
ATOM   2619  N  NE1 . TRP A 1 368 ? -9.048  92.880  106.095 1.00 66.30 ? 368  TRP A NE1 1 
ATOM   2620  C  CE2 . TRP A 1 368 ? -9.046  93.341  104.804 1.00 66.98 ? 368  TRP A CE2 1 
ATOM   2621  C  CE3 . TRP A 1 368 ? -8.741  92.435  102.568 1.00 66.45 ? 368  TRP A CE3 1 
ATOM   2622  C  CZ2 . TRP A 1 368 ? -9.243  94.637  104.304 1.00 67.65 ? 368  TRP A CZ2 1 
ATOM   2623  C  CZ3 . TRP A 1 368 ? -8.938  93.726  102.071 1.00 65.01 ? 368  TRP A CZ3 1 
ATOM   2624  C  CH2 . TRP A 1 368 ? -9.188  94.807  102.939 1.00 66.99 ? 368  TRP A CH2 1 
ATOM   2625  N  N   . GLN A 1 369 ? -9.689  87.438  101.990 1.00 57.08 ? 369  GLN A N   1 
ATOM   2626  C  CA  . GLN A 1 369 ? -9.313  86.234  101.239 1.00 57.46 ? 369  GLN A CA  1 
ATOM   2627  C  C   . GLN A 1 369 ? -8.193  86.519  100.255 1.00 56.93 ? 369  GLN A C   1 
ATOM   2628  O  O   . GLN A 1 369 ? -8.260  87.473  99.489  1.00 58.92 ? 369  GLN A O   1 
ATOM   2629  C  CB  . GLN A 1 369 ? -10.507 85.649  100.471 1.00 56.56 ? 369  GLN A CB  1 
ATOM   2630  C  CG  . GLN A 1 369 ? -10.158 84.414  99.670  1.00 56.39 ? 369  GLN A CG  1 
ATOM   2631  C  CD  . GLN A 1 369 ? -11.356 83.770  99.000  1.00 59.54 ? 369  GLN A CD  1 
ATOM   2632  O  OE1 . GLN A 1 369 ? -11.279 82.627  98.562  1.00 64.86 ? 369  GLN A OE1 1 
ATOM   2633  N  NE2 . GLN A 1 369 ? -12.460 84.497  98.906  1.00 57.89 ? 369  GLN A NE2 1 
ATOM   2634  N  N   . PHE A 1 370 ? -7.160  85.686  100.283 1.00 56.43 ? 370  PHE A N   1 
ATOM   2635  C  CA  . PHE A 1 370 ? -6.036  85.838  99.378  1.00 56.19 ? 370  PHE A CA  1 
ATOM   2636  C  C   . PHE A 1 370 ? -6.166  84.933  98.159  1.00 57.54 ? 370  PHE A C   1 
ATOM   2637  O  O   . PHE A 1 370 ? -6.730  83.839  98.224  1.00 56.73 ? 370  PHE A O   1 
ATOM   2638  C  CB  . PHE A 1 370 ? -4.723  85.560  100.108 1.00 54.93 ? 370  PHE A CB  1 
ATOM   2639  C  CG  . PHE A 1 370 ? -4.326  86.645  101.056 1.00 51.71 ? 370  PHE A CG  1 
ATOM   2640  C  CD1 . PHE A 1 370 ? -5.045  86.872  102.213 1.00 53.24 ? 370  PHE A CD1 1 
ATOM   2641  C  CD2 . PHE A 1 370 ? -3.251  87.469  100.773 1.00 53.25 ? 370  PHE A CD2 1 
ATOM   2642  C  CE1 . PHE A 1 370 ? -4.699  87.925  103.090 1.00 54.27 ? 370  PHE A CE1 1 
ATOM   2643  C  CE2 . PHE A 1 370 ? -2.899  88.514  101.634 1.00 52.50 ? 370  PHE A CE2 1 
ATOM   2644  C  CZ  . PHE A 1 370 ? -3.626  88.743  102.794 1.00 53.00 ? 370  PHE A CZ  1 
ATOM   2645  N  N   . LEU A 1 371 ? -5.659  85.411  97.031  1.00 61.38 ? 371  LEU A N   1 
ATOM   2646  C  CA  . LEU A 1 371 ? -5.723  84.640  95.801  1.00 64.95 ? 371  LEU A CA  1 
ATOM   2647  C  C   . LEU A 1 371 ? -4.682  85.071  94.799  1.00 65.44 ? 371  LEU A C   1 
ATOM   2648  O  O   . LEU A 1 371 ? -4.247  86.226  94.788  1.00 65.82 ? 371  LEU A O   1 
ATOM   2649  C  CB  . LEU A 1 371 ? -7.133  84.708  95.177  1.00 66.72 ? 371  LEU A CB  1 
ATOM   2650  C  CG  . LEU A 1 371 ? -7.897  86.009  94.913  1.00 67.81 ? 371  LEU A CG  1 
ATOM   2651  C  CD1 . LEU A 1 371 ? -9.328  85.655  94.499  1.00 70.10 ? 371  LEU A CD1 1 
ATOM   2652  C  CD2 . LEU A 1 371 ? -7.938  86.872  96.154  1.00 70.19 ? 371  LEU A CD2 1 
ATOM   2653  N  N   . SER A 1 372 ? -4.259  84.095  94.001  1.00 67.42 ? 372  SER A N   1 
ATOM   2654  C  CA  . SER A 1 372 ? -3.278  84.259  92.932  1.00 67.76 ? 372  SER A CA  1 
ATOM   2655  C  C   . SER A 1 372 ? -4.140  84.395  91.678  1.00 70.13 ? 372  SER A C   1 
ATOM   2656  O  O   . SER A 1 372 ? -4.788  83.430  91.235  1.00 68.18 ? 372  SER A O   1 
ATOM   2657  C  CB  . SER A 1 372 ? -2.385  83.013  92.836  1.00 66.63 ? 372  SER A CB  1 
ATOM   2658  O  OG  . SER A 1 372 ? -1.486  83.090  91.748  1.00 62.52 ? 372  SER A OG  1 
ATOM   2659  N  N   . GLY A 1 373 ? -4.160  85.600  91.117  1.00 70.31 ? 373  GLY A N   1 
ATOM   2660  C  CA  . GLY A 1 373 ? -4.990  85.808  89.960  1.00 71.99 ? 373  GLY A CA  1 
ATOM   2661  C  C   . GLY A 1 373 ? -6.413  85.768  90.468  1.00 72.54 ? 373  GLY A C   1 
ATOM   2662  O  O   . GLY A 1 373 ? -6.853  86.701  91.144  1.00 72.63 ? 373  GLY A O   1 
ATOM   2663  N  N   . VAL A 1 374 ? -7.122  84.680  90.186  1.00 72.74 ? 374  VAL A N   1 
ATOM   2664  C  CA  . VAL A 1 374 ? -8.508  84.567  90.625  1.00 75.49 ? 374  VAL A CA  1 
ATOM   2665  C  C   . VAL A 1 374 ? -8.747  83.414  91.623  1.00 76.63 ? 374  VAL A C   1 
ATOM   2666  O  O   . VAL A 1 374 ? -9.751  83.412  92.360  1.00 77.39 ? 374  VAL A O   1 
ATOM   2667  C  CB  . VAL A 1 374 ? -9.452  84.386  89.401  1.00 74.68 ? 374  VAL A CB  1 
ATOM   2668  C  CG1 . VAL A 1 374 ? -9.309  82.970  88.829  1.00 73.86 ? 374  VAL A CG1 1 
ATOM   2669  C  CG2 . VAL A 1 374 ? -10.898 84.677  89.801  1.00 75.43 ? 374  VAL A CG2 1 
ATOM   2670  N  N   . THR A 1 375 ? -7.823  82.450  91.648  1.00 74.32 ? 375  THR A N   1 
ATOM   2671  C  CA  . THR A 1 375 ? -7.934  81.286  92.531  1.00 70.87 ? 375  THR A CA  1 
ATOM   2672  C  C   . THR A 1 375 ? -7.356  81.533  93.935  1.00 66.64 ? 375  THR A C   1 
ATOM   2673  O  O   . THR A 1 375 ? -6.259  82.080  94.087  1.00 66.93 ? 375  THR A O   1 
ATOM   2674  C  CB  . THR A 1 375 ? -7.240  80.062  91.898  1.00 72.31 ? 375  THR A CB  1 
ATOM   2675  O  OG1 . THR A 1 375 ? -5.842  80.332  91.759  1.00 72.87 ? 375  THR A OG1 1 
ATOM   2676  C  CG2 . THR A 1 375 ? -7.841  79.756  90.510  1.00 70.94 ? 375  THR A CG2 1 
ATOM   2677  N  N   . PRO A 1 376 ? -8.094  81.125  94.985  1.00 61.75 ? 376  PRO A N   1 
ATOM   2678  C  CA  . PRO A 1 376 ? -7.658  81.309  96.372  1.00 57.88 ? 376  PRO A CA  1 
ATOM   2679  C  C   . PRO A 1 376 ? -6.431  80.495  96.758  1.00 55.90 ? 376  PRO A C   1 
ATOM   2680  O  O   . PRO A 1 376 ? -6.288  79.332  96.362  1.00 52.91 ? 376  PRO A O   1 
ATOM   2681  C  CB  . PRO A 1 376 ? -8.883  80.883  97.182  1.00 55.80 ? 376  PRO A CB  1 
ATOM   2682  C  CG  . PRO A 1 376 ? -10.018 81.062  96.237  1.00 59.32 ? 376  PRO A CG  1 
ATOM   2683  C  CD  . PRO A 1 376 ? -9.440  80.534  94.954  1.00 60.11 ? 376  PRO A CD  1 
ATOM   2684  N  N   . LEU A 1 377 ? -5.553  81.110  97.544  1.00 53.52 ? 377  LEU A N   1 
ATOM   2685  C  CA  . LEU A 1 377 ? -4.355  80.437  98.024  1.00 54.61 ? 377  LEU A CA  1 
ATOM   2686  C  C   . LEU A 1 377 ? -4.679  79.256  98.983  1.00 56.75 ? 377  LEU A C   1 
ATOM   2687  O  O   . LEU A 1 377 ? -5.685  79.268  99.724  1.00 52.95 ? 377  LEU A O   1 
ATOM   2688  C  CB  . LEU A 1 377 ? -3.459  81.462  98.726  1.00 55.60 ? 377  LEU A CB  1 
ATOM   2689  C  CG  . LEU A 1 377 ? -2.341  82.144  97.933  1.00 56.35 ? 377  LEU A CG  1 
ATOM   2690  C  CD1 . LEU A 1 377 ? -2.775  82.453  96.508  1.00 58.93 ? 377  LEU A CD1 1 
ATOM   2691  C  CD2 . LEU A 1 377 ? -1.954  83.414  98.649  1.00 57.42 ? 377  LEU A CD2 1 
ATOM   2692  N  N   . ASN A 1 378 ? -3.831  78.233  98.960  1.00 56.92 ? 378  ASN A N   1 
ATOM   2693  C  CA  . ASN A 1 378 ? -4.037  77.082  99.827  1.00 59.57 ? 378  ASN A CA  1 
ATOM   2694  C  C   . ASN A 1 378 ? -3.086  77.143  101.022 1.00 59.02 ? 378  ASN A C   1 
ATOM   2695  O  O   . ASN A 1 378 ? -2.969  76.172  101.755 1.00 59.18 ? 378  ASN A O   1 
ATOM   2696  C  CB  . ASN A 1 378 ? -3.814  75.780  99.050  1.00 62.85 ? 378  ASN A CB  1 
ATOM   2697  C  CG  . ASN A 1 378 ? -2.351  75.561  98.682  1.00 70.55 ? 378  ASN A CG  1 
ATOM   2698  O  OD1 . ASN A 1 378 ? -1.647  76.491  98.257  1.00 73.65 ? 378  ASN A OD1 1 
ATOM   2699  N  ND2 . ASN A 1 378 ? -1.886  74.321  98.835  1.00 72.30 ? 378  ASN A ND2 1 
ATOM   2700  N  N   . GLU A 1 379 ? -2.414  78.280  101.211 1.00 57.27 ? 379  GLU A N   1 
ATOM   2701  C  CA  . GLU A 1 379 ? -1.465  78.464  102.320 1.00 57.83 ? 379  GLU A CA  1 
ATOM   2702  C  C   . GLU A 1 379 ? -1.546  79.884  102.863 1.00 57.28 ? 379  GLU A C   1 
ATOM   2703  O  O   . GLU A 1 379 ? -1.995  80.781  102.177 1.00 57.67 ? 379  GLU A O   1 
ATOM   2704  C  CB  . GLU A 1 379 ? -0.026  78.211  101.855 1.00 59.55 ? 379  GLU A CB  1 
ATOM   2705  C  CG  . GLU A 1 379 ? 0.351   76.753  101.714 1.00 66.18 ? 379  GLU A CG  1 
ATOM   2706  C  CD  . GLU A 1 379 ? 1.798   76.561  101.267 1.00 69.34 ? 379  GLU A CD  1 
ATOM   2707  O  OE1 . GLU A 1 379 ? 2.069   76.640  100.040 1.00 72.67 ? 379  GLU A OE1 1 
ATOM   2708  O  OE2 . GLU A 1 379 ? 2.664   76.338  102.147 1.00 66.61 ? 379  GLU A OE2 1 
ATOM   2709  N  N   . GLY A 1 380 ? -1.108  80.093  104.096 1.00 57.44 ? 380  GLY A N   1 
ATOM   2710  C  CA  . GLY A 1 380 ? -1.150  81.430  104.661 1.00 56.38 ? 380  GLY A CA  1 
ATOM   2711  C  C   . GLY A 1 380 ? -0.001  82.289  104.178 1.00 56.87 ? 380  GLY A C   1 
ATOM   2712  O  O   . GLY A 1 380 ? 0.894   81.796  103.499 1.00 56.59 ? 380  GLY A O   1 
ATOM   2713  N  N   . VAL A 1 381 ? -0.015  83.568  104.547 1.00 58.19 ? 381  VAL A N   1 
ATOM   2714  C  CA  . VAL A 1 381 ? 1.020   84.512  104.122 1.00 57.91 ? 381  VAL A CA  1 
ATOM   2715  C  C   . VAL A 1 381 ? 2.415   84.206  104.655 1.00 59.26 ? 381  VAL A C   1 
ATOM   2716  O  O   . VAL A 1 381 ? 3.403   84.634  104.082 1.00 61.32 ? 381  VAL A O   1 
ATOM   2717  C  CB  . VAL A 1 381 ? 0.664   85.946  104.525 1.00 56.68 ? 381  VAL A CB  1 
ATOM   2718  C  CG1 . VAL A 1 381 ? -0.701  86.316  103.962 1.00 54.93 ? 381  VAL A CG1 1 
ATOM   2719  C  CG2 . VAL A 1 381 ? 0.689   86.074  106.034 1.00 56.74 ? 381  VAL A CG2 1 
ATOM   2720  N  N   . ALA A 1 382 ? 2.517   83.469  105.749 1.00 59.93 ? 382  ALA A N   1 
ATOM   2721  C  CA  . ALA A 1 382 ? 3.838   83.157  106.256 1.00 57.12 ? 382  ALA A CA  1 
ATOM   2722  C  C   . ALA A 1 382 ? 4.354   81.868  105.646 1.00 57.21 ? 382  ALA A C   1 
ATOM   2723  O  O   . ALA A 1 382 ? 5.498   81.489  105.902 1.00 62.72 ? 382  ALA A O   1 
ATOM   2724  C  CB  . ALA A 1 382 ? 3.805   83.046  107.773 1.00 56.99 ? 382  ALA A CB  1 
ATOM   2725  N  N   . ASP A 1 383 ? 3.535   81.199  104.837 1.00 54.04 ? 383  ASP A N   1 
ATOM   2726  C  CA  . ASP A 1 383 ? 3.948   79.934  104.234 1.00 55.47 ? 383  ASP A CA  1 
ATOM   2727  C  C   . ASP A 1 383 ? 4.104   79.985  102.713 1.00 58.21 ? 383  ASP A C   1 
ATOM   2728  O  O   . ASP A 1 383 ? 4.973   79.325  102.131 1.00 57.40 ? 383  ASP A O   1 
ATOM   2729  C  CB  . ASP A 1 383 ? 2.932   78.833  104.575 1.00 54.12 ? 383  ASP A CB  1 
ATOM   2730  C  CG  . ASP A 1 383 ? 3.161   78.193  105.947 1.00 54.78 ? 383  ASP A CG  1 
ATOM   2731  O  OD1 . ASP A 1 383 ? 3.966   78.702  106.751 1.00 47.26 ? 383  ASP A OD1 1 
ATOM   2732  O  OD2 . ASP A 1 383 ? 2.500   77.161  106.218 1.00 60.47 ? 383  ASP A OD2 1 
ATOM   2733  N  N   . TYR A 1 384 ? 3.238   80.758  102.073 1.00 61.15 ? 384  TYR A N   1 
ATOM   2734  C  CA  . TYR A 1 384 ? 3.230   80.866  100.618 1.00 64.59 ? 384  TYR A CA  1 
ATOM   2735  C  C   . TYR A 1 384 ? 4.460   81.508  99.996  1.00 65.99 ? 384  TYR A C   1 
ATOM   2736  O  O   . TYR A 1 384 ? 4.976   82.525  100.474 1.00 66.24 ? 384  TYR A O   1 
ATOM   2737  C  CB  . TYR A 1 384 ? 1.997   81.641  100.155 1.00 64.67 ? 384  TYR A CB  1 
ATOM   2738  C  CG  . TYR A 1 384 ? 1.699   81.472  98.689  1.00 65.69 ? 384  TYR A CG  1 
ATOM   2739  C  CD1 . TYR A 1 384 ? 1.224   80.254  98.199  1.00 67.82 ? 384  TYR A CD1 1 
ATOM   2740  C  CD2 . TYR A 1 384 ? 1.855   82.531  97.795  1.00 64.18 ? 384  TYR A CD2 1 
ATOM   2741  C  CE1 . TYR A 1 384 ? 0.899   80.097  96.854  1.00 69.15 ? 384  TYR A CE1 1 
ATOM   2742  C  CE2 . TYR A 1 384 ? 1.537   82.383  96.446  1.00 63.55 ? 384  TYR A CE2 1 
ATOM   2743  C  CZ  . TYR A 1 384 ? 1.057   81.166  95.985  1.00 66.83 ? 384  TYR A CZ  1 
ATOM   2744  O  OH  . TYR A 1 384 ? 0.712   81.007  94.667  1.00 66.66 ? 384  TYR A OH  1 
ATOM   2745  N  N   . ILE A 1 385 ? 4.911   80.910  98.903  1.00 67.42 ? 385  ILE A N   1 
ATOM   2746  C  CA  . ILE A 1 385 ? 6.068   81.430  98.193  1.00 68.48 ? 385  ILE A CA  1 
ATOM   2747  C  C   . ILE A 1 385 ? 5.694   81.899  96.779  1.00 68.50 ? 385  ILE A C   1 
ATOM   2748  O  O   . ILE A 1 385 ? 5.586   81.090  95.843  1.00 63.21 ? 385  ILE A O   1 
ATOM   2749  C  CB  . ILE A 1 385 ? 7.214   80.370  98.142  1.00 68.21 ? 385  ILE A CB  1 
ATOM   2750  C  CG1 . ILE A 1 385 ? 7.808   80.195  99.548  1.00 63.54 ? 385  ILE A CG1 1 
ATOM   2751  C  CG2 . ILE A 1 385 ? 8.303   80.804  97.153  1.00 65.76 ? 385  ILE A CG2 1 
ATOM   2752  C  CD1 . ILE A 1 385 ? 8.812   79.088  99.643  1.00 60.40 ? 385  ILE A CD1 1 
ATOM   2753  N  N   . PRO A 1 386 ? 5.487   83.227  96.623  1.00 70.21 ? 386  PRO A N   1 
ATOM   2754  C  CA  . PRO A 1 386 ? 5.125   83.917  95.376  1.00 72.52 ? 386  PRO A CA  1 
ATOM   2755  C  C   . PRO A 1 386 ? 6.216   83.781  94.309  1.00 75.97 ? 386  PRO A C   1 
ATOM   2756  O  O   . PRO A 1 386 ? 7.416   83.859  94.625  1.00 75.81 ? 386  PRO A O   1 
ATOM   2757  C  CB  . PRO A 1 386 ? 4.963   85.372  95.810  1.00 71.70 ? 386  PRO A CB  1 
ATOM   2758  C  CG  . PRO A 1 386 ? 4.674   85.284  97.279  1.00 70.36 ? 386  PRO A CG  1 
ATOM   2759  C  CD  . PRO A 1 386 ? 5.579   84.190  97.738  1.00 69.06 ? 386  PRO A CD  1 
ATOM   2760  N  N   . PHE A 1 387 ? 5.800   83.581  93.056  1.00 79.24 ? 387  PHE A N   1 
ATOM   2761  C  CA  . PHE A 1 387 ? 6.748   83.444  91.951  1.00 83.26 ? 387  PHE A CA  1 
ATOM   2762  C  C   . PHE A 1 387 ? 7.030   84.774  91.234  1.00 86.72 ? 387  PHE A C   1 
ATOM   2763  O  O   . PHE A 1 387 ? 6.631   85.848  91.701  1.00 86.74 ? 387  PHE A O   1 
ATOM   2764  C  CB  . PHE A 1 387 ? 6.272   82.384  90.942  1.00 81.83 ? 387  PHE A CB  1 
ATOM   2765  C  CG  . PHE A 1 387 ? 4.883   82.616  90.411  1.00 83.70 ? 387  PHE A CG  1 
ATOM   2766  C  CD1 . PHE A 1 387 ? 4.527   83.840  89.851  1.00 83.25 ? 387  PHE A CD1 1 
ATOM   2767  C  CD2 . PHE A 1 387 ? 3.931   81.597  90.454  1.00 83.42 ? 387  PHE A CD2 1 
ATOM   2768  C  CE1 . PHE A 1 387 ? 3.247   84.042  89.342  1.00 83.39 ? 387  PHE A CE1 1 
ATOM   2769  C  CE2 . PHE A 1 387 ? 2.647   81.790  89.948  1.00 82.24 ? 387  PHE A CE2 1 
ATOM   2770  C  CZ  . PHE A 1 387 ? 2.303   83.012  89.392  1.00 83.41 ? 387  PHE A CZ  1 
ATOM   2771  N  N   . ASN A 1 388 ? 7.729   84.678  90.104  1.00 90.11 ? 388  ASN A N   1 
ATOM   2772  C  CA  . ASN A 1 388 ? 8.142   85.819  89.275  1.00 91.49 ? 388  ASN A CA  1 
ATOM   2773  C  C   . ASN A 1 388 ? 7.347   87.118  89.379  1.00 91.43 ? 388  ASN A C   1 
ATOM   2774  O  O   . ASN A 1 388 ? 7.721   88.028  90.118  1.00 91.15 ? 388  ASN A O   1 
ATOM   2775  C  CB  . ASN A 1 388 ? 8.222   85.383  87.803  1.00 94.10 ? 388  ASN A CB  1 
ATOM   2776  C  CG  . ASN A 1 388 ? 6.984   84.624  87.345  1.00 95.89 ? 388  ASN A CG  1 
ATOM   2777  O  OD1 . ASN A 1 388 ? 5.871   85.148  87.391  1.00 97.66 ? 388  ASN A OD1 1 
ATOM   2778  N  ND2 . ASN A 1 388 ? 7.176   83.380  86.897  1.00 95.40 ? 388  ASN A ND2 1 
ATOM   2779  N  N   . HIS A 1 389 ? 6.276   87.213  88.603  1.00 92.07 ? 389  HIS A N   1 
ATOM   2780  C  CA  . HIS A 1 389 ? 5.423   88.393  88.607  1.00 92.55 ? 389  HIS A CA  1 
ATOM   2781  C  C   . HIS A 1 389 ? 4.006   87.964  88.946  1.00 91.25 ? 389  HIS A C   1 
ATOM   2782  O  O   . HIS A 1 389 ? 3.099   88.086  88.120  1.00 90.42 ? 389  HIS A O   1 
ATOM   2783  C  CB  . HIS A 1 389 ? 5.412   89.069  87.232  1.00 95.92 ? 389  HIS A CB  1 
ATOM   2784  C  CG  . HIS A 1 389 ? 6.771   89.406  86.711  1.00 97.91 ? 389  HIS A CG  1 
ATOM   2785  N  ND1 . HIS A 1 389 ? 7.618   88.457  86.181  1.00 99.45 ? 389  HIS A ND1 1 
ATOM   2786  C  CD2 . HIS A 1 389 ? 7.444   90.579  86.670  1.00 98.46 ? 389  HIS A CD2 1 
ATOM   2787  C  CE1 . HIS A 1 389 ? 8.757   89.030  85.837  1.00 99.45 ? 389  HIS A CE1 1 
ATOM   2788  N  NE2 . HIS A 1 389 ? 8.678   90.318  86.124  1.00 99.45 ? 389  HIS A NE2 1 
ATOM   2789  N  N   . GLU A 1 390 ? 3.819   87.453  90.158  1.00 88.80 ? 390  GLU A N   1 
ATOM   2790  C  CA  . GLU A 1 390 ? 2.503   87.010  90.583  1.00 86.36 ? 390  GLU A CA  1 
ATOM   2791  C  C   . GLU A 1 390 ? 1.600   88.165  91.028  1.00 84.77 ? 390  GLU A C   1 
ATOM   2792  O  O   . GLU A 1 390 ? 2.032   89.076  91.747  1.00 83.97 ? 390  GLU A O   1 
ATOM   2793  C  CB  . GLU A 1 390 ? 2.643   86.003  91.706  1.00 84.97 ? 390  GLU A CB  1 
ATOM   2794  N  N   . HIS A 1 391 ? 0.347   88.123  90.581  1.00 81.91 ? 391  HIS A N   1 
ATOM   2795  C  CA  . HIS A 1 391 ? -0.630  89.131  90.961  1.00 80.31 ? 391  HIS A CA  1 
ATOM   2796  C  C   . HIS A 1 391 ? -1.473  88.538  92.103  1.00 80.78 ? 391  HIS A C   1 
ATOM   2797  O  O   . HIS A 1 391 ? -2.430  87.770  91.894  1.00 78.60 ? 391  HIS A O   1 
ATOM   2798  C  CB  . HIS A 1 391 ? -1.524  89.504  89.777  1.00 78.24 ? 391  HIS A CB  1 
ATOM   2799  C  CG  . HIS A 1 391 ? -2.499  90.599  90.081  1.00 77.06 ? 391  HIS A CG  1 
ATOM   2800  N  ND1 . HIS A 1 391 ? -3.663  90.782  89.364  1.00 75.24 ? 391  HIS A ND1 1 
ATOM   2801  C  CD2 . HIS A 1 391 ? -2.493  91.554  91.043  1.00 76.19 ? 391  HIS A CD2 1 
ATOM   2802  C  CE1 . HIS A 1 391 ? -4.335  91.800  89.874  1.00 75.23 ? 391  HIS A CE1 1 
ATOM   2803  N  NE2 . HIS A 1 391 ? -3.647  92.286  90.893  1.00 74.94 ? 391  HIS A NE2 1 
ATOM   2804  N  N   . ILE A 1 392 ? -1.089  88.904  93.317  1.00 81.10 ? 392  ILE A N   1 
ATOM   2805  C  CA  . ILE A 1 392 ? -1.755  88.430  94.512  1.00 82.36 ? 392  ILE A CA  1 
ATOM   2806  C  C   . ILE A 1 392 ? -2.704  89.503  95.045  1.00 83.11 ? 392  ILE A C   1 
ATOM   2807  O  O   . ILE A 1 392 ? -2.280  90.599  95.415  1.00 83.17 ? 392  ILE A O   1 
ATOM   2808  C  CB  . ILE A 1 392 ? -0.692  88.035  95.554  1.00 80.61 ? 392  ILE A CB  1 
ATOM   2809  C  CG1 . ILE A 1 392 ? 0.147   86.894  94.979  1.00 79.08 ? 392  ILE A CG1 1 
ATOM   2810  C  CG2 . ILE A 1 392 ? -1.341  87.596  96.843  1.00 80.59 ? 392  ILE A CG2 1 
ATOM   2811  C  CD1 . ILE A 1 392 ? 1.336   86.549  95.798  1.00 80.36 ? 392  ILE A CD1 1 
ATOM   2812  N  N   . THR A 1 393 ? -3.990  89.165  95.076  1.00 83.42 ? 393  THR A N   1 
ATOM   2813  C  CA  . THR A 1 393 ? -5.050  90.070  95.523  1.00 84.23 ? 393  THR A CA  1 
ATOM   2814  C  C   . THR A 1 393 ? -5.579  89.761  96.931  1.00 83.94 ? 393  THR A C   1 
ATOM   2815  O  O   . THR A 1 393 ? -5.539  88.623  97.369  1.00 85.72 ? 393  THR A O   1 
ATOM   2816  C  CB  . THR A 1 393 ? -6.248  90.004  94.549  1.00 83.29 ? 393  THR A CB  1 
ATOM   2817  O  OG1 . THR A 1 393 ? -5.777  90.069  93.195  1.00 83.34 ? 393  THR A OG1 1 
ATOM   2818  C  CG2 . THR A 1 393 ? -7.201  91.140  94.811  1.00 83.55 ? 393  THR A CG2 1 
ATOM   2819  N  N   . ALA A 1 394 ? -6.087  90.781  97.620  1.00 82.78 ? 394  ALA A N   1 
ATOM   2820  C  CA  . ALA A 1 394 ? -6.631  90.629  98.973  1.00 80.41 ? 394  ALA A CA  1 
ATOM   2821  C  C   . ALA A 1 394 ? -8.048  91.180  99.077  1.00 80.08 ? 394  ALA A C   1 
ATOM   2822  O  O   . ALA A 1 394 ? -8.273  92.234  99.671  1.00 79.04 ? 394  ALA A O   1 
ATOM   2823  C  CB  . ALA A 1 394 ? -5.717  91.329  99.985  1.00 78.78 ? 394  ALA A CB  1 
ATOM   2824  N  N   . ASN A 1 395 ? -8.997  90.460  98.489  1.00 79.54 ? 395  ASN A N   1 
ATOM   2825  C  CA  . ASN A 1 395 ? -10.411 90.858  98.486  1.00 78.30 ? 395  ASN A CA  1 
ATOM   2826  C  C   . ASN A 1 395 ? -11.067 90.666  99.877  1.00 75.55 ? 395  ASN A C   1 
ATOM   2827  O  O   . ASN A 1 395 ? -10.955 89.566  100.480 1.00 74.15 ? 395  ASN A O   1 
ATOM   2828  C  CB  . ASN A 1 395 ? -11.137 89.986  97.453  1.00 82.37 ? 395  ASN A CB  1 
ATOM   2829  C  CG  . ASN A 1 395 ? -12.557 90.407  97.056  1.00 86.69 ? 395  ASN A CG  1 
ATOM   2830  O  OD1 . ASN A 1 395 ? -12.964 91.541  97.251  1.00 89.86 ? 395  ASN A OD1 1 
ATOM   2831  N  ND2 . ASN A 1 395 ? -13.302 89.438  96.499  1.00 91.03 ? 395  ASN A ND2 1 
ATOM   2832  N  N   . PHE A 1 396 ? -11.715 91.711  100.400 1.00 72.83 ? 396  PHE A N   1 
ATOM   2833  C  CA  . PHE A 1 396 ? -12.374 91.602  101.697 1.00 69.73 ? 396  PHE A CA  1 
ATOM   2834  C  C   . PHE A 1 396 ? -13.788 91.078  101.436 1.00 68.72 ? 396  PHE A C   1 
ATOM   2835  O  O   . PHE A 1 396 ? -14.726 91.856  101.258 1.00 68.61 ? 396  PHE A O   1 
ATOM   2836  C  CB  . PHE A 1 396 ? -12.447 92.976  102.342 1.00 70.60 ? 396  PHE A CB  1 
ATOM   2837  C  CG  . PHE A 1 396 ? -12.978 92.966  103.759 1.00 73.25 ? 396  PHE A CG  1 
ATOM   2838  C  CD1 . PHE A 1 396 ? -12.184 92.497  104.806 1.00 75.41 ? 396  PHE A CD1 1 
ATOM   2839  C  CD2 . PHE A 1 396 ? -14.280 93.389  104.054 1.00 72.93 ? 396  PHE A CD2 1 
ATOM   2840  C  CE1 . PHE A 1 396 ? -12.668 92.441  106.132 1.00 73.72 ? 396  PHE A CE1 1 
ATOM   2841  C  CE2 . PHE A 1 396 ? -14.774 93.336  105.383 1.00 74.10 ? 396  PHE A CE2 1 
ATOM   2842  C  CZ  . PHE A 1 396 ? -13.956 92.857  106.420 1.00 73.89 ? 396  PHE A CZ  1 
ATOM   2843  N  N   . THR A 1 397 ? -13.932 89.760  101.414 1.00 66.89 ? 397  THR A N   1 
ATOM   2844  C  CA  . THR A 1 397 ? -15.207 89.124  101.142 1.00 64.44 ? 397  THR A CA  1 
ATOM   2845  C  C   . THR A 1 397 ? -15.849 88.556  102.417 1.00 63.45 ? 397  THR A C   1 
ATOM   2846  O  O   . THR A 1 397 ? -15.436 88.847  103.534 1.00 60.73 ? 397  THR A O   1 
ATOM   2847  C  CB  . THR A 1 397 ? -14.982 87.997  100.106 1.00 64.54 ? 397  THR A CB  1 
ATOM   2848  O  OG1 . THR A 1 397 ? -16.228 87.373  99.772  1.00 63.55 ? 397  THR A OG1 1 
ATOM   2849  C  CG2 . THR A 1 397 ? -14.002 86.951  100.671 1.00 65.17 ? 397  THR A CG2 1 
ATOM   2850  N  N   . GLN A 1 398 ? -16.877 87.746  102.234 1.00 65.46 ? 398  GLN A N   1 
ATOM   2851  C  CA  . GLN A 1 398 ? -17.556 87.100  103.347 1.00 68.07 ? 398  GLN A CA  1 
ATOM   2852  C  C   . GLN A 1 398 ? -17.497 85.617  103.041 1.00 67.35 ? 398  GLN A C   1 
ATOM   2853  O  O   . GLN A 1 398 ? -17.159 85.204  101.919 1.00 66.72 ? 398  GLN A O   1 
ATOM   2854  C  CB  . GLN A 1 398 ? -19.018 87.550  103.448 1.00 72.44 ? 398  GLN A CB  1 
ATOM   2855  C  CG  . GLN A 1 398 ? -19.213 89.039  103.767 1.00 78.09 ? 398  GLN A CG  1 
ATOM   2856  C  CD  . GLN A 1 398 ? -20.678 89.399  104.004 1.00 80.94 ? 398  GLN A CD  1 
ATOM   2857  O  OE1 . GLN A 1 398 ? -21.273 89.005  105.015 1.00 83.33 ? 398  GLN A OE1 1 
ATOM   2858  N  NE2 . GLN A 1 398 ? -21.268 90.140  103.068 1.00 80.76 ? 398  GLN A NE2 1 
ATOM   2859  N  N   . TYR A 1 399 ? -17.820 84.807  104.035 1.00 66.43 ? 399  TYR A N   1 
ATOM   2860  C  CA  . TYR A 1 399 ? -17.786 83.369  103.838 1.00 66.27 ? 399  TYR A CA  1 
ATOM   2861  C  C   . TYR A 1 399 ? -19.076 82.746  104.315 1.00 67.77 ? 399  TYR A C   1 
ATOM   2862  O  O   . TYR A 1 399 ? -19.314 81.564  104.000 1.00 69.86 ? 399  TYR A O   1 
ATOM   2863  C  CB  . TYR A 1 399 ? -16.593 82.771  104.577 1.00 61.82 ? 399  TYR A CB  1 
ATOM   2864  C  CG  . TYR A 1 399 ? -16.569 83.063  106.054 1.00 57.73 ? 399  TYR A CG  1 
ATOM   2865  C  CD1 . TYR A 1 399 ? -17.366 82.339  106.947 1.00 55.94 ? 399  TYR A CD1 1 
ATOM   2866  C  CD2 . TYR A 1 399 ? -15.732 84.056  106.568 1.00 57.43 ? 399  TYR A CD2 1 
ATOM   2867  C  CE1 . TYR A 1 399 ? -17.323 82.599  108.321 1.00 56.12 ? 399  TYR A CE1 1 
ATOM   2868  C  CE2 . TYR A 1 399 ? -15.678 84.327  107.932 1.00 56.23 ? 399  TYR A CE2 1 
ATOM   2869  C  CZ  . TYR A 1 399 ? -16.473 83.599  108.802 1.00 56.88 ? 399  TYR A CZ  1 
ATOM   2870  O  OH  . TYR A 1 399 ? -16.411 83.899  110.142 1.00 57.73 ? 399  TYR A OH  1 
ATOM   2871  O  OXT . TYR A 1 399 ? -19.833 83.460  105.002 1.00 72.50 ? 399  TYR A OXT 1 
ATOM   2872  N  N   . SER B 1 7   ? -3.983  34.215  120.464 1.00 95.46 ? 7    SER B N   1 
ATOM   2873  C  CA  . SER B 1 7   ? -3.266  32.978  120.910 1.00 94.89 ? 7    SER B CA  1 
ATOM   2874  C  C   . SER B 1 7   ? -4.217  32.035  121.647 1.00 95.10 ? 7    SER B C   1 
ATOM   2875  O  O   . SER B 1 7   ? -4.913  31.243  121.010 1.00 95.82 ? 7    SER B O   1 
ATOM   2876  C  CB  . SER B 1 7   ? -2.087  33.339  121.820 1.00 95.00 ? 7    SER B CB  1 
ATOM   2877  O  OG  . SER B 1 7   ? -1.386  32.178  122.241 1.00 94.20 ? 7    SER B OG  1 
ATOM   2878  N  N   . CYS B 1 8   ? -4.265  32.128  122.976 1.00 92.90 ? 8    CYS B N   1 
ATOM   2879  C  CA  . CYS B 1 8   ? -5.135  31.254  123.765 1.00 91.31 ? 8    CYS B CA  1 
ATOM   2880  C  C   . CYS B 1 8   ? -6.636  31.452  123.599 1.00 89.40 ? 8    CYS B C   1 
ATOM   2881  O  O   . CYS B 1 8   ? -7.425  30.947  124.399 1.00 88.60 ? 8    CYS B O   1 
ATOM   2882  C  CB  . CYS B 1 8   ? -4.793  31.337  125.254 1.00 92.19 ? 8    CYS B CB  1 
ATOM   2883  S  SG  . CYS B 1 8   ? -4.649  33.005  125.976 1.00 91.21 ? 8    CYS B SG  1 
ATOM   2884  N  N   . SER B 1 9   ? -7.038  32.180  122.569 1.00 86.28 ? 9    SER B N   1 
ATOM   2885  C  CA  . SER B 1 9   ? -8.458  32.370  122.339 1.00 85.02 ? 9    SER B CA  1 
ATOM   2886  C  C   . SER B 1 9   ? -9.154  31.005  122.301 1.00 82.41 ? 9    SER B C   1 
ATOM   2887  O  O   . SER B 1 9   ? -8.522  29.976  122.076 1.00 80.77 ? 9    SER B O   1 
ATOM   2888  C  CB  . SER B 1 9   ? -8.665  33.111  121.025 1.00 85.90 ? 9    SER B CB  1 
ATOM   2889  O  OG  . SER B 1 9   ? -7.841  32.561  120.016 1.00 90.47 ? 9    SER B OG  1 
ATOM   2890  N  N   . VAL B 1 10  ? -10.456 30.995  122.538 1.00 81.63 ? 10   VAL B N   1 
ATOM   2891  C  CA  . VAL B 1 10  ? -11.194 29.745  122.529 1.00 82.09 ? 10   VAL B CA  1 
ATOM   2892  C  C   . VAL B 1 10  ? -11.370 29.262  121.104 1.00 84.68 ? 10   VAL B C   1 
ATOM   2893  O  O   . VAL B 1 10  ? -11.984 29.938  120.276 1.00 84.06 ? 10   VAL B O   1 
ATOM   2894  C  CB  . VAL B 1 10  ? -12.589 29.891  123.186 1.00 79.82 ? 10   VAL B CB  1 
ATOM   2895  C  CG1 . VAL B 1 10  ? -13.419 28.637  122.957 1.00 76.58 ? 10   VAL B CG1 1 
ATOM   2896  C  CG2 . VAL B 1 10  ? -12.429 30.126  124.665 1.00 78.26 ? 10   VAL B CG2 1 
ATOM   2897  N  N   . PRO B 1 11  ? -10.828 28.073  120.802 1.00 86.33 ? 11   PRO B N   1 
ATOM   2898  C  CA  . PRO B 1 11  ? -10.936 27.503  119.462 1.00 87.28 ? 11   PRO B CA  1 
ATOM   2899  C  C   . PRO B 1 11  ? -12.383 27.354  118.998 1.00 88.10 ? 11   PRO B C   1 
ATOM   2900  O  O   . PRO B 1 11  ? -13.152 26.592  119.581 1.00 87.08 ? 11   PRO B O   1 
ATOM   2901  C  CB  . PRO B 1 11  ? -10.224 26.154  119.606 1.00 87.57 ? 11   PRO B CB  1 
ATOM   2902  C  CG  . PRO B 1 11  ? -10.427 25.802  121.047 1.00 87.49 ? 11   PRO B CG  1 
ATOM   2903  C  CD  . PRO B 1 11  ? -10.163 27.126  121.717 1.00 86.89 ? 11   PRO B CD  1 
ATOM   2904  N  N   . SER B 1 12  ? -12.737 28.091  117.946 1.00 89.84 ? 12   SER B N   1 
ATOM   2905  C  CA  . SER B 1 12  ? -14.080 28.054  117.359 1.00 89.54 ? 12   SER B CA  1 
ATOM   2906  C  C   . SER B 1 12  ? -14.453 26.625  116.992 1.00 87.66 ? 12   SER B C   1 
ATOM   2907  O  O   . SER B 1 12  ? -14.286 26.196  115.851 1.00 87.17 ? 12   SER B O   1 
ATOM   2908  C  CB  . SER B 1 12  ? -14.122 28.948  116.117 1.00 91.10 ? 12   SER B CB  1 
ATOM   2909  O  OG  . SER B 1 12  ? -12.832 29.032  115.526 1.00 92.05 ? 12   SER B OG  1 
ATOM   2910  N  N   . ALA B 1 13  ? -14.963 25.904  117.982 1.00 85.79 ? 13   ALA B N   1 
ATOM   2911  C  CA  . ALA B 1 13  ? -15.349 24.503  117.849 1.00 85.90 ? 13   ALA B CA  1 
ATOM   2912  C  C   . ALA B 1 13  ? -15.818 24.147  119.251 1.00 85.41 ? 13   ALA B C   1 
ATOM   2913  O  O   . ALA B 1 13  ? -16.682 23.283  119.448 1.00 82.78 ? 13   ALA B O   1 
ATOM   2914  C  CB  . ALA B 1 13  ? -14.123 23.641  117.460 1.00 83.43 ? 13   ALA B CB  1 
ATOM   2915  N  N   . GLN B 1 14  ? -15.211 24.839  120.217 1.00 84.75 ? 14   GLN B N   1 
ATOM   2916  C  CA  . GLN B 1 14  ? -15.514 24.683  121.631 1.00 82.47 ? 14   GLN B CA  1 
ATOM   2917  C  C   . GLN B 1 14  ? -16.473 25.813  121.981 1.00 80.67 ? 14   GLN B C   1 
ATOM   2918  O  O   . GLN B 1 14  ? -17.132 25.791  123.017 1.00 79.06 ? 14   GLN B O   1 
ATOM   2919  C  CB  . GLN B 1 14  ? -14.230 24.809  122.469 1.00 83.14 ? 14   GLN B CB  1 
ATOM   2920  C  CG  . GLN B 1 14  ? -13.148 23.795  122.130 1.00 86.77 ? 14   GLN B CG  1 
ATOM   2921  C  CD  . GLN B 1 14  ? -13.665 22.360  122.166 1.00 88.60 ? 14   GLN B CD  1 
ATOM   2922  O  OE1 . GLN B 1 14  ? -14.510 21.972  121.359 1.00 90.05 ? 14   GLN B OE1 1 
ATOM   2923  N  NE2 . GLN B 1 14  ? -13.160 21.570  123.108 1.00 86.58 ? 14   GLN B NE2 1 
ATOM   2924  N  N   . GLU B 1 15  ? -16.556 26.794  121.090 1.00 78.74 ? 15   GLU B N   1 
ATOM   2925  C  CA  . GLU B 1 15  ? -17.413 27.941  121.317 1.00 78.80 ? 15   GLU B CA  1 
ATOM   2926  C  C   . GLU B 1 15  ? -18.838 27.595  121.745 1.00 76.50 ? 15   GLU B C   1 
ATOM   2927  O  O   . GLU B 1 15  ? -19.444 28.330  122.517 1.00 78.26 ? 15   GLU B O   1 
ATOM   2928  C  CB  . GLU B 1 15  ? -17.427 28.840  120.083 1.00 81.19 ? 15   GLU B CB  1 
ATOM   2929  C  CG  . GLU B 1 15  ? -16.041 29.345  119.703 1.00 88.15 ? 15   GLU B CG  1 
ATOM   2930  C  CD  . GLU B 1 15  ? -16.072 30.525  118.735 1.00 92.85 ? 15   GLU B CD  1 
ATOM   2931  O  OE1 . GLU B 1 15  ? -16.833 30.466  117.735 1.00 93.01 ? 15   GLU B OE1 1 
ATOM   2932  O  OE2 . GLU B 1 15  ? -15.322 31.505  118.978 1.00 93.70 ? 15   GLU B OE2 1 
ATOM   2933  N  N   . PRO B 1 16  ? -19.400 26.483  121.248 1.00 73.53 ? 16   PRO B N   1 
ATOM   2934  C  CA  . PRO B 1 16  ? -20.774 26.123  121.651 1.00 70.11 ? 16   PRO B CA  1 
ATOM   2935  C  C   . PRO B 1 16  ? -20.838 25.811  123.151 1.00 66.10 ? 16   PRO B C   1 
ATOM   2936  O  O   . PRO B 1 16  ? -21.891 25.892  123.788 1.00 62.93 ? 16   PRO B O   1 
ATOM   2937  C  CB  . PRO B 1 16  ? -21.084 24.905  120.778 1.00 69.87 ? 16   PRO B CB  1 
ATOM   2938  C  CG  . PRO B 1 16  ? -20.277 25.186  119.532 1.00 71.52 ? 16   PRO B CG  1 
ATOM   2939  C  CD  . PRO B 1 16  ? -18.958 25.676  120.096 1.00 72.86 ? 16   PRO B CD  1 
ATOM   2940  N  N   . LEU B 1 17  ? -19.686 25.445  123.696 1.00 62.96 ? 17   LEU B N   1 
ATOM   2941  C  CA  . LEU B 1 17  ? -19.540 25.155  125.117 1.00 60.43 ? 17   LEU B CA  1 
ATOM   2942  C  C   . LEU B 1 17  ? -19.752 26.472  125.898 1.00 59.06 ? 17   LEU B C   1 
ATOM   2943  O  O   . LEU B 1 17  ? -20.504 26.529  126.882 1.00 58.74 ? 17   LEU B O   1 
ATOM   2944  C  CB  . LEU B 1 17  ? -18.129 24.616  125.353 1.00 58.78 ? 17   LEU B CB  1 
ATOM   2945  C  CG  . LEU B 1 17  ? -17.941 23.335  126.156 1.00 59.26 ? 17   LEU B CG  1 
ATOM   2946  C  CD1 . LEU B 1 17  ? -19.139 22.407  125.978 1.00 55.41 ? 17   LEU B CD1 1 
ATOM   2947  C  CD2 . LEU B 1 17  ? -16.635 22.672  125.714 1.00 54.38 ? 17   LEU B CD2 1 
ATOM   2948  N  N   . VAL B 1 18  ? -19.074 27.522  125.432 1.00 57.06 ? 18   VAL B N   1 
ATOM   2949  C  CA  . VAL B 1 18  ? -19.146 28.863  126.012 1.00 52.31 ? 18   VAL B CA  1 
ATOM   2950  C  C   . VAL B 1 18  ? -20.545 29.467  125.859 1.00 51.58 ? 18   VAL B C   1 
ATOM   2951  O  O   . VAL B 1 18  ? -21.101 30.022  126.804 1.00 50.77 ? 18   VAL B O   1 
ATOM   2952  C  CB  . VAL B 1 18  ? -18.135 29.801  125.329 1.00 48.73 ? 18   VAL B CB  1 
ATOM   2953  C  CG1 . VAL B 1 18  ? -18.114 31.135  126.013 1.00 46.17 ? 18   VAL B CG1 1 
ATOM   2954  C  CG2 . VAL B 1 18  ? -16.760 29.171  125.351 1.00 49.93 ? 18   VAL B CG2 1 
ATOM   2955  N  N   . ASN B 1 19  ? -21.113 29.360  124.667 1.00 50.23 ? 19   ASN B N   1 
ATOM   2956  C  CA  . ASN B 1 19  ? -22.431 29.925  124.421 1.00 51.89 ? 19   ASN B CA  1 
ATOM   2957  C  C   . ASN B 1 19  ? -23.428 29.334  125.407 1.00 51.80 ? 19   ASN B C   1 
ATOM   2958  O  O   . ASN B 1 19  ? -24.285 30.035  125.962 1.00 51.33 ? 19   ASN B O   1 
ATOM   2959  C  CB  . ASN B 1 19  ? -22.886 29.629  122.980 1.00 52.10 ? 19   ASN B CB  1 
ATOM   2960  C  CG  . ASN B 1 19  ? -21.927 30.171  121.939 1.00 52.47 ? 19   ASN B CG  1 
ATOM   2961  O  OD1 . ASN B 1 19  ? -21.068 31.011  122.237 1.00 52.62 ? 19   ASN B OD1 1 
ATOM   2962  N  ND2 . ASN B 1 19  ? -22.078 29.705  120.707 1.00 51.36 ? 19   ASN B ND2 1 
ATOM   2963  N  N   . GLY B 1 20  ? -23.310 28.027  125.617 1.00 52.84 ? 20   GLY B N   1 
ATOM   2964  C  CA  . GLY B 1 20  ? -24.214 27.343  126.521 1.00 47.25 ? 20   GLY B CA  1 
ATOM   2965  C  C   . GLY B 1 20  ? -24.270 27.993  127.887 1.00 46.71 ? 20   GLY B C   1 
ATOM   2966  O  O   . GLY B 1 20  ? -25.372 28.252  128.416 1.00 46.59 ? 20   GLY B O   1 
ATOM   2967  N  N   . ILE B 1 21  ? -23.098 28.275  128.465 1.00 43.92 ? 21   ILE B N   1 
ATOM   2968  C  CA  . ILE B 1 21  ? -23.099 28.870  129.783 1.00 42.62 ? 21   ILE B CA  1 
ATOM   2969  C  C   . ILE B 1 21  ? -23.585 30.292  129.724 1.00 42.11 ? 21   ILE B C   1 
ATOM   2970  O  O   . ILE B 1 21  ? -24.250 30.741  130.648 1.00 44.00 ? 21   ILE B O   1 
ATOM   2971  C  CB  . ILE B 1 21  ? -21.734 28.788  130.492 1.00 37.96 ? 21   ILE B CB  1 
ATOM   2972  C  CG1 . ILE B 1 21  ? -20.653 29.561  129.735 1.00 39.34 ? 21   ILE B CG1 1 
ATOM   2973  C  CG2 . ILE B 1 21  ? -21.370 27.343  130.679 1.00 40.19 ? 21   ILE B CG2 1 
ATOM   2974  C  CD1 . ILE B 1 21  ? -19.281 29.528  130.444 1.00 27.97 ? 21   ILE B CD1 1 
ATOM   2975  N  N   . GLN B 1 22  ? -23.298 30.991  128.632 1.00 44.17 ? 22   GLN B N   1 
ATOM   2976  C  CA  . GLN B 1 22  ? -23.767 32.361  128.510 1.00 45.95 ? 22   GLN B CA  1 
ATOM   2977  C  C   . GLN B 1 22  ? -25.279 32.364  128.556 1.00 48.29 ? 22   GLN B C   1 
ATOM   2978  O  O   . GLN B 1 22  ? -25.876 33.286  129.125 1.00 51.29 ? 22   GLN B O   1 
ATOM   2979  C  CB  . GLN B 1 22  ? -23.314 33.003  127.210 1.00 44.42 ? 22   GLN B CB  1 
ATOM   2980  C  CG  . GLN B 1 22  ? -23.931 34.350  126.996 1.00 43.05 ? 22   GLN B CG  1 
ATOM   2981  C  CD  . GLN B 1 22  ? -23.225 35.120  125.923 1.00 45.85 ? 22   GLN B CD  1 
ATOM   2982  O  OE1 . GLN B 1 22  ? -22.150 34.719  125.470 1.00 49.52 ? 22   GLN B OE1 1 
ATOM   2983  N  NE2 . GLN B 1 22  ? -23.811 36.239  125.507 1.00 48.87 ? 22   GLN B NE2 1 
ATOM   2984  N  N   . VAL B 1 23  ? -25.899 31.332  127.981 1.00 46.54 ? 23   VAL B N   1 
ATOM   2985  C  CA  . VAL B 1 23  ? -27.352 31.251  127.986 1.00 45.71 ? 23   VAL B CA  1 
ATOM   2986  C  C   . VAL B 1 23  ? -27.858 30.950  129.392 1.00 44.37 ? 23   VAL B C   1 
ATOM   2987  O  O   . VAL B 1 23  ? -28.868 31.485  129.820 1.00 45.47 ? 23   VAL B O   1 
ATOM   2988  C  CB  . VAL B 1 23  ? -27.876 30.166  126.993 1.00 50.31 ? 23   VAL B CB  1 
ATOM   2989  C  CG1 . VAL B 1 23  ? -29.413 30.068  127.067 1.00 43.81 ? 23   VAL B CG1 1 
ATOM   2990  C  CG2 . VAL B 1 23  ? -27.456 30.526  125.563 1.00 47.98 ? 23   VAL B CG2 1 
ATOM   2991  N  N   . LEU B 1 24  ? -27.172 30.089  130.124 1.00 44.27 ? 24   LEU B N   1 
ATOM   2992  C  CA  . LEU B 1 24  ? -27.618 29.814  131.486 1.00 42.40 ? 24   LEU B CA  1 
ATOM   2993  C  C   . LEU B 1 24  ? -27.589 31.100  132.290 1.00 41.67 ? 24   LEU B C   1 
ATOM   2994  O  O   . LEU B 1 24  ? -28.526 31.397  133.049 1.00 40.19 ? 24   LEU B O   1 
ATOM   2995  C  CB  . LEU B 1 24  ? -26.709 28.791  132.156 1.00 44.54 ? 24   LEU B CB  1 
ATOM   2996  C  CG  . LEU B 1 24  ? -26.817 27.381  131.582 1.00 40.86 ? 24   LEU B CG  1 
ATOM   2997  C  CD1 . LEU B 1 24  ? -25.883 26.465  132.327 1.00 41.17 ? 24   LEU B CD1 1 
ATOM   2998  C  CD2 . LEU B 1 24  ? -28.260 26.905  131.721 1.00 36.53 ? 24   LEU B CD2 1 
ATOM   2999  N  N   . MET B 1 25  ? -26.515 31.872  132.113 1.00 40.33 ? 25   MET B N   1 
ATOM   3000  C  CA  . MET B 1 25  ? -26.352 33.132  132.841 1.00 40.66 ? 25   MET B CA  1 
ATOM   3001  C  C   . MET B 1 25  ? -27.434 34.150  132.482 1.00 42.50 ? 25   MET B C   1 
ATOM   3002  O  O   . MET B 1 25  ? -28.040 34.778  133.357 1.00 38.98 ? 25   MET B O   1 
ATOM   3003  C  CB  . MET B 1 25  ? -24.972 33.717  132.573 1.00 34.89 ? 25   MET B CB  1 
ATOM   3004  C  CG  . MET B 1 25  ? -24.699 34.990  133.323 1.00 38.25 ? 25   MET B CG  1 
ATOM   3005  S  SD  . MET B 1 25  ? -23.191 35.764  132.736 1.00 46.37 ? 25   MET B SD  1 
ATOM   3006  C  CE  . MET B 1 25  ? -23.777 36.538  131.199 1.00 44.36 ? 25   MET B CE  1 
ATOM   3007  N  N   . GLU B 1 26  ? -27.688 34.304  131.187 1.00 47.36 ? 26   GLU B N   1 
ATOM   3008  C  CA  . GLU B 1 26  ? -28.685 35.266  130.741 1.00 47.65 ? 26   GLU B CA  1 
ATOM   3009  C  C   . GLU B 1 26  ? -30.072 34.850  131.193 1.00 48.58 ? 26   GLU B C   1 
ATOM   3010  O  O   . GLU B 1 26  ? -30.875 35.680  131.623 1.00 47.67 ? 26   GLU B O   1 
ATOM   3011  C  CB  . GLU B 1 26  ? -28.624 35.418  129.225 1.00 44.88 ? 26   GLU B CB  1 
ATOM   3012  C  CG  . GLU B 1 26  ? -27.343 36.040  128.729 1.00 44.06 ? 26   GLU B CG  1 
ATOM   3013  C  CD  . GLU B 1 26  ? -27.430 36.454  127.277 1.00 49.92 ? 26   GLU B CD  1 
ATOM   3014  O  OE1 . GLU B 1 26  ? -28.473 36.167  126.653 1.00 52.97 ? 26   GLU B OE1 1 
ATOM   3015  O  OE2 . GLU B 1 26  ? -26.464 37.066  126.754 1.00 48.94 ? 26   GLU B OE2 1 
ATOM   3016  N  N   . ASN B 1 27  ? -30.347 33.553  131.127 1.00 51.78 ? 27   ASN B N   1 
ATOM   3017  C  CA  . ASN B 1 27  ? -31.654 33.045  131.554 1.00 53.34 ? 27   ASN B CA  1 
ATOM   3018  C  C   . ASN B 1 27  ? -32.021 33.422  132.979 1.00 53.20 ? 27   ASN B C   1 
ATOM   3019  O  O   . ASN B 1 27  ? -33.202 33.518  133.307 1.00 53.42 ? 27   ASN B O   1 
ATOM   3020  C  CB  . ASN B 1 27  ? -31.703 31.532  131.457 1.00 52.18 ? 27   ASN B CB  1 
ATOM   3021  C  CG  . ASN B 1 27  ? -31.983 31.044  130.058 1.00 56.09 ? 27   ASN B CG  1 
ATOM   3022  O  OD1 . ASN B 1 27  ? -32.044 29.841  129.834 1.00 59.83 ? 27   ASN B OD1 1 
ATOM   3023  N  ND2 . ASN B 1 27  ? -32.146 31.963  129.106 1.00 56.92 ? 27   ASN B ND2 1 
ATOM   3024  N  N   . SER B 1 28  ? -31.014 33.628  133.822 1.00 53.92 ? 28   SER B N   1 
ATOM   3025  C  CA  . SER B 1 28  ? -31.249 33.955  135.224 1.00 55.49 ? 28   SER B CA  1 
ATOM   3026  C  C   . SER B 1 28  ? -31.740 35.385  135.466 1.00 56.41 ? 28   SER B C   1 
ATOM   3027  O  O   . SER B 1 28  ? -32.206 35.723  136.561 1.00 59.00 ? 28   SER B O   1 
ATOM   3028  C  CB  . SER B 1 28  ? -29.978 33.691  136.044 1.00 55.90 ? 28   SER B CB  1 
ATOM   3029  O  OG  . SER B 1 28  ? -29.075 34.785  135.984 1.00 60.41 ? 28   SER B OG  1 
ATOM   3030  N  N   . VAL B 1 29  ? -31.646 36.225  134.447 1.00 55.13 ? 29   VAL B N   1 
ATOM   3031  C  CA  . VAL B 1 29  ? -32.081 37.599  134.587 1.00 54.24 ? 29   VAL B CA  1 
ATOM   3032  C  C   . VAL B 1 29  ? -33.612 37.633  134.540 1.00 57.83 ? 29   VAL B C   1 
ATOM   3033  O  O   . VAL B 1 29  ? -34.215 37.174  133.564 1.00 62.24 ? 29   VAL B O   1 
ATOM   3034  C  CB  . VAL B 1 29  ? -31.471 38.444  133.447 1.00 51.58 ? 29   VAL B CB  1 
ATOM   3035  C  CG1 . VAL B 1 29  ? -31.843 39.912  133.611 1.00 49.97 ? 29   VAL B CG1 1 
ATOM   3036  C  CG2 . VAL B 1 29  ? -29.975 38.276  133.450 1.00 45.57 ? 29   VAL B CG2 1 
ATOM   3037  N  N   . THR B 1 30  ? -34.251 38.147  135.589 1.00 57.01 ? 30   THR B N   1 
ATOM   3038  C  CA  . THR B 1 30  ? -35.720 38.220  135.620 1.00 57.77 ? 30   THR B CA  1 
ATOM   3039  C  C   . THR B 1 30  ? -36.154 39.361  136.545 1.00 63.03 ? 30   THR B C   1 
ATOM   3040  O  O   . THR B 1 30  ? -35.377 39.826  137.388 1.00 62.73 ? 30   THR B O   1 
ATOM   3041  C  CB  . THR B 1 30  ? -36.379 36.890  136.117 1.00 54.01 ? 30   THR B CB  1 
ATOM   3042  O  OG1 . THR B 1 30  ? -36.084 36.677  137.508 1.00 55.29 ? 30   THR B OG1 1 
ATOM   3043  C  CG2 . THR B 1 30  ? -35.867 35.704  135.320 1.00 52.41 ? 30   THR B CG2 1 
ATOM   3044  N  N   . SER B 1 31  ? -37.394 39.814  136.394 1.00 66.64 ? 31   SER B N   1 
ATOM   3045  C  CA  . SER B 1 31  ? -37.904 40.923  137.212 1.00 71.93 ? 31   SER B CA  1 
ATOM   3046  C  C   . SER B 1 31  ? -37.688 40.756  138.716 1.00 71.15 ? 31   SER B C   1 
ATOM   3047  O  O   . SER B 1 31  ? -37.442 41.726  139.430 1.00 68.82 ? 31   SER B O   1 
ATOM   3048  C  CB  . SER B 1 31  ? -39.395 41.127  136.936 1.00 75.01 ? 31   SER B CB  1 
ATOM   3049  O  OG  . SER B 1 31  ? -39.603 41.353  135.550 1.00 82.41 ? 31   SER B OG  1 
ATOM   3050  N  N   . SER B 1 32  ? -37.780 39.515  139.182 1.00 72.33 ? 32   SER B N   1 
ATOM   3051  C  CA  . SER B 1 32  ? -37.619 39.185  140.600 1.00 72.20 ? 32   SER B CA  1 
ATOM   3052  C  C   . SER B 1 32  ? -36.166 38.862  141.024 1.00 71.27 ? 32   SER B C   1 
ATOM   3053  O  O   . SER B 1 32  ? -35.800 39.034  142.204 1.00 70.01 ? 32   SER B O   1 
ATOM   3054  C  CB  . SER B 1 32  ? -38.552 38.012  140.952 1.00 71.26 ? 32   SER B CB  1 
ATOM   3055  O  OG  . SER B 1 32  ? -38.494 36.999  139.954 1.00 69.88 ? 32   SER B OG  1 
ATOM   3056  N  N   . ALA B 1 33  ? -35.347 38.381  140.086 1.00 67.50 ? 33   ALA B N   1 
ATOM   3057  C  CA  . ALA B 1 33  ? -33.964 38.074  140.416 1.00 65.42 ? 33   ALA B CA  1 
ATOM   3058  C  C   . ALA B 1 33  ? -33.314 39.396  140.828 1.00 67.69 ? 33   ALA B C   1 
ATOM   3059  O  O   . ALA B 1 33  ? -33.607 40.457  140.243 1.00 68.51 ? 33   ALA B O   1 
ATOM   3060  C  CB  . ALA B 1 33  ? -33.240 37.466  139.206 1.00 57.12 ? 33   ALA B CB  1 
ATOM   3061  N  N   . TYR B 1 34  ? -32.470 39.346  141.860 1.00 69.12 ? 34   TYR B N   1 
ATOM   3062  C  CA  . TYR B 1 34  ? -31.749 40.537  142.339 1.00 66.16 ? 34   TYR B CA  1 
ATOM   3063  C  C   . TYR B 1 34  ? -30.703 40.841  141.255 1.00 59.47 ? 34   TYR B C   1 
ATOM   3064  O  O   . TYR B 1 34  ? -29.953 39.957  140.855 1.00 58.13 ? 34   TYR B O   1 
ATOM   3065  C  CB  . TYR B 1 34  ? -31.067 40.234  143.671 1.00 71.47 ? 34   TYR B CB  1 
ATOM   3066  C  CG  . TYR B 1 34  ? -30.401 41.428  144.302 1.00 78.00 ? 34   TYR B CG  1 
ATOM   3067  C  CD1 . TYR B 1 34  ? -31.153 42.501  144.802 1.00 79.13 ? 34   TYR B CD1 1 
ATOM   3068  C  CD2 . TYR B 1 34  ? -29.006 41.486  144.415 1.00 81.74 ? 34   TYR B CD2 1 
ATOM   3069  C  CE1 . TYR B 1 34  ? -30.522 43.609  145.407 1.00 80.63 ? 34   TYR B CE1 1 
ATOM   3070  C  CE2 . TYR B 1 34  ? -28.361 42.585  145.017 1.00 81.99 ? 34   TYR B CE2 1 
ATOM   3071  C  CZ  . TYR B 1 34  ? -29.121 43.640  145.513 1.00 82.74 ? 34   TYR B CZ  1 
ATOM   3072  O  OH  . TYR B 1 34  ? -28.471 44.696  146.132 1.00 83.34 ? 34   TYR B OH  1 
ATOM   3073  N  N   . PRO B 1 35  ? -30.638 42.098  140.786 1.00 54.52 ? 35   PRO B N   1 
ATOM   3074  C  CA  . PRO B 1 35  ? -29.736 42.601  139.739 1.00 51.41 ? 35   PRO B CA  1 
ATOM   3075  C  C   . PRO B 1 35  ? -28.240 42.362  139.947 1.00 51.01 ? 35   PRO B C   1 
ATOM   3076  O  O   . PRO B 1 35  ? -27.625 42.947  140.856 1.00 47.92 ? 35   PRO B O   1 
ATOM   3077  C  CB  . PRO B 1 35  ? -30.052 44.100  139.679 1.00 51.87 ? 35   PRO B CB  1 
ATOM   3078  C  CG  . PRO B 1 35  ? -31.260 44.277  140.544 1.00 53.34 ? 35   PRO B CG  1 
ATOM   3079  C  CD  . PRO B 1 35  ? -31.163 43.221  141.572 1.00 52.24 ? 35   PRO B CD  1 
ATOM   3080  N  N   . ASN B 1 36  ? -27.648 41.523  139.093 1.00 48.25 ? 36   ASN B N   1 
ATOM   3081  C  CA  . ASN B 1 36  ? -26.228 41.234  139.209 1.00 44.45 ? 36   ASN B CA  1 
ATOM   3082  C  C   . ASN B 1 36  ? -25.424 42.006  138.155 1.00 42.55 ? 36   ASN B C   1 
ATOM   3083  O  O   . ASN B 1 36  ? -25.382 41.629  136.975 1.00 41.24 ? 36   ASN B O   1 
ATOM   3084  C  CB  . ASN B 1 36  ? -25.978 39.737  139.091 1.00 42.65 ? 36   ASN B CB  1 
ATOM   3085  C  CG  . ASN B 1 36  ? -24.539 39.372  139.396 1.00 50.05 ? 36   ASN B CG  1 
ATOM   3086  O  OD1 . ASN B 1 36  ? -24.232 38.222  139.731 1.00 48.78 ? 36   ASN B OD1 1 
ATOM   3087  N  ND2 . ASN B 1 36  ? -23.637 40.356  139.278 1.00 52.27 ? 36   ASN B ND2 1 
ATOM   3088  N  N   . PRO B 1 37  ? -24.757 43.097  138.582 1.00 39.67 ? 37   PRO B N   1 
ATOM   3089  C  CA  . PRO B 1 37  ? -23.961 43.914  137.661 1.00 35.39 ? 37   PRO B CA  1 
ATOM   3090  C  C   . PRO B 1 37  ? -22.835 43.141  136.971 1.00 36.17 ? 37   PRO B C   1 
ATOM   3091  O  O   . PRO B 1 37  ? -22.481 43.417  135.820 1.00 37.79 ? 37   PRO B O   1 
ATOM   3092  C  CB  . PRO B 1 37  ? -23.462 45.040  138.556 1.00 33.22 ? 37   PRO B CB  1 
ATOM   3093  C  CG  . PRO B 1 37  ? -23.365 44.395  139.910 1.00 34.78 ? 37   PRO B CG  1 
ATOM   3094  C  CD  . PRO B 1 37  ? -24.608 43.553  139.979 1.00 33.22 ? 37   PRO B CD  1 
ATOM   3095  N  N   . SER B 1 38  ? -22.284 42.151  137.657 1.00 34.40 ? 38   SER B N   1 
ATOM   3096  C  CA  . SER B 1 38  ? -21.218 41.382  137.055 1.00 35.50 ? 38   SER B CA  1 
ATOM   3097  C  C   . SER B 1 38  ? -21.761 40.686  135.826 1.00 36.93 ? 38   SER B C   1 
ATOM   3098  O  O   . SER B 1 38  ? -21.036 40.495  134.854 1.00 35.61 ? 38   SER B O   1 
ATOM   3099  C  CB  . SER B 1 38  ? -20.673 40.340  138.043 1.00 36.77 ? 38   SER B CB  1 
ATOM   3100  O  OG  . SER B 1 38  ? -20.012 40.960  139.135 1.00 38.88 ? 38   SER B OG  1 
ATOM   3101  N  N   . ILE B 1 39  ? -23.037 40.293  135.880 1.00 36.81 ? 39   ILE B N   1 
ATOM   3102  C  CA  . ILE B 1 39  ? -23.647 39.596  134.756 1.00 34.02 ? 39   ILE B CA  1 
ATOM   3103  C  C   . ILE B 1 39  ? -23.813 40.519  133.572 1.00 34.84 ? 39   ILE B C   1 
ATOM   3104  O  O   . ILE B 1 39  ? -23.505 40.153  132.427 1.00 31.06 ? 39   ILE B O   1 
ATOM   3105  C  CB  . ILE B 1 39  ? -25.012 39.023  135.128 1.00 33.31 ? 39   ILE B CB  1 
ATOM   3106  C  CG1 . ILE B 1 39  ? -24.835 37.939  136.199 1.00 32.02 ? 39   ILE B CG1 1 
ATOM   3107  C  CG2 . ILE B 1 39  ? -25.678 38.431  133.893 1.00 30.22 ? 39   ILE B CG2 1 
ATOM   3108  C  CD1 . ILE B 1 39  ? -26.103 37.214  136.563 1.00 20.28 ? 39   ILE B CD1 1 
ATOM   3109  N  N   . LEU B 1 40  ? -24.306 41.719  133.856 1.00 35.06 ? 40   LEU B N   1 
ATOM   3110  C  CA  . LEU B 1 40  ? -24.516 42.690  132.815 1.00 35.52 ? 40   LEU B CA  1 
ATOM   3111  C  C   . LEU B 1 40  ? -23.186 42.973  132.127 1.00 39.75 ? 40   LEU B C   1 
ATOM   3112  O  O   . LEU B 1 40  ? -23.123 43.036  130.890 1.00 39.44 ? 40   LEU B O   1 
ATOM   3113  C  CB  . LEU B 1 40  ? -25.113 43.967  133.388 1.00 33.15 ? 40   LEU B CB  1 
ATOM   3114  C  CG  . LEU B 1 40  ? -25.299 45.045  132.321 1.00 29.42 ? 40   LEU B CG  1 
ATOM   3115  C  CD1 . LEU B 1 40  ? -25.984 44.467  131.115 1.00 29.92 ? 40   LEU B CD1 1 
ATOM   3116  C  CD2 . LEU B 1 40  ? -26.122 46.169  132.877 1.00 31.16 ? 40   LEU B CD2 1 
ATOM   3117  N  N   . ILE B 1 41  ? -22.120 43.122  132.915 1.00 38.51 ? 41   ILE B N   1 
ATOM   3118  C  CA  . ILE B 1 41  ? -20.814 43.374  132.327 1.00 39.29 ? 41   ILE B CA  1 
ATOM   3119  C  C   . ILE B 1 41  ? -20.421 42.181  131.455 1.00 41.52 ? 41   ILE B C   1 
ATOM   3120  O  O   . ILE B 1 41  ? -19.916 42.344  130.346 1.00 42.11 ? 41   ILE B O   1 
ATOM   3121  C  CB  . ILE B 1 41  ? -19.756 43.584  133.420 1.00 41.75 ? 41   ILE B CB  1 
ATOM   3122  C  CG1 . ILE B 1 41  ? -19.962 44.953  134.073 1.00 41.89 ? 41   ILE B CG1 1 
ATOM   3123  C  CG2 . ILE B 1 41  ? -18.342 43.430  132.849 1.00 39.30 ? 41   ILE B CG2 1 
ATOM   3124  C  CD1 . ILE B 1 41  ? -19.161 45.114  135.351 1.00 41.85 ? 41   ILE B CD1 1 
ATOM   3125  N  N   . ALA B 1 42  ? -20.666 40.973  131.948 1.00 42.51 ? 42   ALA B N   1 
ATOM   3126  C  CA  . ALA B 1 42  ? -20.310 39.785  131.183 1.00 43.38 ? 42   ALA B CA  1 
ATOM   3127  C  C   . ALA B 1 42  ? -21.019 39.780  129.822 1.00 43.86 ? 42   ALA B C   1 
ATOM   3128  O  O   . ALA B 1 42  ? -20.364 39.668  128.796 1.00 43.05 ? 42   ALA B O   1 
ATOM   3129  C  CB  . ALA B 1 42  ? -20.647 38.513  131.977 1.00 41.25 ? 42   ALA B CB  1 
ATOM   3130  N  N   . MET B 1 43  ? -22.343 39.923  129.799 1.00 44.49 ? 43   MET B N   1 
ATOM   3131  C  CA  . MET B 1 43  ? -23.024 39.919  128.516 1.00 44.58 ? 43   MET B CA  1 
ATOM   3132  C  C   . MET B 1 43  ? -22.681 41.116  127.611 1.00 44.23 ? 43   MET B C   1 
ATOM   3133  O  O   . MET B 1 43  ? -22.655 40.975  126.389 1.00 43.30 ? 43   MET B O   1 
ATOM   3134  C  CB  . MET B 1 43  ? -24.539 39.761  128.694 1.00 45.39 ? 43   MET B CB  1 
ATOM   3135  C  CG  . MET B 1 43  ? -25.181 40.649  129.719 1.00 51.77 ? 43   MET B CG  1 
ATOM   3136  S  SD  . MET B 1 43  ? -26.845 40.027  130.117 1.00 54.64 ? 43   MET B SD  1 
ATOM   3137  C  CE  . MET B 1 43  ? -27.657 40.398  128.547 1.00 49.26 ? 43   MET B CE  1 
ATOM   3138  N  N   . ASN B 1 44  ? -22.380 42.282  128.172 1.00 41.06 ? 44   ASN B N   1 
ATOM   3139  C  CA  . ASN B 1 44  ? -22.036 43.395  127.292 1.00 38.24 ? 44   ASN B CA  1 
ATOM   3140  C  C   . ASN B 1 44  ? -20.681 43.158  126.658 1.00 37.31 ? 44   ASN B C   1 
ATOM   3141  O  O   . ASN B 1 44  ? -20.463 43.480  125.509 1.00 42.13 ? 44   ASN B O   1 
ATOM   3142  C  CB  . ASN B 1 44  ? -22.036 44.723  128.053 1.00 36.67 ? 44   ASN B CB  1 
ATOM   3143  C  CG  . ASN B 1 44  ? -23.437 45.197  128.364 1.00 38.45 ? 44   ASN B CG  1 
ATOM   3144  O  OD1 . ASN B 1 44  ? -24.391 44.804  127.688 1.00 43.69 ? 44   ASN B OD1 1 
ATOM   3145  N  ND2 . ASN B 1 44  ? -23.575 46.047  129.359 1.00 37.54 ? 44   ASN B ND2 1 
ATOM   3146  N  N   . LEU B 1 45  ? -19.781 42.555  127.411 1.00 37.89 ? 45   LEU B N   1 
ATOM   3147  C  CA  . LEU B 1 45  ? -18.425 42.290  126.945 1.00 40.00 ? 45   LEU B CA  1 
ATOM   3148  C  C   . LEU B 1 45  ? -18.401 41.136  125.955 1.00 43.77 ? 45   LEU B C   1 
ATOM   3149  O  O   . LEU B 1 45  ? -17.472 40.999  125.159 1.00 46.92 ? 45   LEU B O   1 
ATOM   3150  C  CB  . LEU B 1 45  ? -17.551 41.947  128.150 1.00 38.68 ? 45   LEU B CB  1 
ATOM   3151  C  CG  . LEU B 1 45  ? -16.309 42.781  128.479 1.00 43.68 ? 45   LEU B CG  1 
ATOM   3152  C  CD1 . LEU B 1 45  ? -16.496 44.262  128.128 1.00 42.34 ? 45   LEU B CD1 1 
ATOM   3153  C  CD2 . LEU B 1 45  ? -15.994 42.588  129.961 1.00 37.67 ? 45   LEU B CD2 1 
ATOM   3154  N  N   . ALA B 1 46  ? -19.429 40.302  126.008 1.00 43.22 ? 46   ALA B N   1 
ATOM   3155  C  CA  . ALA B 1 46  ? -19.496 39.144  125.144 1.00 43.23 ? 46   ALA B CA  1 
ATOM   3156  C  C   . ALA B 1 46  ? -20.453 39.350  123.969 1.00 43.10 ? 46   ALA B C   1 
ATOM   3157  O  O   . ALA B 1 46  ? -20.410 38.605  122.996 1.00 40.55 ? 46   ALA B O   1 
ATOM   3158  C  CB  . ALA B 1 46  ? -19.941 37.909  125.975 1.00 44.61 ? 46   ALA B CB  1 
ATOM   3159  N  N   . GLY B 1 47  ? -21.312 40.359  124.062 1.00 41.30 ? 47   GLY B N   1 
ATOM   3160  C  CA  . GLY B 1 47  ? -22.273 40.583  123.010 1.00 39.06 ? 47   GLY B CA  1 
ATOM   3161  C  C   . GLY B 1 47  ? -23.429 39.743  123.457 1.00 40.57 ? 47   GLY B C   1 
ATOM   3162  O  O   . GLY B 1 47  ? -23.377 38.531  123.395 1.00 42.48 ? 47   GLY B O   1 
ATOM   3163  N  N   . ALA B 1 48  ? -24.478 40.395  123.922 1.00 44.72 ? 48   ALA B N   1 
ATOM   3164  C  CA  . ALA B 1 48  ? -25.629 39.711  124.473 1.00 46.65 ? 48   ALA B CA  1 
ATOM   3165  C  C   . ALA B 1 48  ? -26.532 38.987  123.490 1.00 49.29 ? 48   ALA B C   1 
ATOM   3166  O  O   . ALA B 1 48  ? -26.704 39.429  122.363 1.00 51.82 ? 48   ALA B O   1 
ATOM   3167  C  CB  . ALA B 1 48  ? -26.439 40.701  125.279 1.00 45.94 ? 48   ALA B CB  1 
ATOM   3168  N  N   . TYR B 1 49  ? -27.115 37.878  123.943 1.00 50.34 ? 49   TYR B N   1 
ATOM   3169  C  CA  . TYR B 1 49  ? -28.043 37.082  123.140 1.00 50.11 ? 49   TYR B CA  1 
ATOM   3170  C  C   . TYR B 1 49  ? -29.481 37.557  123.406 1.00 51.32 ? 49   TYR B C   1 
ATOM   3171  O  O   . TYR B 1 49  ? -30.198 38.013  122.505 1.00 53.33 ? 49   TYR B O   1 
ATOM   3172  C  CB  . TYR B 1 49  ? -27.966 35.602  123.516 1.00 48.06 ? 49   TYR B CB  1 
ATOM   3173  C  CG  . TYR B 1 49  ? -26.655 34.917  123.214 1.00 48.71 ? 49   TYR B CG  1 
ATOM   3174  C  CD1 . TYR B 1 49  ? -25.851 35.342  122.171 1.00 50.18 ? 49   TYR B CD1 1 
ATOM   3175  C  CD2 . TYR B 1 49  ? -26.245 33.793  123.943 1.00 50.31 ? 49   TYR B CD2 1 
ATOM   3176  C  CE1 . TYR B 1 49  ? -24.659 34.667  121.852 1.00 53.43 ? 49   TYR B CE1 1 
ATOM   3177  C  CE2 . TYR B 1 49  ? -25.052 33.105  123.625 1.00 50.64 ? 49   TYR B CE2 1 
ATOM   3178  C  CZ  . TYR B 1 49  ? -24.268 33.556  122.577 1.00 51.23 ? 49   TYR B CZ  1 
ATOM   3179  O  OH  . TYR B 1 49  ? -23.097 32.913  122.247 1.00 53.77 ? 49   TYR B OH  1 
ATOM   3180  N  N   . ASN B 1 50  ? -29.896 37.446  124.657 1.00 48.69 ? 50   ASN B N   1 
ATOM   3181  C  CA  . ASN B 1 50  ? -31.229 37.853  125.053 1.00 47.45 ? 50   ASN B CA  1 
ATOM   3182  C  C   . ASN B 1 50  ? -31.337 39.370  125.270 1.00 50.16 ? 50   ASN B C   1 
ATOM   3183  O  O   . ASN B 1 50  ? -31.132 39.869  126.388 1.00 48.64 ? 50   ASN B O   1 
ATOM   3184  C  CB  . ASN B 1 50  ? -31.590 37.104  126.317 1.00 43.43 ? 50   ASN B CB  1 
ATOM   3185  C  CG  . ASN B 1 50  ? -32.989 37.373  126.767 1.00 45.96 ? 50   ASN B CG  1 
ATOM   3186  O  OD1 . ASN B 1 50  ? -33.549 36.581  127.534 1.00 42.81 ? 50   ASN B OD1 1 
ATOM   3187  N  ND2 . ASN B 1 50  ? -33.577 38.501  126.311 1.00 43.15 ? 50   ASN B ND2 1 
ATOM   3188  N  N   . LEU B 1 51  ? -31.697 40.100  124.212 1.00 51.16 ? 51   LEU B N   1 
ATOM   3189  C  CA  . LEU B 1 51  ? -31.783 41.556  124.309 1.00 50.61 ? 51   LEU B CA  1 
ATOM   3190  C  C   . LEU B 1 51  ? -32.760 42.136  125.324 1.00 49.86 ? 51   LEU B C   1 
ATOM   3191  O  O   . LEU B 1 51  ? -32.555 43.258  125.802 1.00 50.99 ? 51   LEU B O   1 
ATOM   3192  C  CB  . LEU B 1 51  ? -32.062 42.163  122.932 1.00 48.06 ? 51   LEU B CB  1 
ATOM   3193  C  CG  . LEU B 1 51  ? -30.976 41.885  121.895 1.00 49.55 ? 51   LEU B CG  1 
ATOM   3194  C  CD1 . LEU B 1 51  ? -31.065 42.922  120.820 1.00 46.54 ? 51   LEU B CD1 1 
ATOM   3195  C  CD2 . LEU B 1 51  ? -29.580 41.930  122.529 1.00 52.09 ? 51   LEU B CD2 1 
ATOM   3196  N  N   . LYS B 1 52  ? -33.698 41.394  125.668 1.00 50.47 ? 52   LYS B N   1 
ATOM   3197  C  CA  . LYS B 1 52  ? -34.750 41.868  126.598 1.00 51.09 ? 52   LYS B CA  1 
ATOM   3198  C  C   . LYS B 1 52  ? -34.214 41.671  128.013 1.00 49.35 ? 52   LYS B C   1 
ATOM   3199  O  O   . LYS B 1 52  ? -34.573 42.493  128.916 1.00 47.11 ? 52   LYS B O   1 
ATOM   3200  C  CB  . LYS B 1 52  ? -36.016 41.021  126.476 1.00 54.99 ? 52   LYS B CB  1 
ATOM   3201  C  CG  . LYS B 1 52  ? -37.314 41.795  126.532 1.00 60.11 ? 52   LYS B CG  1 
ATOM   3202  C  CD  . LYS B 1 52  ? -38.594 40.802  126.708 1.00 65.42 ? 52   LYS B CD  1 
ATOM   3203  C  CE  . LYS B 1 52  ? -38.911 39.947  125.425 1.00 67.34 ? 52   LYS B CE  1 
ATOM   3204  N  NZ  . LYS B 1 52  ? -40.164 39.011  125.503 1.00 69.03 ? 52   LYS B NZ  1 
ATOM   3205  N  N   . ALA B 1 53  ? -33.453 40.702  128.238 1.00 45.41 ? 53   ALA B N   1 
ATOM   3206  C  CA  . ALA B 1 53  ? -32.817 40.518  129.542 1.00 45.38 ? 53   ALA B CA  1 
ATOM   3207  C  C   . ALA B 1 53  ? -31.793 41.650  129.743 1.00 43.10 ? 53   ALA B C   1 
ATOM   3208  O  O   . ALA B 1 53  ? -31.727 42.272  130.814 1.00 40.07 ? 53   ALA B O   1 
ATOM   3209  C  CB  . ALA B 1 53  ? -32.116 39.165  129.605 1.00 46.74 ? 53   ALA B CB  1 
ATOM   3210  N  N   . GLN B 1 54  ? -31.004 41.919  128.703 1.00 41.69 ? 54   GLN B N   1 
ATOM   3211  C  CA  . GLN B 1 54  ? -30.004 42.974  128.783 1.00 42.20 ? 54   GLN B CA  1 
ATOM   3212  C  C   . GLN B 1 54  ? -30.630 44.306  129.143 1.00 42.87 ? 54   GLN B C   1 
ATOM   3213  O  O   . GLN B 1 54  ? -30.089 45.047  129.962 1.00 44.58 ? 54   GLN B O   1 
ATOM   3214  C  CB  . GLN B 1 54  ? -29.264 43.104  127.462 1.00 41.05 ? 54   GLN B CB  1 
ATOM   3215  C  CG  . GLN B 1 54  ? -28.408 44.320  127.370 1.00 41.49 ? 54   GLN B CG  1 
ATOM   3216  C  CD  . GLN B 1 54  ? -27.790 44.435  126.009 1.00 43.06 ? 54   GLN B CD  1 
ATOM   3217  O  OE1 . GLN B 1 54  ? -26.569 44.385  125.873 1.00 45.48 ? 54   GLN B OE1 1 
ATOM   3218  N  NE2 . GLN B 1 54  ? -28.626 44.580  124.983 1.00 42.78 ? 54   GLN B NE2 1 
ATOM   3219  N  N   . LYS B 1 55  ? -31.773 44.607  128.534 1.00 44.63 ? 55   LYS B N   1 
ATOM   3220  C  CA  . LYS B 1 55  ? -32.461 45.867  128.793 1.00 46.77 ? 55   LYS B CA  1 
ATOM   3221  C  C   . LYS B 1 55  ? -32.988 45.906  130.236 1.00 44.79 ? 55   LYS B C   1 
ATOM   3222  O  O   . LYS B 1 55  ? -32.778 46.870  130.993 1.00 43.66 ? 55   LYS B O   1 
ATOM   3223  C  CB  . LYS B 1 55  ? -33.603 46.054  127.781 1.00 49.64 ? 55   LYS B CB  1 
ATOM   3224  C  CG  . LYS B 1 55  ? -34.414 47.326  128.031 1.00 59.84 ? 55   LYS B CG  1 
ATOM   3225  C  CD  . LYS B 1 55  ? -35.298 47.708  126.849 1.00 64.30 ? 55   LYS B CD  1 
ATOM   3226  C  CE  . LYS B 1 55  ? -36.082 48.988  127.146 1.00 69.59 ? 55   LYS B CE  1 
ATOM   3227  N  NZ  . LYS B 1 55  ? -36.852 49.504  125.949 1.00 72.77 ? 55   LYS B NZ  1 
ATOM   3228  N  N   . LEU B 1 56  ? -33.663 44.835  130.612 1.00 43.70 ? 56   LEU B N   1 
ATOM   3229  C  CA  . LEU B 1 56  ? -34.216 44.711  131.945 1.00 41.28 ? 56   LEU B CA  1 
ATOM   3230  C  C   . LEU B 1 56  ? -33.115 44.893  132.993 1.00 40.04 ? 56   LEU B C   1 
ATOM   3231  O  O   . LEU B 1 56  ? -33.265 45.683  133.921 1.00 40.52 ? 56   LEU B O   1 
ATOM   3232  C  CB  . LEU B 1 56  ? -34.880 43.339  132.087 1.00 42.94 ? 56   LEU B CB  1 
ATOM   3233  C  CG  . LEU B 1 56  ? -35.345 42.981  133.490 1.00 46.69 ? 56   LEU B CG  1 
ATOM   3234  C  CD1 . LEU B 1 56  ? -36.224 44.097  134.037 1.00 49.03 ? 56   LEU B CD1 1 
ATOM   3235  C  CD2 . LEU B 1 56  ? -36.077 41.670  133.457 1.00 46.45 ? 56   LEU B CD2 1 
ATOM   3236  N  N   . LEU B 1 57  ? -32.009 44.169  132.846 1.00 35.35 ? 57   LEU B N   1 
ATOM   3237  C  CA  . LEU B 1 57  ? -30.911 44.298  133.795 1.00 35.53 ? 57   LEU B CA  1 
ATOM   3238  C  C   . LEU B 1 57  ? -30.355 45.721  133.819 1.00 37.11 ? 57   LEU B C   1 
ATOM   3239  O  O   . LEU B 1 57  ? -30.148 46.289  134.892 1.00 38.98 ? 57   LEU B O   1 
ATOM   3240  C  CB  . LEU B 1 57  ? -29.810 43.307  133.466 1.00 33.08 ? 57   LEU B CB  1 
ATOM   3241  C  CG  . LEU B 1 57  ? -28.714 43.152  134.508 1.00 33.28 ? 57   LEU B CG  1 
ATOM   3242  C  CD1 . LEU B 1 57  ? -29.319 43.090  135.894 1.00 34.81 ? 57   LEU B CD1 1 
ATOM   3243  C  CD2 . LEU B 1 57  ? -27.913 41.869  134.204 1.00 34.10 ? 57   LEU B CD2 1 
ATOM   3244  N  N   . THR B 1 58  ? -30.133 46.311  132.648 1.00 37.59 ? 58   THR B N   1 
ATOM   3245  C  CA  . THR B 1 58  ? -29.646 47.690  132.595 1.00 36.67 ? 58   THR B CA  1 
ATOM   3246  C  C   . THR B 1 58  ? -30.581 48.588  133.390 1.00 39.53 ? 58   THR B C   1 
ATOM   3247  O  O   . THR B 1 58  ? -30.143 49.394  134.202 1.00 39.27 ? 58   THR B O   1 
ATOM   3248  C  CB  . THR B 1 58  ? -29.612 48.217  131.154 1.00 33.83 ? 58   THR B CB  1 
ATOM   3249  O  OG1 . THR B 1 58  ? -28.755 47.387  130.383 1.00 29.22 ? 58   THR B OG1 1 
ATOM   3250  C  CG2 . THR B 1 58  ? -29.086 49.669  131.104 1.00 31.32 ? 58   THR B CG2 1 
ATOM   3251  N  N   . TYR B 1 59  ? -31.879 48.445  133.145 1.00 42.81 ? 59   TYR B N   1 
ATOM   3252  C  CA  . TYR B 1 59  ? -32.870 49.259  133.843 1.00 46.84 ? 59   TYR B CA  1 
ATOM   3253  C  C   . TYR B 1 59  ? -32.879 49.013  135.344 1.00 44.42 ? 59   TYR B C   1 
ATOM   3254  O  O   . TYR B 1 59  ? -32.924 49.951  136.115 1.00 43.93 ? 59   TYR B O   1 
ATOM   3255  C  CB  . TYR B 1 59  ? -34.272 49.020  133.252 1.00 54.65 ? 59   TYR B CB  1 
ATOM   3256  C  CG  . TYR B 1 59  ? -34.507 49.738  131.935 1.00 65.59 ? 59   TYR B CG  1 
ATOM   3257  C  CD1 . TYR B 1 59  ? -33.473 49.877  130.994 1.00 70.35 ? 59   TYR B CD1 1 
ATOM   3258  C  CD2 . TYR B 1 59  ? -35.755 50.276  131.620 1.00 69.62 ? 59   TYR B CD2 1 
ATOM   3259  C  CE1 . TYR B 1 59  ? -33.676 50.536  129.777 1.00 72.14 ? 59   TYR B CE1 1 
ATOM   3260  C  CE2 . TYR B 1 59  ? -35.970 50.939  130.398 1.00 73.73 ? 59   TYR B CE2 1 
ATOM   3261  C  CZ  . TYR B 1 59  ? -34.925 51.065  129.486 1.00 73.79 ? 59   TYR B CZ  1 
ATOM   3262  O  OH  . TYR B 1 59  ? -35.131 51.728  128.294 1.00 76.95 ? 59   TYR B OH  1 
ATOM   3263  N  N   . GLN B 1 60  ? -32.846 47.756  135.771 1.00 44.10 ? 60   GLN B N   1 
ATOM   3264  C  CA  . GLN B 1 60  ? -32.844 47.500  137.195 1.00 44.17 ? 60   GLN B CA  1 
ATOM   3265  C  C   . GLN B 1 60  ? -31.610 48.186  137.780 1.00 47.15 ? 60   GLN B C   1 
ATOM   3266  O  O   . GLN B 1 60  ? -31.721 48.899  138.775 1.00 46.63 ? 60   GLN B O   1 
ATOM   3267  C  CB  . GLN B 1 60  ? -32.817 45.996  137.473 1.00 43.19 ? 60   GLN B CB  1 
ATOM   3268  C  CG  . GLN B 1 60  ? -34.030 45.260  136.939 1.00 45.66 ? 60   GLN B CG  1 
ATOM   3269  C  CD  . GLN B 1 60  ? -33.920 43.761  137.108 1.00 47.81 ? 60   GLN B CD  1 
ATOM   3270  O  OE1 . GLN B 1 60  ? -32.910 43.154  136.746 1.00 49.09 ? 60   GLN B OE1 1 
ATOM   3271  N  NE2 . GLN B 1 60  ? -34.968 43.148  137.643 1.00 50.65 ? 60   GLN B NE2 1 
ATOM   3272  N  N   . LEU B 1 61  ? -30.443 47.990  137.157 1.00 47.72 ? 61   LEU B N   1 
ATOM   3273  C  CA  . LEU B 1 61  ? -29.221 48.610  137.648 1.00 47.30 ? 61   LEU B CA  1 
ATOM   3274  C  C   . LEU B 1 61  ? -29.313 50.136  137.734 1.00 47.73 ? 61   LEU B C   1 
ATOM   3275  O  O   . LEU B 1 61  ? -28.795 50.723  138.680 1.00 48.09 ? 61   LEU B O   1 
ATOM   3276  C  CB  . LEU B 1 61  ? -28.029 48.183  136.803 1.00 46.96 ? 61   LEU B CB  1 
ATOM   3277  C  CG  . LEU B 1 61  ? -27.193 47.013  137.330 1.00 47.94 ? 61   LEU B CG  1 
ATOM   3278  C  CD1 . LEU B 1 61  ? -27.796 46.402  138.568 1.00 44.95 ? 61   LEU B CD1 1 
ATOM   3279  C  CD2 . LEU B 1 61  ? -27.057 45.996  136.233 1.00 46.68 ? 61   LEU B CD2 1 
ATOM   3280  N  N   . MET B 1 62  ? -29.935 50.786  136.756 1.00 47.30 ? 62   MET B N   1 
ATOM   3281  C  CA  . MET B 1 62  ? -30.115 52.236  136.840 1.00 52.69 ? 62   MET B CA  1 
ATOM   3282  C  C   . MET B 1 62  ? -31.099 52.370  137.992 1.00 57.92 ? 62   MET B C   1 
ATOM   3283  O  O   . MET B 1 62  ? -31.862 51.447  138.240 1.00 62.10 ? 62   MET B O   1 
ATOM   3284  C  CB  . MET B 1 62  ? -30.781 52.779  135.575 1.00 49.91 ? 62   MET B CB  1 
ATOM   3285  C  CG  . MET B 1 62  ? -29.922 52.759  134.336 1.00 51.19 ? 62   MET B CG  1 
ATOM   3286  S  SD  . MET B 1 62  ? -30.857 52.756  132.760 1.00 55.18 ? 62   MET B SD  1 
ATOM   3287  C  CE  . MET B 1 62  ? -31.655 54.399  132.797 1.00 48.84 ? 62   MET B CE  1 
ATOM   3288  N  N   . SER B 1 63  ? -31.091 53.475  138.719 1.00 64.14 ? 63   SER B N   1 
ATOM   3289  C  CA  . SER B 1 63  ? -32.059 53.643  139.819 1.00 71.93 ? 63   SER B CA  1 
ATOM   3290  C  C   . SER B 1 63  ? -31.842 52.834  141.101 1.00 74.19 ? 63   SER B C   1 
ATOM   3291  O  O   . SER B 1 63  ? -32.525 53.077  142.104 1.00 75.98 ? 63   SER B O   1 
ATOM   3292  C  CB  . SER B 1 63  ? -33.482 53.325  139.329 1.00 72.71 ? 63   SER B CB  1 
ATOM   3293  O  OG  . SER B 1 63  ? -33.806 51.976  139.624 1.00 70.45 ? 63   SER B OG  1 
ATOM   3294  N  N   . SER B 1 64  ? -30.923 51.876  141.081 1.00 76.87 ? 64   SER B N   1 
ATOM   3295  C  CA  . SER B 1 64  ? -30.704 51.052  142.269 1.00 81.28 ? 64   SER B CA  1 
ATOM   3296  C  C   . SER B 1 64  ? -30.159 51.836  143.472 1.00 83.40 ? 64   SER B C   1 
ATOM   3297  O  O   . SER B 1 64  ? -28.938 51.871  143.686 1.00 85.88 ? 64   SER B O   1 
ATOM   3298  C  CB  . SER B 1 64  ? -29.768 49.869  141.947 1.00 79.25 ? 64   SER B CB  1 
ATOM   3299  O  OG  . SER B 1 64  ? -28.482 50.311  141.563 1.00 76.45 ? 64   SER B OG  1 
ATOM   3300  N  N   . ASP B 1 65  ? -31.065 52.446  144.246 1.00 82.06 ? 65   ASP B N   1 
ATOM   3301  C  CA  . ASP B 1 65  ? -30.710 53.221  145.443 1.00 81.55 ? 65   ASP B CA  1 
ATOM   3302  C  C   . ASP B 1 65  ? -29.196 53.169  145.724 1.00 80.94 ? 65   ASP B C   1 
ATOM   3303  O  O   . ASP B 1 65  ? -28.692 52.192  146.282 1.00 79.41 ? 65   ASP B O   1 
ATOM   3304  C  CB  . ASP B 1 65  ? -31.477 52.677  146.664 1.00 82.55 ? 65   ASP B CB  1 
ATOM   3305  C  CG  . ASP B 1 65  ? -31.560 53.685  147.829 1.00 84.28 ? 65   ASP B CG  1 
ATOM   3306  O  OD1 . ASP B 1 65  ? -30.636 54.516  148.003 1.00 84.67 ? 65   ASP B OD1 1 
ATOM   3307  O  OD2 . ASP B 1 65  ? -32.553 53.632  148.589 1.00 82.66 ? 65   ASP B OD2 1 
ATOM   3308  N  N   . ASN B 1 66  ? -28.486 54.229  145.342 1.00 80.49 ? 66   ASN B N   1 
ATOM   3309  C  CA  . ASN B 1 66  ? -27.035 54.319  145.514 1.00 80.78 ? 66   ASN B CA  1 
ATOM   3310  C  C   . ASN B 1 66  ? -26.525 54.237  146.955 1.00 80.39 ? 66   ASN B C   1 
ATOM   3311  O  O   . ASN B 1 66  ? -25.322 54.215  147.193 1.00 77.15 ? 66   ASN B O   1 
ATOM   3312  C  CB  . ASN B 1 66  ? -26.523 55.622  144.898 1.00 82.15 ? 66   ASN B CB  1 
ATOM   3313  C  CG  . ASN B 1 66  ? -27.163 55.935  143.556 1.00 81.83 ? 66   ASN B CG  1 
ATOM   3314  O  OD1 . ASN B 1 66  ? -27.334 55.058  142.711 1.00 82.43 ? 66   ASN B OD1 1 
ATOM   3315  N  ND2 . ASN B 1 66  ? -27.504 57.200  143.351 1.00 82.31 ? 66   ASN B ND2 1 
ATOM   3316  N  N   . ASN B 1 67  ? -27.440 54.194  147.913 1.00 83.85 ? 67   ASN B N   1 
ATOM   3317  C  CA  . ASN B 1 67  ? -27.065 54.140  149.319 1.00 84.89 ? 67   ASN B CA  1 
ATOM   3318  C  C   . ASN B 1 67  ? -27.020 52.723  149.873 1.00 84.44 ? 67   ASN B C   1 
ATOM   3319  O  O   . ASN B 1 67  ? -26.351 52.456  150.875 1.00 84.79 ? 67   ASN B O   1 
ATOM   3320  C  CB  . ASN B 1 67  ? -28.040 54.983  150.153 1.00 87.62 ? 67   ASN B CB  1 
ATOM   3321  C  CG  . ASN B 1 67  ? -27.963 56.469  149.830 1.00 89.01 ? 67   ASN B CG  1 
ATOM   3322  O  OD1 . ASN B 1 67  ? -28.699 57.275  150.404 1.00 89.66 ? 67   ASN B OD1 1 
ATOM   3323  N  ND2 . ASN B 1 67  ? -27.073 56.836  148.911 1.00 90.42 ? 67   ASN B ND2 1 
ATOM   3324  N  N   . ASP B 1 68  ? -27.732 51.809  149.232 1.00 82.62 ? 68   ASP B N   1 
ATOM   3325  C  CA  . ASP B 1 68  ? -27.745 50.439  149.716 1.00 80.96 ? 68   ASP B CA  1 
ATOM   3326  C  C   . ASP B 1 68  ? -26.550 49.688  149.172 1.00 76.70 ? 68   ASP B C   1 
ATOM   3327  O  O   . ASP B 1 68  ? -26.329 48.527  149.528 1.00 80.73 ? 68   ASP B O   1 
ATOM   3328  C  CB  . ASP B 1 68  ? -29.026 49.728  149.273 1.00 84.19 ? 68   ASP B CB  1 
ATOM   3329  C  CG  . ASP B 1 68  ? -30.260 50.571  149.499 1.00 89.06 ? 68   ASP B CG  1 
ATOM   3330  O  OD1 . ASP B 1 68  ? -30.142 51.630  150.161 1.00 91.52 ? 68   ASP B OD1 1 
ATOM   3331  O  OD2 . ASP B 1 68  ? -31.346 50.174  149.019 1.00 90.27 ? 68   ASP B OD2 1 
ATOM   3332  N  N   . LEU B 1 69  ? -25.765 50.351  148.331 1.00 67.21 ? 69   LEU B N   1 
ATOM   3333  C  CA  . LEU B 1 69  ? -24.647 49.677  147.712 1.00 61.06 ? 69   LEU B CA  1 
ATOM   3334  C  C   . LEU B 1 69  ? -23.319 49.798  148.406 1.00 56.07 ? 69   LEU B C   1 
ATOM   3335  O  O   . LEU B 1 69  ? -22.958 50.861  148.887 1.00 57.10 ? 69   LEU B O   1 
ATOM   3336  C  CB  . LEU B 1 69  ? -24.504 50.160  146.275 1.00 62.85 ? 69   LEU B CB  1 
ATOM   3337  C  CG  . LEU B 1 69  ? -25.717 49.924  145.383 1.00 60.82 ? 69   LEU B CG  1 
ATOM   3338  C  CD1 . LEU B 1 69  ? -25.393 50.474  144.007 1.00 60.34 ? 69   LEU B CD1 1 
ATOM   3339  C  CD2 . LEU B 1 69  ? -26.063 48.426  145.313 1.00 59.18 ? 69   LEU B CD2 1 
ATOM   3340  N  N   . THR B 1 70  ? -22.580 48.700  148.453 1.00 50.26 ? 70   THR B N   1 
ATOM   3341  C  CA  . THR B 1 70  ? -21.272 48.758  149.069 1.00 46.52 ? 70   THR B CA  1 
ATOM   3342  C  C   . THR B 1 70  ? -20.295 49.338  148.058 1.00 46.40 ? 70   THR B C   1 
ATOM   3343  O  O   . THR B 1 70  ? -20.578 49.407  146.850 1.00 46.00 ? 70   THR B O   1 
ATOM   3344  C  CB  . THR B 1 70  ? -20.743 47.360  149.461 1.00 46.63 ? 70   THR B CB  1 
ATOM   3345  O  OG1 . THR B 1 70  ? -20.553 46.559  148.278 1.00 44.68 ? 70   THR B OG1 1 
ATOM   3346  C  CG2 . THR B 1 70  ? -21.718 46.669  150.415 1.00 42.69 ? 70   THR B CG2 1 
ATOM   3347  N  N   . ILE B 1 71  ? -19.150 49.760  148.571 1.00 43.75 ? 71   ILE B N   1 
ATOM   3348  C  CA  . ILE B 1 71  ? -18.061 50.282  147.781 1.00 41.35 ? 71   ILE B CA  1 
ATOM   3349  C  C   . ILE B 1 71  ? -17.905 49.374  146.525 1.00 43.70 ? 71   ILE B C   1 
ATOM   3350  O  O   . ILE B 1 71  ? -17.846 49.871  145.386 1.00 42.92 ? 71   ILE B O   1 
ATOM   3351  C  CB  . ILE B 1 71  ? -16.801 50.290  148.702 1.00 47.02 ? 71   ILE B CB  1 
ATOM   3352  C  CG1 . ILE B 1 71  ? -16.307 51.705  148.881 1.00 53.12 ? 71   ILE B CG1 1 
ATOM   3353  C  CG2 . ILE B 1 71  ? -15.665 49.417  148.188 1.00 45.95 ? 71   ILE B CG2 1 
ATOM   3354  C  CD1 . ILE B 1 71  ? -15.036 51.722  149.739 1.00 60.50 ? 71   ILE B CD1 1 
ATOM   3355  N  N   . GLY B 1 72  ? -17.881 48.053  146.736 1.00 40.82 ? 72   GLY B N   1 
ATOM   3356  C  CA  . GLY B 1 72  ? -17.750 47.098  145.640 1.00 45.87 ? 72   GLY B CA  1 
ATOM   3357  C  C   . GLY B 1 72  ? -18.956 46.981  144.705 1.00 49.50 ? 72   GLY B C   1 
ATOM   3358  O  O   . GLY B 1 72  ? -18.790 46.861  143.484 1.00 48.53 ? 72   GLY B O   1 
ATOM   3359  N  N   . HIS B 1 73  ? -20.165 46.990  145.273 1.00 54.30 ? 73   HIS B N   1 
ATOM   3360  C  CA  . HIS B 1 73  ? -21.400 46.925  144.480 1.00 57.00 ? 73   HIS B CA  1 
ATOM   3361  C  C   . HIS B 1 73  ? -21.320 48.102  143.518 1.00 53.11 ? 73   HIS B C   1 
ATOM   3362  O  O   . HIS B 1 73  ? -21.434 47.955  142.308 1.00 51.65 ? 73   HIS B O   1 
ATOM   3363  C  CB  . HIS B 1 73  ? -22.659 47.199  145.322 1.00 66.57 ? 73   HIS B CB  1 
ATOM   3364  C  CG  . HIS B 1 73  ? -23.115 46.069  146.188 1.00 74.27 ? 73   HIS B CG  1 
ATOM   3365  N  ND1 . HIS B 1 73  ? -24.154 46.210  147.089 1.00 77.07 ? 73   HIS B ND1 1 
ATOM   3366  C  CD2 . HIS B 1 73  ? -22.706 44.784  146.282 1.00 77.50 ? 73   HIS B CD2 1 
ATOM   3367  C  CE1 . HIS B 1 73  ? -24.364 45.060  147.701 1.00 78.87 ? 73   HIS B CE1 1 
ATOM   3368  N  NE2 . HIS B 1 73  ? -23.499 44.177  147.230 1.00 81.79 ? 73   HIS B NE2 1 
ATOM   3369  N  N   . LEU B 1 74  ? -21.147 49.282  144.100 1.00 48.26 ? 74   LEU B N   1 
ATOM   3370  C  CA  . LEU B 1 74  ? -21.095 50.516  143.332 1.00 46.50 ? 74   LEU B CA  1 
ATOM   3371  C  C   . LEU B 1 74  ? -20.163 50.433  142.143 1.00 44.68 ? 74   LEU B C   1 
ATOM   3372  O  O   . LEU B 1 74  ? -20.580 50.659  141.003 1.00 44.58 ? 74   LEU B O   1 
ATOM   3373  C  CB  . LEU B 1 74  ? -20.684 51.679  144.231 1.00 42.00 ? 74   LEU B CB  1 
ATOM   3374  C  CG  . LEU B 1 74  ? -21.457 52.992  144.158 1.00 39.47 ? 74   LEU B CG  1 
ATOM   3375  C  CD1 . LEU B 1 74  ? -22.796 52.819  143.493 1.00 37.75 ? 74   LEU B CD1 1 
ATOM   3376  C  CD2 . LEU B 1 74  ? -21.624 53.507  145.579 1.00 41.35 ? 74   LEU B CD2 1 
ATOM   3377  N  N   . GLY B 1 75  ? -18.907 50.102  142.408 1.00 41.48 ? 75   GLY B N   1 
ATOM   3378  C  CA  . GLY B 1 75  ? -17.947 50.015  141.326 1.00 41.13 ? 75   GLY B CA  1 
ATOM   3379  C  C   . GLY B 1 75  ? -18.428 49.135  140.187 1.00 40.71 ? 75   GLY B C   1 
ATOM   3380  O  O   . GLY B 1 75  ? -18.334 49.494  139.008 1.00 43.22 ? 75   GLY B O   1 
ATOM   3381  N  N   . LEU B 1 76  ? -18.947 47.972  140.546 1.00 37.70 ? 76   LEU B N   1 
ATOM   3382  C  CA  . LEU B 1 76  ? -19.444 47.013  139.573 1.00 36.65 ? 76   LEU B CA  1 
ATOM   3383  C  C   . LEU B 1 76  ? -20.629 47.575  138.791 1.00 36.85 ? 76   LEU B C   1 
ATOM   3384  O  O   . LEU B 1 76  ? -20.745 47.398  137.579 1.00 34.82 ? 76   LEU B O   1 
ATOM   3385  C  CB  . LEU B 1 76  ? -19.841 45.723  140.299 1.00 35.76 ? 76   LEU B CB  1 
ATOM   3386  C  CG  . LEU B 1 76  ? -19.000 44.461  140.065 1.00 39.88 ? 76   LEU B CG  1 
ATOM   3387  C  CD1 . LEU B 1 76  ? -17.593 44.767  139.626 1.00 36.67 ? 76   LEU B CD1 1 
ATOM   3388  C  CD2 . LEU B 1 76  ? -18.998 43.663  141.352 1.00 41.90 ? 76   LEU B CD2 1 
ATOM   3389  N  N   . THR B 1 77  ? -21.515 48.261  139.497 1.00 40.02 ? 77   THR B N   1 
ATOM   3390  C  CA  . THR B 1 77  ? -22.687 48.846  138.871 1.00 40.19 ? 77   THR B CA  1 
ATOM   3391  C  C   . THR B 1 77  ? -22.269 49.938  137.899 1.00 39.01 ? 77   THR B C   1 
ATOM   3392  O  O   . THR B 1 77  ? -22.815 50.042  136.810 1.00 38.01 ? 77   THR B O   1 
ATOM   3393  C  CB  . THR B 1 77  ? -23.632 49.389  139.951 1.00 37.85 ? 77   THR B CB  1 
ATOM   3394  O  OG1 . THR B 1 77  ? -24.133 48.274  140.687 1.00 43.75 ? 77   THR B OG1 1 
ATOM   3395  C  CG2 . THR B 1 77  ? -24.816 50.134  139.355 1.00 40.00 ? 77   THR B CG2 1 
ATOM   3396  N  N   . ILE B 1 78  ? -21.285 50.737  138.288 1.00 38.01 ? 78   ILE B N   1 
ATOM   3397  C  CA  . ILE B 1 78  ? -20.835 51.808  137.428 1.00 38.18 ? 78   ILE B CA  1 
ATOM   3398  C  C   . ILE B 1 78  ? -20.288 51.228  136.131 1.00 39.54 ? 78   ILE B C   1 
ATOM   3399  O  O   . ILE B 1 78  ? -20.544 51.747  135.041 1.00 37.79 ? 78   ILE B O   1 
ATOM   3400  C  CB  . ILE B 1 78  ? -19.781 52.679  138.156 1.00 35.30 ? 78   ILE B CB  1 
ATOM   3401  C  CG1 . ILE B 1 78  ? -20.499 53.510  139.247 1.00 36.94 ? 78   ILE B CG1 1 
ATOM   3402  C  CG2 . ILE B 1 78  ? -19.012 53.532  137.157 1.00 24.15 ? 78   ILE B CG2 1 
ATOM   3403  C  CD1 . ILE B 1 78  ? -19.562 54.271  140.213 1.00 36.15 ? 78   ILE B CD1 1 
ATOM   3404  N  N   . MET B 1 79  ? -19.555 50.131  136.236 1.00 39.72 ? 79   MET B N   1 
ATOM   3405  C  CA  . MET B 1 79  ? -19.002 49.544  135.029 1.00 40.10 ? 79   MET B CA  1 
ATOM   3406  C  C   . MET B 1 79  ? -20.109 48.877  134.211 1.00 38.31 ? 79   MET B C   1 
ATOM   3407  O  O   . MET B 1 79  ? -20.120 48.966  132.977 1.00 38.37 ? 79   MET B O   1 
ATOM   3408  C  CB  . MET B 1 79  ? -17.877 48.566  135.370 1.00 38.58 ? 79   MET B CB  1 
ATOM   3409  C  CG  . MET B 1 79  ? -16.725 49.219  136.110 1.00 41.28 ? 79   MET B CG  1 
ATOM   3410  S  SD  . MET B 1 79  ? -15.249 48.158  136.203 1.00 49.56 ? 79   MET B SD  1 
ATOM   3411  C  CE  . MET B 1 79  ? -15.593 47.180  137.664 1.00 45.95 ? 79   MET B CE  1 
ATOM   3412  N  N   . ALA B 1 80  ? -21.051 48.229  134.882 1.00 35.81 ? 80   ALA B N   1 
ATOM   3413  C  CA  . ALA B 1 80  ? -22.143 47.607  134.151 1.00 34.98 ? 80   ALA B CA  1 
ATOM   3414  C  C   . ALA B 1 80  ? -22.834 48.677  133.274 1.00 33.97 ? 80   ALA B C   1 
ATOM   3415  O  O   . ALA B 1 80  ? -22.906 48.559  132.034 1.00 34.25 ? 80   ALA B O   1 
ATOM   3416  C  CB  . ALA B 1 80  ? -23.128 46.993  135.110 1.00 27.20 ? 80   ALA B CB  1 
ATOM   3417  N  N   . LEU B 1 81  ? -23.319 49.728  133.917 1.00 31.44 ? 81   LEU B N   1 
ATOM   3418  C  CA  . LEU B 1 81  ? -24.001 50.797  133.216 1.00 32.63 ? 81   LEU B CA  1 
ATOM   3419  C  C   . LEU B 1 81  ? -23.169 51.342  132.032 1.00 34.43 ? 81   LEU B C   1 
ATOM   3420  O  O   . LEU B 1 81  ? -23.685 51.565  130.921 1.00 33.82 ? 81   LEU B O   1 
ATOM   3421  C  CB  . LEU B 1 81  ? -24.363 51.906  134.221 1.00 28.94 ? 81   LEU B CB  1 
ATOM   3422  C  CG  . LEU B 1 81  ? -25.419 51.420  135.220 1.00 30.34 ? 81   LEU B CG  1 
ATOM   3423  C  CD1 . LEU B 1 81  ? -25.833 52.514  136.233 1.00 28.59 ? 81   LEU B CD1 1 
ATOM   3424  C  CD2 . LEU B 1 81  ? -26.636 50.964  134.420 1.00 31.33 ? 81   LEU B CD2 1 
ATOM   3425  N  N   . THR B 1 82  ? -21.886 51.547  132.280 1.00 34.59 ? 82   THR B N   1 
ATOM   3426  C  CA  . THR B 1 82  ? -20.984 52.039  131.259 1.00 35.04 ? 82   THR B CA  1 
ATOM   3427  C  C   . THR B 1 82  ? -20.935 51.042  130.094 1.00 37.09 ? 82   THR B C   1 
ATOM   3428  O  O   . THR B 1 82  ? -20.956 51.447  128.927 1.00 39.30 ? 82   THR B O   1 
ATOM   3429  C  CB  . THR B 1 82  ? -19.567 52.226  131.836 1.00 33.70 ? 82   THR B CB  1 
ATOM   3430  O  OG1 . THR B 1 82  ? -19.613 53.196  132.891 1.00 35.08 ? 82   THR B OG1 1 
ATOM   3431  C  CG2 . THR B 1 82  ? -18.625 52.691  130.773 1.00 27.15 ? 82   THR B CG2 1 
ATOM   3432  N  N   . SER B 1 83  ? -20.887 49.743  130.384 1.00 37.78 ? 83   SER B N   1 
ATOM   3433  C  CA  . SER B 1 83  ? -20.832 48.767  129.289 1.00 37.67 ? 83   SER B CA  1 
ATOM   3434  C  C   . SER B 1 83  ? -22.153 48.724  128.531 1.00 36.96 ? 83   SER B C   1 
ATOM   3435  O  O   . SER B 1 83  ? -22.260 48.058  127.516 1.00 38.11 ? 83   SER B O   1 
ATOM   3436  C  CB  . SER B 1 83  ? -20.485 47.368  129.795 1.00 36.35 ? 83   SER B CB  1 
ATOM   3437  O  OG  . SER B 1 83  ? -21.520 46.851  130.601 1.00 37.12 ? 83   SER B OG  1 
ATOM   3438  N  N   . SER B 1 84  ? -23.165 49.413  129.044 1.00 37.17 ? 84   SER B N   1 
ATOM   3439  C  CA  . SER B 1 84  ? -24.456 49.486  128.370 1.00 37.50 ? 84   SER B CA  1 
ATOM   3440  C  C   . SER B 1 84  ? -24.589 50.887  127.805 1.00 36.66 ? 84   SER B C   1 
ATOM   3441  O  O   . SER B 1 84  ? -25.666 51.289  127.378 1.00 37.54 ? 84   SER B O   1 
ATOM   3442  C  CB  . SER B 1 84  ? -25.624 49.213  129.332 1.00 36.71 ? 84   SER B CB  1 
ATOM   3443  O  OG  . SER B 1 84  ? -25.900 47.830  129.451 1.00 38.54 ? 84   SER B OG  1 
ATOM   3444  N  N   . CYS B 1 85  ? -23.480 51.617  127.811 1.00 37.09 ? 85   CYS B N   1 
ATOM   3445  C  CA  . CYS B 1 85  ? -23.446 52.986  127.311 1.00 40.10 ? 85   CYS B CA  1 
ATOM   3446  C  C   . CYS B 1 85  ? -24.434 53.884  128.036 1.00 40.83 ? 85   CYS B C   1 
ATOM   3447  O  O   . CYS B 1 85  ? -25.037 54.783  127.442 1.00 40.60 ? 85   CYS B O   1 
ATOM   3448  C  CB  . CYS B 1 85  ? -23.710 53.011  125.802 1.00 41.91 ? 85   CYS B CB  1 
ATOM   3449  S  SG  . CYS B 1 85  ? -22.452 52.058  124.858 1.00 48.64 ? 85   CYS B SG  1 
ATOM   3450  N  N   . ARG B 1 86  ? -24.581 53.643  129.335 1.00 40.86 ? 86   ARG B N   1 
ATOM   3451  C  CA  . ARG B 1 86  ? -25.487 54.432  130.172 1.00 40.21 ? 86   ARG B CA  1 
ATOM   3452  C  C   . ARG B 1 86  ? -24.704 55.290  131.134 1.00 40.93 ? 86   ARG B C   1 
ATOM   3453  O  O   . ARG B 1 86  ? -23.665 54.871  131.639 1.00 43.21 ? 86   ARG B O   1 
ATOM   3454  C  CB  . ARG B 1 86  ? -26.399 53.499  130.949 1.00 39.78 ? 86   ARG B CB  1 
ATOM   3455  C  CG  . ARG B 1 86  ? -27.465 52.915  130.086 1.00 39.55 ? 86   ARG B CG  1 
ATOM   3456  C  CD  . ARG B 1 86  ? -28.517 53.962  129.790 1.00 36.44 ? 86   ARG B CD  1 
ATOM   3457  N  NE  . ARG B 1 86  ? -29.637 53.356  129.092 1.00 35.45 ? 86   ARG B NE  1 
ATOM   3458  C  CZ  . ARG B 1 86  ? -30.807 53.948  128.877 1.00 38.96 ? 86   ARG B CZ  1 
ATOM   3459  N  NH1 . ARG B 1 86  ? -31.035 55.197  129.310 1.00 31.93 ? 86   ARG B NH1 1 
ATOM   3460  N  NH2 . ARG B 1 86  ? -31.749 53.270  128.228 1.00 33.41 ? 86   ARG B NH2 1 
ATOM   3461  N  N   . ASP B 1 87  ? -25.201 56.489  131.393 1.00 42.74 ? 87   ASP B N   1 
ATOM   3462  C  CA  . ASP B 1 87  ? -24.529 57.403  132.303 1.00 44.36 ? 87   ASP B CA  1 
ATOM   3463  C  C   . ASP B 1 87  ? -24.758 56.950  133.736 1.00 46.57 ? 87   ASP B C   1 
ATOM   3464  O  O   . ASP B 1 87  ? -25.838 57.122  134.279 1.00 45.44 ? 87   ASP B O   1 
ATOM   3465  C  CB  . ASP B 1 87  ? -25.061 58.821  132.106 1.00 46.26 ? 87   ASP B CB  1 
ATOM   3466  C  CG  . ASP B 1 87  ? -24.330 59.830  132.954 1.00 48.63 ? 87   ASP B CG  1 
ATOM   3467  O  OD1 . ASP B 1 87  ? -23.441 59.419  133.725 1.00 52.24 ? 87   ASP B OD1 1 
ATOM   3468  O  OD2 . ASP B 1 87  ? -24.638 61.034  132.851 1.00 51.25 ? 87   ASP B OD2 1 
ATOM   3469  N  N   . PRO B 1 88  ? -23.727 56.377  134.378 1.00 49.62 ? 88   PRO B N   1 
ATOM   3470  C  CA  . PRO B 1 88  ? -23.894 55.916  135.757 1.00 51.01 ? 88   PRO B CA  1 
ATOM   3471  C  C   . PRO B 1 88  ? -24.285 57.124  136.589 1.00 53.22 ? 88   PRO B C   1 
ATOM   3472  O  O   . PRO B 1 88  ? -24.886 57.015  137.672 1.00 52.83 ? 88   PRO B O   1 
ATOM   3473  C  CB  . PRO B 1 88  ? -22.500 55.395  136.127 1.00 49.63 ? 88   PRO B CB  1 
ATOM   3474  C  CG  . PRO B 1 88  ? -21.786 55.253  134.816 1.00 50.25 ? 88   PRO B CG  1 
ATOM   3475  C  CD  . PRO B 1 88  ? -22.300 56.410  134.028 1.00 50.29 ? 88   PRO B CD  1 
ATOM   3476  N  N   . GLY B 1 89  ? -23.919 58.280  136.048 1.00 54.69 ? 89   GLY B N   1 
ATOM   3477  C  CA  . GLY B 1 89  ? -24.195 59.541  136.691 1.00 56.21 ? 89   GLY B CA  1 
ATOM   3478  C  C   . GLY B 1 89  ? -23.829 59.596  138.162 1.00 55.16 ? 89   GLY B C   1 
ATOM   3479  O  O   . GLY B 1 89  ? -22.701 59.332  138.579 1.00 55.23 ? 89   GLY B O   1 
ATOM   3480  N  N   . ASP B 1 90  ? -24.837 59.953  138.935 1.00 56.00 ? 90   ASP B N   1 
ATOM   3481  C  CA  . ASP B 1 90  ? -24.770 60.120  140.368 1.00 56.65 ? 90   ASP B CA  1 
ATOM   3482  C  C   . ASP B 1 90  ? -23.959 59.076  141.135 1.00 54.91 ? 90   ASP B C   1 
ATOM   3483  O  O   . ASP B 1 90  ? -23.314 59.403  142.141 1.00 57.02 ? 90   ASP B O   1 
ATOM   3484  C  CB  . ASP B 1 90  ? -26.200 60.165  140.889 1.00 61.45 ? 90   ASP B CB  1 
ATOM   3485  C  CG  . ASP B 1 90  ? -26.323 60.952  142.148 1.00 68.54 ? 90   ASP B CG  1 
ATOM   3486  O  OD1 . ASP B 1 90  ? -25.276 61.460  142.615 1.00 73.01 ? 90   ASP B OD1 1 
ATOM   3487  O  OD2 . ASP B 1 90  ? -27.460 61.062  142.666 1.00 71.79 ? 90   ASP B OD2 1 
ATOM   3488  N  N   . LYS B 1 91  ? -23.991 57.828  140.674 1.00 51.14 ? 91   LYS B N   1 
ATOM   3489  C  CA  . LYS B 1 91  ? -23.264 56.744  141.337 1.00 45.24 ? 91   LYS B CA  1 
ATOM   3490  C  C   . LYS B 1 91  ? -21.759 56.963  141.423 1.00 45.96 ? 91   LYS B C   1 
ATOM   3491  O  O   . LYS B 1 91  ? -21.103 56.502  142.357 1.00 45.89 ? 91   LYS B O   1 
ATOM   3492  C  CB  . LYS B 1 91  ? -23.531 55.424  140.623 1.00 40.02 ? 91   LYS B CB  1 
ATOM   3493  C  CG  . LYS B 1 91  ? -24.944 54.926  140.807 1.00 35.33 ? 91   LYS B CG  1 
ATOM   3494  C  CD  . LYS B 1 91  ? -25.195 53.683  139.993 1.00 38.61 ? 91   LYS B CD  1 
ATOM   3495  C  CE  . LYS B 1 91  ? -26.661 53.444  139.801 1.00 38.77 ? 91   LYS B CE  1 
ATOM   3496  N  NZ  . LYS B 1 91  ? -27.348 53.218  141.064 1.00 45.62 ? 91   LYS B NZ  1 
ATOM   3497  N  N   . VAL B 1 92  ? -21.215 57.684  140.452 1.00 45.28 ? 92   VAL B N   1 
ATOM   3498  C  CA  . VAL B 1 92  ? -19.787 57.932  140.407 1.00 40.85 ? 92   VAL B CA  1 
ATOM   3499  C  C   . VAL B 1 92  ? -19.310 58.896  141.475 1.00 40.20 ? 92   VAL B C   1 
ATOM   3500  O  O   . VAL B 1 92  ? -18.282 58.657  142.103 1.00 38.06 ? 92   VAL B O   1 
ATOM   3501  C  CB  . VAL B 1 92  ? -19.380 58.418  139.009 1.00 38.04 ? 92   VAL B CB  1 
ATOM   3502  C  CG1 . VAL B 1 92  ? -17.917 58.724  138.967 1.00 35.45 ? 92   VAL B CG1 1 
ATOM   3503  C  CG2 . VAL B 1 92  ? -19.690 57.338  137.999 1.00 38.78 ? 92   VAL B CG2 1 
ATOM   3504  N  N   . SER B 1 93  ? -20.040 59.983  141.698 1.00 41.57 ? 93   SER B N   1 
ATOM   3505  C  CA  . SER B 1 93  ? -19.608 60.917  142.738 1.00 44.96 ? 93   SER B CA  1 
ATOM   3506  C  C   . SER B 1 93  ? -19.805 60.280  144.132 1.00 45.60 ? 93   SER B C   1 
ATOM   3507  O  O   . SER B 1 93  ? -18.959 60.443  145.019 1.00 44.79 ? 93   SER B O   1 
ATOM   3508  C  CB  . SER B 1 93  ? -20.361 62.222  142.624 1.00 37.63 ? 93   SER B CB  1 
ATOM   3509  O  OG  . SER B 1 93  ? -21.708 61.934  142.342 1.00 52.80 ? 93   SER B OG  1 
ATOM   3510  N  N   . ILE B 1 94  ? -20.889 59.529  144.306 1.00 43.33 ? 94   ILE B N   1 
ATOM   3511  C  CA  . ILE B 1 94  ? -21.140 58.874  145.571 1.00 43.98 ? 94   ILE B CA  1 
ATOM   3512  C  C   . ILE B 1 94  ? -19.974 57.953  145.908 1.00 43.95 ? 94   ILE B C   1 
ATOM   3513  O  O   . ILE B 1 94  ? -19.505 57.902  147.050 1.00 45.45 ? 94   ILE B O   1 
ATOM   3514  C  CB  . ILE B 1 94  ? -22.425 58.055  145.502 1.00 46.84 ? 94   ILE B CB  1 
ATOM   3515  C  CG1 . ILE B 1 94  ? -23.606 59.012  145.368 1.00 51.13 ? 94   ILE B CG1 1 
ATOM   3516  C  CG2 . ILE B 1 94  ? -22.559 57.169  146.737 1.00 47.29 ? 94   ILE B CG2 1 
ATOM   3517  C  CD1 . ILE B 1 94  ? -24.936 58.339  145.119 1.00 53.89 ? 94   ILE B CD1 1 
ATOM   3518  N  N   . LEU B 1 95  ? -19.497 57.229  144.906 1.00 42.12 ? 95   LEU B N   1 
ATOM   3519  C  CA  . LEU B 1 95  ? -18.384 56.320  145.129 1.00 42.48 ? 95   LEU B CA  1 
ATOM   3520  C  C   . LEU B 1 95  ? -17.083 57.104  145.325 1.00 44.16 ? 95   LEU B C   1 
ATOM   3521  O  O   . LEU B 1 95  ? -16.259 56.768  146.181 1.00 45.72 ? 95   LEU B O   1 
ATOM   3522  C  CB  . LEU B 1 95  ? -18.239 55.355  143.946 1.00 37.77 ? 95   LEU B CB  1 
ATOM   3523  C  CG  . LEU B 1 95  ? -17.111 54.327  144.110 1.00 39.02 ? 95   LEU B CG  1 
ATOM   3524  C  CD1 . LEU B 1 95  ? -17.420 53.428  145.289 1.00 34.44 ? 95   LEU B CD1 1 
ATOM   3525  C  CD2 . LEU B 1 95  ? -16.941 53.478  142.859 1.00 35.48 ? 95   LEU B CD2 1 
ATOM   3526  N  N   . GLN B 1 96  ? -16.909 58.154  144.529 1.00 43.66 ? 96   GLN B N   1 
ATOM   3527  C  CA  . GLN B 1 96  ? -15.713 58.973  144.606 1.00 44.59 ? 96   GLN B CA  1 
ATOM   3528  C  C   . GLN B 1 96  ? -15.563 59.548  146.013 1.00 44.83 ? 96   GLN B C   1 
ATOM   3529  O  O   . GLN B 1 96  ? -14.483 59.495  146.588 1.00 47.38 ? 96   GLN B O   1 
ATOM   3530  C  CB  . GLN B 1 96  ? -15.793 60.083  143.541 1.00 46.26 ? 96   GLN B CB  1 
ATOM   3531  C  CG  . GLN B 1 96  ? -14.650 61.103  143.474 1.00 45.97 ? 96   GLN B CG  1 
ATOM   3532  C  CD  . GLN B 1 96  ? -13.267 60.496  143.283 1.00 50.96 ? 96   GLN B CD  1 
ATOM   3533  O  OE1 . GLN B 1 96  ? -13.072 59.571  142.495 1.00 54.19 ? 96   GLN B OE1 1 
ATOM   3534  N  NE2 . GLN B 1 96  ? -12.289 61.040  143.993 1.00 52.08 ? 96   GLN B NE2 1 
ATOM   3535  N  N   . ARG B 1 97  ? -16.652 60.060  146.581 1.00 45.37 ? 97   ARG B N   1 
ATOM   3536  C  CA  . ARG B 1 97  ? -16.599 60.656  147.918 1.00 46.30 ? 97   ARG B CA  1 
ATOM   3537  C  C   . ARG B 1 97  ? -16.315 59.602  148.984 1.00 44.86 ? 97   ARG B C   1 
ATOM   3538  O  O   . ARG B 1 97  ? -15.585 59.863  149.941 1.00 45.56 ? 97   ARG B O   1 
ATOM   3539  C  CB  . ARG B 1 97  ? -17.896 61.435  148.210 1.00 45.46 ? 97   ARG B CB  1 
ATOM   3540  C  CG  . ARG B 1 97  ? -18.350 62.209  146.977 1.00 54.25 ? 97   ARG B CG  1 
ATOM   3541  C  CD  . ARG B 1 97  ? -18.859 63.600  147.236 1.00 55.57 ? 97   ARG B CD  1 
ATOM   3542  N  NE  . ARG B 1 97  ? -20.108 63.592  147.983 1.00 55.54 ? 97   ARG B NE  1 
ATOM   3543  C  CZ  . ARG B 1 97  ? -20.636 64.690  148.497 1.00 54.65 ? 97   ARG B CZ  1 
ATOM   3544  N  NH1 . ARG B 1 97  ? -20.009 65.843  148.319 1.00 55.64 ? 97   ARG B NH1 1 
ATOM   3545  N  NH2 . ARG B 1 97  ? -21.754 64.637  149.206 1.00 56.52 ? 97   ARG B NH2 1 
ATOM   3546  N  N   . GLN B 1 98  ? -16.880 58.410  148.823 1.00 40.87 ? 98   GLN B N   1 
ATOM   3547  C  CA  . GLN B 1 98  ? -16.592 57.356  149.773 1.00 36.27 ? 98   GLN B CA  1 
ATOM   3548  C  C   . GLN B 1 98  ? -15.105 56.964  149.655 1.00 36.84 ? 98   GLN B C   1 
ATOM   3549  O  O   . GLN B 1 98  ? -14.413 56.845  150.655 1.00 39.42 ? 98   GLN B O   1 
ATOM   3550  C  CB  . GLN B 1 98  ? -17.485 56.144  149.526 1.00 29.37 ? 98   GLN B CB  1 
ATOM   3551  C  CG  . GLN B 1 98  ? -18.730 56.108  150.352 1.00 32.10 ? 98   GLN B CG  1 
ATOM   3552  C  CD  . GLN B 1 98  ? -19.773 55.118  149.858 1.00 34.61 ? 98   GLN B CD  1 
ATOM   3553  O  OE1 . GLN B 1 98  ? -20.649 55.471  149.070 1.00 38.92 ? 98   GLN B OE1 1 
ATOM   3554  N  NE2 . GLN B 1 98  ? -19.686 53.879  150.315 1.00 35.25 ? 98   GLN B NE2 1 
ATOM   3555  N  N   . MET B 1 99  ? -14.583 56.777  148.452 1.00 37.57 ? 99   MET B N   1 
ATOM   3556  C  CA  . MET B 1 99  ? -13.179 56.391  148.372 1.00 40.10 ? 99   MET B CA  1 
ATOM   3557  C  C   . MET B 1 99  ? -12.212 57.468  148.817 1.00 43.41 ? 99   MET B C   1 
ATOM   3558  O  O   . MET B 1 99  ? -11.103 57.162  149.240 1.00 44.12 ? 99   MET B O   1 
ATOM   3559  C  CB  . MET B 1 99  ? -12.804 55.925  146.974 1.00 36.50 ? 99   MET B CB  1 
ATOM   3560  C  CG  . MET B 1 99  ? -13.514 54.652  146.565 1.00 40.43 ? 99   MET B CG  1 
ATOM   3561  S  SD  . MET B 1 99  ? -13.452 53.317  147.815 1.00 38.66 ? 99   MET B SD  1 
ATOM   3562  C  CE  . MET B 1 99  ? -11.658 52.799  147.706 1.00 25.62 ? 99   MET B CE  1 
ATOM   3563  N  N   . GLU B 1 100 ? -12.594 58.735  148.716 1.00 46.70 ? 100  GLU B N   1 
ATOM   3564  C  CA  . GLU B 1 100 ? -11.683 59.771  149.187 1.00 49.45 ? 100  GLU B CA  1 
ATOM   3565  C  C   . GLU B 1 100 ? -11.520 59.603  150.715 1.00 48.94 ? 100  GLU B C   1 
ATOM   3566  O  O   . GLU B 1 100 ? -10.530 60.049  151.318 1.00 49.03 ? 100  GLU B O   1 
ATOM   3567  C  CB  . GLU B 1 100 ? -12.235 61.154  148.854 1.00 50.27 ? 100  GLU B CB  1 
ATOM   3568  C  CG  . GLU B 1 100 ? -12.221 61.466  147.379 1.00 56.21 ? 100  GLU B CG  1 
ATOM   3569  C  CD  . GLU B 1 100 ? -12.795 62.843  147.077 1.00 59.77 ? 100  GLU B CD  1 
ATOM   3570  O  OE1 . GLU B 1 100 ? -13.687 63.285  147.834 1.00 63.73 ? 100  GLU B OE1 1 
ATOM   3571  O  OE2 . GLU B 1 100 ? -12.368 63.476  146.082 1.00 59.71 ? 100  GLU B OE2 1 
ATOM   3572  N  N   . ASN B 1 101 ? -12.487 58.921  151.315 1.00 46.08 ? 101  ASN B N   1 
ATOM   3573  C  CA  . ASN B 1 101 ? -12.502 58.692  152.743 1.00 46.71 ? 101  ASN B CA  1 
ATOM   3574  C  C   . ASN B 1 101 ? -12.106 57.279  153.144 1.00 51.01 ? 101  ASN B C   1 
ATOM   3575  O  O   . ASN B 1 101 ? -12.145 56.921  154.328 1.00 53.50 ? 101  ASN B O   1 
ATOM   3576  C  CB  . ASN B 1 101 ? -13.900 58.985  153.275 1.00 44.66 ? 101  ASN B CB  1 
ATOM   3577  C  CG  . ASN B 1 101 ? -14.106 60.444  153.566 1.00 43.25 ? 101  ASN B CG  1 
ATOM   3578  O  OD1 . ASN B 1 101 ? -13.573 60.960  154.557 1.00 43.22 ? 101  ASN B OD1 1 
ATOM   3579  N  ND2 . ASN B 1 101 ? -14.864 61.131  152.706 1.00 34.78 ? 101  ASN B ND2 1 
ATOM   3580  N  N   . TRP B 1 102 ? -11.713 56.470  152.171 1.00 52.77 ? 102  TRP B N   1 
ATOM   3581  C  CA  . TRP B 1 102 ? -11.371 55.095  152.468 1.00 51.80 ? 102  TRP B CA  1 
ATOM   3582  C  C   . TRP B 1 102 ? -9.969  54.880  152.997 1.00 54.16 ? 102  TRP B C   1 
ATOM   3583  O  O   . TRP B 1 102 ? -8.994  55.454  152.508 1.00 54.26 ? 102  TRP B O   1 
ATOM   3584  C  CB  . TRP B 1 102 ? -11.587 54.209  151.227 1.00 49.51 ? 102  TRP B CB  1 
ATOM   3585  C  CG  . TRP B 1 102 ? -11.388 52.748  151.525 1.00 50.19 ? 102  TRP B CG  1 
ATOM   3586  C  CD1 . TRP B 1 102 ? -12.324 51.859  151.994 1.00 47.17 ? 102  TRP B CD1 1 
ATOM   3587  C  CD2 . TRP B 1 102 ? -10.144 52.040  151.503 1.00 49.15 ? 102  TRP B CD2 1 
ATOM   3588  N  NE1 . TRP B 1 102 ? -11.730 50.651  152.270 1.00 49.24 ? 102  TRP B NE1 1 
ATOM   3589  C  CE2 . TRP B 1 102 ? -10.394 50.736  151.979 1.00 47.88 ? 102  TRP B CE2 1 
ATOM   3590  C  CE3 . TRP B 1 102 ? -8.838  52.390  151.134 1.00 47.98 ? 102  TRP B CE3 1 
ATOM   3591  C  CZ2 . TRP B 1 102 ? -9.387  49.780  152.096 1.00 48.40 ? 102  TRP B CZ2 1 
ATOM   3592  C  CZ3 . TRP B 1 102 ? -7.843  51.447  151.248 1.00 50.37 ? 102  TRP B CZ3 1 
ATOM   3593  C  CH2 . TRP B 1 102 ? -8.120  50.153  151.729 1.00 47.94 ? 102  TRP B CH2 1 
ATOM   3594  N  N   . ALA B 1 103 ? -9.895  54.031  154.012 1.00 57.91 ? 103  ALA B N   1 
ATOM   3595  C  CA  . ALA B 1 103 ? -8.640  53.638  154.631 1.00 59.13 ? 103  ALA B CA  1 
ATOM   3596  C  C   . ALA B 1 103 ? -8.865  52.212  155.117 1.00 61.20 ? 103  ALA B C   1 
ATOM   3597  O  O   . ALA B 1 103 ? -10.008 51.763  155.292 1.00 60.27 ? 103  ALA B O   1 
ATOM   3598  C  CB  . ALA B 1 103 ? -8.306  54.544  155.792 1.00 56.54 ? 103  ALA B CB  1 
ATOM   3599  N  N   . PRO B 1 104 ? -7.779  51.463  155.310 1.00 64.23 ? 104  PRO B N   1 
ATOM   3600  C  CA  . PRO B 1 104 ? -7.873  50.079  155.783 1.00 65.39 ? 104  PRO B CA  1 
ATOM   3601  C  C   . PRO B 1 104 ? -8.084  50.095  157.293 1.00 67.60 ? 104  PRO B C   1 
ATOM   3602  O  O   . PRO B 1 104 ? -7.461  50.905  157.990 1.00 67.60 ? 104  PRO B O   1 
ATOM   3603  C  CB  . PRO B 1 104 ? -6.519  49.507  155.401 1.00 66.42 ? 104  PRO B CB  1 
ATOM   3604  C  CG  . PRO B 1 104 ? -5.601  50.705  155.634 1.00 68.36 ? 104  PRO B CG  1 
ATOM   3605  C  CD  . PRO B 1 104 ? -6.386  51.832  154.991 1.00 66.12 ? 104  PRO B CD  1 
ATOM   3606  N  N   . SER B 1 105 ? -8.956  49.219  157.794 1.00 69.89 ? 105  SER B N   1 
ATOM   3607  C  CA  . SER B 1 105 ? -9.238  49.149  159.234 1.00 71.20 ? 105  SER B CA  1 
ATOM   3608  C  C   . SER B 1 105 ? -7.983  49.049  160.112 1.00 71.88 ? 105  SER B C   1 
ATOM   3609  O  O   . SER B 1 105 ? -7.954  49.585  161.227 1.00 71.38 ? 105  SER B O   1 
ATOM   3610  C  CB  . SER B 1 105 ? -10.176 47.967  159.547 1.00 72.29 ? 105  SER B CB  1 
ATOM   3611  O  OG  . SER B 1 105 ? -9.633  46.712  159.149 1.00 72.81 ? 105  SER B OG  1 
ATOM   3612  N  N   . SER B 1 106 ? -6.951  48.373  159.612 1.00 71.46 ? 106  SER B N   1 
ATOM   3613  C  CA  . SER B 1 106 ? -5.711  48.211  160.372 1.00 73.76 ? 106  SER B CA  1 
ATOM   3614  C  C   . SER B 1 106 ? -4.556  47.758  159.470 1.00 75.86 ? 106  SER B C   1 
ATOM   3615  O  O   . SER B 1 106 ? -4.791  47.178  158.396 1.00 75.12 ? 106  SER B O   1 
ATOM   3616  C  CB  . SER B 1 106 ? -5.911  47.193  161.489 1.00 72.60 ? 106  SER B CB  1 
ATOM   3617  O  OG  . SER B 1 106 ? -4.665  46.707  161.972 1.00 67.50 ? 106  SER B OG  1 
ATOM   3618  N  N   . PRO B 1 107 ? -3.296  47.996  159.905 1.00 77.02 ? 107  PRO B N   1 
ATOM   3619  C  CA  . PRO B 1 107 ? -2.081  47.634  159.153 1.00 77.77 ? 107  PRO B CA  1 
ATOM   3620  C  C   . PRO B 1 107 ? -1.897  46.150  159.199 1.00 78.97 ? 107  PRO B C   1 
ATOM   3621  O  O   . PRO B 1 107 ? -0.757  45.672  159.394 1.00 81.81 ? 107  PRO B O   1 
ATOM   3622  C  CB  . PRO B 1 107 ? -0.954  48.329  159.936 1.00 77.82 ? 107  PRO B CB  1 
ATOM   3623  C  CG  . PRO B 1 107 ? -1.629  49.157  160.991 1.00 78.49 ? 107  PRO B CG  1 
ATOM   3624  C  CD  . PRO B 1 107 ? -2.942  48.498  161.246 1.00 77.43 ? 107  PRO B CD  1 
ATOM   3625  N  N   . ASN B 1 108 ? -3.005  45.440  159.057 1.00 81.19 ? 108  ASN B N   1 
ATOM   3626  C  CA  . ASN B 1 108 ? -2.970  44.021  159.184 1.00 82.73 ? 108  ASN B CA  1 
ATOM   3627  C  C   . ASN B 1 108 ? -4.385  43.477  158.997 1.00 79.73 ? 108  ASN B C   1 
ATOM   3628  O  O   . ASN B 1 108 ? -4.794  42.587  159.720 1.00 79.95 ? 108  ASN B O   1 
ATOM   3629  C  CB  . ASN B 1 108 ? -2.442  43.628  160.593 1.00 89.02 ? 108  ASN B CB  1 
ATOM   3630  C  CG  . ASN B 1 108 ? -0.955  43.254  160.619 1.00 93.20 ? 108  ASN B CG  1 
ATOM   3631  O  OD1 . ASN B 1 108 ? -0.371  43.103  161.727 1.00 95.80 ? 108  ASN B OD1 1 
ATOM   3632  N  ND2 . ASN B 1 108 ? -0.329  43.075  159.419 1.00 91.15 ? 108  ASN B ND2 1 
ATOM   3633  N  N   . ALA B 1 109 ? -5.123  44.019  158.033 1.00 76.29 ? 109  ALA B N   1 
ATOM   3634  C  CA  . ALA B 1 109 ? -6.480  43.590  157.807 1.00 70.32 ? 109  ALA B CA  1 
ATOM   3635  C  C   . ALA B 1 109 ? -6.429  42.447  156.855 1.00 67.41 ? 109  ALA B C   1 
ATOM   3636  O  O   . ALA B 1 109 ? -5.476  42.298  156.109 1.00 64.83 ? 109  ALA B O   1 
ATOM   3637  C  CB  . ALA B 1 109 ? -7.273  44.719  157.246 1.00 71.05 ? 109  ALA B CB  1 
ATOM   3638  N  N   . GLU B 1 110 ? -7.469  41.639  156.904 1.00 65.24 ? 110  GLU B N   1 
ATOM   3639  C  CA  . GLU B 1 110 ? -7.632  40.496  156.037 1.00 63.86 ? 110  GLU B CA  1 
ATOM   3640  C  C   . GLU B 1 110 ? -7.525  41.001  154.583 1.00 62.62 ? 110  GLU B C   1 
ATOM   3641  O  O   . GLU B 1 110 ? -8.105  42.030  154.217 1.00 61.50 ? 110  GLU B O   1 
ATOM   3642  C  CB  . GLU B 1 110 ? -9.010  39.875  156.309 1.00 67.03 ? 110  GLU B CB  1 
ATOM   3643  C  CG  . GLU B 1 110 ? -10.219 40.825  156.010 1.00 73.62 ? 110  GLU B CG  1 
ATOM   3644  C  CD  . GLU B 1 110 ? -10.535 41.911  157.088 1.00 75.39 ? 110  GLU B CD  1 
ATOM   3645  O  OE1 . GLU B 1 110 ? -9.606  42.584  157.617 1.00 72.10 ? 110  GLU B OE1 1 
ATOM   3646  O  OE2 . GLU B 1 110 ? -11.743 42.111  157.388 1.00 76.64 ? 110  GLU B OE2 1 
ATOM   3647  N  N   . ALA B 1 111 ? -6.739  40.311  153.769 1.00 60.13 ? 111  ALA B N   1 
ATOM   3648  C  CA  . ALA B 1 111 ? -6.564  40.715  152.383 1.00 57.90 ? 111  ALA B CA  1 
ATOM   3649  C  C   . ALA B 1 111 ? -7.892  40.898  151.619 1.00 57.11 ? 111  ALA B C   1 
ATOM   3650  O  O   . ALA B 1 111 ? -7.989  41.736  150.728 1.00 59.03 ? 111  ALA B O   1 
ATOM   3651  C  CB  . ALA B 1 111 ? -5.681  39.702  151.666 1.00 55.88 ? 111  ALA B CB  1 
ATOM   3652  N  N   . SER B 1 112 ? -8.909  40.120  151.953 1.00 54.33 ? 112  SER B N   1 
ATOM   3653  C  CA  . SER B 1 112 ? -10.191 40.238  151.272 1.00 53.74 ? 112  SER B CA  1 
ATOM   3654  C  C   . SER B 1 112 ? -10.844 41.622  151.468 1.00 52.72 ? 112  SER B C   1 
ATOM   3655  O  O   . SER B 1 112 ? -11.774 41.998  150.746 1.00 48.64 ? 112  SER B O   1 
ATOM   3656  C  CB  . SER B 1 112 ? -11.142 39.171  151.795 1.00 55.56 ? 112  SER B CB  1 
ATOM   3657  O  OG  . SER B 1 112 ? -11.480 39.460  153.143 1.00 58.72 ? 112  SER B OG  1 
ATOM   3658  N  N   . ALA B 1 113 ? -10.373 42.373  152.456 1.00 51.65 ? 113  ALA B N   1 
ATOM   3659  C  CA  . ALA B 1 113 ? -10.940 43.693  152.714 1.00 50.51 ? 113  ALA B CA  1 
ATOM   3660  C  C   . ALA B 1 113 ? -10.524 44.705  151.652 1.00 49.49 ? 113  ALA B C   1 
ATOM   3661  O  O   . ALA B 1 113 ? -11.042 45.812  151.610 1.00 49.95 ? 113  ALA B O   1 
ATOM   3662  C  CB  . ALA B 1 113 ? -10.514 44.186  154.092 1.00 51.12 ? 113  ALA B CB  1 
ATOM   3663  N  N   . PHE B 1 114 ? -9.582  44.328  150.799 1.00 47.75 ? 114  PHE B N   1 
ATOM   3664  C  CA  . PHE B 1 114 ? -9.134  45.229  149.766 1.00 49.64 ? 114  PHE B CA  1 
ATOM   3665  C  C   . PHE B 1 114 ? -9.831  44.942  148.442 1.00 48.12 ? 114  PHE B C   1 
ATOM   3666  O  O   . PHE B 1 114 ? -9.569  45.596  147.433 1.00 46.19 ? 114  PHE B O   1 
ATOM   3667  C  CB  . PHE B 1 114 ? -7.619  45.126  149.618 1.00 53.03 ? 114  PHE B CB  1 
ATOM   3668  C  CG  . PHE B 1 114 ? -6.877  45.496  150.861 1.00 58.23 ? 114  PHE B CG  1 
ATOM   3669  C  CD1 . PHE B 1 114 ? -7.029  46.750  151.428 1.00 61.87 ? 114  PHE B CD1 1 
ATOM   3670  C  CD2 . PHE B 1 114 ? -6.024  44.592  151.476 1.00 61.14 ? 114  PHE B CD2 1 
ATOM   3671  C  CE1 . PHE B 1 114 ? -6.338  47.099  152.594 1.00 62.94 ? 114  PHE B CE1 1 
ATOM   3672  C  CE2 . PHE B 1 114 ? -5.332  44.941  152.641 1.00 61.61 ? 114  PHE B CE2 1 
ATOM   3673  C  CZ  . PHE B 1 114 ? -5.493  46.196  153.193 1.00 60.95 ? 114  PHE B CZ  1 
ATOM   3674  N  N   . TYR B 1 115 ? -10.732 43.968  148.453 1.00 47.14 ? 115  TYR B N   1 
ATOM   3675  C  CA  . TYR B 1 115 ? -11.456 43.608  147.238 1.00 46.24 ? 115  TYR B CA  1 
ATOM   3676  C  C   . TYR B 1 115 ? -12.416 44.708  146.754 1.00 42.41 ? 115  TYR B C   1 
ATOM   3677  O  O   . TYR B 1 115 ? -12.346 45.134  145.594 1.00 43.12 ? 115  TYR B O   1 
ATOM   3678  C  CB  . TYR B 1 115 ? -12.229 42.312  147.440 1.00 41.57 ? 115  TYR B CB  1 
ATOM   3679  C  CG  . TYR B 1 115 ? -12.752 41.756  146.138 1.00 42.06 ? 115  TYR B CG  1 
ATOM   3680  C  CD1 . TYR B 1 115 ? -11.906 41.064  145.262 1.00 38.52 ? 115  TYR B CD1 1 
ATOM   3681  C  CD2 . TYR B 1 115 ? -14.098 41.927  145.768 1.00 38.64 ? 115  TYR B CD2 1 
ATOM   3682  C  CE1 . TYR B 1 115 ? -12.393 40.553  144.051 1.00 41.55 ? 115  TYR B CE1 1 
ATOM   3683  C  CE2 . TYR B 1 115 ? -14.586 41.420  144.568 1.00 36.47 ? 115  TYR B CE2 1 
ATOM   3684  C  CZ  . TYR B 1 115 ? -13.731 40.733  143.718 1.00 39.16 ? 115  TYR B CZ  1 
ATOM   3685  O  OH  . TYR B 1 115 ? -14.203 40.190  142.550 1.00 42.36 ? 115  TYR B OH  1 
ATOM   3686  N  N   . GLY B 1 116 ? -13.317 45.143  147.633 1.00 40.14 ? 116  GLY B N   1 
ATOM   3687  C  CA  . GLY B 1 116 ? -14.248 46.212  147.296 1.00 39.09 ? 116  GLY B CA  1 
ATOM   3688  C  C   . GLY B 1 116 ? -13.480 47.464  146.869 1.00 39.78 ? 116  GLY B C   1 
ATOM   3689  O  O   . GLY B 1 116 ? -13.842 48.116  145.900 1.00 38.51 ? 116  GLY B O   1 
ATOM   3690  N  N   . PRO B 1 117 ? -12.416 47.838  147.592 1.00 40.25 ? 117  PRO B N   1 
ATOM   3691  C  CA  . PRO B 1 117 ? -11.634 49.019  147.220 1.00 39.33 ? 117  PRO B CA  1 
ATOM   3692  C  C   . PRO B 1 117 ? -10.975 48.887  145.843 1.00 38.79 ? 117  PRO B C   1 
ATOM   3693  O  O   . PRO B 1 117 ? -10.794 49.890  145.148 1.00 40.83 ? 117  PRO B O   1 
ATOM   3694  C  CB  . PRO B 1 117 ? -10.606 49.118  148.348 1.00 41.35 ? 117  PRO B CB  1 
ATOM   3695  C  CG  . PRO B 1 117 ? -11.372 48.597  149.520 1.00 39.90 ? 117  PRO B CG  1 
ATOM   3696  C  CD  . PRO B 1 117 ? -12.076 47.390  148.956 1.00 38.02 ? 117  PRO B CD  1 
ATOM   3697  N  N   . SER B 1 118 ? -10.595 47.668  145.460 1.00 38.18 ? 118  SER B N   1 
ATOM   3698  C  CA  . SER B 1 118 ? -9.961  47.435  144.147 1.00 40.58 ? 118  SER B CA  1 
ATOM   3699  C  C   . SER B 1 118 ? -11.002 47.679  143.061 1.00 41.44 ? 118  SER B C   1 
ATOM   3700  O  O   . SER B 1 118 ? -10.757 48.403  142.099 1.00 40.60 ? 118  SER B O   1 
ATOM   3701  C  CB  . SER B 1 118 ? -9.434  45.997  144.016 1.00 37.76 ? 118  SER B CB  1 
ATOM   3702  O  OG  . SER B 1 118 ? -8.283  45.791  144.817 1.00 40.41 ? 118  SER B OG  1 
ATOM   3703  N  N   . LEU B 1 119 ? -12.167 47.068  143.244 1.00 42.06 ? 119  LEU B N   1 
ATOM   3704  C  CA  . LEU B 1 119 ? -13.279 47.209  142.326 1.00 40.70 ? 119  LEU B CA  1 
ATOM   3705  C  C   . LEU B 1 119 ? -13.595 48.701  142.156 1.00 40.59 ? 119  LEU B C   1 
ATOM   3706  O  O   . LEU B 1 119 ? -13.696 49.201  141.038 1.00 40.65 ? 119  LEU B O   1 
ATOM   3707  C  CB  . LEU B 1 119 ? -14.484 46.474  142.910 1.00 39.27 ? 119  LEU B CB  1 
ATOM   3708  C  CG  . LEU B 1 119 ? -15.221 45.410  142.090 1.00 43.50 ? 119  LEU B CG  1 
ATOM   3709  C  CD1 . LEU B 1 119 ? -14.331 44.851  140.985 1.00 40.68 ? 119  LEU B CD1 1 
ATOM   3710  C  CD2 . LEU B 1 119 ? -15.710 44.305  143.048 1.00 37.21 ? 119  LEU B CD2 1 
ATOM   3711  N  N   . ALA B 1 120 ? -13.729 49.404  143.276 1.00 38.42 ? 120  ALA B N   1 
ATOM   3712  C  CA  . ALA B 1 120 ? -14.051 50.823  143.275 1.00 36.84 ? 120  ALA B CA  1 
ATOM   3713  C  C   . ALA B 1 120 ? -13.008 51.647  142.542 1.00 36.98 ? 120  ALA B C   1 
ATOM   3714  O  O   . ALA B 1 120 ? -13.330 52.482  141.699 1.00 35.39 ? 120  ALA B O   1 
ATOM   3715  C  CB  . ALA B 1 120 ? -14.178 51.318  144.717 1.00 35.64 ? 120  ALA B CB  1 
ATOM   3716  N  N   . ILE B 1 121 ? -11.750 51.424  142.877 1.00 36.70 ? 121  ILE B N   1 
ATOM   3717  C  CA  . ILE B 1 121 ? -10.709 52.180  142.236 1.00 37.70 ? 121  ILE B CA  1 
ATOM   3718  C  C   . ILE B 1 121 ? -10.711 51.896  140.748 1.00 37.83 ? 121  ILE B C   1 
ATOM   3719  O  O   . ILE B 1 121 ? -10.441 52.789  139.961 1.00 43.48 ? 121  ILE B O   1 
ATOM   3720  C  CB  . ILE B 1 121 ? -9.323  51.885  142.879 1.00 38.81 ? 121  ILE B CB  1 
ATOM   3721  C  CG1 . ILE B 1 121 ? -9.314  52.439  144.294 1.00 38.14 ? 121  ILE B CG1 1 
ATOM   3722  C  CG2 . ILE B 1 121 ? -8.191  52.553  142.098 1.00 29.53 ? 121  ILE B CG2 1 
ATOM   3723  C  CD1 . ILE B 1 121 ? -8.103  52.021  145.084 1.00 43.00 ? 121  ILE B CD1 1 
ATOM   3724  N  N   . LEU B 1 122 ? -11.030 50.675  140.338 1.00 37.97 ? 122  LEU B N   1 
ATOM   3725  C  CA  . LEU B 1 122 ? -11.061 50.385  138.899 1.00 38.62 ? 122  LEU B CA  1 
ATOM   3726  C  C   . LEU B 1 122 ? -12.122 51.264  138.222 1.00 39.29 ? 122  LEU B C   1 
ATOM   3727  O  O   . LEU B 1 122 ? -11.844 51.961  137.241 1.00 41.77 ? 122  LEU B O   1 
ATOM   3728  C  CB  . LEU B 1 122 ? -11.355 48.907  138.630 1.00 38.32 ? 122  LEU B CB  1 
ATOM   3729  C  CG  . LEU B 1 122 ? -11.485 48.526  137.149 1.00 40.75 ? 122  LEU B CG  1 
ATOM   3730  C  CD1 . LEU B 1 122 ? -10.264 48.952  136.392 1.00 38.43 ? 122  LEU B CD1 1 
ATOM   3731  C  CD2 . LEU B 1 122 ? -11.678 47.025  137.023 1.00 42.54 ? 122  LEU B CD2 1 
ATOM   3732  N  N   . ALA B 1 123 ? -13.323 51.271  138.771 1.00 34.86 ? 123  ALA B N   1 
ATOM   3733  C  CA  . ALA B 1 123 ? -14.383 52.068  138.198 1.00 36.40 ? 123  ALA B CA  1 
ATOM   3734  C  C   . ALA B 1 123 ? -14.020 53.550  138.114 1.00 38.73 ? 123  ALA B C   1 
ATOM   3735  O  O   . ALA B 1 123 ? -14.209 54.213  137.071 1.00 36.18 ? 123  ALA B O   1 
ATOM   3736  C  CB  . ALA B 1 123 ? -15.647 51.895  139.022 1.00 37.99 ? 123  ALA B CB  1 
ATOM   3737  N  N   . LEU B 1 124 ? -13.522 54.057  139.233 1.00 38.01 ? 124  LEU B N   1 
ATOM   3738  C  CA  . LEU B 1 124 ? -13.144 55.447  139.358 1.00 37.12 ? 124  LEU B CA  1 
ATOM   3739  C  C   . LEU B 1 124 ? -12.040 55.778  138.389 1.00 37.35 ? 124  LEU B C   1 
ATOM   3740  O  O   . LEU B 1 124 ? -12.052 56.830  137.749 1.00 38.32 ? 124  LEU B O   1 
ATOM   3741  C  CB  . LEU B 1 124 ? -12.692 55.741  140.802 1.00 36.25 ? 124  LEU B CB  1 
ATOM   3742  C  CG  . LEU B 1 124 ? -13.632 56.413  141.815 1.00 37.83 ? 124  LEU B CG  1 
ATOM   3743  C  CD1 . LEU B 1 124 ? -15.145 56.247  141.504 1.00 35.96 ? 124  LEU B CD1 1 
ATOM   3744  C  CD2 . LEU B 1 124 ? -13.308 55.836  143.149 1.00 40.38 ? 124  LEU B CD2 1 
ATOM   3745  N  N   . CYS B 1 125 ? -11.081 54.882  138.268 1.00 36.82 ? 125  CYS B N   1 
ATOM   3746  C  CA  . CYS B 1 125 ? -9.975  55.151  137.378 1.00 40.92 ? 125  CYS B CA  1 
ATOM   3747  C  C   . CYS B 1 125 ? -10.486 55.285  135.937 1.00 41.48 ? 125  CYS B C   1 
ATOM   3748  O  O   . CYS B 1 125 ? -9.938  56.037  135.136 1.00 42.63 ? 125  CYS B O   1 
ATOM   3749  C  CB  . CYS B 1 125 ? -8.934  54.036  137.495 1.00 38.53 ? 125  CYS B CB  1 
ATOM   3750  S  SG  . CYS B 1 125 ? -7.599  54.164  136.271 1.00 47.77 ? 125  CYS B SG  1 
ATOM   3751  N  N   . GLN B 1 126 ? -11.546 54.563  135.612 1.00 41.30 ? 126  GLN B N   1 
ATOM   3752  C  CA  . GLN B 1 126 ? -12.091 54.608  134.272 1.00 39.46 ? 126  GLN B CA  1 
ATOM   3753  C  C   . GLN B 1 126 ? -12.844 55.887  133.960 1.00 40.71 ? 126  GLN B C   1 
ATOM   3754  O  O   . GLN B 1 126 ? -12.925 56.293  132.805 1.00 40.92 ? 126  GLN B O   1 
ATOM   3755  C  CB  . GLN B 1 126 ? -13.001 53.415  134.050 1.00 38.51 ? 126  GLN B CB  1 
ATOM   3756  C  CG  . GLN B 1 126 ? -12.260 52.125  133.830 1.00 37.56 ? 126  GLN B CG  1 
ATOM   3757  C  CD  . GLN B 1 126 ? -13.202 50.939  133.771 1.00 40.76 ? 126  GLN B CD  1 
ATOM   3758  O  OE1 . GLN B 1 126 ? -12.793 49.808  133.483 1.00 46.28 ? 126  GLN B OE1 1 
ATOM   3759  N  NE2 . GLN B 1 126 ? -14.472 51.188  134.044 1.00 40.50 ? 126  GLN B NE2 1 
ATOM   3760  N  N   . LYS B 1 127 ? -13.399 56.520  134.984 1.00 39.82 ? 127  LYS B N   1 
ATOM   3761  C  CA  . LYS B 1 127 ? -14.150 57.765  134.800 1.00 40.88 ? 127  LYS B CA  1 
ATOM   3762  C  C   . LYS B 1 127 ? -13.298 59.035  134.926 1.00 39.36 ? 127  LYS B C   1 
ATOM   3763  O  O   . LYS B 1 127 ? -13.556 60.039  134.275 1.00 40.24 ? 127  LYS B O   1 
ATOM   3764  C  CB  . LYS B 1 127 ? -15.302 57.835  135.809 1.00 39.76 ? 127  LYS B CB  1 
ATOM   3765  C  CG  . LYS B 1 127 ? -16.410 56.809  135.561 1.00 45.14 ? 127  LYS B CG  1 
ATOM   3766  C  CD  . LYS B 1 127 ? -17.286 57.186  134.356 1.00 48.03 ? 127  LYS B CD  1 
ATOM   3767  C  CE  . LYS B 1 127 ? -18.142 56.010  133.882 1.00 49.72 ? 127  LYS B CE  1 
ATOM   3768  N  NZ  . LYS B 1 127 ? -17.295 54.854  133.425 1.00 54.31 ? 127  LYS B NZ  1 
ATOM   3769  N  N   . ASN B 1 128 ? -12.285 58.999  135.775 1.00 39.36 ? 128  ASN B N   1 
ATOM   3770  C  CA  . ASN B 1 128 ? -11.427 60.159  135.967 1.00 36.35 ? 128  ASN B CA  1 
ATOM   3771  C  C   . ASN B 1 128 ? -10.175 59.653  136.643 1.00 36.05 ? 128  ASN B C   1 
ATOM   3772  O  O   . ASN B 1 128 ? -10.105 59.578  137.862 1.00 36.62 ? 128  ASN B O   1 
ATOM   3773  C  CB  . ASN B 1 128 ? -12.150 61.179  136.835 1.00 28.34 ? 128  ASN B CB  1 
ATOM   3774  C  CG  . ASN B 1 128 ? -11.417 62.484  136.942 1.00 34.14 ? 128  ASN B CG  1 
ATOM   3775  O  OD1 . ASN B 1 128 ? -12.021 63.483  137.329 1.00 38.74 ? 128  ASN B OD1 1 
ATOM   3776  N  ND2 . ASN B 1 128 ? -10.111 62.500  136.616 1.00 27.46 ? 128  ASN B ND2 1 
ATOM   3777  N  N   . SER B 1 129 ? -9.183  59.300  135.837 1.00 38.24 ? 129  SER B N   1 
ATOM   3778  C  CA  . SER B 1 129 ? -7.950  58.751  136.369 1.00 40.34 ? 129  SER B CA  1 
ATOM   3779  C  C   . SER B 1 129 ? -7.210  59.704  137.286 1.00 40.76 ? 129  SER B C   1 
ATOM   3780  O  O   . SER B 1 129 ? -6.686  59.298  138.318 1.00 44.34 ? 129  SER B O   1 
ATOM   3781  C  CB  . SER B 1 129 ? -7.044  58.301  135.222 1.00 39.86 ? 129  SER B CB  1 
ATOM   3782  O  OG  . SER B 1 129 ? -6.820  59.360  134.306 1.00 39.60 ? 129  SER B OG  1 
ATOM   3783  N  N   . GLU B 1 130 ? -7.175  60.976  136.933 1.00 43.45 ? 130  GLU B N   1 
ATOM   3784  C  CA  . GLU B 1 130 ? -6.450  61.946  137.763 1.00 45.28 ? 130  GLU B CA  1 
ATOM   3785  C  C   . GLU B 1 130 ? -7.077  62.122  139.141 1.00 42.71 ? 130  GLU B C   1 
ATOM   3786  O  O   . GLU B 1 130 ? -6.372  62.198  140.149 1.00 41.63 ? 130  GLU B O   1 
ATOM   3787  C  CB  . GLU B 1 130 ? -6.356  63.312  137.056 1.00 44.49 ? 130  GLU B CB  1 
ATOM   3788  C  CG  . GLU B 1 130 ? -5.477  64.276  137.777 1.00 48.57 ? 130  GLU B CG  1 
ATOM   3789  C  CD  . GLU B 1 130 ? -5.096  65.465  136.937 1.00 53.21 ? 130  GLU B CD  1 
ATOM   3790  O  OE1 . GLU B 1 130 ? -5.735  65.692  135.892 1.00 55.06 ? 130  GLU B OE1 1 
ATOM   3791  O  OE2 . GLU B 1 130 ? -4.154  66.180  137.328 1.00 57.03 ? 130  GLU B OE2 1 
ATOM   3792  N  N   . ALA B 1 131 ? -8.400  62.183  139.180 1.00 40.26 ? 131  ALA B N   1 
ATOM   3793  C  CA  . ALA B 1 131 ? -9.100  62.352  140.442 1.00 41.80 ? 131  ALA B CA  1 
ATOM   3794  C  C   . ALA B 1 131 ? -8.881  61.128  141.333 1.00 43.40 ? 131  ALA B C   1 
ATOM   3795  O  O   . ALA B 1 131 ? -8.967  61.210  142.559 1.00 43.60 ? 131  ALA B O   1 
ATOM   3796  C  CB  . ALA B 1 131 ? -10.585 62.551  140.191 1.00 39.31 ? 131  ALA B CB  1 
ATOM   3797  N  N   . THR B 1 132 ? -8.595  59.998  140.698 1.00 44.06 ? 132  THR B N   1 
ATOM   3798  C  CA  . THR B 1 132 ? -8.362  58.732  141.381 1.00 45.38 ? 132  THR B CA  1 
ATOM   3799  C  C   . THR B 1 132 ? -6.927  58.550  141.894 1.00 43.26 ? 132  THR B C   1 
ATOM   3800  O  O   . THR B 1 132 ? -6.724  57.846  142.877 1.00 45.08 ? 132  THR B O   1 
ATOM   3801  C  CB  . THR B 1 132 ? -8.746  57.538  140.443 1.00 47.87 ? 132  THR B CB  1 
ATOM   3802  O  OG1 . THR B 1 132 ? -10.135 57.635  140.130 1.00 52.58 ? 132  THR B OG1 1 
ATOM   3803  C  CG2 . THR B 1 132 ? -8.503  56.185  141.103 1.00 44.87 ? 132  THR B CG2 1 
ATOM   3804  N  N   . LEU B 1 133 ? -5.947  59.177  141.246 1.00 41.84 ? 133  LEU B N   1 
ATOM   3805  C  CA  . LEU B 1 133 ? -4.523  59.094  141.665 1.00 41.24 ? 133  LEU B CA  1 
ATOM   3806  C  C   . LEU B 1 133 ? -4.259  59.068  143.187 1.00 40.83 ? 133  LEU B C   1 
ATOM   3807  O  O   . LEU B 1 133 ? -3.663  58.113  143.702 1.00 41.71 ? 133  LEU B O   1 
ATOM   3808  C  CB  . LEU B 1 133 ? -3.713  60.259  141.068 1.00 36.87 ? 133  LEU B CB  1 
ATOM   3809  C  CG  . LEU B 1 133 ? -2.484  59.964  140.208 1.00 34.40 ? 133  LEU B CG  1 
ATOM   3810  C  CD1 . LEU B 1 133 ? -1.476  61.081  140.410 1.00 32.31 ? 133  LEU B CD1 1 
ATOM   3811  C  CD2 . LEU B 1 133 ? -1.840  58.634  140.575 1.00 31.91 ? 133  LEU B CD2 1 
ATOM   3812  N  N   . PRO B 1 134 ? -4.699  60.113  143.922 1.00 39.78 ? 134  PRO B N   1 
ATOM   3813  C  CA  . PRO B 1 134 ? -4.478  60.151  145.377 1.00 40.49 ? 134  PRO B CA  1 
ATOM   3814  C  C   . PRO B 1 134 ? -4.957  58.872  146.053 1.00 42.40 ? 134  PRO B C   1 
ATOM   3815  O  O   . PRO B 1 134 ? -4.225  58.258  146.835 1.00 46.45 ? 134  PRO B O   1 
ATOM   3816  C  CB  . PRO B 1 134 ? -5.299  61.364  145.839 1.00 39.25 ? 134  PRO B CB  1 
ATOM   3817  C  CG  . PRO B 1 134 ? -5.296  62.259  144.638 1.00 40.84 ? 134  PRO B CG  1 
ATOM   3818  C  CD  . PRO B 1 134 ? -5.535  61.251  143.496 1.00 38.20 ? 134  PRO B CD  1 
ATOM   3819  N  N   . ILE B 1 135 ? -6.192  58.480  145.757 1.00 37.28 ? 135  ILE B N   1 
ATOM   3820  C  CA  . ILE B 1 135 ? -6.756  57.284  146.345 1.00 33.30 ? 135  ILE B CA  1 
ATOM   3821  C  C   . ILE B 1 135 ? -5.978  56.023  145.996 1.00 36.18 ? 135  ILE B C   1 
ATOM   3822  O  O   . ILE B 1 135 ? -5.735  55.182  146.866 1.00 39.99 ? 135  ILE B O   1 
ATOM   3823  C  CB  . ILE B 1 135 ? -8.186  57.115  145.890 1.00 33.93 ? 135  ILE B CB  1 
ATOM   3824  C  CG1 . ILE B 1 135 ? -8.992  58.303  146.376 1.00 30.63 ? 135  ILE B CG1 1 
ATOM   3825  C  CG2 . ILE B 1 135 ? -8.746  55.791  146.374 1.00 28.51 ? 135  ILE B CG2 1 
ATOM   3826  C  CD1 . ILE B 1 135 ? -10.287 58.445  145.677 1.00 33.80 ? 135  ILE B CD1 1 
ATOM   3827  N  N   . ALA B 1 136 ? -5.577  55.880  144.737 1.00 32.31 ? 136  ALA B N   1 
ATOM   3828  C  CA  . ALA B 1 136 ? -4.845  54.684  144.344 1.00 36.07 ? 136  ALA B CA  1 
ATOM   3829  C  C   . ALA B 1 136 ? -3.440  54.629  144.945 1.00 38.51 ? 136  ALA B C   1 
ATOM   3830  O  O   . ALA B 1 136 ? -2.908  53.548  145.181 1.00 37.84 ? 136  ALA B O   1 
ATOM   3831  C  CB  . ALA B 1 136 ? -4.770  54.572  142.815 1.00 32.58 ? 136  ALA B CB  1 
ATOM   3832  N  N   . VAL B 1 137 ? -2.831  55.785  145.169 1.00 39.72 ? 137  VAL B N   1 
ATOM   3833  C  CA  . VAL B 1 137 ? -1.499  55.803  145.747 1.00 43.94 ? 137  VAL B CA  1 
ATOM   3834  C  C   . VAL B 1 137 ? -1.610  55.290  147.173 1.00 47.60 ? 137  VAL B C   1 
ATOM   3835  O  O   . VAL B 1 137 ? -0.838  54.427  147.620 1.00 50.15 ? 137  VAL B O   1 
ATOM   3836  C  CB  . VAL B 1 137 ? -0.912  57.232  145.776 1.00 44.43 ? 137  VAL B CB  1 
ATOM   3837  C  CG1 . VAL B 1 137 ? 0.226   57.312  146.804 1.00 40.91 ? 137  VAL B CG1 1 
ATOM   3838  C  CG2 . VAL B 1 137 ? -0.408  57.622  144.358 1.00 38.19 ? 137  VAL B CG2 1 
ATOM   3839  N  N   . ARG B 1 138 ? -2.584  55.829  147.883 1.00 46.79 ? 138  ARG B N   1 
ATOM   3840  C  CA  . ARG B 1 138 ? -2.818  55.442  149.246 1.00 49.08 ? 138  ARG B CA  1 
ATOM   3841  C  C   . ARG B 1 138 ? -3.032  53.915  149.257 1.00 50.83 ? 138  ARG B C   1 
ATOM   3842  O  O   . ARG B 1 138 ? -2.387  53.171  150.007 1.00 52.95 ? 138  ARG B O   1 
ATOM   3843  C  CB  . ARG B 1 138 ? -4.047  56.190  149.738 1.00 51.90 ? 138  ARG B CB  1 
ATOM   3844  C  CG  . ARG B 1 138 ? -4.133  56.350  151.226 1.00 58.27 ? 138  ARG B CG  1 
ATOM   3845  C  CD  . ARG B 1 138 ? -5.355  57.179  151.594 1.00 63.26 ? 138  ARG B CD  1 
ATOM   3846  N  NE  . ARG B 1 138 ? -5.345  58.471  150.906 1.00 63.34 ? 138  ARG B NE  1 
ATOM   3847  C  CZ  . ARG B 1 138 ? -6.405  58.998  150.295 1.00 63.76 ? 138  ARG B CZ  1 
ATOM   3848  N  NH1 . ARG B 1 138 ? -7.575  58.348  150.278 1.00 60.32 ? 138  ARG B NH1 1 
ATOM   3849  N  NH2 . ARG B 1 138 ? -6.289  60.175  149.697 1.00 61.36 ? 138  ARG B NH2 1 
ATOM   3850  N  N   . PHE B 1 139 ? -3.918  53.455  148.387 1.00 49.89 ? 139  PHE B N   1 
ATOM   3851  C  CA  . PHE B 1 139 ? -4.241  52.036  148.282 1.00 48.91 ? 139  PHE B CA  1 
ATOM   3852  C  C   . PHE B 1 139 ? -3.004  51.156  148.010 1.00 49.39 ? 139  PHE B C   1 
ATOM   3853  O  O   . PHE B 1 139 ? -2.828  50.102  148.624 1.00 50.12 ? 139  PHE B O   1 
ATOM   3854  C  CB  . PHE B 1 139 ? -5.283  51.868  147.177 1.00 46.22 ? 139  PHE B CB  1 
ATOM   3855  C  CG  . PHE B 1 139 ? -5.673  50.452  146.912 1.00 45.29 ? 139  PHE B CG  1 
ATOM   3856  C  CD1 . PHE B 1 139 ? -6.494  49.766  147.813 1.00 44.55 ? 139  PHE B CD1 1 
ATOM   3857  C  CD2 . PHE B 1 139 ? -5.245  49.806  145.743 1.00 41.48 ? 139  PHE B CD2 1 
ATOM   3858  C  CE1 . PHE B 1 139 ? -6.892  48.449  147.558 1.00 44.72 ? 139  PHE B CE1 1 
ATOM   3859  C  CE2 . PHE B 1 139 ? -5.630  48.489  145.471 1.00 43.03 ? 139  PHE B CE2 1 
ATOM   3860  C  CZ  . PHE B 1 139 ? -6.461  47.804  146.383 1.00 45.04 ? 139  PHE B CZ  1 
ATOM   3861  N  N   . ALA B 1 140 ? -2.148  51.588  147.091 1.00 48.42 ? 140  ALA B N   1 
ATOM   3862  C  CA  . ALA B 1 140 ? -0.939  50.836  146.748 1.00 49.25 ? 140  ALA B CA  1 
ATOM   3863  C  C   . ALA B 1 140 ? -0.033  50.657  147.968 1.00 49.92 ? 140  ALA B C   1 
ATOM   3864  O  O   . ALA B 1 140 ? 0.417   49.551  148.263 1.00 47.36 ? 140  ALA B O   1 
ATOM   3865  C  CB  . ALA B 1 140 ? -0.170  51.553  145.621 1.00 46.07 ? 140  ALA B CB  1 
ATOM   3866  N  N   . LYS B 1 141 ? 0.240   51.760  148.660 1.00 52.29 ? 141  LYS B N   1 
ATOM   3867  C  CA  . LYS B 1 141 ? 1.074   51.729  149.851 1.00 52.39 ? 141  LYS B CA  1 
ATOM   3868  C  C   . LYS B 1 141 ? 0.465   50.771  150.868 1.00 53.95 ? 141  LYS B C   1 
ATOM   3869  O  O   . LYS B 1 141 ? 1.110   49.812  151.296 1.00 54.81 ? 141  LYS B O   1 
ATOM   3870  C  CB  . LYS B 1 141 ? 1.198   53.135  150.439 1.00 47.53 ? 141  LYS B CB  1 
ATOM   3871  C  CG  . LYS B 1 141 ? 2.137   53.969  149.641 1.00 46.84 ? 141  LYS B CG  1 
ATOM   3872  C  CD  . LYS B 1 141 ? 2.125   55.386  150.110 1.00 49.45 ? 141  LYS B CD  1 
ATOM   3873  C  CE  . LYS B 1 141 ? 3.025   56.230  149.211 1.00 51.62 ? 141  LYS B CE  1 
ATOM   3874  N  NZ  . LYS B 1 141 ? 2.967   57.691  149.548 1.00 56.71 ? 141  LYS B NZ  1 
ATOM   3875  N  N   . THR B 1 142 ? -0.784  51.033  151.233 1.00 54.19 ? 142  THR B N   1 
ATOM   3876  C  CA  . THR B 1 142 ? -1.501  50.208  152.175 1.00 53.64 ? 142  THR B CA  1 
ATOM   3877  C  C   . THR B 1 142 ? -1.388  48.741  151.796 1.00 55.66 ? 142  THR B C   1 
ATOM   3878  O  O   . THR B 1 142 ? -1.213  47.875  152.651 1.00 57.36 ? 142  THR B O   1 
ATOM   3879  C  CB  . THR B 1 142 ? -2.974  50.616  152.202 1.00 54.45 ? 142  THR B CB  1 
ATOM   3880  O  OG1 . THR B 1 142 ? -3.123  51.749  153.059 1.00 53.92 ? 142  THR B OG1 1 
ATOM   3881  C  CG2 . THR B 1 142 ? -3.859  49.469  152.696 1.00 57.08 ? 142  THR B CG2 1 
ATOM   3882  N  N   . LEU B 1 143 ? -1.490  48.470  150.501 1.00 57.10 ? 143  LEU B N   1 
ATOM   3883  C  CA  . LEU B 1 143 ? -1.428  47.111  149.981 1.00 57.29 ? 143  LEU B CA  1 
ATOM   3884  C  C   . LEU B 1 143 ? -0.033  46.538  150.160 1.00 57.54 ? 143  LEU B C   1 
ATOM   3885  O  O   . LEU B 1 143 ? 0.150   45.375  150.495 1.00 57.65 ? 143  LEU B O   1 
ATOM   3886  C  CB  . LEU B 1 143 ? -1.816  47.129  148.508 1.00 57.37 ? 143  LEU B CB  1 
ATOM   3887  C  CG  . LEU B 1 143 ? -2.447  45.848  147.970 1.00 60.05 ? 143  LEU B CG  1 
ATOM   3888  C  CD1 . LEU B 1 143 ? -3.443  45.263  148.967 1.00 61.41 ? 143  LEU B CD1 1 
ATOM   3889  C  CD2 . LEU B 1 143 ? -3.133  46.179  146.677 1.00 59.30 ? 143  LEU B CD2 1 
ATOM   3890  N  N   . LEU B 1 144 ? 0.953   47.384  149.940 1.00 59.26 ? 144  LEU B N   1 
ATOM   3891  C  CA  . LEU B 1 144 ? 2.343   47.005  150.082 1.00 60.39 ? 144  LEU B CA  1 
ATOM   3892  C  C   . LEU B 1 144 ? 2.641   46.597  151.538 1.00 63.53 ? 144  LEU B C   1 
ATOM   3893  O  O   . LEU B 1 144 ? 3.122   45.492  151.800 1.00 62.99 ? 144  LEU B O   1 
ATOM   3894  C  CB  . LEU B 1 144 ? 3.218   48.193  149.679 1.00 57.65 ? 144  LEU B CB  1 
ATOM   3895  C  CG  . LEU B 1 144 ? 4.540   47.846  149.015 1.00 57.46 ? 144  LEU B CG  1 
ATOM   3896  C  CD1 . LEU B 1 144 ? 4.300   46.765  147.954 1.00 56.68 ? 144  LEU B CD1 1 
ATOM   3897  C  CD2 . LEU B 1 144 ? 5.157   49.097  148.404 1.00 54.46 ? 144  LEU B CD2 1 
ATOM   3898  N  N   . ALA B 1 145 ? 2.340   47.498  152.474 1.00 64.71 ? 145  ALA B N   1 
ATOM   3899  C  CA  . ALA B 1 145 ? 2.574   47.282  153.900 1.00 64.68 ? 145  ALA B CA  1 
ATOM   3900  C  C   . ALA B 1 145 ? 1.810   46.099  154.500 1.00 68.75 ? 145  ALA B C   1 
ATOM   3901  O  O   . ALA B 1 145 ? 2.273   45.490  155.471 1.00 71.17 ? 145  ALA B O   1 
ATOM   3902  C  CB  . ALA B 1 145 ? 2.223   48.540  154.664 1.00 62.83 ? 145  ALA B CB  1 
ATOM   3903  N  N   . ASN B 1 146 ? 0.644   45.775  153.941 1.00 69.33 ? 146  ASN B N   1 
ATOM   3904  C  CA  . ASN B 1 146 ? -0.155  44.675  154.459 1.00 68.57 ? 146  ASN B CA  1 
ATOM   3905  C  C   . ASN B 1 146 ? 0.647   43.390  154.461 1.00 70.27 ? 146  ASN B C   1 
ATOM   3906  O  O   . ASN B 1 146 ? 1.400   43.116  153.527 1.00 70.29 ? 146  ASN B O   1 
ATOM   3907  C  CB  . ASN B 1 146 ? -1.402  44.482  153.619 1.00 70.45 ? 146  ASN B CB  1 
ATOM   3908  C  CG  . ASN B 1 146 ? -2.376  43.523  154.255 1.00 71.08 ? 146  ASN B CG  1 
ATOM   3909  O  OD1 . ASN B 1 146 ? -3.035  43.851  155.247 1.00 69.13 ? 146  ASN B OD1 1 
ATOM   3910  N  ND2 . ASN B 1 146 ? -2.469  42.320  153.693 1.00 73.52 ? 146  ASN B ND2 1 
ATOM   3911  N  N   . SER B 1 147 ? 0.477   42.599  155.517 1.00 72.64 ? 147  SER B N   1 
ATOM   3912  C  CA  . SER B 1 147 ? 1.204   41.339  155.663 1.00 72.31 ? 147  SER B CA  1 
ATOM   3913  C  C   . SER B 1 147 ? 0.276   40.132  155.562 1.00 70.52 ? 147  SER B C   1 
ATOM   3914  O  O   . SER B 1 147 ? 0.706   39.041  155.196 1.00 72.24 ? 147  SER B O   1 
ATOM   3915  C  CB  . SER B 1 147 ? 1.921   41.315  157.014 1.00 74.65 ? 147  SER B CB  1 
ATOM   3916  O  OG  . SER B 1 147 ? 2.675   42.501  157.210 1.00 76.06 ? 147  SER B OG  1 
ATOM   3917  N  N   . SER B 1 148 ? -0.992  40.341  155.897 1.00 67.32 ? 148  SER B N   1 
ATOM   3918  C  CA  . SER B 1 148 ? -2.007  39.294  155.849 1.00 65.27 ? 148  SER B CA  1 
ATOM   3919  C  C   . SER B 1 148 ? -1.853  38.327  154.668 1.00 63.73 ? 148  SER B C   1 
ATOM   3920  O  O   . SER B 1 148 ? -1.413  38.720  153.588 1.00 64.84 ? 148  SER B O   1 
ATOM   3921  C  CB  . SER B 1 148 ? -3.391  39.943  155.807 1.00 64.34 ? 148  SER B CB  1 
ATOM   3922  O  OG  . SER B 1 148 ? -4.387  38.977  155.523 1.00 67.50 ? 148  SER B OG  1 
ATOM   3923  N  N   . PRO B 1 149 ? -2.218  37.044  154.865 1.00 62.40 ? 149  PRO B N   1 
ATOM   3924  C  CA  . PRO B 1 149 ? -2.130  36.002  153.830 1.00 60.22 ? 149  PRO B CA  1 
ATOM   3925  C  C   . PRO B 1 149 ? -2.703  36.464  152.494 1.00 60.16 ? 149  PRO B C   1 
ATOM   3926  O  O   . PRO B 1 149 ? -3.690  37.187  152.452 1.00 63.77 ? 149  PRO B O   1 
ATOM   3927  C  CB  . PRO B 1 149 ? -2.932  34.846  154.433 1.00 59.43 ? 149  PRO B CB  1 
ATOM   3928  C  CG  . PRO B 1 149 ? -2.673  34.991  155.890 1.00 60.95 ? 149  PRO B CG  1 
ATOM   3929  C  CD  . PRO B 1 149 ? -2.778  36.493  156.115 1.00 61.69 ? 149  PRO B CD  1 
ATOM   3930  N  N   . PHE B 1 150 ? -2.087  36.027  151.405 1.00 59.05 ? 150  PHE B N   1 
ATOM   3931  C  CA  . PHE B 1 150 ? -2.515  36.405  150.064 1.00 58.66 ? 150  PHE B CA  1 
ATOM   3932  C  C   . PHE B 1 150 ? -3.825  35.781  149.579 1.00 60.03 ? 150  PHE B C   1 
ATOM   3933  O  O   . PHE B 1 150 ? -4.054  34.581  149.757 1.00 62.31 ? 150  PHE B O   1 
ATOM   3934  C  CB  . PHE B 1 150 ? -1.420  36.048  149.077 1.00 55.32 ? 150  PHE B CB  1 
ATOM   3935  C  CG  . PHE B 1 150 ? -1.750  36.394  147.672 1.00 55.66 ? 150  PHE B CG  1 
ATOM   3936  C  CD1 . PHE B 1 150 ? -1.752  37.726  147.247 1.00 53.55 ? 150  PHE B CD1 1 
ATOM   3937  C  CD2 . PHE B 1 150 ? -2.034  35.388  146.748 1.00 57.83 ? 150  PHE B CD2 1 
ATOM   3938  C  CE1 . PHE B 1 150 ? -2.024  38.054  145.916 1.00 51.60 ? 150  PHE B CE1 1 
ATOM   3939  C  CE2 . PHE B 1 150 ? -2.309  35.703  145.409 1.00 57.59 ? 150  PHE B CE2 1 
ATOM   3940  C  CZ  . PHE B 1 150 ? -2.302  37.043  144.994 1.00 55.55 ? 150  PHE B CZ  1 
ATOM   3941  N  N   . ASN B 1 151 ? -4.663  36.603  148.939 1.00 59.21 ? 151  ASN B N   1 
ATOM   3942  C  CA  . ASN B 1 151 ? -5.948  36.158  148.391 1.00 57.59 ? 151  ASN B CA  1 
ATOM   3943  C  C   . ASN B 1 151 ? -5.996  36.398  146.865 1.00 54.89 ? 151  ASN B C   1 
ATOM   3944  O  O   . ASN B 1 151 ? -6.024  37.537  146.407 1.00 54.09 ? 151  ASN B O   1 
ATOM   3945  C  CB  . ASN B 1 151 ? -7.095  36.893  149.087 1.00 58.92 ? 151  ASN B CB  1 
ATOM   3946  C  CG  . ASN B 1 151 ? -8.403  36.712  148.376 1.00 64.34 ? 151  ASN B CG  1 
ATOM   3947  O  OD1 . ASN B 1 151 ? -8.733  35.607  147.928 1.00 71.26 ? 151  ASN B OD1 1 
ATOM   3948  N  ND2 . ASN B 1 151 ? -9.163  37.792  148.258 1.00 65.87 ? 151  ASN B ND2 1 
ATOM   3949  N  N   . VAL B 1 152 ? -6.002  35.315  146.091 1.00 52.29 ? 152  VAL B N   1 
ATOM   3950  C  CA  . VAL B 1 152 ? -6.010  35.393  144.631 1.00 52.23 ? 152  VAL B CA  1 
ATOM   3951  C  C   . VAL B 1 152 ? -6.973  36.430  144.085 1.00 49.35 ? 152  VAL B C   1 
ATOM   3952  O  O   . VAL B 1 152 ? -6.582  37.248  143.262 1.00 43.61 ? 152  VAL B O   1 
ATOM   3953  C  CB  . VAL B 1 152 ? -6.376  34.036  143.957 1.00 53.81 ? 152  VAL B CB  1 
ATOM   3954  C  CG1 . VAL B 1 152 ? -6.129  34.120  142.452 1.00 53.17 ? 152  VAL B CG1 1 
ATOM   3955  C  CG2 . VAL B 1 152 ? -5.571  32.937  144.537 1.00 56.58 ? 152  VAL B CG2 1 
ATOM   3956  N  N   . ASP B 1 153 ? -8.227  36.367  144.530 1.00 49.65 ? 153  ASP B N   1 
ATOM   3957  C  CA  . ASP B 1 153 ? -9.259  37.303  144.096 1.00 49.99 ? 153  ASP B CA  1 
ATOM   3958  C  C   . ASP B 1 153 ? -8.854  38.762  144.268 1.00 48.03 ? 153  ASP B C   1 
ATOM   3959  O  O   . ASP B 1 153 ? -8.805  39.526  143.300 1.00 47.83 ? 153  ASP B O   1 
ATOM   3960  C  CB  . ASP B 1 153 ? -10.548 37.038  144.856 1.00 52.80 ? 153  ASP B CB  1 
ATOM   3961  C  CG  . ASP B 1 153 ? -11.241 35.797  144.370 1.00 61.19 ? 153  ASP B CG  1 
ATOM   3962  O  OD1 . ASP B 1 153 ? -10.812 35.287  143.316 1.00 68.94 ? 153  ASP B OD1 1 
ATOM   3963  O  OD2 . ASP B 1 153 ? -12.208 35.329  145.012 1.00 64.52 ? 153  ASP B OD2 1 
ATOM   3964  N  N   . THR B 1 154 ? -8.569  39.147  145.502 1.00 43.90 ? 154  THR B N   1 
ATOM   3965  C  CA  . THR B 1 154 ? -8.161  40.501  145.763 1.00 40.83 ? 154  THR B CA  1 
ATOM   3966  C  C   . THR B 1 154 ? -6.937  40.815  144.915 1.00 40.97 ? 154  THR B C   1 
ATOM   3967  O  O   . THR B 1 154 ? -6.831  41.912  144.363 1.00 41.35 ? 154  THR B O   1 
ATOM   3968  C  CB  . THR B 1 154 ? -7.852  40.697  147.264 1.00 40.94 ? 154  THR B CB  1 
ATOM   3969  O  OG1 . THR B 1 154 ? -9.086  40.720  147.989 1.00 37.57 ? 154  THR B OG1 1 
ATOM   3970  C  CG2 . THR B 1 154 ? -7.092  42.008  147.511 1.00 41.47 ? 154  THR B CG2 1 
ATOM   3971  N  N   . GLY B 1 155 ? -6.012  39.864  144.811 1.00 37.79 ? 155  GLY B N   1 
ATOM   3972  C  CA  . GLY B 1 155 ? -4.831  40.093  143.994 1.00 40.21 ? 155  GLY B CA  1 
ATOM   3973  C  C   . GLY B 1 155 ? -5.162  40.398  142.529 1.00 40.63 ? 155  GLY B C   1 
ATOM   3974  O  O   . GLY B 1 155 ? -4.564  41.275  141.920 1.00 38.70 ? 155  GLY B O   1 
ATOM   3975  N  N   . ALA B 1 156 ? -6.131  39.678  141.979 1.00 40.81 ? 156  ALA B N   1 
ATOM   3976  C  CA  . ALA B 1 156 ? -6.557  39.859  140.607 1.00 42.34 ? 156  ALA B CA  1 
ATOM   3977  C  C   . ALA B 1 156 ? -7.216  41.224  140.427 1.00 43.29 ? 156  ALA B C   1 
ATOM   3978  O  O   . ALA B 1 156 ? -6.857  42.003  139.547 1.00 43.73 ? 156  ALA B O   1 
ATOM   3979  C  CB  . ALA B 1 156 ? -7.526  38.759  140.242 1.00 41.12 ? 156  ALA B CB  1 
ATOM   3980  N  N   . MET B 1 157 ? -8.181  41.529  141.274 1.00 43.89 ? 157  MET B N   1 
ATOM   3981  C  CA  . MET B 1 157 ? -8.867  42.808  141.155 1.00 44.90 ? 157  MET B CA  1 
ATOM   3982  C  C   . MET B 1 157 ? -7.921  43.996  141.370 1.00 43.55 ? 157  MET B C   1 
ATOM   3983  O  O   . MET B 1 157 ? -8.043  45.047  140.723 1.00 39.41 ? 157  MET B O   1 
ATOM   3984  C  CB  . MET B 1 157 ? -10.027 42.883  142.159 1.00 44.76 ? 157  MET B CB  1 
ATOM   3985  C  CG  . MET B 1 157 ? -11.096 43.886  141.748 1.00 49.63 ? 157  MET B CG  1 
ATOM   3986  S  SD  . MET B 1 157 ? -11.568 43.599  140.031 1.00 51.02 ? 157  MET B SD  1 
ATOM   3987  C  CE  . MET B 1 157 ? -12.172 41.874  140.144 1.00 51.99 ? 157  MET B CE  1 
ATOM   3988  N  N   . ALA B 1 158 ? -6.988  43.828  142.298 1.00 41.65 ? 158  ALA B N   1 
ATOM   3989  C  CA  . ALA B 1 158 ? -6.069  44.896  142.594 1.00 39.14 ? 158  ALA B CA  1 
ATOM   3990  C  C   . ALA B 1 158 ? -5.168  45.163  141.412 1.00 39.50 ? 158  ALA B C   1 
ATOM   3991  O  O   . ALA B 1 158 ? -4.855  46.326  141.140 1.00 38.08 ? 158  ALA B O   1 
ATOM   3992  C  CB  . ALA B 1 158 ? -5.253  44.561  143.807 1.00 36.37 ? 158  ALA B CB  1 
ATOM   3993  N  N   . THR B 1 159 ? -4.745  44.118  140.697 1.00 40.34 ? 159  THR B N   1 
ATOM   3994  C  CA  . THR B 1 159 ? -3.859  44.385  139.577 1.00 40.38 ? 159  THR B CA  1 
ATOM   3995  C  C   . THR B 1 159 ? -4.642  45.092  138.491 1.00 41.47 ? 159  THR B C   1 
ATOM   3996  O  O   . THR B 1 159 ? -4.125  46.023  137.854 1.00 41.54 ? 159  THR B O   1 
ATOM   3997  C  CB  . THR B 1 159 ? -3.161  43.124  138.990 1.00 42.77 ? 159  THR B CB  1 
ATOM   3998  O  OG1 . THR B 1 159 ? -3.861  42.690  137.828 1.00 46.32 ? 159  THR B OG1 1 
ATOM   3999  C  CG2 . THR B 1 159 ? -3.071  42.013  139.997 1.00 37.56 ? 159  THR B CG2 1 
ATOM   4000  N  N   . LEU B 1 160 ? -5.889  44.680  138.278 1.00 38.78 ? 160  LEU B N   1 
ATOM   4001  C  CA  . LEU B 1 160 ? -6.700  45.373  137.280 1.00 37.87 ? 160  LEU B CA  1 
ATOM   4002  C  C   . LEU B 1 160 ? -6.803  46.862  137.652 1.00 35.79 ? 160  LEU B C   1 
ATOM   4003  O  O   . LEU B 1 160 ? -6.571  47.732  136.820 1.00 38.43 ? 160  LEU B O   1 
ATOM   4004  C  CB  . LEU B 1 160 ? -8.111  44.773  137.175 1.00 37.05 ? 160  LEU B CB  1 
ATOM   4005  C  CG  . LEU B 1 160 ? -8.247  43.358  136.598 1.00 38.71 ? 160  LEU B CG  1 
ATOM   4006  C  CD1 . LEU B 1 160 ? -9.709  42.937  136.579 1.00 37.29 ? 160  LEU B CD1 1 
ATOM   4007  C  CD2 . LEU B 1 160 ? -7.670  43.338  135.207 1.00 40.61 ? 160  LEU B CD2 1 
ATOM   4008  N  N   . ALA B 1 161 ? -7.138  47.162  138.899 1.00 33.80 ? 161  ALA B N   1 
ATOM   4009  C  CA  . ALA B 1 161 ? -7.259  48.559  139.317 1.00 33.17 ? 161  ALA B CA  1 
ATOM   4010  C  C   . ALA B 1 161 ? -5.952  49.291  139.167 1.00 35.08 ? 161  ALA B C   1 
ATOM   4011  O  O   . ALA B 1 161 ? -5.900  50.372  138.594 1.00 38.88 ? 161  ALA B O   1 
ATOM   4012  C  CB  . ALA B 1 161 ? -7.721  48.652  140.747 1.00 33.60 ? 161  ALA B CB  1 
ATOM   4013  N  N   . LEU B 1 162 ? -4.876  48.702  139.663 1.00 35.48 ? 162  LEU B N   1 
ATOM   4014  C  CA  . LEU B 1 162 ? -3.593  49.362  139.565 1.00 34.95 ? 162  LEU B CA  1 
ATOM   4015  C  C   . LEU B 1 162 ? -3.045  49.430  138.139 1.00 36.40 ? 162  LEU B C   1 
ATOM   4016  O  O   . LEU B 1 162 ? -2.265  50.320  137.824 1.00 36.49 ? 162  LEU B O   1 
ATOM   4017  C  CB  . LEU B 1 162 ? -2.601  48.702  140.528 1.00 36.91 ? 162  LEU B CB  1 
ATOM   4018  C  CG  . LEU B 1 162 ? -2.379  49.350  141.913 1.00 37.94 ? 162  LEU B CG  1 
ATOM   4019  C  CD1 . LEU B 1 162 ? -3.393  50.429  142.217 1.00 32.00 ? 162  LEU B CD1 1 
ATOM   4020  C  CD2 . LEU B 1 162 ? -2.434  48.255  142.974 1.00 40.55 ? 162  LEU B CD2 1 
ATOM   4021  N  N   . THR B 1 163 ? -3.435  48.499  137.271 1.00 38.18 ? 163  THR B N   1 
ATOM   4022  C  CA  . THR B 1 163 ? -2.973  48.555  135.878 1.00 39.52 ? 163  THR B CA  1 
ATOM   4023  C  C   . THR B 1 163 ? -3.699  49.741  135.203 1.00 40.58 ? 163  THR B C   1 
ATOM   4024  O  O   . THR B 1 163 ? -3.095  50.516  134.458 1.00 38.43 ? 163  THR B O   1 
ATOM   4025  C  CB  . THR B 1 163 ? -3.286  47.236  135.097 1.00 42.85 ? 163  THR B CB  1 
ATOM   4026  O  OG1 . THR B 1 163 ? -2.526  46.155  135.654 1.00 38.66 ? 163  THR B OG1 1 
ATOM   4027  C  CG2 . THR B 1 163 ? -2.943  47.384  133.618 1.00 35.57 ? 163  THR B CG2 1 
ATOM   4028  N  N   . CYS B 1 164 ? -4.992  49.890  135.464 1.00 38.47 ? 164  CYS B N   1 
ATOM   4029  C  CA  . CYS B 1 164 ? -5.688  51.029  134.892 1.00 42.70 ? 164  CYS B CA  1 
ATOM   4030  C  C   . CYS B 1 164 ? -4.878  52.288  135.230 1.00 40.37 ? 164  CYS B C   1 
ATOM   4031  O  O   . CYS B 1 164 ? -4.526  53.049  134.350 1.00 43.41 ? 164  CYS B O   1 
ATOM   4032  C  CB  . CYS B 1 164 ? -7.121  51.156  135.446 1.00 45.15 ? 164  CYS B CB  1 
ATOM   4033  S  SG  . CYS B 1 164 ? -8.006  52.664  134.887 1.00 53.15 ? 164  CYS B SG  1 
ATOM   4034  N  N   . MET B 1 165 ? -4.571  52.496  136.504 1.00 41.00 ? 165  MET B N   1 
ATOM   4035  C  CA  . MET B 1 165 ? -3.797  53.678  136.936 1.00 43.02 ? 165  MET B CA  1 
ATOM   4036  C  C   . MET B 1 165 ? -2.387  53.791  136.348 1.00 40.09 ? 165  MET B C   1 
ATOM   4037  O  O   . MET B 1 165 ? -1.915  54.868  135.998 1.00 37.98 ? 165  MET B O   1 
ATOM   4038  C  CB  . MET B 1 165 ? -3.659  53.698  138.464 1.00 40.59 ? 165  MET B CB  1 
ATOM   4039  C  CG  . MET B 1 165 ? -4.952  53.952  139.173 1.00 43.48 ? 165  MET B CG  1 
ATOM   4040  S  SD  . MET B 1 165 ? -5.661  55.519  138.682 1.00 46.97 ? 165  MET B SD  1 
ATOM   4041  C  CE  . MET B 1 165 ? -4.567  56.642  139.349 1.00 42.03 ? 165  MET B CE  1 
ATOM   4042  N  N   . TYR B 1 166 ? -1.709  52.662  136.295 1.00 36.78 ? 166  TYR B N   1 
ATOM   4043  C  CA  . TYR B 1 166 ? -0.362  52.607  135.793 1.00 36.77 ? 166  TYR B CA  1 
ATOM   4044  C  C   . TYR B 1 166 ? -0.268  53.209  134.417 1.00 39.71 ? 166  TYR B C   1 
ATOM   4045  O  O   . TYR B 1 166 ? 0.733   53.827  134.080 1.00 38.89 ? 166  TYR B O   1 
ATOM   4046  C  CB  . TYR B 1 166 ? 0.055   51.162  135.710 1.00 39.52 ? 166  TYR B CB  1 
ATOM   4047  C  CG  . TYR B 1 166 ? 1.460   50.940  135.237 1.00 43.85 ? 166  TYR B CG  1 
ATOM   4048  C  CD1 . TYR B 1 166 ? 2.540   51.049  136.123 1.00 45.33 ? 166  TYR B CD1 1 
ATOM   4049  C  CD2 . TYR B 1 166 ? 1.712   50.523  133.929 1.00 43.45 ? 166  TYR B CD2 1 
ATOM   4050  C  CE1 . TYR B 1 166 ? 3.834   50.731  135.721 1.00 44.52 ? 166  TYR B CE1 1 
ATOM   4051  C  CE2 . TYR B 1 166 ? 3.001   50.200  133.515 1.00 44.80 ? 166  TYR B CE2 1 
ATOM   4052  C  CZ  . TYR B 1 166 ? 4.054   50.299  134.421 1.00 47.28 ? 166  TYR B CZ  1 
ATOM   4053  O  OH  . TYR B 1 166 ? 5.308   49.901  134.035 1.00 49.50 ? 166  TYR B OH  1 
ATOM   4054  N  N   . ASN B 1 167 ? -1.312  53.006  133.615 1.00 38.78 ? 167  ASN B N   1 
ATOM   4055  C  CA  . ASN B 1 167 ? -1.318  53.491  132.266 1.00 37.69 ? 167  ASN B CA  1 
ATOM   4056  C  C   . ASN B 1 167 ? -1.894  54.892  132.101 1.00 41.12 ? 167  ASN B C   1 
ATOM   4057  O  O   . ASN B 1 167 ? -1.881  55.434  130.996 1.00 44.16 ? 167  ASN B O   1 
ATOM   4058  C  CB  . ASN B 1 167 ? -2.078  52.516  131.377 1.00 41.69 ? 167  ASN B CB  1 
ATOM   4059  C  CG  . ASN B 1 167 ? -1.406  51.167  131.281 1.00 45.49 ? 167  ASN B CG  1 
ATOM   4060  O  OD1 . ASN B 1 167 ? -0.182  51.083  131.277 1.00 46.40 ? 167  ASN B OD1 1 
ATOM   4061  N  ND2 . ASN B 1 167 ? -2.208  50.097  131.178 1.00 46.56 ? 167  ASN B ND2 1 
ATOM   4062  N  N   . LYS B 1 168 ? -2.397  55.487  133.177 1.00 38.58 ? 168  LYS B N   1 
ATOM   4063  C  CA  . LYS B 1 168 ? -2.976  56.823  133.081 1.00 37.03 ? 168  LYS B CA  1 
ATOM   4064  C  C   . LYS B 1 168 ? -2.291  57.827  133.978 1.00 39.72 ? 168  LYS B C   1 
ATOM   4065  O  O   . LYS B 1 168 ? -2.947  58.729  134.504 1.00 39.79 ? 168  LYS B O   1 
ATOM   4066  C  CB  . LYS B 1 168 ? -4.473  56.823  133.438 1.00 35.54 ? 168  LYS B CB  1 
ATOM   4067  C  CG  . LYS B 1 168 ? -5.404  56.142  132.428 1.00 40.00 ? 168  LYS B CG  1 
ATOM   4068  C  CD  . LYS B 1 168 ? -5.406  56.817  131.061 1.00 41.81 ? 168  LYS B CD  1 
ATOM   4069  C  CE  . LYS B 1 168 ? -6.417  56.144  130.099 1.00 47.35 ? 168  LYS B CE  1 
ATOM   4070  N  NZ  . LYS B 1 168 ? -6.462  56.721  128.700 1.00 49.71 ? 168  LYS B NZ  1 
ATOM   4071  N  N   . ILE B 1 169 ? -0.986  57.678  134.172 1.00 40.53 ? 169  ILE B N   1 
ATOM   4072  C  CA  . ILE B 1 169 ? -0.234  58.615  135.007 1.00 40.17 ? 169  ILE B CA  1 
ATOM   4073  C  C   . ILE B 1 169 ? -0.278  59.971  134.290 1.00 39.51 ? 169  ILE B C   1 
ATOM   4074  O  O   . ILE B 1 169 ? 0.183   60.083  133.162 1.00 38.48 ? 169  ILE B O   1 
ATOM   4075  C  CB  . ILE B 1 169 ? 1.266   58.208  135.103 1.00 46.57 ? 169  ILE B CB  1 
ATOM   4076  C  CG1 . ILE B 1 169 ? 1.422   56.807  135.708 1.00 47.23 ? 169  ILE B CG1 1 
ATOM   4077  C  CG2 . ILE B 1 169 ? 2.024   59.248  135.910 1.00 43.49 ? 169  ILE B CG2 1 
ATOM   4078  C  CD1 . ILE B 1 169 ? 0.977   56.707  137.158 1.00 48.87 ? 169  ILE B CD1 1 
ATOM   4079  N  N   . PRO B 1 170 ? -0.800  61.024  134.940 1.00 40.90 ? 170  PRO B N   1 
ATOM   4080  C  CA  . PRO B 1 170 ? -0.878  62.348  134.301 1.00 38.42 ? 170  PRO B CA  1 
ATOM   4081  C  C   . PRO B 1 170 ? 0.434   62.848  133.811 1.00 39.88 ? 170  PRO B C   1 
ATOM   4082  O  O   . PRO B 1 170 ? 1.399   62.854  134.565 1.00 40.12 ? 170  PRO B O   1 
ATOM   4083  C  CB  . PRO B 1 170 ? -1.413  63.245  135.402 1.00 36.24 ? 170  PRO B CB  1 
ATOM   4084  C  CG  . PRO B 1 170 ? -2.286  62.326  136.182 1.00 38.98 ? 170  PRO B CG  1 
ATOM   4085  C  CD  . PRO B 1 170 ? -1.428  61.060  136.273 1.00 41.77 ? 170  PRO B CD  1 
ATOM   4086  N  N   . VAL B 1 171 ? 0.465   63.282  132.550 1.00 42.11 ? 171  VAL B N   1 
ATOM   4087  C  CA  . VAL B 1 171 ? 1.680   63.818  131.963 1.00 41.14 ? 171  VAL B CA  1 
ATOM   4088  C  C   . VAL B 1 171 ? 2.217   64.925  132.879 1.00 45.95 ? 171  VAL B C   1 
ATOM   4089  O  O   . VAL B 1 171 ? 1.467   65.794  133.342 1.00 38.27 ? 171  VAL B O   1 
ATOM   4090  C  CB  . VAL B 1 171 ? 1.419   64.417  130.579 1.00 40.31 ? 171  VAL B CB  1 
ATOM   4091  C  CG1 . VAL B 1 171 ? 2.548   65.390  130.224 1.00 31.67 ? 171  VAL B CG1 1 
ATOM   4092  C  CG2 . VAL B 1 171 ? 1.308   63.283  129.528 1.00 41.33 ? 171  VAL B CG2 1 
ATOM   4093  N  N   . GLY B 1 172 ? 3.517   64.871  133.163 1.00 49.46 ? 172  GLY B N   1 
ATOM   4094  C  CA  . GLY B 1 172 ? 4.113   65.883  134.008 1.00 52.88 ? 172  GLY B CA  1 
ATOM   4095  C  C   . GLY B 1 172 ? 4.049   65.673  135.516 1.00 57.84 ? 172  GLY B C   1 
ATOM   4096  O  O   . GLY B 1 172 ? 4.454   66.546  136.266 1.00 59.03 ? 172  GLY B O   1 
ATOM   4097  N  N   . SER B 1 173 ? 3.545   64.541  135.984 1.00 63.06 ? 173  SER B N   1 
ATOM   4098  C  CA  . SER B 1 173 ? 3.482   64.287  137.430 1.00 69.67 ? 173  SER B CA  1 
ATOM   4099  C  C   . SER B 1 173 ? 4.526   63.228  137.762 1.00 75.20 ? 173  SER B C   1 
ATOM   4100  O  O   . SER B 1 173 ? 4.500   62.648  138.824 1.00 79.60 ? 173  SER B O   1 
ATOM   4101  C  CB  . SER B 1 173 ? 2.122   63.726  137.822 1.00 69.79 ? 173  SER B CB  1 
ATOM   4102  O  OG  . SER B 1 173 ? 1.904   62.479  137.182 1.00 70.66 ? 173  SER B OG  1 
ATOM   4103  N  N   . GLU B 1 174 ? 5.413   62.984  136.805 1.00 80.74 ? 174  GLU B N   1 
ATOM   4104  C  CA  . GLU B 1 174 ? 6.442   61.967  136.884 1.00 84.29 ? 174  GLU B CA  1 
ATOM   4105  C  C   . GLU B 1 174 ? 7.267   61.734  138.172 1.00 85.58 ? 174  GLU B C   1 
ATOM   4106  O  O   . GLU B 1 174 ? 8.466   61.424  138.137 1.00 87.94 ? 174  GLU B O   1 
ATOM   4107  C  CB  . GLU B 1 174 ? 7.244   62.083  135.602 1.00 85.01 ? 174  GLU B CB  1 
ATOM   4108  C  CG  . GLU B 1 174 ? 6.301   61.509  134.592 1.00 86.25 ? 174  GLU B CG  1 
ATOM   4109  C  CD  . GLU B 1 174 ? 6.052   62.183  133.255 1.00 88.44 ? 174  GLU B CD  1 
ATOM   4110  O  OE1 . GLU B 1 174 ? 6.936   62.006  132.410 1.00 86.64 ? 174  GLU B OE1 1 
ATOM   4111  O  OE2 . GLU B 1 174 ? 4.970   62.824  133.015 1.00 89.89 ? 174  GLU B OE2 1 
ATOM   4112  N  N   . GLU B 1 175 ? 6.571   61.833  139.314 1.00 81.86 ? 175  GLU B N   1 
ATOM   4113  C  CA  . GLU B 1 175 ? 7.190   61.636  140.605 1.00 78.15 ? 175  GLU B CA  1 
ATOM   4114  C  C   . GLU B 1 175 ? 7.056   60.187  141.143 1.00 75.78 ? 175  GLU B C   1 
ATOM   4115  O  O   . GLU B 1 175 ? 6.554   59.957  142.253 1.00 75.17 ? 175  GLU B O   1 
ATOM   4116  C  CB  . GLU B 1 175 ? 6.634   62.662  141.590 1.00 79.85 ? 175  GLU B CB  1 
ATOM   4117  C  CG  . GLU B 1 175 ? 5.130   62.684  141.780 1.00 83.79 ? 175  GLU B CG  1 
ATOM   4118  C  CD  . GLU B 1 175 ? 4.733   63.505  142.998 1.00 86.86 ? 175  GLU B CD  1 
ATOM   4119  O  OE1 . GLU B 1 175 ? 5.321   64.589  143.200 1.00 86.68 ? 175  GLU B OE1 1 
ATOM   4120  O  OE2 . GLU B 1 175 ? 3.839   63.061  143.758 1.00 89.62 ? 175  GLU B OE2 1 
ATOM   4121  N  N   . GLY B 1 176 ? 7.496   59.212  140.345 1.00 69.14 ? 176  GLY B N   1 
ATOM   4122  C  CA  . GLY B 1 176 ? 7.474   57.831  140.788 1.00 63.84 ? 176  GLY B CA  1 
ATOM   4123  C  C   . GLY B 1 176 ? 6.182   57.147  141.209 1.00 64.26 ? 176  GLY B C   1 
ATOM   4124  O  O   . GLY B 1 176 ? 6.215   56.174  141.980 1.00 64.18 ? 176  GLY B O   1 
ATOM   4125  N  N   . TYR B 1 177 ? 5.042   57.643  140.731 1.00 62.42 ? 177  TYR B N   1 
ATOM   4126  C  CA  . TYR B 1 177 ? 3.760   57.012  141.007 1.00 54.59 ? 177  TYR B CA  1 
ATOM   4127  C  C   . TYR B 1 177 ? 3.826   55.709  140.221 1.00 52.39 ? 177  TYR B C   1 
ATOM   4128  O  O   . TYR B 1 177 ? 3.394   54.652  140.679 1.00 46.90 ? 177  TYR B O   1 
ATOM   4129  C  CB  . TYR B 1 177 ? 2.638   57.851  140.445 1.00 56.95 ? 177  TYR B CB  1 
ATOM   4130  C  CG  . TYR B 1 177 ? 2.295   59.054  141.258 1.00 59.65 ? 177  TYR B CG  1 
ATOM   4131  C  CD1 . TYR B 1 177 ? 1.954   58.926  142.592 1.00 62.74 ? 177  TYR B CD1 1 
ATOM   4132  C  CD2 . TYR B 1 177 ? 2.230   60.313  140.681 1.00 63.59 ? 177  TYR B CD2 1 
ATOM   4133  C  CE1 . TYR B 1 177 ? 1.546   60.019  143.347 1.00 65.00 ? 177  TYR B CE1 1 
ATOM   4134  C  CE2 . TYR B 1 177 ? 1.821   61.419  141.424 1.00 66.81 ? 177  TYR B CE2 1 
ATOM   4135  C  CZ  . TYR B 1 177 ? 1.480   61.259  142.763 1.00 66.63 ? 177  TYR B CZ  1 
ATOM   4136  O  OH  . TYR B 1 177 ? 1.085   62.333  143.533 1.00 67.26 ? 177  TYR B OH  1 
ATOM   4137  N  N   . ARG B 1 178 ? 4.388   55.814  139.022 1.00 52.06 ? 178  ARG B N   1 
ATOM   4138  C  CA  . ARG B 1 178 ? 4.524   54.675  138.138 1.00 56.23 ? 178  ARG B CA  1 
ATOM   4139  C  C   . ARG B 1 178 ? 5.389   53.617  138.809 1.00 56.60 ? 178  ARG B C   1 
ATOM   4140  O  O   . ARG B 1 178 ? 5.126   52.425  138.686 1.00 57.08 ? 178  ARG B O   1 
ATOM   4141  C  CB  . ARG B 1 178 ? 5.138   55.129  136.815 1.00 59.65 ? 178  ARG B CB  1 
ATOM   4142  C  CG  . ARG B 1 178 ? 5.145   54.093  135.704 1.00 64.70 ? 178  ARG B CG  1 
ATOM   4143  C  CD  . ARG B 1 178 ? 6.073   54.554  134.599 1.00 67.98 ? 178  ARG B CD  1 
ATOM   4144  N  NE  . ARG B 1 178 ? 6.252   53.549  133.562 1.00 71.00 ? 178  ARG B NE  1 
ATOM   4145  C  CZ  . ARG B 1 178 ? 5.270   53.103  132.787 1.00 74.43 ? 178  ARG B CZ  1 
ATOM   4146  N  NH1 . ARG B 1 178 ? 4.023   53.571  132.931 1.00 72.11 ? 178  ARG B NH1 1 
ATOM   4147  N  NH2 . ARG B 1 178 ? 5.544   52.198  131.857 1.00 72.96 ? 178  ARG B NH2 1 
ATOM   4148  N  N   . SER B 1 179 ? 6.417   54.060  139.526 1.00 58.54 ? 179  SER B N   1 
ATOM   4149  C  CA  . SER B 1 179 ? 7.310   53.142  140.238 1.00 58.67 ? 179  SER B CA  1 
ATOM   4150  C  C   . SER B 1 179 ? 6.506   52.362  141.287 1.00 55.12 ? 179  SER B C   1 
ATOM   4151  O  O   . SER B 1 179 ? 6.543   51.122  141.330 1.00 50.45 ? 179  SER B O   1 
ATOM   4152  C  CB  . SER B 1 179 ? 8.416   53.934  140.938 1.00 60.16 ? 179  SER B CB  1 
ATOM   4153  O  OG  . SER B 1 179 ? 9.006   54.841  140.035 1.00 67.58 ? 179  SER B OG  1 
ATOM   4154  N  N   . LEU B 1 180 ? 5.784   53.115  142.120 1.00 51.96 ? 180  LEU B N   1 
ATOM   4155  C  CA  . LEU B 1 180 ? 4.958   52.542  143.170 1.00 53.33 ? 180  LEU B CA  1 
ATOM   4156  C  C   . LEU B 1 180 ? 4.026   51.461  142.622 1.00 54.24 ? 180  LEU B C   1 
ATOM   4157  O  O   . LEU B 1 180 ? 4.038   50.319  143.081 1.00 55.19 ? 180  LEU B O   1 
ATOM   4158  C  CB  . LEU B 1 180 ? 4.111   53.628  143.828 1.00 52.34 ? 180  LEU B CB  1 
ATOM   4159  C  CG  . LEU B 1 180 ? 3.676   53.388  145.278 1.00 53.66 ? 180  LEU B CG  1 
ATOM   4160  C  CD1 . LEU B 1 180 ? 2.311   54.041  145.467 1.00 55.84 ? 180  LEU B CD1 1 
ATOM   4161  C  CD2 . LEU B 1 180 ? 3.612   51.913  145.620 1.00 50.88 ? 180  LEU B CD2 1 
ATOM   4162  N  N   . PHE B 1 181 ? 3.223   51.823  141.628 1.00 52.56 ? 181  PHE B N   1 
ATOM   4163  C  CA  . PHE B 1 181 ? 2.278   50.876  141.078 1.00 49.74 ? 181  PHE B CA  1 
ATOM   4164  C  C   . PHE B 1 181 ? 2.983   49.671  140.478 1.00 51.52 ? 181  PHE B C   1 
ATOM   4165  O  O   . PHE B 1 181 ? 2.602   48.514  140.747 1.00 51.05 ? 181  PHE B O   1 
ATOM   4166  C  CB  . PHE B 1 181 ? 1.383   51.551  140.018 1.00 48.69 ? 181  PHE B CB  1 
ATOM   4167  C  CG  . PHE B 1 181 ? 0.572   52.727  140.536 1.00 44.49 ? 181  PHE B CG  1 
ATOM   4168  C  CD1 . PHE B 1 181 ? 0.053   52.725  141.831 1.00 43.17 ? 181  PHE B CD1 1 
ATOM   4169  C  CD2 . PHE B 1 181 ? 0.316   53.823  139.716 1.00 39.61 ? 181  PHE B CD2 1 
ATOM   4170  C  CE1 . PHE B 1 181 ? -0.711  53.806  142.302 1.00 43.25 ? 181  PHE B CE1 1 
ATOM   4171  C  CE2 . PHE B 1 181 ? -0.445  54.902  140.174 1.00 40.36 ? 181  PHE B CE2 1 
ATOM   4172  C  CZ  . PHE B 1 181 ? -0.958  54.899  141.461 1.00 39.32 ? 181  PHE B CZ  1 
ATOM   4173  N  N   . GLY B 1 182 ? 4.003   49.939  139.661 1.00 50.07 ? 182  GLY B N   1 
ATOM   4174  C  CA  . GLY B 1 182 ? 4.737   48.855  139.022 1.00 49.49 ? 182  GLY B CA  1 
ATOM   4175  C  C   . GLY B 1 182 ? 5.209   47.837  140.044 1.00 51.11 ? 182  GLY B C   1 
ATOM   4176  O  O   . GLY B 1 182 ? 5.113   46.628  139.826 1.00 49.52 ? 182  GLY B O   1 
ATOM   4177  N  N   . GLN B 1 183 ? 5.699   48.350  141.174 1.00 50.87 ? 183  GLN B N   1 
ATOM   4178  C  CA  . GLN B 1 183 ? 6.204   47.526  142.260 1.00 52.84 ? 183  GLN B CA  1 
ATOM   4179  C  C   . GLN B 1 183 ? 5.095   46.627  142.814 1.00 51.03 ? 183  GLN B C   1 
ATOM   4180  O  O   . GLN B 1 183 ? 5.195   45.396  142.770 1.00 52.31 ? 183  GLN B O   1 
ATOM   4181  C  CB  . GLN B 1 183 ? 6.797   48.432  143.368 1.00 55.52 ? 183  GLN B CB  1 
ATOM   4182  C  CG  . GLN B 1 183 ? 7.607   47.708  144.468 1.00 62.86 ? 183  GLN B CG  1 
ATOM   4183  C  CD  . GLN B 1 183 ? 8.699   46.780  143.899 1.00 72.64 ? 183  GLN B CD  1 
ATOM   4184  O  OE1 . GLN B 1 183 ? 9.627   47.230  143.199 1.00 71.65 ? 183  GLN B OE1 1 
ATOM   4185  N  NE2 . GLN B 1 183 ? 8.585   45.473  144.196 1.00 74.47 ? 183  GLN B NE2 1 
ATOM   4186  N  N   . VAL B 1 184 ? 4.045   47.242  143.339 1.00 47.43 ? 184  VAL B N   1 
ATOM   4187  C  CA  . VAL B 1 184 ? 2.931   46.487  143.878 1.00 46.69 ? 184  VAL B CA  1 
ATOM   4188  C  C   . VAL B 1 184 ? 2.412   45.466  142.855 1.00 45.65 ? 184  VAL B C   1 
ATOM   4189  O  O   . VAL B 1 184 ? 2.079   44.333  143.200 1.00 44.84 ? 184  VAL B O   1 
ATOM   4190  C  CB  . VAL B 1 184 ? 1.795   47.433  144.272 1.00 48.55 ? 184  VAL B CB  1 
ATOM   4191  C  CG1 . VAL B 1 184 ? 0.562   46.640  144.651 1.00 47.69 ? 184  VAL B CG1 1 
ATOM   4192  C  CG2 . VAL B 1 184 ? 2.241   48.305  145.431 1.00 50.06 ? 184  VAL B CG2 1 
ATOM   4193  N  N   . LEU B 1 185 ? 2.353   45.866  141.595 1.00 43.69 ? 185  LEU B N   1 
ATOM   4194  C  CA  . LEU B 1 185 ? 1.872   44.963  140.568 1.00 45.94 ? 185  LEU B CA  1 
ATOM   4195  C  C   . LEU B 1 185 ? 2.804   43.750  140.421 1.00 46.43 ? 185  LEU B C   1 
ATOM   4196  O  O   . LEU B 1 185 ? 2.346   42.617  140.278 1.00 44.06 ? 185  LEU B O   1 
ATOM   4197  C  CB  . LEU B 1 185 ? 1.717   45.729  139.237 1.00 46.41 ? 185  LEU B CB  1 
ATOM   4198  C  CG  . LEU B 1 185 ? 0.522   46.697  139.181 1.00 45.89 ? 185  LEU B CG  1 
ATOM   4199  C  CD1 . LEU B 1 185 ? 0.698   47.756  138.079 1.00 44.49 ? 185  LEU B CD1 1 
ATOM   4200  C  CD2 . LEU B 1 185 ? -0.736  45.886  138.968 1.00 42.70 ? 185  LEU B CD2 1 
ATOM   4201  N  N   . LYS B 1 186 ? 4.109   43.999  140.468 1.00 48.35 ? 186  LYS B N   1 
ATOM   4202  C  CA  . LYS B 1 186 ? 5.126   42.952  140.367 1.00 50.48 ? 186  LYS B CA  1 
ATOM   4203  C  C   . LYS B 1 186 ? 4.973   41.939  141.520 1.00 51.76 ? 186  LYS B C   1 
ATOM   4204  O  O   . LYS B 1 186 ? 5.020   40.733  141.305 1.00 51.01 ? 186  LYS B O   1 
ATOM   4205  C  CB  . LYS B 1 186 ? 6.525   43.583  140.431 1.00 55.05 ? 186  LYS B CB  1 
ATOM   4206  C  CG  . LYS B 1 186 ? 7.527   43.027  139.426 1.00 61.17 ? 186  LYS B CG  1 
ATOM   4207  C  CD  . LYS B 1 186 ? 7.642   41.507  139.508 1.00 70.76 ? 186  LYS B CD  1 
ATOM   4208  C  CE  . LYS B 1 186 ? 8.601   40.955  138.452 1.00 73.74 ? 186  LYS B CE  1 
ATOM   4209  N  NZ  . LYS B 1 186 ? 8.717   39.465  138.531 1.00 79.29 ? 186  LYS B NZ  1 
ATOM   4210  N  N   . ASP B 1 187 ? 4.808   42.439  142.742 1.00 52.01 ? 187  ASP B N   1 
ATOM   4211  C  CA  . ASP B 1 187 ? 4.632   41.575  143.899 1.00 54.59 ? 187  ASP B CA  1 
ATOM   4212  C  C   . ASP B 1 187 ? 3.439   40.675  143.684 1.00 53.73 ? 187  ASP B C   1 
ATOM   4213  O  O   . ASP B 1 187 ? 3.512   39.464  143.881 1.00 54.34 ? 187  ASP B O   1 
ATOM   4214  C  CB  . ASP B 1 187 ? 4.368   42.407  145.142 1.00 61.16 ? 187  ASP B CB  1 
ATOM   4215  C  CG  . ASP B 1 187 ? 5.572   43.208  145.570 1.00 68.35 ? 187  ASP B CG  1 
ATOM   4216  O  OD1 . ASP B 1 187 ? 6.486   43.403  144.735 1.00 71.62 ? 187  ASP B OD1 1 
ATOM   4217  O  OD2 . ASP B 1 187 ? 5.598   43.650  146.744 1.00 73.62 ? 187  ASP B OD2 1 
ATOM   4218  N  N   . ILE B 1 188 ? 2.333   41.291  143.285 1.00 49.39 ? 188  ILE B N   1 
ATOM   4219  C  CA  . ILE B 1 188 ? 1.101   40.583  143.054 1.00 43.63 ? 188  ILE B CA  1 
ATOM   4220  C  C   . ILE B 1 188 ? 1.198   39.507  141.965 1.00 45.00 ? 188  ILE B C   1 
ATOM   4221  O  O   . ILE B 1 188 ? 0.680   38.398  142.144 1.00 46.60 ? 188  ILE B O   1 
ATOM   4222  C  CB  . ILE B 1 188 ? -0.027  41.587  142.733 1.00 41.42 ? 188  ILE B CB  1 
ATOM   4223  C  CG1 . ILE B 1 188 ? -0.158  42.594  143.873 1.00 38.96 ? 188  ILE B CG1 1 
ATOM   4224  C  CG2 . ILE B 1 188 ? -1.340  40.870  142.540 1.00 37.91 ? 188  ILE B CG2 1 
ATOM   4225  C  CD1 . ILE B 1 188 ? -1.256  43.652  143.641 1.00 37.27 ? 188  ILE B CD1 1 
ATOM   4226  N  N   . VAL B 1 189 ? 1.847   39.778  140.840 1.00 42.38 ? 189  VAL B N   1 
ATOM   4227  C  CA  . VAL B 1 189 ? 1.908   38.709  139.848 1.00 44.31 ? 189  VAL B CA  1 
ATOM   4228  C  C   . VAL B 1 189 ? 2.707   37.544  140.422 1.00 45.50 ? 189  VAL B C   1 
ATOM   4229  O  O   . VAL B 1 189 ? 2.431   36.387  140.130 1.00 47.64 ? 189  VAL B O   1 
ATOM   4230  C  CB  . VAL B 1 189 ? 2.607   39.111  138.525 1.00 48.08 ? 189  VAL B CB  1 
ATOM   4231  C  CG1 . VAL B 1 189 ? 1.697   38.785  137.348 1.00 46.51 ? 189  VAL B CG1 1 
ATOM   4232  C  CG2 . VAL B 1 189 ? 3.028   40.564  138.551 1.00 53.14 ? 189  VAL B CG2 1 
ATOM   4233  N  N   . GLU B 1 190 ? 3.724   37.843  141.213 1.00 47.42 ? 190  GLU B N   1 
ATOM   4234  C  CA  . GLU B 1 190 ? 4.512   36.774  141.800 1.00 53.64 ? 190  GLU B CA  1 
ATOM   4235  C  C   . GLU B 1 190 ? 3.602   35.915  142.650 1.00 55.42 ? 190  GLU B C   1 
ATOM   4236  O  O   . GLU B 1 190 ? 3.622   34.696  142.535 1.00 59.51 ? 190  GLU B O   1 
ATOM   4237  C  CB  . GLU B 1 190 ? 5.652   37.319  142.666 1.00 56.05 ? 190  GLU B CB  1 
ATOM   4238  C  CG  . GLU B 1 190 ? 6.854   37.763  141.857 1.00 64.01 ? 190  GLU B CG  1 
ATOM   4239  C  CD  . GLU B 1 190 ? 7.307   36.682  140.893 1.00 70.11 ? 190  GLU B CD  1 
ATOM   4240  O  OE1 . GLU B 1 190 ? 7.261   35.489  141.302 1.00 72.26 ? 190  GLU B OE1 1 
ATOM   4241  O  OE2 . GLU B 1 190 ? 7.711   37.031  139.748 1.00 65.77 ? 190  GLU B OE2 1 
ATOM   4242  N  N   . LYS B 1 191 ? 2.801   36.544  143.501 1.00 54.49 ? 191  LYS B N   1 
ATOM   4243  C  CA  . LYS B 1 191 ? 1.893   35.790  144.351 1.00 55.80 ? 191  LYS B CA  1 
ATOM   4244  C  C   . LYS B 1 191 ? 0.752   35.157  143.549 1.00 57.68 ? 191  LYS B C   1 
ATOM   4245  O  O   . LYS B 1 191 ? 0.264   34.068  143.893 1.00 59.35 ? 191  LYS B O   1 
ATOM   4246  C  CB  . LYS B 1 191 ? 1.333   36.687  145.453 1.00 51.01 ? 191  LYS B CB  1 
ATOM   4247  C  CG  . LYS B 1 191 ? 2.422   37.294  146.312 1.00 52.61 ? 191  LYS B CG  1 
ATOM   4248  C  CD  . LYS B 1 191 ? 1.875   38.294  147.317 1.00 54.91 ? 191  LYS B CD  1 
ATOM   4249  C  CE  . LYS B 1 191 ? 3.010   39.027  148.032 1.00 54.24 ? 191  LYS B CE  1 
ATOM   4250  N  NZ  . LYS B 1 191 ? 2.487   40.065  148.973 1.00 53.94 ? 191  LYS B NZ  1 
ATOM   4251  N  N   . ILE B 1 192 ? 0.307   35.814  142.483 1.00 57.06 ? 192  ILE B N   1 
ATOM   4252  C  CA  . ILE B 1 192 ? -0.766  35.206  141.717 1.00 55.91 ? 192  ILE B CA  1 
ATOM   4253  C  C   . ILE B 1 192 ? -0.160  33.987  141.056 1.00 57.70 ? 192  ILE B C   1 
ATOM   4254  O  O   . ILE B 1 192 ? -0.768  32.921  141.016 1.00 60.08 ? 192  ILE B O   1 
ATOM   4255  C  CB  . ILE B 1 192 ? -1.356  36.146  140.675 1.00 50.52 ? 192  ILE B CB  1 
ATOM   4256  C  CG1 . ILE B 1 192 ? -2.060  37.304  141.373 1.00 47.83 ? 192  ILE B CG1 1 
ATOM   4257  C  CG2 . ILE B 1 192 ? -2.375  35.392  139.834 1.00 49.74 ? 192  ILE B CG2 1 
ATOM   4258  C  CD1 . ILE B 1 192 ? -2.614  38.370  140.426 1.00 43.90 ? 192  ILE B CD1 1 
ATOM   4259  N  N   . SER B 1 193 ? 1.043   34.142  140.527 1.00 59.94 ? 193  SER B N   1 
ATOM   4260  C  CA  . SER B 1 193 ? 1.729   33.000  139.946 1.00 63.74 ? 193  SER B CA  1 
ATOM   4261  C  C   . SER B 1 193 ? 1.977   32.193  141.220 1.00 64.86 ? 193  SER B C   1 
ATOM   4262  O  O   . SER B 1 193 ? 1.865   32.743  142.312 1.00 67.56 ? 193  SER B O   1 
ATOM   4263  C  CB  . SER B 1 193 ? 3.060   33.442  139.344 1.00 64.19 ? 193  SER B CB  1 
ATOM   4264  O  OG  . SER B 1 193 ? 3.707   32.355  138.705 1.00 72.29 ? 193  SER B OG  1 
ATOM   4265  N  N   . MET B 1 194 ? 2.289   30.911  141.120 1.00 64.12 ? 194  MET B N   1 
ATOM   4266  C  CA  . MET B 1 194 ? 2.548   30.131  142.338 1.00 65.78 ? 194  MET B CA  1 
ATOM   4267  C  C   . MET B 1 194 ? 1.284   29.918  143.158 1.00 63.53 ? 194  MET B C   1 
ATOM   4268  O  O   . MET B 1 194 ? 1.324   29.624  144.353 1.00 63.58 ? 194  MET B O   1 
ATOM   4269  C  CB  . MET B 1 194 ? 3.661   30.784  143.204 1.00 67.98 ? 194  MET B CB  1 
ATOM   4270  C  CG  . MET B 1 194 ? 3.240   31.765  144.306 1.00 69.46 ? 194  MET B CG  1 
ATOM   4271  S  SD  . MET B 1 194 ? 4.703   32.363  145.256 1.00 78.43 ? 194  MET B SD  1 
ATOM   4272  C  CE  . MET B 1 194 ? 4.034   32.434  146.972 1.00 75.19 ? 194  MET B CE  1 
ATOM   4273  N  N   . LYS B 1 195 ? 0.163   30.090  142.477 1.00 60.93 ? 195  LYS B N   1 
ATOM   4274  C  CA  . LYS B 1 195 ? -1.166  29.881  143.014 1.00 58.59 ? 195  LYS B CA  1 
ATOM   4275  C  C   . LYS B 1 195 ? -1.789  29.206  141.794 1.00 59.34 ? 195  LYS B C   1 
ATOM   4276  O  O   . LYS B 1 195 ? -2.972  28.875  141.769 1.00 59.50 ? 195  LYS B O   1 
ATOM   4277  C  CB  . LYS B 1 195 ? -1.857  31.213  143.341 1.00 58.27 ? 195  LYS B CB  1 
ATOM   4278  C  CG  . LYS B 1 195 ? -1.766  31.654  144.803 1.00 56.14 ? 195  LYS B CG  1 
ATOM   4279  C  CD  . LYS B 1 195 ? -2.606  30.756  145.691 1.00 56.19 ? 195  LYS B CD  1 
ATOM   4280  C  CE  . LYS B 1 195 ? -2.156  30.773  147.165 1.00 59.15 ? 195  LYS B CE  1 
ATOM   4281  N  NZ  . LYS B 1 195 ? -2.847  31.768  148.054 1.00 60.35 ? 195  LYS B NZ  1 
ATOM   4282  N  N   . ILE B 1 196 ? -0.937  29.006  140.788 1.00 58.07 ? 196  ILE B N   1 
ATOM   4283  C  CA  . ILE B 1 196 ? -1.295  28.366  139.535 1.00 59.33 ? 196  ILE B CA  1 
ATOM   4284  C  C   . ILE B 1 196 ? -0.948  26.885  139.665 1.00 61.40 ? 196  ILE B C   1 
ATOM   4285  O  O   . ILE B 1 196 ? 0.218   26.537  139.783 1.00 59.78 ? 196  ILE B O   1 
ATOM   4286  C  CB  . ILE B 1 196 ? -0.460  28.936  138.336 1.00 59.44 ? 196  ILE B CB  1 
ATOM   4287  C  CG1 . ILE B 1 196 ? -0.741  30.419  138.122 1.00 58.17 ? 196  ILE B CG1 1 
ATOM   4288  C  CG2 . ILE B 1 196 ? -0.789  28.185  137.059 1.00 54.78 ? 196  ILE B CG2 1 
ATOM   4289  C  CD1 . ILE B 1 196 ? -0.012  30.996  136.921 1.00 53.31 ? 196  ILE B CD1 1 
ATOM   4290  N  N   . LYS B 1 197 ? -1.958  26.020  139.648 1.00 66.28 ? 197  LYS B N   1 
ATOM   4291  C  CA  . LYS B 1 197 ? -1.744  24.573  139.729 1.00 69.89 ? 197  LYS B CA  1 
ATOM   4292  C  C   . LYS B 1 197 ? -1.062  24.167  138.435 1.00 71.47 ? 197  LYS B C   1 
ATOM   4293  O  O   . LYS B 1 197 ? -0.829  25.007  137.570 1.00 72.42 ? 197  LYS B O   1 
ATOM   4294  C  CB  . LYS B 1 197 ? -3.075  23.814  139.822 1.00 71.56 ? 197  LYS B CB  1 
ATOM   4295  C  CG  . LYS B 1 197 ? -3.770  23.801  141.177 1.00 76.95 ? 197  LYS B CG  1 
ATOM   4296  C  CD  . LYS B 1 197 ? -4.121  25.193  141.666 1.00 82.37 ? 197  LYS B CD  1 
ATOM   4297  C  CE  . LYS B 1 197 ? -3.169  25.649  142.770 1.00 86.28 ? 197  LYS B CE  1 
ATOM   4298  N  NZ  . LYS B 1 197 ? -3.290  24.795  143.992 1.00 89.34 ? 197  LYS B NZ  1 
ATOM   4299  N  N   . ASP B 1 198 ? -0.755  22.881  138.292 1.00 73.18 ? 198  ASP B N   1 
ATOM   4300  C  CA  . ASP B 1 198 ? -0.117  22.405  137.072 1.00 74.60 ? 198  ASP B CA  1 
ATOM   4301  C  C   . ASP B 1 198 ? -1.143  22.163  135.993 1.00 72.07 ? 198  ASP B C   1 
ATOM   4302  O  O   . ASP B 1 198 ? -0.841  22.245  134.806 1.00 72.44 ? 198  ASP B O   1 
ATOM   4303  C  CB  . ASP B 1 198 ? 0.644   21.108  137.313 1.00 79.80 ? 198  ASP B CB  1 
ATOM   4304  C  CG  . ASP B 1 198 ? 1.918   21.326  138.083 1.00 85.46 ? 198  ASP B CG  1 
ATOM   4305  O  OD1 . ASP B 1 198 ? 1.827   21.581  139.305 1.00 91.41 ? 198  ASP B OD1 1 
ATOM   4306  O  OD2 . ASP B 1 198 ? 3.005   21.260  137.464 1.00 86.77 ? 198  ASP B OD2 1 
ATOM   4307  N  N   . ASN B 1 199 ? -2.361  21.860  136.414 1.00 68.64 ? 199  ASN B N   1 
ATOM   4308  C  CA  . ASN B 1 199 ? -3.440  21.596  135.474 1.00 65.52 ? 199  ASN B CA  1 
ATOM   4309  C  C   . ASN B 1 199 ? -3.953  22.847  134.787 1.00 63.59 ? 199  ASN B C   1 
ATOM   4310  O  O   . ASN B 1 199 ? -4.839  22.758  133.949 1.00 64.82 ? 199  ASN B O   1 
ATOM   4311  C  CB  . ASN B 1 199 ? -4.605  20.907  136.189 1.00 65.54 ? 199  ASN B CB  1 
ATOM   4312  C  CG  . ASN B 1 199 ? -5.317  21.820  137.192 1.00 66.73 ? 199  ASN B CG  1 
ATOM   4313  O  OD1 . ASN B 1 199 ? -4.700  22.657  137.870 1.00 63.06 ? 199  ASN B OD1 1 
ATOM   4314  N  ND2 . ASN B 1 199 ? -6.628  21.639  137.302 1.00 65.36 ? 199  ASN B ND2 1 
ATOM   4315  N  N   . GLY B 1 200 ? -3.417  24.009  135.153 1.00 62.73 ? 200  GLY B N   1 
ATOM   4316  C  CA  . GLY B 1 200 ? -3.857  25.251  134.542 1.00 61.68 ? 200  GLY B CA  1 
ATOM   4317  C  C   . GLY B 1 200 ? -4.735  26.145  135.411 1.00 61.92 ? 200  GLY B C   1 
ATOM   4318  O  O   . GLY B 1 200 ? -4.865  27.339  135.136 1.00 62.65 ? 200  GLY B O   1 
ATOM   4319  N  N   . ILE B 1 201 ? -5.341  25.577  136.450 1.00 58.26 ? 201  ILE B N   1 
ATOM   4320  C  CA  . ILE B 1 201 ? -6.213  26.321  137.356 1.00 55.17 ? 201  ILE B CA  1 
ATOM   4321  C  C   . ILE B 1 201 ? -5.446  27.311  138.203 1.00 52.90 ? 201  ILE B C   1 
ATOM   4322  O  O   . ILE B 1 201 ? -4.314  27.034  138.577 1.00 53.73 ? 201  ILE B O   1 
ATOM   4323  C  CB  . ILE B 1 201 ? -6.948  25.354  138.283 1.00 58.36 ? 201  ILE B CB  1 
ATOM   4324  C  CG1 . ILE B 1 201 ? -8.075  24.686  137.511 1.00 58.67 ? 201  ILE B CG1 1 
ATOM   4325  C  CG2 . ILE B 1 201 ? -7.463  26.069  139.529 1.00 57.82 ? 201  ILE B CG2 1 
ATOM   4326  C  CD1 . ILE B 1 201 ? -8.707  23.561  138.288 1.00 66.85 ? 201  ILE B CD1 1 
ATOM   4327  N  N   . ILE B 1 202 ? -6.059  28.455  138.510 1.00 51.00 ? 202  ILE B N   1 
ATOM   4328  C  CA  . ILE B 1 202 ? -5.406  29.473  139.341 1.00 51.98 ? 202  ILE B CA  1 
ATOM   4329  C  C   . ILE B 1 202 ? -6.226  29.711  140.602 1.00 51.31 ? 202  ILE B C   1 
ATOM   4330  O  O   . ILE B 1 202 ? -7.283  30.315  140.529 1.00 54.15 ? 202  ILE B O   1 
ATOM   4331  C  CB  . ILE B 1 202 ? -5.275  30.809  138.590 1.00 52.01 ? 202  ILE B CB  1 
ATOM   4332  C  CG1 . ILE B 1 202 ? -4.734  30.544  137.176 1.00 50.57 ? 202  ILE B CG1 1 
ATOM   4333  C  CG2 . ILE B 1 202 ? -4.376  31.776  139.397 1.00 47.14 ? 202  ILE B CG2 1 
ATOM   4334  C  CD1 . ILE B 1 202 ? -4.673  31.782  136.289 1.00 53.10 ? 202  ILE B CD1 1 
ATOM   4335  N  N   . GLY B 1 203 ? -5.720  29.264  141.751 1.00 50.24 ? 203  GLY B N   1 
ATOM   4336  C  CA  . GLY B 1 203 ? -6.453  29.392  143.003 1.00 48.75 ? 203  GLY B CA  1 
ATOM   4337  C  C   . GLY B 1 203 ? -7.387  28.195  143.007 1.00 48.64 ? 203  GLY B C   1 
ATOM   4338  O  O   . GLY B 1 203 ? -7.078  27.133  143.544 1.00 49.39 ? 203  GLY B O   1 
ATOM   4339  N  N   . ASP B 1 204 ? -8.543  28.381  142.390 1.00 45.25 ? 204  ASP B N   1 
ATOM   4340  C  CA  . ASP B 1 204 ? -9.506  27.325  142.247 1.00 45.68 ? 204  ASP B CA  1 
ATOM   4341  C  C   . ASP B 1 204 ? -10.273 27.636  140.948 1.00 45.62 ? 204  ASP B C   1 
ATOM   4342  O  O   . ASP B 1 204 ? -10.045 28.652  140.307 1.00 40.55 ? 204  ASP B O   1 
ATOM   4343  C  CB  . ASP B 1 204 ? -10.394 27.208  143.500 1.00 46.66 ? 204  ASP B CB  1 
ATOM   4344  C  CG  . ASP B 1 204 ? -11.593 28.120  143.482 1.00 50.17 ? 204  ASP B CG  1 
ATOM   4345  O  OD1 . ASP B 1 204 ? -11.690 28.979  142.591 1.00 58.93 ? 204  ASP B OD1 1 
ATOM   4346  O  OD2 . ASP B 1 204 ? -12.449 27.977  144.380 1.00 52.53 ? 204  ASP B OD2 1 
ATOM   4347  N  N   . ILE B 1 205 ? -11.160 26.757  140.527 1.00 48.16 ? 205  ILE B N   1 
ATOM   4348  C  CA  . ILE B 1 205 ? -11.833 27.020  139.282 1.00 51.89 ? 205  ILE B CA  1 
ATOM   4349  C  C   . ILE B 1 205 ? -12.625 28.312  139.255 1.00 49.39 ? 205  ILE B C   1 
ATOM   4350  O  O   . ILE B 1 205 ? -12.731 28.969  138.224 1.00 48.03 ? 205  ILE B O   1 
ATOM   4351  C  CB  . ILE B 1 205 ? -12.735 25.819  138.892 1.00 56.18 ? 205  ILE B CB  1 
ATOM   4352  C  CG1 . ILE B 1 205 ? -13.351 25.188  140.133 1.00 56.98 ? 205  ILE B CG1 1 
ATOM   4353  C  CG2 . ILE B 1 205 ? -11.891 24.756  138.178 1.00 60.78 ? 205  ILE B CG2 1 
ATOM   4354  C  CD1 . ILE B 1 205 ? -13.878 23.766  139.888 1.00 59.34 ? 205  ILE B CD1 1 
ATOM   4355  N  N   . TYR B 1 206 ? -13.135 28.720  140.401 1.00 45.65 ? 206  TYR B N   1 
ATOM   4356  C  CA  . TYR B 1 206 ? -13.960 29.899  140.413 1.00 42.57 ? 206  TYR B CA  1 
ATOM   4357  C  C   . TYR B 1 206 ? -13.285 31.251  140.556 1.00 41.06 ? 206  TYR B C   1 
ATOM   4358  O  O   . TYR B 1 206 ? -13.948 32.287  140.494 1.00 36.65 ? 206  TYR B O   1 
ATOM   4359  C  CB  . TYR B 1 206 ? -15.066 29.668  141.431 1.00 44.09 ? 206  TYR B CB  1 
ATOM   4360  C  CG  . TYR B 1 206 ? -15.825 28.397  141.064 1.00 46.39 ? 206  TYR B CG  1 
ATOM   4361  C  CD1 . TYR B 1 206 ? -16.716 28.364  139.970 1.00 45.68 ? 206  TYR B CD1 1 
ATOM   4362  C  CD2 . TYR B 1 206 ? -15.600 27.212  141.762 1.00 43.77 ? 206  TYR B CD2 1 
ATOM   4363  C  CE1 . TYR B 1 206 ? -17.358 27.176  139.594 1.00 42.54 ? 206  TYR B CE1 1 
ATOM   4364  C  CE2 . TYR B 1 206 ? -16.224 26.029  141.400 1.00 43.55 ? 206  TYR B CE2 1 
ATOM   4365  C  CZ  . TYR B 1 206 ? -17.104 26.005  140.321 1.00 46.73 ? 206  TYR B CZ  1 
ATOM   4366  O  OH  . TYR B 1 206 ? -17.706 24.800  139.998 1.00 41.44 ? 206  TYR B OH  1 
ATOM   4367  N  N   . SER B 1 207 ? -11.964 31.247  140.687 1.00 38.60 ? 207  SER B N   1 
ATOM   4368  C  CA  . SER B 1 207 ? -11.246 32.492  140.787 1.00 39.60 ? 207  SER B CA  1 
ATOM   4369  C  C   . SER B 1 207 ? -10.228 32.562  139.660 1.00 40.55 ? 207  SER B C   1 
ATOM   4370  O  O   . SER B 1 207 ? -9.423  33.496  139.582 1.00 40.30 ? 207  SER B O   1 
ATOM   4371  C  CB  . SER B 1 207 ? -10.573 32.595  142.132 1.00 36.63 ? 207  SER B CB  1 
ATOM   4372  O  OG  . SER B 1 207 ? -9.602  31.603  142.182 1.00 48.48 ? 207  SER B OG  1 
ATOM   4373  N  N   . THR B 1 208 ? -10.282 31.569  138.772 1.00 42.40 ? 208  THR B N   1 
ATOM   4374  C  CA  . THR B 1 208 ? -9.399  31.524  137.596 1.00 43.99 ? 208  THR B CA  1 
ATOM   4375  C  C   . THR B 1 208 ? -9.727  32.637  136.567 1.00 40.92 ? 208  THR B C   1 
ATOM   4376  O  O   . THR B 1 208 ? -8.822  33.218  135.974 1.00 41.10 ? 208  THR B O   1 
ATOM   4377  C  CB  . THR B 1 208 ? -9.495  30.156  136.879 1.00 46.09 ? 208  THR B CB  1 
ATOM   4378  O  OG1 . THR B 1 208 ? -8.971  29.134  137.733 1.00 49.38 ? 208  THR B OG1 1 
ATOM   4379  C  CG2 . THR B 1 208 ? -8.712  30.181  135.569 1.00 43.56 ? 208  THR B CG2 1 
ATOM   4380  N  N   . GLY B 1 209 ? -11.014 32.902  136.343 1.00 38.06 ? 209  GLY B N   1 
ATOM   4381  C  CA  . GLY B 1 209 ? -11.405 33.950  135.419 1.00 37.95 ? 209  GLY B CA  1 
ATOM   4382  C  C   . GLY B 1 209 ? -10.751 35.290  135.750 1.00 40.62 ? 209  GLY B C   1 
ATOM   4383  O  O   . GLY B 1 209 ? -10.063 35.875  134.916 1.00 41.38 ? 209  GLY B O   1 
ATOM   4384  N  N   . LEU B 1 210 ? -10.931 35.787  136.966 1.00 38.76 ? 210  LEU B N   1 
ATOM   4385  C  CA  . LEU B 1 210 ? -10.336 37.062  137.284 1.00 41.56 ? 210  LEU B CA  1 
ATOM   4386  C  C   . LEU B 1 210 ? -8.824  36.961  137.235 1.00 43.46 ? 210  LEU B C   1 
ATOM   4387  O  O   . LEU B 1 210 ? -8.141  37.889  136.799 1.00 44.01 ? 210  LEU B O   1 
ATOM   4388  C  CB  . LEU B 1 210 ? -10.802 37.568  138.670 1.00 43.94 ? 210  LEU B CB  1 
ATOM   4389  C  CG  . LEU B 1 210 ? -12.301 37.840  138.820 1.00 47.47 ? 210  LEU B CG  1 
ATOM   4390  C  CD1 . LEU B 1 210 ? -12.540 38.591  140.097 1.00 50.19 ? 210  LEU B CD1 1 
ATOM   4391  C  CD2 . LEU B 1 210 ? -12.827 38.656  137.626 1.00 48.63 ? 210  LEU B CD2 1 
ATOM   4392  N  N   . ALA B 1 211 ? -8.286  35.831  137.669 1.00 44.74 ? 211  ALA B N   1 
ATOM   4393  C  CA  . ALA B 1 211 ? -6.842  35.691  137.666 1.00 43.57 ? 211  ALA B CA  1 
ATOM   4394  C  C   . ALA B 1 211 ? -6.362  35.858  136.249 1.00 43.51 ? 211  ALA B C   1 
ATOM   4395  O  O   . ALA B 1 211 ? -5.396  36.603  136.007 1.00 44.09 ? 211  ALA B O   1 
ATOM   4396  C  CB  . ALA B 1 211 ? -6.439  34.339  138.201 1.00 48.10 ? 211  ALA B CB  1 
ATOM   4397  N  N   . MET B 1 212 ? -7.042  35.180  135.318 1.00 39.28 ? 212  MET B N   1 
ATOM   4398  C  CA  . MET B 1 212 ? -6.695  35.255  133.898 1.00 41.25 ? 212  MET B CA  1 
ATOM   4399  C  C   . MET B 1 212 ? -6.682  36.692  133.407 1.00 39.88 ? 212  MET B C   1 
ATOM   4400  O  O   . MET B 1 212 ? -5.790  37.096  132.675 1.00 37.12 ? 212  MET B O   1 
ATOM   4401  C  CB  . MET B 1 212 ? -7.686  34.463  133.041 1.00 46.27 ? 212  MET B CB  1 
ATOM   4402  C  CG  . MET B 1 212 ? -7.542  32.961  133.133 1.00 51.64 ? 212  MET B CG  1 
ATOM   4403  S  SD  . MET B 1 212 ? -8.733  32.165  132.046 1.00 65.27 ? 212  MET B SD  1 
ATOM   4404  C  CE  . MET B 1 212 ? -7.913  32.372  130.447 1.00 64.70 ? 212  MET B CE  1 
ATOM   4405  N  N   . GLN B 1 213 ? -7.678  37.470  133.814 1.00 38.44 ? 213  GLN B N   1 
ATOM   4406  C  CA  . GLN B 1 213 ? -7.744  38.856  133.397 1.00 34.88 ? 213  GLN B CA  1 
ATOM   4407  C  C   . GLN B 1 213 ? -6.530  39.585  133.890 1.00 32.99 ? 213  GLN B C   1 
ATOM   4408  O  O   . GLN B 1 213 ? -5.827  40.250  133.127 1.00 35.30 ? 213  GLN B O   1 
ATOM   4409  C  CB  . GLN B 1 213 ? -9.002  39.541  133.942 1.00 34.87 ? 213  GLN B CB  1 
ATOM   4410  C  CG  . GLN B 1 213 ? -10.308 39.064  133.325 1.00 32.50 ? 213  GLN B CG  1 
ATOM   4411  C  CD  . GLN B 1 213 ? -11.462 39.971  133.698 1.00 39.68 ? 213  GLN B CD  1 
ATOM   4412  O  OE1 . GLN B 1 213 ? -12.611 39.540  133.801 1.00 42.58 ? 213  GLN B OE1 1 
ATOM   4413  N  NE2 . GLN B 1 213 ? -11.164 41.246  133.892 1.00 39.89 ? 213  GLN B NE2 1 
ATOM   4414  N  N   . ALA B 1 214 ? -6.271  39.457  135.177 1.00 35.67 ? 214  ALA B N   1 
ATOM   4415  C  CA  . ALA B 1 214 ? -5.142  40.147  135.780 1.00 38.00 ? 214  ALA B CA  1 
ATOM   4416  C  C   . ALA B 1 214 ? -3.820  39.741  135.112 1.00 41.52 ? 214  ALA B C   1 
ATOM   4417  O  O   . ALA B 1 214 ? -2.997  40.597  134.797 1.00 45.98 ? 214  ALA B O   1 
ATOM   4418  C  CB  . ALA B 1 214 ? -5.116  39.872  137.295 1.00 34.71 ? 214  ALA B CB  1 
ATOM   4419  N  N   . LEU B 1 215 ? -3.614  38.450  134.870 1.00 42.33 ? 215  LEU B N   1 
ATOM   4420  C  CA  . LEU B 1 215 ? -2.376  38.016  134.222 1.00 44.18 ? 215  LEU B CA  1 
ATOM   4421  C  C   . LEU B 1 215 ? -2.218  38.539  132.795 1.00 46.20 ? 215  LEU B C   1 
ATOM   4422  O  O   . LEU B 1 215 ? -1.108  38.817  132.352 1.00 43.69 ? 215  LEU B O   1 
ATOM   4423  C  CB  . LEU B 1 215 ? -2.299  36.498  134.193 1.00 43.66 ? 215  LEU B CB  1 
ATOM   4424  C  CG  . LEU B 1 215 ? -1.997  35.860  135.542 1.00 44.34 ? 215  LEU B CG  1 
ATOM   4425  C  CD1 . LEU B 1 215 ? -2.020  34.348  135.364 1.00 42.25 ? 215  LEU B CD1 1 
ATOM   4426  C  CD2 . LEU B 1 215 ? -0.658  36.352  136.070 1.00 37.63 ? 215  LEU B CD2 1 
ATOM   4427  N  N   . SER B 1 216 ? -3.334  38.639  132.077 1.00 46.66 ? 216  SER B N   1 
ATOM   4428  C  CA  . SER B 1 216 ? -3.357  39.133  130.706 1.00 45.94 ? 216  SER B CA  1 
ATOM   4429  C  C   . SER B 1 216 ? -3.038  40.607  130.624 1.00 45.56 ? 216  SER B C   1 
ATOM   4430  O  O   . SER B 1 216 ? -2.584  41.082  129.606 1.00 45.30 ? 216  SER B O   1 
ATOM   4431  C  CB  . SER B 1 216 ? -4.747  38.965  130.105 1.00 45.96 ? 216  SER B CB  1 
ATOM   4432  O  OG  . SER B 1 216 ? -5.148  37.612  130.123 1.00 59.69 ? 216  SER B OG  1 
ATOM   4433  N  N   . VAL B 1 217 ? -3.251  41.316  131.718 1.00 47.14 ? 217  VAL B N   1 
ATOM   4434  C  CA  . VAL B 1 217 ? -3.110  42.757  131.729 1.00 46.67 ? 217  VAL B CA  1 
ATOM   4435  C  C   . VAL B 1 217 ? -1.953  43.451  132.460 1.00 46.66 ? 217  VAL B C   1 
ATOM   4436  O  O   . VAL B 1 217 ? -1.624  44.597  132.115 1.00 45.27 ? 217  VAL B O   1 
ATOM   4437  C  CB  . VAL B 1 217 ? -4.498  43.332  132.192 1.00 46.82 ? 217  VAL B CB  1 
ATOM   4438  C  CG1 . VAL B 1 217 ? -4.358  44.599  132.977 1.00 43.87 ? 217  VAL B CG1 1 
ATOM   4439  C  CG2 . VAL B 1 217 ? -5.360  43.542  130.984 1.00 42.18 ? 217  VAL B CG2 1 
ATOM   4440  N  N   . THR B 1 218 ? -1.338  42.790  133.447 1.00 46.57 ? 218  THR B N   1 
ATOM   4441  C  CA  . THR B 1 218 ? -0.225  43.401  134.207 1.00 48.33 ? 218  THR B CA  1 
ATOM   4442  C  C   . THR B 1 218 ? 0.937   43.811  133.340 1.00 49.19 ? 218  THR B C   1 
ATOM   4443  O  O   . THR B 1 218 ? 1.400   43.027  132.503 1.00 46.05 ? 218  THR B O   1 
ATOM   4444  C  CB  . THR B 1 218 ? 0.430   42.470  135.217 1.00 49.65 ? 218  THR B CB  1 
ATOM   4445  O  OG1 . THR B 1 218 ? -0.325  41.265  135.339 1.00 54.64 ? 218  THR B OG1 1 
ATOM   4446  C  CG2 . THR B 1 218 ? 0.576   43.175  136.543 1.00 48.16 ? 218  THR B CG2 1 
ATOM   4447  N  N   . PRO B 1 219 ? 1.473   45.015  133.577 1.00 49.04 ? 219  PRO B N   1 
ATOM   4448  C  CA  . PRO B 1 219 ? 2.601   45.469  132.771 1.00 52.83 ? 219  PRO B CA  1 
ATOM   4449  C  C   . PRO B 1 219 ? 3.771   44.487  132.761 1.00 59.15 ? 219  PRO B C   1 
ATOM   4450  O  O   . PRO B 1 219 ? 4.315   44.169  131.693 1.00 60.79 ? 219  PRO B O   1 
ATOM   4451  C  CB  . PRO B 1 219 ? 2.943   46.831  133.374 1.00 47.46 ? 219  PRO B CB  1 
ATOM   4452  C  CG  . PRO B 1 219 ? 2.411   46.745  134.765 1.00 51.02 ? 219  PRO B CG  1 
ATOM   4453  C  CD  . PRO B 1 219 ? 1.126   45.998  134.612 1.00 49.56 ? 219  PRO B CD  1 
ATOM   4454  N  N   . GLU B 1 220 ? 4.164   43.986  133.924 1.00 64.61 ? 220  GLU B N   1 
ATOM   4455  C  CA  . GLU B 1 220 ? 5.281   43.048  133.944 1.00 70.47 ? 220  GLU B CA  1 
ATOM   4456  C  C   . GLU B 1 220 ? 4.893   41.682  134.489 1.00 72.79 ? 220  GLU B C   1 
ATOM   4457  O  O   . GLU B 1 220 ? 4.368   41.562  135.604 1.00 70.96 ? 220  GLU B O   1 
ATOM   4458  C  CB  . GLU B 1 220 ? 6.452   43.614  134.746 1.00 71.22 ? 220  GLU B CB  1 
ATOM   4459  C  CG  . GLU B 1 220 ? 7.630   42.673  134.804 1.00 76.35 ? 220  GLU B CG  1 
ATOM   4460  C  CD  . GLU B 1 220 ? 8.869   43.326  135.392 1.00 80.29 ? 220  GLU B CD  1 
ATOM   4461  O  OE1 . GLU B 1 220 ? 8.739   44.049  136.410 1.00 81.00 ? 220  GLU B OE1 1 
ATOM   4462  O  OE2 . GLU B 1 220 ? 9.975   43.111  134.840 1.00 79.56 ? 220  GLU B OE2 1 
ATOM   4463  N  N   . PRO B 1 221 ? 5.162   40.628  133.701 1.00 75.48 ? 221  PRO B N   1 
ATOM   4464  C  CA  . PRO B 1 221 ? 4.856   39.237  134.059 1.00 77.97 ? 221  PRO B CA  1 
ATOM   4465  C  C   . PRO B 1 221 ? 5.775   38.716  135.173 1.00 78.61 ? 221  PRO B C   1 
ATOM   4466  O  O   . PRO B 1 221 ? 6.752   39.377  135.543 1.00 77.16 ? 221  PRO B O   1 
ATOM   4467  C  CB  . PRO B 1 221 ? 5.041   38.500  132.730 1.00 78.12 ? 221  PRO B CB  1 
ATOM   4468  C  CG  . PRO B 1 221 ? 6.199   39.236  132.121 1.00 78.46 ? 221  PRO B CG  1 
ATOM   4469  C  CD  . PRO B 1 221 ? 5.883   40.698  132.414 1.00 75.89 ? 221  PRO B CD  1 
ATOM   4470  N  N   . SER B 1 222 ? 5.451   37.546  135.720 1.00 80.46 ? 222  SER B N   1 
ATOM   4471  C  CA  . SER B 1 222 ? 6.279   36.964  136.776 1.00 82.24 ? 222  SER B CA  1 
ATOM   4472  C  C   . SER B 1 222 ? 7.417   36.132  136.170 1.00 84.13 ? 222  SER B C   1 
ATOM   4473  O  O   . SER B 1 222 ? 7.352   35.740  134.996 1.00 83.17 ? 222  SER B O   1 
ATOM   4474  C  CB  . SER B 1 222 ? 5.427   36.104  137.725 1.00 78.52 ? 222  SER B CB  1 
ATOM   4475  O  OG  . SER B 1 222 ? 4.633   35.172  137.024 1.00 76.52 ? 222  SER B OG  1 
ATOM   4476  N  N   . LYS B 1 223 ? 8.462   35.891  136.963 1.00 86.74 ? 223  LYS B N   1 
ATOM   4477  C  CA  . LYS B 1 223 ? 9.615   35.107  136.515 1.00 89.99 ? 223  LYS B CA  1 
ATOM   4478  C  C   . LYS B 1 223 ? 9.105   33.746  136.042 1.00 91.09 ? 223  LYS B C   1 
ATOM   4479  O  O   . LYS B 1 223 ? 9.439   33.288  134.947 1.00 89.72 ? 223  LYS B O   1 
ATOM   4480  C  CB  . LYS B 1 223 ? 10.619  34.936  137.662 1.00 91.52 ? 223  LYS B CB  1 
ATOM   4481  C  CG  . LYS B 1 223 ? 12.008  34.464  137.229 1.00 95.49 ? 223  LYS B CG  1 
ATOM   4482  C  CD  . LYS B 1 223 ? 11.992  33.027  136.693 1.00 97.23 ? 223  LYS B CD  1 
ATOM   4483  C  CE  . LYS B 1 223 ? 13.383  32.556  136.277 1.00 97.21 ? 223  LYS B CE  1 
ATOM   4484  N  NZ  . LYS B 1 223 ? 13.963  33.335  135.140 1.00 95.50 ? 223  LYS B NZ  1 
ATOM   4485  N  N   . LYS B 1 224 ? 8.311   33.099  136.891 1.00 93.70 ? 224  LYS B N   1 
ATOM   4486  C  CA  . LYS B 1 224 ? 7.692   31.817  136.558 1.00 95.63 ? 224  LYS B CA  1 
ATOM   4487  C  C   . LYS B 1 224 ? 6.665   32.297  135.544 1.00 95.85 ? 224  LYS B C   1 
ATOM   4488  O  O   . LYS B 1 224 ? 5.906   33.219  135.848 1.00 97.14 ? 224  LYS B O   1 
ATOM   4489  C  CB  . LYS B 1 224 ? 6.989   31.250  137.796 1.00 97.05 ? 224  LYS B CB  1 
ATOM   4490  C  CG  . LYS B 1 224 ? 6.224   29.949  137.595 1.00 99.09 ? 224  LYS B CG  1 
ATOM   4491  C  CD  . LYS B 1 224 ? 5.382   29.632  138.848 1.00 99.45 ? 224  LYS B CD  1 
ATOM   4492  C  CE  . LYS B 1 224 ? 4.701   28.262  138.768 1.00 99.45 ? 224  LYS B CE  1 
ATOM   4493  N  NZ  . LYS B 1 224 ? 3.770   28.003  139.916 1.00 97.22 ? 224  LYS B NZ  1 
ATOM   4494  N  N   . GLU B 1 225 ? 6.615   31.716  134.352 1.00 94.56 ? 225  GLU B N   1 
ATOM   4495  C  CA  . GLU B 1 225 ? 5.652   32.248  133.409 1.00 93.54 ? 225  GLU B CA  1 
ATOM   4496  C  C   . GLU B 1 225 ? 4.360   31.480  133.202 1.00 91.50 ? 225  GLU B C   1 
ATOM   4497  O  O   . GLU B 1 225 ? 4.318   30.250  133.292 1.00 92.83 ? 225  GLU B O   1 
ATOM   4498  C  CB  . GLU B 1 225 ? 6.305   32.491  132.066 1.00 95.11 ? 225  GLU B CB  1 
ATOM   4499  C  CG  . GLU B 1 225 ? 5.730   33.723  131.408 1.00 98.52 ? 225  GLU B CG  1 
ATOM   4500  C  CD  . GLU B 1 225 ? 5.644   33.573  129.910 1.00 99.45 ? 225  GLU B CD  1 
ATOM   4501  O  OE1 . GLU B 1 225 ? 6.615   33.030  129.320 1.00 99.45 ? 225  GLU B OE1 1 
ATOM   4502  O  OE2 . GLU B 1 225 ? 4.610   34.000  129.333 1.00 99.45 ? 225  GLU B OE2 1 
ATOM   4503  N  N   . TRP B 1 226 ? 3.313   32.237  132.887 1.00 85.59 ? 226  TRP B N   1 
ATOM   4504  C  CA  . TRP B 1 226 ? 1.986   31.694  132.683 1.00 80.48 ? 226  TRP B CA  1 
ATOM   4505  C  C   . TRP B 1 226 ? 1.665   31.227  131.263 1.00 79.62 ? 226  TRP B C   1 
ATOM   4506  O  O   . TRP B 1 226 ? 1.831   31.949  130.276 1.00 78.47 ? 226  TRP B O   1 
ATOM   4507  C  CB  . TRP B 1 226 ? 0.964   32.730  133.156 1.00 76.67 ? 226  TRP B CB  1 
ATOM   4508  C  CG  . TRP B 1 226 ? -0.465  32.423  132.855 1.00 70.93 ? 226  TRP B CG  1 
ATOM   4509  C  CD1 . TRP B 1 226 ? -1.169  31.310  133.221 1.00 71.55 ? 226  TRP B CD1 1 
ATOM   4510  C  CD2 . TRP B 1 226 ? -1.384  33.268  132.164 1.00 69.59 ? 226  TRP B CD2 1 
ATOM   4511  N  NE1 . TRP B 1 226 ? -2.480  31.413  132.801 1.00 70.79 ? 226  TRP B NE1 1 
ATOM   4512  C  CE2 . TRP B 1 226 ? -2.637  32.608  132.151 1.00 69.86 ? 226  TRP B CE2 1 
ATOM   4513  C  CE3 . TRP B 1 226 ? -1.274  34.519  131.556 1.00 67.11 ? 226  TRP B CE3 1 
ATOM   4514  C  CZ2 . TRP B 1 226 ? -3.767  33.160  131.553 1.00 69.11 ? 226  TRP B CZ2 1 
ATOM   4515  C  CZ3 . TRP B 1 226 ? -2.395  35.065  130.963 1.00 69.24 ? 226  TRP B CZ3 1 
ATOM   4516  C  CH2 . TRP B 1 226 ? -3.628  34.385  130.967 1.00 68.69 ? 226  TRP B CH2 1 
ATOM   4517  N  N   . ASN B 1 227 ? 1.195   29.989  131.195 1.00 79.57 ? 227  ASN B N   1 
ATOM   4518  C  CA  . ASN B 1 227 ? 0.796   29.343  129.952 1.00 79.47 ? 227  ASN B CA  1 
ATOM   4519  C  C   . ASN B 1 227 ? -0.724  29.557  129.836 1.00 77.62 ? 227  ASN B C   1 
ATOM   4520  O  O   . ASN B 1 227 ? -1.518  28.788  130.394 1.00 76.74 ? 227  ASN B O   1 
ATOM   4521  C  CB  . ASN B 1 227 ? 1.139   27.841  130.027 1.00 80.36 ? 227  ASN B CB  1 
ATOM   4522  C  CG  . ASN B 1 227 ? 0.624   27.049  128.827 1.00 84.72 ? 227  ASN B CG  1 
ATOM   4523  O  OD1 . ASN B 1 227 ? -0.131  27.569  127.989 1.00 85.89 ? 227  ASN B OD1 1 
ATOM   4524  N  ND2 . ASN B 1 227 ? 1.021   25.776  128.747 1.00 84.45 ? 227  ASN B ND2 1 
ATOM   4525  N  N   . CYS B 1 228 ? -1.124  30.606  129.121 1.00 75.08 ? 228  CYS B N   1 
ATOM   4526  C  CA  . CYS B 1 228 ? -2.536  30.907  128.968 1.00 74.40 ? 228  CYS B CA  1 
ATOM   4527  C  C   . CYS B 1 228 ? -3.397  29.813  128.313 1.00 72.11 ? 228  CYS B C   1 
ATOM   4528  O  O   . CYS B 1 228 ? -4.476  29.503  128.816 1.00 70.06 ? 228  CYS B O   1 
ATOM   4529  C  CB  . CYS B 1 228 ? -2.727  32.231  128.219 1.00 77.82 ? 228  CYS B CB  1 
ATOM   4530  S  SG  . CYS B 1 228 ? -4.496  32.620  127.968 1.00 88.11 ? 228  CYS B SG  1 
ATOM   4531  N  N   . LYS B 1 229 ? -2.943  29.229  127.205 1.00 70.60 ? 229  LYS B N   1 
ATOM   4532  C  CA  . LYS B 1 229 ? -3.731  28.188  126.535 1.00 69.11 ? 229  LYS B CA  1 
ATOM   4533  C  C   . LYS B 1 229 ? -3.998  27.009  127.466 1.00 66.95 ? 229  LYS B C   1 
ATOM   4534  O  O   . LYS B 1 229 ? -5.054  26.388  127.414 1.00 64.85 ? 229  LYS B O   1 
ATOM   4535  C  CB  . LYS B 1 229 ? -3.022  27.683  125.272 1.00 72.46 ? 229  LYS B CB  1 
ATOM   4536  C  CG  . LYS B 1 229 ? -3.797  26.577  124.544 1.00 75.12 ? 229  LYS B CG  1 
ATOM   4537  C  CD  . LYS B 1 229 ? -2.952  25.836  123.506 1.00 73.69 ? 229  LYS B CD  1 
ATOM   4538  C  CE  . LYS B 1 229 ? -3.707  24.632  122.897 1.00 74.21 ? 229  LYS B CE  1 
ATOM   4539  N  NZ  . LYS B 1 229 ? -4.990  24.970  122.193 1.00 71.43 ? 229  LYS B NZ  1 
ATOM   4540  N  N   . LYS B 1 230 ? -3.026  26.696  128.310 1.00 66.79 ? 230  LYS B N   1 
ATOM   4541  C  CA  . LYS B 1 230 ? -3.173  25.609  129.275 1.00 66.80 ? 230  LYS B CA  1 
ATOM   4542  C  C   . LYS B 1 230 ? -4.398  25.876  130.154 1.00 64.05 ? 230  LYS B C   1 
ATOM   4543  O  O   . LYS B 1 230 ? -5.290  25.038  130.293 1.00 63.11 ? 230  LYS B O   1 
ATOM   4544  C  CB  . LYS B 1 230 ? -1.928  25.537  130.152 1.00 68.15 ? 230  LYS B CB  1 
ATOM   4545  C  CG  . LYS B 1 230 ? -1.950  24.433  131.174 1.00 72.29 ? 230  LYS B CG  1 
ATOM   4546  C  CD  . LYS B 1 230 ? -0.848  23.438  130.892 1.00 76.13 ? 230  LYS B CD  1 
ATOM   4547  C  CE  . LYS B 1 230 ? -0.355  22.776  132.176 1.00 76.11 ? 230  LYS B CE  1 
ATOM   4548  N  NZ  . LYS B 1 230 ? 0.585   21.640  131.897 1.00 80.73 ? 230  LYS B NZ  1 
ATOM   4549  N  N   . THR B 1 231 ? -4.424  27.066  130.739 1.00 59.56 ? 231  THR B N   1 
ATOM   4550  C  CA  . THR B 1 231 ? -5.511  27.474  131.601 1.00 55.60 ? 231  THR B CA  1 
ATOM   4551  C  C   . THR B 1 231 ? -6.868  27.541  130.912 1.00 52.35 ? 231  THR B C   1 
ATOM   4552  O  O   . THR B 1 231 ? -7.873  27.072  131.445 1.00 49.58 ? 231  THR B O   1 
ATOM   4553  C  CB  . THR B 1 231 ? -5.233  28.856  132.211 1.00 54.65 ? 231  THR B CB  1 
ATOM   4554  O  OG1 . THR B 1 231 ? -4.032  28.803  132.994 1.00 52.92 ? 231  THR B OG1 1 
ATOM   4555  C  CG2 . THR B 1 231 ? -6.428  29.302  133.069 1.00 50.60 ? 231  THR B CG2 1 
ATOM   4556  N  N   . THR B 1 232 ? -6.926  28.128  129.732 1.00 50.72 ? 232  THR B N   1 
ATOM   4557  C  CA  . THR B 1 232 ? -8.232  28.231  129.123 1.00 54.41 ? 232  THR B CA  1 
ATOM   4558  C  C   . THR B 1 232 ? -8.741  26.851  128.708 1.00 55.43 ? 232  THR B C   1 
ATOM   4559  O  O   . THR B 1 232 ? -9.939  26.546  128.845 1.00 54.06 ? 232  THR B O   1 
ATOM   4560  C  CB  . THR B 1 232 ? -8.229  29.319  127.975 1.00 54.59 ? 232  THR B CB  1 
ATOM   4561  O  OG1 . THR B 1 232 ? -8.994  28.875  126.840 1.00 52.79 ? 232  THR B OG1 1 
ATOM   4562  C  CG2 . THR B 1 232 ? -6.823  29.665  127.592 1.00 54.67 ? 232  THR B CG2 1 
ATOM   4563  N  N   . ASP B 1 233 ? -7.828  25.992  128.258 1.00 56.16 ? 233  ASP B N   1 
ATOM   4564  C  CA  . ASP B 1 233 ? -8.231  24.648  127.873 1.00 55.90 ? 233  ASP B CA  1 
ATOM   4565  C  C   . ASP B 1 233 ? -8.775  23.929  129.119 1.00 54.43 ? 233  ASP B C   1 
ATOM   4566  O  O   . ASP B 1 233 ? -9.839  23.301  129.070 1.00 55.03 ? 233  ASP B O   1 
ATOM   4567  C  CB  . ASP B 1 233 ? -7.056  23.867  127.268 1.00 59.17 ? 233  ASP B CB  1 
ATOM   4568  C  CG  . ASP B 1 233 ? -6.678  24.343  125.851 1.00 66.80 ? 233  ASP B CG  1 
ATOM   4569  O  OD1 . ASP B 1 233 ? -7.477  25.072  125.205 1.00 70.89 ? 233  ASP B OD1 1 
ATOM   4570  O  OD2 . ASP B 1 233 ? -5.576  23.969  125.378 1.00 68.55 ? 233  ASP B OD2 1 
ATOM   4571  N  N   . MET B 1 234 ? -8.072  24.043  130.242 1.00 50.02 ? 234  MET B N   1 
ATOM   4572  C  CA  . MET B 1 234 ? -8.532  23.398  131.458 1.00 50.81 ? 234  MET B CA  1 
ATOM   4573  C  C   . MET B 1 234 ? -9.921  23.924  131.853 1.00 52.12 ? 234  MET B C   1 
ATOM   4574  O  O   . MET B 1 234 ? -10.771 23.156  132.342 1.00 51.17 ? 234  MET B O   1 
ATOM   4575  C  CB  . MET B 1 234 ? -7.518  23.610  132.583 1.00 52.99 ? 234  MET B CB  1 
ATOM   4576  C  CG  . MET B 1 234 ? -7.754  22.753  133.798 1.00 58.32 ? 234  MET B CG  1 
ATOM   4577  S  SD  . MET B 1 234 ? -8.514  21.137  133.401 1.00 73.59 ? 234  MET B SD  1 
ATOM   4578  C  CE  . MET B 1 234 ? -7.119  20.000  133.351 1.00 72.43 ? 234  MET B CE  1 
ATOM   4579  N  N   . ILE B 1 235 ? -10.166 25.219  131.631 1.00 47.67 ? 235  ILE B N   1 
ATOM   4580  C  CA  . ILE B 1 235 ? -11.468 25.790  131.949 1.00 47.21 ? 235  ILE B CA  1 
ATOM   4581  C  C   . ILE B 1 235 ? -12.533 25.200  131.002 1.00 50.66 ? 235  ILE B C   1 
ATOM   4582  O  O   . ILE B 1 235 ? -13.673 24.910  131.422 1.00 49.73 ? 235  ILE B O   1 
ATOM   4583  C  CB  . ILE B 1 235 ? -11.445 27.344  131.838 1.00 47.92 ? 235  ILE B CB  1 
ATOM   4584  C  CG1 . ILE B 1 235 ? -10.706 27.924  133.034 1.00 46.39 ? 235  ILE B CG1 1 
ATOM   4585  C  CG2 . ILE B 1 235 ? -12.856 27.915  131.812 1.00 39.57 ? 235  ILE B CG2 1 
ATOM   4586  C  CD1 . ILE B 1 235 ? -11.361 27.593  134.368 1.00 51.75 ? 235  ILE B CD1 1 
ATOM   4587  N  N   . LEU B 1 236 ? -12.178 25.014  129.730 1.00 50.24 ? 236  LEU B N   1 
ATOM   4588  C  CA  . LEU B 1 236 ? -13.139 24.432  128.802 1.00 51.85 ? 236  LEU B CA  1 
ATOM   4589  C  C   . LEU B 1 236 ? -13.558 23.009  129.228 1.00 53.65 ? 236  LEU B C   1 
ATOM   4590  O  O   . LEU B 1 236 ? -14.736 22.659  129.122 1.00 55.48 ? 236  LEU B O   1 
ATOM   4591  C  CB  . LEU B 1 236 ? -12.574 24.421  127.384 1.00 52.45 ? 236  LEU B CB  1 
ATOM   4592  C  CG  . LEU B 1 236 ? -12.574 25.781  126.686 1.00 51.26 ? 236  LEU B CG  1 
ATOM   4593  C  CD1 . LEU B 1 236 ? -11.663 25.743  125.485 1.00 50.22 ? 236  LEU B CD1 1 
ATOM   4594  C  CD2 . LEU B 1 236 ? -13.995 26.151  126.307 1.00 47.12 ? 236  LEU B CD2 1 
ATOM   4595  N  N   . ASN B 1 237 ? -12.609 22.195  129.698 1.00 52.52 ? 237  ASN B N   1 
ATOM   4596  C  CA  . ASN B 1 237 ? -12.938 20.840  130.156 1.00 55.62 ? 237  ASN B CA  1 
ATOM   4597  C  C   . ASN B 1 237 ? -13.788 20.950  131.411 1.00 53.78 ? 237  ASN B C   1 
ATOM   4598  O  O   . ASN B 1 237 ? -14.723 20.168  131.634 1.00 51.08 ? 237  ASN B O   1 
ATOM   4599  C  CB  . ASN B 1 237 ? -11.674 20.013  130.488 1.00 60.71 ? 237  ASN B CB  1 
ATOM   4600  C  CG  . ASN B 1 237 ? -11.028 19.383  129.243 1.00 67.06 ? 237  ASN B CG  1 
ATOM   4601  O  OD1 . ASN B 1 237 ? -11.587 19.429  128.131 1.00 67.42 ? 237  ASN B OD1 1 
ATOM   4602  N  ND2 . ASN B 1 237 ? -9.844  18.794  129.427 1.00 66.88 ? 237  ASN B ND2 1 
ATOM   4603  N  N   . GLU B 1 238 ? -13.443 21.937  132.227 1.00 52.84 ? 238  GLU B N   1 
ATOM   4604  C  CA  . GLU B 1 238 ? -14.143 22.187  133.472 1.00 51.11 ? 238  GLU B CA  1 
ATOM   4605  C  C   . GLU B 1 238 ? -15.610 22.445  133.137 1.00 49.27 ? 238  GLU B C   1 
ATOM   4606  O  O   . GLU B 1 238 ? -16.517 21.937  133.827 1.00 44.56 ? 238  GLU B O   1 
ATOM   4607  C  CB  . GLU B 1 238 ? -13.506 23.387  134.166 1.00 54.63 ? 238  GLU B CB  1 
ATOM   4608  C  CG  . GLU B 1 238 ? -13.286 23.224  135.654 1.00 59.31 ? 238  GLU B CG  1 
ATOM   4609  C  CD  . GLU B 1 238 ? -12.583 21.920  136.024 1.00 63.06 ? 238  GLU B CD  1 
ATOM   4610  O  OE1 . GLU B 1 238 ? -13.203 20.845  135.846 1.00 62.43 ? 238  GLU B OE1 1 
ATOM   4611  O  OE2 . GLU B 1 238 ? -11.419 21.970  136.496 1.00 61.64 ? 238  GLU B OE2 1 
ATOM   4612  N  N   . ILE B 1 239 ? -15.847 23.209  132.068 1.00 46.65 ? 239  ILE B N   1 
ATOM   4613  C  CA  . ILE B 1 239 ? -17.224 23.492  131.667 1.00 45.95 ? 239  ILE B CA  1 
ATOM   4614  C  C   . ILE B 1 239 ? -17.870 22.183  131.311 1.00 45.26 ? 239  ILE B C   1 
ATOM   4615  O  O   . ILE B 1 239 ? -18.993 21.914  131.731 1.00 42.37 ? 239  ILE B O   1 
ATOM   4616  C  CB  . ILE B 1 239 ? -17.317 24.427  130.439 1.00 47.10 ? 239  ILE B CB  1 
ATOM   4617  C  CG1 . ILE B 1 239 ? -16.771 25.806  130.808 1.00 46.94 ? 239  ILE B CG1 1 
ATOM   4618  C  CG2 . ILE B 1 239 ? -18.791 24.571  129.985 1.00 44.86 ? 239  ILE B CG2 1 
ATOM   4619  C  CD1 . ILE B 1 239 ? -16.808 26.796  129.681 1.00 45.78 ? 239  ILE B CD1 1 
ATOM   4620  N  N   . LYS B 1 240 ? -17.150 21.382  130.527 1.00 46.65 ? 240  LYS B N   1 
ATOM   4621  C  CA  . LYS B 1 240 ? -17.619 20.073  130.102 1.00 49.82 ? 240  LYS B CA  1 
ATOM   4622  C  C   . LYS B 1 240 ? -17.980 19.173  131.296 1.00 52.10 ? 240  LYS B C   1 
ATOM   4623  O  O   . LYS B 1 240 ? -18.965 18.414  131.250 1.00 50.90 ? 240  LYS B O   1 
ATOM   4624  C  CB  . LYS B 1 240 ? -16.561 19.394  129.218 1.00 52.94 ? 240  LYS B CB  1 
ATOM   4625  C  CG  . LYS B 1 240 ? -16.781 19.646  127.721 1.00 56.73 ? 240  LYS B CG  1 
ATOM   4626  C  CD  . LYS B 1 240 ? -15.686 19.061  126.834 1.00 58.61 ? 240  LYS B CD  1 
ATOM   4627  C  CE  . LYS B 1 240 ? -14.368 19.796  127.013 1.00 61.21 ? 240  LYS B CE  1 
ATOM   4628  N  NZ  . LYS B 1 240 ? -13.490 19.692  125.814 1.00 61.50 ? 240  LYS B NZ  1 
ATOM   4629  N  N   . GLN B 1 241 ? -17.188 19.249  132.361 1.00 51.47 ? 241  GLN B N   1 
ATOM   4630  C  CA  . GLN B 1 241 ? -17.472 18.452  133.543 1.00 54.60 ? 241  GLN B CA  1 
ATOM   4631  C  C   . GLN B 1 241 ? -18.746 18.932  134.229 1.00 55.81 ? 241  GLN B C   1 
ATOM   4632  O  O   . GLN B 1 241 ? -19.205 18.299  135.164 1.00 58.52 ? 241  GLN B O   1 
ATOM   4633  C  CB  . GLN B 1 241 ? -16.303 18.510  134.536 1.00 59.37 ? 241  GLN B CB  1 
ATOM   4634  C  CG  . GLN B 1 241 ? -15.232 17.456  134.310 1.00 65.53 ? 241  GLN B CG  1 
ATOM   4635  C  CD  . GLN B 1 241 ? -15.800 16.021  134.375 1.00 73.62 ? 241  GLN B CD  1 
ATOM   4636  O  OE1 . GLN B 1 241 ? -16.405 15.618  135.384 1.00 73.94 ? 241  GLN B OE1 1 
ATOM   4637  N  NE2 . GLN B 1 241 ? -15.606 15.248  133.299 1.00 71.69 ? 241  GLN B NE2 1 
ATOM   4638  N  N   . GLY B 1 242 ? -19.316 20.046  133.771 1.00 55.30 ? 242  GLY B N   1 
ATOM   4639  C  CA  . GLY B 1 242 ? -20.530 20.562  134.383 1.00 52.52 ? 242  GLY B CA  1 
ATOM   4640  C  C   . GLY B 1 242 ? -20.303 21.495  135.572 1.00 52.30 ? 242  GLY B C   1 
ATOM   4641  O  O   . GLY B 1 242 ? -21.230 21.782  136.328 1.00 51.36 ? 242  GLY B O   1 
ATOM   4642  N  N   . LYS B 1 243 ? -19.078 21.993  135.719 1.00 51.19 ? 243  LYS B N   1 
ATOM   4643  C  CA  . LYS B 1 243 ? -18.705 22.894  136.813 1.00 49.43 ? 243  LYS B CA  1 
ATOM   4644  C  C   . LYS B 1 243 ? -19.243 24.348  136.753 1.00 47.12 ? 243  LYS B C   1 
ATOM   4645  O  O   . LYS B 1 243 ? -18.945 25.157  137.628 1.00 44.81 ? 243  LYS B O   1 
ATOM   4646  C  CB  . LYS B 1 243 ? -17.171 22.937  136.914 1.00 53.67 ? 243  LYS B CB  1 
ATOM   4647  C  CG  . LYS B 1 243 ? -16.507 21.576  137.070 1.00 56.29 ? 243  LYS B CG  1 
ATOM   4648  C  CD  . LYS B 1 243 ? -16.735 20.996  138.455 1.00 58.93 ? 243  LYS B CD  1 
ATOM   4649  C  CE  . LYS B 1 243 ? -15.890 19.742  138.670 1.00 66.80 ? 243  LYS B CE  1 
ATOM   4650  N  NZ  . LYS B 1 243 ? -14.395 19.887  138.415 1.00 69.70 ? 243  LYS B NZ  1 
ATOM   4651  N  N   . PHE B 1 244 ? -20.008 24.693  135.724 1.00 44.28 ? 244  PHE B N   1 
ATOM   4652  C  CA  . PHE B 1 244 ? -20.540 26.039  135.622 1.00 41.19 ? 244  PHE B CA  1 
ATOM   4653  C  C   . PHE B 1 244 ? -22.028 26.098  135.329 1.00 43.61 ? 244  PHE B C   1 
ATOM   4654  O  O   . PHE B 1 244 ? -22.458 26.048  134.188 1.00 43.72 ? 244  PHE B O   1 
ATOM   4655  C  CB  . PHE B 1 244 ? -19.803 26.824  134.557 1.00 38.36 ? 244  PHE B CB  1 
ATOM   4656  C  CG  . PHE B 1 244 ? -18.377 27.120  134.903 1.00 40.90 ? 244  PHE B CG  1 
ATOM   4657  C  CD1 . PHE B 1 244 ? -17.373 26.222  134.577 1.00 41.40 ? 244  PHE B CD1 1 
ATOM   4658  C  CD2 . PHE B 1 244 ? -18.033 28.310  135.534 1.00 35.39 ? 244  PHE B CD2 1 
ATOM   4659  C  CE1 . PHE B 1 244 ? -16.045 26.514  134.872 1.00 45.31 ? 244  PHE B CE1 1 
ATOM   4660  C  CE2 . PHE B 1 244 ? -16.713 28.599  135.833 1.00 38.40 ? 244  PHE B CE2 1 
ATOM   4661  C  CZ  . PHE B 1 244 ? -15.713 27.712  135.504 1.00 38.04 ? 244  PHE B CZ  1 
ATOM   4662  N  N   . HIS B 1 245 ? -22.821 26.215  136.374 1.00 47.09 ? 245  HIS B N   1 
ATOM   4663  C  CA  . HIS B 1 245 ? -24.254 26.313  136.220 1.00 50.81 ? 245  HIS B CA  1 
ATOM   4664  C  C   . HIS B 1 245 ? -24.676 27.624  136.902 1.00 48.60 ? 245  HIS B C   1 
ATOM   4665  O  O   . HIS B 1 245 ? -25.682 28.229  136.537 1.00 48.27 ? 245  HIS B O   1 
ATOM   4666  C  CB  . HIS B 1 245 ? -24.925 25.082  136.871 1.00 60.01 ? 245  HIS B CB  1 
ATOM   4667  C  CG  . HIS B 1 245 ? -25.805 25.395  138.058 1.00 73.56 ? 245  HIS B CG  1 
ATOM   4668  N  ND1 . HIS B 1 245 ? -27.110 25.835  137.935 1.00 79.05 ? 245  HIS B ND1 1 
ATOM   4669  C  CD2 . HIS B 1 245 ? -25.564 25.323  139.393 1.00 75.77 ? 245  HIS B CD2 1 
ATOM   4670  C  CE1 . HIS B 1 245 ? -27.631 26.018  139.139 1.00 77.99 ? 245  HIS B CE1 1 
ATOM   4671  N  NE2 . HIS B 1 245 ? -26.713 25.716  140.040 1.00 76.76 ? 245  HIS B NE2 1 
ATOM   4672  N  N   . ASN B 1 246 ? -23.874 28.059  137.875 1.00 45.45 ? 246  ASN B N   1 
ATOM   4673  C  CA  . ASN B 1 246 ? -24.148 29.257  138.651 1.00 41.37 ? 246  ASN B CA  1 
ATOM   4674  C  C   . ASN B 1 246 ? -23.887 30.560  137.903 1.00 40.75 ? 246  ASN B C   1 
ATOM   4675  O  O   . ASN B 1 246 ? -22.764 30.854  137.477 1.00 41.26 ? 246  ASN B O   1 
ATOM   4676  C  CB  . ASN B 1 246 ? -23.335 29.237  139.936 1.00 40.66 ? 246  ASN B CB  1 
ATOM   4677  C  CG  . ASN B 1 246 ? -23.581 30.455  140.782 1.00 44.05 ? 246  ASN B CG  1 
ATOM   4678  O  OD1 . ASN B 1 246 ? -22.638 31.126  141.196 1.00 49.58 ? 246  ASN B OD1 1 
ATOM   4679  N  ND2 . ASN B 1 246 ? -24.851 30.759  141.043 1.00 37.25 ? 246  ASN B ND2 1 
ATOM   4680  N  N   . PRO B 1 247 ? -24.939 31.377  137.757 1.00 40.93 ? 247  PRO B N   1 
ATOM   4681  C  CA  . PRO B 1 247 ? -24.860 32.664  137.052 1.00 39.50 ? 247  PRO B CA  1 
ATOM   4682  C  C   . PRO B 1 247 ? -23.651 33.538  137.355 1.00 40.42 ? 247  PRO B C   1 
ATOM   4683  O  O   . PRO B 1 247 ? -22.971 34.021  136.435 1.00 39.73 ? 247  PRO B O   1 
ATOM   4684  C  CB  . PRO B 1 247 ? -26.178 33.324  137.424 1.00 38.06 ? 247  PRO B CB  1 
ATOM   4685  C  CG  . PRO B 1 247 ? -27.132 32.096  137.496 1.00 33.22 ? 247  PRO B CG  1 
ATOM   4686  C  CD  . PRO B 1 247 ? -26.314 31.108  138.246 1.00 33.93 ? 247  PRO B CD  1 
ATOM   4687  N  N   . MET B 1 248 ? -23.376 33.744  138.636 1.00 41.45 ? 248  MET B N   1 
ATOM   4688  C  CA  . MET B 1 248 ? -22.256 34.583  139.038 1.00 42.75 ? 248  MET B CA  1 
ATOM   4689  C  C   . MET B 1 248 ? -20.913 33.929  138.621 1.00 41.54 ? 248  MET B C   1 
ATOM   4690  O  O   . MET B 1 248 ? -20.007 34.588  138.111 1.00 40.45 ? 248  MET B O   1 
ATOM   4691  C  CB  . MET B 1 248 ? -22.357 34.852  140.561 1.00 44.29 ? 248  MET B CB  1 
ATOM   4692  C  CG  . MET B 1 248 ? -21.241 35.689  141.151 1.00 47.93 ? 248  MET B CG  1 
ATOM   4693  S  SD  . MET B 1 248 ? -20.978 37.257  140.308 1.00 52.53 ? 248  MET B SD  1 
ATOM   4694  C  CE  . MET B 1 248 ? -21.851 38.371  141.379 1.00 54.35 ? 248  MET B CE  1 
ATOM   4695  N  N   . SER B 1 249 ? -20.797 32.622  138.802 1.00 44.25 ? 249  SER B N   1 
ATOM   4696  C  CA  . SER B 1 249 ? -19.565 31.926  138.427 1.00 44.33 ? 249  SER B CA  1 
ATOM   4697  C  C   . SER B 1 249 ? -19.313 32.093  136.933 1.00 43.72 ? 249  SER B C   1 
ATOM   4698  O  O   . SER B 1 249 ? -18.161 32.255  136.496 1.00 44.79 ? 249  SER B O   1 
ATOM   4699  C  CB  . SER B 1 249 ? -19.669 30.424  138.753 1.00 42.29 ? 249  SER B CB  1 
ATOM   4700  O  OG  . SER B 1 249 ? -20.054 30.207  140.102 1.00 39.78 ? 249  SER B OG  1 
ATOM   4701  N  N   . ILE B 1 250 ? -20.395 32.027  136.151 1.00 40.85 ? 250  ILE B N   1 
ATOM   4702  C  CA  . ILE B 1 250 ? -20.301 32.167  134.703 1.00 39.03 ? 250  ILE B CA  1 
ATOM   4703  C  C   . ILE B 1 250 ? -19.919 33.599  134.320 1.00 39.65 ? 250  ILE B C   1 
ATOM   4704  O  O   . ILE B 1 250 ? -19.092 33.820  133.431 1.00 39.92 ? 250  ILE B O   1 
ATOM   4705  C  CB  . ILE B 1 250 ? -21.644 31.772  134.023 1.00 40.05 ? 250  ILE B CB  1 
ATOM   4706  C  CG1 . ILE B 1 250 ? -22.032 30.339  134.434 1.00 41.88 ? 250  ILE B CG1 1 
ATOM   4707  C  CG2 . ILE B 1 250 ? -21.518 31.880  132.494 1.00 37.57 ? 250  ILE B CG2 1 
ATOM   4708  C  CD1 . ILE B 1 250 ? -23.441 29.906  134.026 1.00 35.85 ? 250  ILE B CD1 1 
ATOM   4709  N  N   . ALA B 1 251 ? -20.521 34.569  135.007 1.00 38.82 ? 251  ALA B N   1 
ATOM   4710  C  CA  . ALA B 1 251 ? -20.240 35.971  134.752 1.00 36.56 ? 251  ALA B CA  1 
ATOM   4711  C  C   . ALA B 1 251 ? -18.775 36.254  134.976 1.00 36.95 ? 251  ALA B C   1 
ATOM   4712  O  O   . ALA B 1 251 ? -18.208 37.185  134.389 1.00 39.59 ? 251  ALA B O   1 
ATOM   4713  C  CB  . ALA B 1 251 ? -21.070 36.840  135.657 1.00 35.90 ? 251  ALA B CB  1 
ATOM   4714  N  N   . GLN B 1 252 ? -18.143 35.449  135.821 1.00 38.75 ? 252  GLN B N   1 
ATOM   4715  C  CA  . GLN B 1 252 ? -16.739 35.666  136.098 1.00 36.67 ? 252  GLN B CA  1 
ATOM   4716  C  C   . GLN B 1 252 ? -15.742 34.937  135.231 1.00 37.24 ? 252  GLN B C   1 
ATOM   4717  O  O   . GLN B 1 252 ? -14.544 35.217  135.329 1.00 39.92 ? 252  GLN B O   1 
ATOM   4718  C  CB  . GLN B 1 252 ? -16.482 35.474  137.581 1.00 35.83 ? 252  GLN B CB  1 
ATOM   4719  C  CG  . GLN B 1 252 ? -17.147 36.594  138.371 1.00 35.14 ? 252  GLN B CG  1 
ATOM   4720  C  CD  . GLN B 1 252 ? -16.876 36.547  139.870 1.00 39.52 ? 252  GLN B CD  1 
ATOM   4721  O  OE1 . GLN B 1 252 ? -16.774 35.463  140.456 1.00 39.91 ? 252  GLN B OE1 1 
ATOM   4722  N  NE2 . GLN B 1 252 ? -16.786 37.728  140.506 1.00 35.63 ? 252  GLN B NE2 1 
ATOM   4723  N  N   . ILE B 1 253 ? -16.198 34.020  134.377 1.00 36.45 ? 253  ILE B N   1 
ATOM   4724  C  CA  . ILE B 1 253 ? -15.255 33.394  133.429 1.00 39.78 ? 253  ILE B CA  1 
ATOM   4725  C  C   . ILE B 1 253 ? -15.558 33.858  132.008 1.00 39.33 ? 253  ILE B C   1 
ATOM   4726  O  O   . ILE B 1 253 ? -14.656 33.924  131.173 1.00 41.11 ? 253  ILE B O   1 
ATOM   4727  C  CB  . ILE B 1 253 ? -15.292 31.821  133.314 1.00 41.22 ? 253  ILE B CB  1 
ATOM   4728  C  CG1 . ILE B 1 253 ? -16.464 31.270  134.092 1.00 44.40 ? 253  ILE B CG1 1 
ATOM   4729  C  CG2 . ILE B 1 253 ? -13.914 31.223  133.603 1.00 37.47 ? 253  ILE B CG2 1 
ATOM   4730  C  CD1 . ILE B 1 253 ? -17.680 31.152  133.238 1.00 48.36 ? 253  ILE B CD1 1 
ATOM   4731  N  N   . LEU B 1 254 ? -16.816 34.160  131.720 1.00 37.55 ? 254  LEU B N   1 
ATOM   4732  C  CA  . LEU B 1 254 ? -17.171 34.550  130.364 1.00 39.45 ? 254  LEU B CA  1 
ATOM   4733  C  C   . LEU B 1 254 ? -16.205 35.556  129.712 1.00 41.91 ? 254  LEU B C   1 
ATOM   4734  O  O   . LEU B 1 254 ? -15.629 35.280  128.659 1.00 41.71 ? 254  LEU B O   1 
ATOM   4735  C  CB  . LEU B 1 254 ? -18.584 35.109  130.333 1.00 41.97 ? 254  LEU B CB  1 
ATOM   4736  C  CG  . LEU B 1 254 ? -19.435 34.523  129.225 1.00 46.53 ? 254  LEU B CG  1 
ATOM   4737  C  CD1 . LEU B 1 254 ? -20.722 35.352  129.075 1.00 44.88 ? 254  LEU B CD1 1 
ATOM   4738  C  CD2 . LEU B 1 254 ? -18.619 34.500  127.939 1.00 47.55 ? 254  LEU B CD2 1 
ATOM   4739  N  N   . PRO B 1 255 ? -15.979 36.722  130.353 1.00 41.19 ? 255  PRO B N   1 
ATOM   4740  C  CA  . PRO B 1 255 ? -15.079 37.707  129.758 1.00 38.79 ? 255  PRO B CA  1 
ATOM   4741  C  C   . PRO B 1 255 ? -13.765 37.110  129.288 1.00 39.50 ? 255  PRO B C   1 
ATOM   4742  O  O   . PRO B 1 255 ? -13.326 37.354  128.161 1.00 39.59 ? 255  PRO B O   1 
ATOM   4743  C  CB  . PRO B 1 255 ? -14.903 38.740  130.876 1.00 38.44 ? 255  PRO B CB  1 
ATOM   4744  C  CG  . PRO B 1 255 ? -16.190 38.624  131.637 1.00 38.28 ? 255  PRO B CG  1 
ATOM   4745  C  CD  . PRO B 1 255 ? -16.371 37.134  131.712 1.00 39.67 ? 255  PRO B CD  1 
ATOM   4746  N  N   . SER B 1 256 ? -13.131 36.327  130.149 1.00 42.68 ? 256  SER B N   1 
ATOM   4747  C  CA  . SER B 1 256 ? -11.851 35.720  129.793 1.00 45.18 ? 256  SER B CA  1 
ATOM   4748  C  C   . SER B 1 256 ? -12.038 34.840  128.570 1.00 47.01 ? 256  SER B C   1 
ATOM   4749  O  O   . SER B 1 256 ? -11.238 34.867  127.639 1.00 47.86 ? 256  SER B O   1 
ATOM   4750  C  CB  . SER B 1 256 ? -11.306 34.868  130.941 1.00 43.08 ? 256  SER B CB  1 
ATOM   4751  O  OG  . SER B 1 256 ? -10.904 35.668  132.029 1.00 44.70 ? 256  SER B OG  1 
ATOM   4752  N  N   . LEU B 1 257 ? -13.117 34.069  128.567 1.00 48.17 ? 257  LEU B N   1 
ATOM   4753  C  CA  . LEU B 1 257 ? -13.392 33.175  127.458 1.00 49.96 ? 257  LEU B CA  1 
ATOM   4754  C  C   . LEU B 1 257 ? -13.657 33.930  126.140 1.00 51.65 ? 257  LEU B C   1 
ATOM   4755  O  O   . LEU B 1 257 ? -13.688 33.336  125.052 1.00 52.79 ? 257  LEU B O   1 
ATOM   4756  C  CB  . LEU B 1 257 ? -14.572 32.255  127.828 1.00 47.92 ? 257  LEU B CB  1 
ATOM   4757  C  CG  . LEU B 1 257 ? -14.259 31.207  128.930 1.00 49.23 ? 257  LEU B CG  1 
ATOM   4758  C  CD1 . LEU B 1 257 ? -15.525 30.383  129.233 1.00 45.29 ? 257  LEU B CD1 1 
ATOM   4759  C  CD2 . LEU B 1 257 ? -13.105 30.269  128.496 1.00 44.22 ? 257  LEU B CD2 1 
ATOM   4760  N  N   . LYS B 1 258 ? -13.804 35.245  126.242 1.00 50.80 ? 258  LYS B N   1 
ATOM   4761  C  CA  . LYS B 1 258 ? -14.090 36.074  125.088 1.00 47.47 ? 258  LYS B CA  1 
ATOM   4762  C  C   . LYS B 1 258 ? -12.936 37.008  124.770 1.00 47.19 ? 258  LYS B C   1 
ATOM   4763  O  O   . LYS B 1 258 ? -13.096 37.934  123.983 1.00 49.87 ? 258  LYS B O   1 
ATOM   4764  C  CB  . LYS B 1 258 ? -15.357 36.893  125.353 1.00 48.70 ? 258  LYS B CB  1 
ATOM   4765  C  CG  . LYS B 1 258 ? -16.633 36.071  125.431 1.00 49.11 ? 258  LYS B CG  1 
ATOM   4766  C  CD  . LYS B 1 258 ? -16.912 35.467  124.086 1.00 54.61 ? 258  LYS B CD  1 
ATOM   4767  C  CE  . LYS B 1 258 ? -18.289 34.826  123.998 1.00 58.66 ? 258  LYS B CE  1 
ATOM   4768  N  NZ  . LYS B 1 258 ? -18.560 34.386  122.611 1.00 54.87 ? 258  LYS B NZ  1 
ATOM   4769  N  N   . GLY B 1 259 ? -11.773 36.777  125.373 1.00 43.95 ? 259  GLY B N   1 
ATOM   4770  C  CA  . GLY B 1 259 ? -10.643 37.657  125.108 1.00 39.42 ? 259  GLY B CA  1 
ATOM   4771  C  C   . GLY B 1 259 ? -10.844 39.060  125.676 1.00 43.14 ? 259  GLY B C   1 
ATOM   4772  O  O   . GLY B 1 259 ? -10.263 40.039  125.199 1.00 44.77 ? 259  GLY B O   1 
ATOM   4773  N  N   . LYS B 1 260 ? -11.656 39.180  126.719 1.00 42.20 ? 260  LYS B N   1 
ATOM   4774  C  CA  . LYS B 1 260 ? -11.897 40.495  127.302 1.00 43.02 ? 260  LYS B CA  1 
ATOM   4775  C  C   . LYS B 1 260 ? -11.551 40.570  128.787 1.00 41.68 ? 260  LYS B C   1 
ATOM   4776  O  O   . LYS B 1 260 ? -11.424 39.543  129.469 1.00 44.06 ? 260  LYS B O   1 
ATOM   4777  C  CB  . LYS B 1 260 ? -13.382 40.857  127.142 1.00 45.62 ? 260  LYS B CB  1 
ATOM   4778  C  CG  . LYS B 1 260 ? -13.940 40.736  125.729 1.00 48.03 ? 260  LYS B CG  1 
ATOM   4779  C  CD  . LYS B 1 260 ? -13.417 41.850  124.903 1.00 52.86 ? 260  LYS B CD  1 
ATOM   4780  C  CE  . LYS B 1 260 ? -14.262 42.084  123.687 1.00 55.83 ? 260  LYS B CE  1 
ATOM   4781  N  NZ  . LYS B 1 260 ? -13.888 43.391  123.079 1.00 58.36 ? 260  LYS B NZ  1 
ATOM   4782  N  N   . THR B 1 261 ? -11.385 41.791  129.285 1.00 40.17 ? 261  THR B N   1 
ATOM   4783  C  CA  . THR B 1 261 ? -11.176 42.001  130.725 1.00 41.32 ? 261  THR B CA  1 
ATOM   4784  C  C   . THR B 1 261 ? -12.043 43.201  131.065 1.00 40.11 ? 261  THR B C   1 
ATOM   4785  O  O   . THR B 1 261 ? -12.561 43.866  130.167 1.00 38.04 ? 261  THR B O   1 
ATOM   4786  C  CB  . THR B 1 261 ? -9.730  42.346  131.125 1.00 40.50 ? 261  THR B CB  1 
ATOM   4787  O  OG1 . THR B 1 261 ? -9.415  43.682  130.712 1.00 43.37 ? 261  THR B OG1 1 
ATOM   4788  C  CG2 . THR B 1 261 ? -8.774  41.364  130.525 1.00 35.62 ? 261  THR B CG2 1 
ATOM   4789  N  N   . TYR B 1 262 ? -12.210 43.479  132.351 1.00 38.33 ? 262  TYR B N   1 
ATOM   4790  C  CA  . TYR B 1 262 ? -13.019 44.620  132.759 1.00 34.30 ? 262  TYR B CA  1 
ATOM   4791  C  C   . TYR B 1 262 ? -12.383 45.916  132.273 1.00 34.18 ? 262  TYR B C   1 
ATOM   4792  O  O   . TYR B 1 262 ? -12.998 46.983  132.335 1.00 34.33 ? 262  TYR B O   1 
ATOM   4793  C  CB  . TYR B 1 262 ? -13.147 44.672  134.280 1.00 35.75 ? 262  TYR B CB  1 
ATOM   4794  C  CG  . TYR B 1 262 ? -13.999 43.588  134.889 1.00 36.63 ? 262  TYR B CG  1 
ATOM   4795  C  CD1 . TYR B 1 262 ? -14.950 42.903  134.125 1.00 35.01 ? 262  TYR B CD1 1 
ATOM   4796  C  CD2 . TYR B 1 262 ? -13.909 43.296  136.245 1.00 34.44 ? 262  TYR B CD2 1 
ATOM   4797  C  CE1 . TYR B 1 262 ? -15.785 41.962  134.705 1.00 35.42 ? 262  TYR B CE1 1 
ATOM   4798  C  CE2 . TYR B 1 262 ? -14.748 42.361  136.828 1.00 32.89 ? 262  TYR B CE2 1 
ATOM   4799  C  CZ  . TYR B 1 262 ? -15.680 41.701  136.055 1.00 33.55 ? 262  TYR B CZ  1 
ATOM   4800  O  OH  . TYR B 1 262 ? -16.519 40.777  136.634 1.00 38.17 ? 262  TYR B OH  1 
ATOM   4801  N  N   . LEU B 1 263 ? -11.138 45.852  131.825 1.00 33.11 ? 263  LEU B N   1 
ATOM   4802  C  CA  . LEU B 1 263 ? -10.505 47.074  131.353 1.00 35.42 ? 263  LEU B CA  1 
ATOM   4803  C  C   . LEU B 1 263 ? -11.097 47.451  130.009 1.00 36.00 ? 263  LEU B C   1 
ATOM   4804  O  O   . LEU B 1 263 ? -10.891 48.560  129.546 1.00 36.32 ? 263  LEU B O   1 
ATOM   4805  C  CB  . LEU B 1 263 ? -8.985  46.918  131.198 1.00 33.10 ? 263  LEU B CB  1 
ATOM   4806  C  CG  . LEU B 1 263 ? -8.173  46.680  132.469 1.00 34.61 ? 263  LEU B CG  1 
ATOM   4807  C  CD1 . LEU B 1 263 ? -6.723  46.797  132.152 1.00 30.50 ? 263  LEU B CD1 1 
ATOM   4808  C  CD2 . LEU B 1 263 ? -8.547  47.693  133.520 1.00 29.35 ? 263  LEU B CD2 1 
ATOM   4809  N  N   . ASP B 1 264 ? -11.830 46.534  129.386 1.00 35.40 ? 264  ASP B N   1 
ATOM   4810  C  CA  . ASP B 1 264 ? -12.419 46.812  128.082 1.00 38.62 ? 264  ASP B CA  1 
ATOM   4811  C  C   . ASP B 1 264 ? -13.762 47.478  128.183 1.00 42.08 ? 264  ASP B C   1 
ATOM   4812  O  O   . ASP B 1 264 ? -14.281 47.954  127.176 1.00 45.27 ? 264  ASP B O   1 
ATOM   4813  C  CB  . ASP B 1 264 ? -12.575 45.535  127.262 1.00 40.95 ? 264  ASP B CB  1 
ATOM   4814  C  CG  . ASP B 1 264 ? -11.255 44.875  126.992 1.00 44.41 ? 264  ASP B CG  1 
ATOM   4815  O  OD1 . ASP B 1 264 ? -10.323 45.618  126.632 1.00 44.85 ? 264  ASP B OD1 1 
ATOM   4816  O  OD2 . ASP B 1 264 ? -11.145 43.637  127.132 1.00 49.73 ? 264  ASP B OD2 1 
ATOM   4817  N  N   . VAL B 1 265 ? -14.320 47.520  129.390 1.00 43.19 ? 265  VAL B N   1 
ATOM   4818  C  CA  . VAL B 1 265 ? -15.624 48.127  129.604 1.00 44.78 ? 265  VAL B CA  1 
ATOM   4819  C  C   . VAL B 1 265 ? -15.783 49.516  128.953 1.00 44.11 ? 265  VAL B C   1 
ATOM   4820  O  O   . VAL B 1 265 ? -16.751 49.771  128.244 1.00 44.28 ? 265  VAL B O   1 
ATOM   4821  C  CB  . VAL B 1 265 ? -15.944 48.193  131.127 1.00 44.20 ? 265  VAL B CB  1 
ATOM   4822  C  CG1 . VAL B 1 265 ? -17.055 49.178  131.406 1.00 45.78 ? 265  VAL B CG1 1 
ATOM   4823  C  CG2 . VAL B 1 265 ? -16.383 46.819  131.611 1.00 44.21 ? 265  VAL B CG2 1 
ATOM   4824  N  N   . PRO B 1 266 ? -14.833 50.426  129.170 1.00 44.13 ? 266  PRO B N   1 
ATOM   4825  C  CA  . PRO B 1 266 ? -15.017 51.737  128.543 1.00 42.01 ? 266  PRO B CA  1 
ATOM   4826  C  C   . PRO B 1 266 ? -15.072 51.702  127.023 1.00 41.35 ? 266  PRO B C   1 
ATOM   4827  O  O   . PRO B 1 266 ? -15.659 52.588  126.422 1.00 43.09 ? 266  PRO B O   1 
ATOM   4828  C  CB  . PRO B 1 266 ? -13.816 52.532  129.043 1.00 40.82 ? 266  PRO B CB  1 
ATOM   4829  C  CG  . PRO B 1 266 ? -13.518 51.903  130.369 1.00 43.76 ? 266  PRO B CG  1 
ATOM   4830  C  CD  . PRO B 1 266 ? -13.661 50.427  130.060 1.00 43.68 ? 266  PRO B CD  1 
ATOM   4831  N  N   . GLN B 1 267 ? -14.470 50.691  126.399 1.00 40.63 ? 267  GLN B N   1 
ATOM   4832  C  CA  . GLN B 1 267 ? -14.452 50.594  124.935 1.00 39.88 ? 267  GLN B CA  1 
ATOM   4833  C  C   . GLN B 1 267 ? -15.592 49.829  124.273 1.00 41.30 ? 267  GLN B C   1 
ATOM   4834  O  O   . GLN B 1 267 ? -15.585 49.650  123.063 1.00 43.76 ? 267  GLN B O   1 
ATOM   4835  C  CB  . GLN B 1 267 ? -13.143 49.973  124.455 1.00 39.03 ? 267  GLN B CB  1 
ATOM   4836  C  CG  . GLN B 1 267 ? -11.963 50.897  124.457 1.00 44.05 ? 267  GLN B CG  1 
ATOM   4837  C  CD  . GLN B 1 267 ? -11.528 51.299  125.860 1.00 55.61 ? 267  GLN B CD  1 
ATOM   4838  O  OE1 . GLN B 1 267 ? -11.022 50.469  126.641 1.00 54.37 ? 267  GLN B OE1 1 
ATOM   4839  N  NE2 . GLN B 1 267 ? -11.721 52.585  126.194 1.00 56.33 ? 267  GLN B NE2 1 
ATOM   4840  N  N   . VAL B 1 268 ? -16.566 49.368  125.039 1.00 41.61 ? 268  VAL B N   1 
ATOM   4841  C  CA  . VAL B 1 268 ? -17.679 48.635  124.453 1.00 44.02 ? 268  VAL B CA  1 
ATOM   4842  C  C   . VAL B 1 268 ? -18.522 49.481  123.505 1.00 46.04 ? 268  VAL B C   1 
ATOM   4843  O  O   . VAL B 1 268 ? -18.833 50.634  123.800 1.00 50.16 ? 268  VAL B O   1 
ATOM   4844  C  CB  . VAL B 1 268 ? -18.610 48.082  125.559 1.00 43.35 ? 268  VAL B CB  1 
ATOM   4845  C  CG1 . VAL B 1 268 ? -19.900 47.561  124.953 1.00 43.00 ? 268  VAL B CG1 1 
ATOM   4846  C  CG2 . VAL B 1 268 ? -17.909 46.981  126.322 1.00 42.14 ? 268  VAL B CG2 1 
ATOM   4847  N  N   . THR B 1 269 ? -18.889 48.887  122.376 1.00 48.12 ? 269  THR B N   1 
ATOM   4848  C  CA  . THR B 1 269 ? -19.748 49.513  121.365 1.00 51.89 ? 269  THR B CA  1 
ATOM   4849  C  C   . THR B 1 269 ? -21.181 49.050  121.643 1.00 53.82 ? 269  THR B C   1 
ATOM   4850  O  O   . THR B 1 269 ? -21.405 47.867  121.875 1.00 55.48 ? 269  THR B O   1 
ATOM   4851  C  CB  . THR B 1 269 ? -19.388 49.024  119.961 1.00 52.91 ? 269  THR B CB  1 
ATOM   4852  O  OG1 . THR B 1 269 ? -18.058 49.437  119.648 1.00 52.98 ? 269  THR B OG1 1 
ATOM   4853  C  CG2 . THR B 1 269 ? -20.361 49.586  118.914 1.00 56.90 ? 269  THR B CG2 1 
ATOM   4854  N  N   . CYS B 1 270 ? -22.155 49.951  121.611 1.00 56.20 ? 270  CYS B N   1 
ATOM   4855  C  CA  . CYS B 1 270 ? -23.516 49.528  121.881 1.00 57.89 ? 270  CYS B CA  1 
ATOM   4856  C  C   . CYS B 1 270 ? -24.362 49.443  120.639 1.00 63.80 ? 270  CYS B C   1 
ATOM   4857  O  O   . CYS B 1 270 ? -24.170 50.199  119.688 1.00 60.07 ? 270  CYS B O   1 
ATOM   4858  C  CB  . CYS B 1 270 ? -24.155 50.430  122.921 1.00 54.91 ? 270  CYS B CB  1 
ATOM   4859  S  SG  . CYS B 1 270 ? -23.330 50.242  124.531 1.00 53.43 ? 270  CYS B SG  1 
ATOM   4860  N  N   . SER B 1 271 ? -25.311 48.504  120.695 1.00 74.91 ? 271  SER B N   1 
ATOM   4861  C  CA  . SER B 1 271 ? -26.245 48.140  119.609 1.00 81.89 ? 271  SER B CA  1 
ATOM   4862  C  C   . SER B 1 271 ? -25.409 47.653  118.434 1.00 86.63 ? 271  SER B C   1 
ATOM   4863  O  O   . SER B 1 271 ? -25.327 48.317  117.395 1.00 84.52 ? 271  SER B O   1 
ATOM   4864  C  CB  . SER B 1 271 ? -27.151 49.299  119.161 1.00 80.61 ? 271  SER B CB  1 
ATOM   4865  O  OG  . SER B 1 271 ? -28.215 48.786  118.368 1.00 77.91 ? 271  SER B OG  1 
ATOM   4866  N  N   . PRO B 1 272 ? -24.762 46.475  118.608 1.00 93.22 ? 272  PRO B N   1 
ATOM   4867  C  CA  . PRO B 1 272 ? -23.888 45.770  117.656 1.00 96.23 ? 272  PRO B CA  1 
ATOM   4868  C  C   . PRO B 1 272 ? -24.362 45.729  116.198 1.00 98.11 ? 272  PRO B C   1 
ATOM   4869  O  O   . PRO B 1 272 ? -25.565 45.766  115.900 1.00 99.30 ? 272  PRO B O   1 
ATOM   4870  C  CB  . PRO B 1 272 ? -23.766 44.370  118.271 1.00 95.76 ? 272  PRO B CB  1 
ATOM   4871  C  CG  . PRO B 1 272 ? -23.767 44.672  119.743 1.00 95.29 ? 272  PRO B CG  1 
ATOM   4872  C  CD  . PRO B 1 272 ? -24.905 45.681  119.851 1.00 94.41 ? 272  PRO B CD  1 
ATOM   4873  N  N   . ASP B 1 273 ? -23.388 45.653  115.299 1.00 98.42 ? 273  ASP B N   1 
ATOM   4874  C  CA  . ASP B 1 273 ? -23.648 45.602  113.871 1.00 99.18 ? 273  ASP B CA  1 
ATOM   4875  C  C   . ASP B 1 273 ? -23.530 44.132  113.440 1.00 99.45 ? 273  ASP B C   1 
ATOM   4876  O  O   . ASP B 1 273 ? -22.602 43.808  112.655 1.00 99.45 ? 273  ASP B O   1 
ATOM   4877  C  CB  . ASP B 1 273 ? -22.623 46.481  113.127 1.00 99.45 ? 273  ASP B CB  1 
ATOM   4878  C  CG  . ASP B 1 273 ? -23.021 46.767  111.674 1.00 99.45 ? 273  ASP B CG  1 
ATOM   4879  O  OD1 . ASP B 1 273 ? -23.152 45.800  110.885 1.00 99.45 ? 273  ASP B OD1 1 
ATOM   4880  O  OD2 . ASP B 1 273 ? -23.197 47.960  111.319 1.00 99.45 ? 273  ASP B OD2 1 
ATOM   4881  N  N   . SER C 1 7   ? -59.199 50.108  115.240 1.00 99.45 ? 7    SER C N   1 
ATOM   4882  C  CA  . SER C 1 7   ? -58.829 49.867  116.670 1.00 99.45 ? 7    SER C CA  1 
ATOM   4883  C  C   . SER C 1 7   ? -59.526 50.879  117.565 1.00 99.44 ? 7    SER C C   1 
ATOM   4884  O  O   . SER C 1 7   ? -59.585 50.719  118.793 1.00 99.27 ? 7    SER C O   1 
ATOM   4885  C  CB  . SER C 1 7   ? -57.310 49.997  116.867 1.00 99.45 ? 7    SER C CB  1 
ATOM   4886  O  OG  . SER C 1 7   ? -56.597 48.960  116.209 1.00 98.68 ? 7    SER C OG  1 
ATOM   4887  N  N   . CYS C 1 8   ? -60.058 51.920  116.936 1.00 98.44 ? 8    CYS C N   1 
ATOM   4888  C  CA  . CYS C 1 8   ? -60.722 52.984  117.669 1.00 96.73 ? 8    CYS C CA  1 
ATOM   4889  C  C   . CYS C 1 8   ? -61.733 53.725  116.812 1.00 94.92 ? 8    CYS C C   1 
ATOM   4890  O  O   . CYS C 1 8   ? -61.707 54.956  116.717 1.00 95.09 ? 8    CYS C O   1 
ATOM   4891  C  CB  . CYS C 1 8   ? -59.668 53.950  118.186 1.00 97.56 ? 8    CYS C CB  1 
ATOM   4892  S  SG  . CYS C 1 8   ? -58.293 54.135  117.000 1.00 99.45 ? 8    CYS C SG  1 
ATOM   4893  N  N   . SER C 1 9   ? -62.617 52.965  116.181 1.00 91.71 ? 9    SER C N   1 
ATOM   4894  C  CA  . SER C 1 9   ? -63.651 53.549  115.355 1.00 90.15 ? 9    SER C CA  1 
ATOM   4895  C  C   . SER C 1 9   ? -64.655 54.186  116.300 1.00 90.13 ? 9    SER C C   1 
ATOM   4896  O  O   . SER C 1 9   ? -64.539 54.052  117.521 1.00 87.58 ? 9    SER C O   1 
ATOM   4897  C  CB  . SER C 1 9   ? -64.326 52.462  114.546 1.00 89.06 ? 9    SER C CB  1 
ATOM   4898  O  OG  . SER C 1 9   ? -63.351 51.551  114.099 1.00 91.39 ? 9    SER C OG  1 
ATOM   4899  N  N   . VAL C 1 10  ? -65.635 54.892  115.747 1.00 90.70 ? 10   VAL C N   1 
ATOM   4900  C  CA  . VAL C 1 10  ? -66.637 55.505  116.597 1.00 91.19 ? 10   VAL C CA  1 
ATOM   4901  C  C   . VAL C 1 10  ? -67.682 54.443  116.870 1.00 92.81 ? 10   VAL C C   1 
ATOM   4902  O  O   . VAL C 1 10  ? -68.231 53.852  115.925 1.00 92.37 ? 10   VAL C O   1 
ATOM   4903  C  CB  . VAL C 1 10  ? -67.296 56.712  115.932 1.00 90.11 ? 10   VAL C CB  1 
ATOM   4904  C  CG1 . VAL C 1 10  ? -68.346 57.290  116.857 1.00 89.27 ? 10   VAL C CG1 1 
ATOM   4905  C  CG2 . VAL C 1 10  ? -66.244 57.763  115.625 1.00 90.94 ? 10   VAL C CG2 1 
ATOM   4906  N  N   . PRO C 1 11  ? -67.963 54.178  118.170 1.00 93.53 ? 11   PRO C N   1 
ATOM   4907  C  CA  . PRO C 1 11  ? -68.937 53.182  118.635 1.00 92.83 ? 11   PRO C CA  1 
ATOM   4908  C  C   . PRO C 1 11  ? -70.307 53.342  117.988 1.00 92.42 ? 11   PRO C C   1 
ATOM   4909  O  O   . PRO C 1 11  ? -70.938 54.390  118.128 1.00 91.35 ? 11   PRO C O   1 
ATOM   4910  C  CB  . PRO C 1 11  ? -68.998 53.428  120.150 1.00 91.46 ? 11   PRO C CB  1 
ATOM   4911  C  CG  . PRO C 1 11  ? -67.658 53.982  120.473 1.00 91.23 ? 11   PRO C CG  1 
ATOM   4912  C  CD  . PRO C 1 11  ? -67.421 54.931  119.321 1.00 93.17 ? 11   PRO C CD  1 
ATOM   4913  N  N   . SER C 1 12  ? -70.759 52.310  117.278 1.00 92.60 ? 12   SER C N   1 
ATOM   4914  C  CA  . SER C 1 12  ? -72.076 52.350  116.646 1.00 92.98 ? 12   SER C CA  1 
ATOM   4915  C  C   . SER C 1 12  ? -73.072 52.442  117.791 1.00 90.46 ? 12   SER C C   1 
ATOM   4916  O  O   . SER C 1 12  ? -73.590 51.433  118.269 1.00 90.30 ? 12   SER C O   1 
ATOM   4917  C  CB  . SER C 1 12  ? -72.326 51.078  115.830 1.00 95.94 ? 12   SER C CB  1 
ATOM   4918  O  OG  . SER C 1 12  ? -71.458 51.017  114.708 1.00 99.45 ? 12   SER C OG  1 
ATOM   4919  N  N   . ALA C 1 13  ? -73.324 53.670  118.223 1.00 86.69 ? 13   ALA C N   1 
ATOM   4920  C  CA  . ALA C 1 13  ? -74.212 53.945  119.342 1.00 83.38 ? 13   ALA C CA  1 
ATOM   4921  C  C   . ALA C 1 13  ? -74.001 55.420  119.577 1.00 80.25 ? 13   ALA C C   1 
ATOM   4922  O  O   . ALA C 1 13  ? -74.803 56.108  120.216 1.00 77.88 ? 13   ALA C O   1 
ATOM   4923  C  CB  . ALA C 1 13  ? -73.767 53.165  120.556 1.00 83.15 ? 13   ALA C CB  1 
ATOM   4924  N  N   . GLN C 1 14  ? -72.877 55.881  119.049 1.00 77.92 ? 14   GLN C N   1 
ATOM   4925  C  CA  . GLN C 1 14  ? -72.489 57.272  119.123 1.00 74.14 ? 14   GLN C CA  1 
ATOM   4926  C  C   . GLN C 1 14  ? -72.579 57.811  117.701 1.00 69.12 ? 14   GLN C C   1 
ATOM   4927  O  O   . GLN C 1 14  ? -72.530 59.021  117.484 1.00 69.88 ? 14   GLN C O   1 
ATOM   4928  C  CB  . GLN C 1 14  ? -71.058 57.387  119.664 1.00 77.44 ? 14   GLN C CB  1 
ATOM   4929  C  CG  . GLN C 1 14  ? -70.882 56.989  121.130 1.00 77.33 ? 14   GLN C CG  1 
ATOM   4930  C  CD  . GLN C 1 14  ? -71.499 57.995  122.088 1.00 81.76 ? 14   GLN C CD  1 
ATOM   4931  O  OE1 . GLN C 1 14  ? -70.996 58.198  123.190 1.00 81.99 ? 14   GLN C OE1 1 
ATOM   4932  N  NE2 . GLN C 1 14  ? -72.602 58.628  121.674 1.00 85.75 ? 14   GLN C NE2 1 
ATOM   4933  N  N   . GLU C 1 15  ? -72.725 56.902  116.738 1.00 63.45 ? 15   GLU C N   1 
ATOM   4934  C  CA  . GLU C 1 15  ? -72.820 57.306  115.348 1.00 60.47 ? 15   GLU C CA  1 
ATOM   4935  C  C   . GLU C 1 15  ? -73.829 58.443  115.168 1.00 57.41 ? 15   GLU C C   1 
ATOM   4936  O  O   . GLU C 1 15  ? -73.538 59.444  114.499 1.00 55.71 ? 15   GLU C O   1 
ATOM   4937  C  CB  . GLU C 1 15  ? -73.125 56.092  114.453 1.00 58.78 ? 15   GLU C CB  1 
ATOM   4938  C  CG  . GLU C 1 15  ? -71.815 55.354  114.111 1.00 65.06 ? 15   GLU C CG  1 
ATOM   4939  C  CD  . GLU C 1 15  ? -71.948 54.228  113.090 1.00 69.13 ? 15   GLU C CD  1 
ATOM   4940  O  OE1 . GLU C 1 15  ? -72.635 54.418  112.050 1.00 73.48 ? 15   GLU C OE1 1 
ATOM   4941  O  OE2 . GLU C 1 15  ? -71.336 53.159  113.328 1.00 64.34 ? 15   GLU C OE2 1 
ATOM   4942  N  N   . PRO C 1 16  ? -75.003 58.336  115.805 1.00 55.44 ? 16   PRO C N   1 
ATOM   4943  C  CA  . PRO C 1 16  ? -76.003 59.392  115.667 1.00 53.87 ? 16   PRO C CA  1 
ATOM   4944  C  C   . PRO C 1 16  ? -75.385 60.757  115.887 1.00 51.43 ? 16   PRO C C   1 
ATOM   4945  O  O   . PRO C 1 16  ? -75.744 61.748  115.255 1.00 53.09 ? 16   PRO C O   1 
ATOM   4946  C  CB  . PRO C 1 16  ? -77.008 59.047  116.762 1.00 51.10 ? 16   PRO C CB  1 
ATOM   4947  C  CG  . PRO C 1 16  ? -76.996 57.571  116.743 1.00 54.69 ? 16   PRO C CG  1 
ATOM   4948  C  CD  . PRO C 1 16  ? -75.505 57.277  116.699 1.00 57.33 ? 16   PRO C CD  1 
ATOM   4949  N  N   . LEU C 1 17  ? -74.429 60.788  116.788 1.00 47.49 ? 17   LEU C N   1 
ATOM   4950  C  CA  . LEU C 1 17  ? -73.773 62.023  117.158 1.00 45.38 ? 17   LEU C CA  1 
ATOM   4951  C  C   . LEU C 1 17  ? -72.885 62.540  116.061 1.00 44.16 ? 17   LEU C C   1 
ATOM   4952  O  O   . LEU C 1 17  ? -72.754 63.737  115.852 1.00 44.31 ? 17   LEU C O   1 
ATOM   4953  C  CB  . LEU C 1 17  ? -72.966 61.762  118.400 1.00 45.84 ? 17   LEU C CB  1 
ATOM   4954  C  CG  . LEU C 1 17  ? -72.719 62.858  119.419 1.00 46.65 ? 17   LEU C CG  1 
ATOM   4955  C  CD1 . LEU C 1 17  ? -73.848 63.835  119.596 1.00 45.14 ? 17   LEU C CD1 1 
ATOM   4956  C  CD2 . LEU C 1 17  ? -72.517 62.118  120.698 1.00 48.06 ? 17   LEU C CD2 1 
ATOM   4957  N  N   . VAL C 1 18  ? -72.260 61.626  115.352 1.00 43.72 ? 18   VAL C N   1 
ATOM   4958  C  CA  . VAL C 1 18  ? -71.399 62.023  114.255 1.00 44.43 ? 18   VAL C CA  1 
ATOM   4959  C  C   . VAL C 1 18  ? -72.294 62.459  113.092 1.00 42.32 ? 18   VAL C C   1 
ATOM   4960  O  O   . VAL C 1 18  ? -72.031 63.469  112.424 1.00 40.23 ? 18   VAL C O   1 
ATOM   4961  C  CB  . VAL C 1 18  ? -70.504 60.841  113.817 1.00 46.59 ? 18   VAL C CB  1 
ATOM   4962  C  CG1 . VAL C 1 18  ? -69.565 61.279  112.676 1.00 42.55 ? 18   VAL C CG1 1 
ATOM   4963  C  CG2 . VAL C 1 18  ? -69.720 60.326  115.031 1.00 44.07 ? 18   VAL C CG2 1 
ATOM   4964  N  N   . ASN C 1 19  ? -73.350 61.685  112.860 1.00 38.87 ? 19   ASN C N   1 
ATOM   4965  C  CA  . ASN C 1 19  ? -74.298 62.004  111.809 1.00 39.92 ? 19   ASN C CA  1 
ATOM   4966  C  C   . ASN C 1 19  ? -74.810 63.439  112.002 1.00 40.86 ? 19   ASN C C   1 
ATOM   4967  O  O   . ASN C 1 19  ? -74.933 64.220  111.053 1.00 43.91 ? 19   ASN C O   1 
ATOM   4968  C  CB  . ASN C 1 19  ? -75.479 61.043  111.865 1.00 39.13 ? 19   ASN C CB  1 
ATOM   4969  C  CG  . ASN C 1 19  ? -75.067 59.579  111.722 1.00 41.72 ? 19   ASN C CG  1 
ATOM   4970  O  OD1 . ASN C 1 19  ? -74.078 59.237  111.063 1.00 40.99 ? 19   ASN C OD1 1 
ATOM   4971  N  ND2 . ASN C 1 19  ? -75.865 58.702  112.314 1.00 42.71 ? 19   ASN C ND2 1 
ATOM   4972  N  N   . GLY C 1 20  ? -75.090 63.771  113.255 1.00 38.60 ? 20   GLY C N   1 
ATOM   4973  C  CA  . GLY C 1 20  ? -75.605 65.076  113.600 1.00 38.67 ? 20   GLY C CA  1 
ATOM   4974  C  C   . GLY C 1 20  ? -74.697 66.219  113.218 1.00 41.20 ? 20   GLY C C   1 
ATOM   4975  O  O   . GLY C 1 20  ? -75.138 67.207  112.609 1.00 48.24 ? 20   GLY C O   1 
ATOM   4976  N  N   . ILE C 1 21  ? -73.424 66.110  113.555 1.00 40.01 ? 21   ILE C N   1 
ATOM   4977  C  CA  . ILE C 1 21  ? -72.524 67.200  113.217 1.00 42.53 ? 21   ILE C CA  1 
ATOM   4978  C  C   . ILE C 1 21  ? -72.222 67.282  111.725 1.00 41.32 ? 21   ILE C C   1 
ATOM   4979  O  O   . ILE C 1 21  ? -71.899 68.369  111.214 1.00 37.96 ? 21   ILE C O   1 
ATOM   4980  C  CB  . ILE C 1 21  ? -71.188 67.136  113.991 1.00 45.32 ? 21   ILE C CB  1 
ATOM   4981  C  CG1 . ILE C 1 21  ? -70.412 65.891  113.585 1.00 44.02 ? 21   ILE C CG1 1 
ATOM   4982  C  CG2 . ILE C 1 21  ? -71.451 67.218  115.506 1.00 44.65 ? 21   ILE C CG2 1 
ATOM   4983  C  CD1 . ILE C 1 21  ? -69.149 65.730  114.359 1.00 47.59 ? 21   ILE C CD1 1 
ATOM   4984  N  N   . GLN C 1 22  ? -72.310 66.141  111.040 1.00 39.21 ? 22   GLN C N   1 
ATOM   4985  C  CA  . GLN C 1 22  ? -72.101 66.127  109.597 1.00 38.21 ? 22   GLN C CA  1 
ATOM   4986  C  C   . GLN C 1 22  ? -73.207 66.997  108.958 1.00 40.30 ? 22   GLN C C   1 
ATOM   4987  O  O   . GLN C 1 22  ? -72.941 67.847  108.086 1.00 38.43 ? 22   GLN C O   1 
ATOM   4988  C  CB  . GLN C 1 22  ? -72.201 64.710  109.020 1.00 33.70 ? 22   GLN C CB  1 
ATOM   4989  C  CG  . GLN C 1 22  ? -71.967 64.763  107.512 1.00 37.03 ? 22   GLN C CG  1 
ATOM   4990  C  CD  . GLN C 1 22  ? -71.941 63.429  106.860 1.00 36.04 ? 22   GLN C CD  1 
ATOM   4991  O  OE1 . GLN C 1 22  ? -71.669 62.409  107.497 1.00 44.46 ? 22   GLN C OE1 1 
ATOM   4992  N  NE2 . GLN C 1 22  ? -72.203 63.415  105.566 1.00 38.02 ? 22   GLN C NE2 1 
ATOM   4993  N  N   . VAL C 1 23  ? -74.445 66.763  109.409 1.00 38.68 ? 23   VAL C N   1 
ATOM   4994  C  CA  . VAL C 1 23  ? -75.594 67.501  108.927 1.00 36.90 ? 23   VAL C CA  1 
ATOM   4995  C  C   . VAL C 1 23  ? -75.453 68.959  109.329 1.00 37.35 ? 23   VAL C C   1 
ATOM   4996  O  O   . VAL C 1 23  ? -75.812 69.864  108.564 1.00 38.50 ? 23   VAL C O   1 
ATOM   4997  C  CB  . VAL C 1 23  ? -76.958 66.955  109.516 1.00 35.77 ? 23   VAL C CB  1 
ATOM   4998  C  CG1 . VAL C 1 23  ? -78.072 67.969  109.275 1.00 24.99 ? 23   VAL C CG1 1 
ATOM   4999  C  CG2 . VAL C 1 23  ? -77.336 65.621  108.883 1.00 28.53 ? 23   VAL C CG2 1 
ATOM   5000  N  N   . LEU C 1 24  ? -74.933 69.215  110.526 1.00 36.93 ? 24   LEU C N   1 
ATOM   5001  C  CA  . LEU C 1 24  ? -74.804 70.623  110.921 1.00 39.57 ? 24   LEU C CA  1 
ATOM   5002  C  C   . LEU C 1 24  ? -73.815 71.319  110.014 1.00 39.27 ? 24   LEU C C   1 
ATOM   5003  O  O   . LEU C 1 24  ? -74.028 72.455  109.643 1.00 41.52 ? 24   LEU C O   1 
ATOM   5004  C  CB  . LEU C 1 24  ? -74.322 70.774  112.359 1.00 42.94 ? 24   LEU C CB  1 
ATOM   5005  C  CG  . LEU C 1 24  ? -74.833 71.942  113.244 1.00 43.24 ? 24   LEU C CG  1 
ATOM   5006  C  CD1 . LEU C 1 24  ? -73.687 72.381  114.182 1.00 36.47 ? 24   LEU C CD1 1 
ATOM   5007  C  CD2 . LEU C 1 24  ? -75.345 73.140  112.417 1.00 41.49 ? 24   LEU C CD2 1 
ATOM   5008  N  N   . MET C 1 25  ? -72.738 70.619  109.655 1.00 40.50 ? 25   MET C N   1 
ATOM   5009  C  CA  . MET C 1 25  ? -71.695 71.161  108.791 1.00 38.65 ? 25   MET C CA  1 
ATOM   5010  C  C   . MET C 1 25  ? -72.154 71.362  107.354 1.00 40.51 ? 25   MET C C   1 
ATOM   5011  O  O   . MET C 1 25  ? -71.871 72.409  106.767 1.00 38.57 ? 25   MET C O   1 
ATOM   5012  C  CB  . MET C 1 25  ? -70.450 70.253  108.804 1.00 37.43 ? 25   MET C CB  1 
ATOM   5013  C  CG  . MET C 1 25  ? -69.296 70.708  107.887 1.00 34.50 ? 25   MET C CG  1 
ATOM   5014  S  SD  . MET C 1 25  ? -68.094 69.399  107.558 1.00 37.03 ? 25   MET C SD  1 
ATOM   5015  C  CE  . MET C 1 25  ? -68.940 68.317  106.499 1.00 35.65 ? 25   MET C CE  1 
ATOM   5016  N  N   . GLU C 1 26  ? -72.840 70.369  106.788 1.00 39.62 ? 26   GLU C N   1 
ATOM   5017  C  CA  . GLU C 1 26  ? -73.296 70.477  105.405 1.00 40.30 ? 26   GLU C CA  1 
ATOM   5018  C  C   . GLU C 1 26  ? -74.362 71.561  105.357 1.00 40.98 ? 26   GLU C C   1 
ATOM   5019  O  O   . GLU C 1 26  ? -74.477 72.311  104.395 1.00 38.59 ? 26   GLU C O   1 
ATOM   5020  C  CB  . GLU C 1 26  ? -73.896 69.154  104.915 1.00 38.65 ? 26   GLU C CB  1 
ATOM   5021  C  CG  . GLU C 1 26  ? -72.911 68.012  104.781 1.00 42.83 ? 26   GLU C CG  1 
ATOM   5022  C  CD  . GLU C 1 26  ? -73.531 66.760  104.171 1.00 47.03 ? 26   GLU C CD  1 
ATOM   5023  O  OE1 . GLU C 1 26  ? -74.707 66.814  103.721 1.00 53.48 ? 26   GLU C OE1 1 
ATOM   5024  O  OE2 . GLU C 1 26  ? -72.843 65.714  104.133 1.00 46.05 ? 26   GLU C OE2 1 
ATOM   5025  N  N   . ASN C 1 27  ? -75.134 71.662  106.424 1.00 41.67 ? 27   ASN C N   1 
ATOM   5026  C  CA  . ASN C 1 27  ? -76.193 72.646  106.450 1.00 44.21 ? 27   ASN C CA  1 
ATOM   5027  C  C   . ASN C 1 27  ? -75.693 74.077  106.463 1.00 42.77 ? 27   ASN C C   1 
ATOM   5028  O  O   . ASN C 1 27  ? -76.473 75.013  106.380 1.00 41.88 ? 27   ASN C O   1 
ATOM   5029  C  CB  . ASN C 1 27  ? -77.124 72.442  107.659 1.00 51.22 ? 27   ASN C CB  1 
ATOM   5030  C  CG  . ASN C 1 27  ? -78.466 71.800  107.272 1.00 59.31 ? 27   ASN C CG  1 
ATOM   5031  O  OD1 . ASN C 1 27  ? -79.080 72.142  106.234 1.00 65.89 ? 27   ASN C OD1 1 
ATOM   5032  N  ND2 . ASN C 1 27  ? -78.934 70.864  108.108 1.00 65.93 ? 27   ASN C ND2 1 
ATOM   5033  N  N   . SER C 1 28  ? -74.399 74.280  106.582 1.00 42.19 ? 28   SER C N   1 
ATOM   5034  C  CA  . SER C 1 28  ? -73.936 75.645  106.595 1.00 40.47 ? 28   SER C CA  1 
ATOM   5035  C  C   . SER C 1 28  ? -73.603 76.162  105.188 1.00 43.37 ? 28   SER C C   1 
ATOM   5036  O  O   . SER C 1 28  ? -73.396 77.363  105.012 1.00 43.77 ? 28   SER C O   1 
ATOM   5037  C  CB  . SER C 1 28  ? -72.737 75.778  107.538 1.00 36.96 ? 28   SER C CB  1 
ATOM   5038  O  OG  . SER C 1 28  ? -71.559 75.271  106.972 1.00 34.02 ? 28   SER C OG  1 
ATOM   5039  N  N   . VAL C 1 29  ? -73.564 75.279  104.189 1.00 43.55 ? 29   VAL C N   1 
ATOM   5040  C  CA  . VAL C 1 29  ? -73.253 75.702  102.809 1.00 48.82 ? 29   VAL C CA  1 
ATOM   5041  C  C   . VAL C 1 29  ? -74.414 76.483  102.167 1.00 50.92 ? 29   VAL C C   1 
ATOM   5042  O  O   . VAL C 1 29  ? -75.537 75.983  102.019 1.00 50.94 ? 29   VAL C O   1 
ATOM   5043  C  CB  . VAL C 1 29  ? -72.906 74.469  101.917 1.00 49.84 ? 29   VAL C CB  1 
ATOM   5044  C  CG1 . VAL C 1 29  ? -72.374 74.914  100.556 1.00 49.03 ? 29   VAL C CG1 1 
ATOM   5045  C  CG2 . VAL C 1 29  ? -71.884 73.597  102.630 1.00 48.86 ? 29   VAL C CG2 1 
ATOM   5046  N  N   . THR C 1 30  ? -74.152 77.725  101.799 1.00 54.50 ? 30   THR C N   1 
ATOM   5047  C  CA  . THR C 1 30  ? -75.202 78.553  101.191 1.00 58.16 ? 30   THR C CA  1 
ATOM   5048  C  C   . THR C 1 30  ? -74.585 79.449  100.104 1.00 62.58 ? 30   THR C C   1 
ATOM   5049  O  O   . THR C 1 30  ? -73.358 79.540  99.950  1.00 57.93 ? 30   THR C O   1 
ATOM   5050  C  CB  . THR C 1 30  ? -75.968 79.422  102.271 1.00 53.28 ? 30   THR C CB  1 
ATOM   5051  O  OG1 . THR C 1 30  ? -75.092 80.407  102.867 1.00 51.22 ? 30   THR C OG1 1 
ATOM   5052  C  CG2 . THR C 1 30  ? -76.497 78.524  103.364 1.00 47.03 ? 30   THR C CG2 1 
ATOM   5053  N  N   . SER C 1 31  ? -75.431 80.118  99.341  1.00 68.68 ? 31   SER C N   1 
ATOM   5054  C  CA  . SER C 1 31  ? -74.888 80.936  98.269  1.00 75.46 ? 31   SER C CA  1 
ATOM   5055  C  C   . SER C 1 31  ? -74.079 82.130  98.806  1.00 78.69 ? 31   SER C C   1 
ATOM   5056  O  O   . SER C 1 31  ? -73.189 82.635  98.112  1.00 79.83 ? 31   SER C O   1 
ATOM   5057  C  CB  . SER C 1 31  ? -76.011 81.387  97.308  1.00 77.38 ? 31   SER C CB  1 
ATOM   5058  O  OG  . SER C 1 31  ? -76.898 80.327  96.942  1.00 78.55 ? 31   SER C OG  1 
ATOM   5059  N  N   . SER C 1 32  ? -74.383 82.581  100.026 1.00 80.68 ? 32   SER C N   1 
ATOM   5060  C  CA  . SER C 1 32  ? -73.654 83.705  100.637 1.00 80.48 ? 32   SER C CA  1 
ATOM   5061  C  C   . SER C 1 32  ? -72.545 83.204  101.598 1.00 78.91 ? 32   SER C C   1 
ATOM   5062  O  O   . SER C 1 32  ? -71.601 83.941  101.926 1.00 78.40 ? 32   SER C O   1 
ATOM   5063  C  CB  . SER C 1 32  ? -74.630 84.620  101.392 1.00 79.55 ? 32   SER C CB  1 
ATOM   5064  O  OG  . SER C 1 32  ? -75.443 83.859  102.271 1.00 79.82 ? 32   SER C OG  1 
ATOM   5065  N  N   . ALA C 1 33  ? -72.662 81.957  102.052 1.00 73.93 ? 33   ALA C N   1 
ATOM   5066  C  CA  . ALA C 1 33  ? -71.659 81.414  102.950 1.00 71.25 ? 33   ALA C CA  1 
ATOM   5067  C  C   . ALA C 1 33  ? -70.298 81.497  102.247 1.00 70.91 ? 33   ALA C C   1 
ATOM   5068  O  O   . ALA C 1 33  ? -70.233 81.555  101.010 1.00 74.20 ? 33   ALA C O   1 
ATOM   5069  C  CB  . ALA C 1 33  ? -71.997 79.961  103.314 1.00 68.17 ? 33   ALA C CB  1 
ATOM   5070  N  N   . TYR C 1 34  ? -69.217 81.538  103.030 1.00 67.20 ? 34   TYR C N   1 
ATOM   5071  C  CA  . TYR C 1 34  ? -67.846 81.589  102.495 1.00 60.03 ? 34   TYR C CA  1 
ATOM   5072  C  C   . TYR C 1 34  ? -67.536 80.177  102.014 1.00 55.75 ? 34   TYR C C   1 
ATOM   5073  O  O   . TYR C 1 34  ? -67.614 79.242  102.799 1.00 55.65 ? 34   TYR C O   1 
ATOM   5074  C  CB  . TYR C 1 34  ? -66.892 82.004  103.619 1.00 61.48 ? 34   TYR C CB  1 
ATOM   5075  C  CG  . TYR C 1 34  ? -65.415 81.930  103.298 1.00 62.43 ? 34   TYR C CG  1 
ATOM   5076  C  CD1 . TYR C 1 34  ? -64.745 80.704  103.257 1.00 63.48 ? 34   TYR C CD1 1 
ATOM   5077  C  CD2 . TYR C 1 34  ? -64.687 83.089  103.015 1.00 61.62 ? 34   TYR C CD2 1 
ATOM   5078  C  CE1 . TYR C 1 34  ? -63.386 80.638  102.932 1.00 61.64 ? 34   TYR C CE1 1 
ATOM   5079  C  CE2 . TYR C 1 34  ? -63.333 83.035  102.689 1.00 59.91 ? 34   TYR C CE2 1 
ATOM   5080  C  CZ  . TYR C 1 34  ? -62.693 81.811  102.640 1.00 62.31 ? 34   TYR C CZ  1 
ATOM   5081  O  OH  . TYR C 1 34  ? -61.380 81.758  102.221 1.00 65.85 ? 34   TYR C OH  1 
ATOM   5082  N  N   . PRO C 1 35  ? -67.211 79.996  100.714 1.00 53.23 ? 35   PRO C N   1 
ATOM   5083  C  CA  . PRO C 1 35  ? -66.901 78.673  100.134 1.00 47.75 ? 35   PRO C CA  1 
ATOM   5084  C  C   . PRO C 1 35  ? -65.748 77.991  100.856 1.00 44.61 ? 35   PRO C C   1 
ATOM   5085  O  O   . PRO C 1 35  ? -64.583 78.311  100.639 1.00 42.69 ? 35   PRO C O   1 
ATOM   5086  C  CB  . PRO C 1 35  ? -66.573 79.001  98.679  1.00 45.68 ? 35   PRO C CB  1 
ATOM   5087  C  CG  . PRO C 1 35  ? -67.408 80.201  98.418  1.00 46.03 ? 35   PRO C CG  1 
ATOM   5088  C  CD  . PRO C 1 35  ? -67.210 81.027  99.663  1.00 51.01 ? 35   PRO C CD  1 
ATOM   5089  N  N   . ASN C 1 36  ? -66.077 77.037  101.716 1.00 41.93 ? 36   ASN C N   1 
ATOM   5090  C  CA  . ASN C 1 36  ? -65.055 76.354  102.482 1.00 40.36 ? 36   ASN C CA  1 
ATOM   5091  C  C   . ASN C 1 36  ? -64.639 75.022  101.875 1.00 40.74 ? 36   ASN C C   1 
ATOM   5092  O  O   . ASN C 1 36  ? -65.413 74.059  101.895 1.00 42.68 ? 36   ASN C O   1 
ATOM   5093  C  CB  . ASN C 1 36  ? -65.552 76.104  103.893 1.00 39.92 ? 36   ASN C CB  1 
ATOM   5094  C  CG  . ASN C 1 36  ? -64.452 75.696  104.818 1.00 39.97 ? 36   ASN C CG  1 
ATOM   5095  O  OD1 . ASN C 1 36  ? -63.435 75.149  104.381 1.00 40.06 ? 36   ASN C OD1 1 
ATOM   5096  N  ND2 . ASN C 1 36  ? -64.639 75.947  106.111 1.00 40.60 ? 36   ASN C ND2 1 
ATOM   5097  N  N   . PRO C 1 37  ? -63.406 74.940  101.337 1.00 39.28 ? 37   PRO C N   1 
ATOM   5098  C  CA  . PRO C 1 37  ? -62.917 73.685  100.732 1.00 35.87 ? 37   PRO C CA  1 
ATOM   5099  C  C   . PRO C 1 37  ? -62.752 72.540  101.737 1.00 33.59 ? 37   PRO C C   1 
ATOM   5100  O  O   . PRO C 1 37  ? -62.805 71.360  101.384 1.00 31.36 ? 37   PRO C O   1 
ATOM   5101  C  CB  . PRO C 1 37  ? -61.591 74.093  100.090 1.00 38.17 ? 37   PRO C CB  1 
ATOM   5102  C  CG  . PRO C 1 37  ? -61.157 75.286  100.914 1.00 42.16 ? 37   PRO C CG  1 
ATOM   5103  C  CD  . PRO C 1 37  ? -62.452 76.046  101.122 1.00 37.95 ? 37   PRO C CD  1 
ATOM   5104  N  N   . SER C 1 38  ? -62.576 72.883  103.001 1.00 32.72 ? 38   SER C N   1 
ATOM   5105  C  CA  . SER C 1 38  ? -62.409 71.851  103.996 1.00 33.72 ? 38   SER C CA  1 
ATOM   5106  C  C   . SER C 1 38  ? -63.721 71.145  104.244 1.00 36.19 ? 38   SER C C   1 
ATOM   5107  O  O   . SER C 1 38  ? -63.753 69.927  104.514 1.00 35.32 ? 38   SER C O   1 
ATOM   5108  C  CB  . SER C 1 38  ? -61.888 72.440  105.299 1.00 34.40 ? 38   SER C CB  1 
ATOM   5109  O  OG  . SER C 1 38  ? -60.595 72.987  105.117 1.00 35.56 ? 38   SER C OG  1 
ATOM   5110  N  N   . ILE C 1 39  ? -64.816 71.898  104.164 1.00 35.18 ? 39   ILE C N   1 
ATOM   5111  C  CA  . ILE C 1 39  ? -66.101 71.272  104.385 1.00 31.19 ? 39   ILE C CA  1 
ATOM   5112  C  C   . ILE C 1 39  ? -66.402 70.346  103.226 1.00 33.97 ? 39   ILE C C   1 
ATOM   5113  O  O   . ILE C 1 39  ? -66.912 69.246  103.442 1.00 35.81 ? 39   ILE C O   1 
ATOM   5114  C  CB  . ILE C 1 39  ? -67.206 72.287  104.510 1.00 32.38 ? 39   ILE C CB  1 
ATOM   5115  C  CG1 . ILE C 1 39  ? -67.005 73.091  105.820 1.00 32.26 ? 39   ILE C CG1 1 
ATOM   5116  C  CG2 . ILE C 1 39  ? -68.569 71.549  104.434 1.00 24.84 ? 39   ILE C CG2 1 
ATOM   5117  C  CD1 . ILE C 1 39  ? -68.042 74.167  106.086 1.00 27.65 ? 39   ILE C CD1 1 
ATOM   5118  N  N   . LEU C 1 40  ? -66.077 70.775  102.002 1.00 30.98 ? 40   LEU C N   1 
ATOM   5119  C  CA  . LEU C 1 40  ? -66.327 69.936  100.839 1.00 32.82 ? 40   LEU C CA  1 
ATOM   5120  C  C   . LEU C 1 40  ? -65.539 68.644  100.931 1.00 32.83 ? 40   LEU C C   1 
ATOM   5121  O  O   . LEU C 1 40  ? -66.076 67.590  100.607 1.00 34.90 ? 40   LEU C O   1 
ATOM   5122  C  CB  . LEU C 1 40  ? -65.983 70.655  99.522  1.00 36.79 ? 40   LEU C CB  1 
ATOM   5123  C  CG  . LEU C 1 40  ? -66.259 69.774  98.277  1.00 33.13 ? 40   LEU C CG  1 
ATOM   5124  C  CD1 . LEU C 1 40  ? -67.712 69.313  98.309  1.00 25.03 ? 40   LEU C CD1 1 
ATOM   5125  C  CD2 . LEU C 1 40  ? -65.974 70.561  96.979  1.00 29.18 ? 40   LEU C CD2 1 
ATOM   5126  N  N   . ILE C 1 41  ? -64.268 68.732  101.353 1.00 32.23 ? 41   ILE C N   1 
ATOM   5127  C  CA  . ILE C 1 41  ? -63.426 67.551  101.547 1.00 31.17 ? 41   ILE C CA  1 
ATOM   5128  C  C   . ILE C 1 41  ? -64.060 66.627  102.597 1.00 34.30 ? 41   ILE C C   1 
ATOM   5129  O  O   . ILE C 1 41  ? -64.185 65.413  102.385 1.00 40.70 ? 41   ILE C O   1 
ATOM   5130  C  CB  . ILE C 1 41  ? -61.994 67.940  102.014 1.00 30.85 ? 41   ILE C CB  1 
ATOM   5131  C  CG1 . ILE C 1 41  ? -61.282 68.686  100.877 1.00 32.59 ? 41   ILE C CG1 1 
ATOM   5132  C  CG2 . ILE C 1 41  ? -61.187 66.697  102.368 1.00 27.72 ? 41   ILE C CG2 1 
ATOM   5133  C  CD1 . ILE C 1 41  ? -59.949 69.211  101.219 1.00 26.88 ? 41   ILE C CD1 1 
ATOM   5134  N  N   . ALA C 1 42  ? -64.483 67.202  103.718 1.00 31.68 ? 42   ALA C N   1 
ATOM   5135  C  CA  . ALA C 1 42  ? -65.103 66.425  104.776 1.00 30.83 ? 42   ALA C CA  1 
ATOM   5136  C  C   . ALA C 1 42  ? -66.356 65.689  104.323 1.00 34.58 ? 42   ALA C C   1 
ATOM   5137  O  O   . ALA C 1 42  ? -66.462 64.475  104.495 1.00 33.95 ? 42   ALA C O   1 
ATOM   5138  C  CB  . ALA C 1 42  ? -65.444 67.324  105.955 1.00 30.44 ? 42   ALA C CB  1 
ATOM   5139  N  N   . MET C 1 43  ? -67.324 66.397  103.749 1.00 33.29 ? 43   MET C N   1 
ATOM   5140  C  CA  . MET C 1 43  ? -68.520 65.678  103.360 1.00 34.05 ? 43   MET C CA  1 
ATOM   5141  C  C   . MET C 1 43  ? -68.208 64.651  102.274 1.00 34.81 ? 43   MET C C   1 
ATOM   5142  O  O   . MET C 1 43  ? -68.795 63.560  102.238 1.00 30.19 ? 43   MET C O   1 
ATOM   5143  C  CB  . MET C 1 43  ? -69.657 66.634  102.949 1.00 33.91 ? 43   MET C CB  1 
ATOM   5144  C  CG  . MET C 1 43  ? -69.419 67.518  101.747 1.00 41.33 ? 43   MET C CG  1 
ATOM   5145  S  SD  . MET C 1 43  ? -70.700 68.868  101.654 1.00 45.76 ? 43   MET C SD  1 
ATOM   5146  C  CE  . MET C 1 43  ? -72.171 67.876  101.379 1.00 41.02 ? 43   MET C CE  1 
ATOM   5147  N  N   . ASN C 1 44  ? -67.252 64.960  101.407 1.00 34.54 ? 44   ASN C N   1 
ATOM   5148  C  CA  . ASN C 1 44  ? -66.930 63.985  100.394 1.00 35.49 ? 44   ASN C CA  1 
ATOM   5149  C  C   . ASN C 1 44  ? -66.239 62.737  100.997 1.00 36.01 ? 44   ASN C C   1 
ATOM   5150  O  O   . ASN C 1 44  ? -66.473 61.622  100.549 1.00 38.66 ? 44   ASN C O   1 
ATOM   5151  C  CB  . ASN C 1 44  ? -66.093 64.633  99.290  1.00 34.29 ? 44   ASN C CB  1 
ATOM   5152  C  CG  . ASN C 1 44  ? -66.954 65.402  98.305  1.00 37.88 ? 44   ASN C CG  1 
ATOM   5153  O  OD1 . ASN C 1 44  ? -68.179 65.157  98.215  1.00 35.58 ? 44   ASN C OD1 1 
ATOM   5154  N  ND2 . ASN C 1 44  ? -66.339 66.326  97.555  1.00 29.85 ? 44   ASN C ND2 1 
ATOM   5155  N  N   . LEU C 1 45  ? -65.412 62.900  102.022 1.00 33.20 ? 45   LEU C N   1 
ATOM   5156  C  CA  . LEU C 1 45  ? -64.758 61.726  102.589 1.00 34.73 ? 45   LEU C CA  1 
ATOM   5157  C  C   . LEU C 1 45  ? -65.748 60.939  103.427 1.00 34.17 ? 45   LEU C C   1 
ATOM   5158  O  O   . LEU C 1 45  ? -65.618 59.731  103.610 1.00 36.52 ? 45   LEU C O   1 
ATOM   5159  C  CB  . LEU C 1 45  ? -63.553 62.120  103.449 1.00 32.82 ? 45   LEU C CB  1 
ATOM   5160  C  CG  . LEU C 1 45  ? -62.287 62.634  102.764 1.00 29.59 ? 45   LEU C CG  1 
ATOM   5161  C  CD1 . LEU C 1 45  ? -61.291 63.108  103.796 1.00 24.90 ? 45   LEU C CD1 1 
ATOM   5162  C  CD2 . LEU C 1 45  ? -61.683 61.546  101.929 1.00 27.36 ? 45   LEU C CD2 1 
ATOM   5163  N  N   . ALA C 1 46  ? -66.758 61.622  103.925 1.00 35.41 ? 46   ALA C N   1 
ATOM   5164  C  CA  . ALA C 1 46  ? -67.755 60.950  104.746 1.00 37.58 ? 46   ALA C CA  1 
ATOM   5165  C  C   . ALA C 1 46  ? -68.882 60.337  103.942 1.00 37.61 ? 46   ALA C C   1 
ATOM   5166  O  O   . ALA C 1 46  ? -69.485 59.371  104.385 1.00 40.63 ? 46   ALA C O   1 
ATOM   5167  C  CB  . ALA C 1 46  ? -68.350 61.925  105.771 1.00 39.36 ? 46   ALA C CB  1 
ATOM   5168  N  N   . GLY C 1 47  ? -69.156 60.873  102.757 1.00 35.41 ? 47   GLY C N   1 
ATOM   5169  C  CA  . GLY C 1 47  ? -70.273 60.375  101.972 1.00 33.98 ? 47   GLY C CA  1 
ATOM   5170  C  C   . GLY C 1 47  ? -71.288 61.460  102.274 1.00 37.90 ? 47   GLY C C   1 
ATOM   5171  O  O   . GLY C 1 47  ? -71.859 61.492  103.357 1.00 35.47 ? 47   GLY C O   1 
ATOM   5172  N  N   . ALA C 1 48  ? -71.474 62.380  101.327 1.00 38.05 ? 48   ALA C N   1 
ATOM   5173  C  CA  . ALA C 1 48  ? -72.357 63.513  101.522 1.00 36.18 ? 48   ALA C CA  1 
ATOM   5174  C  C   . ALA C 1 48  ? -73.826 63.175  101.708 1.00 38.10 ? 48   ALA C C   1 
ATOM   5175  O  O   . ALA C 1 48  ? -74.341 62.258  101.066 1.00 38.79 ? 48   ALA C O   1 
ATOM   5176  C  CB  . ALA C 1 48  ? -72.204 64.459  100.366 1.00 36.89 ? 48   ALA C CB  1 
ATOM   5177  N  N   . TYR C 1 49  ? -74.502 63.919  102.586 1.00 36.52 ? 49   TYR C N   1 
ATOM   5178  C  CA  . TYR C 1 49  ? -75.932 63.705  102.801 1.00 36.60 ? 49   TYR C CA  1 
ATOM   5179  C  C   . TYR C 1 49  ? -76.720 64.590  101.874 1.00 35.27 ? 49   TYR C C   1 
ATOM   5180  O  O   . TYR C 1 49  ? -77.544 64.117  101.087 1.00 34.16 ? 49   TYR C O   1 
ATOM   5181  C  CB  . TYR C 1 49  ? -76.379 64.046  104.226 1.00 34.50 ? 49   TYR C CB  1 
ATOM   5182  C  CG  . TYR C 1 49  ? -75.929 63.074  105.271 1.00 33.18 ? 49   TYR C CG  1 
ATOM   5183  C  CD1 . TYR C 1 49  ? -75.828 61.709  104.995 1.00 36.18 ? 49   TYR C CD1 1 
ATOM   5184  C  CD2 . TYR C 1 49  ? -75.592 63.516  106.544 1.00 32.00 ? 49   TYR C CD2 1 
ATOM   5185  C  CE1 . TYR C 1 49  ? -75.394 60.807  105.976 1.00 35.50 ? 49   TYR C CE1 1 
ATOM   5186  C  CE2 . TYR C 1 49  ? -75.162 62.619  107.535 1.00 34.20 ? 49   TYR C CE2 1 
ATOM   5187  C  CZ  . TYR C 1 49  ? -75.068 61.278  107.239 1.00 33.69 ? 49   TYR C CZ  1 
ATOM   5188  O  OH  . TYR C 1 49  ? -74.666 60.415  108.222 1.00 40.13 ? 49   TYR C OH  1 
ATOM   5189  N  N   . ASN C 1 50  ? -76.465 65.887  102.001 1.00 34.36 ? 50   ASN C N   1 
ATOM   5190  C  CA  . ASN C 1 50  ? -77.151 66.890  101.202 1.00 35.79 ? 50   ASN C CA  1 
ATOM   5191  C  C   . ASN C 1 50  ? -76.507 67.113  99.826  1.00 37.68 ? 50   ASN C C   1 
ATOM   5192  O  O   . ASN C 1 50  ? -75.564 67.911  99.684  1.00 38.14 ? 50   ASN C O   1 
ATOM   5193  C  CB  . ASN C 1 50  ? -77.180 68.191  101.984 1.00 33.80 ? 50   ASN C CB  1 
ATOM   5194  C  CG  . ASN C 1 50  ? -77.846 69.315  101.225 1.00 40.50 ? 50   ASN C CG  1 
ATOM   5195  O  OD1 . ASN C 1 50  ? -78.055 70.394  101.778 1.00 46.58 ? 50   ASN C OD1 1 
ATOM   5196  N  ND2 . ASN C 1 50  ? -78.171 69.086  99.953  1.00 35.82 ? 50   ASN C ND2 1 
ATOM   5197  N  N   . LEU C 1 51  ? -77.015 66.414  98.814  1.00 35.23 ? 51   LEU C N   1 
ATOM   5198  C  CA  . LEU C 1 51  ? -76.490 66.560  97.469  1.00 34.76 ? 51   LEU C CA  1 
ATOM   5199  C  C   . LEU C 1 51  ? -76.592 67.984  96.890  1.00 34.01 ? 51   LEU C C   1 
ATOM   5200  O  O   . LEU C 1 51  ? -75.778 68.355  96.032  1.00 36.40 ? 51   LEU C O   1 
ATOM   5201  C  CB  . LEU C 1 51  ? -77.167 65.550  96.556  1.00 34.21 ? 51   LEU C CB  1 
ATOM   5202  C  CG  . LEU C 1 51  ? -76.962 64.134  97.107  1.00 40.11 ? 51   LEU C CG  1 
ATOM   5203  C  CD1 . LEU C 1 51  ? -77.691 63.161  96.219  1.00 36.41 ? 51   LEU C CD1 1 
ATOM   5204  C  CD2 . LEU C 1 51  ? -75.459 63.780  97.183  1.00 37.65 ? 51   LEU C CD2 1 
ATOM   5205  N  N   . LYS C 1 52  ? -77.469 68.753  97.352  1.00 36.79 ? 52   LYS C N   1 
ATOM   5206  C  CA  . LYS C 1 52  ? -77.516 70.102  96.885  1.00 37.78 ? 52   LYS C CA  1 
ATOM   5207  C  C   . LYS C 1 52  ? -76.432 70.912  97.440  1.00 36.13 ? 52   LYS C C   1 
ATOM   5208  O  O   . LYS C 1 52  ? -75.831 71.744  96.699  1.00 36.66 ? 52   LYS C O   1 
ATOM   5209  C  CB  . LYS C 1 52  ? -78.563 70.846  97.471  1.00 43.78 ? 52   LYS C CB  1 
ATOM   5210  C  CG  . LYS C 1 52  ? -79.367 71.150  96.512  1.00 49.45 ? 52   LYS C CG  1 
ATOM   5211  C  CD  . LYS C 1 52  ? -80.395 70.580  97.080  1.00 59.43 ? 52   LYS C CD  1 
ATOM   5212  C  CE  . LYS C 1 52  ? -81.449 70.604  95.958  1.00 64.21 ? 52   LYS C CE  1 
ATOM   5213  N  NZ  . LYS C 1 52  ? -82.359 70.396  97.084  1.00 69.92 ? 52   LYS C NZ  1 
ATOM   5214  N  N   . ALA C 1 53  ? -76.279 70.844  98.702  1.00 26.96 ? 53   ALA C N   1 
ATOM   5215  C  CA  . ALA C 1 53  ? -75.181 71.598  99.282  1.00 29.91 ? 53   ALA C CA  1 
ATOM   5216  C  C   . ALA C 1 53  ? -73.869 71.092  98.638  1.00 31.19 ? 53   ALA C C   1 
ATOM   5217  O  O   . ALA C 1 53  ? -72.983 71.879  98.297  1.00 33.59 ? 53   ALA C O   1 
ATOM   5218  C  CB  . ALA C 1 53  ? -75.151 71.425  100.789 1.00 28.81 ? 53   ALA C CB  1 
ATOM   5219  N  N   . GLN C 1 54  ? -73.757 69.784  98.431  1.00 29.61 ? 54   GLN C N   1 
ATOM   5220  C  CA  . GLN C 1 54  ? -72.554 69.249  97.816  1.00 33.51 ? 54   GLN C CA  1 
ATOM   5221  C  C   . GLN C 1 54  ? -72.275 69.871  96.437  1.00 35.86 ? 54   GLN C C   1 
ATOM   5222  O  O   . GLN C 1 54  ? -71.142 70.236  96.115  1.00 37.29 ? 54   GLN C O   1 
ATOM   5223  C  CB  . GLN C 1 54  ? -72.663 67.739  97.664  1.00 31.81 ? 54   GLN C CB  1 
ATOM   5224  C  CG  . GLN C 1 54  ? -71.431 67.141  97.030  1.00 30.50 ? 54   GLN C CG  1 
ATOM   5225  C  CD  . GLN C 1 54  ? -71.624 65.679  96.742  1.00 33.55 ? 54   GLN C CD  1 
ATOM   5226  O  OE1 . GLN C 1 54  ? -70.763 64.857  97.046  1.00 36.85 ? 54   GLN C OE1 1 
ATOM   5227  N  NE2 . GLN C 1 54  ? -72.755 65.342  96.144  1.00 31.99 ? 54   GLN C NE2 1 
ATOM   5228  N  N   . LYS C 1 55  ? -73.315 69.984  95.625  1.00 34.91 ? 55   LYS C N   1 
ATOM   5229  C  CA  . LYS C 1 55  ? -73.174 70.537  94.301  1.00 37.63 ? 55   LYS C CA  1 
ATOM   5230  C  C   . LYS C 1 55  ? -72.887 72.041  94.341  1.00 36.94 ? 55   LYS C C   1 
ATOM   5231  O  O   . LYS C 1 55  ? -72.043 72.562  93.605  1.00 34.77 ? 55   LYS C O   1 
ATOM   5232  C  CB  . LYS C 1 55  ? -74.452 70.253  93.528  1.00 42.80 ? 55   LYS C CB  1 
ATOM   5233  C  CG  . LYS C 1 55  ? -74.451 70.726  92.092  1.00 48.06 ? 55   LYS C CG  1 
ATOM   5234  C  CD  . LYS C 1 55  ? -75.779 70.327  91.467  1.00 54.24 ? 55   LYS C CD  1 
ATOM   5235  C  CE  . LYS C 1 55  ? -76.044 70.982  90.116  1.00 56.09 ? 55   LYS C CE  1 
ATOM   5236  N  NZ  . LYS C 1 55  ? -77.441 70.646  89.694  1.00 54.09 ? 55   LYS C NZ  1 
ATOM   5237  N  N   . LEU C 1 56  ? -73.581 72.747  95.218  1.00 37.30 ? 56   LEU C N   1 
ATOM   5238  C  CA  . LEU C 1 56  ? -73.380 74.181  95.295  1.00 34.84 ? 56   LEU C CA  1 
ATOM   5239  C  C   . LEU C 1 56  ? -71.938 74.514  95.635  1.00 34.49 ? 56   LEU C C   1 
ATOM   5240  O  O   . LEU C 1 56  ? -71.299 75.317  94.942  1.00 35.03 ? 56   LEU C O   1 
ATOM   5241  C  CB  . LEU C 1 56  ? -74.335 74.775  96.320  1.00 36.32 ? 56   LEU C CB  1 
ATOM   5242  C  CG  . LEU C 1 56  ? -74.061 76.216  96.717  1.00 36.99 ? 56   LEU C CG  1 
ATOM   5243  C  CD1 . LEU C 1 56  ? -74.137 77.101  95.489  1.00 41.52 ? 56   LEU C CD1 1 
ATOM   5244  C  CD2 . LEU C 1 56  ? -75.066 76.649  97.755  1.00 37.06 ? 56   LEU C CD2 1 
ATOM   5245  N  N   . LEU C 1 57  ? -71.415 73.871  96.678  1.00 33.61 ? 57   LEU C N   1 
ATOM   5246  C  CA  . LEU C 1 57  ? -70.042 74.109  97.121  1.00 33.60 ? 57   LEU C CA  1 
ATOM   5247  C  C   . LEU C 1 57  ? -69.043 73.782  96.027  1.00 35.97 ? 57   LEU C C   1 
ATOM   5248  O  O   . LEU C 1 57  ? -68.106 74.553  95.752  1.00 38.06 ? 57   LEU C O   1 
ATOM   5249  C  CB  . LEU C 1 57  ? -69.742 73.285  98.375  1.00 32.25 ? 57   LEU C CB  1 
ATOM   5250  C  CG  . LEU C 1 57  ? -68.440 73.562  99.144  1.00 33.64 ? 57   LEU C CG  1 
ATOM   5251  C  CD1 . LEU C 1 57  ? -68.126 75.072  99.233  1.00 28.03 ? 57   LEU C CD1 1 
ATOM   5252  C  CD2 . LEU C 1 57  ? -68.565 72.961  100.547 1.00 29.65 ? 57   LEU C CD2 1 
ATOM   5253  N  N   . THR C 1 58  ? -69.268 72.648  95.377  1.00 35.94 ? 58   THR C N   1 
ATOM   5254  C  CA  . THR C 1 58  ? -68.399 72.236  94.303  1.00 34.30 ? 58   THR C CA  1 
ATOM   5255  C  C   . THR C 1 58  ? -68.356 73.301  93.222  1.00 34.64 ? 58   THR C C   1 
ATOM   5256  O  O   . THR C 1 58  ? -67.277 73.613  92.707  1.00 31.62 ? 58   THR C O   1 
ATOM   5257  C  CB  . THR C 1 58  ? -68.852 70.890  93.709  1.00 35.52 ? 58   THR C CB  1 
ATOM   5258  O  OG1 . THR C 1 58  ? -68.681 69.860  94.696  1.00 39.08 ? 58   THR C OG1 1 
ATOM   5259  C  CG2 . THR C 1 58  ? -68.007 70.524  92.498  1.00 33.48 ? 58   THR C CG2 1 
ATOM   5260  N  N   . TYR C 1 59  ? -69.510 73.872  92.870  1.00 35.21 ? 59   TYR C N   1 
ATOM   5261  C  CA  . TYR C 1 59  ? -69.511 74.906  91.833  1.00 37.73 ? 59   TYR C CA  1 
ATOM   5262  C  C   . TYR C 1 59  ? -68.820 76.199  92.318  1.00 38.99 ? 59   TYR C C   1 
ATOM   5263  O  O   . TYR C 1 59  ? -68.081 76.864  91.565  1.00 36.70 ? 59   TYR C O   1 
ATOM   5264  C  CB  . TYR C 1 59  ? -70.940 75.199  91.351  1.00 37.71 ? 59   TYR C CB  1 
ATOM   5265  C  CG  . TYR C 1 59  ? -71.507 74.110  90.461  1.00 45.03 ? 59   TYR C CG  1 
ATOM   5266  C  CD1 . TYR C 1 59  ? -70.670 73.253  89.747  1.00 50.18 ? 59   TYR C CD1 1 
ATOM   5267  C  CD2 . TYR C 1 59  ? -72.869 73.970  90.278  1.00 48.39 ? 59   TYR C CD2 1 
ATOM   5268  C  CE1 . TYR C 1 59  ? -71.177 72.295  88.874  1.00 48.77 ? 59   TYR C CE1 1 
ATOM   5269  C  CE2 . TYR C 1 59  ? -73.389 73.008  89.398  1.00 53.68 ? 59   TYR C CE2 1 
ATOM   5270  C  CZ  . TYR C 1 59  ? -72.531 72.184  88.700  1.00 52.52 ? 59   TYR C CZ  1 
ATOM   5271  O  OH  . TYR C 1 59  ? -73.035 71.284  87.788  1.00 54.91 ? 59   TYR C OH  1 
ATOM   5272  N  N   . GLN C 1 60  ? -69.025 76.545  93.582  1.00 37.23 ? 60   GLN C N   1 
ATOM   5273  C  CA  . GLN C 1 60  ? -68.385 77.746  94.088  1.00 40.54 ? 60   GLN C CA  1 
ATOM   5274  C  C   . GLN C 1 60  ? -66.867 77.621  94.016  1.00 40.65 ? 60   GLN C C   1 
ATOM   5275  O  O   . GLN C 1 60  ? -66.172 78.591  93.679  1.00 42.20 ? 60   GLN C O   1 
ATOM   5276  C  CB  . GLN C 1 60  ? -68.848 78.034  95.518  1.00 41.43 ? 60   GLN C CB  1 
ATOM   5277  C  CG  . GLN C 1 60  ? -70.354 78.166  95.612  1.00 41.15 ? 60   GLN C CG  1 
ATOM   5278  C  CD  . GLN C 1 60  ? -70.806 78.338  97.014  1.00 39.89 ? 60   GLN C CD  1 
ATOM   5279  O  OE1 . GLN C 1 60  ? -70.407 77.576  97.889  1.00 42.62 ? 60   GLN C OE1 1 
ATOM   5280  N  NE2 . GLN C 1 60  ? -71.650 79.335  97.252  1.00 41.35 ? 60   GLN C NE2 1 
ATOM   5281  N  N   . LEU C 1 61  ? -66.340 76.438  94.325  1.00 39.07 ? 61   LEU C N   1 
ATOM   5282  C  CA  . LEU C 1 61  ? -64.889 76.264  94.257  1.00 37.37 ? 61   LEU C CA  1 
ATOM   5283  C  C   . LEU C 1 61  ? -64.374 76.159  92.826  1.00 36.21 ? 61   LEU C C   1 
ATOM   5284  O  O   . LEU C 1 61  ? -63.305 76.678  92.506  1.00 35.86 ? 61   LEU C O   1 
ATOM   5285  C  CB  . LEU C 1 61  ? -64.462 75.036  95.056  1.00 34.67 ? 61   LEU C CB  1 
ATOM   5286  C  CG  . LEU C 1 61  ? -64.907 75.161  96.505  1.00 35.75 ? 61   LEU C CG  1 
ATOM   5287  C  CD1 . LEU C 1 61  ? -64.687 73.847  97.207  1.00 36.37 ? 61   LEU C CD1 1 
ATOM   5288  C  CD2 . LEU C 1 61  ? -64.171 76.291  97.186  1.00 29.40 ? 61   LEU C CD2 1 
ATOM   5289  N  N   . MET C 1 62  ? -65.122 75.496  91.952  1.00 36.78 ? 62   MET C N   1 
ATOM   5290  C  CA  . MET C 1 62  ? -64.664 75.370  90.572  1.00 37.01 ? 62   MET C CA  1 
ATOM   5291  C  C   . MET C 1 62  ? -64.521 76.763  89.993  1.00 38.88 ? 62   MET C C   1 
ATOM   5292  O  O   . MET C 1 62  ? -63.699 76.994  89.122  1.00 38.90 ? 62   MET C O   1 
ATOM   5293  C  CB  . MET C 1 62  ? -65.655 74.597  89.712  1.00 34.54 ? 62   MET C CB  1 
ATOM   5294  C  CG  . MET C 1 62  ? -65.778 73.109  90.001  1.00 33.83 ? 62   MET C CG  1 
ATOM   5295  S  SD  . MET C 1 62  ? -67.298 72.453  89.229  1.00 37.44 ? 62   MET C SD  1 
ATOM   5296  C  CE  . MET C 1 62  ? -66.992 72.985  87.580  1.00 24.29 ? 62   MET C CE  1 
ATOM   5297  N  N   . SER C 1 63  ? -65.318 77.697  90.491  1.00 40.67 ? 63   SER C N   1 
ATOM   5298  C  CA  . SER C 1 63  ? -65.263 79.043  89.960  1.00 43.97 ? 63   SER C CA  1 
ATOM   5299  C  C   . SER C 1 63  ? -64.473 80.028  90.814  1.00 46.06 ? 63   SER C C   1 
ATOM   5300  O  O   . SER C 1 63  ? -64.482 81.237  90.552  1.00 42.54 ? 63   SER C O   1 
ATOM   5301  C  CB  . SER C 1 63  ? -66.678 79.572  89.724  1.00 44.71 ? 63   SER C CB  1 
ATOM   5302  O  OG  . SER C 1 63  ? -67.255 80.003  90.937  1.00 45.89 ? 63   SER C OG  1 
ATOM   5303  N  N   . SER C 1 64  ? -63.776 79.531  91.830  1.00 48.79 ? 64   SER C N   1 
ATOM   5304  C  CA  . SER C 1 64  ? -62.982 80.438  92.640  1.00 49.63 ? 64   SER C CA  1 
ATOM   5305  C  C   . SER C 1 64  ? -61.870 80.957  91.742  1.00 51.02 ? 64   SER C C   1 
ATOM   5306  O  O   . SER C 1 64  ? -61.395 80.261  90.840  1.00 50.75 ? 64   SER C O   1 
ATOM   5307  C  CB  . SER C 1 64  ? -62.400 79.729  93.860  1.00 49.37 ? 64   SER C CB  1 
ATOM   5308  O  OG  . SER C 1 64  ? -61.606 78.634  93.479  1.00 49.81 ? 64   SER C OG  1 
ATOM   5309  N  N   . ASP C 1 65  ? -61.473 82.198  91.971  1.00 54.10 ? 65   ASP C N   1 
ATOM   5310  C  CA  . ASP C 1 65  ? -60.421 82.811  91.173  1.00 57.47 ? 65   ASP C CA  1 
ATOM   5311  C  C   . ASP C 1 65  ? -59.030 82.407  91.708  1.00 56.19 ? 65   ASP C C   1 
ATOM   5312  O  O   . ASP C 1 65  ? -58.719 82.619  92.879  1.00 53.99 ? 65   ASP C O   1 
ATOM   5313  C  CB  . ASP C 1 65  ? -60.597 84.344  91.205  1.00 61.09 ? 65   ASP C CB  1 
ATOM   5314  C  CG  . ASP C 1 65  ? -59.569 85.087  90.348  1.00 62.63 ? 65   ASP C CG  1 
ATOM   5315  O  OD1 . ASP C 1 65  ? -58.362 84.754  90.382  1.00 61.97 ? 65   ASP C OD1 1 
ATOM   5316  O  OD2 . ASP C 1 65  ? -59.979 86.031  89.648  1.00 66.96 ? 65   ASP C OD2 1 
ATOM   5317  N  N   . ASN C 1 66  ? -58.197 81.842  90.842  1.00 55.35 ? 66   ASN C N   1 
ATOM   5318  C  CA  . ASN C 1 66  ? -56.857 81.433  91.240  1.00 58.17 ? 66   ASN C CA  1 
ATOM   5319  C  C   . ASN C 1 66  ? -56.015 82.554  91.871  1.00 60.40 ? 66   ASN C C   1 
ATOM   5320  O  O   . ASN C 1 66  ? -55.133 82.276  92.685  1.00 60.97 ? 66   ASN C O   1 
ATOM   5321  C  CB  . ASN C 1 66  ? -56.096 80.849  90.046  1.00 58.35 ? 66   ASN C CB  1 
ATOM   5322  C  CG  . ASN C 1 66  ? -56.898 79.790  89.292  1.00 58.82 ? 66   ASN C CG  1 
ATOM   5323  O  OD1 . ASN C 1 66  ? -57.624 78.996  89.883  1.00 61.20 ? 66   ASN C OD1 1 
ATOM   5324  N  ND2 . ASN C 1 66  ? -56.753 79.774  87.980  1.00 59.51 ? 66   ASN C ND2 1 
ATOM   5325  N  N   . ASN C 1 67  ? -56.262 83.810  91.503  1.00 60.93 ? 67   ASN C N   1 
ATOM   5326  C  CA  . ASN C 1 67  ? -55.495 84.911  92.089  1.00 60.84 ? 67   ASN C CA  1 
ATOM   5327  C  C   . ASN C 1 67  ? -55.990 85.349  93.472  1.00 60.78 ? 67   ASN C C   1 
ATOM   5328  O  O   . ASN C 1 67  ? -55.375 86.204  94.120  1.00 60.70 ? 67   ASN C O   1 
ATOM   5329  C  CB  . ASN C 1 67  ? -55.480 86.111  91.147  1.00 61.32 ? 67   ASN C CB  1 
ATOM   5330  C  CG  . ASN C 1 67  ? -54.572 85.901  89.976  1.00 64.38 ? 67   ASN C CG  1 
ATOM   5331  O  OD1 . ASN C 1 67  ? -54.906 86.264  88.847  1.00 67.97 ? 67   ASN C OD1 1 
ATOM   5332  N  ND2 . ASN C 1 67  ? -53.404 85.318  90.227  1.00 63.32 ? 67   ASN C ND2 1 
ATOM   5333  N  N   . ASP C 1 68  ? -57.094 84.766  93.926  1.00 59.85 ? 68   ASP C N   1 
ATOM   5334  C  CA  . ASP C 1 68  ? -57.645 85.102  95.243  1.00 58.67 ? 68   ASP C CA  1 
ATOM   5335  C  C   . ASP C 1 68  ? -57.211 84.094  96.284  1.00 53.94 ? 68   ASP C C   1 
ATOM   5336  O  O   . ASP C 1 68  ? -57.431 84.277  97.473  1.00 54.63 ? 68   ASP C O   1 
ATOM   5337  C  CB  . ASP C 1 68  ? -59.177 85.100  95.205  1.00 61.34 ? 68   ASP C CB  1 
ATOM   5338  C  CG  . ASP C 1 68  ? -59.747 86.364  94.627  1.00 64.41 ? 68   ASP C CG  1 
ATOM   5339  O  OD1 . ASP C 1 68  ? -58.973 87.326  94.433  1.00 66.57 ? 68   ASP C OD1 1 
ATOM   5340  O  OD2 . ASP C 1 68  ? -60.973 86.397  94.380  1.00 66.47 ? 68   ASP C OD2 1 
ATOM   5341  N  N   . LEU C 1 69  ? -56.596 83.021  95.825  1.00 52.02 ? 69   LEU C N   1 
ATOM   5342  C  CA  . LEU C 1 69  ? -56.205 81.954  96.718  1.00 49.30 ? 69   LEU C CA  1 
ATOM   5343  C  C   . LEU C 1 69  ? -54.764 81.971  97.156  1.00 49.41 ? 69   LEU C C   1 
ATOM   5344  O  O   . LEU C 1 69  ? -53.874 82.282  96.368  1.00 53.17 ? 69   LEU C O   1 
ATOM   5345  C  CB  . LEU C 1 69  ? -56.514 80.622  96.042  1.00 46.56 ? 69   LEU C CB  1 
ATOM   5346  C  CG  . LEU C 1 69  ? -57.991 80.483  95.656  1.00 46.26 ? 69   LEU C CG  1 
ATOM   5347  C  CD1 . LEU C 1 69  ? -58.160 79.218  94.830  1.00 40.32 ? 69   LEU C CD1 1 
ATOM   5348  C  CD2 . LEU C 1 69  ? -58.875 80.463  96.923  1.00 42.69 ? 69   LEU C CD2 1 
ATOM   5349  N  N   . THR C 1 70  ? -54.538 81.646  98.423  1.00 46.85 ? 70   THR C N   1 
ATOM   5350  C  CA  . THR C 1 70  ? -53.182 81.545  98.941  1.00 43.76 ? 70   THR C CA  1 
ATOM   5351  C  C   . THR C 1 70  ? -52.704 80.116  98.676  1.00 45.17 ? 70   THR C C   1 
ATOM   5352  O  O   . THR C 1 70  ? -53.499 79.218  98.335  1.00 44.48 ? 70   THR C O   1 
ATOM   5353  C  CB  . THR C 1 70  ? -53.114 81.734  100.442 1.00 42.84 ? 70   THR C CB  1 
ATOM   5354  O  OG1 . THR C 1 70  ? -53.864 80.689  101.070 1.00 42.11 ? 70   THR C OG1 1 
ATOM   5355  C  CG2 . THR C 1 70  ? -53.664 83.092  100.855 1.00 39.22 ? 70   THR C CG2 1 
ATOM   5356  N  N   . ILE C 1 71  ? -51.405 79.910  98.859  1.00 43.71 ? 71   ILE C N   1 
ATOM   5357  C  CA  . ILE C 1 71  ? -50.783 78.607  98.659  1.00 40.52 ? 71   ILE C CA  1 
ATOM   5358  C  C   . ILE C 1 71  ? -51.602 77.501  99.301  1.00 37.92 ? 71   ILE C C   1 
ATOM   5359  O  O   . ILE C 1 71  ? -51.847 76.472  98.693  1.00 37.16 ? 71   ILE C O   1 
ATOM   5360  C  CB  . ILE C 1 71  ? -49.338 78.635  99.233  1.00 45.88 ? 71   ILE C CB  1 
ATOM   5361  C  CG1 . ILE C 1 71  ? -48.392 79.237  98.195  1.00 47.93 ? 71   ILE C CG1 1 
ATOM   5362  C  CG2 . ILE C 1 71  ? -48.878 77.253  99.640  1.00 47.93 ? 71   ILE C CG2 1 
ATOM   5363  C  CD1 . ILE C 1 71  ? -46.975 79.306  98.677  1.00 56.02 ? 71   ILE C CD1 1 
ATOM   5364  N  N   . GLY C 1 72  ? -52.030 77.728  100.534 1.00 37.82 ? 72   GLY C N   1 
ATOM   5365  C  CA  . GLY C 1 72  ? -52.822 76.743  101.245 1.00 38.43 ? 72   GLY C CA  1 
ATOM   5366  C  C   . GLY C 1 72  ? -54.252 76.649  100.743 1.00 38.72 ? 72   GLY C C   1 
ATOM   5367  O  O   . GLY C 1 72  ? -54.819 75.555  100.731 1.00 40.38 ? 72   GLY C O   1 
ATOM   5368  N  N   . HIS C 1 73  ? -54.852 77.783  100.378 1.00 40.57 ? 73   HIS C N   1 
ATOM   5369  C  CA  . HIS C 1 73  ? -56.211 77.789  99.829  1.00 43.25 ? 73   HIS C CA  1 
ATOM   5370  C  C   . HIS C 1 73  ? -56.140 76.841  98.635  1.00 41.92 ? 73   HIS C C   1 
ATOM   5371  O  O   . HIS C 1 73  ? -56.884 75.869  98.518  1.00 40.58 ? 73   HIS C O   1 
ATOM   5372  C  CB  . HIS C 1 73  ? -56.563 79.144  99.240  1.00 44.96 ? 73   HIS C CB  1 
ATOM   5373  C  CG  . HIS C 1 73  ? -56.886 80.197  100.241 1.00 49.05 ? 73   HIS C CG  1 
ATOM   5374  N  ND1 . HIS C 1 73  ? -56.794 81.542  99.942  1.00 53.12 ? 73   HIS C ND1 1 
ATOM   5375  C  CD2 . HIS C 1 73  ? -57.440 80.123  101.470 1.00 51.51 ? 73   HIS C CD2 1 
ATOM   5376  C  CE1 . HIS C 1 73  ? -57.288 82.249  100.941 1.00 54.18 ? 73   HIS C CE1 1 
ATOM   5377  N  NE2 . HIS C 1 73  ? -57.690 81.414  101.881 1.00 51.91 ? 73   HIS C NE2 1 
ATOM   5378  N  N   . LEU C 1 74  ? -55.206 77.168  97.754  1.00 39.87 ? 74   LEU C N   1 
ATOM   5379  C  CA  . LEU C 1 74  ? -54.983 76.435  96.534  1.00 42.76 ? 74   LEU C CA  1 
ATOM   5380  C  C   . LEU C 1 74  ? -54.951 74.935  96.800  1.00 43.33 ? 74   LEU C C   1 
ATOM   5381  O  O   . LEU C 1 74  ? -55.749 74.169  96.250  1.00 44.05 ? 74   LEU C O   1 
ATOM   5382  C  CB  . LEU C 1 74  ? -53.682 76.935  95.891  1.00 43.71 ? 74   LEU C CB  1 
ATOM   5383  C  CG  . LEU C 1 74  ? -53.671 77.359  94.408  1.00 45.50 ? 74   LEU C CG  1 
ATOM   5384  C  CD1 . LEU C 1 74  ? -55.056 77.764  93.944  1.00 46.58 ? 74   LEU C CD1 1 
ATOM   5385  C  CD2 . LEU C 1 74  ? -52.674 78.509  94.218  1.00 43.93 ? 74   LEU C CD2 1 
ATOM   5386  N  N   . GLY C 1 75  ? -54.038 74.514  97.659  1.00 42.25 ? 75   GLY C N   1 
ATOM   5387  C  CA  . GLY C 1 75  ? -53.949 73.102  97.962  1.00 40.91 ? 75   GLY C CA  1 
ATOM   5388  C  C   . GLY C 1 75  ? -55.285 72.538  98.405  1.00 40.55 ? 75   GLY C C   1 
ATOM   5389  O  O   . GLY C 1 75  ? -55.717 71.499  97.908  1.00 39.94 ? 75   GLY C O   1 
ATOM   5390  N  N   . LEU C 1 76  ? -55.941 73.223  99.338  1.00 39.88 ? 76   LEU C N   1 
ATOM   5391  C  CA  . LEU C 1 76  ? -57.220 72.770  99.853  1.00 40.28 ? 76   LEU C CA  1 
ATOM   5392  C  C   . LEU C 1 76  ? -58.235 72.657  98.722  1.00 39.45 ? 76   LEU C C   1 
ATOM   5393  O  O   . LEU C 1 76  ? -58.929 71.650  98.595  1.00 37.63 ? 76   LEU C O   1 
ATOM   5394  C  CB  . LEU C 1 76  ? -57.708 73.734  100.946 1.00 43.01 ? 76   LEU C CB  1 
ATOM   5395  C  CG  . LEU C 1 76  ? -57.788 73.305  102.440 1.00 43.64 ? 76   LEU C CG  1 
ATOM   5396  C  CD1 . LEU C 1 76  ? -57.051 72.048  102.737 1.00 36.98 ? 76   LEU C CD1 1 
ATOM   5397  C  CD2 . LEU C 1 76  ? -57.247 74.425  103.287 1.00 43.87 ? 76   LEU C CD2 1 
ATOM   5398  N  N   . THR C 1 77  ? -58.275 73.672  97.869  1.00 38.71 ? 77   THR C N   1 
ATOM   5399  C  CA  . THR C 1 77  ? -59.211 73.696  96.755  1.00 37.42 ? 77   THR C CA  1 
ATOM   5400  C  C   . THR C 1 77  ? -59.009 72.592  95.723  1.00 35.07 ? 77   THR C C   1 
ATOM   5401  O  O   . THR C 1 77  ? -59.968 72.086  95.142  1.00 35.28 ? 77   THR C O   1 
ATOM   5402  C  CB  . THR C 1 77  ? -59.164 75.057  96.078  1.00 36.12 ? 77   THR C CB  1 
ATOM   5403  O  OG1 . THR C 1 77  ? -59.448 76.061  97.067  1.00 42.38 ? 77   THR C OG1 1 
ATOM   5404  C  CG2 . THR C 1 77  ? -60.212 75.145  94.963  1.00 33.93 ? 77   THR C CG2 1 
ATOM   5405  N  N   . ILE C 1 78  ? -57.754 72.247  95.485  1.00 33.72 ? 78   ILE C N   1 
ATOM   5406  C  CA  . ILE C 1 78  ? -57.398 71.188  94.556  1.00 33.26 ? 78   ILE C CA  1 
ATOM   5407  C  C   . ILE C 1 78  ? -57.906 69.866  95.128  1.00 36.87 ? 78   ILE C C   1 
ATOM   5408  O  O   . ILE C 1 78  ? -58.517 69.053  94.410  1.00 39.85 ? 78   ILE C O   1 
ATOM   5409  C  CB  . ILE C 1 78  ? -55.843 71.152  94.340  1.00 35.30 ? 78   ILE C CB  1 
ATOM   5410  C  CG1 . ILE C 1 78  ? -55.443 72.363  93.491  1.00 28.65 ? 78   ILE C CG1 1 
ATOM   5411  C  CG2 . ILE C 1 78  ? -55.376 69.822  93.667  1.00 22.86 ? 78   ILE C CG2 1 
ATOM   5412  C  CD1 . ILE C 1 78  ? -53.975 72.513  93.349  1.00 39.52 ? 78   ILE C CD1 1 
ATOM   5413  N  N   . MET C 1 79  ? -57.686 69.652  96.424  1.00 36.74 ? 79   MET C N   1 
ATOM   5414  C  CA  . MET C 1 79  ? -58.176 68.424  97.030  1.00 34.35 ? 79   MET C CA  1 
ATOM   5415  C  C   . MET C 1 79  ? -59.707 68.387  97.070  1.00 32.40 ? 79   MET C C   1 
ATOM   5416  O  O   . MET C 1 79  ? -60.301 67.329  96.879  1.00 34.85 ? 79   MET C O   1 
ATOM   5417  C  CB  . MET C 1 79  ? -57.594 68.245  98.432  1.00 31.95 ? 79   MET C CB  1 
ATOM   5418  C  CG  . MET C 1 79  ? -56.123 67.892  98.426  1.00 31.95 ? 79   MET C CG  1 
ATOM   5419  S  SD  . MET C 1 79  ? -55.457 67.484  100.071 1.00 41.76 ? 79   MET C SD  1 
ATOM   5420  C  CE  . MET C 1 79  ? -55.427 69.146  100.845 1.00 27.13 ? 79   MET C CE  1 
ATOM   5421  N  N   . ALA C 1 80  ? -60.357 69.526  97.304  1.00 31.53 ? 80   ALA C N   1 
ATOM   5422  C  CA  . ALA C 1 80  ? -61.820 69.517  97.376  1.00 30.35 ? 80   ALA C CA  1 
ATOM   5423  C  C   . ALA C 1 80  ? -62.356 69.138  96.021  1.00 30.74 ? 80   ALA C C   1 
ATOM   5424  O  O   . ALA C 1 80  ? -63.223 68.265  95.922  1.00 35.66 ? 80   ALA C O   1 
ATOM   5425  C  CB  . ALA C 1 80  ? -62.381 70.872  97.814  1.00 23.73 ? 80   ALA C CB  1 
ATOM   5426  N  N   . LEU C 1 81  ? -61.819 69.760  94.973  1.00 29.81 ? 81   LEU C N   1 
ATOM   5427  C  CA  . LEU C 1 81  ? -62.261 69.470  93.618  1.00 32.06 ? 81   LEU C CA  1 
ATOM   5428  C  C   . LEU C 1 81  ? -62.063 67.993  93.267  1.00 33.47 ? 81   LEU C C   1 
ATOM   5429  O  O   . LEU C 1 81  ? -62.964 67.313  92.762  1.00 32.33 ? 81   LEU C O   1 
ATOM   5430  C  CB  . LEU C 1 81  ? -61.542 70.377  92.630  1.00 32.12 ? 81   LEU C CB  1 
ATOM   5431  C  CG  . LEU C 1 81  ? -62.050 71.820  92.730  1.00 34.44 ? 81   LEU C CG  1 
ATOM   5432  C  CD1 . LEU C 1 81  ? -61.480 72.646  91.619  1.00 34.62 ? 81   LEU C CD1 1 
ATOM   5433  C  CD2 . LEU C 1 81  ? -63.580 71.836  92.641  1.00 33.54 ? 81   LEU C CD2 1 
ATOM   5434  N  N   . THR C 1 82  ? -60.885 67.493  93.559  1.00 34.05 ? 82   THR C N   1 
ATOM   5435  C  CA  . THR C 1 82  ? -60.599 66.094  93.318  1.00 33.94 ? 82   THR C CA  1 
ATOM   5436  C  C   . THR C 1 82  ? -61.574 65.183  94.064  1.00 35.42 ? 82   THR C C   1 
ATOM   5437  O  O   . THR C 1 82  ? -62.016 64.185  93.490  1.00 37.65 ? 82   THR C O   1 
ATOM   5438  C  CB  . THR C 1 82  ? -59.156 65.766  93.752  1.00 35.70 ? 82   THR C CB  1 
ATOM   5439  O  OG1 . THR C 1 82  ? -58.237 66.523  92.937  1.00 37.64 ? 82   THR C OG1 1 
ATOM   5440  C  CG2 . THR C 1 82  ? -58.876 64.274  93.631  1.00 29.56 ? 82   THR C CG2 1 
ATOM   5441  N  N   . SER C 1 83  ? -61.928 65.506  95.318  1.00 33.55 ? 83   SER C N   1 
ATOM   5442  C  CA  . SER C 1 83  ? -62.882 64.649  96.087  1.00 34.61 ? 83   SER C CA  1 
ATOM   5443  C  C   . SER C 1 83  ? -64.295 64.686  95.487  1.00 33.72 ? 83   SER C C   1 
ATOM   5444  O  O   . SER C 1 83  ? -65.155 63.882  95.830  1.00 33.30 ? 83   SER C O   1 
ATOM   5445  C  CB  . SER C 1 83  ? -62.969 65.071  97.574  1.00 31.60 ? 83   SER C CB  1 
ATOM   5446  O  OG  . SER C 1 83  ? -63.733 66.258  97.762  1.00 24.54 ? 83   SER C OG  1 
ATOM   5447  N  N   . SER C 1 84  ? -64.531 65.682  94.640  1.00 33.77 ? 84   SER C N   1 
ATOM   5448  C  CA  . SER C 1 84  ? -65.792 65.832  93.947  1.00 32.71 ? 84   SER C CA  1 
ATOM   5449  C  C   . SER C 1 84  ? -65.660 65.301  92.514  1.00 31.62 ? 84   SER C C   1 
ATOM   5450  O  O   . SER C 1 84  ? -66.565 65.472  91.693  1.00 35.08 ? 84   SER C O   1 
ATOM   5451  C  CB  . SER C 1 84  ? -66.202 67.294  93.916  1.00 30.24 ? 84   SER C CB  1 
ATOM   5452  O  OG  . SER C 1 84  ? -66.958 67.625  95.055  1.00 34.77 ? 84   SER C OG  1 
ATOM   5453  N  N   . CYS C 1 85  ? -64.529 64.659  92.237  1.00 28.57 ? 85   CYS C N   1 
ATOM   5454  C  CA  . CYS C 1 85  ? -64.228 64.094  90.928  1.00 34.23 ? 85   CYS C CA  1 
ATOM   5455  C  C   . CYS C 1 85  ? -64.261 65.153  89.796  1.00 35.82 ? 85   CYS C C   1 
ATOM   5456  O  O   . CYS C 1 85  ? -64.763 64.926  88.687  1.00 37.29 ? 85   CYS C O   1 
ATOM   5457  C  CB  . CYS C 1 85  ? -65.182 62.923  90.630  1.00 33.81 ? 85   CYS C CB  1 
ATOM   5458  S  SG  . CYS C 1 85  ? -65.082 61.567  91.855  1.00 40.69 ? 85   CYS C SG  1 
ATOM   5459  N  N   . ARG C 1 86  ? -63.707 66.314  90.102  1.00 36.26 ? 86   ARG C N   1 
ATOM   5460  C  CA  . ARG C 1 86  ? -63.660 67.422  89.171  1.00 36.48 ? 86   ARG C CA  1 
ATOM   5461  C  C   . ARG C 1 86  ? -62.224 67.726  88.871  1.00 37.77 ? 86   ARG C C   1 
ATOM   5462  O  O   . ARG C 1 86  ? -61.379 67.692  89.765  1.00 38.03 ? 86   ARG C O   1 
ATOM   5463  C  CB  . ARG C 1 86  ? -64.297 68.660  89.798  1.00 35.36 ? 86   ARG C CB  1 
ATOM   5464  C  CG  . ARG C 1 86  ? -65.785 68.633  89.815  1.00 35.61 ? 86   ARG C CG  1 
ATOM   5465  C  CD  . ARG C 1 86  ? -66.288 69.044  88.452  1.00 40.17 ? 86   ARG C CD  1 
ATOM   5466  N  NE  . ARG C 1 86  ? -67.739 68.939  88.344  1.00 40.84 ? 86   ARG C NE  1 
ATOM   5467  C  CZ  . ARG C 1 86  ? -68.411 69.234  87.242  1.00 36.41 ? 86   ARG C CZ  1 
ATOM   5468  N  NH1 . ARG C 1 86  ? -67.736 69.655  86.176  1.00 26.91 ? 86   ARG C NH1 1 
ATOM   5469  N  NH2 . ARG C 1 86  ? -69.737 69.086  87.207  1.00 33.59 ? 86   ARG C NH2 1 
ATOM   5470  N  N   . ASP C 1 87  ? -61.946 68.020  87.608  1.00 39.18 ? 87   ASP C N   1 
ATOM   5471  C  CA  . ASP C 1 87  ? -60.607 68.365  87.187  1.00 38.43 ? 87   ASP C CA  1 
ATOM   5472  C  C   . ASP C 1 87  ? -60.320 69.728  87.828  1.00 41.93 ? 87   ASP C C   1 
ATOM   5473  O  O   . ASP C 1 87  ? -61.167 70.637  87.796  1.00 46.09 ? 87   ASP C O   1 
ATOM   5474  C  CB  . ASP C 1 87  ? -60.571 68.492  85.674  1.00 39.40 ? 87   ASP C CB  1 
ATOM   5475  C  CG  . ASP C 1 87  ? -59.158 68.625  85.130  1.00 44.98 ? 87   ASP C CG  1 
ATOM   5476  O  OD1 . ASP C 1 87  ? -58.209 68.829  85.936  1.00 47.34 ? 87   ASP C OD1 1 
ATOM   5477  O  OD2 . ASP C 1 87  ? -59.003 68.531  83.892  1.00 40.23 ? 87   ASP C OD2 1 
ATOM   5478  N  N   . PRO C 1 88  ? -59.151 69.869  88.459  1.00 39.74 ? 88   PRO C N   1 
ATOM   5479  C  CA  . PRO C 1 88  ? -58.704 71.097  89.124  1.00 42.10 ? 88   PRO C CA  1 
ATOM   5480  C  C   . PRO C 1 88  ? -58.038 71.992  88.091  1.00 44.31 ? 88   PRO C C   1 
ATOM   5481  O  O   . PRO C 1 88  ? -57.931 73.210  88.261  1.00 44.88 ? 88   PRO C O   1 
ATOM   5482  C  CB  . PRO C 1 88  ? -57.681 70.597  90.132  1.00 42.12 ? 88   PRO C CB  1 
ATOM   5483  C  CG  . PRO C 1 88  ? -58.000 69.109  90.258  1.00 42.21 ? 88   PRO C CG  1 
ATOM   5484  C  CD  . PRO C 1 88  ? -58.332 68.727  88.874  1.00 39.63 ? 88   PRO C CD  1 
ATOM   5485  N  N   . GLY C 1 89  ? -57.584 71.339  87.026  1.00 44.95 ? 89   GLY C N   1 
ATOM   5486  C  CA  . GLY C 1 89  ? -56.903 71.999  85.931  1.00 43.91 ? 89   GLY C CA  1 
ATOM   5487  C  C   . GLY C 1 89  ? -55.940 73.081  86.334  1.00 45.26 ? 89   GLY C C   1 
ATOM   5488  O  O   . GLY C 1 89  ? -54.994 72.912  87.115  1.00 47.56 ? 89   GLY C O   1 
ATOM   5489  N  N   . ASP C 1 90  ? -56.202 74.225  85.751  1.00 46.87 ? 90   ASP C N   1 
ATOM   5490  C  CA  . ASP C 1 90  ? -55.442 75.429  85.984  1.00 50.45 ? 90   ASP C CA  1 
ATOM   5491  C  C   . ASP C 1 90  ? -54.707 75.511  87.342  1.00 49.24 ? 90   ASP C C   1 
ATOM   5492  O  O   . ASP C 1 90  ? -53.491 75.737  87.405  1.00 48.10 ? 90   ASP C O   1 
ATOM   5493  C  CB  . ASP C 1 90  ? -56.436 76.575  85.864  1.00 57.80 ? 90   ASP C CB  1 
ATOM   5494  C  CG  . ASP C 1 90  ? -55.810 77.825  85.364  1.00 64.64 ? 90   ASP C CG  1 
ATOM   5495  O  OD1 . ASP C 1 90  ? -54.849 77.698  84.585  1.00 70.62 ? 90   ASP C OD1 1 
ATOM   5496  O  OD2 . ASP C 1 90  ? -56.286 78.927  85.726  1.00 72.03 ? 90   ASP C OD2 1 
ATOM   5497  N  N   . LYS C 1 91  ? -55.466 75.318  88.420  1.00 47.01 ? 91   LYS C N   1 
ATOM   5498  C  CA  . LYS C 1 91  ? -54.959 75.439  89.780  1.00 46.11 ? 91   LYS C CA  1 
ATOM   5499  C  C   . LYS C 1 91  ? -53.696 74.684  90.143  1.00 46.07 ? 91   LYS C C   1 
ATOM   5500  O  O   . LYS C 1 91  ? -52.854 75.196  90.889  1.00 45.09 ? 91   LYS C O   1 
ATOM   5501  C  CB  . LYS C 1 91  ? -56.060 75.085  90.767  1.00 43.37 ? 91   LYS C CB  1 
ATOM   5502  C  CG  . LYS C 1 91  ? -57.413 75.470  90.278  1.00 43.68 ? 91   LYS C CG  1 
ATOM   5503  C  CD  . LYS C 1 91  ? -58.282 76.081  91.365  1.00 45.53 ? 91   LYS C CD  1 
ATOM   5504  C  CE  . LYS C 1 91  ? -59.607 76.536  90.769  1.00 49.18 ? 91   LYS C CE  1 
ATOM   5505  N  NZ  . LYS C 1 91  ? -60.095 77.719  91.492  1.00 51.99 ? 91   LYS C NZ  1 
ATOM   5506  N  N   . VAL C 1 92  ? -53.554 73.470  89.630  1.00 44.62 ? 92   VAL C N   1 
ATOM   5507  C  CA  . VAL C 1 92  ? -52.372 72.686  89.944  1.00 41.53 ? 92   VAL C CA  1 
ATOM   5508  C  C   . VAL C 1 92  ? -51.110 73.283  89.330  1.00 43.57 ? 92   VAL C C   1 
ATOM   5509  O  O   . VAL C 1 92  ? -50.058 73.283  89.956  1.00 43.27 ? 92   VAL C O   1 
ATOM   5510  C  CB  . VAL C 1 92  ? -52.551 71.252  89.472  1.00 39.02 ? 92   VAL C CB  1 
ATOM   5511  C  CG1 . VAL C 1 92  ? -51.299 70.459  89.700  1.00 34.68 ? 92   VAL C CG1 1 
ATOM   5512  C  CG2 . VAL C 1 92  ? -53.701 70.629  90.215  1.00 38.83 ? 92   VAL C CG2 1 
ATOM   5513  N  N   . SER C 1 93  ? -51.209 73.798  88.107  1.00 47.90 ? 93   SER C N   1 
ATOM   5514  C  CA  . SER C 1 93  ? -50.044 74.408  87.446  1.00 49.12 ? 93   SER C CA  1 
ATOM   5515  C  C   . SER C 1 93  ? -49.639 75.644  88.228  1.00 50.50 ? 93   SER C C   1 
ATOM   5516  O  O   . SER C 1 93  ? -48.465 75.849  88.533  1.00 49.95 ? 93   SER C O   1 
ATOM   5517  C  CB  . SER C 1 93  ? -50.378 74.845  86.019  1.00 47.17 ? 93   SER C CB  1 
ATOM   5518  O  OG  . SER C 1 93  ? -50.689 73.739  85.198  1.00 55.11 ? 93   SER C OG  1 
ATOM   5519  N  N   . ILE C 1 94  ? -50.637 76.466  88.533  1.00 48.67 ? 94   ILE C N   1 
ATOM   5520  C  CA  . ILE C 1 94  ? -50.438 77.695  89.262  1.00 48.19 ? 94   ILE C CA  1 
ATOM   5521  C  C   . ILE C 1 94  ? -49.769 77.404  90.581  1.00 49.61 ? 94   ILE C C   1 
ATOM   5522  O  O   . ILE C 1 94  ? -48.781 78.043  90.919  1.00 53.12 ? 94   ILE C O   1 
ATOM   5523  C  CB  . ILE C 1 94  ? -51.795 78.409  89.454  1.00 50.01 ? 94   ILE C CB  1 
ATOM   5524  C  CG1 . ILE C 1 94  ? -52.357 78.720  88.046  1.00 55.64 ? 94   ILE C CG1 1 
ATOM   5525  C  CG2 . ILE C 1 94  ? -51.631 79.666  90.291  1.00 43.91 ? 94   ILE C CG2 1 
ATOM   5526  C  CD1 . ILE C 1 94  ? -53.730 79.402  87.971  1.00 55.79 ? 94   ILE C CD1 1 
ATOM   5527  N  N   . LEU C 1 95  ? -50.279 76.412  91.309  1.00 52.39 ? 95   LEU C N   1 
ATOM   5528  C  CA  . LEU C 1 95  ? -49.720 76.049  92.607  1.00 50.67 ? 95   LEU C CA  1 
ATOM   5529  C  C   . LEU C 1 95  ? -48.297 75.541  92.464  1.00 51.64 ? 95   LEU C C   1 
ATOM   5530  O  O   . LEU C 1 95  ? -47.409 75.973  93.198  1.00 52.96 ? 95   LEU C O   1 
ATOM   5531  C  CB  . LEU C 1 95  ? -50.589 74.984  93.312  1.00 51.63 ? 95   LEU C CB  1 
ATOM   5532  C  CG  . LEU C 1 95  ? -50.111 74.403  94.667  1.00 50.31 ? 95   LEU C CG  1 
ATOM   5533  C  CD1 . LEU C 1 95  ? -49.915 75.522  95.668  1.00 51.50 ? 95   LEU C CD1 1 
ATOM   5534  C  CD2 . LEU C 1 95  ? -51.118 73.410  95.222  1.00 49.80 ? 95   LEU C CD2 1 
ATOM   5535  N  N   . GLN C 1 96  ? -48.076 74.634  91.520  1.00 52.88 ? 96   GLN C N   1 
ATOM   5536  C  CA  . GLN C 1 96  ? -46.748 74.064  91.308  1.00 57.15 ? 96   GLN C CA  1 
ATOM   5537  C  C   . GLN C 1 96  ? -45.696 75.172  91.146  1.00 57.99 ? 96   GLN C C   1 
ATOM   5538  O  O   . GLN C 1 96  ? -44.636 75.122  91.773  1.00 56.45 ? 96   GLN C O   1 
ATOM   5539  C  CB  . GLN C 1 96  ? -46.774 73.137  90.075  1.00 60.79 ? 96   GLN C CB  1 
ATOM   5540  C  CG  . GLN C 1 96  ? -45.468 72.409  89.733  1.00 69.15 ? 96   GLN C CG  1 
ATOM   5541  C  CD  . GLN C 1 96  ? -44.972 71.412  90.819  1.00 77.79 ? 96   GLN C CD  1 
ATOM   5542  O  OE1 . GLN C 1 96  ? -45.698 70.498  91.241  1.00 78.26 ? 96   GLN C OE1 1 
ATOM   5543  N  NE2 . GLN C 1 96  ? -43.715 71.582  91.248  1.00 77.92 ? 96   GLN C NE2 1 
ATOM   5544  N  N   . ARG C 1 97  ? -45.990 76.191  90.341  1.00 58.52 ? 97   ARG C N   1 
ATOM   5545  C  CA  . ARG C 1 97  ? -45.009 77.241  90.143  1.00 59.94 ? 97   ARG C CA  1 
ATOM   5546  C  C   . ARG C 1 97  ? -44.896 78.167  91.331  1.00 58.39 ? 97   ARG C C   1 
ATOM   5547  O  O   . ARG C 1 97  ? -43.819 78.717  91.575  1.00 61.46 ? 97   ARG C O   1 
ATOM   5548  C  CB  . ARG C 1 97  ? -45.262 78.032  88.840  1.00 63.31 ? 97   ARG C CB  1 
ATOM   5549  C  CG  . ARG C 1 97  ? -46.212 79.232  88.895  1.00 66.66 ? 97   ARG C CG  1 
ATOM   5550  C  CD  . ARG C 1 97  ? -46.202 79.964  87.522  1.00 66.37 ? 97   ARG C CD  1 
ATOM   5551  N  NE  . ARG C 1 97  ? -46.940 79.234  86.492  1.00 67.88 ? 97   ARG C NE  1 
ATOM   5552  C  CZ  . ARG C 1 97  ? -48.224 79.443  86.215  1.00 70.80 ? 97   ARG C CZ  1 
ATOM   5553  N  NH1 . ARG C 1 97  ? -48.897 80.374  86.888  1.00 71.06 ? 97   ARG C NH1 1 
ATOM   5554  N  NH2 . ARG C 1 97  ? -48.845 78.702  85.298  1.00 70.62 ? 97   ARG C NH2 1 
ATOM   5555  N  N   . GLN C 1 98  ? -45.975 78.345  92.083  1.00 53.34 ? 98   GLN C N   1 
ATOM   5556  C  CA  . GLN C 1 98  ? -45.868 79.193  93.254  1.00 49.83 ? 98   GLN C CA  1 
ATOM   5557  C  C   . GLN C 1 98  ? -44.986 78.520  94.285  1.00 50.60 ? 98   GLN C C   1 
ATOM   5558  O  O   . GLN C 1 98  ? -44.190 79.181  94.940  1.00 51.03 ? 98   GLN C O   1 
ATOM   5559  C  CB  . GLN C 1 98  ? -47.226 79.473  93.860  1.00 48.90 ? 98   GLN C CB  1 
ATOM   5560  C  CG  . GLN C 1 98  ? -48.009 80.427  93.043  1.00 49.86 ? 98   GLN C CG  1 
ATOM   5561  C  CD  . GLN C 1 98  ? -49.281 80.839  93.703  1.00 53.39 ? 98   GLN C CD  1 
ATOM   5562  O  OE1 . GLN C 1 98  ? -50.117 81.449  93.067  1.00 57.67 ? 98   GLN C OE1 1 
ATOM   5563  N  NE2 . GLN C 1 98  ? -49.440 80.519  94.989  1.00 56.17 ? 98   GLN C NE2 1 
ATOM   5564  N  N   . MET C 1 99  ? -45.133 77.205  94.422  1.00 50.88 ? 99   MET C N   1 
ATOM   5565  C  CA  . MET C 1 99  ? -44.344 76.427  95.378  1.00 54.34 ? 99   MET C CA  1 
ATOM   5566  C  C   . MET C 1 99  ? -42.851 76.320  95.055  1.00 57.13 ? 99   MET C C   1 
ATOM   5567  O  O   . MET C 1 99  ? -42.037 76.210  95.972  1.00 59.55 ? 99   MET C O   1 
ATOM   5568  C  CB  . MET C 1 99  ? -44.906 75.010  95.517  1.00 49.33 ? 99   MET C CB  1 
ATOM   5569  C  CG  . MET C 1 99  ? -46.151 74.926  96.333  1.00 46.85 ? 99   MET C CG  1 
ATOM   5570  S  SD  . MET C 1 99  ? -45.816 75.701  97.884  1.00 45.79 ? 99   MET C SD  1 
ATOM   5571  C  CE  . MET C 1 99  ? -44.565 74.659  98.527  1.00 45.93 ? 99   MET C CE  1 
ATOM   5572  N  N   . GLU C 1 100 ? -42.495 76.323  93.771  1.00 59.57 ? 100  GLU C N   1 
ATOM   5573  C  CA  . GLU C 1 100 ? -41.090 76.236  93.373  1.00 64.06 ? 100  GLU C CA  1 
ATOM   5574  C  C   . GLU C 1 100 ? -40.441 77.563  93.726  1.00 64.23 ? 100  GLU C C   1 
ATOM   5575  O  O   . GLU C 1 100 ? -39.225 77.696  93.740  1.00 65.51 ? 100  GLU C O   1 
ATOM   5576  C  CB  . GLU C 1 100 ? -40.968 75.962  91.863  1.00 65.62 ? 100  GLU C CB  1 
ATOM   5577  C  CG  . GLU C 1 100 ? -41.611 74.638  91.460  1.00 74.19 ? 100  GLU C CG  1 
ATOM   5578  C  CD  . GLU C 1 100 ? -41.606 74.366  89.962  1.00 79.39 ? 100  GLU C CD  1 
ATOM   5579  O  OE1 . GLU C 1 100 ? -41.801 75.320  89.169  1.00 83.27 ? 100  GLU C OE1 1 
ATOM   5580  O  OE2 . GLU C 1 100 ? -41.434 73.183  89.577  1.00 80.85 ? 100  GLU C OE2 1 
ATOM   5581  N  N   . ASN C 1 101 ? -41.286 78.526  94.066  1.00 64.71 ? 101  ASN C N   1 
ATOM   5582  C  CA  . ASN C 1 101 ? -40.875 79.877  94.412  1.00 63.51 ? 101  ASN C CA  1 
ATOM   5583  C  C   . ASN C 1 101 ? -41.059 80.174  95.879  1.00 61.26 ? 101  ASN C C   1 
ATOM   5584  O  O   . ASN C 1 101 ? -40.831 81.301  96.326  1.00 60.18 ? 101  ASN C O   1 
ATOM   5585  C  CB  . ASN C 1 101 ? -41.736 80.859  93.630  1.00 70.43 ? 101  ASN C CB  1 
ATOM   5586  C  CG  . ASN C 1 101 ? -40.925 81.816  92.821  1.00 75.01 ? 101  ASN C CG  1 
ATOM   5587  O  OD1 . ASN C 1 101 ? -40.510 82.867  93.314  1.00 77.26 ? 101  ASN C OD1 1 
ATOM   5588  N  ND2 . ASN C 1 101 ? -40.675 81.458  91.565  1.00 76.91 ? 101  ASN C ND2 1 
ATOM   5589  N  N   . TRP C 1 102 ? -41.508 79.180  96.628  1.00 59.05 ? 102  TRP C N   1 
ATOM   5590  C  CA  . TRP C 1 102 ? -41.748 79.385  98.045  1.00 57.26 ? 102  TRP C CA  1 
ATOM   5591  C  C   . TRP C 1 102 ? -40.536 79.076  98.937  1.00 57.70 ? 102  TRP C C   1 
ATOM   5592  O  O   . TRP C 1 102 ? -39.716 78.189  98.644  1.00 56.96 ? 102  TRP C O   1 
ATOM   5593  C  CB  . TRP C 1 102 ? -42.950 78.544  98.510  1.00 51.96 ? 102  TRP C CB  1 
ATOM   5594  C  CG  . TRP C 1 102 ? -43.145 78.609  99.995  1.00 46.84 ? 102  TRP C CG  1 
ATOM   5595  C  CD1 . TRP C 1 102 ? -43.875 79.530  100.687 1.00 44.66 ? 102  TRP C CD1 1 
ATOM   5596  C  CD2 . TRP C 1 102 ? -42.538 77.757  100.976 1.00 43.26 ? 102  TRP C CD2 1 
ATOM   5597  N  NE1 . TRP C 1 102 ? -43.761 79.309  102.047 1.00 41.52 ? 102  TRP C NE1 1 
ATOM   5598  C  CE2 . TRP C 1 102 ? -42.945 78.226  102.249 1.00 43.97 ? 102  TRP C CE2 1 
ATOM   5599  C  CE3 . TRP C 1 102 ? -41.694 76.643  100.906 1.00 43.34 ? 102  TRP C CE3 1 
ATOM   5600  C  CZ2 . TRP C 1 102 ? -42.535 77.613  103.444 1.00 42.73 ? 102  TRP C CZ2 1 
ATOM   5601  C  CZ3 . TRP C 1 102 ? -41.286 76.029  102.104 1.00 45.49 ? 102  TRP C CZ3 1 
ATOM   5602  C  CH2 . TRP C 1 102 ? -41.710 76.523  103.353 1.00 41.88 ? 102  TRP C CH2 1 
ATOM   5603  N  N   . ALA C 1 103 ? -40.451 79.832  100.026 1.00 56.17 ? 103  ALA C N   1 
ATOM   5604  C  CA  . ALA C 1 103 ? -39.408 79.685  101.030 1.00 56.83 ? 103  ALA C CA  1 
ATOM   5605  C  C   . ALA C 1 103 ? -39.895 80.431  102.264 1.00 56.27 ? 103  ALA C C   1 
ATOM   5606  O  O   . ALA C 1 103 ? -40.600 81.443  102.163 1.00 55.27 ? 103  ALA C O   1 
ATOM   5607  C  CB  . ALA C 1 103 ? -38.114 80.267  100.545 1.00 56.33 ? 103  ALA C CB  1 
ATOM   5608  N  N   . PRO C 1 104 ? -39.558 79.926  103.454 1.00 55.83 ? 104  PRO C N   1 
ATOM   5609  C  CA  . PRO C 1 104 ? -40.041 80.662  104.631 1.00 55.90 ? 104  PRO C CA  1 
ATOM   5610  C  C   . PRO C 1 104 ? -39.417 82.067  104.711 1.00 57.88 ? 104  PRO C C   1 
ATOM   5611  O  O   . PRO C 1 104 ? -38.441 82.367  104.010 1.00 56.89 ? 104  PRO C O   1 
ATOM   5612  C  CB  . PRO C 1 104 ? -39.655 79.742  105.799 1.00 53.06 ? 104  PRO C CB  1 
ATOM   5613  C  CG  . PRO C 1 104 ? -38.472 78.951  105.270 1.00 52.85 ? 104  PRO C CG  1 
ATOM   5614  C  CD  . PRO C 1 104 ? -38.821 78.699  103.818 1.00 52.23 ? 104  PRO C CD  1 
ATOM   5615  N  N   . SER C 1 105 ? -39.983 82.943  105.531 1.00 60.57 ? 105  SER C N   1 
ATOM   5616  C  CA  . SER C 1 105 ? -39.417 84.280  105.667 1.00 65.36 ? 105  SER C CA  1 
ATOM   5617  C  C   . SER C 1 105 ? -38.013 84.273  106.330 1.00 68.63 ? 105  SER C C   1 
ATOM   5618  O  O   . SER C 1 105 ? -37.197 85.159  106.064 1.00 70.49 ? 105  SER C O   1 
ATOM   5619  C  CB  . SER C 1 105 ? -40.387 85.189  106.433 1.00 65.88 ? 105  SER C CB  1 
ATOM   5620  O  OG  . SER C 1 105 ? -40.907 84.551  107.590 1.00 73.49 ? 105  SER C OG  1 
ATOM   5621  N  N   . SER C 1 106 ? -37.727 83.283  107.179 1.00 70.54 ? 106  SER C N   1 
ATOM   5622  C  CA  . SER C 1 106 ? -36.409 83.180  107.812 1.00 73.26 ? 106  SER C CA  1 
ATOM   5623  C  C   . SER C 1 106 ? -36.317 81.825  108.492 1.00 74.87 ? 106  SER C C   1 
ATOM   5624  O  O   . SER C 1 106 ? -37.314 81.101  108.569 1.00 76.33 ? 106  SER C O   1 
ATOM   5625  C  CB  . SER C 1 106 ? -36.216 84.277  108.862 1.00 74.28 ? 106  SER C CB  1 
ATOM   5626  O  OG  . SER C 1 106 ? -36.821 83.916  110.101 1.00 76.29 ? 106  SER C OG  1 
ATOM   5627  N  N   . PRO C 1 107 ? -35.122 81.460  108.992 1.00 75.03 ? 107  PRO C N   1 
ATOM   5628  C  CA  . PRO C 1 107 ? -34.988 80.160  109.663 1.00 73.71 ? 107  PRO C CA  1 
ATOM   5629  C  C   . PRO C 1 107 ? -35.591 80.169  111.051 1.00 71.53 ? 107  PRO C C   1 
ATOM   5630  O  O   . PRO C 1 107 ? -35.632 79.137  111.732 1.00 71.34 ? 107  PRO C O   1 
ATOM   5631  C  CB  . PRO C 1 107 ? -33.481 79.928  109.688 1.00 76.62 ? 107  PRO C CB  1 
ATOM   5632  C  CG  . PRO C 1 107 ? -32.913 81.316  109.676 1.00 76.56 ? 107  PRO C CG  1 
ATOM   5633  C  CD  . PRO C 1 107 ? -33.804 82.064  108.724 1.00 73.80 ? 107  PRO C CD  1 
ATOM   5634  N  N   . ASN C 1 108 ? -36.056 81.340  111.472 1.00 69.97 ? 108  ASN C N   1 
ATOM   5635  C  CA  . ASN C 1 108 ? -36.665 81.454  112.787 1.00 72.68 ? 108  ASN C CA  1 
ATOM   5636  C  C   . ASN C 1 108 ? -38.160 81.719  112.701 1.00 69.79 ? 108  ASN C C   1 
ATOM   5637  O  O   . ASN C 1 108 ? -38.830 81.984  113.709 1.00 70.14 ? 108  ASN C O   1 
ATOM   5638  C  CB  . ASN C 1 108 ? -35.952 82.532  113.598 1.00 76.40 ? 108  ASN C CB  1 
ATOM   5639  C  CG  . ASN C 1 108 ? -34.515 82.129  113.947 1.00 83.27 ? 108  ASN C CG  1 
ATOM   5640  O  OD1 . ASN C 1 108 ? -33.577 82.897  113.715 1.00 85.34 ? 108  ASN C OD1 1 
ATOM   5641  N  ND2 . ASN C 1 108 ? -34.340 80.917  114.501 1.00 82.78 ? 108  ASN C ND2 1 
ATOM   5642  N  N   . ALA C 1 109 ? -38.680 81.616  111.482 1.00 64.13 ? 109  ALA C N   1 
ATOM   5643  C  CA  . ALA C 1 109 ? -40.099 81.813  111.233 1.00 57.98 ? 109  ALA C CA  1 
ATOM   5644  C  C   . ALA C 1 109 ? -40.913 80.856  112.118 1.00 55.10 ? 109  ALA C C   1 
ATOM   5645  O  O   . ALA C 1 109 ? -40.450 79.740  112.436 1.00 53.08 ? 109  ALA C O   1 
ATOM   5646  C  CB  . ALA C 1 109 ? -40.402 81.561  109.753 1.00 54.42 ? 109  ALA C CB  1 
ATOM   5647  N  N   . GLU C 1 110 ? -42.112 81.304  112.503 1.00 48.61 ? 110  GLU C N   1 
ATOM   5648  C  CA  . GLU C 1 110 ? -43.030 80.533  113.346 1.00 48.65 ? 110  GLU C CA  1 
ATOM   5649  C  C   . GLU C 1 110 ? -43.456 79.203  112.699 1.00 49.78 ? 110  GLU C C   1 
ATOM   5650  O  O   . GLU C 1 110 ? -43.628 79.115  111.472 1.00 48.10 ? 110  GLU C O   1 
ATOM   5651  C  CB  . GLU C 1 110 ? -44.288 81.364  113.660 1.00 48.57 ? 110  GLU C CB  1 
ATOM   5652  C  CG  . GLU C 1 110 ? -45.283 81.507  112.507 1.00 52.78 ? 110  GLU C CG  1 
ATOM   5653  C  CD  . GLU C 1 110 ? -44.799 82.438  111.393 1.00 55.88 ? 110  GLU C CD  1 
ATOM   5654  O  OE1 . GLU C 1 110 ? -43.591 82.788  111.358 1.00 60.01 ? 110  GLU C OE1 1 
ATOM   5655  O  OE2 . GLU C 1 110 ? -45.632 82.815  110.542 1.00 54.56 ? 110  GLU C OE2 1 
ATOM   5656  N  N   . ALA C 1 111 ? -43.630 78.175  113.526 1.00 47.23 ? 111  ALA C N   1 
ATOM   5657  C  CA  . ALA C 1 111 ? -44.040 76.866  113.033 1.00 46.77 ? 111  ALA C CA  1 
ATOM   5658  C  C   . ALA C 1 111 ? -45.217 76.904  112.037 1.00 47.65 ? 111  ALA C C   1 
ATOM   5659  O  O   . ALA C 1 111 ? -45.163 76.271  110.986 1.00 49.29 ? 111  ALA C O   1 
ATOM   5660  C  CB  . ALA C 1 111 ? -44.394 75.966  114.213 1.00 45.22 ? 111  ALA C CB  1 
ATOM   5661  N  N   . SER C 1 112 ? -46.274 77.649  112.352 1.00 47.91 ? 112  SER C N   1 
ATOM   5662  C  CA  . SER C 1 112 ? -47.444 77.683  111.474 1.00 44.74 ? 112  SER C CA  1 
ATOM   5663  C  C   . SER C 1 112 ? -47.151 78.234  110.091 1.00 45.90 ? 112  SER C C   1 
ATOM   5664  O  O   . SER C 1 112 ? -48.024 78.217  109.213 1.00 47.58 ? 112  SER C O   1 
ATOM   5665  C  CB  . SER C 1 112 ? -48.588 78.477  112.115 1.00 41.96 ? 112  SER C CB  1 
ATOM   5666  O  OG  . SER C 1 112 ? -48.273 79.856  112.206 1.00 42.85 ? 112  SER C OG  1 
ATOM   5667  N  N   . ALA C 1 113 ? -45.935 78.723  109.872 1.00 43.54 ? 113  ALA C N   1 
ATOM   5668  C  CA  . ALA C 1 113 ? -45.610 79.262  108.555 1.00 41.55 ? 113  ALA C CA  1 
ATOM   5669  C  C   . ALA C 1 113 ? -45.562 78.104  107.552 1.00 43.07 ? 113  ALA C C   1 
ATOM   5670  O  O   . ALA C 1 113 ? -45.660 78.294  106.333 1.00 43.78 ? 113  ALA C O   1 
ATOM   5671  C  CB  . ALA C 1 113 ? -44.278 79.964  108.597 1.00 36.51 ? 113  ALA C CB  1 
ATOM   5672  N  N   . PHE C 1 114 ? -45.429 76.899  108.082 1.00 40.18 ? 114  PHE C N   1 
ATOM   5673  C  CA  . PHE C 1 114 ? -45.348 75.726  107.255 1.00 41.53 ? 114  PHE C CA  1 
ATOM   5674  C  C   . PHE C 1 114 ? -46.700 75.075  106.945 1.00 43.01 ? 114  PHE C C   1 
ATOM   5675  O  O   . PHE C 1 114 ? -46.799 74.196  106.079 1.00 43.32 ? 114  PHE C O   1 
ATOM   5676  C  CB  . PHE C 1 114 ? -44.399 74.743  107.933 1.00 42.14 ? 114  PHE C CB  1 
ATOM   5677  C  CG  . PHE C 1 114 ? -42.973 75.175  107.877 1.00 45.31 ? 114  PHE C CG  1 
ATOM   5678  C  CD1 . PHE C 1 114 ? -42.190 74.879  106.759 1.00 47.56 ? 114  PHE C CD1 1 
ATOM   5679  C  CD2 . PHE C 1 114 ? -42.420 75.943  108.897 1.00 48.48 ? 114  PHE C CD2 1 
ATOM   5680  C  CE1 . PHE C 1 114 ? -40.869 75.345  106.650 1.00 45.92 ? 114  PHE C CE1 1 
ATOM   5681  C  CE2 . PHE C 1 114 ? -41.099 76.421  108.806 1.00 49.33 ? 114  PHE C CE2 1 
ATOM   5682  C  CZ  . PHE C 1 114 ? -40.320 76.117  107.670 1.00 48.88 ? 114  PHE C CZ  1 
ATOM   5683  N  N   . TYR C 1 115 ? -47.747 75.520  107.628 1.00 42.21 ? 115  TYR C N   1 
ATOM   5684  C  CA  . TYR C 1 115 ? -49.083 74.954  107.428 1.00 41.35 ? 115  TYR C CA  1 
ATOM   5685  C  C   . TYR C 1 115 ? -49.553 74.999  105.949 1.00 39.85 ? 115  TYR C C   1 
ATOM   5686  O  O   . TYR C 1 115 ? -49.795 73.953  105.350 1.00 40.30 ? 115  TYR C O   1 
ATOM   5687  C  CB  . TYR C 1 115 ? -50.072 75.664  108.372 1.00 37.90 ? 115  TYR C CB  1 
ATOM   5688  C  CG  . TYR C 1 115 ? -51.427 75.001  108.507 1.00 40.61 ? 115  TYR C CG  1 
ATOM   5689  C  CD1 . TYR C 1 115 ? -52.409 75.171  107.523 1.00 36.99 ? 115  TYR C CD1 1 
ATOM   5690  C  CD2 . TYR C 1 115 ? -51.748 74.244  109.631 1.00 37.04 ? 115  TYR C CD2 1 
ATOM   5691  C  CE1 . TYR C 1 115 ? -53.666 74.617  107.656 1.00 36.68 ? 115  TYR C CE1 1 
ATOM   5692  C  CE2 . TYR C 1 115 ? -53.020 73.683  109.768 1.00 41.47 ? 115  TYR C CE2 1 
ATOM   5693  C  CZ  . TYR C 1 115 ? -53.971 73.881  108.773 1.00 39.34 ? 115  TYR C CZ  1 
ATOM   5694  O  OH  . TYR C 1 115 ? -55.245 73.364  108.901 1.00 44.66 ? 115  TYR C OH  1 
ATOM   5695  N  N   . GLY C 1 116 ? -49.665 76.192  105.366 1.00 39.16 ? 116  GLY C N   1 
ATOM   5696  C  CA  . GLY C 1 116 ? -50.081 76.326  103.973 1.00 41.15 ? 116  GLY C CA  1 
ATOM   5697  C  C   . GLY C 1 116 ? -49.238 75.505  102.995 1.00 43.46 ? 116  GLY C C   1 
ATOM   5698  O  O   . GLY C 1 116 ? -49.772 74.844  102.107 1.00 43.41 ? 116  GLY C O   1 
ATOM   5699  N  N   . PRO C 1 117 ? -47.902 75.566  103.107 1.00 44.36 ? 117  PRO C N   1 
ATOM   5700  C  CA  . PRO C 1 117 ? -47.005 74.811  102.238 1.00 41.64 ? 117  PRO C CA  1 
ATOM   5701  C  C   . PRO C 1 117 ? -47.269 73.302  102.366 1.00 42.20 ? 117  PRO C C   1 
ATOM   5702  O  O   . PRO C 1 117 ? -47.200 72.567  101.376 1.00 45.71 ? 117  PRO C O   1 
ATOM   5703  C  CB  . PRO C 1 117 ? -45.626 75.215  102.755 1.00 41.20 ? 117  PRO C CB  1 
ATOM   5704  C  CG  . PRO C 1 117 ? -45.811 76.619  103.107 1.00 39.95 ? 117  PRO C CG  1 
ATOM   5705  C  CD  . PRO C 1 117 ? -47.143 76.592  103.849 1.00 44.18 ? 117  PRO C CD  1 
ATOM   5706  N  N   . SER C 1 118 ? -47.559 72.834  103.577 1.00 39.05 ? 118  SER C N   1 
ATOM   5707  C  CA  . SER C 1 118 ? -47.854 71.415  103.788 1.00 38.54 ? 118  SER C CA  1 
ATOM   5708  C  C   . SER C 1 118 ? -49.083 71.025  102.958 1.00 40.04 ? 118  SER C C   1 
ATOM   5709  O  O   . SER C 1 118 ? -49.114 69.997  102.272 1.00 38.58 ? 118  SER C O   1 
ATOM   5710  C  CB  . SER C 1 118 ? -48.163 71.142  105.265 1.00 34.51 ? 118  SER C CB  1 
ATOM   5711  O  OG  . SER C 1 118 ? -47.034 71.390  106.059 1.00 36.93 ? 118  SER C OG  1 
ATOM   5712  N  N   . LEU C 1 119 ? -50.115 71.847  103.061 1.00 40.12 ? 119  LEU C N   1 
ATOM   5713  C  CA  . LEU C 1 119 ? -51.332 71.608  102.328 1.00 39.79 ? 119  LEU C CA  1 
ATOM   5714  C  C   . LEU C 1 119 ? -51.037 71.543  100.819 1.00 40.27 ? 119  LEU C C   1 
ATOM   5715  O  O   . LEU C 1 119 ? -51.553 70.677  100.099 1.00 43.62 ? 119  LEU C O   1 
ATOM   5716  C  CB  . LEU C 1 119 ? -52.311 72.730  102.634 1.00 39.85 ? 119  LEU C CB  1 
ATOM   5717  C  CG  . LEU C 1 119 ? -53.583 72.447  103.446 1.00 39.50 ? 119  LEU C CG  1 
ATOM   5718  C  CD1 . LEU C 1 119 ? -53.513 71.146  104.185 1.00 30.45 ? 119  LEU C CD1 1 
ATOM   5719  C  CD2 . LEU C 1 119 ? -53.789 73.618  104.396 1.00 36.42 ? 119  LEU C CD2 1 
ATOM   5720  N  N   . ALA C 1 120 ? -50.192 72.450  100.348 1.00 36.32 ? 120  ALA C N   1 
ATOM   5721  C  CA  . ALA C 1 120 ? -49.848 72.508  98.938  1.00 35.66 ? 120  ALA C CA  1 
ATOM   5722  C  C   . ALA C 1 120 ? -49.067 71.292  98.491  1.00 36.75 ? 120  ALA C C   1 
ATOM   5723  O  O   . ALA C 1 120 ? -49.310 70.732  97.416  1.00 36.70 ? 120  ALA C O   1 
ATOM   5724  C  CB  . ALA C 1 120 ? -49.052 73.753  98.644  1.00 31.02 ? 120  ALA C CB  1 
ATOM   5725  N  N   . ILE C 1 121 ? -48.104 70.890  99.296  1.00 36.67 ? 121  ILE C N   1 
ATOM   5726  C  CA  . ILE C 1 121 ? -47.314 69.748  98.917  1.00 36.47 ? 121  ILE C CA  1 
ATOM   5727  C  C   . ILE C 1 121 ? -48.219 68.530  98.900  1.00 35.31 ? 121  ILE C C   1 
ATOM   5728  O  O   . ILE C 1 121 ? -48.135 67.703  98.002  1.00 36.62 ? 121  ILE C O   1 
ATOM   5729  C  CB  . ILE C 1 121 ? -46.066 69.607  99.867  1.00 37.13 ? 121  ILE C CB  1 
ATOM   5730  C  CG1 . ILE C 1 121 ? -44.934 70.451  99.291  1.00 38.50 ? 121  ILE C CG1 1 
ATOM   5731  C  CG2 . ILE C 1 121 ? -45.594 68.152  100.005 1.00 32.18 ? 121  ILE C CG2 1 
ATOM   5732  C  CD1 . ILE C 1 121 ? -44.122 71.165  100.339 1.00 42.79 ? 121  ILE C CD1 1 
ATOM   5733  N  N   . LEU C 1 122 ? -49.106 68.414  99.867  1.00 35.53 ? 122  LEU C N   1 
ATOM   5734  C  CA  . LEU C 1 122 ? -50.002 67.261  99.853  1.00 36.33 ? 122  LEU C CA  1 
ATOM   5735  C  C   . LEU C 1 122 ? -50.789 67.235  98.530  1.00 36.56 ? 122  LEU C C   1 
ATOM   5736  O  O   . LEU C 1 122 ? -50.788 66.232  97.810  1.00 35.93 ? 122  LEU C O   1 
ATOM   5737  C  CB  . LEU C 1 122 ? -50.957 67.316  101.054 1.00 35.94 ? 122  LEU C CB  1 
ATOM   5738  C  CG  . LEU C 1 122 ? -51.958 66.169  101.179 1.00 34.67 ? 122  LEU C CG  1 
ATOM   5739  C  CD1 . LEU C 1 122 ? -51.269 64.814  100.976 1.00 28.68 ? 122  LEU C CD1 1 
ATOM   5740  C  CD2 . LEU C 1 122 ? -52.635 66.282  102.528 1.00 28.81 ? 122  LEU C CD2 1 
ATOM   5741  N  N   . ALA C 1 123 ? -51.448 68.345  98.203  1.00 36.03 ? 123  ALA C N   1 
ATOM   5742  C  CA  . ALA C 1 123 ? -52.212 68.429  96.960  1.00 36.68 ? 123  ALA C CA  1 
ATOM   5743  C  C   . ALA C 1 123 ? -51.376 68.030  95.738  1.00 37.26 ? 123  ALA C C   1 
ATOM   5744  O  O   . ALA C 1 123 ? -51.786 67.209  94.928  1.00 39.88 ? 123  ALA C O   1 
ATOM   5745  C  CB  . ALA C 1 123 ? -52.725 69.823  96.774  1.00 34.53 ? 123  ALA C CB  1 
ATOM   5746  N  N   . LEU C 1 124 ? -50.211 68.648  95.615  1.00 37.69 ? 124  LEU C N   1 
ATOM   5747  C  CA  . LEU C 1 124 ? -49.276 68.403  94.525  1.00 35.20 ? 124  LEU C CA  1 
ATOM   5748  C  C   . LEU C 1 124 ? -48.783 66.959  94.526  1.00 33.37 ? 124  LEU C C   1 
ATOM   5749  O  O   . LEU C 1 124 ? -48.552 66.381  93.481  1.00 32.69 ? 124  LEU C O   1 
ATOM   5750  C  CB  . LEU C 1 124 ? -48.094 69.382  94.642  1.00 32.43 ? 124  LEU C CB  1 
ATOM   5751  C  CG  . LEU C 1 124 ? -48.114 70.653  93.772  1.00 35.40 ? 124  LEU C CG  1 
ATOM   5752  C  CD1 . LEU C 1 124 ? -49.507 71.138  93.516  1.00 33.54 ? 124  LEU C CD1 1 
ATOM   5753  C  CD2 . LEU C 1 124 ? -47.271 71.727  94.432  1.00 33.02 ? 124  LEU C CD2 1 
ATOM   5754  N  N   . CYS C 1 125 ? -48.620 66.384  95.709  1.00 35.08 ? 125  CYS C N   1 
ATOM   5755  C  CA  . CYS C 1 125 ? -48.171 65.008  95.841  1.00 34.13 ? 125  CYS C CA  1 
ATOM   5756  C  C   . CYS C 1 125 ? -49.276 64.094  95.331  1.00 36.42 ? 125  CYS C C   1 
ATOM   5757  O  O   . CYS C 1 125 ? -49.011 63.056  94.730  1.00 38.62 ? 125  CYS C O   1 
ATOM   5758  C  CB  . CYS C 1 125 ? -47.870 64.683  97.301  1.00 34.63 ? 125  CYS C CB  1 
ATOM   5759  S  SG  . CYS C 1 125 ? -47.462 62.927  97.554  1.00 41.80 ? 125  CYS C SG  1 
ATOM   5760  N  N   . GLN C 1 126 ? -50.524 64.468  95.564  1.00 36.88 ? 126  GLN C N   1 
ATOM   5761  C  CA  . GLN C 1 126 ? -51.616 63.643  95.079  1.00 36.66 ? 126  GLN C CA  1 
ATOM   5762  C  C   . GLN C 1 126 ? -51.773 63.660  93.553  1.00 37.26 ? 126  GLN C C   1 
ATOM   5763  O  O   . GLN C 1 126 ? -52.160 62.660  92.953  1.00 36.44 ? 126  GLN C O   1 
ATOM   5764  C  CB  . GLN C 1 126 ? -52.903 64.059  95.760  1.00 36.49 ? 126  GLN C CB  1 
ATOM   5765  C  CG  . GLN C 1 126 ? -52.954 63.502  97.172  1.00 41.87 ? 126  GLN C CG  1 
ATOM   5766  C  CD  . GLN C 1 126 ? -54.103 64.047  97.970  1.00 41.73 ? 126  GLN C CD  1 
ATOM   5767  O  OE1 . GLN C 1 126 ? -54.405 63.539  99.043  1.00 45.67 ? 126  GLN C OE1 1 
ATOM   5768  N  NE2 . GLN C 1 126 ? -54.758 65.079  97.450  1.00 37.84 ? 126  GLN C NE2 1 
ATOM   5769  N  N   . LYS C 1 127 ? -51.441 64.782  92.929  1.00 36.70 ? 127  LYS C N   1 
ATOM   5770  C  CA  . LYS C 1 127 ? -51.553 64.913  91.490  1.00 38.94 ? 127  LYS C CA  1 
ATOM   5771  C  C   . LYS C 1 127 ? -50.376 64.339  90.738  1.00 39.81 ? 127  LYS C C   1 
ATOM   5772  O  O   . LYS C 1 127 ? -50.553 63.736  89.687  1.00 42.79 ? 127  LYS C O   1 
ATOM   5773  C  CB  . LYS C 1 127 ? -51.735 66.384  91.092  1.00 40.52 ? 127  LYS C CB  1 
ATOM   5774  C  CG  . LYS C 1 127 ? -53.161 66.890  91.336  1.00 50.06 ? 127  LYS C CG  1 
ATOM   5775  C  CD  . LYS C 1 127 ? -54.178 66.007  90.576  1.00 51.76 ? 127  LYS C CD  1 
ATOM   5776  C  CE  . LYS C 1 127 ? -55.580 66.214  91.091  1.00 49.90 ? 127  LYS C CE  1 
ATOM   5777  N  NZ  . LYS C 1 127 ? -55.571 65.981  92.561  1.00 55.34 ? 127  LYS C NZ  1 
ATOM   5778  N  N   . ASN C 1 128 ? -49.170 64.506  91.268  1.00 38.72 ? 128  ASN C N   1 
ATOM   5779  C  CA  . ASN C 1 128 ? -47.989 64.018  90.569  1.00 36.60 ? 128  ASN C CA  1 
ATOM   5780  C  C   . ASN C 1 128 ? -46.829 63.942  91.532  1.00 38.76 ? 128  ASN C C   1 
ATOM   5781  O  O   . ASN C 1 128 ? -46.008 64.849  91.615  1.00 37.44 ? 128  ASN C O   1 
ATOM   5782  C  CB  . ASN C 1 128 ? -47.657 64.957  89.408  1.00 32.63 ? 128  ASN C CB  1 
ATOM   5783  C  CG  . ASN C 1 128 ? -46.463 64.484  88.576  1.00 35.34 ? 128  ASN C CG  1 
ATOM   5784  O  OD1 . ASN C 1 128 ? -46.295 64.909  87.437  1.00 41.46 ? 128  ASN C OD1 1 
ATOM   5785  N  ND2 . ASN C 1 128 ? -45.633 63.622  89.138  1.00 29.12 ? 128  ASN C ND2 1 
ATOM   5786  N  N   . SER C 1 129 ? -46.739 62.824  92.233  1.00 39.70 ? 129  SER C N   1 
ATOM   5787  C  CA  . SER C 1 129 ? -45.704 62.658  93.222  1.00 39.83 ? 129  SER C CA  1 
ATOM   5788  C  C   . SER C 1 129 ? -44.286 62.909  92.751  1.00 39.78 ? 129  SER C C   1 
ATOM   5789  O  O   . SER C 1 129 ? -43.553 63.663  93.379  1.00 41.81 ? 129  SER C O   1 
ATOM   5790  C  CB  . SER C 1 129 ? -45.824 61.268  93.883  1.00 43.52 ? 129  SER C CB  1 
ATOM   5791  O  OG  . SER C 1 129 ? -45.725 60.201  92.953  1.00 52.08 ? 129  SER C OG  1 
ATOM   5792  N  N   . GLU C 1 130 ? -43.877 62.294  91.655  1.00 42.24 ? 130  GLU C N   1 
ATOM   5793  C  CA  . GLU C 1 130 ? -42.507 62.487  91.205  1.00 43.41 ? 130  GLU C CA  1 
ATOM   5794  C  C   . GLU C 1 130 ? -42.158 63.931  90.888  1.00 42.83 ? 130  GLU C C   1 
ATOM   5795  O  O   . GLU C 1 130 ? -41.048 64.368  91.198  1.00 42.79 ? 130  GLU C O   1 
ATOM   5796  C  CB  . GLU C 1 130 ? -42.221 61.589  90.001  1.00 44.73 ? 130  GLU C CB  1 
ATOM   5797  C  CG  . GLU C 1 130 ? -40.840 61.759  89.376  1.00 49.31 ? 130  GLU C CG  1 
ATOM   5798  C  CD  . GLU C 1 130 ? -40.435 60.554  88.511  1.00 56.28 ? 130  GLU C CD  1 
ATOM   5799  O  OE1 . GLU C 1 130 ? -41.332 59.884  87.942  1.00 55.27 ? 130  GLU C OE1 1 
ATOM   5800  O  OE2 . GLU C 1 130 ? -39.220 60.276  88.392  1.00 59.52 ? 130  GLU C OE2 1 
ATOM   5801  N  N   . ALA C 1 131 ? -43.095 64.666  90.286  1.00 42.09 ? 131  ALA C N   1 
ATOM   5802  C  CA  . ALA C 1 131 ? -42.867 66.072  89.918  1.00 42.87 ? 131  ALA C CA  1 
ATOM   5803  C  C   . ALA C 1 131 ? -42.702 66.932  91.168  1.00 44.01 ? 131  ALA C C   1 
ATOM   5804  O  O   . ALA C 1 131 ? -42.174 68.056  91.105  1.00 45.56 ? 131  ALA C O   1 
ATOM   5805  C  CB  . ALA C 1 131 ? -44.052 66.610  89.080  1.00 37.18 ? 131  ALA C CB  1 
ATOM   5806  N  N   . THR C 1 132 ? -43.131 66.378  92.298  1.00 40.26 ? 132  THR C N   1 
ATOM   5807  C  CA  . THR C 1 132 ? -43.131 67.076  93.561  1.00 41.93 ? 132  THR C CA  1 
ATOM   5808  C  C   . THR C 1 132 ? -41.923 66.818  94.451  1.00 44.77 ? 132  THR C C   1 
ATOM   5809  O  O   . THR C 1 132 ? -41.704 67.522  95.442  1.00 47.51 ? 132  THR C O   1 
ATOM   5810  C  CB  . THR C 1 132 ? -44.441 66.739  94.332  1.00 44.05 ? 132  THR C CB  1 
ATOM   5811  O  OG1 . THR C 1 132 ? -45.555 66.976  93.461  1.00 43.90 ? 132  THR C OG1 1 
ATOM   5812  C  CG2 . THR C 1 132 ? -44.594 67.614  95.599  1.00 40.65 ? 132  THR C CG2 1 
ATOM   5813  N  N   . LEU C 1 133 ? -41.124 65.821  94.110  1.00 45.22 ? 133  LEU C N   1 
ATOM   5814  C  CA  . LEU C 1 133 ? -39.943 65.508  94.925  1.00 44.51 ? 133  LEU C CA  1 
ATOM   5815  C  C   . LEU C 1 133 ? -39.058 66.712  95.231  1.00 42.69 ? 133  LEU C C   1 
ATOM   5816  O  O   . LEU C 1 133 ? -38.808 67.036  96.394  1.00 38.19 ? 133  LEU C O   1 
ATOM   5817  C  CB  . LEU C 1 133 ? -39.100 64.415  94.259  1.00 40.86 ? 133  LEU C CB  1 
ATOM   5818  C  CG  . LEU C 1 133 ? -39.547 62.988  94.585  1.00 37.62 ? 133  LEU C CG  1 
ATOM   5819  C  CD1 . LEU C 1 133 ? -38.741 62.025  93.732  1.00 38.87 ? 133  LEU C CD1 1 
ATOM   5820  C  CD2 . LEU C 1 133 ? -39.366 62.704  96.086  1.00 30.45 ? 133  LEU C CD2 1 
ATOM   5821  N  N   . PRO C 1 134 ? -38.572 67.394  94.187  1.00 44.18 ? 134  PRO C N   1 
ATOM   5822  C  CA  . PRO C 1 134 ? -37.710 68.567  94.398  1.00 45.53 ? 134  PRO C CA  1 
ATOM   5823  C  C   . PRO C 1 134 ? -38.271 69.471  95.501  1.00 48.32 ? 134  PRO C C   1 
ATOM   5824  O  O   . PRO C 1 134 ? -37.590 69.741  96.496  1.00 50.03 ? 134  PRO C O   1 
ATOM   5825  C  CB  . PRO C 1 134 ? -37.722 69.267  93.042  1.00 42.00 ? 134  PRO C CB  1 
ATOM   5826  C  CG  . PRO C 1 134 ? -37.929 68.152  92.094  1.00 43.06 ? 134  PRO C CG  1 
ATOM   5827  C  CD  . PRO C 1 134 ? -38.950 67.259  92.773  1.00 40.49 ? 134  PRO C CD  1 
ATOM   5828  N  N   . ILE C 1 135 ? -39.516 69.922  95.327  1.00 47.45 ? 135  ILE C N   1 
ATOM   5829  C  CA  . ILE C 1 135 ? -40.147 70.798  96.302  1.00 44.97 ? 135  ILE C CA  1 
ATOM   5830  C  C   . ILE C 1 135 ? -40.265 70.159  97.678  1.00 43.03 ? 135  ILE C C   1 
ATOM   5831  O  O   . ILE C 1 135 ? -40.033 70.813  98.686  1.00 41.59 ? 135  ILE C O   1 
ATOM   5832  C  CB  . ILE C 1 135 ? -41.553 71.212  95.840  1.00 48.78 ? 135  ILE C CB  1 
ATOM   5833  C  CG1 . ILE C 1 135 ? -41.445 72.169  94.663  1.00 55.61 ? 135  ILE C CG1 1 
ATOM   5834  C  CG2 . ILE C 1 135 ? -42.279 71.932  96.948  1.00 54.90 ? 135  ILE C CG2 1 
ATOM   5835  C  CD1 . ILE C 1 135 ? -42.796 72.579  94.088  1.00 60.93 ? 135  ILE C CD1 1 
ATOM   5836  N  N   . ALA C 1 136 ? -40.619 68.875  97.710  1.00 41.36 ? 136  ALA C N   1 
ATOM   5837  C  CA  . ALA C 1 136 ? -40.803 68.169  98.963  1.00 39.14 ? 136  ALA C CA  1 
ATOM   5838  C  C   . ALA C 1 136 ? -39.499 67.987  99.697  1.00 39.79 ? 136  ALA C C   1 
ATOM   5839  O  O   . ALA C 1 136 ? -39.462 68.098  100.922 1.00 37.65 ? 136  ALA C O   1 
ATOM   5840  C  CB  . ALA C 1 136 ? -41.468 66.839  98.718  1.00 38.44 ? 136  ALA C CB  1 
ATOM   5841  N  N   . VAL C 1 137 ? -38.426 67.721  98.959  1.00 39.54 ? 137  VAL C N   1 
ATOM   5842  C  CA  . VAL C 1 137 ? -37.109 67.549  99.580  1.00 38.33 ? 137  VAL C CA  1 
ATOM   5843  C  C   . VAL C 1 137 ? -36.739 68.863  100.275 1.00 38.86 ? 137  VAL C C   1 
ATOM   5844  O  O   . VAL C 1 137 ? -36.417 68.924  101.480 1.00 39.31 ? 137  VAL C O   1 
ATOM   5845  C  CB  . VAL C 1 137 ? -36.024 67.219  98.521  1.00 35.17 ? 137  VAL C CB  1 
ATOM   5846  C  CG1 . VAL C 1 137 ? -34.650 67.485  99.082  1.00 33.87 ? 137  VAL C CG1 1 
ATOM   5847  C  CG2 . VAL C 1 137 ? -36.119 65.748  98.131  1.00 34.52 ? 137  VAL C CG2 1 
ATOM   5848  N  N   . ARG C 1 138 ? -36.811 69.920  99.494  1.00 38.74 ? 138  ARG C N   1 
ATOM   5849  C  CA  . ARG C 1 138 ? -36.510 71.251  99.975  1.00 42.08 ? 138  ARG C CA  1 
ATOM   5850  C  C   . ARG C 1 138 ? -37.413 71.600  101.170 1.00 44.48 ? 138  ARG C C   1 
ATOM   5851  O  O   . ARG C 1 138 ? -36.982 72.235  102.132 1.00 42.92 ? 138  ARG C O   1 
ATOM   5852  C  CB  . ARG C 1 138 ? -36.700 72.237  98.817  1.00 39.06 ? 138  ARG C CB  1 
ATOM   5853  C  CG  . ARG C 1 138 ? -36.588 73.691  99.156  1.00 40.65 ? 138  ARG C CG  1 
ATOM   5854  C  CD  . ARG C 1 138 ? -35.873 74.431  98.022  1.00 46.53 ? 138  ARG C CD  1 
ATOM   5855  N  NE  . ARG C 1 138 ? -36.197 73.962  96.662  1.00 55.28 ? 138  ARG C NE  1 
ATOM   5856  C  CZ  . ARG C 1 138 ? -37.279 74.300  95.941  1.00 59.84 ? 138  ARG C CZ  1 
ATOM   5857  N  NH1 . ARG C 1 138 ? -38.221 75.134  96.422  1.00 58.59 ? 138  ARG C NH1 1 
ATOM   5858  N  NH2 . ARG C 1 138 ? -37.401 73.828  94.695  1.00 56.02 ? 138  ARG C NH2 1 
ATOM   5859  N  N   . PHE C 1 139 ? -38.670 71.173  101.115 1.00 46.37 ? 139  PHE C N   1 
ATOM   5860  C  CA  . PHE C 1 139 ? -39.605 71.449  102.200 1.00 45.75 ? 139  PHE C CA  1 
ATOM   5861  C  C   . PHE C 1 139 ? -39.193 70.669  103.439 1.00 48.32 ? 139  PHE C C   1 
ATOM   5862  O  O   . PHE C 1 139 ? -39.231 71.205  104.544 1.00 52.85 ? 139  PHE C O   1 
ATOM   5863  C  CB  . PHE C 1 139 ? -41.026 71.035  101.797 1.00 44.49 ? 139  PHE C CB  1 
ATOM   5864  C  CG  . PHE C 1 139 ? -42.053 71.207  102.892 1.00 41.35 ? 139  PHE C CG  1 
ATOM   5865  C  CD1 . PHE C 1 139 ? -42.562 72.464  103.193 1.00 44.01 ? 139  PHE C CD1 1 
ATOM   5866  C  CD2 . PHE C 1 139 ? -42.535 70.111  103.600 1.00 39.49 ? 139  PHE C CD2 1 
ATOM   5867  C  CE1 . PHE C 1 139 ? -43.543 72.626  104.181 1.00 39.95 ? 139  PHE C CE1 1 
ATOM   5868  C  CE2 . PHE C 1 139 ? -43.516 70.262  104.595 1.00 38.96 ? 139  PHE C CE2 1 
ATOM   5869  C  CZ  . PHE C 1 139 ? -44.020 71.517  104.880 1.00 40.01 ? 139  PHE C CZ  1 
ATOM   5870  N  N   . ALA C 1 140 ? -38.805 69.408  103.262 1.00 46.02 ? 140  ALA C N   1 
ATOM   5871  C  CA  . ALA C 1 140 ? -38.423 68.598  104.404 1.00 47.45 ? 140  ALA C CA  1 
ATOM   5872  C  C   . ALA C 1 140 ? -37.203 69.185  105.111 1.00 47.93 ? 140  ALA C C   1 
ATOM   5873  O  O   . ALA C 1 140 ? -37.142 69.220  106.349 1.00 43.29 ? 140  ALA C O   1 
ATOM   5874  C  CB  . ALA C 1 140 ? -38.138 67.157  103.965 1.00 48.26 ? 140  ALA C CB  1 
ATOM   5875  N  N   . LYS C 1 141 ? -36.234 69.652  104.326 1.00 47.16 ? 141  LYS C N   1 
ATOM   5876  C  CA  . LYS C 1 141 ? -35.028 70.210  104.919 1.00 44.43 ? 141  LYS C CA  1 
ATOM   5877  C  C   . LYS C 1 141 ? -35.355 71.511  105.626 1.00 43.01 ? 141  LYS C C   1 
ATOM   5878  O  O   . LYS C 1 141 ? -34.898 71.750  106.745 1.00 43.55 ? 141  LYS C O   1 
ATOM   5879  C  CB  . LYS C 1 141 ? -33.960 70.450  103.855 1.00 46.48 ? 141  LYS C CB  1 
ATOM   5880  C  CG  . LYS C 1 141 ? -33.371 69.176  103.238 1.00 48.67 ? 141  LYS C CG  1 
ATOM   5881  C  CD  . LYS C 1 141 ? -32.463 69.533  102.053 1.00 51.63 ? 141  LYS C CD  1 
ATOM   5882  C  CE  . LYS C 1 141 ? -31.722 68.321  101.532 1.00 55.18 ? 141  LYS C CE  1 
ATOM   5883  N  NZ  . LYS C 1 141 ? -31.062 68.608  100.229 1.00 57.57 ? 141  LYS C NZ  1 
ATOM   5884  N  N   . THR C 1 142 ? -36.165 72.351  104.992 1.00 42.02 ? 142  THR C N   1 
ATOM   5885  C  CA  . THR C 1 142 ? -36.520 73.631  105.587 1.00 38.87 ? 142  THR C CA  1 
ATOM   5886  C  C   . THR C 1 142 ? -37.256 73.467  106.883 1.00 39.61 ? 142  THR C C   1 
ATOM   5887  O  O   . THR C 1 142 ? -37.132 74.300  107.777 1.00 39.06 ? 142  THR C O   1 
ATOM   5888  C  CB  . THR C 1 142 ? -37.373 74.445  104.668 1.00 42.02 ? 142  THR C CB  1 
ATOM   5889  O  OG1 . THR C 1 142 ? -36.616 74.764  103.491 1.00 39.60 ? 142  THR C OG1 1 
ATOM   5890  C  CG2 . THR C 1 142 ? -37.812 75.741  105.374 1.00 44.92 ? 142  THR C CG2 1 
ATOM   5891  N  N   . LEU C 1 143 ? -38.025 72.387  106.981 1.00 42.27 ? 143  LEU C N   1 
ATOM   5892  C  CA  . LEU C 1 143 ? -38.768 72.061  108.202 1.00 43.00 ? 143  LEU C CA  1 
ATOM   5893  C  C   . LEU C 1 143 ? -37.800 71.478  109.252 1.00 44.72 ? 143  LEU C C   1 
ATOM   5894  O  O   . LEU C 1 143 ? -37.856 71.826  110.427 1.00 49.34 ? 143  LEU C O   1 
ATOM   5895  C  CB  . LEU C 1 143 ? -39.882 71.044  107.883 1.00 40.88 ? 143  LEU C CB  1 
ATOM   5896  C  CG  . LEU C 1 143 ? -41.071 70.926  108.866 1.00 38.20 ? 143  LEU C CG  1 
ATOM   5897  C  CD1 . LEU C 1 143 ? -41.751 72.258  108.926 1.00 36.09 ? 143  LEU C CD1 1 
ATOM   5898  C  CD2 . LEU C 1 143 ? -42.060 69.859  108.450 1.00 33.65 ? 143  LEU C CD2 1 
ATOM   5899  N  N   . LEU C 1 144 ? -36.916 70.584  108.833 1.00 46.68 ? 144  LEU C N   1 
ATOM   5900  C  CA  . LEU C 1 144 ? -35.974 70.009  109.773 1.00 47.54 ? 144  LEU C CA  1 
ATOM   5901  C  C   . LEU C 1 144 ? -35.185 71.163  110.435 1.00 48.39 ? 144  LEU C C   1 
ATOM   5902  O  O   . LEU C 1 144 ? -35.014 71.185  111.657 1.00 47.81 ? 144  LEU C O   1 
ATOM   5903  C  CB  . LEU C 1 144 ? -35.033 69.040  109.030 1.00 46.31 ? 144  LEU C CB  1 
ATOM   5904  C  CG  . LEU C 1 144 ? -34.127 68.141  109.867 1.00 45.72 ? 144  LEU C CG  1 
ATOM   5905  C  CD1 . LEU C 1 144 ? -34.999 67.336  110.812 1.00 41.93 ? 144  LEU C CD1 1 
ATOM   5906  C  CD2 . LEU C 1 144 ? -33.268 67.219  108.952 1.00 50.38 ? 144  LEU C CD2 1 
ATOM   5907  N  N   . ALA C 1 145 ? -34.763 72.138  109.624 1.00 48.40 ? 145  ALA C N   1 
ATOM   5908  C  CA  . ALA C 1 145 ? -33.948 73.261  110.080 1.00 45.32 ? 145  ALA C CA  1 
ATOM   5909  C  C   . ALA C 1 145 ? -34.638 74.254  111.038 1.00 47.21 ? 145  ALA C C   1 
ATOM   5910  O  O   . ALA C 1 145 ? -33.986 74.919  111.881 1.00 44.32 ? 145  ALA C O   1 
ATOM   5911  C  CB  . ALA C 1 145 ? -33.364 74.002  108.828 1.00 46.41 ? 145  ALA C CB  1 
ATOM   5912  N  N   . ASN C 1 146 ? -35.959 74.360  110.929 1.00 49.73 ? 146  ASN C N   1 
ATOM   5913  C  CA  . ASN C 1 146 ? -36.714 75.292  111.774 1.00 48.88 ? 146  ASN C CA  1 
ATOM   5914  C  C   . ASN C 1 146 ? -36.714 74.915  113.264 1.00 53.18 ? 146  ASN C C   1 
ATOM   5915  O  O   . ASN C 1 146 ? -36.870 73.731  113.622 1.00 55.23 ? 146  ASN C O   1 
ATOM   5916  C  CB  . ASN C 1 146 ? -38.145 75.376  111.291 1.00 46.72 ? 146  ASN C CB  1 
ATOM   5917  C  CG  . ASN C 1 146 ? -38.973 76.385  112.079 1.00 50.18 ? 146  ASN C CG  1 
ATOM   5918  O  OD1 . ASN C 1 146 ? -38.954 77.593  111.792 1.00 45.91 ? 146  ASN C OD1 1 
ATOM   5919  N  ND2 . ASN C 1 146 ? -39.705 75.897  113.092 1.00 48.04 ? 146  ASN C ND2 1 
ATOM   5920  N  N   . SER C 1 147 ? -36.571 75.927  114.128 1.00 54.53 ? 147  SER C N   1 
ATOM   5921  C  CA  . SER C 1 147 ? -36.528 75.713  115.578 1.00 54.20 ? 147  SER C CA  1 
ATOM   5922  C  C   . SER C 1 147 ? -37.739 76.239  116.347 1.00 53.97 ? 147  SER C C   1 
ATOM   5923  O  O   . SER C 1 147 ? -37.906 75.898  117.510 1.00 56.18 ? 147  SER C O   1 
ATOM   5924  C  CB  . SER C 1 147 ? -35.287 76.383  116.202 1.00 53.56 ? 147  SER C CB  1 
ATOM   5925  O  OG  . SER C 1 147 ? -34.083 76.101  115.513 1.00 64.48 ? 147  SER C OG  1 
ATOM   5926  N  N   . SER C 1 148 ? -38.569 77.082  115.736 1.00 52.50 ? 148  SER C N   1 
ATOM   5927  C  CA  . SER C 1 148 ? -39.728 77.662  116.443 1.00 48.84 ? 148  SER C CA  1 
ATOM   5928  C  C   . SER C 1 148 ? -40.550 76.693  117.283 1.00 46.84 ? 148  SER C C   1 
ATOM   5929  O  O   . SER C 1 148 ? -40.557 75.482  117.049 1.00 46.01 ? 148  SER C O   1 
ATOM   5930  C  CB  . SER C 1 148 ? -40.644 78.374  115.458 1.00 47.73 ? 148  SER C CB  1 
ATOM   5931  O  OG  . SER C 1 148 ? -39.891 79.290  114.682 1.00 53.09 ? 148  SER C OG  1 
ATOM   5932  N  N   . PRO C 1 149 ? -41.256 77.222  118.293 1.00 48.04 ? 149  PRO C N   1 
ATOM   5933  C  CA  . PRO C 1 149 ? -42.081 76.362  119.167 1.00 47.44 ? 149  PRO C CA  1 
ATOM   5934  C  C   . PRO C 1 149 ? -43.140 75.611  118.370 1.00 47.20 ? 149  PRO C C   1 
ATOM   5935  O  O   . PRO C 1 149 ? -43.888 76.210  117.584 1.00 46.68 ? 149  PRO C O   1 
ATOM   5936  C  CB  . PRO C 1 149 ? -42.674 77.346  120.183 1.00 44.76 ? 149  PRO C CB  1 
ATOM   5937  C  CG  . PRO C 1 149 ? -42.674 78.657  119.446 1.00 44.27 ? 149  PRO C CG  1 
ATOM   5938  C  CD  . PRO C 1 149 ? -41.376 78.647  118.667 1.00 43.44 ? 149  PRO C CD  1 
ATOM   5939  N  N   . PHE C 1 150 ? -43.191 74.302  118.595 1.00 45.56 ? 150  PHE C N   1 
ATOM   5940  C  CA  . PHE C 1 150 ? -44.086 73.407  117.883 1.00 47.21 ? 150  PHE C CA  1 
ATOM   5941  C  C   . PHE C 1 150 ? -45.572 73.741  117.843 1.00 49.31 ? 150  PHE C C   1 
ATOM   5942  O  O   . PHE C 1 150 ? -46.172 74.127  118.852 1.00 52.36 ? 150  PHE C O   1 
ATOM   5943  C  CB  . PHE C 1 150 ? -43.925 71.994  118.438 1.00 46.86 ? 150  PHE C CB  1 
ATOM   5944  C  CG  . PHE C 1 150 ? -44.521 70.927  117.563 1.00 48.14 ? 150  PHE C CG  1 
ATOM   5945  C  CD1 . PHE C 1 150 ? -44.066 70.743  116.256 1.00 44.85 ? 150  PHE C CD1 1 
ATOM   5946  C  CD2 . PHE C 1 150 ? -45.501 70.078  118.056 1.00 48.83 ? 150  PHE C CD2 1 
ATOM   5947  C  CE1 . PHE C 1 150 ? -44.569 69.742  115.473 1.00 44.25 ? 150  PHE C CE1 1 
ATOM   5948  C  CE2 . PHE C 1 150 ? -46.016 69.057  117.267 1.00 46.84 ? 150  PHE C CE2 1 
ATOM   5949  C  CZ  . PHE C 1 150 ? -45.543 68.892  115.971 1.00 46.81 ? 150  PHE C CZ  1 
ATOM   5950  N  N   . ASN C 1 151 ? -46.160 73.557  116.664 1.00 47.43 ? 151  ASN C N   1 
ATOM   5951  C  CA  . ASN C 1 151 ? -47.588 73.772  116.447 1.00 47.76 ? 151  ASN C CA  1 
ATOM   5952  C  C   . ASN C 1 151 ? -48.183 72.450  115.966 1.00 46.40 ? 151  ASN C C   1 
ATOM   5953  O  O   . ASN C 1 151 ? -47.851 71.985  114.886 1.00 46.48 ? 151  ASN C O   1 
ATOM   5954  C  CB  . ASN C 1 151 ? -47.819 74.832  115.386 1.00 52.03 ? 151  ASN C CB  1 
ATOM   5955  C  CG  . ASN C 1 151 ? -49.274 75.015  115.089 1.00 52.06 ? 151  ASN C CG  1 
ATOM   5956  O  OD1 . ASN C 1 151 ? -50.013 75.531  115.918 1.00 54.36 ? 151  ASN C OD1 1 
ATOM   5957  N  ND2 . ASN C 1 151 ? -49.706 74.573  113.914 1.00 50.64 ? 151  ASN C ND2 1 
ATOM   5958  N  N   . VAL C 1 152 ? -49.070 71.855  116.755 1.00 44.20 ? 152  VAL C N   1 
ATOM   5959  C  CA  . VAL C 1 152 ? -49.634 70.561  116.399 1.00 42.22 ? 152  VAL C CA  1 
ATOM   5960  C  C   . VAL C 1 152 ? -50.392 70.549  115.086 1.00 42.77 ? 152  VAL C C   1 
ATOM   5961  O  O   . VAL C 1 152 ? -50.213 69.636  114.273 1.00 40.24 ? 152  VAL C O   1 
ATOM   5962  C  CB  . VAL C 1 152 ? -50.542 70.029  117.515 1.00 39.67 ? 152  VAL C CB  1 
ATOM   5963  C  CG1 . VAL C 1 152 ? -51.064 68.664  117.135 1.00 36.27 ? 152  VAL C CG1 1 
ATOM   5964  C  CG2 . VAL C 1 152 ? -49.758 69.945  118.796 1.00 38.87 ? 152  VAL C CG2 1 
ATOM   5965  N  N   . ASP C 1 153 ? -51.238 71.558  114.880 1.00 43.76 ? 153  ASP C N   1 
ATOM   5966  C  CA  . ASP C 1 153 ? -52.013 71.662  113.640 1.00 45.95 ? 153  ASP C CA  1 
ATOM   5967  C  C   . ASP C 1 153 ? -51.038 71.566  112.452 1.00 45.19 ? 153  ASP C C   1 
ATOM   5968  O  O   . ASP C 1 153 ? -51.250 70.769  111.545 1.00 44.04 ? 153  ASP C O   1 
ATOM   5969  C  CB  . ASP C 1 153 ? -52.782 73.005  113.564 1.00 50.42 ? 153  ASP C CB  1 
ATOM   5970  C  CG  . ASP C 1 153 ? -53.520 73.359  114.873 1.00 58.05 ? 153  ASP C CG  1 
ATOM   5971  O  OD1 . ASP C 1 153 ? -52.838 73.479  115.929 1.00 64.05 ? 153  ASP C OD1 1 
ATOM   5972  O  OD2 . ASP C 1 153 ? -54.769 73.530  114.850 1.00 52.89 ? 153  ASP C OD2 1 
ATOM   5973  N  N   . THR C 1 154 ? -49.960 72.361  112.482 1.00 42.39 ? 154  THR C N   1 
ATOM   5974  C  CA  . THR C 1 154 ? -48.985 72.365  111.405 1.00 43.29 ? 154  THR C CA  1 
ATOM   5975  C  C   . THR C 1 154 ? -48.231 71.053  111.291 1.00 42.29 ? 154  THR C C   1 
ATOM   5976  O  O   . THR C 1 154 ? -47.972 70.563  110.185 1.00 41.97 ? 154  THR C O   1 
ATOM   5977  C  CB  . THR C 1 154 ? -47.946 73.488  111.563 1.00 44.89 ? 154  THR C CB  1 
ATOM   5978  O  OG1 . THR C 1 154 ? -48.612 74.752  111.606 1.00 47.69 ? 154  THR C OG1 1 
ATOM   5979  C  CG2 . THR C 1 154 ? -46.988 73.499  110.359 1.00 42.62 ? 154  THR C CG2 1 
ATOM   5980  N  N   . GLY C 1 155 ? -47.873 70.485  112.429 1.00 39.86 ? 155  GLY C N   1 
ATOM   5981  C  CA  . GLY C 1 155 ? -47.160 69.230  112.400 1.00 38.86 ? 155  GLY C CA  1 
ATOM   5982  C  C   . GLY C 1 155 ? -48.016 68.162  111.748 1.00 37.54 ? 155  GLY C C   1 
ATOM   5983  O  O   . GLY C 1 155 ? -47.526 67.360  110.952 1.00 34.86 ? 155  GLY C O   1 
ATOM   5984  N  N   . ALA C 1 156 ? -49.305 68.173  112.069 1.00 36.95 ? 156  ALA C N   1 
ATOM   5985  C  CA  . ALA C 1 156 ? -50.239 67.195  111.531 1.00 35.97 ? 156  ALA C CA  1 
ATOM   5986  C  C   . ALA C 1 156 ? -50.321 67.324  109.999 1.00 37.34 ? 156  ALA C C   1 
ATOM   5987  O  O   . ALA C 1 156 ? -50.237 66.339  109.254 1.00 35.56 ? 156  ALA C O   1 
ATOM   5988  C  CB  . ALA C 1 156 ? -51.582 67.406  112.167 1.00 35.67 ? 156  ALA C CB  1 
ATOM   5989  N  N   . MET C 1 157 ? -50.470 68.547  109.519 1.00 36.79 ? 157  MET C N   1 
ATOM   5990  C  CA  . MET C 1 157 ? -50.523 68.747  108.087 1.00 37.75 ? 157  MET C CA  1 
ATOM   5991  C  C   . MET C 1 157 ? -49.214 68.326  107.470 1.00 38.98 ? 157  MET C C   1 
ATOM   5992  O  O   . MET C 1 157 ? -49.202 67.695  106.423 1.00 42.00 ? 157  MET C O   1 
ATOM   5993  C  CB  . MET C 1 157 ? -50.771 70.204  107.741 1.00 39.67 ? 157  MET C CB  1 
ATOM   5994  C  CG  . MET C 1 157 ? -52.176 70.635  108.028 1.00 46.72 ? 157  MET C CG  1 
ATOM   5995  S  SD  . MET C 1 157 ? -53.332 69.551  107.205 1.00 49.21 ? 157  MET C SD  1 
ATOM   5996  C  CE  . MET C 1 157 ? -54.842 70.528  107.459 1.00 43.30 ? 157  MET C CE  1 
ATOM   5997  N  N   . ALA C 1 158 ? -48.105 68.678  108.108 1.00 37.36 ? 158  ALA C N   1 
ATOM   5998  C  CA  . ALA C 1 158 ? -46.808 68.320  107.568 1.00 35.26 ? 158  ALA C CA  1 
ATOM   5999  C  C   . ALA C 1 158 ? -46.567 66.809  107.522 1.00 36.36 ? 158  ALA C C   1 
ATOM   6000  O  O   . ALA C 1 158 ? -45.903 66.323  106.602 1.00 36.30 ? 158  ALA C O   1 
ATOM   6001  C  CB  . ALA C 1 158 ? -45.730 68.980  108.362 1.00 38.32 ? 158  ALA C CB  1 
ATOM   6002  N  N   . THR C 1 159 ? -47.093 66.045  108.482 1.00 33.70 ? 159  THR C N   1 
ATOM   6003  C  CA  . THR C 1 159 ? -46.832 64.616  108.402 1.00 35.34 ? 159  THR C CA  1 
ATOM   6004  C  C   . THR C 1 159 ? -47.645 63.963  107.270 1.00 37.29 ? 159  THR C C   1 
ATOM   6005  O  O   . THR C 1 159 ? -47.162 63.043  106.599 1.00 39.31 ? 159  THR C O   1 
ATOM   6006  C  CB  . THR C 1 159 ? -46.987 63.910  109.819 1.00 33.78 ? 159  THR C CB  1 
ATOM   6007  O  OG1 . THR C 1 159 ? -47.970 62.863  109.798 1.00 35.73 ? 159  THR C OG1 1 
ATOM   6008  C  CG2 . THR C 1 159 ? -47.340 64.922  110.862 1.00 32.49 ? 159  THR C CG2 1 
ATOM   6009  N  N   . LEU C 1 160 ? -48.852 64.473  107.019 1.00 38.34 ? 160  LEU C N   1 
ATOM   6010  C  CA  . LEU C 1 160 ? -49.681 63.954  105.930 1.00 37.89 ? 160  LEU C CA  1 
ATOM   6011  C  C   . LEU C 1 160 ? -48.953 64.161  104.594 1.00 38.84 ? 160  LEU C C   1 
ATOM   6012  O  O   . LEU C 1 160 ? -48.826 63.236  103.766 1.00 37.31 ? 160  LEU C O   1 
ATOM   6013  C  CB  . LEU C 1 160 ? -51.014 64.691  105.864 1.00 36.56 ? 160  LEU C CB  1 
ATOM   6014  C  CG  . LEU C 1 160 ? -52.022 64.404  106.973 1.00 40.01 ? 160  LEU C CG  1 
ATOM   6015  C  CD1 . LEU C 1 160 ? -53.279 65.315  106.812 1.00 34.55 ? 160  LEU C CD1 1 
ATOM   6016  C  CD2 . LEU C 1 160 ? -52.369 62.914  106.927 1.00 34.90 ? 160  LEU C CD2 1 
ATOM   6017  N  N   . ALA C 1 161 ? -48.480 65.384  104.392 1.00 37.46 ? 161  ALA C N   1 
ATOM   6018  C  CA  . ALA C 1 161 ? -47.794 65.709  103.167 1.00 38.41 ? 161  ALA C CA  1 
ATOM   6019  C  C   . ALA C 1 161 ? -46.559 64.842  103.026 1.00 38.02 ? 161  ALA C C   1 
ATOM   6020  O  O   . ALA C 1 161 ? -46.341 64.227  101.971 1.00 35.98 ? 161  ALA C O   1 
ATOM   6021  C  CB  . ALA C 1 161 ? -47.421 67.173  103.146 1.00 38.86 ? 161  ALA C CB  1 
ATOM   6022  N  N   . LEU C 1 162 ? -45.771 64.748  104.094 1.00 36.32 ? 162  LEU C N   1 
ATOM   6023  C  CA  . LEU C 1 162 ? -44.559 63.956  103.998 1.00 35.92 ? 162  LEU C CA  1 
ATOM   6024  C  C   . LEU C 1 162 ? -44.841 62.483  103.846 1.00 35.75 ? 162  LEU C C   1 
ATOM   6025  O  O   . LEU C 1 162 ? -44.105 61.786  103.130 1.00 32.44 ? 162  LEU C O   1 
ATOM   6026  C  CB  . LEU C 1 162 ? -43.623 64.222  105.178 1.00 36.14 ? 162  LEU C CB  1 
ATOM   6027  C  CG  . LEU C 1 162 ? -42.454 65.189  104.881 1.00 37.96 ? 162  LEU C CG  1 
ATOM   6028  C  CD1 . LEU C 1 162 ? -42.592 65.919  103.539 1.00 35.27 ? 162  LEU C CD1 1 
ATOM   6029  C  CD2 . LEU C 1 162 ? -42.389 66.187  106.000 1.00 35.46 ? 162  LEU C CD2 1 
ATOM   6030  N  N   . THR C 1 163 ? -45.913 62.005  104.481 1.00 33.44 ? 163  THR C N   1 
ATOM   6031  C  CA  . THR C 1 163 ? -46.260 60.590  104.353 1.00 34.66 ? 163  THR C CA  1 
ATOM   6032  C  C   . THR C 1 163 ? -46.737 60.287  102.929 1.00 36.97 ? 163  THR C C   1 
ATOM   6033  O  O   . THR C 1 163 ? -46.582 59.185  102.417 1.00 33.88 ? 163  THR C O   1 
ATOM   6034  C  CB  . THR C 1 163 ? -47.376 60.189  105.283 1.00 35.76 ? 163  THR C CB  1 
ATOM   6035  O  OG1 . THR C 1 163 ? -46.971 60.390  106.641 1.00 34.30 ? 163  THR C OG1 1 
ATOM   6036  C  CG2 . THR C 1 163 ? -47.724 58.717  105.051 1.00 31.50 ? 163  THR C CG2 1 
ATOM   6037  N  N   . CYS C 1 164 ? -47.346 61.274  102.292 1.00 39.45 ? 164  CYS C N   1 
ATOM   6038  C  CA  . CYS C 1 164 ? -47.791 61.060  100.943 1.00 39.89 ? 164  CYS C CA  1 
ATOM   6039  C  C   . CYS C 1 164 ? -46.536 60.790  100.119 1.00 40.86 ? 164  CYS C C   1 
ATOM   6040  O  O   . CYS C 1 164 ? -46.465 59.776  99.441  1.00 41.44 ? 164  CYS C O   1 
ATOM   6041  C  CB  . CYS C 1 164 ? -48.550 62.291  100.413 1.00 41.91 ? 164  CYS C CB  1 
ATOM   6042  S  SG  . CYS C 1 164 ? -49.045 62.163  98.653  1.00 45.32 ? 164  CYS C SG  1 
ATOM   6043  N  N   . MET C 1 165 ? -45.547 61.687  100.200 1.00 40.18 ? 165  MET C N   1 
ATOM   6044  C  CA  . MET C 1 165 ? -44.296 61.552  99.439  1.00 40.82 ? 165  MET C CA  1 
ATOM   6045  C  C   . MET C 1 165 ? -43.525 60.287  99.798  1.00 41.72 ? 165  MET C C   1 
ATOM   6046  O  O   . MET C 1 165 ? -42.991 59.587  98.939  1.00 38.56 ? 165  MET C O   1 
ATOM   6047  C  CB  . MET C 1 165 ? -43.401 62.747  99.704  1.00 40.62 ? 165  MET C CB  1 
ATOM   6048  C  CG  . MET C 1 165 ? -43.987 64.046  99.240  1.00 44.03 ? 165  MET C CG  1 
ATOM   6049  S  SD  . MET C 1 165 ? -44.202 64.094  97.487  1.00 46.97 ? 165  MET C SD  1 
ATOM   6050  C  CE  . MET C 1 165 ? -42.738 63.226  96.923  1.00 49.26 ? 165  MET C CE  1 
ATOM   6051  N  N   . TYR C 1 166 ? -43.470 60.023  101.095 1.00 42.10 ? 166  TYR C N   1 
ATOM   6052  C  CA  . TYR C 1 166 ? -42.782 58.868  101.621 1.00 40.56 ? 166  TYR C CA  1 
ATOM   6053  C  C   . TYR C 1 166 ? -43.246 57.598  100.954 1.00 40.09 ? 166  TYR C C   1 
ATOM   6054  O  O   . TYR C 1 166 ? -42.454 56.689  100.734 1.00 41.82 ? 166  TYR C O   1 
ATOM   6055  C  CB  . TYR C 1 166 ? -43.043 58.757  103.107 1.00 38.55 ? 166  TYR C CB  1 
ATOM   6056  C  CG  . TYR C 1 166 ? -42.390 57.564  103.749 1.00 43.13 ? 166  TYR C CG  1 
ATOM   6057  C  CD1 . TYR C 1 166 ? -41.052 57.623  104.195 1.00 43.64 ? 166  TYR C CD1 1 
ATOM   6058  C  CD2 . TYR C 1 166 ? -43.117 56.400  103.978 1.00 36.54 ? 166  TYR C CD2 1 
ATOM   6059  C  CE1 . TYR C 1 166 ? -40.465 56.545  104.877 1.00 45.36 ? 166  TYR C CE1 1 
ATOM   6060  C  CE2 . TYR C 1 166 ? -42.550 55.326  104.646 1.00 43.76 ? 166  TYR C CE2 1 
ATOM   6061  C  CZ  . TYR C 1 166 ? -41.224 55.392  105.111 1.00 47.83 ? 166  TYR C CZ  1 
ATOM   6062  O  OH  . TYR C 1 166 ? -40.704 54.343  105.870 1.00 39.59 ? 166  TYR C OH  1 
ATOM   6063  N  N   . ASN C 1 167 ? -44.530 57.522  100.627 1.00 41.44 ? 167  ASN C N   1 
ATOM   6064  C  CA  . ASN C 1 167 ? -45.049 56.308  100.015 1.00 41.95 ? 167  ASN C CA  1 
ATOM   6065  C  C   . ASN C 1 167 ? -45.010 56.255  98.514  1.00 43.33 ? 167  ASN C C   1 
ATOM   6066  O  O   . ASN C 1 167 ? -45.412 55.248  97.937  1.00 45.71 ? 167  ASN C O   1 
ATOM   6067  C  CB  . ASN C 1 167 ? -46.475 56.045  100.449 1.00 43.99 ? 167  ASN C CB  1 
ATOM   6068  C  CG  . ASN C 1 167 ? -46.584 55.681  101.919 1.00 46.28 ? 167  ASN C CG  1 
ATOM   6069  O  OD1 . ASN C 1 167 ? -45.906 54.771  102.410 1.00 42.60 ? 167  ASN C OD1 1 
ATOM   6070  N  ND2 . ASN C 1 167 ? -47.455 56.392  102.630 1.00 43.73 ? 167  ASN C ND2 1 
ATOM   6071  N  N   . LYS C 1 168 ? -44.531 57.317  97.875  1.00 42.02 ? 168  LYS C N   1 
ATOM   6072  C  CA  . LYS C 1 168 ? -44.459 57.325  96.426  1.00 40.35 ? 168  LYS C CA  1 
ATOM   6073  C  C   . LYS C 1 168 ? -43.069 57.596  95.918  1.00 43.26 ? 168  LYS C C   1 
ATOM   6074  O  O   . LYS C 1 168 ? -42.894 58.369  94.961  1.00 44.59 ? 168  LYS C O   1 
ATOM   6075  C  CB  . LYS C 1 168 ? -45.401 58.367  95.847  1.00 41.42 ? 168  LYS C CB  1 
ATOM   6076  C  CG  . LYS C 1 168 ? -46.855 58.147  96.171  1.00 39.81 ? 168  LYS C CG  1 
ATOM   6077  C  CD  . LYS C 1 168 ? -47.387 56.939  95.483  1.00 41.75 ? 168  LYS C CD  1 
ATOM   6078  C  CE  . LYS C 1 168 ? -48.870 56.819  95.736  1.00 46.94 ? 168  LYS C CE  1 
ATOM   6079  N  NZ  . LYS C 1 168 ? -49.493 55.648  95.047  1.00 51.01 ? 168  LYS C NZ  1 
ATOM   6080  N  N   . ILE C 1 169 ? -42.076 56.976  96.562  1.00 46.39 ? 169  ILE C N   1 
ATOM   6081  C  CA  . ILE C 1 169 ? -40.683 57.114  96.126  1.00 46.54 ? 169  ILE C CA  1 
ATOM   6082  C  C   . ILE C 1 169 ? -40.528 56.352  94.800  1.00 45.04 ? 169  ILE C C   1 
ATOM   6083  O  O   . ILE C 1 169 ? -40.662 55.117  94.741  1.00 45.72 ? 169  ILE C O   1 
ATOM   6084  C  CB  . ILE C 1 169 ? -39.682 56.505  97.148  1.00 47.81 ? 169  ILE C CB  1 
ATOM   6085  C  CG1 . ILE C 1 169 ? -39.785 57.233  98.504  1.00 49.89 ? 169  ILE C CG1 1 
ATOM   6086  C  CG2 . ILE C 1 169 ? -38.278 56.553  96.566  1.00 45.25 ? 169  ILE C CG2 1 
ATOM   6087  C  CD1 . ILE C 1 169 ? -39.583 58.739  98.431  1.00 48.96 ? 169  ILE C CD1 1 
ATOM   6088  N  N   . PRO C 1 170 ? -40.258 57.080  93.723  1.00 40.68 ? 170  PRO C N   1 
ATOM   6089  C  CA  . PRO C 1 170 ? -40.084 56.467  92.410  1.00 42.53 ? 170  PRO C CA  1 
ATOM   6090  C  C   . PRO C 1 170 ? -39.084 55.299  92.443  1.00 44.15 ? 170  PRO C C   1 
ATOM   6091  O  O   . PRO C 1 170 ? -37.985 55.421  92.991  1.00 46.33 ? 170  PRO C O   1 
ATOM   6092  C  CB  . PRO C 1 170 ? -39.571 57.622  91.546  1.00 42.64 ? 170  PRO C CB  1 
ATOM   6093  C  CG  . PRO C 1 170 ? -40.120 58.857  92.234  1.00 44.76 ? 170  PRO C CG  1 
ATOM   6094  C  CD  . PRO C 1 170 ? -39.967 58.520  93.697  1.00 43.44 ? 170  PRO C CD  1 
ATOM   6095  N  N   . VAL C 1 171 ? -39.487 54.173  91.858  1.00 46.36 ? 171  VAL C N   1 
ATOM   6096  C  CA  . VAL C 1 171 ? -38.648 52.976  91.729  1.00 47.22 ? 171  VAL C CA  1 
ATOM   6097  C  C   . VAL C 1 171 ? -37.403 53.347  90.934  1.00 50.18 ? 171  VAL C C   1 
ATOM   6098  O  O   . VAL C 1 171 ? -37.505 53.980  89.877  1.00 50.61 ? 171  VAL C O   1 
ATOM   6099  C  CB  . VAL C 1 171 ? -39.391 51.888  90.934  1.00 47.08 ? 171  VAL C CB  1 
ATOM   6100  C  CG1 . VAL C 1 171 ? -38.420 50.814  90.428  1.00 47.26 ? 171  VAL C CG1 1 
ATOM   6101  C  CG2 . VAL C 1 171 ? -40.459 51.280  91.793  1.00 44.23 ? 171  VAL C CG2 1 
ATOM   6102  N  N   . GLY C 1 172 ? -36.237 52.950  91.431  1.00 54.03 ? 172  GLY C N   1 
ATOM   6103  C  CA  . GLY C 1 172 ? -34.998 53.252  90.732  1.00 63.59 ? 172  GLY C CA  1 
ATOM   6104  C  C   . GLY C 1 172 ? -34.362 54.531  91.245  1.00 68.92 ? 172  GLY C C   1 
ATOM   6105  O  O   . GLY C 1 172 ? -33.138 54.616  91.410  1.00 71.51 ? 172  GLY C O   1 
ATOM   6106  N  N   . SER C 1 173 ? -35.196 55.545  91.452  1.00 73.63 ? 173  SER C N   1 
ATOM   6107  C  CA  . SER C 1 173 ? -34.753 56.834  91.983  1.00 80.13 ? 173  SER C CA  1 
ATOM   6108  C  C   . SER C 1 173 ? -34.588 56.541  93.457  1.00 80.04 ? 173  SER C C   1 
ATOM   6109  O  O   . SER C 1 173 ? -35.453 56.877  94.267  1.00 80.45 ? 173  SER C O   1 
ATOM   6110  C  CB  . SER C 1 173 ? -35.843 57.897  91.756  1.00 84.07 ? 173  SER C CB  1 
ATOM   6111  O  OG  . SER C 1 173 ? -35.455 59.194  92.187  1.00 86.01 ? 173  SER C OG  1 
ATOM   6112  N  N   . GLU C 1 174 ? -33.470 55.928  93.818  1.00 80.61 ? 174  GLU C N   1 
ATOM   6113  C  CA  . GLU C 1 174 ? -33.267 55.521  95.217  1.00 85.43 ? 174  GLU C CA  1 
ATOM   6114  C  C   . GLU C 1 174 ? -32.324 56.380  96.139  1.00 86.46 ? 174  GLU C C   1 
ATOM   6115  O  O   . GLU C 1 174 ? -31.631 55.874  97.022  1.00 84.23 ? 174  GLU C O   1 
ATOM   6116  C  CB  . GLU C 1 174 ? -32.757 54.065  95.191  1.00 89.29 ? 174  GLU C CB  1 
ATOM   6117  C  CG  . GLU C 1 174 ? -33.503 53.170  94.132  1.00 94.91 ? 174  GLU C CG  1 
ATOM   6118  C  CD  . GLU C 1 174 ? -34.943 52.813  94.534  1.00 98.62 ? 174  GLU C CD  1 
ATOM   6119  O  OE1 . GLU C 1 174 ? -35.893 53.046  93.742  1.00 99.45 ? 174  GLU C OE1 1 
ATOM   6120  O  OE2 . GLU C 1 174 ? -35.126 52.296  95.656  1.00 99.45 ? 174  GLU C OE2 1 
ATOM   6121  N  N   . GLU C 1 175 ? -32.325 57.685  96.046  1.00 86.78 ? 175  GLU C N   1 
ATOM   6122  C  CA  . GLU C 1 175 ? -31.359 58.426  96.860  1.00 88.28 ? 175  GLU C CA  1 
ATOM   6123  C  C   . GLU C 1 175 ? -31.668 58.912  98.278  1.00 84.29 ? 175  GLU C C   1 
ATOM   6124  O  O   . GLU C 1 175 ? -31.721 60.095  98.413  1.00 86.88 ? 175  GLU C O   1 
ATOM   6125  C  CB  . GLU C 1 175 ? -30.926 59.758  96.193  1.00 92.59 ? 175  GLU C CB  1 
ATOM   6126  C  CG  . GLU C 1 175 ? -30.727 59.941  94.789  1.00 97.88 ? 175  GLU C CG  1 
ATOM   6127  C  CD  . GLU C 1 175 ? -31.987 60.531  94.201  1.00 99.44 ? 175  GLU C CD  1 
ATOM   6128  O  OE1 . GLU C 1 175 ? -33.022 59.976  94.678  1.00 99.44 ? 175  GLU C OE1 1 
ATOM   6129  O  OE2 . GLU C 1 175 ? -31.966 61.458  93.279  1.00 99.44 ? 175  GLU C OE2 1 
ATOM   6130  N  N   . GLY C 1 176 ? -31.887 58.165  99.357  1.00 77.28 ? 176  GLY C N   1 
ATOM   6131  C  CA  . GLY C 1 176 ? -32.119 58.872  100.653 1.00 70.43 ? 176  GLY C CA  1 
ATOM   6132  C  C   . GLY C 1 176 ? -33.341 59.799  100.778 1.00 66.31 ? 176  GLY C C   1 
ATOM   6133  O  O   . GLY C 1 176 ? -33.560 60.410  101.842 1.00 65.87 ? 176  GLY C O   1 
ATOM   6134  N  N   . TYR C 1 177 ? -34.138 59.919  99.708  1.00 60.02 ? 177  TYR C N   1 
ATOM   6135  C  CA  . TYR C 1 177 ? -35.380 60.734  99.764  1.00 53.22 ? 177  TYR C CA  1 
ATOM   6136  C  C   . TYR C 1 177 ? -36.217 60.119  100.853 1.00 50.10 ? 177  TYR C C   1 
ATOM   6137  O  O   . TYR C 1 177 ? -36.787 60.820  101.685 1.00 49.36 ? 177  TYR C O   1 
ATOM   6138  C  CB  . TYR C 1 177 ? -36.216 60.583  98.504  1.00 53.17 ? 177  TYR C CB  1 
ATOM   6139  C  CG  . TYR C 1 177 ? -35.722 61.350  97.329  1.00 56.16 ? 177  TYR C CG  1 
ATOM   6140  C  CD1 . TYR C 1 177 ? -34.459 61.099  96.796  1.00 59.85 ? 177  TYR C CD1 1 
ATOM   6141  C  CD2 . TYR C 1 177 ? -36.553 62.290  96.700  1.00 58.59 ? 177  TYR C CD2 1 
ATOM   6142  C  CE1 . TYR C 1 177 ? -34.045 61.759  95.664  1.00 62.60 ? 177  TYR C CE1 1 
ATOM   6143  C  CE2 . TYR C 1 177 ? -36.152 62.961  95.557  1.00 60.35 ? 177  TYR C CE2 1 
ATOM   6144  C  CZ  . TYR C 1 177 ? -34.891 62.680  95.044  1.00 62.16 ? 177  TYR C CZ  1 
ATOM   6145  O  OH  . TYR C 1 177 ? -34.475 63.296  93.901  1.00 66.11 ? 177  TYR C OH  1 
ATOM   6146  N  N   . ARG C 1 178 ? -36.292 58.793  100.818 1.00 45.23 ? 178  ARG C N   1 
ATOM   6147  C  CA  . ARG C 1 178 ? -37.072 58.069  101.794 1.00 47.37 ? 178  ARG C CA  1 
ATOM   6148  C  C   . ARG C 1 178 ? -36.505 58.337  103.171 1.00 47.43 ? 178  ARG C C   1 
ATOM   6149  O  O   . ARG C 1 178 ? -37.246 58.556  104.149 1.00 46.55 ? 178  ARG C O   1 
ATOM   6150  C  CB  . ARG C 1 178 ? -37.030 56.580  101.477 1.00 51.56 ? 178  ARG C CB  1 
ATOM   6151  C  CG  . ARG C 1 178 ? -37.925 55.707  102.340 1.00 59.74 ? 178  ARG C CG  1 
ATOM   6152  C  CD  . ARG C 1 178 ? -37.792 54.237  101.933 1.00 64.91 ? 178  ARG C CD  1 
ATOM   6153  N  NE  . ARG C 1 178 ? -38.393 53.320  102.900 1.00 67.83 ? 178  ARG C NE  1 
ATOM   6154  C  CZ  . ARG C 1 178 ? -39.700 53.170  103.081 1.00 70.27 ? 178  ARG C CZ  1 
ATOM   6155  N  NH1 . ARG C 1 178 ? -40.564 53.881  102.358 1.00 72.53 ? 178  ARG C NH1 1 
ATOM   6156  N  NH2 . ARG C 1 178 ? -40.140 52.297  103.982 1.00 70.29 ? 178  ARG C NH2 1 
ATOM   6157  N  N   . SER C 1 179 ? -35.178 58.346  103.228 1.00 46.97 ? 179  SER C N   1 
ATOM   6158  C  CA  . SER C 1 179 ? -34.467 58.572  104.471 1.00 47.05 ? 179  SER C CA  1 
ATOM   6159  C  C   . SER C 1 179 ? -34.842 59.936  105.023 1.00 45.31 ? 179  SER C C   1 
ATOM   6160  O  O   . SER C 1 179 ? -35.285 60.053  106.173 1.00 45.70 ? 179  SER C O   1 
ATOM   6161  C  CB  . SER C 1 179 ? -32.956 58.479  104.226 1.00 53.23 ? 179  SER C CB  1 
ATOM   6162  O  OG  . SER C 1 179 ? -32.229 58.997  105.333 1.00 62.33 ? 179  SER C OG  1 
ATOM   6163  N  N   . LEU C 1 180 ? -34.679 60.961  104.192 1.00 41.87 ? 180  LEU C N   1 
ATOM   6164  C  CA  . LEU C 1 180 ? -34.999 62.333  104.568 1.00 40.81 ? 180  LEU C CA  1 
ATOM   6165  C  C   . LEU C 1 180 ? -36.427 62.442  105.103 1.00 41.32 ? 180  LEU C C   1 
ATOM   6166  O  O   . LEU C 1 180 ? -36.660 62.874  106.235 1.00 42.04 ? 180  LEU C O   1 
ATOM   6167  C  CB  . LEU C 1 180 ? -34.863 63.225  103.345 1.00 39.82 ? 180  LEU C CB  1 
ATOM   6168  C  CG  . LEU C 1 180 ? -34.365 64.656  103.480 1.00 40.90 ? 180  LEU C CG  1 
ATOM   6169  C  CD1 . LEU C 1 180 ? -34.989 65.483  102.329 1.00 43.12 ? 180  LEU C CD1 1 
ATOM   6170  C  CD2 . LEU C 1 180 ? -34.722 65.235  104.813 1.00 37.25 ? 180  LEU C CD2 1 
ATOM   6171  N  N   . PHE C 1 181 ? -37.390 62.046  104.279 1.00 40.04 ? 181  PHE C N   1 
ATOM   6172  C  CA  . PHE C 1 181 ? -38.782 62.133  104.691 1.00 40.67 ? 181  PHE C CA  1 
ATOM   6173  C  C   . PHE C 1 181 ? -39.064 61.305  105.945 1.00 42.29 ? 181  PHE C C   1 
ATOM   6174  O  O   . PHE C 1 181 ? -39.707 61.784  106.897 1.00 45.43 ? 181  PHE C O   1 
ATOM   6175  C  CB  . PHE C 1 181 ? -39.714 61.684  103.565 1.00 36.79 ? 181  PHE C CB  1 
ATOM   6176  C  CG  . PHE C 1 181 ? -39.512 62.414  102.266 1.00 33.28 ? 181  PHE C CG  1 
ATOM   6177  C  CD1 . PHE C 1 181 ? -39.205 63.772  102.244 1.00 33.06 ? 181  PHE C CD1 1 
ATOM   6178  C  CD2 . PHE C 1 181 ? -39.700 61.753  101.063 1.00 30.21 ? 181  PHE C CD2 1 
ATOM   6179  C  CE1 . PHE C 1 181 ? -39.090 64.473  101.034 1.00 32.88 ? 181  PHE C CE1 1 
ATOM   6180  C  CE2 . PHE C 1 181 ? -39.593 62.428  99.856  1.00 32.96 ? 181  PHE C CE2 1 
ATOM   6181  C  CZ  . PHE C 1 181 ? -39.287 63.796  99.837  1.00 33.69 ? 181  PHE C CZ  1 
ATOM   6182  N  N   . GLY C 1 182 ? -38.601 60.065  105.969 1.00 38.10 ? 182  GLY C N   1 
ATOM   6183  C  CA  . GLY C 1 182 ? -38.872 59.289  107.161 1.00 39.01 ? 182  GLY C CA  1 
ATOM   6184  C  C   . GLY C 1 182 ? -38.333 59.945  108.427 1.00 39.78 ? 182  GLY C C   1 
ATOM   6185  O  O   . GLY C 1 182 ? -38.995 60.004  109.484 1.00 38.17 ? 182  GLY C O   1 
ATOM   6186  N  N   . GLN C 1 183 ? -37.120 60.471  108.313 1.00 38.83 ? 183  GLN C N   1 
ATOM   6187  C  CA  . GLN C 1 183 ? -36.483 61.088  109.447 1.00 39.23 ? 183  GLN C CA  1 
ATOM   6188  C  C   . GLN C 1 183 ? -37.277 62.307  109.931 1.00 38.71 ? 183  GLN C C   1 
ATOM   6189  O  O   . GLN C 1 183 ? -37.594 62.414  111.112 1.00 40.08 ? 183  GLN C O   1 
ATOM   6190  C  CB  . GLN C 1 183 ? -35.035 61.411  109.071 1.00 42.75 ? 183  GLN C CB  1 
ATOM   6191  C  CG  . GLN C 1 183 ? -34.132 61.675  110.257 1.00 50.75 ? 183  GLN C CG  1 
ATOM   6192  C  CD  . GLN C 1 183 ? -34.314 60.655  111.376 1.00 54.40 ? 183  GLN C CD  1 
ATOM   6193  O  OE1 . GLN C 1 183 ? -34.062 59.440  111.189 1.00 49.74 ? 183  GLN C OE1 1 
ATOM   6194  N  NE2 . GLN C 1 183 ? -34.764 61.143  112.553 1.00 50.29 ? 183  GLN C NE2 1 
ATOM   6195  N  N   . VAL C 1 184 ? -37.639 63.198  109.016 1.00 38.35 ? 184  VAL C N   1 
ATOM   6196  C  CA  . VAL C 1 184 ? -38.425 64.368  109.380 1.00 37.56 ? 184  VAL C CA  1 
ATOM   6197  C  C   . VAL C 1 184 ? -39.782 63.958  109.935 1.00 37.80 ? 184  VAL C C   1 
ATOM   6198  O  O   . VAL C 1 184 ? -40.344 64.663  110.780 1.00 37.74 ? 184  VAL C O   1 
ATOM   6199  C  CB  . VAL C 1 184 ? -38.641 65.285  108.170 1.00 39.69 ? 184  VAL C CB  1 
ATOM   6200  C  CG1 . VAL C 1 184 ? -39.547 66.448  108.546 1.00 35.04 ? 184  VAL C CG1 1 
ATOM   6201  C  CG2 . VAL C 1 184 ? -37.302 65.781  107.679 1.00 36.89 ? 184  VAL C CG2 1 
ATOM   6202  N  N   . LEU C 1 185 ? -40.314 62.830  109.465 1.00 36.25 ? 185  LEU C N   1 
ATOM   6203  C  CA  . LEU C 1 185 ? -41.595 62.336  109.982 1.00 38.73 ? 185  LEU C CA  1 
ATOM   6204  C  C   . LEU C 1 185 ? -41.444 61.807  111.401 1.00 40.28 ? 185  LEU C C   1 
ATOM   6205  O  O   . LEU C 1 185 ? -42.291 62.035  112.254 1.00 38.51 ? 185  LEU C O   1 
ATOM   6206  C  CB  . LEU C 1 185 ? -42.149 61.210  109.111 1.00 40.09 ? 185  LEU C CB  1 
ATOM   6207  C  CG  . LEU C 1 185 ? -42.814 61.588  107.788 1.00 41.18 ? 185  LEU C CG  1 
ATOM   6208  C  CD1 . LEU C 1 185 ? -42.710 60.414  106.795 1.00 36.17 ? 185  LEU C CD1 1 
ATOM   6209  C  CD2 . LEU C 1 185 ? -44.264 62.002  108.058 1.00 38.39 ? 185  LEU C CD2 1 
ATOM   6210  N  N   . LYS C 1 186 ? -40.356 61.094  111.654 1.00 45.31 ? 186  LYS C N   1 
ATOM   6211  C  CA  . LYS C 1 186 ? -40.117 60.539  112.981 1.00 49.79 ? 186  LYS C CA  1 
ATOM   6212  C  C   . LYS C 1 186 ? -40.047 61.694  113.993 1.00 48.89 ? 186  LYS C C   1 
ATOM   6213  O  O   . LYS C 1 186 ? -40.582 61.628  115.118 1.00 48.07 ? 186  LYS C O   1 
ATOM   6214  C  CB  . LYS C 1 186 ? -38.794 59.774  112.961 1.00 54.65 ? 186  LYS C CB  1 
ATOM   6215  C  CG  . LYS C 1 186 ? -38.808 58.505  113.779 1.00 63.92 ? 186  LYS C CG  1 
ATOM   6216  C  CD  . LYS C 1 186 ? -39.246 58.792  115.214 1.00 72.09 ? 186  LYS C CD  1 
ATOM   6217  C  CE  . LYS C 1 186 ? -39.272 57.522  116.046 1.00 76.09 ? 186  LYS C CE  1 
ATOM   6218  N  NZ  . LYS C 1 186 ? -39.352 57.827  117.500 1.00 79.41 ? 186  LYS C NZ  1 
ATOM   6219  N  N   . ASP C 1 187 ? -39.375 62.746  113.532 1.00 46.50 ? 187  ASP C N   1 
ATOM   6220  C  CA  . ASP C 1 187 ? -39.132 63.981  114.244 1.00 45.79 ? 187  ASP C CA  1 
ATOM   6221  C  C   . ASP C 1 187 ? -40.428 64.631  114.683 1.00 48.63 ? 187  ASP C C   1 
ATOM   6222  O  O   . ASP C 1 187 ? -40.628 64.950  115.862 1.00 47.69 ? 187  ASP C O   1 
ATOM   6223  C  CB  . ASP C 1 187 ? -38.388 64.923  113.319 1.00 49.39 ? 187  ASP C CB  1 
ATOM   6224  C  CG  . ASP C 1 187 ? -37.743 66.076  114.069 1.00 56.92 ? 187  ASP C CG  1 
ATOM   6225  O  OD1 . ASP C 1 187 ? -36.984 65.792  115.021 1.00 61.32 ? 187  ASP C OD1 1 
ATOM   6226  O  OD2 . ASP C 1 187 ? -37.984 67.261  113.728 1.00 56.88 ? 187  ASP C OD2 1 
ATOM   6227  N  N   . ILE C 1 188 ? -41.310 64.824  113.708 1.00 48.52 ? 188  ILE C N   1 
ATOM   6228  C  CA  . ILE C 1 188 ? -42.611 65.422  113.938 1.00 47.05 ? 188  ILE C CA  1 
ATOM   6229  C  C   . ILE C 1 188 ? -43.496 64.557  114.820 1.00 46.21 ? 188  ILE C C   1 
ATOM   6230  O  O   . ILE C 1 188 ? -44.163 65.062  115.721 1.00 47.55 ? 188  ILE C O   1 
ATOM   6231  C  CB  . ILE C 1 188 ? -43.290 65.693  112.605 1.00 44.82 ? 188  ILE C CB  1 
ATOM   6232  C  CG1 . ILE C 1 188 ? -42.508 66.766  111.866 1.00 43.77 ? 188  ILE C CG1 1 
ATOM   6233  C  CG2 . ILE C 1 188 ? -44.700 66.173  112.817 1.00 48.36 ? 188  ILE C CG2 1 
ATOM   6234  C  CD1 . ILE C 1 188 ? -42.957 66.973  110.454 1.00 46.02 ? 188  ILE C CD1 1 
ATOM   6235  N  N   . VAL C 1 189 ? -43.498 63.256  114.585 1.00 47.95 ? 189  VAL C N   1 
ATOM   6236  C  CA  . VAL C 1 189 ? -44.316 62.377  115.422 1.00 52.17 ? 189  VAL C CA  1 
ATOM   6237  C  C   . VAL C 1 189 ? -43.928 62.513  116.885 1.00 52.38 ? 189  VAL C C   1 
ATOM   6238  O  O   . VAL C 1 189 ? -44.790 62.564  117.751 1.00 51.30 ? 189  VAL C O   1 
ATOM   6239  C  CB  . VAL C 1 189 ? -44.157 60.935  114.997 1.00 50.74 ? 189  VAL C CB  1 
ATOM   6240  C  CG1 . VAL C 1 189 ? -45.127 60.060  115.746 1.00 52.19 ? 189  VAL C CG1 1 
ATOM   6241  C  CG2 . VAL C 1 189 ? -44.402 60.854  113.507 1.00 58.98 ? 189  VAL C CG2 1 
ATOM   6242  N  N   . GLU C 1 190 ? -42.622 62.587  117.141 1.00 55.00 ? 190  GLU C N   1 
ATOM   6243  C  CA  . GLU C 1 190 ? -42.120 62.740  118.494 1.00 55.64 ? 190  GLU C CA  1 
ATOM   6244  C  C   . GLU C 1 190 ? -42.715 63.994  119.114 1.00 53.36 ? 190  GLU C C   1 
ATOM   6245  O  O   . GLU C 1 190 ? -43.182 63.972  120.253 1.00 52.47 ? 190  GLU C O   1 
ATOM   6246  C  CB  . GLU C 1 190 ? -40.578 62.824  118.511 1.00 60.87 ? 190  GLU C CB  1 
ATOM   6247  C  CG  . GLU C 1 190 ? -39.884 61.478  118.634 1.00 67.86 ? 190  GLU C CG  1 
ATOM   6248  C  CD  . GLU C 1 190 ? -40.627 60.547  119.598 1.00 76.87 ? 190  GLU C CD  1 
ATOM   6249  O  OE1 . GLU C 1 190 ? -41.146 61.050  120.629 1.00 79.73 ? 190  GLU C OE1 1 
ATOM   6250  O  OE2 . GLU C 1 190 ? -40.693 59.317  119.334 1.00 81.39 ? 190  GLU C OE2 1 
ATOM   6251  N  N   . LYS C 1 191 ? -42.706 65.085  118.359 1.00 50.13 ? 191  LYS C N   1 
ATOM   6252  C  CA  . LYS C 1 191 ? -43.260 66.333  118.856 1.00 49.51 ? 191  LYS C CA  1 
ATOM   6253  C  C   . LYS C 1 191 ? -44.776 66.324  118.943 1.00 51.25 ? 191  LYS C C   1 
ATOM   6254  O  O   . LYS C 1 191 ? -45.344 67.061  119.753 1.00 52.07 ? 191  LYS C O   1 
ATOM   6255  C  CB  . LYS C 1 191 ? -42.822 67.497  117.988 1.00 48.05 ? 191  LYS C CB  1 
ATOM   6256  C  CG  . LYS C 1 191 ? -41.329 67.647  117.916 1.00 48.64 ? 191  LYS C CG  1 
ATOM   6257  C  CD  . LYS C 1 191 ? -40.963 68.893  117.129 1.00 48.63 ? 191  LYS C CD  1 
ATOM   6258  C  CE  . LYS C 1 191 ? -39.470 69.052  117.006 1.00 46.30 ? 191  LYS C CE  1 
ATOM   6259  N  NZ  . LYS C 1 191 ? -39.155 69.844  115.796 1.00 53.36 ? 191  LYS C NZ  1 
ATOM   6260  N  N   . ILE C 1 192 ? -45.444 65.531  118.103 1.00 53.01 ? 192  ILE C N   1 
ATOM   6261  C  CA  . ILE C 1 192 ? -46.906 65.459  118.187 1.00 52.15 ? 192  ILE C CA  1 
ATOM   6262  C  C   . ILE C 1 192 ? -47.181 64.667  119.450 1.00 53.89 ? 192  ILE C C   1 
ATOM   6263  O  O   . ILE C 1 192 ? -47.977 65.097  120.294 1.00 53.47 ? 192  ILE C O   1 
ATOM   6264  C  CB  . ILE C 1 192 ? -47.566 64.753  116.951 1.00 47.51 ? 192  ILE C CB  1 
ATOM   6265  C  CG1 . ILE C 1 192 ? -47.687 65.755  115.799 1.00 42.39 ? 192  ILE C CG1 1 
ATOM   6266  C  CG2 . ILE C 1 192 ? -48.975 64.239  117.312 1.00 41.19 ? 192  ILE C CG2 1 
ATOM   6267  C  CD1 . ILE C 1 192 ? -47.976 65.127  114.448 1.00 41.14 ? 192  ILE C CD1 1 
ATOM   6268  N  N   . SER C 1 193 ? -46.518 63.516  119.588 1.00 55.77 ? 193  SER C N   1 
ATOM   6269  C  CA  . SER C 1 193 ? -46.697 62.735  120.797 1.00 62.14 ? 193  SER C CA  1 
ATOM   6270  C  C   . SER C 1 193 ? -46.141 63.687  121.835 1.00 64.27 ? 193  SER C C   1 
ATOM   6271  O  O   . SER C 1 193 ? -45.433 64.618  121.478 1.00 67.54 ? 193  SER C O   1 
ATOM   6272  C  CB  . SER C 1 193 ? -45.867 61.468  120.768 1.00 61.29 ? 193  SER C CB  1 
ATOM   6273  O  OG  . SER C 1 193 ? -46.060 60.783  121.994 1.00 68.39 ? 193  SER C OG  1 
ATOM   6274  N  N   . MET C 1 194 ? -46.456 63.508  123.102 1.00 64.62 ? 194  MET C N   1 
ATOM   6275  C  CA  . MET C 1 194 ? -45.904 64.437  124.086 1.00 68.83 ? 194  MET C CA  1 
ATOM   6276  C  C   . MET C 1 194 ? -46.552 65.815  124.013 1.00 66.28 ? 194  MET C C   1 
ATOM   6277  O  O   . MET C 1 194 ? -46.079 66.781  124.613 1.00 66.59 ? 194  MET C O   1 
ATOM   6278  C  CB  . MET C 1 194 ? -44.359 64.545  123.960 1.00 73.07 ? 194  MET C CB  1 
ATOM   6279  C  CG  . MET C 1 194 ? -43.779 65.778  123.227 1.00 74.05 ? 194  MET C CG  1 
ATOM   6280  S  SD  . MET C 1 194 ? -41.918 65.699  123.136 1.00 79.19 ? 194  MET C SD  1 
ATOM   6281  C  CE  . MET C 1 194 ? -41.459 67.462  123.188 1.00 74.33 ? 194  MET C CE  1 
ATOM   6282  N  N   . LYS C 1 195 ? -47.627 65.901  123.243 1.00 63.14 ? 195  LYS C N   1 
ATOM   6283  C  CA  . LYS C 1 195 ? -48.429 67.116  123.183 1.00 57.16 ? 195  LYS C CA  1 
ATOM   6284  C  C   . LYS C 1 195 ? -49.763 66.482  123.499 1.00 54.78 ? 195  LYS C C   1 
ATOM   6285  O  O   . LYS C 1 195 ? -50.781 67.146  123.671 1.00 55.96 ? 195  LYS C O   1 
ATOM   6286  C  CB  . LYS C 1 195 ? -48.429 67.744  121.802 1.00 57.01 ? 195  LYS C CB  1 
ATOM   6287  C  CG  . LYS C 1 195 ? -47.400 68.840  121.646 1.00 57.52 ? 195  LYS C CG  1 
ATOM   6288  C  CD  . LYS C 1 195 ? -47.711 70.028  122.532 1.00 57.77 ? 195  LYS C CD  1 
ATOM   6289  C  CE  . LYS C 1 195 ? -46.701 71.143  122.311 1.00 57.18 ? 195  LYS C CE  1 
ATOM   6290  N  NZ  . LYS C 1 195 ? -47.165 72.437  122.885 1.00 59.38 ? 195  LYS C NZ  1 
ATOM   6291  N  N   . ILE C 1 196 ? -49.704 65.158  123.602 1.00 52.57 ? 196  ILE C N   1 
ATOM   6292  C  CA  . ILE C 1 196 ? -50.837 64.318  123.917 1.00 52.22 ? 196  ILE C CA  1 
ATOM   6293  C  C   . ILE C 1 196 ? -51.133 64.307  125.422 1.00 56.14 ? 196  ILE C C   1 
ATOM   6294  O  O   . ILE C 1 196 ? -50.366 63.744  126.210 1.00 57.48 ? 196  ILE C O   1 
ATOM   6295  C  CB  . ILE C 1 196 ? -50.550 62.888  123.481 1.00 49.23 ? 196  ILE C CB  1 
ATOM   6296  C  CG1 . ILE C 1 196 ? -50.312 62.847  121.972 1.00 49.82 ? 196  ILE C CG1 1 
ATOM   6297  C  CG2 . ILE C 1 196 ? -51.665 61.974  123.939 1.00 43.30 ? 196  ILE C CG2 1 
ATOM   6298  C  CD1 . ILE C 1 196 ? -50.080 61.447  121.433 1.00 51.27 ? 196  ILE C CD1 1 
ATOM   6299  N  N   . LYS C 1 197 ? -52.238 64.944  125.808 1.00 58.15 ? 197  LYS C N   1 
ATOM   6300  C  CA  . LYS C 1 197 ? -52.693 64.994  127.194 1.00 57.56 ? 197  LYS C CA  1 
ATOM   6301  C  C   . LYS C 1 197 ? -53.158 63.610  127.665 1.00 60.30 ? 197  LYS C C   1 
ATOM   6302  O  O   . LYS C 1 197 ? -53.388 62.691  126.865 1.00 59.29 ? 197  LYS C O   1 
ATOM   6303  C  CB  . LYS C 1 197 ? -53.872 65.954  127.322 1.00 58.12 ? 197  LYS C CB  1 
ATOM   6304  C  CG  . LYS C 1 197 ? -53.544 67.359  127.718 1.00 59.13 ? 197  LYS C CG  1 
ATOM   6305  C  CD  . LYS C 1 197 ? -52.803 68.102  126.656 1.00 60.70 ? 197  LYS C CD  1 
ATOM   6306  C  CE  . LYS C 1 197 ? -52.579 69.532  127.128 1.00 65.13 ? 197  LYS C CE  1 
ATOM   6307  N  NZ  . LYS C 1 197 ? -53.866 70.203  127.493 1.00 62.55 ? 197  LYS C NZ  1 
ATOM   6308  N  N   . ASP C 1 198 ? -53.326 63.471  128.974 1.00 64.23 ? 198  ASP C N   1 
ATOM   6309  C  CA  . ASP C 1 198 ? -53.767 62.201  129.535 1.00 66.51 ? 198  ASP C CA  1 
ATOM   6310  C  C   . ASP C 1 198 ? -55.250 62.036  129.263 1.00 64.45 ? 198  ASP C C   1 
ATOM   6311  O  O   . ASP C 1 198 ? -55.737 60.901  129.137 1.00 64.77 ? 198  ASP C O   1 
ATOM   6312  C  CB  . ASP C 1 198 ? -53.480 62.153  131.039 1.00 71.17 ? 198  ASP C CB  1 
ATOM   6313  C  CG  . ASP C 1 198 ? -52.002 62.287  131.345 1.00 76.63 ? 198  ASP C CG  1 
ATOM   6314  O  OD1 . ASP C 1 198 ? -51.207 62.514  130.396 1.00 79.79 ? 198  ASP C OD1 1 
ATOM   6315  O  OD2 . ASP C 1 198 ? -51.632 62.171  132.532 1.00 82.43 ? 198  ASP C OD2 1 
ATOM   6316  N  N   . ASN C 1 199 ? -55.958 63.168  129.168 1.00 60.58 ? 199  ASN C N   1 
ATOM   6317  C  CA  . ASN C 1 199 ? -57.392 63.152  128.875 1.00 58.76 ? 199  ASN C CA  1 
ATOM   6318  C  C   . ASN C 1 199 ? -57.670 62.713  127.424 1.00 58.39 ? 199  ASN C C   1 
ATOM   6319  O  O   . ASN C 1 199 ? -58.802 62.377  127.096 1.00 61.10 ? 199  ASN C O   1 
ATOM   6320  C  CB  . ASN C 1 199 ? -58.052 64.523  129.145 1.00 55.98 ? 199  ASN C CB  1 
ATOM   6321  C  CG  . ASN C 1 199 ? -57.419 65.647  128.361 1.00 56.43 ? 199  ASN C CG  1 
ATOM   6322  O  OD1 . ASN C 1 199 ? -56.779 65.414  127.338 1.00 59.38 ? 199  ASN C OD1 1 
ATOM   6323  N  ND2 . ASN C 1 199 ? -57.605 66.879  128.824 1.00 51.84 ? 199  ASN C ND2 1 
ATOM   6324  N  N   . GLY C 1 200 ? -56.650 62.713  126.564 1.00 54.57 ? 200  GLY C N   1 
ATOM   6325  C  CA  . GLY C 1 200 ? -56.847 62.264  125.196 1.00 51.90 ? 200  GLY C CA  1 
ATOM   6326  C  C   . GLY C 1 200 ? -56.653 63.340  124.146 1.00 50.18 ? 200  GLY C C   1 
ATOM   6327  O  O   . GLY C 1 200 ? -56.452 63.060  122.960 1.00 47.21 ? 200  GLY C O   1 
ATOM   6328  N  N   . ILE C 1 201 ? -56.730 64.582  124.591 1.00 48.71 ? 201  ILE C N   1 
ATOM   6329  C  CA  . ILE C 1 201 ? -56.555 65.717  123.713 1.00 50.19 ? 201  ILE C CA  1 
ATOM   6330  C  C   . ILE C 1 201 ? -55.144 65.656  123.150 1.00 53.62 ? 201  ILE C C   1 
ATOM   6331  O  O   . ILE C 1 201 ? -54.253 65.072  123.773 1.00 56.38 ? 201  ILE C O   1 
ATOM   6332  C  CB  . ILE C 1 201 ? -56.734 67.042  124.498 1.00 49.44 ? 201  ILE C CB  1 
ATOM   6333  C  CG1 . ILE C 1 201 ? -58.212 67.294  124.759 1.00 46.95 ? 201  ILE C CG1 1 
ATOM   6334  C  CG2 . ILE C 1 201 ? -56.070 68.210  123.765 1.00 47.93 ? 201  ILE C CG2 1 
ATOM   6335  C  CD1 . ILE C 1 201 ? -58.463 68.655  125.379 1.00 54.05 ? 201  ILE C CD1 1 
ATOM   6336  N  N   . ILE C 1 202 ? -54.947 66.237  121.966 1.00 53.07 ? 202  ILE C N   1 
ATOM   6337  C  CA  . ILE C 1 202 ? -53.634 66.278  121.338 1.00 51.43 ? 202  ILE C CA  1 
ATOM   6338  C  C   . ILE C 1 202 ? -53.391 67.731  120.942 1.00 52.58 ? 202  ILE C C   1 
ATOM   6339  O  O   . ILE C 1 202 ? -53.901 68.205  119.927 1.00 50.95 ? 202  ILE C O   1 
ATOM   6340  C  CB  . ILE C 1 202 ? -53.570 65.374  120.106 1.00 47.75 ? 202  ILE C CB  1 
ATOM   6341  C  CG1 . ILE C 1 202 ? -54.110 63.988  120.461 1.00 48.35 ? 202  ILE C CG1 1 
ATOM   6342  C  CG2 . ILE C 1 202 ? -52.128 65.257  119.640 1.00 46.98 ? 202  ILE C CG2 1 
ATOM   6343  C  CD1 . ILE C 1 202 ? -54.018 62.970  119.336 1.00 48.05 ? 202  ILE C CD1 1 
ATOM   6344  N  N   . GLY C 1 203 ? -52.599 68.425  121.754 1.00 52.67 ? 203  GLY C N   1 
ATOM   6345  C  CA  . GLY C 1 203 ? -52.342 69.827  121.516 1.00 52.17 ? 203  GLY C CA  1 
ATOM   6346  C  C   . GLY C 1 203 ? -53.500 70.479  122.240 1.00 55.68 ? 203  GLY C C   1 
ATOM   6347  O  O   . GLY C 1 203 ? -53.403 70.770  123.440 1.00 57.24 ? 203  GLY C O   1 
ATOM   6348  N  N   . ASP C 1 204 ? -54.603 70.692  121.520 1.00 56.43 ? 204  ASP C N   1 
ATOM   6349  C  CA  . ASP C 1 204 ? -55.826 71.271  122.083 1.00 55.95 ? 204  ASP C CA  1 
ATOM   6350  C  C   . ASP C 1 204 ? -56.974 70.618  121.327 1.00 55.56 ? 204  ASP C C   1 
ATOM   6351  O  O   . ASP C 1 204 ? -56.724 69.901  120.357 1.00 56.18 ? 204  ASP C O   1 
ATOM   6352  C  CB  . ASP C 1 204 ? -55.848 72.783  121.907 1.00 58.91 ? 204  ASP C CB  1 
ATOM   6353  C  CG  . ASP C 1 204 ? -55.770 73.210  120.450 1.00 65.82 ? 204  ASP C CG  1 
ATOM   6354  O  OD1 . ASP C 1 204 ? -56.709 72.907  119.681 1.00 68.49 ? 204  ASP C OD1 1 
ATOM   6355  O  OD2 . ASP C 1 204 ? -54.763 73.857  120.070 1.00 67.74 ? 204  ASP C OD2 1 
ATOM   6356  N  N   . ILE C 1 205 ? -58.220 70.842  121.745 1.00 53.98 ? 205  ILE C N   1 
ATOM   6357  C  CA  . ILE C 1 205 ? -59.335 70.184  121.062 1.00 52.17 ? 205  ILE C CA  1 
ATOM   6358  C  C   . ILE C 1 205 ? -59.426 70.468  119.589 1.00 51.85 ? 205  ILE C C   1 
ATOM   6359  O  O   . ILE C 1 205 ? -59.668 69.568  118.795 1.00 54.11 ? 205  ILE C O   1 
ATOM   6360  C  CB  . ILE C 1 205 ? -60.698 70.563  121.613 1.00 51.02 ? 205  ILE C CB  1 
ATOM   6361  C  CG1 . ILE C 1 205 ? -60.668 71.994  122.108 1.00 51.75 ? 205  ILE C CG1 1 
ATOM   6362  C  CG2 . ILE C 1 205 ? -61.151 69.557  122.614 1.00 52.48 ? 205  ILE C CG2 1 
ATOM   6363  C  CD1 . ILE C 1 205 ? -62.052 72.554  122.242 1.00 56.71 ? 205  ILE C CD1 1 
ATOM   6364  N  N   . TYR C 1 206 ? -59.258 71.728  119.222 1.00 52.05 ? 206  TYR C N   1 
ATOM   6365  C  CA  . TYR C 1 206 ? -59.360 72.106  117.826 1.00 50.08 ? 206  TYR C CA  1 
ATOM   6366  C  C   . TYR C 1 206 ? -58.173 71.738  116.973 1.00 48.00 ? 206  TYR C C   1 
ATOM   6367  O  O   . TYR C 1 206 ? -58.160 72.022  115.775 1.00 46.99 ? 206  TYR C O   1 
ATOM   6368  C  CB  . TYR C 1 206 ? -59.686 73.589  117.724 1.00 50.12 ? 206  TYR C CB  1 
ATOM   6369  C  CG  . TYR C 1 206 ? -60.987 73.855  118.415 1.00 49.99 ? 206  TYR C CG  1 
ATOM   6370  C  CD1 . TYR C 1 206 ? -62.108 73.071  118.130 1.00 50.29 ? 206  TYR C CD1 1 
ATOM   6371  C  CD2 . TYR C 1 206 ? -61.088 74.821  119.408 1.00 48.34 ? 206  TYR C CD2 1 
ATOM   6372  C  CE1 . TYR C 1 206 ? -63.291 73.242  118.829 1.00 52.33 ? 206  TYR C CE1 1 
ATOM   6373  C  CE2 . TYR C 1 206 ? -62.260 75.002  120.106 1.00 49.39 ? 206  TYR C CE2 1 
ATOM   6374  C  CZ  . TYR C 1 206 ? -63.359 74.211  119.818 1.00 51.22 ? 206  TYR C CZ  1 
ATOM   6375  O  OH  . TYR C 1 206 ? -64.516 74.389  120.530 1.00 53.67 ? 206  TYR C OH  1 
ATOM   6376  N  N   . SER C 1 207 ? -57.186 71.087  117.577 1.00 44.79 ? 207  SER C N   1 
ATOM   6377  C  CA  . SER C 1 207 ? -56.040 70.649  116.802 1.00 46.37 ? 207  SER C CA  1 
ATOM   6378  C  C   . SER C 1 207 ? -55.991 69.118  116.862 1.00 41.73 ? 207  SER C C   1 
ATOM   6379  O  O   . SER C 1 207 ? -55.245 68.467  116.133 1.00 42.41 ? 207  SER C O   1 
ATOM   6380  C  CB  . SER C 1 207 ? -54.740 71.265  117.331 1.00 47.61 ? 207  SER C CB  1 
ATOM   6381  O  OG  . SER C 1 207 ? -54.341 70.636  118.531 1.00 56.67 ? 207  SER C OG  1 
ATOM   6382  N  N   . THR C 1 208 ? -56.833 68.537  117.694 1.00 39.53 ? 208  THR C N   1 
ATOM   6383  C  CA  . THR C 1 208 ? -56.844 67.087  117.834 1.00 40.13 ? 208  THR C CA  1 
ATOM   6384  C  C   . THR C 1 208 ? -57.264 66.307  116.573 1.00 42.57 ? 208  THR C C   1 
ATOM   6385  O  O   . THR C 1 208 ? -56.668 65.266  116.267 1.00 41.29 ? 208  THR C O   1 
ATOM   6386  C  CB  . THR C 1 208 ? -57.740 66.694  119.030 1.00 41.97 ? 208  THR C CB  1 
ATOM   6387  O  OG1 . THR C 1 208 ? -57.372 67.488  120.172 1.00 40.27 ? 208  THR C OG1 1 
ATOM   6388  C  CG2 . THR C 1 208 ? -57.596 65.213  119.355 1.00 33.92 ? 208  THR C CG2 1 
ATOM   6389  N  N   . GLY C 1 209 ? -58.278 66.797  115.845 1.00 45.23 ? 209  GLY C N   1 
ATOM   6390  C  CA  . GLY C 1 209 ? -58.726 66.104  114.635 1.00 41.29 ? 209  GLY C CA  1 
ATOM   6391  C  C   . GLY C 1 209 ? -57.594 65.884  113.636 1.00 42.40 ? 209  GLY C C   1 
ATOM   6392  O  O   . GLY C 1 209 ? -57.358 64.756  113.176 1.00 39.62 ? 209  GLY C O   1 
ATOM   6393  N  N   . LEU C 1 210 ? -56.884 66.958  113.292 1.00 40.14 ? 210  LEU C N   1 
ATOM   6394  C  CA  . LEU C 1 210 ? -55.783 66.837  112.356 1.00 42.10 ? 210  LEU C CA  1 
ATOM   6395  C  C   . LEU C 1 210 ? -54.703 65.918  112.936 1.00 43.39 ? 210  LEU C C   1 
ATOM   6396  O  O   . LEU C 1 210 ? -54.135 65.092  112.235 1.00 44.76 ? 210  LEU C O   1 
ATOM   6397  C  CB  . LEU C 1 210 ? -55.189 68.209  112.058 1.00 43.65 ? 210  LEU C CB  1 
ATOM   6398  C  CG  . LEU C 1 210 ? -56.142 69.194  111.377 1.00 48.30 ? 210  LEU C CG  1 
ATOM   6399  C  CD1 . LEU C 1 210 ? -55.472 70.597  111.139 1.00 45.84 ? 210  LEU C CD1 1 
ATOM   6400  C  CD2 . LEU C 1 210 ? -56.576 68.552  110.072 1.00 44.14 ? 210  LEU C CD2 1 
ATOM   6401  N  N   . ALA C 1 211 ? -54.429 66.045  114.226 1.00 43.93 ? 211  ALA C N   1 
ATOM   6402  C  CA  . ALA C 1 211 ? -53.414 65.209  114.841 1.00 42.71 ? 211  ALA C CA  1 
ATOM   6403  C  C   . ALA C 1 211 ? -53.806 63.747  114.718 1.00 42.67 ? 211  ALA C C   1 
ATOM   6404  O  O   . ALA C 1 211 ? -52.949 62.892  114.537 1.00 44.80 ? 211  ALA C O   1 
ATOM   6405  C  CB  . ALA C 1 211 ? -53.230 65.598  116.314 1.00 40.98 ? 211  ALA C CB  1 
ATOM   6406  N  N   . MET C 1 212 ? -55.098 63.453  114.804 1.00 42.49 ? 212  MET C N   1 
ATOM   6407  C  CA  . MET C 1 212 ? -55.537 62.067  114.689 1.00 43.75 ? 212  MET C CA  1 
ATOM   6408  C  C   . MET C 1 212 ? -55.238 61.527  113.297 1.00 44.24 ? 212  MET C C   1 
ATOM   6409  O  O   . MET C 1 212 ? -54.856 60.355  113.126 1.00 42.76 ? 212  MET C O   1 
ATOM   6410  C  CB  . MET C 1 212 ? -57.031 61.952  114.968 1.00 46.89 ? 212  MET C CB  1 
ATOM   6411  C  CG  . MET C 1 212 ? -57.455 62.338  116.377 1.00 47.29 ? 212  MET C CG  1 
ATOM   6412  S  SD  . MET C 1 212 ? -59.244 62.111  116.580 1.00 50.45 ? 212  MET C SD  1 
ATOM   6413  C  CE  . MET C 1 212 ? -59.333 60.359  116.618 1.00 43.03 ? 212  MET C CE  1 
ATOM   6414  N  N   . GLN C 1 213 ? -55.414 62.377  112.292 1.00 43.45 ? 213  GLN C N   1 
ATOM   6415  C  CA  . GLN C 1 213 ? -55.133 61.927  110.943 1.00 43.93 ? 213  GLN C CA  1 
ATOM   6416  C  C   . GLN C 1 213 ? -53.669 61.597  110.813 1.00 43.41 ? 213  GLN C C   1 
ATOM   6417  O  O   . GLN C 1 213 ? -53.313 60.539  110.297 1.00 44.49 ? 213  GLN C O   1 
ATOM   6418  C  CB  . GLN C 1 213 ? -55.497 62.987  109.925 1.00 44.43 ? 213  GLN C CB  1 
ATOM   6419  C  CG  . GLN C 1 213 ? -56.971 63.151  109.710 1.00 44.88 ? 213  GLN C CG  1 
ATOM   6420  C  CD  . GLN C 1 213 ? -57.255 63.989  108.488 1.00 44.83 ? 213  GLN C CD  1 
ATOM   6421  O  OE1 . GLN C 1 213 ? -58.147 64.832  108.493 1.00 44.56 ? 213  GLN C OE1 1 
ATOM   6422  N  NE2 . GLN C 1 213 ? -56.493 63.753  107.421 1.00 44.61 ? 213  GLN C NE2 1 
ATOM   6423  N  N   . ALA C 1 214 ? -52.820 62.504  111.287 1.00 42.76 ? 214  ALA C N   1 
ATOM   6424  C  CA  . ALA C 1 214 ? -51.381 62.295  111.214 1.00 42.47 ? 214  ALA C CA  1 
ATOM   6425  C  C   . ALA C 1 214 ? -50.950 61.012  111.928 1.00 40.69 ? 214  ALA C C   1 
ATOM   6426  O  O   . ALA C 1 214 ? -50.259 60.176  111.355 1.00 40.63 ? 214  ALA C O   1 
ATOM   6427  C  CB  . ALA C 1 214 ? -50.633 63.511  111.790 1.00 42.49 ? 214  ALA C CB  1 
ATOM   6428  N  N   . LEU C 1 215 ? -51.379 60.838  113.166 1.00 39.37 ? 215  LEU C N   1 
ATOM   6429  C  CA  . LEU C 1 215 ? -50.972 59.661  113.895 1.00 41.80 ? 215  LEU C CA  1 
ATOM   6430  C  C   . LEU C 1 215 ? -51.408 58.345  113.249 1.00 44.81 ? 215  LEU C C   1 
ATOM   6431  O  O   . LEU C 1 215 ? -50.693 57.351  113.314 1.00 49.35 ? 215  LEU C O   1 
ATOM   6432  C  CB  . LEU C 1 215 ? -51.451 59.744  115.356 1.00 38.54 ? 215  LEU C CB  1 
ATOM   6433  C  CG  . LEU C 1 215 ? -50.848 60.917  116.151 1.00 39.26 ? 215  LEU C CG  1 
ATOM   6434  C  CD1 . LEU C 1 215 ? -51.522 61.037  117.509 1.00 30.87 ? 215  LEU C CD1 1 
ATOM   6435  C  CD2 . LEU C 1 215 ? -49.325 60.745  116.288 1.00 36.59 ? 215  LEU C CD2 1 
ATOM   6436  N  N   . SER C 1 216 ? -52.555 58.314  112.597 1.00 47.54 ? 216  SER C N   1 
ATOM   6437  C  CA  . SER C 1 216 ? -53.003 57.048  111.996 1.00 49.79 ? 216  SER C CA  1 
ATOM   6438  C  C   . SER C 1 216 ? -52.328 56.738  110.680 1.00 48.32 ? 216  SER C C   1 
ATOM   6439  O  O   . SER C 1 216 ? -52.515 55.658  110.108 1.00 47.97 ? 216  SER C O   1 
ATOM   6440  C  CB  . SER C 1 216 ? -54.516 57.082  111.779 1.00 49.42 ? 216  SER C CB  1 
ATOM   6441  O  OG  . SER C 1 216 ? -54.922 58.418  111.533 1.00 49.31 ? 216  SER C OG  1 
ATOM   6442  N  N   . VAL C 1 217 ? -51.502 57.672  110.238 1.00 46.54 ? 217  VAL C N   1 
ATOM   6443  C  CA  . VAL C 1 217 ? -50.866 57.537  108.959 1.00 46.17 ? 217  VAL C CA  1 
ATOM   6444  C  C   . VAL C 1 217 ? -49.326 57.577  108.867 1.00 50.39 ? 217  VAL C C   1 
ATOM   6445  O  O   . VAL C 1 217 ? -48.770 57.156  107.832 1.00 47.30 ? 217  VAL C O   1 
ATOM   6446  C  CB  . VAL C 1 217 ? -51.500 58.595  108.060 1.00 43.98 ? 217  VAL C CB  1 
ATOM   6447  C  CG1 . VAL C 1 217 ? -50.463 59.310  107.253 1.00 42.13 ? 217  VAL C CG1 1 
ATOM   6448  C  CG2 . VAL C 1 217 ? -52.561 57.950  107.217 1.00 40.47 ? 217  VAL C CG2 1 
ATOM   6449  N  N   . THR C 1 218 ? -48.631 58.078  109.902 1.00 51.76 ? 218  THR C N   1 
ATOM   6450  C  CA  . THR C 1 218 ? -47.165 58.135  109.812 1.00 55.35 ? 218  THR C CA  1 
ATOM   6451  C  C   . THR C 1 218 ? -46.602 56.731  109.755 1.00 58.20 ? 218  THR C C   1 
ATOM   6452  O  O   . THR C 1 218 ? -47.057 55.825  110.463 1.00 56.13 ? 218  THR C O   1 
ATOM   6453  C  CB  . THR C 1 218 ? -46.454 58.855  111.004 1.00 54.42 ? 218  THR C CB  1 
ATOM   6454  O  OG1 . THR C 1 218 ? -47.166 58.612  112.220 1.00 53.04 ? 218  THR C OG1 1 
ATOM   6455  C  CG2 . THR C 1 218 ? -46.306 60.351  110.740 1.00 58.56 ? 218  THR C CG2 1 
ATOM   6456  N  N   . PRO C 1 219 ? -45.588 56.536  108.912 1.00 60.60 ? 219  PRO C N   1 
ATOM   6457  C  CA  . PRO C 1 219 ? -44.951 55.228  108.761 1.00 64.35 ? 219  PRO C CA  1 
ATOM   6458  C  C   . PRO C 1 219 ? -44.286 54.708  110.038 1.00 68.63 ? 219  PRO C C   1 
ATOM   6459  O  O   . PRO C 1 219 ? -44.215 53.500  110.253 1.00 68.04 ? 219  PRO C O   1 
ATOM   6460  C  CB  . PRO C 1 219 ? -43.965 55.462  107.623 1.00 64.75 ? 219  PRO C CB  1 
ATOM   6461  C  CG  . PRO C 1 219 ? -43.641 56.939  107.748 1.00 66.53 ? 219  PRO C CG  1 
ATOM   6462  C  CD  . PRO C 1 219 ? -44.977 57.546  108.030 1.00 60.68 ? 219  PRO C CD  1 
ATOM   6463  N  N   . GLU C 1 220 ? -43.828 55.620  110.895 1.00 74.98 ? 220  GLU C N   1 
ATOM   6464  C  CA  . GLU C 1 220 ? -43.153 55.242  112.140 1.00 80.93 ? 220  GLU C CA  1 
ATOM   6465  C  C   . GLU C 1 220 ? -43.709 55.912  113.413 1.00 84.64 ? 220  GLU C C   1 
ATOM   6466  O  O   . GLU C 1 220 ? -43.503 57.115  113.637 1.00 81.79 ? 220  GLU C O   1 
ATOM   6467  C  CB  . GLU C 1 220 ? -41.662 55.567  112.011 1.00 83.41 ? 220  GLU C CB  1 
ATOM   6468  C  CG  . GLU C 1 220 ? -40.854 55.399  113.287 1.00 88.03 ? 220  GLU C CG  1 
ATOM   6469  C  CD  . GLU C 1 220 ? -40.663 53.942  113.679 1.00 91.90 ? 220  GLU C CD  1 
ATOM   6470  O  OE1 . GLU C 1 220 ? -41.681 53.223  113.848 1.00 92.28 ? 220  GLU C OE1 1 
ATOM   6471  O  OE2 . GLU C 1 220 ? -39.488 53.521  113.819 1.00 92.61 ? 220  GLU C OE2 1 
ATOM   6472  N  N   . PRO C 1 221 ? -44.408 55.134  114.272 1.00 88.79 ? 221  PRO C N   1 
ATOM   6473  C  CA  . PRO C 1 221 ? -44.974 55.680  115.515 1.00 91.14 ? 221  PRO C CA  1 
ATOM   6474  C  C   . PRO C 1 221 ? -43.886 56.219  116.441 1.00 93.56 ? 221  PRO C C   1 
ATOM   6475  O  O   . PRO C 1 221 ? -42.688 56.083  116.163 1.00 93.98 ? 221  PRO C O   1 
ATOM   6476  C  CB  . PRO C 1 221 ? -45.715 54.481  116.122 1.00 90.67 ? 221  PRO C CB  1 
ATOM   6477  C  CG  . PRO C 1 221 ? -44.924 53.311  115.648 1.00 90.78 ? 221  PRO C CG  1 
ATOM   6478  C  CD  . PRO C 1 221 ? -44.655 53.680  114.188 1.00 90.99 ? 221  PRO C CD  1 
ATOM   6479  N  N   . SER C 1 222 ? -44.301 56.845  117.536 1.00 95.36 ? 222  SER C N   1 
ATOM   6480  C  CA  . SER C 1 222 ? -43.336 57.388  118.483 1.00 97.27 ? 222  SER C CA  1 
ATOM   6481  C  C   . SER C 1 222 ? -43.098 56.354  119.582 1.00 97.52 ? 222  SER C C   1 
ATOM   6482  O  O   . SER C 1 222 ? -43.909 55.441  119.758 1.00 95.54 ? 222  SER C O   1 
ATOM   6483  C  CB  . SER C 1 222 ? -43.860 58.698  119.089 1.00 98.29 ? 222  SER C CB  1 
ATOM   6484  O  OG  . SER C 1 222 ? -45.056 58.483  119.820 1.00 99.45 ? 222  SER C OG  1 
ATOM   6485  N  N   . LYS C 1 223 ? -41.985 56.489  120.303 1.00 98.44 ? 223  LYS C N   1 
ATOM   6486  C  CA  . LYS C 1 223 ? -41.662 55.565  121.396 1.00 99.45 ? 223  LYS C CA  1 
ATOM   6487  C  C   . LYS C 1 223 ? -42.859 55.386  122.337 1.00 99.45 ? 223  LYS C C   1 
ATOM   6488  O  O   . LYS C 1 223 ? -43.313 54.257  122.564 1.00 98.45 ? 223  LYS C O   1 
ATOM   6489  C  CB  . LYS C 1 223 ? -40.450 56.068  122.196 1.00 99.12 ? 223  LYS C CB  1 
ATOM   6490  C  CG  . LYS C 1 223 ? -39.160 55.330  121.885 1.00 99.45 ? 223  LYS C CG  1 
ATOM   6491  C  CD  . LYS C 1 223 ? -39.262 53.840  122.221 1.00 99.45 ? 223  LYS C CD  1 
ATOM   6492  C  CE  . LYS C 1 223 ? -37.989 53.065  121.802 1.00 99.45 ? 223  LYS C CE  1 
ATOM   6493  N  NZ  . LYS C 1 223 ? -36.710 53.537  122.439 1.00 99.45 ? 223  LYS C NZ  1 
ATOM   6494  N  N   . LYS C 1 224 ? -43.356 56.502  122.882 1.00 99.45 ? 224  LYS C N   1 
ATOM   6495  C  CA  . LYS C 1 224 ? -44.503 56.473  123.786 1.00 99.45 ? 224  LYS C CA  1 
ATOM   6496  C  C   . LYS C 1 224 ? -45.764 56.187  122.970 1.00 99.45 ? 224  LYS C C   1 
ATOM   6497  O  O   . LYS C 1 224 ? -46.133 56.954  122.067 1.00 99.45 ? 224  LYS C O   1 
ATOM   6498  C  CB  . LYS C 1 224 ? -44.659 57.807  124.537 1.00 99.45 ? 224  LYS C CB  1 
ATOM   6499  C  CG  . LYS C 1 224 ? -45.728 57.764  125.638 1.00 99.45 ? 224  LYS C CG  1 
ATOM   6500  C  CD  . LYS C 1 224 ? -46.066 59.150  126.176 1.00 99.45 ? 224  LYS C CD  1 
ATOM   6501  C  CE  . LYS C 1 224 ? -47.269 59.103  127.108 1.00 98.62 ? 224  LYS C CE  1 
ATOM   6502  N  NZ  . LYS C 1 224 ? -47.761 60.469  127.434 1.00 98.15 ? 224  LYS C NZ  1 
ATOM   6503  N  N   . GLU C 1 225 ? -46.413 55.073  123.303 1.00 98.96 ? 225  GLU C N   1 
ATOM   6504  C  CA  . GLU C 1 225 ? -47.623 54.627  122.626 1.00 97.75 ? 225  GLU C CA  1 
ATOM   6505  C  C   . GLU C 1 225 ? -48.790 55.611  122.744 1.00 96.61 ? 225  GLU C C   1 
ATOM   6506  O  O   . GLU C 1 225 ? -48.939 56.310  123.750 1.00 95.78 ? 225  GLU C O   1 
ATOM   6507  C  CB  . GLU C 1 225 ? -48.019 53.258  123.170 1.00 97.62 ? 225  GLU C CB  1 
ATOM   6508  C  CG  . GLU C 1 225 ? -49.271 52.685  122.571 1.00 98.57 ? 225  GLU C CG  1 
ATOM   6509  C  CD  . GLU C 1 225 ? -49.497 51.268  123.032 1.00 99.45 ? 225  GLU C CD  1 
ATOM   6510  O  OE1 . GLU C 1 225 ? -49.410 51.028  124.263 1.00 99.45 ? 225  GLU C OE1 1 
ATOM   6511  O  OE2 . GLU C 1 225 ? -49.759 50.400  122.169 1.00 99.45 ? 225  GLU C OE2 1 
ATOM   6512  N  N   . TRP C 1 226 ? -49.610 55.665  121.697 1.00 94.83 ? 226  TRP C N   1 
ATOM   6513  C  CA  . TRP C 1 226 ? -50.756 56.562  121.670 1.00 91.42 ? 226  TRP C CA  1 
ATOM   6514  C  C   . TRP C 1 226 ? -52.083 55.840  121.775 1.00 89.98 ? 226  TRP C C   1 
ATOM   6515  O  O   . TRP C 1 226 ? -52.464 55.068  120.884 1.00 87.74 ? 226  TRP C O   1 
ATOM   6516  C  CB  . TRP C 1 226 ? -50.753 57.400  120.396 1.00 88.70 ? 226  TRP C CB  1 
ATOM   6517  C  CG  . TRP C 1 226 ? -52.073 58.070  120.117 1.00 86.22 ? 226  TRP C CG  1 
ATOM   6518  C  CD1 . TRP C 1 226 ? -52.760 58.930  120.940 1.00 85.23 ? 226  TRP C CD1 1 
ATOM   6519  C  CD2 . TRP C 1 226 ? -52.846 57.967  118.915 1.00 84.48 ? 226  TRP C CD2 1 
ATOM   6520  N  NE1 . TRP C 1 226 ? -53.909 59.367  120.318 1.00 84.17 ? 226  TRP C NE1 1 
ATOM   6521  C  CE2 . TRP C 1 226 ? -53.988 58.790  119.076 1.00 83.85 ? 226  TRP C CE2 1 
ATOM   6522  C  CE3 . TRP C 1 226 ? -52.688 57.255  117.717 1.00 81.89 ? 226  TRP C CE3 1 
ATOM   6523  C  CZ2 . TRP C 1 226 ? -54.960 58.926  118.078 1.00 82.25 ? 226  TRP C CZ2 1 
ATOM   6524  C  CZ3 . TRP C 1 226 ? -53.653 57.389  116.727 1.00 80.14 ? 226  TRP C CZ3 1 
ATOM   6525  C  CH2 . TRP C 1 226 ? -54.777 58.217  116.916 1.00 80.72 ? 226  TRP C CH2 1 
ATOM   6526  N  N   . ASN C 1 227 ? -52.785 56.118  122.870 1.00 88.68 ? 227  ASN C N   1 
ATOM   6527  C  CA  . ASN C 1 227 ? -54.087 55.526  123.115 1.00 87.68 ? 227  ASN C CA  1 
ATOM   6528  C  C   . ASN C 1 227 ? -55.079 56.241  122.203 1.00 85.32 ? 227  ASN C C   1 
ATOM   6529  O  O   . ASN C 1 227 ? -55.539 57.352  122.492 1.00 83.21 ? 227  ASN C O   1 
ATOM   6530  C  CB  . ASN C 1 227 ? -54.499 55.698  124.581 1.00 88.96 ? 227  ASN C CB  1 
ATOM   6531  C  CG  . ASN C 1 227 ? -55.678 54.818  124.956 1.00 90.69 ? 227  ASN C CG  1 
ATOM   6532  O  OD1 . ASN C 1 227 ? -56.620 54.655  124.174 1.00 91.46 ? 227  ASN C OD1 1 
ATOM   6533  N  ND2 . ASN C 1 227 ? -55.634 54.246  126.155 1.00 91.16 ? 227  ASN C ND2 1 
ATOM   6534  N  N   . CYS C 1 228 ? -55.395 55.596  121.091 1.00 82.76 ? 228  CYS C N   1 
ATOM   6535  C  CA  . CYS C 1 228 ? -56.317 56.158  120.125 1.00 81.45 ? 228  CYS C CA  1 
ATOM   6536  C  C   . CYS C 1 228 ? -57.759 56.208  120.632 1.00 77.48 ? 228  CYS C C   1 
ATOM   6537  O  O   . CYS C 1 228 ? -58.433 57.228  120.498 1.00 75.26 ? 228  CYS C O   1 
ATOM   6538  C  CB  . CYS C 1 228 ? -56.234 55.362  118.826 1.00 86.10 ? 228  CYS C CB  1 
ATOM   6539  S  SG  . CYS C 1 228 ? -57.433 55.887  117.565 1.00 94.29 ? 228  CYS C SG  1 
ATOM   6540  N  N   . LYS C 1 229 ? -58.226 55.111  121.217 1.00 74.05 ? 229  LYS C N   1 
ATOM   6541  C  CA  . LYS C 1 229 ? -59.578 55.053  121.752 1.00 71.09 ? 229  LYS C CA  1 
ATOM   6542  C  C   . LYS C 1 229 ? -59.821 56.152  122.779 1.00 67.12 ? 229  LYS C C   1 
ATOM   6543  O  O   . LYS C 1 229 ? -60.871 56.777  122.799 1.00 65.83 ? 229  LYS C O   1 
ATOM   6544  C  CB  . LYS C 1 229 ? -59.842 53.699  122.401 1.00 71.19 ? 229  LYS C CB  1 
ATOM   6545  C  CG  . LYS C 1 229 ? -61.174 53.648  123.108 1.00 74.13 ? 229  LYS C CG  1 
ATOM   6546  C  CD  . LYS C 1 229 ? -61.289 52.415  123.975 1.00 79.06 ? 229  LYS C CD  1 
ATOM   6547  C  CE  . LYS C 1 229 ? -62.579 52.432  124.784 1.00 81.19 ? 229  LYS C CE  1 
ATOM   6548  N  NZ  . LYS C 1 229 ? -63.779 52.539  123.904 1.00 85.56 ? 229  LYS C NZ  1 
ATOM   6549  N  N   . LYS C 1 230 ? -58.854 56.375  123.649 1.00 65.81 ? 230  LYS C N   1 
ATOM   6550  C  CA  . LYS C 1 230 ? -58.990 57.414  124.662 1.00 67.53 ? 230  LYS C CA  1 
ATOM   6551  C  C   . LYS C 1 230 ? -59.273 58.761  123.990 1.00 66.13 ? 230  LYS C C   1 
ATOM   6552  O  O   . LYS C 1 230 ? -60.114 59.532  124.462 1.00 63.28 ? 230  LYS C O   1 
ATOM   6553  C  CB  . LYS C 1 230 ? -57.702 57.497  125.505 1.00 73.30 ? 230  LYS C CB  1 
ATOM   6554  C  CG  . LYS C 1 230 ? -57.594 58.694  126.466 1.00 75.92 ? 230  LYS C CG  1 
ATOM   6555  C  CD  . LYS C 1 230 ? -58.601 58.614  127.597 1.00 82.54 ? 230  LYS C CD  1 
ATOM   6556  C  CE  . LYS C 1 230 ? -58.418 59.792  128.555 1.00 85.83 ? 230  LYS C CE  1 
ATOM   6557  N  NZ  . LYS C 1 230 ? -59.428 59.857  129.660 1.00 87.97 ? 230  LYS C NZ  1 
ATOM   6558  N  N   . THR C 1 231 ? -58.573 59.038  122.888 1.00 63.41 ? 231  THR C N   1 
ATOM   6559  C  CA  . THR C 1 231 ? -58.763 60.290  122.175 1.00 60.62 ? 231  THR C CA  1 
ATOM   6560  C  C   . THR C 1 231 ? -60.125 60.359  121.472 1.00 58.95 ? 231  THR C C   1 
ATOM   6561  O  O   . THR C 1 231 ? -60.831 61.377  121.561 1.00 57.77 ? 231  THR C O   1 
ATOM   6562  C  CB  . THR C 1 231 ? -57.623 60.538  121.125 1.00 61.26 ? 231  THR C CB  1 
ATOM   6563  O  OG1 . THR C 1 231 ? -56.392 60.832  121.805 1.00 59.20 ? 231  THR C OG1 1 
ATOM   6564  C  CG2 . THR C 1 231 ? -57.970 61.724  120.212 1.00 56.70 ? 231  THR C CG2 1 
ATOM   6565  N  N   . THR C 1 232 ? -60.510 59.291  120.780 1.00 54.89 ? 232  THR C N   1 
ATOM   6566  C  CA  . THR C 1 232 ? -61.780 59.336  120.082 1.00 55.68 ? 232  THR C CA  1 
ATOM   6567  C  C   . THR C 1 232 ? -62.957 59.475  121.050 1.00 54.40 ? 232  THR C C   1 
ATOM   6568  O  O   . THR C 1 232 ? -63.923 60.195  120.764 1.00 53.89 ? 232  THR C O   1 
ATOM   6569  C  CB  . THR C 1 232 ? -61.935 58.134  119.097 1.00 55.98 ? 232  THR C CB  1 
ATOM   6570  O  OG1 . THR C 1 232 ? -63.317 57.801  118.953 1.00 58.34 ? 232  THR C OG1 1 
ATOM   6571  C  CG2 . THR C 1 232 ? -61.168 56.936  119.563 1.00 60.74 ? 232  THR C CG2 1 
ATOM   6572  N  N   . ASP C 1 233 ? -62.863 58.829  122.208 1.00 54.36 ? 233  ASP C N   1 
ATOM   6573  C  CA  . ASP C 1 233 ? -63.915 58.947  123.222 1.00 54.29 ? 233  ASP C CA  1 
ATOM   6574  C  C   . ASP C 1 233 ? -63.978 60.371  123.792 1.00 50.21 ? 233  ASP C C   1 
ATOM   6575  O  O   . ASP C 1 233 ? -65.044 60.905  124.044 1.00 47.53 ? 233  ASP C O   1 
ATOM   6576  C  CB  . ASP C 1 233 ? -63.677 57.963  124.359 1.00 56.68 ? 233  ASP C CB  1 
ATOM   6577  C  CG  . ASP C 1 233 ? -63.982 56.540  123.963 1.00 62.52 ? 233  ASP C CG  1 
ATOM   6578  O  OD1 . ASP C 1 233 ? -64.477 56.309  122.831 1.00 64.61 ? 233  ASP C OD1 1 
ATOM   6579  O  OD2 . ASP C 1 233 ? -63.732 55.645  124.791 1.00 64.57 ? 233  ASP C OD2 1 
ATOM   6580  N  N   . MET C 1 234 ? -62.827 60.981  124.009 1.00 50.24 ? 234  MET C N   1 
ATOM   6581  C  CA  . MET C 1 234 ? -62.809 62.338  124.521 1.00 53.20 ? 234  MET C CA  1 
ATOM   6582  C  C   . MET C 1 234 ? -63.477 63.244  123.473 1.00 54.61 ? 234  MET C C   1 
ATOM   6583  O  O   . MET C 1 234 ? -64.179 64.203  123.815 1.00 55.56 ? 234  MET C O   1 
ATOM   6584  C  CB  . MET C 1 234 ? -61.362 62.782  124.775 1.00 53.66 ? 234  MET C CB  1 
ATOM   6585  C  CG  . MET C 1 234 ? -61.211 64.244  125.162 1.00 63.60 ? 234  MET C CG  1 
ATOM   6586  S  SD  . MET C 1 234 ? -61.319 65.422  123.755 1.00 72.76 ? 234  MET C SD  1 
ATOM   6587  C  CE  . MET C 1 234 ? -59.792 65.054  122.914 1.00 70.83 ? 234  MET C CE  1 
ATOM   6588  N  N   . ILE C 1 235 ? -63.265 62.936  122.192 1.00 52.63 ? 235  ILE C N   1 
ATOM   6589  C  CA  . ILE C 1 235 ? -63.841 63.740  121.130 1.00 51.14 ? 235  ILE C CA  1 
ATOM   6590  C  C   . ILE C 1 235 ? -65.357 63.651  121.125 1.00 49.96 ? 235  ILE C C   1 
ATOM   6591  O  O   . ILE C 1 235 ? -66.039 64.670  121.054 1.00 49.88 ? 235  ILE C O   1 
ATOM   6592  C  CB  . ILE C 1 235 ? -63.270 63.336  119.742 1.00 52.01 ? 235  ILE C CB  1 
ATOM   6593  C  CG1 . ILE C 1 235 ? -61.858 63.917  119.586 1.00 51.48 ? 235  ILE C CG1 1 
ATOM   6594  C  CG2 . ILE C 1 235 ? -64.170 63.880  118.613 1.00 50.31 ? 235  ILE C CG2 1 
ATOM   6595  C  CD1 . ILE C 1 235 ? -61.789 65.480  119.641 1.00 49.01 ? 235  ILE C CD1 1 
ATOM   6596  N  N   . LEU C 1 236 ? -65.889 62.437  121.188 1.00 50.06 ? 236  LEU C N   1 
ATOM   6597  C  CA  . LEU C 1 236 ? -67.340 62.271  121.231 1.00 51.67 ? 236  LEU C CA  1 
ATOM   6598  C  C   . LEU C 1 236 ? -67.942 63.101  122.383 1.00 56.55 ? 236  LEU C C   1 
ATOM   6599  O  O   . LEU C 1 236 ? -68.870 63.885  122.156 1.00 58.41 ? 236  LEU C O   1 
ATOM   6600  C  CB  . LEU C 1 236 ? -67.693 60.796  121.388 1.00 43.62 ? 236  LEU C CB  1 
ATOM   6601  C  CG  . LEU C 1 236 ? -67.080 59.967  120.257 1.00 46.40 ? 236  LEU C CG  1 
ATOM   6602  C  CD1 . LEU C 1 236 ? -67.445 58.509  120.372 1.00 45.95 ? 236  LEU C CD1 1 
ATOM   6603  C  CD2 . LEU C 1 236 ? -67.576 60.488  118.934 1.00 47.02 ? 236  LEU C CD2 1 
ATOM   6604  N  N   . ASN C 1 237 ? -67.414 62.954  123.602 1.00 58.66 ? 237  ASN C N   1 
ATOM   6605  C  CA  . ASN C 1 237 ? -67.922 63.733  124.728 1.00 61.03 ? 237  ASN C CA  1 
ATOM   6606  C  C   . ASN C 1 237 ? -67.832 65.214  124.450 1.00 58.13 ? 237  ASN C C   1 
ATOM   6607  O  O   . ASN C 1 237 ? -68.734 65.974  124.795 1.00 57.91 ? 237  ASN C O   1 
ATOM   6608  C  CB  . ASN C 1 237 ? -67.147 63.448  126.022 1.00 68.37 ? 237  ASN C CB  1 
ATOM   6609  C  CG  . ASN C 1 237 ? -67.377 62.054  126.522 1.00 77.43 ? 237  ASN C CG  1 
ATOM   6610  O  OD1 . ASN C 1 237 ? -68.481 61.523  126.366 1.00 81.71 ? 237  ASN C OD1 1 
ATOM   6611  N  ND2 . ASN C 1 237 ? -66.349 61.440  127.132 1.00 81.11 ? 237  ASN C ND2 1 
ATOM   6612  N  N   . GLU C 1 238 ? -66.747 65.640  123.827 1.00 56.58 ? 238  GLU C N   1 
ATOM   6613  C  CA  . GLU C 1 238 ? -66.603 67.062  123.570 1.00 58.06 ? 238  GLU C CA  1 
ATOM   6614  C  C   . GLU C 1 238 ? -67.720 67.538  122.653 1.00 54.96 ? 238  GLU C C   1 
ATOM   6615  O  O   . GLU C 1 238 ? -68.192 68.679  122.769 1.00 51.26 ? 238  GLU C O   1 
ATOM   6616  C  CB  . GLU C 1 238 ? -65.208 67.368  122.994 1.00 60.49 ? 238  GLU C CB  1 
ATOM   6617  C  CG  . GLU C 1 238 ? -64.468 68.480  123.764 1.00 66.63 ? 238  GLU C CG  1 
ATOM   6618  C  CD  . GLU C 1 238 ? -64.642 68.383  125.302 1.00 70.20 ? 238  GLU C CD  1 
ATOM   6619  O  OE1 . GLU C 1 238 ? -64.407 67.288  125.872 1.00 72.77 ? 238  GLU C OE1 1 
ATOM   6620  O  OE2 . GLU C 1 238 ? -65.008 69.400  125.945 1.00 68.96 ? 238  GLU C OE2 1 
ATOM   6621  N  N   . ILE C 1 239 ? -68.154 66.655  121.756 1.00 53.42 ? 239  ILE C N   1 
ATOM   6622  C  CA  . ILE C 1 239 ? -69.242 66.995  120.845 1.00 53.95 ? 239  ILE C CA  1 
ATOM   6623  C  C   . ILE C 1 239 ? -70.518 67.130  121.670 1.00 54.58 ? 239  ILE C C   1 
ATOM   6624  O  O   . ILE C 1 239 ? -71.265 68.097  121.498 1.00 54.33 ? 239  ILE C O   1 
ATOM   6625  C  CB  . ILE C 1 239 ? -69.462 65.906  119.771 1.00 54.62 ? 239  ILE C CB  1 
ATOM   6626  C  CG1 . ILE C 1 239 ? -68.253 65.836  118.830 1.00 51.81 ? 239  ILE C CG1 1 
ATOM   6627  C  CG2 . ILE C 1 239 ? -70.747 66.201  118.977 1.00 48.54 ? 239  ILE C CG2 1 
ATOM   6628  C  CD1 . ILE C 1 239 ? -68.193 64.523  118.045 1.00 50.80 ? 239  ILE C CD1 1 
ATOM   6629  N  N   . LYS C 1 240 ? -70.763 66.161  122.558 1.00 53.18 ? 240  LYS C N   1 
ATOM   6630  C  CA  . LYS C 1 240 ? -71.934 66.204  123.432 1.00 55.34 ? 240  LYS C CA  1 
ATOM   6631  C  C   . LYS C 1 240 ? -71.941 67.423  124.359 1.00 55.46 ? 240  LYS C C   1 
ATOM   6632  O  O   . LYS C 1 240 ? -72.970 67.721  124.946 1.00 58.21 ? 240  LYS C O   1 
ATOM   6633  C  CB  . LYS C 1 240 ? -72.035 64.940  124.289 1.00 56.11 ? 240  LYS C CB  1 
ATOM   6634  C  CG  . LYS C 1 240 ? -71.950 63.662  123.474 1.00 64.67 ? 240  LYS C CG  1 
ATOM   6635  C  CD  . LYS C 1 240 ? -72.189 62.401  124.318 1.00 70.33 ? 240  LYS C CD  1 
ATOM   6636  C  CE  . LYS C 1 240 ? -73.678 62.073  124.477 1.00 72.79 ? 240  LYS C CE  1 
ATOM   6637  N  NZ  . LYS C 1 240 ? -74.505 63.159  125.081 1.00 72.24 ? 240  LYS C NZ  1 
ATOM   6638  N  N   . GLN C 1 241 ? -70.817 68.121  124.492 1.00 52.61 ? 241  GLN C N   1 
ATOM   6639  C  CA  . GLN C 1 241 ? -70.754 69.293  125.356 1.00 52.61 ? 241  GLN C CA  1 
ATOM   6640  C  C   . GLN C 1 241 ? -70.885 70.553  124.534 1.00 51.92 ? 241  GLN C C   1 
ATOM   6641  O  O   . GLN C 1 241 ? -70.678 71.661  125.045 1.00 51.72 ? 241  GLN C O   1 
ATOM   6642  C  CB  . GLN C 1 241 ? -69.424 69.340  126.110 1.00 57.30 ? 241  GLN C CB  1 
ATOM   6643  C  CG  . GLN C 1 241 ? -69.233 68.219  127.121 1.00 62.28 ? 241  GLN C CG  1 
ATOM   6644  C  CD  . GLN C 1 241 ? -70.321 68.223  128.183 1.00 67.82 ? 241  GLN C CD  1 
ATOM   6645  O  OE1 . GLN C 1 241 ? -70.581 69.249  128.835 1.00 70.75 ? 241  GLN C OE1 1 
ATOM   6646  N  NE2 . GLN C 1 241 ? -70.962 67.080  128.365 1.00 66.32 ? 241  GLN C NE2 1 
ATOM   6647  N  N   . GLY C 1 242 ? -71.188 70.379  123.250 1.00 49.35 ? 242  GLY C N   1 
ATOM   6648  C  CA  . GLY C 1 242 ? -71.340 71.524  122.366 1.00 49.35 ? 242  GLY C CA  1 
ATOM   6649  C  C   . GLY C 1 242 ? -70.078 72.228  121.906 1.00 49.28 ? 242  GLY C C   1 
ATOM   6650  O  O   . GLY C 1 242 ? -70.135 73.370  121.473 1.00 47.79 ? 242  GLY C O   1 
ATOM   6651  N  N   . LYS C 1 243 ? -68.941 71.550  121.971 1.00 53.47 ? 243  LYS C N   1 
ATOM   6652  C  CA  . LYS C 1 243 ? -67.671 72.152  121.561 1.00 56.90 ? 243  LYS C CA  1 
ATOM   6653  C  C   . LYS C 1 243 ? -67.469 72.249  120.042 1.00 56.64 ? 243  LYS C C   1 
ATOM   6654  O  O   . LYS C 1 243 ? -66.697 73.083  119.554 1.00 53.50 ? 243  LYS C O   1 
ATOM   6655  C  CB  . LYS C 1 243 ? -66.505 71.369  122.169 1.00 61.10 ? 243  LYS C CB  1 
ATOM   6656  C  CG  . LYS C 1 243 ? -66.423 71.460  123.678 1.00 67.42 ? 243  LYS C CG  1 
ATOM   6657  C  CD  . LYS C 1 243 ? -66.073 72.876  124.144 1.00 72.00 ? 243  LYS C CD  1 
ATOM   6658  C  CE  . LYS C 1 243 ? -66.121 72.975  125.679 1.00 75.77 ? 243  LYS C CE  1 
ATOM   6659  N  NZ  . LYS C 1 243 ? -65.191 72.018  126.381 1.00 73.53 ? 243  LYS C NZ  1 
ATOM   6660  N  N   . PHE C 1 244 ? -68.175 71.410  119.293 1.00 56.11 ? 244  PHE C N   1 
ATOM   6661  C  CA  . PHE C 1 244 ? -68.020 71.409  117.848 1.00 52.25 ? 244  PHE C CA  1 
ATOM   6662  C  C   . PHE C 1 244 ? -69.211 71.944  117.075 1.00 50.60 ? 244  PHE C C   1 
ATOM   6663  O  O   . PHE C 1 244 ? -69.789 71.261  116.241 1.00 48.16 ? 244  PHE C O   1 
ATOM   6664  C  CB  . PHE C 1 244 ? -67.671 70.003  117.398 1.00 48.50 ? 244  PHE C CB  1 
ATOM   6665  C  CG  . PHE C 1 244 ? -66.315 69.552  117.856 1.00 51.22 ? 244  PHE C CG  1 
ATOM   6666  C  CD1 . PHE C 1 244 ? -65.156 70.053  117.259 1.00 48.57 ? 244  PHE C CD1 1 
ATOM   6667  C  CD2 . PHE C 1 244 ? -66.185 68.633  118.891 1.00 51.06 ? 244  PHE C CD2 1 
ATOM   6668  C  CE1 . PHE C 1 244 ? -63.884 69.645  117.684 1.00 44.43 ? 244  PHE C CE1 1 
ATOM   6669  C  CE2 . PHE C 1 244 ? -64.912 68.221  119.320 1.00 49.66 ? 244  PHE C CE2 1 
ATOM   6670  C  CZ  . PHE C 1 244 ? -63.759 68.735  118.706 1.00 43.35 ? 244  PHE C CZ  1 
ATOM   6671  N  N   . HIS C 1 245 ? -69.575 73.185  117.351 1.00 50.93 ? 245  HIS C N   1 
ATOM   6672  C  CA  . HIS C 1 245 ? -70.684 73.786  116.639 1.00 52.02 ? 245  HIS C CA  1 
ATOM   6673  C  C   . HIS C 1 245 ? -70.160 74.526  115.402 1.00 48.00 ? 245  HIS C C   1 
ATOM   6674  O  O   . HIS C 1 245 ? -70.897 74.747  114.449 1.00 48.35 ? 245  HIS C O   1 
ATOM   6675  C  CB  . HIS C 1 245 ? -71.499 74.714  117.573 1.00 53.32 ? 245  HIS C CB  1 
ATOM   6676  C  CG  . HIS C 1 245 ? -70.696 75.799  118.220 1.00 62.87 ? 245  HIS C CG  1 
ATOM   6677  N  ND1 . HIS C 1 245 ? -70.572 77.062  117.678 1.00 67.53 ? 245  HIS C ND1 1 
ATOM   6678  C  CD2 . HIS C 1 245 ? -69.940 75.797  119.346 1.00 67.34 ? 245  HIS C CD2 1 
ATOM   6679  C  CE1 . HIS C 1 245 ? -69.771 77.791  118.441 1.00 69.02 ? 245  HIS C CE1 1 
ATOM   6680  N  NE2 . HIS C 1 245 ? -69.374 77.046  119.460 1.00 69.59 ? 245  HIS C NE2 1 
ATOM   6681  N  N   . ASN C 1 246 ? -68.882 74.875  115.394 1.00 44.88 ? 246  ASN C N   1 
ATOM   6682  C  CA  . ASN C 1 246 ? -68.325 75.577  114.243 1.00 46.88 ? 246  ASN C CA  1 
ATOM   6683  C  C   . ASN C 1 246 ? -68.183 74.591  113.071 1.00 47.46 ? 246  ASN C C   1 
ATOM   6684  O  O   . ASN C 1 246 ? -67.529 73.552  113.205 1.00 45.24 ? 246  ASN C O   1 
ATOM   6685  C  CB  . ASN C 1 246 ? -66.956 76.175  114.597 1.00 45.46 ? 246  ASN C CB  1 
ATOM   6686  C  CG  . ASN C 1 246 ? -66.466 77.160  113.559 1.00 45.12 ? 246  ASN C CG  1 
ATOM   6687  O  OD1 . ASN C 1 246 ? -66.331 76.825  112.376 1.00 51.38 ? 246  ASN C OD1 1 
ATOM   6688  N  ND2 . ASN C 1 246 ? -66.204 78.380  113.987 1.00 35.52 ? 246  ASN C ND2 1 
ATOM   6689  N  N   . PRO C 1 247 ? -68.801 74.899  111.906 1.00 47.88 ? 247  PRO C N   1 
ATOM   6690  C  CA  . PRO C 1 247 ? -68.688 73.969  110.769 1.00 45.80 ? 247  PRO C CA  1 
ATOM   6691  C  C   . PRO C 1 247 ? -67.249 73.602  110.419 1.00 44.77 ? 247  PRO C C   1 
ATOM   6692  O  O   . PRO C 1 247 ? -66.950 72.438  110.117 1.00 42.21 ? 247  PRO C O   1 
ATOM   6693  C  CB  . PRO C 1 247 ? -69.427 74.694  109.635 1.00 44.01 ? 247  PRO C CB  1 
ATOM   6694  C  CG  . PRO C 1 247 ? -69.430 76.133  110.053 1.00 42.46 ? 247  PRO C CG  1 
ATOM   6695  C  CD  . PRO C 1 247 ? -69.612 76.077  111.543 1.00 44.71 ? 247  PRO C CD  1 
ATOM   6696  N  N   . MET C 1 248 ? -66.361 74.589  110.478 1.00 43.82 ? 248  MET C N   1 
ATOM   6697  C  CA  . MET C 1 248 ? -64.950 74.342  110.189 1.00 44.15 ? 248  MET C CA  1 
ATOM   6698  C  C   . MET C 1 248 ? -64.355 73.373  111.221 1.00 42.48 ? 248  MET C C   1 
ATOM   6699  O  O   . MET C 1 248 ? -63.464 72.580  110.900 1.00 38.93 ? 248  MET C O   1 
ATOM   6700  C  CB  . MET C 1 248 ? -64.132 75.645  110.211 1.00 44.23 ? 248  MET C CB  1 
ATOM   6701  C  CG  . MET C 1 248 ? -62.639 75.410  109.936 1.00 44.63 ? 248  MET C CG  1 
ATOM   6702  S  SD  . MET C 1 248 ? -62.307 74.563  108.335 1.00 46.39 ? 248  MET C SD  1 
ATOM   6703  C  CE  . MET C 1 248 ? -60.565 74.965  108.032 1.00 39.57 ? 248  MET C CE  1 
ATOM   6704  N  N   . SER C 1 249 ? -64.818 73.454  112.467 1.00 40.04 ? 249  SER C N   1 
ATOM   6705  C  CA  . SER C 1 249 ? -64.279 72.547  113.462 1.00 40.57 ? 249  SER C CA  1 
ATOM   6706  C  C   . SER C 1 249 ? -64.824 71.148  113.186 1.00 37.69 ? 249  SER C C   1 
ATOM   6707  O  O   . SER C 1 249 ? -64.164 70.144  113.455 1.00 39.48 ? 249  SER C O   1 
ATOM   6708  C  CB  . SER C 1 249 ? -64.599 73.021  114.890 1.00 40.30 ? 249  SER C CB  1 
ATOM   6709  O  OG  . SER C 1 249 ? -65.957 72.836  115.220 1.00 49.32 ? 249  SER C OG  1 
ATOM   6710  N  N   . ILE C 1 250 ? -66.021 71.074  112.625 1.00 37.57 ? 250  ILE C N   1 
ATOM   6711  C  CA  . ILE C 1 250 ? -66.592 69.776  112.296 1.00 37.37 ? 250  ILE C CA  1 
ATOM   6712  C  C   . ILE C 1 250 ? -65.818 69.178  111.116 1.00 37.65 ? 250  ILE C C   1 
ATOM   6713  O  O   . ILE C 1 250 ? -65.539 67.971  111.056 1.00 38.76 ? 250  ILE C O   1 
ATOM   6714  C  CB  . ILE C 1 250 ? -68.067 69.923  111.940 1.00 35.08 ? 250  ILE C CB  1 
ATOM   6715  C  CG1 . ILE C 1 250 ? -68.770 70.587  113.137 1.00 35.02 ? 250  ILE C CG1 1 
ATOM   6716  C  CG2 . ILE C 1 250 ? -68.655 68.557  111.542 1.00 23.85 ? 250  ILE C CG2 1 
ATOM   6717  C  CD1 . ILE C 1 250 ? -70.207 70.986  112.882 1.00 36.25 ? 250  ILE C CD1 1 
ATOM   6718  N  N   . ALA C 1 251 ? -65.439 70.049  110.195 1.00 36.36 ? 251  ALA C N   1 
ATOM   6719  C  CA  . ALA C 1 251 ? -64.703 69.634  109.028 1.00 37.45 ? 251  ALA C CA  1 
ATOM   6720  C  C   . ALA C 1 251 ? -63.385 68.985  109.398 1.00 43.33 ? 251  ALA C C   1 
ATOM   6721  O  O   . ALA C 1 251 ? -62.949 68.039  108.724 1.00 45.99 ? 251  ALA C O   1 
ATOM   6722  C  CB  . ALA C 1 251 ? -64.454 70.812  108.146 1.00 37.30 ? 251  ALA C CB  1 
ATOM   6723  N  N   . GLN C 1 252 ? -62.741 69.466  110.465 1.00 44.68 ? 252  GLN C N   1 
ATOM   6724  C  CA  . GLN C 1 252 ? -61.461 68.881  110.837 1.00 43.75 ? 252  GLN C CA  1 
ATOM   6725  C  C   . GLN C 1 252 ? -61.530 67.623  111.692 1.00 43.61 ? 252  GLN C C   1 
ATOM   6726  O  O   . GLN C 1 252 ? -60.501 66.988  111.908 1.00 44.87 ? 252  GLN C O   1 
ATOM   6727  C  CB  . GLN C 1 252 ? -60.520 69.947  111.454 1.00 40.63 ? 252  GLN C CB  1 
ATOM   6728  C  CG  . GLN C 1 252 ? -60.183 71.024  110.402 1.00 39.49 ? 252  GLN C CG  1 
ATOM   6729  C  CD  . GLN C 1 252 ? -59.099 72.060  110.781 1.00 38.84 ? 252  GLN C CD  1 
ATOM   6730  O  OE1 . GLN C 1 252 ? -58.928 72.424  111.947 1.00 40.52 ? 252  GLN C OE1 1 
ATOM   6731  N  NE2 . GLN C 1 252 ? -58.398 72.574  109.758 1.00 34.85 ? 252  GLN C NE2 1 
ATOM   6732  N  N   . ILE C 1 253 ? -62.711 67.220  112.159 1.00 40.41 ? 253  ILE C N   1 
ATOM   6733  C  CA  . ILE C 1 253 ? -62.747 65.991  112.948 1.00 40.84 ? 253  ILE C CA  1 
ATOM   6734  C  C   . ILE C 1 253 ? -63.519 64.919  112.267 1.00 39.60 ? 253  ILE C C   1 
ATOM   6735  O  O   . ILE C 1 253 ? -63.285 63.731  112.490 1.00 40.97 ? 253  ILE C O   1 
ATOM   6736  C  CB  . ILE C 1 253 ? -63.404 66.159  114.327 1.00 46.76 ? 253  ILE C CB  1 
ATOM   6737  C  CG1 . ILE C 1 253 ? -64.697 66.946  114.182 1.00 48.65 ? 253  ILE C CG1 1 
ATOM   6738  C  CG2 . ILE C 1 253 ? -62.424 66.804  115.320 1.00 48.74 ? 253  ILE C CG2 1 
ATOM   6739  C  CD1 . ILE C 1 253 ? -65.526 66.964  115.450 1.00 51.38 ? 253  ILE C CD1 1 
ATOM   6740  N  N   . LEU C 1 254 ? -64.461 65.338  111.424 1.00 42.09 ? 254  LEU C N   1 
ATOM   6741  C  CA  . LEU C 1 254 ? -65.328 64.387  110.713 1.00 36.04 ? 254  LEU C CA  1 
ATOM   6742  C  C   . LEU C 1 254 ? -64.533 63.300  110.047 1.00 35.28 ? 254  LEU C C   1 
ATOM   6743  O  O   . LEU C 1 254 ? -64.831 62.108  110.223 1.00 36.86 ? 254  LEU C O   1 
ATOM   6744  C  CB  . LEU C 1 254 ? -66.161 65.076  109.640 1.00 33.18 ? 254  LEU C CB  1 
ATOM   6745  C  CG  . LEU C 1 254 ? -67.665 64.743  109.557 1.00 37.68 ? 254  LEU C CG  1 
ATOM   6746  C  CD1 . LEU C 1 254 ? -68.116 64.873  108.115 1.00 33.72 ? 254  LEU C CD1 1 
ATOM   6747  C  CD2 . LEU C 1 254 ? -67.974 63.352  110.070 1.00 35.60 ? 254  LEU C CD2 1 
ATOM   6748  N  N   . PRO C 1 255 ? -63.503 63.688  109.272 1.00 31.51 ? 255  PRO C N   1 
ATOM   6749  C  CA  . PRO C 1 255 ? -62.712 62.666  108.594 1.00 33.68 ? 255  PRO C CA  1 
ATOM   6750  C  C   . PRO C 1 255 ? -62.268 61.571  109.528 1.00 35.00 ? 255  PRO C C   1 
ATOM   6751  O  O   . PRO C 1 255 ? -62.497 60.385  109.246 1.00 33.52 ? 255  PRO C O   1 
ATOM   6752  C  CB  . PRO C 1 255 ? -61.559 63.463  107.988 1.00 33.61 ? 255  PRO C CB  1 
ATOM   6753  C  CG  . PRO C 1 255 ? -62.231 64.783  107.659 1.00 29.02 ? 255  PRO C CG  1 
ATOM   6754  C  CD  . PRO C 1 255 ? -63.050 65.042  108.900 1.00 29.85 ? 255  PRO C CD  1 
ATOM   6755  N  N   . SER C 1 256 ? -61.664 61.963  110.650 1.00 36.60 ? 256  SER C N   1 
ATOM   6756  C  CA  . SER C 1 256 ? -61.175 60.978  111.615 1.00 37.70 ? 256  SER C CA  1 
ATOM   6757  C  C   . SER C 1 256 ? -62.287 60.111  112.152 1.00 39.01 ? 256  SER C C   1 
ATOM   6758  O  O   . SER C 1 256 ? -62.126 58.880  112.242 1.00 35.98 ? 256  SER C O   1 
ATOM   6759  C  CB  . SER C 1 256 ? -60.455 61.663  112.769 1.00 37.27 ? 256  SER C CB  1 
ATOM   6760  O  OG  . SER C 1 256 ? -59.137 61.965  112.374 1.00 46.20 ? 256  SER C OG  1 
ATOM   6761  N  N   . LEU C 1 257 ? -63.416 60.752  112.489 1.00 39.07 ? 257  LEU C N   1 
ATOM   6762  C  CA  . LEU C 1 257 ? -64.570 60.037  113.018 1.00 39.67 ? 257  LEU C CA  1 
ATOM   6763  C  C   . LEU C 1 257 ? -65.148 59.039  112.023 1.00 39.29 ? 257  LEU C C   1 
ATOM   6764  O  O   . LEU C 1 257 ? -65.881 58.139  112.401 1.00 43.50 ? 257  LEU C O   1 
ATOM   6765  C  CB  . LEU C 1 257 ? -65.636 61.040  113.475 1.00 43.54 ? 257  LEU C CB  1 
ATOM   6766  C  CG  . LEU C 1 257 ? -65.142 61.901  114.649 1.00 44.49 ? 257  LEU C CG  1 
ATOM   6767  C  CD1 . LEU C 1 257 ? -66.169 62.935  115.060 1.00 45.75 ? 257  LEU C CD1 1 
ATOM   6768  C  CD2 . LEU C 1 257 ? -64.853 60.990  115.811 1.00 45.31 ? 257  LEU C CD2 1 
ATOM   6769  N  N   . LYS C 1 258 ? -64.822 59.194  110.745 1.00 39.75 ? 258  LYS C N   1 
ATOM   6770  C  CA  . LYS C 1 258 ? -65.317 58.274  109.733 1.00 37.14 ? 258  LYS C CA  1 
ATOM   6771  C  C   . LYS C 1 258 ? -64.185 57.320  109.330 1.00 37.86 ? 258  LYS C C   1 
ATOM   6772  O  O   . LYS C 1 258 ? -64.343 56.491  108.435 1.00 38.07 ? 258  LYS C O   1 
ATOM   6773  C  CB  . LYS C 1 258 ? -65.839 59.066  108.520 1.00 38.85 ? 258  LYS C CB  1 
ATOM   6774  C  CG  . LYS C 1 258 ? -67.227 59.704  108.698 1.00 38.94 ? 258  LYS C CG  1 
ATOM   6775  C  CD  . LYS C 1 258 ? -68.296 58.633  108.857 1.00 46.09 ? 258  LYS C CD  1 
ATOM   6776  C  CE  . LYS C 1 258 ? -69.682 59.033  108.353 1.00 50.75 ? 258  LYS C CE  1 
ATOM   6777  N  NZ  . LYS C 1 258 ? -70.428 59.865  109.346 1.00 57.33 ? 258  LYS C NZ  1 
ATOM   6778  N  N   . GLY C 1 259 ? -63.037 57.433  109.995 1.00 36.75 ? 259  GLY C N   1 
ATOM   6779  C  CA  . GLY C 1 259 ? -61.921 56.555  109.689 1.00 33.49 ? 259  GLY C CA  1 
ATOM   6780  C  C   . GLY C 1 259 ? -61.208 56.865  108.387 1.00 36.42 ? 259  GLY C C   1 
ATOM   6781  O  O   . GLY C 1 259 ? -60.686 55.971  107.735 1.00 36.66 ? 259  GLY C O   1 
ATOM   6782  N  N   . LYS C 1 260 ? -61.155 58.138  108.016 1.00 36.46 ? 260  LYS C N   1 
ATOM   6783  C  CA  . LYS C 1 260 ? -60.509 58.551  106.764 1.00 37.87 ? 260  LYS C CA  1 
ATOM   6784  C  C   . LYS C 1 260 ? -59.539 59.694  107.035 1.00 38.43 ? 260  LYS C C   1 
ATOM   6785  O  O   . LYS C 1 260 ? -59.529 60.281  108.120 1.00 38.36 ? 260  LYS C O   1 
ATOM   6786  C  CB  . LYS C 1 260 ? -61.555 59.088  105.763 1.00 38.71 ? 260  LYS C CB  1 
ATOM   6787  C  CG  . LYS C 1 260 ? -62.718 58.170  105.446 1.00 37.52 ? 260  LYS C CG  1 
ATOM   6788  C  CD  . LYS C 1 260 ? -62.304 57.170  104.439 1.00 45.02 ? 260  LYS C CD  1 
ATOM   6789  C  CE  . LYS C 1 260 ? -63.479 56.323  103.938 1.00 52.99 ? 260  LYS C CE  1 
ATOM   6790  N  NZ  . LYS C 1 260 ? -63.039 55.220  102.969 1.00 53.81 ? 260  LYS C NZ  1 
ATOM   6791  N  N   . THR C 1 261 ? -58.729 60.032  106.044 1.00 36.09 ? 261  THR C N   1 
ATOM   6792  C  CA  . THR C 1 261 ? -57.835 61.169  106.220 1.00 41.26 ? 261  THR C CA  1 
ATOM   6793  C  C   . THR C 1 261 ? -57.741 61.810  104.864 1.00 40.71 ? 261  THR C C   1 
ATOM   6794  O  O   . THR C 1 261 ? -58.223 61.232  103.892 1.00 41.10 ? 261  THR C O   1 
ATOM   6795  C  CB  . THR C 1 261 ? -56.394 60.782  106.667 1.00 41.58 ? 261  THR C CB  1 
ATOM   6796  O  OG1 . THR C 1 261 ? -55.666 60.255  105.545 1.00 38.41 ? 261  THR C OG1 1 
ATOM   6797  C  CG2 . THR C 1 261 ? -56.446 59.761  107.832 1.00 41.87 ? 261  THR C CG2 1 
ATOM   6798  N  N   . TYR C 1 262 ? -57.136 62.997  104.806 1.00 36.83 ? 262  TYR C N   1 
ATOM   6799  C  CA  . TYR C 1 262 ? -56.944 63.690  103.548 1.00 35.13 ? 262  TYR C CA  1 
ATOM   6800  C  C   . TYR C 1 262 ? -56.193 62.837  102.519 1.00 38.74 ? 262  TYR C C   1 
ATOM   6801  O  O   . TYR C 1 262 ? -56.186 63.167  101.330 1.00 40.34 ? 262  TYR C O   1 
ATOM   6802  C  CB  . TYR C 1 262 ? -56.178 64.980  103.768 1.00 29.83 ? 262  TYR C CB  1 
ATOM   6803  C  CG  . TYR C 1 262 ? -56.952 65.990  104.561 1.00 34.14 ? 262  TYR C CG  1 
ATOM   6804  C  CD1 . TYR C 1 262 ? -58.328 65.858  104.745 1.00 31.39 ? 262  TYR C CD1 1 
ATOM   6805  C  CD2 . TYR C 1 262 ? -56.333 67.136  105.044 1.00 35.71 ? 262  TYR C CD2 1 
ATOM   6806  C  CE1 . TYR C 1 262 ? -59.063 66.846  105.372 1.00 35.43 ? 262  TYR C CE1 1 
ATOM   6807  C  CE2 . TYR C 1 262 ? -57.061 68.141  105.677 1.00 39.09 ? 262  TYR C CE2 1 
ATOM   6808  C  CZ  . TYR C 1 262 ? -58.430 67.997  105.829 1.00 39.26 ? 262  TYR C CZ  1 
ATOM   6809  O  OH  . TYR C 1 262 ? -59.174 69.043  106.347 1.00 38.78 ? 262  TYR C OH  1 
ATOM   6810  N  N   . LEU C 1 263 ? -55.555 61.754  102.963 1.00 38.67 ? 263  LEU C N   1 
ATOM   6811  C  CA  . LEU C 1 263 ? -54.832 60.882  102.044 1.00 41.16 ? 263  LEU C CA  1 
ATOM   6812  C  C   . LEU C 1 263 ? -55.802 60.008  101.265 1.00 40.90 ? 263  LEU C C   1 
ATOM   6813  O  O   . LEU C 1 263 ? -55.441 59.428  100.255 1.00 42.65 ? 263  LEU C O   1 
ATOM   6814  C  CB  . LEU C 1 263 ? -53.837 59.981  102.801 1.00 39.67 ? 263  LEU C CB  1 
ATOM   6815  C  CG  . LEU C 1 263 ? -52.696 60.696  103.508 1.00 39.21 ? 263  LEU C CG  1 
ATOM   6816  C  CD1 . LEU C 1 263 ? -51.699 59.676  103.987 1.00 38.28 ? 263  LEU C CD1 1 
ATOM   6817  C  CD2 . LEU C 1 263 ? -52.045 61.701  102.549 1.00 35.09 ? 263  LEU C CD2 1 
ATOM   6818  N  N   . ASP C 1 264 ? -57.035 59.905  101.745 1.00 43.11 ? 264  ASP C N   1 
ATOM   6819  C  CA  . ASP C 1 264 ? -58.034 59.072  101.085 1.00 44.32 ? 264  ASP C CA  1 
ATOM   6820  C  C   . ASP C 1 264 ? -58.757 59.820  99.956  1.00 43.32 ? 264  ASP C C   1 
ATOM   6821  O  O   . ASP C 1 264 ? -59.460 59.221  99.157  1.00 40.27 ? 264  ASP C O   1 
ATOM   6822  C  CB  . ASP C 1 264 ? -59.042 58.561  102.128 1.00 46.60 ? 264  ASP C CB  1 
ATOM   6823  C  CG  . ASP C 1 264 ? -58.378 57.716  103.223 1.00 52.93 ? 264  ASP C CG  1 
ATOM   6824  O  OD1 . ASP C 1 264 ? -57.598 56.796  102.889 1.00 56.76 ? 264  ASP C OD1 1 
ATOM   6825  O  OD2 . ASP C 1 264 ? -58.639 57.958  104.422 1.00 56.16 ? 264  ASP C OD2 1 
ATOM   6826  N  N   . VAL C 1 265 ? -58.558 61.135  99.906  1.00 43.36 ? 265  VAL C N   1 
ATOM   6827  C  CA  . VAL C 1 265 ? -59.174 62.005  98.907  1.00 40.50 ? 265  VAL C CA  1 
ATOM   6828  C  C   . VAL C 1 265 ? -59.071 61.498  97.480  1.00 38.00 ? 265  VAL C C   1 
ATOM   6829  O  O   . VAL C 1 265 ? -60.032 61.555  96.725  1.00 39.61 ? 265  VAL C O   1 
ATOM   6830  C  CB  . VAL C 1 265 ? -58.560 63.430  98.953  1.00 38.53 ? 265  VAL C CB  1 
ATOM   6831  C  CG1 . VAL C 1 265 ? -58.954 64.208  97.717  1.00 36.19 ? 265  VAL C CG1 1 
ATOM   6832  C  CG2 . VAL C 1 265 ? -59.036 64.161  100.206 1.00 37.93 ? 265  VAL C CG2 1 
ATOM   6833  N  N   . PRO C 1 266 ? -57.898 61.015  97.081  1.00 34.24 ? 266  PRO C N   1 
ATOM   6834  C  CA  . PRO C 1 266 ? -57.838 60.548  95.705  1.00 32.16 ? 266  PRO C CA  1 
ATOM   6835  C  C   . PRO C 1 266 ? -58.694 59.325  95.427  1.00 32.05 ? 266  PRO C C   1 
ATOM   6836  O  O   . PRO C 1 266 ? -59.045 59.052  94.277  1.00 32.40 ? 266  PRO C O   1 
ATOM   6837  C  CB  . PRO C 1 266 ? -56.351 60.299  95.502  1.00 30.98 ? 266  PRO C CB  1 
ATOM   6838  C  CG  . PRO C 1 266 ? -55.721 61.348  96.368  1.00 32.85 ? 266  PRO C CG  1 
ATOM   6839  C  CD  . PRO C 1 266 ? -56.546 61.240  97.616  1.00 35.49 ? 266  PRO C CD  1 
ATOM   6840  N  N   . GLN C 1 267 ? -59.038 58.591  96.473  1.00 33.10 ? 267  GLN C N   1 
ATOM   6841  C  CA  . GLN C 1 267 ? -59.829 57.379  96.309  1.00 36.56 ? 267  GLN C CA  1 
ATOM   6842  C  C   . GLN C 1 267 ? -61.324 57.599  96.482  1.00 36.06 ? 267  GLN C C   1 
ATOM   6843  O  O   . GLN C 1 267 ? -62.087 56.648  96.559  1.00 38.17 ? 267  GLN C O   1 
ATOM   6844  C  CB  . GLN C 1 267 ? -59.368 56.301  97.301  1.00 38.07 ? 267  GLN C CB  1 
ATOM   6845  C  CG  . GLN C 1 267 ? -58.017 55.693  96.998  1.00 49.09 ? 267  GLN C CG  1 
ATOM   6846  C  CD  . GLN C 1 267 ? -56.839 56.618  97.337  1.00 60.36 ? 267  GLN C CD  1 
ATOM   6847  O  OE1 . GLN C 1 267 ? -56.512 56.843  98.517  1.00 64.02 ? 267  GLN C OE1 1 
ATOM   6848  N  NE2 . GLN C 1 267 ? -56.193 57.156  96.298  1.00 64.39 ? 267  GLN C NE2 1 
ATOM   6849  N  N   . VAL C 1 268 ? -61.759 58.844  96.552  1.00 37.26 ? 268  VAL C N   1 
ATOM   6850  C  CA  . VAL C 1 268 ? -63.176 59.088  96.754  1.00 41.35 ? 268  VAL C CA  1 
ATOM   6851  C  C   . VAL C 1 268 ? -64.052 58.646  95.575  1.00 42.72 ? 268  VAL C C   1 
ATOM   6852  O  O   . VAL C 1 268 ? -63.755 58.950  94.428  1.00 46.57 ? 268  VAL C O   1 
ATOM   6853  C  CB  . VAL C 1 268 ? -63.431 60.573  97.070  1.00 40.27 ? 268  VAL C CB  1 
ATOM   6854  C  CG1 . VAL C 1 268 ? -64.894 60.902  96.899  1.00 42.48 ? 268  VAL C CG1 1 
ATOM   6855  C  CG2 . VAL C 1 268 ? -63.004 60.868  98.507  1.00 42.01 ? 268  VAL C CG2 1 
ATOM   6856  N  N   . THR C 1 269 ? -65.116 57.908  95.882  1.00 41.25 ? 269  THR C N   1 
ATOM   6857  C  CA  . THR C 1 269 ? -66.084 57.419  94.909  1.00 39.28 ? 269  THR C CA  1 
ATOM   6858  C  C   . THR C 1 269 ? -67.156 58.487  94.772  1.00 41.96 ? 269  THR C C   1 
ATOM   6859  O  O   . THR C 1 269 ? -67.731 58.913  95.766  1.00 46.14 ? 269  THR C O   1 
ATOM   6860  C  CB  . THR C 1 269 ? -66.778 56.141  95.422  1.00 37.42 ? 269  THR C CB  1 
ATOM   6861  O  OG1 . THR C 1 269 ? -65.870 55.035  95.359  1.00 41.70 ? 269  THR C OG1 1 
ATOM   6862  C  CG2 . THR C 1 269 ? -67.999 55.834  94.606  1.00 39.05 ? 269  THR C CG2 1 
ATOM   6863  N  N   . CYS C 1 270 ? -67.448 58.923  93.557  1.00 45.45 ? 270  CYS C N   1 
ATOM   6864  C  CA  . CYS C 1 270 ? -68.493 59.920  93.384  1.00 52.41 ? 270  CYS C CA  1 
ATOM   6865  C  C   . CYS C 1 270 ? -69.824 59.347  92.917  1.00 59.23 ? 270  CYS C C   1 
ATOM   6866  O  O   . CYS C 1 270 ? -69.867 58.448  92.070  1.00 57.37 ? 270  CYS C O   1 
ATOM   6867  C  CB  . CYS C 1 270 ? -68.035 61.004  92.434  1.00 49.82 ? 270  CYS C CB  1 
ATOM   6868  S  SG  . CYS C 1 270 ? -66.644 61.951  93.114  1.00 50.69 ? 270  CYS C SG  1 
ATOM   6869  N  N   . SER C 1 271 ? -70.902 59.903  93.475  1.00 69.35 ? 271  SER C N   1 
ATOM   6870  C  CA  . SER C 1 271 ? -72.288 59.483  93.208  1.00 80.46 ? 271  SER C CA  1 
ATOM   6871  C  C   . SER C 1 271 ? -72.453 58.037  93.698  1.00 87.12 ? 271  SER C C   1 
ATOM   6872  O  O   . SER C 1 271 ? -72.824 57.151  92.923  1.00 86.93 ? 271  SER C O   1 
ATOM   6873  C  CB  . SER C 1 271 ? -72.622 59.578  91.709  1.00 80.19 ? 271  SER C CB  1 
ATOM   6874  O  OG  . SER C 1 271 ? -74.018 59.698  91.504  1.00 78.43 ? 271  SER C OG  1 
ATOM   6875  N  N   . PRO C 1 272 ? -72.173 57.795  95.006  1.00 93.92 ? 272  PRO C N   1 
ATOM   6876  C  CA  . PRO C 1 272 ? -72.236 56.512  95.736  1.00 97.03 ? 272  PRO C CA  1 
ATOM   6877  C  C   . PRO C 1 272 ? -73.520 55.684  95.615  1.00 99.00 ? 272  PRO C C   1 
ATOM   6878  O  O   . PRO C 1 272 ? -74.636 56.222  95.630  1.00 99.45 ? 272  PRO C O   1 
ATOM   6879  C  CB  . PRO C 1 272 ? -71.954 56.922  97.191  1.00 97.42 ? 272  PRO C CB  1 
ATOM   6880  C  CG  . PRO C 1 272 ? -71.042 58.109  97.031  1.00 97.16 ? 272  PRO C CG  1 
ATOM   6881  C  CD  . PRO C 1 272 ? -71.742 58.877  95.920  1.00 95.18 ? 272  PRO C CD  1 
ATOM   6882  N  N   . ASP C 1 273 ? -73.345 54.366  95.513  1.00 99.45 ? 273  ASP C N   1 
ATOM   6883  C  CA  . ASP C 1 273 ? -74.469 53.441  95.397  1.00 99.45 ? 273  ASP C CA  1 
ATOM   6884  C  C   . ASP C 1 273 ? -75.078 53.174  96.776  1.00 99.45 ? 273  ASP C C   1 
ATOM   6885  O  O   . ASP C 1 273 ? -74.996 52.061  97.298  1.00 99.45 ? 273  ASP C O   1 
ATOM   6886  C  CB  . ASP C 1 273 ? -74.006 52.120  94.761  1.00 99.45 ? 273  ASP C CB  1 
ATOM   6887  C  CG  . ASP C 1 273 ? -74.795 51.768  93.511  1.00 99.45 ? 273  ASP C CG  1 
ATOM   6888  O  OD1 . ASP C 1 273 ? -76.050 51.765  93.590  1.00 99.45 ? 273  ASP C OD1 1 
ATOM   6889  O  OD2 . ASP C 1 273 ? -74.159 51.496  92.461  1.00 96.02 ? 273  ASP C OD2 1 
ATOM   6890  N  N   . THR C 1 289 ? -80.124 99.629  121.546 1.00 87.28 ? 289  THR C N   1 
ATOM   6891  C  CA  . THR C 1 289 ? -79.666 98.271  121.081 1.00 90.08 ? 289  THR C CA  1 
ATOM   6892  C  C   . THR C 1 289 ? -79.014 97.530  122.281 1.00 92.63 ? 289  THR C C   1 
ATOM   6893  O  O   . THR C 1 289 ? -78.253 96.603  122.082 1.00 93.98 ? 289  THR C O   1 
ATOM   6894  C  CB  . THR C 1 289 ? -78.533 98.448  119.968 1.00 87.48 ? 289  THR C CB  1 
ATOM   6895  O  OG1 . THR C 1 289 ? -79.096 98.917  118.735 0.00 87.94 ? 289  THR C OG1 1 
ATOM   6896  C  CG2 . THR C 1 289 ? -77.777 97.067  119.754 0.00 87.94 ? 289  THR C CG2 1 
ATOM   6897  N  N   . SER C 1 290 ? -79.364 97.855  123.505 1.00 99.17 ? 290  SER C N   1 
ATOM   6898  C  CA  . SER C 1 290 ? -78.450 97.270  124.447 1.00 99.05 ? 290  SER C CA  1 
ATOM   6899  C  C   . SER C 1 290 ? -78.493 96.289  125.608 1.00 99.09 ? 290  SER C C   1 
ATOM   6900  O  O   . SER C 1 290 ? -78.883 95.159  125.438 1.00 98.76 ? 290  SER C O   1 
ATOM   6901  C  CB  . SER C 1 290 ? -77.584 98.414  124.943 1.00 99.17 ? 290  SER C CB  1 
ATOM   6902  O  OG  . SER C 1 290 ? -76.424 97.860  125.530 1.00 99.17 ? 290  SER C OG  1 
ATOM   6903  N  N   . ALA C 1 291 ? -77.882 96.807  126.695 1.00 99.07 ? 291  ALA C N   1 
ATOM   6904  C  CA  . ALA C 1 291 ? -77.624 96.236  128.030 1.00 98.96 ? 291  ALA C CA  1 
ATOM   6905  C  C   . ALA C 1 291 ? -78.323 94.953  128.387 1.00 99.04 ? 291  ALA C C   1 
ATOM   6906  O  O   . ALA C 1 291 ? -79.257 94.570  127.702 1.00 99.17 ? 291  ALA C O   1 
ATOM   6907  C  CB  . ALA C 1 291 ? -77.903 97.262  129.108 1.00 98.73 ? 291  ALA C CB  1 
ATOM   6908  N  N   . SER C 1 292 ? -77.884 94.292  129.466 1.00 98.91 ? 292  SER C N   1 
ATOM   6909  C  CA  . SER C 1 292 ? -78.563 93.049  129.810 1.00 99.02 ? 292  SER C CA  1 
ATOM   6910  C  C   . SER C 1 292 ? -78.390 92.339  131.157 1.00 98.95 ? 292  SER C C   1 
ATOM   6911  O  O   . SER C 1 292 ? -79.244 92.526  132.046 1.00 99.17 ? 292  SER C O   1 
ATOM   6912  C  CB  . SER C 1 292 ? -78.342 92.048  128.705 1.00 99.17 ? 292  SER C CB  1 
ATOM   6913  O  OG  . SER C 1 292 ? -77.526 92.601  127.677 1.00 99.17 ? 292  SER C OG  1 
ATOM   6914  N  N   . ASN C 1 293 ? -77.330 91.542  131.353 1.00 96.32 ? 293  ASN C N   1 
ATOM   6915  C  CA  . ASN C 1 293 ? -77.126 90.838  132.643 1.00 97.36 ? 293  ASN C CA  1 
ATOM   6916  C  C   . ASN C 1 293 ? -75.705 90.585  133.026 1.00 97.80 ? 293  ASN C C   1 
ATOM   6917  O  O   . ASN C 1 293 ? -75.415 90.157  134.150 1.00 97.88 ? 293  ASN C O   1 
ATOM   6918  C  CB  . ASN C 1 293 ? -77.723 89.425  132.679 1.00 97.90 ? 293  ASN C CB  1 
ATOM   6919  C  CG  . ASN C 1 293 ? -79.197 89.391  132.448 1.00 99.45 ? 293  ASN C CG  1 
ATOM   6920  O  OD1 . ASN C 1 293 ? -79.900 90.355  132.715 1.00 99.45 ? 293  ASN C OD1 1 
ATOM   6921  N  ND2 . ASN C 1 293 ? -79.688 88.256  131.960 1.00 98.62 ? 293  ASN C ND2 1 
ATOM   6922  N  N   . ILE C 1 294 ? -74.827 90.761  132.069 1.00 97.97 ? 294  ILE C N   1 
ATOM   6923  C  CA  . ILE C 1 294 ? -73.451 90.464  132.311 1.00 97.71 ? 294  ILE C CA  1 
ATOM   6924  C  C   . ILE C 1 294 ? -72.675 91.687  131.913 1.00 96.69 ? 294  ILE C C   1 
ATOM   6925  O  O   . ILE C 1 294 ? -73.120 92.475  131.068 1.00 93.60 ? 294  ILE C O   1 
ATOM   6926  C  CB  . ILE C 1 294 ? -73.075 89.207  131.481 1.00 99.24 ? 294  ILE C CB  1 
ATOM   6927  C  CG1 . ILE C 1 294 ? -73.041 87.979  132.401 1.00 97.73 ? 294  ILE C CG1 1 
ATOM   6928  C  CG2 . ILE C 1 294 ? -71.821 89.456  130.655 1.00 99.45 ? 294  ILE C CG2 1 
ATOM   6929  C  CD1 . ILE C 1 294 ? -71.682 87.357  132.578 1.00 99.21 ? 294  ILE C CD1 1 
ATOM   6930  N  N   . THR C 1 295 ? -71.540 91.878  132.563 1.00 96.81 ? 295  THR C N   1 
ATOM   6931  C  CA  . THR C 1 295 ? -70.726 93.025  132.235 1.00 98.50 ? 295  THR C CA  1 
ATOM   6932  C  C   . THR C 1 295 ? -69.315 92.512  132.019 1.00 97.29 ? 295  THR C C   1 
ATOM   6933  O  O   . THR C 1 295 ? -68.776 91.734  132.820 1.00 97.05 ? 295  THR C O   1 
ATOM   6934  C  CB  . THR C 1 295 ? -70.762 94.109  133.357 1.00 99.45 ? 295  THR C CB  1 
ATOM   6935  O  OG1 . THR C 1 295 ? -69.677 93.896  134.269 1.00 99.45 ? 295  THR C OG1 1 
ATOM   6936  C  CG2 . THR C 1 295 ? -72.102 94.059  134.120 1.00 99.22 ? 295  THR C CG2 1 
ATOM   6937  N  N   . VAL C 1 296 ? -68.725 92.933  130.912 1.00 95.11 ? 296  VAL C N   1 
ATOM   6938  C  CA  . VAL C 1 296 ? -67.387 92.494  130.588 1.00 93.15 ? 296  VAL C CA  1 
ATOM   6939  C  C   . VAL C 1 296 ? -66.465 93.702  130.468 1.00 91.17 ? 296  VAL C C   1 
ATOM   6940  O  O   . VAL C 1 296 ? -66.880 94.797  130.062 1.00 90.37 ? 296  VAL C O   1 
ATOM   6941  C  CB  . VAL C 1 296 ? -67.366 91.684  129.253 1.00 93.92 ? 296  VAL C CB  1 
ATOM   6942  C  CG1 . VAL C 1 296 ? -66.389 90.503  129.380 1.00 92.45 ? 296  VAL C CG1 1 
ATOM   6943  C  CG2 . VAL C 1 296 ? -68.780 91.196  128.888 1.00 92.85 ? 296  VAL C CG2 1 
ATOM   6944  N  N   . ILE C 1 297 ? -65.205 93.477  130.823 1.00 89.28 ? 297  ILE C N   1 
ATOM   6945  C  CA  . ILE C 1 297 ? -64.164 94.501  130.786 1.00 89.10 ? 297  ILE C CA  1 
ATOM   6946  C  C   . ILE C 1 297 ? -63.274 94.276  129.544 1.00 87.20 ? 297  ILE C C   1 
ATOM   6947  O  O   . ILE C 1 297 ? -62.524 93.296  129.458 1.00 85.87 ? 297  ILE C O   1 
ATOM   6948  C  CB  . ILE C 1 297 ? -63.355 94.413  132.092 1.00 87.59 ? 297  ILE C CB  1 
ATOM   6949  C  CG1 . ILE C 1 297 ? -64.054 93.434  133.040 0.00 88.43 ? 297  ILE C CG1 1 
ATOM   6950  C  CG2 . ILE C 1 297 ? -63.297 95.788  132.761 0.00 89.19 ? 297  ILE C CG2 1 
ATOM   6951  C  CD1 . ILE C 1 297 ? -63.116 92.733  133.990 0.00 88.76 ? 297  ILE C CD1 1 
ATOM   6952  N  N   . TYR C 1 298 ? -63.370 95.196  128.591 1.00 87.33 ? 298  TYR C N   1 
ATOM   6953  C  CA  . TYR C 1 298 ? -62.644 95.071  127.342 1.00 90.34 ? 298  TYR C CA  1 
ATOM   6954  C  C   . TYR C 1 298 ? -61.557 96.126  127.089 1.00 90.70 ? 298  TYR C C   1 
ATOM   6955  O  O   . TYR C 1 298 ? -61.831 97.311  126.893 1.00 90.88 ? 298  TYR C O   1 
ATOM   6956  C  CB  . TYR C 1 298 ? -63.682 95.035  126.197 1.00 91.38 ? 298  TYR C CB  1 
ATOM   6957  C  CG  . TYR C 1 298 ? -63.149 94.869  124.787 1.00 92.35 ? 298  TYR C CG  1 
ATOM   6958  C  CD1 . TYR C 1 298 ? -62.068 94.026  124.511 1.00 93.83 ? 298  TYR C CD1 1 
ATOM   6959  C  CD2 . TYR C 1 298 ? -63.751 95.537  123.721 1.00 94.05 ? 298  TYR C CD2 1 
ATOM   6960  C  CE1 . TYR C 1 298 ? -61.596 93.854  123.203 1.00 94.91 ? 298  TYR C CE1 1 
ATOM   6961  C  CE2 . TYR C 1 298 ? -63.290 95.373  122.407 1.00 96.14 ? 298  TYR C CE2 1 
ATOM   6962  C  CZ  . TYR C 1 298 ? -62.212 94.529  122.155 1.00 95.51 ? 298  TYR C CZ  1 
ATOM   6963  O  OH  . TYR C 1 298 ? -61.764 94.357  120.860 1.00 93.49 ? 298  TYR C OH  1 
ATOM   6964  N  N   . THR C 1 299 ? -60.318 95.645  127.078 1.00 91.57 ? 299  THR C N   1 
ATOM   6965  C  CA  . THR C 1 299 ? -59.117 96.436  126.843 1.00 92.19 ? 299  THR C CA  1 
ATOM   6966  C  C   . THR C 1 299 ? -58.625 96.261  125.402 1.00 93.33 ? 299  THR C C   1 
ATOM   6967  O  O   . THR C 1 299 ? -58.622 95.146  124.878 1.00 93.14 ? 299  THR C O   1 
ATOM   6968  C  CB  . THR C 1 299 ? -57.973 95.934  127.719 1.00 92.47 ? 299  THR C CB  1 
ATOM   6969  O  OG1 . THR C 1 299 ? -58.459 94.920  128.603 1.00 91.70 ? 299  THR C OG1 1 
ATOM   6970  C  CG2 . THR C 1 299 ? -57.409 97.025  128.517 1.00 90.39 ? 299  THR C CG2 1 
ATOM   6971  N  N   . ILE C 1 300 ? -58.192 97.349  124.770 1.00 93.62 ? 300  ILE C N   1 
ATOM   6972  C  CA  . ILE C 1 300 ? -57.644 97.276  123.416 1.00 93.43 ? 300  ILE C CA  1 
ATOM   6973  C  C   . ILE C 1 300 ? -56.249 97.900  123.506 1.00 93.15 ? 300  ILE C C   1 
ATOM   6974  O  O   . ILE C 1 300 ? -56.082 98.979  124.062 1.00 93.14 ? 300  ILE C O   1 
ATOM   6975  C  CB  . ILE C 1 300 ? -58.532 98.014  122.391 1.00 93.24 ? 300  ILE C CB  1 
ATOM   6976  C  CG1 . ILE C 1 300 ? -58.304 99.521  122.448 1.00 94.36 ? 300  ILE C CG1 1 
ATOM   6977  C  CG2 . ILE C 1 300 ? -59.980 97.695  122.666 1.00 90.34 ? 300  ILE C CG2 1 
ATOM   6978  C  CD1 . ILE C 1 300 ? -59.119 100.291 121.412 1.00 96.57 ? 300  ILE C CD1 1 
ATOM   6979  N  N   . ASN C 1 301 ? -55.248 97.227  122.953 1.00 93.90 ? 301  ASN C N   1 
ATOM   6980  C  CA  . ASN C 1 301 ? -53.866 97.695  123.080 1.00 94.87 ? 301  ASN C CA  1 
ATOM   6981  C  C   . ASN C 1 301 ? -53.061 97.829  121.778 1.00 94.73 ? 301  ASN C C   1 
ATOM   6982  O  O   . ASN C 1 301 ? -53.520 97.428  120.714 1.00 97.37 ? 301  ASN C O   1 
ATOM   6983  C  CB  . ASN C 1 301 ? -53.148 96.736  124.041 1.00 95.40 ? 301  ASN C CB  1 
ATOM   6984  C  CG  . ASN C 1 301 ? -51.984 97.375  124.745 1.00 95.81 ? 301  ASN C CG  1 
ATOM   6985  O  OD1 . ASN C 1 301 ? -51.759 98.587  124.631 1.00 95.93 ? 301  ASN C OD1 1 
ATOM   6986  N  ND2 . ASN C 1 301 ? -51.232 96.566  125.492 1.00 95.53 ? 301  ASN C ND2 1 
ATOM   6987  N  N   . ASN C 1 302 ? -51.853 98.383  121.882 1.00 94.49 ? 302  ASN C N   1 
ATOM   6988  C  CA  . ASN C 1 302 ? -50.955 98.571  120.739 1.00 94.86 ? 302  ASN C CA  1 
ATOM   6989  C  C   . ASN C 1 302 ? -49.622 99.111  121.266 1.00 95.66 ? 302  ASN C C   1 
ATOM   6990  O  O   . ASN C 1 302 ? -49.590 99.769  122.297 1.00 95.71 ? 302  ASN C O   1 
ATOM   6991  C  CB  . ASN C 1 302 ? -51.581 99.564  119.745 1.00 93.21 ? 302  ASN C CB  1 
ATOM   6992  C  CG  . ASN C 1 302 ? -50.715 99.811  118.513 1.00 93.67 ? 302  ASN C CG  1 
ATOM   6993  O  OD1 . ASN C 1 302 ? -51.171 100.346 117.534 1.00 93.19 ? 302  ASN C OD1 1 
ATOM   6994  N  ND2 . ASN C 1 302 ? -49.471 99.441  118.568 1.00 91.94 ? 302  ASN C ND2 1 
ATOM   6995  N  N   . GLN C 1 303 ? -48.528 98.834  120.566 1.00 96.57 ? 303  GLN C N   1 
ATOM   6996  C  CA  . GLN C 1 303 ? -47.214 99.318  120.974 1.00 96.11 ? 303  GLN C CA  1 
ATOM   6997  C  C   . GLN C 1 303 ? -46.344 99.343  119.732 1.00 96.89 ? 303  GLN C C   1 
ATOM   6998  O  O   . GLN C 1 303 ? -45.945 98.226  119.342 1.00 97.27 ? 303  GLN C O   1 
ATOM   6999  C  CB  . GLN C 1 303 ? -46.601 98.344  121.987 1.00 94.42 ? 303  GLN C CB  1 
ATOM   7000  C  CG  . GLN C 1 303 ? -47.148 98.518  123.377 1.00 94.00 ? 303  GLN C CG  1 
ATOM   7001  C  CD  . GLN C 1 303 ? -47.589 97.234  124.007 1.00 93.99 ? 303  GLN C CD  1 
ATOM   7002  O  OE1 . GLN C 1 303 ? -47.668 97.142  125.229 1.00 91.97 ? 303  GLN C OE1 1 
ATOM   7003  N  NE2 . GLN C 1 303 ? -47.898 96.229  123.182 1.00 98.18 ? 303  GLN C NE2 1 
ATOM   7004  N  N   . LEU C 1 304 ? -46.023 100.517 119.115 1.00 98.46 ? 304  LEU C N   1 
ATOM   7005  C  CA  . LEU C 1 304 ? -45.169 100.420 117.901 1.00 99.14 ? 304  LEU C CA  1 
ATOM   7006  C  C   . LEU C 1 304 ? -44.267 101.265 116.977 1.00 99.45 ? 304  LEU C C   1 
ATOM   7007  O  O   . LEU C 1 304 ? -43.602 102.235 117.367 1.00 99.45 ? 304  LEU C O   1 
ATOM   7008  C  CB  . LEU C 1 304 ? -45.906 99.559  116.900 1.00 99.13 ? 304  LEU C CB  1 
ATOM   7009  C  CG  . LEU C 1 304 ? -44.939 98.351  117.129 1.00 98.98 ? 304  LEU C CG  1 
ATOM   7010  C  CD1 . LEU C 1 304 ? -44.212 98.177  115.924 1.00 98.40 ? 304  LEU C CD1 1 
ATOM   7011  C  CD2 . LEU C 1 304 ? -43.743 98.476  118.261 1.00 97.33 ? 304  LEU C CD2 1 
ATOM   7012  N  N   . ARG C 1 305 ? -44.171 100.670 115.764 1.00 99.45 ? 305  ARG C N   1 
ATOM   7013  C  CA  . ARG C 1 305 ? -43.439 101.067 114.542 1.00 99.45 ? 305  ARG C CA  1 
ATOM   7014  C  C   . ARG C 1 305 ? -44.302 102.241 114.134 1.00 99.45 ? 305  ARG C C   1 
ATOM   7015  O  O   . ARG C 1 305 ? -44.386 103.171 114.943 1.00 99.45 ? 305  ARG C O   1 
ATOM   7016  C  CB  . ARG C 1 305 ? -43.508 99.978  113.419 1.00 99.45 ? 305  ARG C CB  1 
ATOM   7017  C  CG  . ARG C 1 305 ? -42.952 98.550  113.708 1.00 99.45 ? 305  ARG C CG  1 
ATOM   7018  C  CD  . ARG C 1 305 ? -43.747 97.470  112.953 1.00 99.42 ? 305  ARG C CD  1 
ATOM   7019  N  NE  . ARG C 1 305 ? -42.854 96.448  112.425 1.00 99.45 ? 305  ARG C NE  1 
ATOM   7020  C  CZ  . ARG C 1 305 ? -43.149 95.660  111.394 1.00 99.45 ? 305  ARG C CZ  1 
ATOM   7021  N  NH1 . ARG C 1 305 ? -44.325 95.778  110.781 1.00 98.79 ? 305  ARG C NH1 1 
ATOM   7022  N  NH2 . ARG C 1 305 ? -42.261 94.767  110.963 1.00 99.45 ? 305  ARG C NH2 1 
ATOM   7023  N  N   . GLY C 1 306 ? -44.965 102.179 112.955 1.00 99.45 ? 306  GLY C N   1 
ATOM   7024  C  CA  . GLY C 1 306 ? -45.824 103.273 112.484 1.00 99.45 ? 306  GLY C CA  1 
ATOM   7025  C  C   . GLY C 1 306 ? -46.573 104.004 113.600 1.00 99.45 ? 306  GLY C C   1 
ATOM   7026  O  O   . GLY C 1 306 ? -47.704 104.466 113.419 1.00 99.45 ? 306  GLY C O   1 
ATOM   7027  N  N   . VAL C 1 307 ? -45.897 104.133 114.742 1.00 99.45 ? 307  VAL C N   1 
ATOM   7028  C  CA  . VAL C 1 307 ? -46.366 104.750 115.983 1.00 99.45 ? 307  VAL C CA  1 
ATOM   7029  C  C   . VAL C 1 307 ? -47.866 104.523 116.215 1.00 99.45 ? 307  VAL C C   1 
ATOM   7030  O  O   . VAL C 1 307 ? -48.394 103.429 115.943 1.00 99.45 ? 307  VAL C O   1 
ATOM   7031  C  CB  . VAL C 1 307 ? -45.997 106.280 116.035 1.00 98.40 ? 307  VAL C CB  1 
ATOM   7032  C  CG1 . VAL C 1 307 ? -44.467 106.459 116.037 1.00 96.81 ? 307  VAL C CG1 1 
ATOM   7033  C  CG2 . VAL C 1 307 ? -46.621 107.019 114.864 1.00 97.26 ? 307  VAL C CG2 1 
ATOM   7034  N  N   . GLU C 1 308 ? -48.545 105.540 116.741 1.00 99.45 ? 308  GLU C N   1 
ATOM   7035  C  CA  . GLU C 1 308 ? -49.981 105.449 117.002 1.00 99.45 ? 308  GLU C CA  1 
ATOM   7036  C  C   . GLU C 1 308 ? -50.312 104.449 118.096 1.00 99.45 ? 308  GLU C C   1 
ATOM   7037  O  O   . GLU C 1 308 ? -51.060 103.503 117.866 1.00 99.02 ? 308  GLU C O   1 
ATOM   7038  C  CB  . GLU C 1 308 ? -50.719 105.000 115.756 1.00 99.09 ? 308  GLU C CB  1 
ATOM   7039  C  CG  . GLU C 1 308 ? -52.179 104.938 115.994 1.00 99.45 ? 308  GLU C CG  1 
ATOM   7040  C  CD  . GLU C 1 308 ? -52.782 106.262 115.703 1.00 99.45 ? 308  GLU C CD  1 
ATOM   7041  O  OE1 . GLU C 1 308 ? -52.569 106.667 114.615 1.00 98.72 ? 308  GLU C OE1 1 
ATOM   7042  O  OE2 . GLU C 1 308 ? -53.435 106.941 116.479 1.00 99.45 ? 308  GLU C OE2 1 
ATOM   7043  N  N   . LEU C 1 309 ? -49.774 104.646 119.286 1.00 99.45 ? 309  LEU C N   1 
ATOM   7044  C  CA  . LEU C 1 309 ? -50.048 103.705 120.352 1.00 99.44 ? 309  LEU C CA  1 
ATOM   7045  C  C   . LEU C 1 309 ? -51.408 103.953 120.988 1.00 99.23 ? 309  LEU C C   1 
ATOM   7046  O  O   . LEU C 1 309 ? -51.899 105.079 121.031 1.00 99.45 ? 309  LEU C O   1 
ATOM   7047  C  CB  . LEU C 1 309 ? -48.938 103.773 121.402 1.00 99.28 ? 309  LEU C CB  1 
ATOM   7048  C  CG  . LEU C 1 309 ? -47.530 103.765 120.804 1.00 98.99 ? 309  LEU C CG  1 
ATOM   7049  C  CD1 . LEU C 1 309 ? -46.496 103.590 121.904 1.00 98.95 ? 309  LEU C CD1 1 
ATOM   7050  C  CD2 . LEU C 1 309 ? -47.431 102.646 119.806 1.00 99.45 ? 309  LEU C CD2 1 
ATOM   7051  N  N   . LEU C 1 310 ? -52.016 102.874 121.461 1.00 98.64 ? 310  LEU C N   1 
ATOM   7052  C  CA  . LEU C 1 310 ? -53.316 102.919 122.114 1.00 98.08 ? 310  LEU C CA  1 
ATOM   7053  C  C   . LEU C 1 310 ? -53.191 102.199 123.447 1.00 98.09 ? 310  LEU C C   1 
ATOM   7054  O  O   . LEU C 1 310 ? -52.118 101.712 123.803 1.00 99.45 ? 310  LEU C O   1 
ATOM   7055  C  CB  . LEU C 1 310 ? -54.370 102.190 121.276 1.00 98.97 ? 310  LEU C CB  1 
ATOM   7056  C  CG  . LEU C 1 310 ? -54.755 102.742 119.905 1.00 99.45 ? 310  LEU C CG  1 
ATOM   7057  C  CD1 . LEU C 1 310 ? -54.975 101.611 118.917 1.00 97.80 ? 310  LEU C CD1 1 
ATOM   7058  C  CD2 . LEU C 1 310 ? -56.008 103.558 120.053 1.00 99.45 ? 310  LEU C CD2 1 
ATOM   7059  N  N   . PHE C 1 311 ? -54.310 102.126 124.159 1.00 97.05 ? 311  PHE C N   1 
ATOM   7060  C  CA  . PHE C 1 311 ? -54.425 101.459 125.458 1.00 96.98 ? 311  PHE C CA  1 
ATOM   7061  C  C   . PHE C 1 311 ? -55.632 102.125 126.091 1.00 97.30 ? 311  PHE C C   1 
ATOM   7062  O  O   . PHE C 1 311 ? -55.509 103.178 126.708 1.00 98.66 ? 311  PHE C O   1 
ATOM   7063  C  CB  . PHE C 1 311 ? -53.186 101.694 126.333 1.00 97.52 ? 311  PHE C CB  1 
ATOM   7064  C  CG  . PHE C 1 311 ? -53.068 100.747 127.518 1.00 98.31 ? 311  PHE C CG  1 
ATOM   7065  C  CD1 . PHE C 1 311 ? -54.188 100.390 128.269 1.00 96.34 ? 311  PHE C CD1 1 
ATOM   7066  C  CD2 . PHE C 1 311 ? -51.812 100.269 127.925 1.00 98.49 ? 311  PHE C CD2 1 
ATOM   7067  C  CE1 . PHE C 1 311 ? -54.060 99.577  129.409 1.00 96.71 ? 311  PHE C CE1 1 
ATOM   7068  C  CE2 . PHE C 1 311 ? -51.676 99.454  129.064 1.00 97.54 ? 311  PHE C CE2 1 
ATOM   7069  C  CZ  . PHE C 1 311 ? -52.800 99.111  129.806 1.00 96.67 ? 311  PHE C CZ  1 
ATOM   7070  N  N   . ASN C 1 312 ? -56.802 101.521 125.909 1.00 97.65 ? 312  ASN C N   1 
ATOM   7071  C  CA  . ASN C 1 312 ? -58.051 102.061 126.445 1.00 97.89 ? 312  ASN C CA  1 
ATOM   7072  C  C   . ASN C 1 312 ? -59.027 100.961 126.856 1.00 97.16 ? 312  ASN C C   1 
ATOM   7073  O  O   . ASN C 1 312 ? -59.387 100.115 126.041 1.00 98.91 ? 312  ASN C O   1 
ATOM   7074  C  CB  . ASN C 1 312 ? -58.736 102.965 125.407 1.00 98.38 ? 312  ASN C CB  1 
ATOM   7075  C  CG  . ASN C 1 312 ? -58.451 104.443 125.630 1.00 99.45 ? 312  ASN C CG  1 
ATOM   7076  O  OD1 . ASN C 1 312 ? -58.240 104.882 126.762 1.00 99.45 ? 312  ASN C OD1 1 
ATOM   7077  N  ND2 . ASN C 1 312 ? -58.472 105.222 124.550 1.00 99.45 ? 312  ASN C ND2 1 
ATOM   7078  N  N   . GLU C 1 313 ? -59.460 100.985 128.116 1.00 96.47 ? 313  GLU C N   1 
ATOM   7079  C  CA  . GLU C 1 313 ? -60.405 99.996  128.647 1.00 95.65 ? 313  GLU C CA  1 
ATOM   7080  C  C   . GLU C 1 313 ? -61.851 100.447 128.485 1.00 96.44 ? 313  GLU C C   1 
ATOM   7081  O  O   . GLU C 1 313 ? -62.135 101.479 127.869 1.00 98.13 ? 313  GLU C O   1 
ATOM   7082  C  CB  . GLU C 1 313 ? -60.155 99.732  130.135 1.00 95.05 ? 313  GLU C CB  1 
ATOM   7083  C  CG  . GLU C 1 313 ? -59.044 98.744  130.444 1.00 96.55 ? 313  GLU C CG  1 
ATOM   7084  C  CD  . GLU C 1 313 ? -57.638 99.274  130.125 1.00 99.23 ? 313  GLU C CD  1 
ATOM   7085  O  OE1 . GLU C 1 313 ? -57.438 99.844  129.026 1.00 99.45 ? 313  GLU C OE1 1 
ATOM   7086  O  OE2 . GLU C 1 313 ? -56.719 99.094  130.960 1.00 98.77 ? 313  GLU C OE2 1 
ATOM   7087  N  N   . THR C 1 314 ? -62.759 99.661  129.055 1.00 95.36 ? 314  THR C N   1 
ATOM   7088  C  CA  . THR C 1 314 ? -64.191 99.935  129.002 1.00 94.93 ? 314  THR C CA  1 
ATOM   7089  C  C   . THR C 1 314 ? -64.889 98.767  129.671 1.00 94.68 ? 314  THR C C   1 
ATOM   7090  O  O   . THR C 1 314 ? -64.285 97.712  129.874 1.00 95.46 ? 314  THR C O   1 
ATOM   7091  C  CB  . THR C 1 314 ? -64.671 100.071 127.547 1.00 93.01 ? 314  THR C CB  1 
ATOM   7092  N  N   . ILE C 1 315 ? -66.148 98.966  130.039 1.00 93.82 ? 315  ILE C N   1 
ATOM   7093  C  CA  . ILE C 1 315 ? -66.935 97.916  130.669 1.00 93.60 ? 315  ILE C CA  1 
ATOM   7094  C  C   . ILE C 1 315 ? -68.217 97.830  129.841 1.00 93.87 ? 315  ILE C C   1 
ATOM   7095  O  O   . ILE C 1 315 ? -68.887 98.841  129.621 1.00 92.27 ? 315  ILE C O   1 
ATOM   7096  C  CB  . ILE C 1 315 ? -67.240 98.276  132.124 1.00 91.59 ? 315  ILE C CB  1 
ATOM   7097  N  N   . ASN C 1 316 ? -68.549 96.631  129.366 1.00 94.37 ? 316  ASN C N   1 
ATOM   7098  C  CA  . ASN C 1 316 ? -69.734 96.461  128.529 1.00 94.12 ? 316  ASN C CA  1 
ATOM   7099  C  C   . ASN C 1 316 ? -70.870 95.655  129.165 1.00 94.13 ? 316  ASN C C   1 
ATOM   7100  O  O   . ASN C 1 316 ? -70.643 94.742  129.969 1.00 91.34 ? 316  ASN C O   1 
ATOM   7101  C  CB  . ASN C 1 316 ? -69.332 95.841  127.179 1.00 93.68 ? 316  ASN C CB  1 
ATOM   7102  N  N   . VAL C 1 317 ? -72.095 96.011  128.787 1.00 93.61 ? 317  VAL C N   1 
ATOM   7103  C  CA  . VAL C 1 317 ? -73.284 95.349  129.288 1.00 95.30 ? 317  VAL C CA  1 
ATOM   7104  C  C   . VAL C 1 317 ? -73.849 94.417  128.221 1.00 96.74 ? 317  VAL C C   1 
ATOM   7105  O  O   . VAL C 1 317 ? -74.629 94.849  127.375 1.00 98.76 ? 317  VAL C O   1 
ATOM   7106  C  CB  . VAL C 1 317 ? -74.325 96.387  129.672 1.00 93.93 ? 317  VAL C CB  1 
ATOM   7107  N  N   . SER C 1 318 ? -73.461 93.141  128.258 1.00 97.87 ? 318  SER C N   1 
ATOM   7108  C  CA  . SER C 1 318 ? -73.936 92.147  127.284 1.00 97.89 ? 318  SER C CA  1 
ATOM   7109  C  C   . SER C 1 318 ? -74.975 91.237  127.901 1.00 97.81 ? 318  SER C C   1 
ATOM   7110  O  O   . SER C 1 318 ? -74.938 90.970  129.109 1.00 98.30 ? 318  SER C O   1 
ATOM   7111  C  CB  . SER C 1 318 ? -72.760 91.307  126.775 1.00 98.24 ? 318  SER C CB  1 
ATOM   7112  O  OG  . SER C 1 318 ? -71.781 92.115  126.140 1.00 99.45 ? 318  SER C OG  1 
ATOM   7113  N  N   . VAL C 1 319 ? -75.883 90.727  127.071 1.00 97.77 ? 319  VAL C N   1 
ATOM   7114  C  CA  . VAL C 1 319 ? -76.954 89.851  127.567 1.00 97.38 ? 319  VAL C CA  1 
ATOM   7115  C  C   . VAL C 1 319 ? -76.455 88.615  128.311 1.00 97.79 ? 319  VAL C C   1 
ATOM   7116  O  O   . VAL C 1 319 ? -75.276 88.373  128.467 1.00 98.22 ? 319  VAL C O   1 
ATOM   7117  C  CB  . VAL C 1 319 ? -77.888 89.404  126.416 1.00 97.66 ? 319  VAL C CB  1 
ATOM   7118  C  CG1 . VAL C 1 319 ? -78.184 90.554  125.465 1.00 96.72 ? 319  VAL C CG1 1 
ATOM   7119  C  CG2 . VAL C 1 319 ? -77.276 88.227  125.660 1.00 99.45 ? 319  VAL C CG2 1 
ATOM   7120  N  N   . LYS C 1 320 ? -77.440 87.884  128.787 1.00 98.54 ? 320  LYS C N   1 
ATOM   7121  C  CA  . LYS C 1 320 ? -77.329 86.658  129.554 1.00 98.92 ? 320  LYS C CA  1 
ATOM   7122  C  C   . LYS C 1 320 ? -76.029 86.000  129.917 1.00 99.03 ? 320  LYS C C   1 
ATOM   7123  O  O   . LYS C 1 320 ? -75.726 85.751  131.047 1.00 99.17 ? 320  LYS C O   1 
ATOM   7124  C  CB  . LYS C 1 320 ? -78.165 85.600  128.847 1.00 99.10 ? 320  LYS C CB  1 
ATOM   7125  N  N   . SER C 1 321 ? -75.291 85.740  128.867 1.00 99.17 ? 321  SER C N   1 
ATOM   7126  C  CA  . SER C 1 321 ? -74.031 85.001  128.811 1.00 99.17 ? 321  SER C CA  1 
ATOM   7127  C  C   . SER C 1 321 ? -74.587 84.536  127.545 1.00 99.17 ? 321  SER C C   1 
ATOM   7128  O  O   . SER C 1 321 ? -75.770 84.500  127.341 1.00 99.17 ? 321  SER C O   1 
ATOM   7129  C  CB  . SER C 1 321 ? -73.964 83.848  129.812 1.00 99.09 ? 321  SER C CB  1 
ATOM   7130  N  N   . GLY C 1 322 ? -73.841 84.195  126.551 1.00 98.67 ? 322  GLY C N   1 
ATOM   7131  C  CA  . GLY C 1 322 ? -74.589 83.817  125.315 1.00 97.78 ? 322  GLY C CA  1 
ATOM   7132  C  C   . GLY C 1 322 ? -73.922 84.929  124.588 1.00 97.25 ? 322  GLY C C   1 
ATOM   7133  O  O   . GLY C 1 322 ? -72.687 84.816  124.375 1.00 97.11 ? 322  GLY C O   1 
ATOM   7134  N  N   . SER C 1 323 ? -74.666 85.996  124.245 1.00 99.25 ? 323  SER C N   1 
ATOM   7135  C  CA  . SER C 1 323 ? -74.117 87.096  123.441 1.00 99.16 ? 323  SER C CA  1 
ATOM   7136  C  C   . SER C 1 323 ? -72.637 86.820  123.341 1.00 98.46 ? 323  SER C C   1 
ATOM   7137  O  O   . SER C 1 323 ? -71.878 87.194  124.226 1.00 99.45 ? 323  SER C O   1 
ATOM   7138  C  CB  . SER C 1 323 ? -74.355 88.449  124.115 1.00 97.45 ? 323  SER C CB  1 
ATOM   7139  O  OG  . SER C 1 323 ? -75.531 89.055  123.606 1.00 99.45 ? 323  SER C OG  1 
ATOM   7140  N  N   . VAL C 1 324 ? -72.253 86.090  122.301 1.00 95.82 ? 324  VAL C N   1 
ATOM   7141  C  CA  . VAL C 1 324 ? -70.864 85.738  122.044 1.00 91.81 ? 324  VAL C CA  1 
ATOM   7142  C  C   . VAL C 1 324 ? -69.951 86.916  122.391 1.00 90.37 ? 324  VAL C C   1 
ATOM   7143  O  O   . VAL C 1 324 ? -70.421 88.049  122.573 1.00 92.84 ? 324  VAL C O   1 
ATOM   7144  C  CB  . VAL C 1 324 ? -70.686 85.381  120.560 1.00 90.63 ? 324  VAL C CB  1 
ATOM   7145  C  CG1 . VAL C 1 324 ? -71.441 84.119  120.236 1.00 88.95 ? 324  VAL C CG1 1 
ATOM   7146  C  CG2 . VAL C 1 324 ? -71.183 86.523  119.687 1.00 90.49 ? 324  VAL C CG2 1 
ATOM   7147  N  N   . LEU C 1 325 ? -68.648 86.685  122.432 1.00 87.05 ? 325  LEU C N   1 
ATOM   7148  C  CA  . LEU C 1 325 ? -67.763 87.785  122.752 1.00 84.37 ? 325  LEU C CA  1 
ATOM   7149  C  C   . LEU C 1 325 ? -67.877 88.893  121.691 1.00 82.29 ? 325  LEU C C   1 
ATOM   7150  O  O   . LEU C 1 325 ? -67.407 90.004  121.895 1.00 81.65 ? 325  LEU C O   1 
ATOM   7151  C  CB  . LEU C 1 325 ? -66.321 87.273  122.867 1.00 86.25 ? 325  LEU C CB  1 
ATOM   7152  C  CG  . LEU C 1 325 ? -65.212 88.236  123.312 1.00 86.52 ? 325  LEU C CG  1 
ATOM   7153  C  CD1 . LEU C 1 325 ? -64.653 88.968  122.112 1.00 88.11 ? 325  LEU C CD1 1 
ATOM   7154  C  CD2 . LEU C 1 325 ? -65.750 89.215  124.349 1.00 87.13 ? 325  LEU C CD2 1 
ATOM   7155  N  N   . LEU C 1 326 ? -68.528 88.599  120.568 1.00 81.40 ? 326  LEU C N   1 
ATOM   7156  C  CA  . LEU C 1 326 ? -68.672 89.587  119.491 1.00 81.86 ? 326  LEU C CA  1 
ATOM   7157  C  C   . LEU C 1 326 ? -69.711 90.666  119.801 1.00 83.68 ? 326  LEU C C   1 
ATOM   7158  O  O   . LEU C 1 326 ? -69.648 91.771  119.246 1.00 84.41 ? 326  LEU C O   1 
ATOM   7159  C  CB  . LEU C 1 326 ? -69.023 88.904  118.156 1.00 77.37 ? 326  LEU C CB  1 
ATOM   7160  C  CG  . LEU C 1 326 ? -69.296 89.847  116.968 1.00 75.46 ? 326  LEU C CG  1 
ATOM   7161  C  CD1 . LEU C 1 326 ? -68.010 90.533  116.531 1.00 73.14 ? 326  LEU C CD1 1 
ATOM   7162  C  CD2 . LEU C 1 326 ? -69.893 89.069  115.804 1.00 74.72 ? 326  LEU C CD2 1 
ATOM   7163  N  N   . VAL C 1 327 ? -70.667 90.354  120.675 1.00 83.21 ? 327  VAL C N   1 
ATOM   7164  C  CA  . VAL C 1 327 ? -71.685 91.337  121.032 1.00 83.93 ? 327  VAL C CA  1 
ATOM   7165  C  C   . VAL C 1 327 ? -70.995 92.442  121.822 1.00 82.96 ? 327  VAL C C   1 
ATOM   7166  O  O   . VAL C 1 327 ? -71.284 93.634  121.654 1.00 80.76 ? 327  VAL C O   1 
ATOM   7167  C  CB  . VAL C 1 327 ? -72.799 90.695  121.863 1.00 84.05 ? 327  VAL C CB  1 
ATOM   7168  C  CG1 . VAL C 1 327 ? -73.708 91.763  122.427 1.00 83.02 ? 327  VAL C CG1 1 
ATOM   7169  C  CG2 . VAL C 1 327 ? -73.598 89.744  120.976 1.00 84.56 ? 327  VAL C CG2 1 
ATOM   7170  N  N   . VAL C 1 328 ? -70.056 92.019  122.660 1.00 82.11 ? 328  VAL C N   1 
ATOM   7171  C  CA  . VAL C 1 328 ? -69.265 92.927  123.473 1.00 81.89 ? 328  VAL C CA  1 
ATOM   7172  C  C   . VAL C 1 328 ? -68.562 93.980  122.611 1.00 83.66 ? 328  VAL C C   1 
ATOM   7173  O  O   . VAL C 1 328 ? -68.633 95.180  122.895 1.00 84.05 ? 328  VAL C O   1 
ATOM   7174  C  CB  . VAL C 1 328 ? -68.191 92.154  124.256 1.00 78.82 ? 328  VAL C CB  1 
ATOM   7175  C  CG1 . VAL C 1 328 ? -67.429 93.098  125.159 1.00 79.30 ? 328  VAL C CG1 1 
ATOM   7176  C  CG2 . VAL C 1 328 ? -68.831 91.042  125.056 1.00 76.19 ? 328  VAL C CG2 1 
ATOM   7177  N  N   . LEU C 1 329 ? -67.885 93.528  121.558 1.00 85.41 ? 329  LEU C N   1 
ATOM   7178  C  CA  . LEU C 1 329 ? -67.159 94.444  120.680 1.00 87.81 ? 329  LEU C CA  1 
ATOM   7179  C  C   . LEU C 1 329 ? -68.112 95.347  119.924 1.00 88.40 ? 329  LEU C C   1 
ATOM   7180  O  O   . LEU C 1 329 ? -67.781 96.493  119.634 1.00 87.31 ? 329  LEU C O   1 
ATOM   7181  C  CB  . LEU C 1 329 ? -66.299 93.686  119.655 1.00 88.27 ? 329  LEU C CB  1 
ATOM   7182  C  CG  . LEU C 1 329 ? -65.548 92.400  120.008 1.00 88.73 ? 329  LEU C CG  1 
ATOM   7183  C  CD1 . LEU C 1 329 ? -64.651 92.064  118.829 1.00 90.27 ? 329  LEU C CD1 1 
ATOM   7184  C  CD2 . LEU C 1 329 ? -64.719 92.546  121.265 1.00 87.98 ? 329  LEU C CD2 1 
ATOM   7185  N  N   . GLU C 1 330 ? -69.291 94.827  119.594 1.00 90.75 ? 330  GLU C N   1 
ATOM   7186  C  CA  . GLU C 1 330 ? -70.264 95.617  118.849 1.00 94.20 ? 330  GLU C CA  1 
ATOM   7187  C  C   . GLU C 1 330 ? -70.807 96.760  119.691 1.00 94.85 ? 330  GLU C C   1 
ATOM   7188  O  O   . GLU C 1 330 ? -70.891 97.898  119.224 1.00 95.14 ? 330  GLU C O   1 
ATOM   7189  C  CB  . GLU C 1 330 ? -71.416 94.738  118.352 1.00 94.02 ? 330  GLU C CB  1 
ATOM   7190  C  CG  . GLU C 1 330 ? -71.009 93.757  117.268 1.00 95.49 ? 330  GLU C CG  1 
ATOM   7191  C  CD  . GLU C 1 330 ? -72.184 92.958  116.730 1.00 96.61 ? 330  GLU C CD  1 
ATOM   7192  O  OE1 . GLU C 1 330 ? -73.193 92.840  117.454 1.00 98.03 ? 330  GLU C OE1 1 
ATOM   7193  O  OE2 . GLU C 1 330 ? -72.098 92.436  115.595 1.00 95.54 ? 330  GLU C OE2 1 
ATOM   7194  N  N   . GLU C 1 331 ? -71.168 96.450  120.931 1.00 94.98 ? 331  GLU C N   1 
ATOM   7195  C  CA  . GLU C 1 331 ? -71.695 97.457  121.836 1.00 95.76 ? 331  GLU C CA  1 
ATOM   7196  C  C   . GLU C 1 331 ? -70.637 98.487  122.167 1.00 95.94 ? 331  GLU C C   1 
ATOM   7197  O  O   . GLU C 1 331 ? -70.936 99.680  122.248 1.00 95.62 ? 331  GLU C O   1 
ATOM   7198  C  CB  . GLU C 1 331 ? -72.216 96.803  123.116 1.00 97.07 ? 331  GLU C CB  1 
ATOM   7199  C  CG  . GLU C 1 331 ? -73.625 96.216  122.965 1.00 98.87 ? 331  GLU C CG  1 
ATOM   7200  C  CD  . GLU C 1 331 ? -74.681 97.274  122.629 1.00 99.45 ? 331  GLU C CD  1 
ATOM   7201  O  OE1 . GLU C 1 331 ? -74.750 97.762  121.476 1.00 99.45 ? 331  GLU C OE1 1 
ATOM   7202  O  OE2 . GLU C 1 331 ? -75.447 97.628  123.540 1.00 99.45 ? 331  GLU C OE2 1 
ATOM   7203  N  N   . ALA C 1 332 ? -69.403 98.023  122.355 1.00 96.54 ? 332  ALA C N   1 
ATOM   7204  C  CA  . ALA C 1 332 ? -68.290 98.913  122.652 1.00 96.22 ? 332  ALA C CA  1 
ATOM   7205  C  C   . ALA C 1 332 ? -68.134 99.915  121.499 1.00 97.10 ? 332  ALA C C   1 
ATOM   7206  O  O   . ALA C 1 332 ? -67.746 101.066 121.709 1.00 97.95 ? 332  ALA C O   1 
ATOM   7207  C  CB  . ALA C 1 332 ? -67.024 98.111  122.835 1.00 94.27 ? 332  ALA C CB  1 
ATOM   7208  N  N   . GLN C 1 333 ? -68.446 99.478  120.282 1.00 97.93 ? 333  GLN C N   1 
ATOM   7209  C  CA  . GLN C 1 333 ? -68.356 100.356 119.117 1.00 98.35 ? 333  GLN C CA  1 
ATOM   7210  C  C   . GLN C 1 333 ? -69.569 101.289 119.084 1.00 98.19 ? 333  GLN C C   1 
ATOM   7211  O  O   . GLN C 1 333 ? -69.533 102.348 118.459 1.00 97.21 ? 333  GLN C O   1 
ATOM   7212  C  CB  . GLN C 1 333 ? -68.300 99.530  117.825 1.00 98.55 ? 333  GLN C CB  1 
ATOM   7213  C  CG  . GLN C 1 333 ? -68.250 100.378 116.559 1.00 99.29 ? 333  GLN C CG  1 
ATOM   7214  C  CD  . GLN C 1 333 ? -68.384 99.556  115.293 1.00 98.59 ? 333  GLN C CD  1 
ATOM   7215  O  OE1 . GLN C 1 333 ? -69.228 98.666  115.218 1.00 98.46 ? 333  GLN C OE1 1 
ATOM   7216  N  NE2 . GLN C 1 333 ? -67.563 99.860  114.283 1.00 97.89 ? 333  GLN C NE2 1 
ATOM   7217  N  N   . ARG C 1 334 ? -70.641 100.882 119.763 1.00 98.89 ? 334  ARG C N   1 
ATOM   7218  C  CA  . ARG C 1 334 ? -71.872 101.668 119.829 1.00 99.24 ? 334  ARG C CA  1 
ATOM   7219  C  C   . ARG C 1 334 ? -71.617 102.910 120.671 1.00 99.15 ? 334  ARG C C   1 
ATOM   7220  O  O   . ARG C 1 334 ? -71.930 104.022 120.238 1.00 99.45 ? 334  ARG C O   1 
ATOM   7221  C  CB  . ARG C 1 334 ? -73.010 100.841 120.451 1.00 99.45 ? 334  ARG C CB  1 
ATOM   7222  C  CG  . ARG C 1 334 ? -74.393 101.454 120.290 1.00 99.23 ? 334  ARG C CG  1 
ATOM   7223  C  CD  . ARG C 1 334 ? -74.750 101.629 118.811 1.00 99.45 ? 334  ARG C CD  1 
ATOM   7224  N  NE  . ARG C 1 334 ? -76.081 102.213 118.611 1.00 99.45 ? 334  ARG C NE  1 
ATOM   7225  C  CZ  . ARG C 1 334 ? -76.392 103.499 118.797 1.00 99.45 ? 334  ARG C CZ  1 
ATOM   7226  N  NH1 . ARG C 1 334 ? -75.463 104.367 119.191 1.00 99.45 ? 334  ARG C NH1 1 
ATOM   7227  N  NH2 . ARG C 1 334 ? -77.639 103.917 118.592 1.00 99.45 ? 334  ARG C NH2 1 
ATOM   7228  N  N   . LYS C 1 335 ? -71.051 102.716 121.868 1.00 98.53 ? 335  LYS C N   1 
ATOM   7229  C  CA  . LYS C 1 335 ? -70.719 103.824 122.767 1.00 97.59 ? 335  LYS C CA  1 
ATOM   7230  C  C   . LYS C 1 335 ? -69.915 104.841 121.970 1.00 99.21 ? 335  LYS C C   1 
ATOM   7231  O  O   . LYS C 1 335 ? -69.720 105.980 122.398 1.00 99.45 ? 335  LYS C O   1 
ATOM   7232  C  CB  . LYS C 1 335 ? -69.880 103.335 123.939 1.00 94.81 ? 335  LYS C CB  1 
ATOM   7233  C  CG  . LYS C 1 335 ? -70.585 102.356 124.824 1.00 94.17 ? 335  LYS C CG  1 
ATOM   7234  C  CD  . LYS C 1 335 ? -69.633 101.887 125.896 1.00 95.11 ? 335  LYS C CD  1 
ATOM   7235  C  CE  . LYS C 1 335 ? -70.265 100.849 126.795 1.00 95.01 ? 335  LYS C CE  1 
ATOM   7236  N  NZ  . LYS C 1 335 ? -69.227 100.233 127.668 1.00 95.69 ? 335  LYS C NZ  1 
ATOM   7237  N  N   . ASN C 1 336 ? -69.426 104.388 120.818 1.00 99.45 ? 336  ASN C N   1 
ATOM   7238  C  CA  . ASN C 1 336 ? -68.658 105.193 119.875 1.00 99.45 ? 336  ASN C CA  1 
ATOM   7239  C  C   . ASN C 1 336 ? -67.353 105.821 120.368 1.00 98.54 ? 336  ASN C C   1 
ATOM   7240  O  O   . ASN C 1 336 ? -66.931 106.842 119.823 1.00 98.13 ? 336  ASN C O   1 
ATOM   7241  C  CB  . ASN C 1 336 ? -69.574 106.284 119.270 1.00 98.85 ? 336  ASN C CB  1 
ATOM   7242  N  N   . PRO C 1 337 ? -66.698 105.236 121.395 1.00 98.20 ? 337  PRO C N   1 
ATOM   7243  C  CA  . PRO C 1 337 ? -65.447 105.868 121.830 1.00 98.62 ? 337  PRO C CA  1 
ATOM   7244  C  C   . PRO C 1 337 ? -64.424 105.781 120.694 1.00 99.45 ? 337  PRO C C   1 
ATOM   7245  O  O   . PRO C 1 337 ? -63.224 105.552 120.917 1.00 99.45 ? 337  PRO C O   1 
ATOM   7246  C  CB  . PRO C 1 337 ? -65.047 105.047 123.060 1.00 96.96 ? 337  PRO C CB  1 
ATOM   7247  C  CG  . PRO C 1 337 ? -66.363 104.595 123.599 1.00 97.01 ? 337  PRO C CG  1 
ATOM   7248  C  CD  . PRO C 1 337 ? -67.083 104.171 122.337 1.00 97.97 ? 337  PRO C CD  1 
ATOM   7249  N  N   . MET C 1 338 ? -64.941 105.956 119.477 1.00 99.45 ? 338  MET C N   1 
ATOM   7250  C  CA  . MET C 1 338 ? -64.184 105.935 118.229 1.00 99.45 ? 338  MET C CA  1 
ATOM   7251  C  C   . MET C 1 338 ? -63.428 104.632 118.021 1.00 99.45 ? 338  MET C C   1 
ATOM   7252  O  O   . MET C 1 338 ? -62.935 104.373 116.915 1.00 99.45 ? 338  MET C O   1 
ATOM   7253  C  CB  . MET C 1 338 ? -63.205 107.127 118.154 1.00 99.45 ? 338  MET C CB  1 
ATOM   7254  C  CG  . MET C 1 338 ? -62.577 107.328 116.764 1.00 99.45 ? 338  MET C CG  1 
ATOM   7255  S  SD  . MET C 1 338 ? -61.343 108.655 116.673 1.00 99.45 ? 338  MET C SD  1 
ATOM   7256  C  CE  . MET C 1 338 ? -59.787 107.702 116.970 1.00 99.30 ? 338  MET C CE  1 
ATOM   7257  N  N   . PHE C 1 339 ? -63.325 103.815 119.070 1.00 99.45 ? 339  PHE C N   1 
ATOM   7258  C  CA  . PHE C 1 339 ? -62.629 102.543 118.928 1.00 98.86 ? 339  PHE C CA  1 
ATOM   7259  C  C   . PHE C 1 339 ? -63.607 101.500 118.358 1.00 98.38 ? 339  PHE C C   1 
ATOM   7260  O  O   . PHE C 1 339 ? -64.132 100.613 119.044 1.00 96.74 ? 339  PHE C O   1 
ATOM   7261  C  CB  . PHE C 1 339 ? -61.970 102.122 120.263 1.00 97.95 ? 339  PHE C CB  1 
ATOM   7262  C  CG  . PHE C 1 339 ? -62.882 101.419 121.232 1.00 96.39 ? 339  PHE C CG  1 
ATOM   7263  C  CD1 . PHE C 1 339 ? -64.112 101.953 121.582 1.00 95.38 ? 339  PHE C CD1 1 
ATOM   7264  C  CD2 . PHE C 1 339 ? -62.480 100.219 121.820 1.00 95.86 ? 339  PHE C CD2 1 
ATOM   7265  C  CE1 . PHE C 1 339 ? -64.923 101.299 122.505 1.00 94.74 ? 339  PHE C CE1 1 
ATOM   7266  C  CE2 . PHE C 1 339 ? -63.284 99.560  122.742 1.00 93.35 ? 339  PHE C CE2 1 
ATOM   7267  C  CZ  . PHE C 1 339 ? -64.505 100.099 123.084 1.00 94.17 ? 339  PHE C CZ  1 
ATOM   7268  N  N   . LYS C 1 340 ? -63.863 101.674 117.064 1.00 97.67 ? 340  LYS C N   1 
ATOM   7269  C  CA  . LYS C 1 340 ? -64.742 100.809 116.303 1.00 96.02 ? 340  LYS C CA  1 
ATOM   7270  C  C   . LYS C 1 340 ? -63.825 99.759  115.698 1.00 94.81 ? 340  LYS C C   1 
ATOM   7271  O  O   . LYS C 1 340 ? -62.627 99.737  115.985 1.00 93.48 ? 340  LYS C O   1 
ATOM   7272  C  CB  . LYS C 1 340 ? -65.443 101.602 115.189 1.00 97.09 ? 340  LYS C CB  1 
ATOM   7273  C  CG  . LYS C 1 340 ? -64.604 101.865 113.936 1.00 97.62 ? 340  LYS C CG  1 
ATOM   7274  C  CD  . LYS C 1 340 ? -63.478 102.865 114.176 1.00 99.45 ? 340  LYS C CD  1 
ATOM   7275  C  CE  . LYS C 1 340 ? -62.704 103.161 112.881 1.00 99.45 ? 340  LYS C CE  1 
ATOM   7276  N  NZ  . LYS C 1 340 ? -61.572 104.114 113.092 1.00 98.90 ? 340  LYS C NZ  1 
ATOM   7277  N  N   . PHE C 1 341 ? -64.372 98.903  114.848 1.00 93.22 ? 341  PHE C N   1 
ATOM   7278  C  CA  . PHE C 1 341 ? -63.553 97.870  114.249 1.00 90.19 ? 341  PHE C CA  1 
ATOM   7279  C  C   . PHE C 1 341 ? -64.101 97.345  112.942 1.00 88.70 ? 341  PHE C C   1 
ATOM   7280  O  O   . PHE C 1 341 ? -65.187 97.724  112.504 1.00 89.77 ? 341  PHE C O   1 
ATOM   7281  C  CB  . PHE C 1 341 ? -63.379 96.711  115.236 1.00 88.16 ? 341  PHE C CB  1 
ATOM   7282  C  CG  . PHE C 1 341 ? -64.647 95.959  115.534 1.00 86.24 ? 341  PHE C CG  1 
ATOM   7283  C  CD1 . PHE C 1 341 ? -65.770 96.614  116.029 1.00 85.41 ? 341  PHE C CD1 1 
ATOM   7284  C  CD2 . PHE C 1 341 ? -64.704 94.579  115.361 1.00 87.00 ? 341  PHE C CD2 1 
ATOM   7285  C  CE1 . PHE C 1 341 ? -66.931 95.903  116.353 1.00 84.55 ? 341  PHE C CE1 1 
ATOM   7286  C  CE2 . PHE C 1 341 ? -65.863 93.860  115.683 1.00 85.89 ? 341  PHE C CE2 1 
ATOM   7287  C  CZ  . PHE C 1 341 ? -66.975 94.524  116.180 1.00 84.85 ? 341  PHE C CZ  1 
ATOM   7288  N  N   . GLU C 1 342 ? -63.323 96.468  112.325 1.00 86.01 ? 342  GLU C N   1 
ATOM   7289  C  CA  . GLU C 1 342 ? -63.698 95.850  111.077 1.00 83.64 ? 342  GLU C CA  1 
ATOM   7290  C  C   . GLU C 1 342 ? -63.550 94.351  111.251 1.00 81.78 ? 342  GLU C C   1 
ATOM   7291  O  O   . GLU C 1 342 ? -62.747 93.879  112.061 1.00 80.44 ? 342  GLU C O   1 
ATOM   7292  C  CB  . GLU C 1 342 ? -62.799 96.361  109.959 1.00 84.36 ? 342  GLU C CB  1 
ATOM   7293  C  CG  . GLU C 1 342 ? -63.005 97.831  109.670 1.00 88.26 ? 342  GLU C CG  1 
ATOM   7294  C  CD  . GLU C 1 342 ? -62.035 98.358  108.640 1.00 92.13 ? 342  GLU C CD  1 
ATOM   7295  O  OE1 . GLU C 1 342 ? -61.379 97.532  107.969 1.00 95.24 ? 342  GLU C OE1 1 
ATOM   7296  O  OE2 . GLU C 1 342 ? -61.933 99.598  108.493 1.00 94.76 ? 342  GLU C OE2 1 
ATOM   7297  N  N   . THR C 1 343 ? -64.337 93.597  110.501 1.00 79.70 ? 343  THR C N   1 
ATOM   7298  C  CA  . THR C 1 343 ? -64.265 92.159  110.602 1.00 77.09 ? 343  THR C CA  1 
ATOM   7299  C  C   . THR C 1 343 ? -64.125 91.573  109.199 1.00 75.01 ? 343  THR C C   1 
ATOM   7300  O  O   . THR C 1 343 ? -64.715 92.074  108.249 1.00 75.56 ? 343  THR C O   1 
ATOM   7301  C  CB  . THR C 1 343 ? -65.525 91.612  111.324 1.00 76.48 ? 343  THR C CB  1 
ATOM   7302  O  OG1 . THR C 1 343 ? -65.204 90.372  111.952 1.00 77.39 ? 343  THR C OG1 1 
ATOM   7303  C  CG2 . THR C 1 343 ? -66.686 91.402  110.345 1.00 75.83 ? 343  THR C CG2 1 
ATOM   7304  N  N   . THR C 1 344 ? -63.313 90.534  109.065 1.00 73.18 ? 344  THR C N   1 
ATOM   7305  C  CA  . THR C 1 344 ? -63.125 89.882  107.773 1.00 71.13 ? 344  THR C CA  1 
ATOM   7306  C  C   . THR C 1 344 ? -63.488 88.378  107.842 1.00 69.05 ? 344  THR C C   1 
ATOM   7307  O  O   . THR C 1 344 ? -63.110 87.667  108.794 1.00 68.61 ? 344  THR C O   1 
ATOM   7308  C  CB  . THR C 1 344 ? -61.678 90.068  107.275 1.00 71.07 ? 344  THR C CB  1 
ATOM   7309  O  OG1 . THR C 1 344 ? -61.475 89.273  106.105 1.00 71.62 ? 344  THR C OG1 1 
ATOM   7310  C  CG2 . THR C 1 344 ? -60.686 89.639  108.337 1.00 74.44 ? 344  THR C CG2 1 
ATOM   7311  N  N   . MET C 1 345 ? -64.235 87.919  106.833 1.00 64.02 ? 345  MET C N   1 
ATOM   7312  C  CA  . MET C 1 345 ? -64.706 86.530  106.736 1.00 59.42 ? 345  MET C CA  1 
ATOM   7313  C  C   . MET C 1 345 ? -63.669 85.504  106.285 1.00 54.32 ? 345  MET C C   1 
ATOM   7314  O  O   . MET C 1 345 ? -62.899 85.757  105.358 1.00 53.90 ? 345  MET C O   1 
ATOM   7315  C  CB  . MET C 1 345 ? -65.907 86.450  105.782 1.00 60.98 ? 345  MET C CB  1 
ATOM   7316  C  CG  . MET C 1 345 ? -67.213 86.083  106.445 1.00 60.04 ? 345  MET C CG  1 
ATOM   7317  S  SD  . MET C 1 345 ? -67.071 84.576  107.442 1.00 59.09 ? 345  MET C SD  1 
ATOM   7318  C  CE  . MET C 1 345 ? -68.618 84.664  108.404 1.00 60.12 ? 345  MET C CE  1 
ATOM   7319  N  N   . THR C 1 346 ? -63.681 84.337  106.927 1.00 49.91 ? 346  THR C N   1 
ATOM   7320  C  CA  . THR C 1 346 ? -62.749 83.259  106.595 1.00 47.60 ? 346  THR C CA  1 
ATOM   7321  C  C   . THR C 1 346 ? -63.384 81.876  106.798 1.00 45.86 ? 346  THR C C   1 
ATOM   7322  O  O   . THR C 1 346 ? -64.525 81.763  107.203 1.00 42.10 ? 346  THR C O   1 
ATOM   7323  C  CB  . THR C 1 346 ? -61.470 83.344  107.468 1.00 50.74 ? 346  THR C CB  1 
ATOM   7324  O  OG1 . THR C 1 346 ? -61.784 82.992  108.824 1.00 54.26 ? 346  THR C OG1 1 
ATOM   7325  C  CG2 . THR C 1 346 ? -60.897 84.766  107.444 1.00 48.36 ? 346  THR C CG2 1 
ATOM   7326  N  N   . SER C 1 347 ? -62.626 80.824  106.528 1.00 46.34 ? 347  SER C N   1 
ATOM   7327  C  CA  . SER C 1 347 ? -63.124 79.465  106.694 1.00 46.40 ? 347  SER C CA  1 
ATOM   7328  C  C   . SER C 1 347 ? -63.496 79.124  108.140 1.00 46.53 ? 347  SER C C   1 
ATOM   7329  O  O   . SER C 1 347 ? -64.189 78.151  108.374 1.00 48.08 ? 347  SER C O   1 
ATOM   7330  C  CB  . SER C 1 347 ? -62.077 78.464  106.200 1.00 48.52 ? 347  SER C CB  1 
ATOM   7331  O  OG  . SER C 1 347 ? -60.882 78.588  106.950 1.00 44.64 ? 347  SER C OG  1 
ATOM   7332  N  N   . TRP C 1 348 ? -63.038 79.908  109.114 1.00 47.76 ? 348  TRP C N   1 
ATOM   7333  C  CA  . TRP C 1 348 ? -63.354 79.615  110.518 1.00 47.27 ? 348  TRP C CA  1 
ATOM   7334  C  C   . TRP C 1 348 ? -64.384 80.591  111.061 1.00 49.30 ? 348  TRP C C   1 
ATOM   7335  O  O   . TRP C 1 348 ? -64.864 80.431  112.184 1.00 48.91 ? 348  TRP C O   1 
ATOM   7336  C  CB  . TRP C 1 348 ? -62.092 79.688  111.406 1.00 44.32 ? 348  TRP C CB  1 
ATOM   7337  C  CG  . TRP C 1 348 ? -61.340 78.399  111.569 1.00 40.01 ? 348  TRP C CG  1 
ATOM   7338  C  CD1 . TRP C 1 348 ? -60.273 77.965  110.831 1.00 37.45 ? 348  TRP C CD1 1 
ATOM   7339  C  CD2 . TRP C 1 348 ? -61.624 77.357  112.517 1.00 38.07 ? 348  TRP C CD2 1 
ATOM   7340  N  NE1 . TRP C 1 348 ? -59.877 76.719  111.265 1.00 38.50 ? 348  TRP C NE1 1 
ATOM   7341  C  CE2 . TRP C 1 348 ? -60.690 76.326  112.298 1.00 38.65 ? 348  TRP C CE2 1 
ATOM   7342  C  CE3 . TRP C 1 348 ? -62.585 77.194  113.527 1.00 39.28 ? 348  TRP C CE3 1 
ATOM   7343  C  CZ2 . TRP C 1 348 ? -60.689 75.147  113.053 1.00 39.64 ? 348  TRP C CZ2 1 
ATOM   7344  C  CZ3 . TRP C 1 348 ? -62.581 76.022  114.271 1.00 37.92 ? 348  TRP C CZ3 1 
ATOM   7345  C  CH2 . TRP C 1 348 ? -61.638 75.016  114.032 1.00 35.67 ? 348  TRP C CH2 1 
ATOM   7346  N  N   . GLY C 1 349 ? -64.697 81.614  110.271 1.00 49.12 ? 349  GLY C N   1 
ATOM   7347  C  CA  . GLY C 1 349 ? -65.662 82.602  110.700 1.00 51.72 ? 349  GLY C CA  1 
ATOM   7348  C  C   . GLY C 1 349 ? -65.161 84.042  110.661 1.00 55.31 ? 349  GLY C C   1 
ATOM   7349  O  O   . GLY C 1 349 ? -64.233 84.396  109.907 1.00 53.24 ? 349  GLY C O   1 
ATOM   7350  N  N   . LEU C 1 350 ? -65.802 84.886  111.469 1.00 57.21 ? 350  LEU C N   1 
ATOM   7351  C  CA  . LEU C 1 350 ? -65.445 86.295  111.542 1.00 57.68 ? 350  LEU C CA  1 
ATOM   7352  C  C   . LEU C 1 350 ? -64.130 86.521  112.267 1.00 58.11 ? 350  LEU C C   1 
ATOM   7353  O  O   . LEU C 1 350 ? -63.949 86.096  113.414 1.00 55.67 ? 350  LEU C O   1 
ATOM   7354  C  CB  . LEU C 1 350 ? -66.543 87.103  112.245 1.00 58.56 ? 350  LEU C CB  1 
ATOM   7355  C  CG  . LEU C 1 350 ? -67.771 87.567  111.456 1.00 59.59 ? 350  LEU C CG  1 
ATOM   7356  C  CD1 . LEU C 1 350 ? -67.378 88.020  110.035 1.00 59.49 ? 350  LEU C CD1 1 
ATOM   7357  C  CD2 . LEU C 1 350 ? -68.742 86.429  111.394 1.00 61.49 ? 350  LEU C CD2 1 
ATOM   7358  N  N   . VAL C 1 351 ? -63.220 87.192  111.576 1.00 58.03 ? 351  VAL C N   1 
ATOM   7359  C  CA  . VAL C 1 351 ? -61.921 87.517  112.137 1.00 60.16 ? 351  VAL C CA  1 
ATOM   7360  C  C   . VAL C 1 351 ? -61.902 89.015  112.410 1.00 60.67 ? 351  VAL C C   1 
ATOM   7361  O  O   . VAL C 1 351 ? -62.269 89.811  111.539 1.00 59.78 ? 351  VAL C O   1 
ATOM   7362  C  CB  . VAL C 1 351 ? -60.749 87.188  111.143 1.00 57.96 ? 351  VAL C CB  1 
ATOM   7363  C  CG1 . VAL C 1 351 ? -59.497 87.955  111.508 1.00 55.90 ? 351  VAL C CG1 1 
ATOM   7364  C  CG2 . VAL C 1 351 ? -60.432 85.749  111.197 1.00 55.77 ? 351  VAL C CG2 1 
ATOM   7365  N  N   . VAL C 1 352 ? -61.487 89.403  113.612 1.00 61.92 ? 352  VAL C N   1 
ATOM   7366  C  CA  . VAL C 1 352 ? -61.383 90.823  113.906 1.00 65.87 ? 352  VAL C CA  1 
ATOM   7367  C  C   . VAL C 1 352 ? -60.085 91.255  113.222 1.00 67.95 ? 352  VAL C C   1 
ATOM   7368  O  O   . VAL C 1 352 ? -58.988 90.953  113.704 1.00 68.54 ? 352  VAL C O   1 
ATOM   7369  C  CB  . VAL C 1 352 ? -61.293 91.105  115.418 1.00 65.31 ? 352  VAL C CB  1 
ATOM   7370  C  CG1 . VAL C 1 352 ? -61.158 92.600  115.643 1.00 66.96 ? 352  VAL C CG1 1 
ATOM   7371  C  CG2 . VAL C 1 352 ? -62.531 90.585  116.127 1.00 61.24 ? 352  VAL C CG2 1 
ATOM   7372  N  N   . SER C 1 353 ? -60.222 91.940  112.089 1.00 69.68 ? 353  SER C N   1 
ATOM   7373  C  CA  . SER C 1 353 ? -59.072 92.379  111.310 1.00 75.26 ? 353  SER C CA  1 
ATOM   7374  C  C   . SER C 1 353 ? -58.575 93.803  111.578 1.00 78.05 ? 353  SER C C   1 
ATOM   7375  O  O   . SER C 1 353 ? -57.462 94.172  111.185 1.00 78.18 ? 353  SER C O   1 
ATOM   7376  C  CB  . SER C 1 353 ? -59.394 92.226  109.821 1.00 75.90 ? 353  SER C CB  1 
ATOM   7377  O  OG  . SER C 1 353 ? -60.707 92.676  109.527 1.00 77.50 ? 353  SER C OG  1 
ATOM   7378  N  N   . SER C 1 354 ? -59.393 94.604  112.247 1.00 80.98 ? 354  SER C N   1 
ATOM   7379  C  CA  . SER C 1 354 ? -59.012 95.978  112.515 1.00 83.07 ? 354  SER C CA  1 
ATOM   7380  C  C   . SER C 1 354 ? -59.702 96.530  113.748 1.00 85.17 ? 354  SER C C   1 
ATOM   7381  O  O   . SER C 1 354 ? -60.871 96.246  113.990 1.00 85.90 ? 354  SER C O   1 
ATOM   7382  C  CB  . SER C 1 354 ? -59.360 96.846  111.311 1.00 82.35 ? 354  SER C CB  1 
ATOM   7383  O  OG  . SER C 1 354 ? -59.038 98.196  111.559 1.00 83.62 ? 354  SER C OG  1 
ATOM   7384  N  N   . ILE C 1 355 ? -58.964 97.315  114.528 1.00 87.59 ? 355  ILE C N   1 
ATOM   7385  C  CA  . ILE C 1 355 ? -59.501 97.944  115.733 1.00 88.54 ? 355  ILE C CA  1 
ATOM   7386  C  C   . ILE C 1 355 ? -58.969 99.368  115.825 1.00 90.43 ? 355  ILE C C   1 
ATOM   7387  O  O   . ILE C 1 355 ? -57.758 99.588  115.827 1.00 89.78 ? 355  ILE C O   1 
ATOM   7388  C  CB  . ILE C 1 355 ? -59.093 97.206  117.023 1.00 87.13 ? 355  ILE C CB  1 
ATOM   7389  C  CG1 . ILE C 1 355 ? -59.664 95.787  117.028 1.00 84.67 ? 355  ILE C CG1 1 
ATOM   7390  C  CG2 . ILE C 1 355 ? -59.594 97.988  118.234 1.00 86.40 ? 355  ILE C CG2 1 
ATOM   7391  C  CD1 . ILE C 1 355 ? -59.360 95.011  118.298 1.00 81.99 ? 355  ILE C CD1 1 
ATOM   7392  N  N   . ASN C 1 356 ? -59.888 100.325 115.910 1.00 92.33 ? 356  ASN C N   1 
ATOM   7393  C  CA  . ASN C 1 356 ? -59.545 101.741 115.995 1.00 92.73 ? 356  ASN C CA  1 
ATOM   7394  C  C   . ASN C 1 356 ? -58.594 102.149 114.862 1.00 92.61 ? 356  ASN C C   1 
ATOM   7395  O  O   . ASN C 1 356 ? -57.509 102.677 115.088 1.00 91.43 ? 356  ASN C O   1 
ATOM   7396  C  CB  . ASN C 1 356 ? -58.931 102.057 117.366 1.00 93.91 ? 356  ASN C CB  1 
ATOM   7397  C  CG  . ASN C 1 356 ? -58.964 103.537 117.689 1.00 93.65 ? 356  ASN C CG  1 
ATOM   7398  O  OD1 . ASN C 1 356 ? -59.996 104.189 117.538 1.00 93.71 ? 356  ASN C OD1 1 
ATOM   7399  N  ND2 . ASN C 1 356 ? -57.840 104.074 118.142 1.00 93.41 ? 356  ASN C ND2 1 
ATOM   7400  N  N   . ASN C 1 357 ? -59.028 101.874 113.638 1.00 92.70 ? 357  ASN C N   1 
ATOM   7401  C  CA  . ASN C 1 357 ? -58.291 102.198 112.426 1.00 92.71 ? 357  ASN C CA  1 
ATOM   7402  C  C   . ASN C 1 357 ? -56.868 101.656 112.241 1.00 92.21 ? 357  ASN C C   1 
ATOM   7403  O  O   . ASN C 1 357 ? -55.994 102.347 111.717 1.00 92.17 ? 357  ASN C O   1 
ATOM   7404  C  CB  . ASN C 1 357 ? -58.299 103.710 112.218 1.00 94.72 ? 357  ASN C CB  1 
ATOM   7405  C  CG  . ASN C 1 357 ? -59.014 104.113 110.938 1.00 97.19 ? 357  ASN C CG  1 
ATOM   7406  O  OD1 . ASN C 1 357 ? -58.521 103.871 109.827 1.00 96.39 ? 357  ASN C OD1 1 
ATOM   7407  N  ND2 . ASN C 1 357 ? -60.188 104.720 111.084 1.00 98.19 ? 357  ASN C ND2 1 
ATOM   7408  N  N   . ILE C 1 358 ? -56.646 100.411 112.649 1.00 91.92 ? 358  ILE C N   1 
ATOM   7409  C  CA  . ILE C 1 358 ? -55.346 99.758  112.480 1.00 90.07 ? 358  ILE C CA  1 
ATOM   7410  C  C   . ILE C 1 358 ? -55.561 98.266  112.168 1.00 88.85 ? 358  ILE C C   1 
ATOM   7411  O  O   . ILE C 1 358 ? -55.917 97.462  113.044 1.00 86.84 ? 358  ILE C O   1 
ATOM   7412  C  CB  . ILE C 1 358 ? -54.451 99.947  113.729 1.00 89.33 ? 358  ILE C CB  1 
ATOM   7413  C  CG1 . ILE C 1 358 ? -53.618 98.691  113.970 1.00 88.82 ? 358  ILE C CG1 1 
ATOM   7414  C  CG2 . ILE C 1 358 ? -55.290 100.327 114.919 1.00 90.14 ? 358  ILE C CG2 1 
ATOM   7415  C  CD1 . ILE C 1 358 ? -52.843 98.726  115.246 1.00 88.98 ? 358  ILE C CD1 1 
ATOM   7416  N  N   . ALA C 1 359 ? -55.348 97.924  110.897 1.00 86.98 ? 359  ALA C N   1 
ATOM   7417  C  CA  . ALA C 1 359 ? -55.533 96.569  110.386 1.00 84.81 ? 359  ALA C CA  1 
ATOM   7418  C  C   . ALA C 1 359 ? -54.385 95.598  110.657 1.00 84.21 ? 359  ALA C C   1 
ATOM   7419  O  O   . ALA C 1 359 ? -53.262 95.997  110.985 1.00 83.42 ? 359  ALA C O   1 
ATOM   7420  C  CB  . ALA C 1 359 ? -55.808 96.627  108.885 1.00 83.26 ? 359  ALA C CB  1 
ATOM   7421  N  N   . GLU C 1 360 ? -54.689 94.314  110.484 1.00 82.28 ? 360  GLU C N   1 
ATOM   7422  C  CA  . GLU C 1 360 ? -53.736 93.243  110.698 1.00 79.94 ? 360  GLU C CA  1 
ATOM   7423  C  C   . GLU C 1 360 ? -52.506 93.240  109.775 1.00 79.32 ? 360  GLU C C   1 
ATOM   7424  O  O   . GLU C 1 360 ? -51.380 93.215  110.261 1.00 82.59 ? 360  GLU C O   1 
ATOM   7425  C  CB  . GLU C 1 360 ? -54.462 91.893  110.634 1.00 78.42 ? 360  GLU C CB  1 
ATOM   7426  C  CG  . GLU C 1 360 ? -55.403 91.723  109.445 1.00 79.06 ? 360  GLU C CG  1 
ATOM   7427  C  CD  . GLU C 1 360 ? -56.240 90.446  109.530 1.00 80.39 ? 360  GLU C CD  1 
ATOM   7428  O  OE1 . GLU C 1 360 ? -56.275 89.835  110.620 1.00 81.49 ? 360  GLU C OE1 1 
ATOM   7429  O  OE2 . GLU C 1 360 ? -56.874 90.058  108.516 1.00 79.25 ? 360  GLU C OE2 1 
ATOM   7430  N  N   . ASN C 1 361 ? -52.690 93.275  108.461 1.00 76.16 ? 361  ASN C N   1 
ATOM   7431  C  CA  . ASN C 1 361 ? -51.542 93.243  107.540 1.00 75.37 ? 361  ASN C CA  1 
ATOM   7432  C  C   . ASN C 1 361 ? -50.578 92.070  107.775 1.00 73.60 ? 361  ASN C C   1 
ATOM   7433  O  O   . ASN C 1 361 ? -49.661 92.143  108.604 1.00 69.64 ? 361  ASN C O   1 
ATOM   7434  C  CB  . ASN C 1 361 ? -50.740 94.548  107.602 1.00 75.85 ? 361  ASN C CB  1 
ATOM   7435  C  CG  . ASN C 1 361 ? -49.664 94.623  106.520 1.00 76.59 ? 361  ASN C CG  1 
ATOM   7436  O  OD1 . ASN C 1 361 ? -48.974 95.630  106.382 1.00 77.81 ? 361  ASN C OD1 1 
ATOM   7437  N  ND2 . ASN C 1 361 ? -49.524 93.553  105.747 1.00 77.47 ? 361  ASN C ND2 1 
ATOM   7438  N  N   . VAL C 1 362 ? -50.768 91.010  106.998 1.00 73.48 ? 362  VAL C N   1 
ATOM   7439  C  CA  . VAL C 1 362 ? -49.950 89.812  107.110 1.00 73.68 ? 362  VAL C CA  1 
ATOM   7440  C  C   . VAL C 1 362 ? -48.499 90.010  106.660 1.00 73.83 ? 362  VAL C C   1 
ATOM   7441  O  O   . VAL C 1 362 ? -47.635 89.175  106.937 1.00 73.58 ? 362  VAL C O   1 
ATOM   7442  C  CB  . VAL C 1 362 ? -50.581 88.672  106.301 1.00 72.81 ? 362  VAL C CB  1 
ATOM   7443  C  CG1 . VAL C 1 362 ? -50.242 88.841  104.822 1.00 71.62 ? 362  VAL C CG1 1 
ATOM   7444  C  CG2 . VAL C 1 362 ? -50.128 87.333  106.847 1.00 73.84 ? 362  VAL C CG2 1 
ATOM   7445  N  N   . ASN C 1 363 ? -48.229 91.106  105.962 1.00 75.83 ? 363  ASN C N   1 
ATOM   7446  C  CA  . ASN C 1 363 ? -46.866 91.395  105.504 1.00 79.44 ? 363  ASN C CA  1 
ATOM   7447  C  C   . ASN C 1 363 ? -45.956 91.675  106.707 1.00 79.93 ? 363  ASN C C   1 
ATOM   7448  O  O   . ASN C 1 363 ? -44.763 91.381  106.686 1.00 79.85 ? 363  ASN C O   1 
ATOM   7449  C  CB  . ASN C 1 363 ? -46.858 92.615  104.571 1.00 81.28 ? 363  ASN C CB  1 
ATOM   7450  C  CG  . ASN C 1 363 ? -47.356 92.291  103.167 1.00 82.84 ? 363  ASN C CG  1 
ATOM   7451  O  OD1 . ASN C 1 363 ? -48.005 93.118  102.517 1.00 82.79 ? 363  ASN C OD1 1 
ATOM   7452  N  ND2 . ASN C 1 363 ? -47.035 91.094  102.684 1.00 82.23 ? 363  ASN C ND2 1 
ATOM   7453  N  N   . HIS C 1 364 ? -46.536 92.248  107.756 1.00 79.64 ? 364  HIS C N   1 
ATOM   7454  C  CA  . HIS C 1 364 ? -45.790 92.565  108.961 1.00 77.29 ? 364  HIS C CA  1 
ATOM   7455  C  C   . HIS C 1 364 ? -46.001 91.493  110.018 1.00 75.60 ? 364  HIS C C   1 
ATOM   7456  O  O   . HIS C 1 364 ? -45.694 91.712  111.184 1.00 73.17 ? 364  HIS C O   1 
ATOM   7457  C  CB  . HIS C 1 364 ? -46.234 93.929  109.499 1.00 80.72 ? 364  HIS C CB  1 
ATOM   7458  C  CG  . HIS C 1 364 ? -46.042 95.049  108.521 1.00 85.32 ? 364  HIS C CG  1 
ATOM   7459  N  ND1 . HIS C 1 364 ? -46.631 96.287  108.676 1.00 86.64 ? 364  HIS C ND1 1 
ATOM   7460  C  CD2 . HIS C 1 364 ? -45.333 95.112  107.366 1.00 85.94 ? 364  HIS C CD2 1 
ATOM   7461  C  CE1 . HIS C 1 364 ? -46.297 97.062  107.658 1.00 85.57 ? 364  HIS C CE1 1 
ATOM   7462  N  NE2 . HIS C 1 364 ? -45.510 96.373  106.848 1.00 85.86 ? 364  HIS C NE2 1 
ATOM   7463  N  N   . LYS C 1 365 ? -46.518 90.335  109.602 1.00 74.56 ? 365  LYS C N   1 
ATOM   7464  C  CA  . LYS C 1 365 ? -46.765 89.222  110.520 1.00 73.00 ? 365  LYS C CA  1 
ATOM   7465  C  C   . LYS C 1 365 ? -47.433 89.797  111.759 1.00 70.94 ? 365  LYS C C   1 
ATOM   7466  O  O   . LYS C 1 365 ? -47.135 89.412  112.887 1.00 69.10 ? 365  LYS C O   1 
ATOM   7467  C  CB  . LYS C 1 365 ? -45.444 88.542  110.924 1.00 75.33 ? 365  LYS C CB  1 
ATOM   7468  C  CG  . LYS C 1 365 ? -45.250 87.094  110.447 1.00 77.42 ? 365  LYS C CG  1 
ATOM   7469  C  CD  . LYS C 1 365 ? -44.864 87.010  108.970 1.00 80.55 ? 365  LYS C CD  1 
ATOM   7470  C  CE  . LYS C 1 365 ? -44.653 85.557  108.507 1.00 83.59 ? 365  LYS C CE  1 
ATOM   7471  N  NZ  . LYS C 1 365 ? -43.491 84.873  109.162 1.00 83.55 ? 365  LYS C NZ  1 
ATOM   7472  N  N   . THR C 1 366 ? -48.355 90.719  111.546 1.00 69.96 ? 366  THR C N   1 
ATOM   7473  C  CA  . THR C 1 366 ? -49.008 91.343  112.670 1.00 70.84 ? 366  THR C CA  1 
ATOM   7474  C  C   . THR C 1 366 ? -50.539 91.192  112.687 1.00 69.50 ? 366  THR C C   1 
ATOM   7475  O  O   . THR C 1 366 ? -51.189 91.222  111.647 1.00 68.64 ? 366  THR C O   1 
ATOM   7476  C  CB  . THR C 1 366 ? -48.573 92.825  112.726 1.00 73.08 ? 366  THR C CB  1 
ATOM   7477  O  OG1 . THR C 1 366 ? -48.982 93.390  113.973 1.00 78.76 ? 366  THR C OG1 1 
ATOM   7478  C  CG2 . THR C 1 366 ? -49.154 93.623  111.565 1.00 71.64 ? 366  THR C CG2 1 
ATOM   7479  N  N   . TYR C 1 367 ? -51.109 91.022  113.879 1.00 68.54 ? 367  TYR C N   1 
ATOM   7480  C  CA  . TYR C 1 367 ? -52.555 90.840  114.027 1.00 67.35 ? 367  TYR C CA  1 
ATOM   7481  C  C   . TYR C 1 367 ? -53.047 91.172  115.441 1.00 68.58 ? 367  TYR C C   1 
ATOM   7482  O  O   . TYR C 1 367 ? -52.269 91.544  116.316 1.00 68.13 ? 367  TYR C O   1 
ATOM   7483  C  CB  . TYR C 1 367 ? -52.921 89.386  113.766 1.00 62.16 ? 367  TYR C CB  1 
ATOM   7484  C  CG  . TYR C 1 367 ? -52.531 88.492  114.931 1.00 59.21 ? 367  TYR C CG  1 
ATOM   7485  C  CD1 . TYR C 1 367 ? -51.191 88.333  115.294 1.00 56.79 ? 367  TYR C CD1 1 
ATOM   7486  C  CD2 . TYR C 1 367 ? -53.500 87.813  115.674 1.00 54.83 ? 367  TYR C CD2 1 
ATOM   7487  C  CE1 . TYR C 1 367 ? -50.826 87.517  116.362 1.00 56.76 ? 367  TYR C CE1 1 
ATOM   7488  C  CE2 . TYR C 1 367 ? -53.144 86.995  116.744 1.00 54.71 ? 367  TYR C CE2 1 
ATOM   7489  C  CZ  . TYR C 1 367 ? -51.810 86.847  117.079 1.00 56.76 ? 367  TYR C CZ  1 
ATOM   7490  O  OH  . TYR C 1 367 ? -51.457 86.003  118.102 1.00 57.87 ? 367  TYR C OH  1 
ATOM   7491  N  N   . TRP C 1 368 ? -54.345 90.983  115.660 1.00 68.95 ? 368  TRP C N   1 
ATOM   7492  C  CA  . TRP C 1 368 ? -54.945 91.240  116.958 1.00 71.40 ? 368  TRP C CA  1 
ATOM   7493  C  C   . TRP C 1 368 ? -55.177 89.936  117.728 1.00 71.95 ? 368  TRP C C   1 
ATOM   7494  O  O   . TRP C 1 368 ? -55.998 89.108  117.330 1.00 73.85 ? 368  TRP C O   1 
ATOM   7495  C  CB  . TRP C 1 368 ? -56.288 91.973  116.795 1.00 75.73 ? 368  TRP C CB  1 
ATOM   7496  C  CG  . TRP C 1 368 ? -56.196 93.403  116.313 1.00 78.11 ? 368  TRP C CG  1 
ATOM   7497  C  CD1 . TRP C 1 368 ? -56.311 93.850  115.025 1.00 79.85 ? 368  TRP C CD1 1 
ATOM   7498  C  CD2 . TRP C 1 368 ? -55.945 94.561  117.120 1.00 79.65 ? 368  TRP C CD2 1 
ATOM   7499  N  NE1 . TRP C 1 368 ? -56.146 95.219  114.980 1.00 81.61 ? 368  TRP C NE1 1 
ATOM   7500  C  CE2 . TRP C 1 368 ? -55.916 95.679  116.251 1.00 81.19 ? 368  TRP C CE2 1 
ATOM   7501  C  CE3 . TRP C 1 368 ? -55.734 94.762  118.493 1.00 79.32 ? 368  TRP C CE3 1 
ATOM   7502  C  CZ2 . TRP C 1 368 ? -55.687 96.982  116.713 1.00 81.27 ? 368  TRP C CZ2 1 
ATOM   7503  C  CZ3 . TRP C 1 368 ? -55.507 96.056  118.953 1.00 77.78 ? 368  TRP C CZ3 1 
ATOM   7504  C  CH2 . TRP C 1 368 ? -55.483 97.149  118.063 1.00 80.24 ? 368  TRP C CH2 1 
ATOM   7505  N  N   . GLN C 1 369 ? -54.464 89.748  118.833 1.00 71.57 ? 369  GLN C N   1 
ATOM   7506  C  CA  . GLN C 1 369 ? -54.640 88.536  119.627 1.00 70.92 ? 369  GLN C CA  1 
ATOM   7507  C  C   . GLN C 1 369 ? -55.568 88.777  120.806 1.00 72.89 ? 369  GLN C C   1 
ATOM   7508  O  O   . GLN C 1 369 ? -55.412 89.744  121.537 1.00 76.16 ? 369  GLN C O   1 
ATOM   7509  C  CB  . GLN C 1 369 ? -53.299 88.026  120.144 1.00 67.92 ? 369  GLN C CB  1 
ATOM   7510  C  CG  . GLN C 1 369 ? -53.438 86.786  121.001 1.00 66.51 ? 369  GLN C CG  1 
ATOM   7511  C  CD  . GLN C 1 369 ? -52.105 86.184  121.407 1.00 65.79 ? 369  GLN C CD  1 
ATOM   7512  O  OE1 . GLN C 1 369 ? -52.043 85.027  121.820 1.00 68.71 ? 369  GLN C OE1 1 
ATOM   7513  N  NE2 . GLN C 1 369 ? -51.038 86.965  121.304 1.00 63.54 ? 369  GLN C NE2 1 
ATOM   7514  N  N   . PHE C 1 370 ? -56.535 87.892  120.991 1.00 74.99 ? 370  PHE C N   1 
ATOM   7515  C  CA  . PHE C 1 370 ? -57.488 88.021  122.084 1.00 75.96 ? 370  PHE C CA  1 
ATOM   7516  C  C   . PHE C 1 370 ? -57.095 87.127  123.236 1.00 77.08 ? 370  PHE C C   1 
ATOM   7517  O  O   . PHE C 1 370 ? -56.560 86.040  123.031 1.00 78.68 ? 370  PHE C O   1 
ATOM   7518  C  CB  . PHE C 1 370 ? -58.912 87.663  121.615 1.00 77.16 ? 370  PHE C CB  1 
ATOM   7519  C  CG  . PHE C 1 370 ? -59.551 88.727  120.763 1.00 77.02 ? 370  PHE C CG  1 
ATOM   7520  C  CD1 . PHE C 1 370 ? -59.071 88.996  119.489 1.00 75.56 ? 370  PHE C CD1 1 
ATOM   7521  C  CD2 . PHE C 1 370 ? -60.589 89.509  121.265 1.00 78.48 ? 370  PHE C CD2 1 
ATOM   7522  C  CE1 . PHE C 1 370 ? -59.608 90.031  118.722 1.00 78.68 ? 370  PHE C CE1 1 
ATOM   7523  C  CE2 . PHE C 1 370 ? -61.136 90.552  120.505 1.00 79.33 ? 370  PHE C CE2 1 
ATOM   7524  C  CZ  . PHE C 1 370 ? -60.642 90.814  119.232 1.00 77.89 ? 370  PHE C CZ  1 
ATOM   7525  N  N   . LEU C 1 371 ? -57.353 87.593  124.453 1.00 78.08 ? 371  LEU C N   1 
ATOM   7526  C  CA  . LEU C 1 371 ? -57.035 86.814  125.634 1.00 77.65 ? 371  LEU C CA  1 
ATOM   7527  C  C   . LEU C 1 371 ? -57.871 87.194  126.841 1.00 75.76 ? 371  LEU C C   1 
ATOM   7528  O  O   . LEU C 1 371 ? -58.301 88.335  126.985 1.00 74.07 ? 371  LEU C O   1 
ATOM   7529  C  CB  . LEU C 1 371 ? -55.534 86.906  125.951 1.00 79.54 ? 371  LEU C CB  1 
ATOM   7530  C  CG  . LEU C 1 371 ? -54.792 88.245  126.058 1.00 81.88 ? 371  LEU C CG  1 
ATOM   7531  C  CD1 . LEU C 1 371 ? -53.302 87.942  126.189 1.00 82.45 ? 371  LEU C CD1 1 
ATOM   7532  C  CD2 . LEU C 1 371 ? -55.027 89.124  124.846 1.00 80.46 ? 371  LEU C CD2 1 
ATOM   7533  N  N   . SER C 1 372 ? -58.123 86.186  127.670 1.00 76.13 ? 372  SER C N   1 
ATOM   7534  C  CA  . SER C 1 372 ? -58.890 86.298  128.897 1.00 77.27 ? 372  SER C CA  1 
ATOM   7535  C  C   . SER C 1 372 ? -57.813 86.482  129.963 1.00 79.42 ? 372  SER C C   1 
ATOM   7536  O  O   . SER C 1 372 ? -57.061 85.544  130.276 1.00 78.84 ? 372  SER C O   1 
ATOM   7537  C  CB  . SER C 1 372 ? -59.667 84.999  129.126 1.00 76.34 ? 372  SER C CB  1 
ATOM   7538  O  OG  . SER C 1 372 ? -60.388 85.013  130.340 1.00 80.90 ? 372  SER C OG  1 
ATOM   7539  N  N   . GLY C 1 373 ? -57.726 87.692  130.513 1.00 79.27 ? 373  GLY C N   1 
ATOM   7540  C  CA  . GLY C 1 373 ? -56.698 87.942  131.497 1.00 79.20 ? 373  GLY C CA  1 
ATOM   7541  C  C   . GLY C 1 373 ? -55.368 87.971  130.763 1.00 79.03 ? 373  GLY C C   1 
ATOM   7542  O  O   . GLY C 1 373 ? -55.041 88.956  130.102 1.00 77.82 ? 373  GLY C O   1 
ATOM   7543  N  N   . VAL C 1 374 ? -54.604 86.891  130.851 1.00 78.95 ? 374  VAL C N   1 
ATOM   7544  C  CA  . VAL C 1 374 ? -53.315 86.855  130.172 1.00 81.78 ? 374  VAL C CA  1 
ATOM   7545  C  C   . VAL C 1 374 ? -53.212 85.706  129.142 1.00 82.47 ? 374  VAL C C   1 
ATOM   7546  O  O   . VAL C 1 374 ? -52.354 85.730  128.243 1.00 80.63 ? 374  VAL C O   1 
ATOM   7547  C  CB  . VAL C 1 374 ? -52.163 86.719  131.202 1.00 82.59 ? 374  VAL C CB  1 
ATOM   7548  C  CG1 . VAL C 1 374 ? -52.162 85.305  131.804 1.00 81.63 ? 374  VAL C CG1 1 
ATOM   7549  C  CG2 . VAL C 1 374 ? -50.824 87.052  130.541 1.00 83.02 ? 374  VAL C CG2 1 
ATOM   7550  N  N   . THR C 1 375 ? -54.090 84.711  129.283 1.00 82.45 ? 375  THR C N   1 
ATOM   7551  C  CA  . THR C 1 375 ? -54.110 83.548  128.389 1.00 81.09 ? 375  THR C CA  1 
ATOM   7552  C  C   . THR C 1 375 ? -54.965 83.784  127.130 1.00 77.78 ? 375  THR C C   1 
ATOM   7553  O  O   . THR C 1 375 ? -56.091 84.287  127.209 1.00 76.09 ? 375  THR C O   1 
ATOM   7554  C  CB  . THR C 1 375 ? -54.630 82.293  129.136 1.00 80.99 ? 375  THR C CB  1 
ATOM   7555  O  OG1 . THR C 1 375 ? -55.992 82.502  129.527 1.00 82.55 ? 375  THR C OG1 1 
ATOM   7556  C  CG2 . THR C 1 375 ? -53.775 82.026  130.389 1.00 79.32 ? 375  THR C CG2 1 
ATOM   7557  N  N   . PRO C 1 376 ? -54.432 83.414  125.950 1.00 74.46 ? 376  PRO C N   1 
ATOM   7558  C  CA  . PRO C 1 376 ? -55.138 83.591  124.676 1.00 71.64 ? 376  PRO C CA  1 
ATOM   7559  C  C   . PRO C 1 376 ? -56.380 82.713  124.543 1.00 68.82 ? 376  PRO C C   1 
ATOM   7560  O  O   . PRO C 1 376 ? -56.405 81.569  125.015 1.00 67.67 ? 376  PRO C O   1 
ATOM   7561  C  CB  . PRO C 1 376 ? -54.074 83.232  123.631 1.00 71.02 ? 376  PRO C CB  1 
ATOM   7562  C  CG  . PRO C 1 376 ? -52.774 83.438  124.353 1.00 72.39 ? 376  PRO C CG  1 
ATOM   7563  C  CD  . PRO C 1 376 ? -53.084 82.873  125.714 1.00 73.21 ? 376  PRO C CD  1 
ATOM   7564  N  N   . LEU C 1 377 ? -57.405 83.261  123.898 1.00 65.92 ? 377  LEU C N   1 
ATOM   7565  C  CA  . LEU C 1 377 ? -58.655 82.543  123.660 1.00 66.66 ? 377  LEU C CA  1 
ATOM   7566  C  C   . LEU C 1 377 ? -58.488 81.378  122.658 1.00 65.91 ? 377  LEU C C   1 
ATOM   7567  O  O   . LEU C 1 377 ? -57.682 81.444  121.728 1.00 64.62 ? 377  LEU C O   1 
ATOM   7568  C  CB  . LEU C 1 377 ? -59.714 83.528  123.150 1.00 67.60 ? 377  LEU C CB  1 
ATOM   7569  C  CG  . LEU C 1 377 ? -60.699 84.131  124.157 1.00 69.81 ? 377  LEU C CG  1 
ATOM   7570  C  CD1 . LEU C 1 377 ? -60.009 84.444  125.459 1.00 70.83 ? 377  LEU C CD1 1 
ATOM   7571  C  CD2 . LEU C 1 377 ? -61.305 85.382  123.564 1.00 69.83 ? 377  LEU C CD2 1 
ATOM   7572  N  N   . ASN C 1 378 ? -59.242 80.304  122.858 1.00 64.89 ? 378  ASN C N   1 
ATOM   7573  C  CA  . ASN C 1 378 ? -59.158 79.169  121.955 1.00 67.38 ? 378  ASN C CA  1 
ATOM   7574  C  C   . ASN C 1 378 ? -60.318 79.165  120.957 1.00 68.32 ? 378  ASN C C   1 
ATOM   7575  O  O   . ASN C 1 378 ? -60.533 78.161  120.286 1.00 69.06 ? 378  ASN C O   1 
ATOM   7576  C  CB  . ASN C 1 378 ? -59.175 77.866  122.747 1.00 69.55 ? 378  ASN C CB  1 
ATOM   7577  C  CG  . ASN C 1 378 ? -60.523 77.598  123.390 1.00 74.19 ? 378  ASN C CG  1 
ATOM   7578  O  OD1 . ASN C 1 378 ? -61.117 78.489  124.012 1.00 77.27 ? 378  ASN C OD1 1 
ATOM   7579  N  ND2 . ASN C 1 378 ? -61.016 76.367  123.253 1.00 72.93 ? 378  ASN C ND2 1 
ATOM   7580  N  N   . GLU C 1 379 ? -61.061 80.277  120.873 1.00 67.50 ? 379  GLU C N   1 
ATOM   7581  C  CA  . GLU C 1 379 ? -62.214 80.426  119.972 1.00 66.48 ? 379  GLU C CA  1 
ATOM   7582  C  C   . GLU C 1 379 ? -62.304 81.865  119.436 1.00 65.71 ? 379  GLU C C   1 
ATOM   7583  O  O   . GLU C 1 379 ? -61.762 82.791  120.029 1.00 63.54 ? 379  GLU C O   1 
ATOM   7584  C  CB  . GLU C 1 379 ? -63.520 80.088  120.711 1.00 66.67 ? 379  GLU C CB  1 
ATOM   7585  C  CG  . GLU C 1 379 ? -63.758 78.614  120.932 1.00 70.59 ? 379  GLU C CG  1 
ATOM   7586  C  CD  . GLU C 1 379 ? -65.069 78.319  121.652 1.00 76.54 ? 379  GLU C CD  1 
ATOM   7587  O  OE1 . GLU C 1 379 ? -65.109 78.349  122.907 1.00 77.10 ? 379  GLU C OE1 1 
ATOM   7588  O  OE2 . GLU C 1 379 ? -66.070 78.057  120.951 1.00 81.06 ? 379  GLU C OE2 1 
ATOM   7589  N  N   . GLY C 1 380 ? -62.997 82.060  118.321 1.00 65.08 ? 380  GLY C N   1 
ATOM   7590  C  CA  . GLY C 1 380 ? -63.121 83.400  117.774 1.00 63.56 ? 380  GLY C CA  1 
ATOM   7591  C  C   . GLY C 1 380 ? -64.192 84.205  118.482 1.00 63.59 ? 380  GLY C C   1 
ATOM   7592  O  O   . GLY C 1 380 ? -64.946 83.675  119.307 1.00 61.25 ? 380  GLY C O   1 
ATOM   7593  N  N   . VAL C 1 381 ? -64.266 85.489  118.144 1.00 62.53 ? 381  VAL C N   1 
ATOM   7594  C  CA  . VAL C 1 381 ? -65.246 86.386  118.745 1.00 63.26 ? 381  VAL C CA  1 
ATOM   7595  C  C   . VAL C 1 381 ? -66.719 86.007  118.502 1.00 65.33 ? 381  VAL C C   1 
ATOM   7596  O  O   . VAL C 1 381 ? -67.602 86.405  119.258 1.00 65.47 ? 381  VAL C O   1 
ATOM   7597  C  CB  . VAL C 1 381 ? -65.038 87.840  118.263 1.00 60.35 ? 381  VAL C CB  1 
ATOM   7598  C  CG1 . VAL C 1 381 ? -63.626 88.303  118.593 1.00 59.86 ? 381  VAL C CG1 1 
ATOM   7599  C  CG2 . VAL C 1 381 ? -65.332 87.944  116.792 1.00 56.02 ? 381  VAL C CG2 1 
ATOM   7600  N  N   . ALA C 1 382 ? -66.996 85.248  117.452 1.00 66.19 ? 382  ALA C N   1 
ATOM   7601  C  CA  . ALA C 1 382 ? -68.371 84.864  117.189 1.00 66.28 ? 382  ALA C CA  1 
ATOM   7602  C  C   . ALA C 1 382 ? -68.697 83.531  117.864 1.00 66.53 ? 382  ALA C C   1 
ATOM   7603  O  O   . ALA C 1 382 ? -69.834 83.062  117.823 1.00 68.93 ? 382  ALA C O   1 
ATOM   7604  C  CB  . ALA C 1 382 ? -68.614 84.780  115.687 1.00 66.56 ? 382  ALA C CB  1 
ATOM   7605  N  N   . ASP C 1 383 ? -67.710 82.930  118.513 1.00 66.80 ? 383  ASP C N   1 
ATOM   7606  C  CA  . ASP C 1 383 ? -67.936 81.646  119.168 1.00 68.79 ? 383  ASP C CA  1 
ATOM   7607  C  C   . ASP C 1 383 ? -67.786 81.668  120.685 1.00 69.69 ? 383  ASP C C   1 
ATOM   7608  O  O   . ASP C 1 383 ? -68.453 80.911  121.406 1.00 67.57 ? 383  ASP C O   1 
ATOM   7609  C  CB  . ASP C 1 383 ? -66.967 80.609  118.612 1.00 69.77 ? 383  ASP C CB  1 
ATOM   7610  C  CG  . ASP C 1 383 ? -67.456 79.968  117.341 1.00 73.25 ? 383  ASP C CG  1 
ATOM   7611  O  OD1 . ASP C 1 383 ? -68.412 80.486  116.714 1.00 72.65 ? 383  ASP C OD1 1 
ATOM   7612  O  OD2 . ASP C 1 383 ? -66.861 78.933  116.970 1.00 76.53 ? 383  ASP C OD2 1 
ATOM   7613  N  N   . TYR C 1 384 ? -66.893 82.529  121.157 1.00 72.12 ? 384  TYR C N   1 
ATOM   7614  C  CA  . TYR C 1 384 ? -66.595 82.644  122.580 1.00 75.65 ? 384  TYR C CA  1 
ATOM   7615  C  C   . TYR C 1 384 ? -67.686 83.263  123.430 1.00 75.77 ? 384  TYR C C   1 
ATOM   7616  O  O   . TYR C 1 384 ? -68.251 84.309  123.090 1.00 72.70 ? 384  TYR C O   1 
ATOM   7617  C  CB  . TYR C 1 384 ? -65.314 83.454  122.786 1.00 79.44 ? 384  TYR C CB  1 
ATOM   7618  C  CG  . TYR C 1 384 ? -64.715 83.294  124.160 1.00 81.44 ? 384  TYR C CG  1 
ATOM   7619  C  CD1 . TYR C 1 384 ? -64.155 82.077  124.557 1.00 81.48 ? 384  TYR C CD1 1 
ATOM   7620  C  CD2 . TYR C 1 384 ? -64.709 84.353  125.063 1.00 81.96 ? 384  TYR C CD2 1 
ATOM   7621  C  CE1 . TYR C 1 384 ? -63.602 81.917  125.821 1.00 83.16 ? 384  TYR C CE1 1 
ATOM   7622  C  CE2 . TYR C 1 384 ? -64.160 84.205  126.328 1.00 84.72 ? 384  TYR C CE2 1 
ATOM   7623  C  CZ  . TYR C 1 384 ? -63.606 82.985  126.703 1.00 84.16 ? 384  TYR C CZ  1 
ATOM   7624  O  OH  . TYR C 1 384 ? -63.048 82.850  127.955 1.00 85.54 ? 384  TYR C OH  1 
ATOM   7625  N  N   . ILE C 1 385 ? -67.948 82.615  124.560 1.00 77.55 ? 385  ILE C N   1 
ATOM   7626  C  CA  . ILE C 1 385 ? -68.956 83.087  125.492 1.00 80.87 ? 385  ILE C CA  1 
ATOM   7627  C  C   . ILE C 1 385 ? -68.327 83.574  126.800 1.00 83.73 ? 385  ILE C C   1 
ATOM   7628  O  O   . ILE C 1 385 ? -67.990 82.775  127.678 1.00 84.11 ? 385  ILE C O   1 
ATOM   7629  C  CB  . ILE C 1 385 ? -69.986 81.980  125.775 1.00 79.85 ? 385  ILE C CB  1 
ATOM   7630  C  CG1 . ILE C 1 385 ? -70.799 81.711  124.494 1.00 80.89 ? 385  ILE C CG1 1 
ATOM   7631  C  CG2 . ILE C 1 385 ? -70.872 82.379  126.945 1.00 78.32 ? 385  ILE C CG2 1 
ATOM   7632  C  CD1 . ILE C 1 385 ? -71.764 80.538  124.579 1.00 76.82 ? 385  ILE C CD1 1 
ATOM   7633  N  N   . PRO C 1 386 ? -68.155 84.906  126.932 1.00 86.00 ? 386  PRO C N   1 
ATOM   7634  C  CA  . PRO C 1 386 ? -67.575 85.590  128.098 1.00 88.00 ? 386  PRO C CA  1 
ATOM   7635  C  C   . PRO C 1 386 ? -68.426 85.379  129.350 1.00 90.48 ? 386  PRO C C   1 
ATOM   7636  O  O   . PRO C 1 386 ? -69.660 85.347  129.263 1.00 91.44 ? 386  PRO C O   1 
ATOM   7637  C  CB  . PRO C 1 386 ? -67.578 87.061  127.675 1.00 87.65 ? 386  PRO C CB  1 
ATOM   7638  C  CG  . PRO C 1 386 ? -67.567 87.007  126.178 1.00 87.02 ? 386  PRO C CG  1 
ATOM   7639  C  CD  . PRO C 1 386 ? -68.507 85.880  125.882 1.00 85.40 ? 386  PRO C CD  1 
ATOM   7640  N  N   . PHE C 1 387 ? -67.774 85.247  130.506 1.00 93.15 ? 387  PHE C N   1 
ATOM   7641  C  CA  . PHE C 1 387 ? -68.489 85.058  131.773 1.00 95.19 ? 387  PHE C CA  1 
ATOM   7642  C  C   . PHE C 1 387 ? -68.686 86.365  132.557 1.00 96.06 ? 387  PHE C C   1 
ATOM   7643  O  O   . PHE C 1 387 ? -68.384 87.451  132.051 1.00 96.50 ? 387  PHE C O   1 
ATOM   7644  C  CB  . PHE C 1 387 ? -67.773 84.018  132.652 1.00 95.53 ? 387  PHE C CB  1 
ATOM   7645  C  CG  . PHE C 1 387 ? -66.317 84.309  132.893 1.00 96.10 ? 387  PHE C CG  1 
ATOM   7646  C  CD1 . PHE C 1 387 ? -65.909 85.546  133.399 1.00 96.22 ? 387  PHE C CD1 1 
ATOM   7647  C  CD2 . PHE C 1 387 ? -65.352 83.334  132.640 1.00 94.96 ? 387  PHE C CD2 1 
ATOM   7648  C  CE1 . PHE C 1 387 ? -64.562 85.807  133.650 1.00 96.87 ? 387  PHE C CE1 1 
ATOM   7649  C  CE2 . PHE C 1 387 ? -64.003 83.583  132.886 1.00 94.46 ? 387  PHE C CE2 1 
ATOM   7650  C  CZ  . PHE C 1 387 ? -63.606 84.822  133.393 1.00 96.65 ? 387  PHE C CZ  1 
ATOM   7651  N  N   . ASN C 1 388 ? -69.194 86.240  133.785 1.00 97.67 ? 388  ASN C N   1 
ATOM   7652  C  CA  . ASN C 1 388 ? -69.481 87.369  134.688 1.00 98.23 ? 388  ASN C CA  1 
ATOM   7653  C  C   . ASN C 1 388 ? -68.760 88.703  134.449 1.00 98.60 ? 388  ASN C C   1 
ATOM   7654  O  O   . ASN C 1 388 ? -69.303 89.602  133.795 1.00 98.11 ? 388  ASN C O   1 
ATOM   7655  C  CB  . ASN C 1 388 ? -69.278 86.929  136.146 1.00 98.20 ? 388  ASN C CB  1 
ATOM   7656  C  CG  . ASN C 1 388 ? -67.939 86.248  136.374 1.00 99.45 ? 388  ASN C CG  1 
ATOM   7657  O  OD1 . ASN C 1 388 ? -66.878 86.832  136.126 1.00 99.45 ? 388  ASN C OD1 1 
ATOM   7658  N  ND2 . ASN C 1 388 ? -67.981 85.001  136.851 1.00 99.45 ? 388  ASN C ND2 1 
ATOM   7659  N  N   . HIS C 1 389 ? -67.558 88.840  135.006 1.00 98.70 ? 389  HIS C N   1 
ATOM   7660  C  CA  . HIS C 1 389 ? -66.766 90.061  134.859 1.00 99.27 ? 389  HIS C CA  1 
ATOM   7661  C  C   . HIS C 1 389 ? -65.420 89.710  134.241 1.00 99.45 ? 389  HIS C C   1 
ATOM   7662  O  O   . HIS C 1 389 ? -64.374 89.911  134.870 1.00 99.45 ? 389  HIS C O   1 
ATOM   7663  C  CB  . HIS C 1 389 ? -66.516 90.730  136.222 1.00 99.45 ? 389  HIS C CB  1 
ATOM   7664  C  CG  . HIS C 1 389 ? -67.761 90.998  137.010 1.00 99.45 ? 389  HIS C CG  1 
ATOM   7665  N  ND1 . HIS C 1 389 ? -68.426 90.012  137.712 1.00 99.18 ? 389  HIS C ND1 1 
ATOM   7666  C  CD2 . HIS C 1 389 ? -68.484 92.132  137.175 1.00 99.45 ? 389  HIS C CD2 1 
ATOM   7667  C  CE1 . HIS C 1 389 ? -69.507 90.527  138.271 1.00 99.45 ? 389  HIS C CE1 1 
ATOM   7668  N  NE2 . HIS C 1 389 ? -69.566 91.811  137.960 1.00 99.45 ? 389  HIS C NE2 1 
ATOM   7669  N  N   . GLU C 1 390 ? -65.445 89.188  133.015 1.00 98.33 ? 390  GLU C N   1 
ATOM   7670  C  CA  . GLU C 1 390 ? -64.217 88.801  132.327 1.00 95.75 ? 390  GLU C CA  1 
ATOM   7671  C  C   . GLU C 1 390 ? -63.471 89.996  131.735 1.00 94.55 ? 390  GLU C C   1 
ATOM   7672  O  O   . GLU C 1 390 ? -64.074 90.901  131.136 1.00 92.23 ? 390  GLU C O   1 
ATOM   7673  C  CB  . GLU C 1 390 ? -64.526 87.778  131.227 1.00 96.23 ? 390  GLU C CB  1 
ATOM   7674  N  N   . HIS C 1 391 ? -62.153 89.999  131.933 1.00 92.71 ? 391  HIS C N   1 
ATOM   7675  C  CA  . HIS C 1 391 ? -61.307 91.053  131.395 1.00 90.58 ? 391  HIS C CA  1 
ATOM   7676  C  C   . HIS C 1 391 ? -60.684 90.499  130.118 1.00 91.42 ? 391  HIS C C   1 
ATOM   7677  O  O   . HIS C 1 391 ? -59.688 89.760  130.147 1.00 91.98 ? 391  HIS C O   1 
ATOM   7678  C  CB  . HIS C 1 391 ? -60.202 91.439  132.370 1.00 86.92 ? 391  HIS C CB  1 
ATOM   7679  C  CG  . HIS C 1 391 ? -59.357 92.573  131.883 1.00 84.17 ? 391  HIS C CG  1 
ATOM   7680  N  ND1 . HIS C 1 391 ? -58.095 92.826  132.373 1.00 83.13 ? 391  HIS C ND1 1 
ATOM   7681  C  CD2 . HIS C 1 391 ? -59.592 93.514  130.937 1.00 82.68 ? 391  HIS C CD2 1 
ATOM   7682  C  CE1 . HIS C 1 391 ? -57.587 93.873  131.747 1.00 83.18 ? 391  HIS C CE1 1 
ATOM   7683  N  NE2 . HIS C 1 391 ? -58.475 94.309  130.871 1.00 82.24 ? 391  HIS C NE2 1 
ATOM   7684  N  N   . ILE C 1 392 ? -61.294 90.862  128.999 1.00 90.54 ? 392  ILE C N   1 
ATOM   7685  C  CA  . ILE C 1 392 ? -60.851 90.411  127.703 1.00 88.63 ? 392  ILE C CA  1 
ATOM   7686  C  C   . ILE C 1 392 ? -60.088 91.535  127.034 1.00 86.58 ? 392  ILE C C   1 
ATOM   7687  O  O   . ILE C 1 392 ? -60.625 92.620  126.829 1.00 85.10 ? 392  ILE C O   1 
ATOM   7688  C  CB  . ILE C 1 392 ? -62.078 89.968  126.877 1.00 90.64 ? 392  ILE C CB  1 
ATOM   7689  C  CG1 . ILE C 1 392 ? -62.749 88.796  127.604 1.00 90.82 ? 392  ILE C CG1 1 
ATOM   7690  C  CG2 . ILE C 1 392 ? -61.674 89.558  125.469 1.00 90.44 ? 392  ILE C CG2 1 
ATOM   7691  C  CD1 . ILE C 1 392 ? -64.071 88.388  127.033 1.00 94.45 ? 392  ILE C CD1 1 
ATOM   7692  N  N   . THR C 1 393 ? -58.827 91.254  126.713 1.00 85.33 ? 393  THR C N   1 
ATOM   7693  C  CA  . THR C 1 393 ? -57.922 92.211  126.085 1.00 84.73 ? 393  THR C CA  1 
ATOM   7694  C  C   . THR C 1 393 ? -57.656 91.917  124.598 1.00 84.87 ? 393  THR C C   1 
ATOM   7695  O  O   . THR C 1 393 ? -57.736 90.768  124.163 1.00 84.32 ? 393  THR C O   1 
ATOM   7696  C  CB  . THR C 1 393 ? -56.574 92.203  126.825 1.00 84.78 ? 393  THR C CB  1 
ATOM   7697  O  OG1 . THR C 1 393 ? -56.803 92.211  128.246 1.00 82.31 ? 393  THR C OG1 1 
ATOM   7698  C  CG2 . THR C 1 393 ? -55.736 93.407  126.411 1.00 83.56 ? 393  THR C CG2 1 
ATOM   7699  N  N   . ALA C 1 394 ? -57.332 92.960  123.830 1.00 83.69 ? 394  ALA C N   1 
ATOM   7700  C  CA  . ALA C 1 394 ? -57.043 92.820  122.398 1.00 81.74 ? 394  ALA C CA  1 
ATOM   7701  C  C   . ALA C 1 394 ? -55.703 93.442  122.022 1.00 81.08 ? 394  ALA C C   1 
ATOM   7702  O  O   . ALA C 1 394 ? -55.662 94.500  121.398 1.00 82.15 ? 394  ALA C O   1 
ATOM   7703  C  CB  . ALA C 1 394 ? -58.168 93.446  121.566 1.00 78.95 ? 394  ALA C CB  1 
ATOM   7704  N  N   . ASN C 1 395 ? -54.619 92.775  122.411 1.00 80.86 ? 395  ASN C N   1 
ATOM   7705  C  CA  . ASN C 1 395 ? -53.242 93.233  122.152 1.00 80.41 ? 395  ASN C CA  1 
ATOM   7706  C  C   . ASN C 1 395 ? -52.837 93.066  120.659 1.00 80.07 ? 395  ASN C C   1 
ATOM   7707  O  O   . ASN C 1 395 ? -52.992 91.955  120.077 1.00 79.77 ? 395  ASN C O   1 
ATOM   7708  C  CB  . ASN C 1 395 ? -52.293 92.401  123.032 1.00 81.39 ? 395  ASN C CB  1 
ATOM   7709  C  CG  . ASN C 1 395 ? -50.835 92.877  123.144 1.00 81.63 ? 395  ASN C CG  1 
ATOM   7710  O  OD1 . ASN C 1 395 ? -50.520 94.037  122.923 1.00 82.72 ? 395  ASN C OD1 1 
ATOM   7711  N  ND2 . ASN C 1 395 ? -49.951 91.928  123.493 1.00 84.48 ? 395  ASN C ND2 1 
ATOM   7712  N  N   . PHE C 1 396 ? -52.346 94.140  120.033 1.00 78.26 ? 396  PHE C N   1 
ATOM   7713  C  CA  . PHE C 1 396 ? -51.938 94.060  118.633 1.00 75.84 ? 396  PHE C CA  1 
ATOM   7714  C  C   . PHE C 1 396 ? -50.479 93.594  118.586 1.00 75.41 ? 396  PHE C C   1 
ATOM   7715  O  O   . PHE C 1 396 ? -49.551 94.415  118.506 1.00 76.60 ? 396  PHE C O   1 
ATOM   7716  C  CB  . PHE C 1 396 ? -52.057 95.437  118.002 1.00 74.73 ? 396  PHE C CB  1 
ATOM   7717  C  CG  . PHE C 1 396 ? -51.816 95.455  116.509 1.00 74.28 ? 396  PHE C CG  1 
ATOM   7718  C  CD1 . PHE C 1 396 ? -52.782 94.959  115.633 1.00 74.11 ? 396  PHE C CD1 1 
ATOM   7719  C  CD2 . PHE C 1 396 ? -50.614 95.947  115.970 1.00 73.99 ? 396  PHE C CD2 1 
ATOM   7720  C  CE1 . PHE C 1 396 ? -52.570 94.942  114.233 1.00 75.59 ? 396  PHE C CE1 1 
ATOM   7721  C  CE2 . PHE C 1 396 ? -50.387 95.934  114.560 1.00 75.29 ? 396  PHE C CE2 1 
ATOM   7722  C  CZ  . PHE C 1 396 ? -51.376 95.427  113.695 1.00 75.07 ? 396  PHE C CZ  1 
ATOM   7723  N  N   . THR C 1 397 ? -50.288 92.280  118.624 1.00 72.69 ? 397  THR C N   1 
ATOM   7724  C  CA  . THR C 1 397 ? -48.964 91.687  118.635 1.00 70.07 ? 397  THR C CA  1 
ATOM   7725  C  C   . THR C 1 397 ? -48.554 91.175  117.245 1.00 70.10 ? 397  THR C C   1 
ATOM   7726  O  O   . THR C 1 397 ? -49.176 91.482  116.234 1.00 68.35 ? 397  THR C O   1 
ATOM   7727  C  CB  . THR C 1 397 ? -48.966 90.540  119.690 1.00 67.58 ? 397  THR C CB  1 
ATOM   7728  O  OG1 . THR C 1 397 ? -47.662 89.968  119.825 1.00 66.61 ? 397  THR C OG1 1 
ATOM   7729  C  CG2 . THR C 1 397 ? -49.963 89.466  119.293 1.00 68.18 ? 397  THR C CG2 1 
ATOM   7730  N  N   . GLN C 1 398 ? -47.479 90.404  117.209 1.00 72.49 ? 398  GLN C N   1 
ATOM   7731  C  CA  . GLN C 1 398 ? -46.987 89.803  115.979 1.00 72.68 ? 398  GLN C CA  1 
ATOM   7732  C  C   . GLN C 1 398 ? -46.915 88.324  116.281 1.00 71.54 ? 398  GLN C C   1 
ATOM   7733  O  O   . GLN C 1 398 ? -46.991 87.909  117.445 1.00 70.19 ? 398  GLN C O   1 
ATOM   7734  C  CB  . GLN C 1 398 ? -45.592 90.316  115.628 1.00 73.91 ? 398  GLN C CB  1 
ATOM   7735  C  CG  . GLN C 1 398 ? -45.546 91.790  115.293 1.00 76.35 ? 398  GLN C CG  1 
ATOM   7736  C  CD  . GLN C 1 398 ? -44.188 92.225  114.775 1.00 77.05 ? 398  GLN C CD  1 
ATOM   7737  O  OE1 . GLN C 1 398 ? -43.783 91.857  113.669 1.00 76.67 ? 398  GLN C OE1 1 
ATOM   7738  N  NE2 . GLN C 1 398 ? -43.470 93.008  115.580 1.00 76.53 ? 398  GLN C NE2 1 
ATOM   7739  N  N   . TYR C 1 399 ? -46.758 87.530  115.235 1.00 71.03 ? 399  TYR C N   1 
ATOM   7740  C  CA  . TYR C 1 399 ? -46.689 86.090  115.398 1.00 72.75 ? 399  TYR C CA  1 
ATOM   7741  C  C   . TYR C 1 399 ? -45.500 85.545  114.626 1.00 74.16 ? 399  TYR C C   1 
ATOM   7742  O  O   . TYR C 1 399 ? -45.090 84.397  114.906 1.00 77.57 ? 399  TYR C O   1 
ATOM   7743  C  CB  . TYR C 1 399 ? -47.999 85.440  114.918 1.00 69.36 ? 399  TYR C CB  1 
ATOM   7744  C  CG  . TYR C 1 399 ? -48.335 85.714  113.469 1.00 66.46 ? 399  TYR C CG  1 
ATOM   7745  C  CD1 . TYR C 1 399 ? -47.685 85.040  112.442 1.00 65.09 ? 399  TYR C CD1 1 
ATOM   7746  C  CD2 . TYR C 1 399 ? -49.292 86.675  113.126 1.00 66.41 ? 399  TYR C CD2 1 
ATOM   7747  C  CE1 . TYR C 1 399 ? -47.977 85.318  111.108 1.00 65.18 ? 399  TYR C CE1 1 
ATOM   7748  C  CE2 . TYR C 1 399 ? -49.593 86.961  111.801 1.00 63.64 ? 399  TYR C CE2 1 
ATOM   7749  C  CZ  . TYR C 1 399 ? -48.931 86.279  110.794 1.00 64.90 ? 399  TYR C CZ  1 
ATOM   7750  O  OH  . TYR C 1 399 ? -49.219 86.557  109.477 1.00 63.18 ? 399  TYR C OH  1 
ATOM   7751  O  OXT . TYR C 1 399 ? -45.004 86.275  113.743 1.00 74.32 ? 399  TYR C OXT 1 
ATOM   7752  N  N   . SER D 1 7   ? -62.703 36.738  101.477 1.00 85.85 ? 7    SER D N   1 
ATOM   7753  C  CA  . SER D 1 7   ? -63.490 35.507  101.162 1.00 87.09 ? 7    SER D CA  1 
ATOM   7754  C  C   . SER D 1 7   ? -62.676 34.552  100.291 1.00 86.88 ? 7    SER D C   1 
ATOM   7755  O  O   . SER D 1 7   ? -61.891 33.755  100.812 1.00 88.66 ? 7    SER D O   1 
ATOM   7756  C  CB  . SER D 1 7   ? -64.812 35.870  100.454 1.00 88.44 ? 7    SER D CB  1 
ATOM   7757  O  OG  . SER D 1 7   ? -65.599 34.720  100.151 1.00 84.97 ? 7    SER D OG  1 
ATOM   7758  N  N   . CYS D 1 8   ? -62.847 34.636  98.972  1.00 84.32 ? 8    CYS D N   1 
ATOM   7759  C  CA  . CYS D 1 8   ? -62.124 33.749  98.068  1.00 82.78 ? 8    CYS D CA  1 
ATOM   7760  C  C   . CYS D 1 8   ? -60.617 33.963  97.973  1.00 80.06 ? 8    CYS D C   1 
ATOM   7761  O  O   . CYS D 1 8   ? -59.981 33.459  97.045  1.00 78.84 ? 8    CYS D O   1 
ATOM   7762  C  CB  . CYS D 1 8   ? -62.724 33.787  96.661  1.00 82.48 ? 8    CYS D CB  1 
ATOM   7763  S  SG  . CYS D 1 8   ? -63.039 35.449  95.987  1.00 88.41 ? 8    CYS D SG  1 
ATOM   7764  N  N   . SER D 1 9   ? -60.044 34.697  98.920  1.00 76.08 ? 9    SER D N   1 
ATOM   7765  C  CA  . SER D 1 9   ? -58.603 34.907  98.912  1.00 75.69 ? 9    SER D CA  1 
ATOM   7766  C  C   . SER D 1 9   ? -57.924 33.540  98.857  1.00 73.06 ? 9    SER D C   1 
ATOM   7767  O  O   . SER D 1 9   ? -58.513 32.540  99.248  1.00 72.37 ? 9    SER D O   1 
ATOM   7768  C  CB  . SER D 1 9   ? -58.179 35.644  100.178 1.00 77.24 ? 9    SER D CB  1 
ATOM   7769  O  OG  . SER D 1 9   ? -58.754 35.038  101.318 1.00 77.32 ? 9    SER D OG  1 
ATOM   7770  N  N   . VAL D 1 10  ? -56.697 33.491  98.356  1.00 70.37 ? 10   VAL D N   1 
ATOM   7771  C  CA  . VAL D 1 10  ? -55.985 32.225  98.272  1.00 69.72 ? 10   VAL D CA  1 
ATOM   7772  C  C   . VAL D 1 10  ? -55.571 31.775  99.666  1.00 71.86 ? 10   VAL D C   1 
ATOM   7773  O  O   . VAL D 1 10  ? -54.840 32.484  100.361 1.00 70.43 ? 10   VAL D O   1 
ATOM   7774  C  CB  . VAL D 1 10  ? -54.732 32.346  97.401  1.00 68.17 ? 10   VAL D CB  1 
ATOM   7775  C  CG1 . VAL D 1 10  ? -53.867 31.103  97.539  1.00 65.40 ? 10   VAL D CG1 1 
ATOM   7776  C  CG2 . VAL D 1 10  ? -55.135 32.535  95.968  1.00 66.98 ? 10   VAL D CG2 1 
ATOM   7777  N  N   . PRO D 1 11  ? -56.023 30.576  100.084 1.00 73.91 ? 11   PRO D N   1 
ATOM   7778  C  CA  . PRO D 1 11  ? -55.706 30.021  101.405 1.00 75.04 ? 11   PRO D CA  1 
ATOM   7779  C  C   . PRO D 1 11  ? -54.206 29.879  101.634 1.00 78.07 ? 11   PRO D C   1 
ATOM   7780  O  O   . PRO D 1 11  ? -53.540 29.120  100.929 1.00 80.28 ? 11   PRO D O   1 
ATOM   7781  C  CB  . PRO D 1 11  ? -56.443 28.677  101.398 1.00 72.75 ? 11   PRO D CB  1 
ATOM   7782  C  CG  . PRO D 1 11  ? -56.455 28.290  99.955  1.00 71.91 ? 11   PRO D CG  1 
ATOM   7783  C  CD  . PRO D 1 11  ? -56.784 29.599  99.277  1.00 73.68 ? 11   PRO D CD  1 
ATOM   7784  N  N   . SER D 1 12  ? -53.682 30.624  102.610 1.00 80.64 ? 12   SER D N   1 
ATOM   7785  C  CA  . SER D 1 12  ? -52.250 30.603  102.944 1.00 82.31 ? 12   SER D CA  1 
ATOM   7786  C  C   . SER D 1 12  ? -51.835 29.176  103.240 1.00 81.30 ? 12   SER D C   1 
ATOM   7787  O  O   . SER D 1 12  ? -51.838 28.742  104.386 1.00 83.24 ? 12   SER D O   1 
ATOM   7788  C  CB  . SER D 1 12  ? -51.977 31.509  104.156 1.00 84.55 ? 12   SER D CB  1 
ATOM   7789  O  OG  . SER D 1 12  ? -53.152 31.665  104.941 1.00 87.24 ? 12   SER D OG  1 
ATOM   7790  N  N   . ALA D 1 13  ? -51.482 28.453  102.187 1.00 78.81 ? 13   ALA D N   1 
ATOM   7791  C  CA  . ALA D 1 13  ? -51.103 27.049  102.273 1.00 76.19 ? 13   ALA D CA  1 
ATOM   7792  C  C   . ALA D 1 13  ? -50.894 26.682  100.830 1.00 74.49 ? 13   ALA D C   1 
ATOM   7793  O  O   . ALA D 1 13  ? -50.111 25.800  100.493 1.00 74.01 ? 13   ALA D O   1 
ATOM   7794  C  CB  . ALA D 1 13  ? -52.249 26.227  102.856 1.00 76.86 ? 13   ALA D CB  1 
ATOM   7795  N  N   . GLN D 1 14  ? -51.636 27.382  99.984  1.00 73.54 ? 14   GLN D N   1 
ATOM   7796  C  CA  . GLN D 1 14  ? -51.556 27.215  98.547  1.00 73.00 ? 14   GLN D CA  1 
ATOM   7797  C  C   . GLN D 1 14  ? -50.674 28.345  98.029  1.00 70.59 ? 14   GLN D C   1 
ATOM   7798  O  O   . GLN D 1 14  ? -50.234 28.324  96.881  1.00 72.19 ? 14   GLN D O   1 
ATOM   7799  C  CB  . GLN D 1 14  ? -52.951 27.317  97.911  1.00 74.91 ? 14   GLN D CB  1 
ATOM   7800  C  CG  . GLN D 1 14  ? -53.963 26.309  98.433  1.00 76.76 ? 14   GLN D CG  1 
ATOM   7801  C  CD  . GLN D 1 14  ? -53.438 24.887  98.364  1.00 78.66 ? 14   GLN D CD  1 
ATOM   7802  O  OE1 . GLN D 1 14  ? -52.474 24.536  99.055  1.00 82.07 ? 14   GLN D OE1 1 
ATOM   7803  N  NE2 . GLN D 1 14  ? -54.059 24.061  97.527  1.00 76.96 ? 14   GLN D NE2 1 
ATOM   7804  N  N   . GLU D 1 15  ? -50.408 29.322  98.893  1.00 66.60 ? 15   GLU D N   1 
ATOM   7805  C  CA  . GLU D 1 15  ? -49.610 30.476  98.515  1.00 64.43 ? 15   GLU D CA  1 
ATOM   7806  C  C   . GLU D 1 15  ? -48.292 30.138  97.837  1.00 60.72 ? 15   GLU D C   1 
ATOM   7807  O  O   . GLU D 1 15  ? -47.865 30.839  96.925  1.00 59.35 ? 15   GLU D O   1 
ATOM   7808  C  CB  . GLU D 1 15  ? -49.376 31.368  99.728  1.00 66.70 ? 15   GLU D CB  1 
ATOM   7809  C  CG  . GLU D 1 15  ? -50.680 31.900  100.305 1.00 74.82 ? 15   GLU D CG  1 
ATOM   7810  C  CD  . GLU D 1 15  ? -50.496 33.105  101.228 1.00 80.16 ? 15   GLU D CD  1 
ATOM   7811  O  OE1 . GLU D 1 15  ? -49.561 33.099  102.062 1.00 82.71 ? 15   GLU D OE1 1 
ATOM   7812  O  OE2 . GLU D 1 15  ? -51.300 34.058  101.130 1.00 82.68 ? 15   GLU D OE2 1 
ATOM   7813  N  N   . PRO D 1 16  ? -47.627 29.063  98.275  1.00 58.48 ? 16   PRO D N   1 
ATOM   7814  C  CA  . PRO D 1 16  ? -46.349 28.682  97.657  1.00 55.88 ? 16   PRO D CA  1 
ATOM   7815  C  C   . PRO D 1 16  ? -46.545 28.393  96.160  1.00 54.02 ? 16   PRO D C   1 
ATOM   7816  O  O   . PRO D 1 16  ? -45.626 28.563  95.342  1.00 51.42 ? 16   PRO D O   1 
ATOM   7817  C  CB  . PRO D 1 16  ? -45.948 27.447  98.459  1.00 54.92 ? 16   PRO D CB  1 
ATOM   7818  C  CG  . PRO D 1 16  ? -46.530 27.748  99.822  1.00 52.22 ? 16   PRO D CG  1 
ATOM   7819  C  CD  . PRO D 1 16  ? -47.891 28.266  99.489  1.00 53.46 ? 16   PRO D CD  1 
ATOM   7820  N  N   . LEU D 1 17  ? -47.759 27.965  95.824  1.00 51.42 ? 17   LEU D N   1 
ATOM   7821  C  CA  . LEU D 1 17  ? -48.160 27.674  94.441  1.00 53.10 ? 17   LEU D CA  1 
ATOM   7822  C  C   . LEU D 1 17  ? -48.110 28.979  93.612  1.00 50.09 ? 17   LEU D C   1 
ATOM   7823  O  O   . LEU D 1 17  ? -47.574 29.020  92.497  1.00 50.01 ? 17   LEU D O   1 
ATOM   7824  C  CB  . LEU D 1 17  ? -49.584 27.103  94.442  1.00 52.23 ? 17   LEU D CB  1 
ATOM   7825  C  CG  . LEU D 1 17  ? -49.876 25.838  93.635  1.00 53.50 ? 17   LEU D CG  1 
ATOM   7826  C  CD1 . LEU D 1 17  ? -48.661 24.924  93.613  1.00 51.76 ? 17   LEU D CD1 1 
ATOM   7827  C  CD2 . LEU D 1 17  ? -51.087 25.132  94.250  1.00 51.12 ? 17   LEU D CD2 1 
ATOM   7828  N  N   . VAL D 1 18  ? -48.664 30.037  94.198  1.00 47.70 ? 18   VAL D N   1 
ATOM   7829  C  CA  . VAL D 1 18  ? -48.696 31.366  93.608  1.00 47.23 ? 18   VAL D CA  1 
ATOM   7830  C  C   . VAL D 1 18  ? -47.289 31.975  93.527  1.00 47.63 ? 18   VAL D C   1 
ATOM   7831  O  O   . VAL D 1 18  ? -46.897 32.540  92.496  1.00 47.09 ? 18   VAL D O   1 
ATOM   7832  C  CB  . VAL D 1 18  ? -49.588 32.297  94.449  1.00 45.32 ? 18   VAL D CB  1 
ATOM   7833  C  CG1 . VAL D 1 18  ? -49.749 33.639  93.761  1.00 44.72 ? 18   VAL D CG1 1 
ATOM   7834  C  CG2 . VAL D 1 18  ? -50.925 31.661  94.650  1.00 46.29 ? 18   VAL D CG2 1 
ATOM   7835  N  N   . ASN D 1 19  ? -46.536 31.868  94.615  1.00 47.43 ? 19   ASN D N   1 
ATOM   7836  C  CA  . ASN D 1 19  ? -45.182 32.405  94.626  1.00 50.17 ? 19   ASN D CA  1 
ATOM   7837  C  C   . ASN D 1 19  ? -44.372 31.780  93.507  1.00 48.57 ? 19   ASN D C   1 
ATOM   7838  O  O   . ASN D 1 19  ? -43.601 32.467  92.826  1.00 49.68 ? 19   ASN D O   1 
ATOM   7839  C  CB  . ASN D 1 19  ? -44.493 32.143  95.966  1.00 51.58 ? 19   ASN D CB  1 
ATOM   7840  C  CG  . ASN D 1 19  ? -45.286 32.701  97.155  1.00 55.39 ? 19   ASN D CG  1 
ATOM   7841  O  OD1 . ASN D 1 19  ? -46.217 33.503  96.989  1.00 52.55 ? 19   ASN D OD1 1 
ATOM   7842  N  ND2 . ASN D 1 19  ? -44.914 32.275  98.360  1.00 54.43 ? 19   ASN D ND2 1 
ATOM   7843  N  N   . GLY D 1 20  ? -44.563 30.483  93.304  1.00 46.17 ? 20   GLY D N   1 
ATOM   7844  C  CA  . GLY D 1 20  ? -43.828 29.807  92.253  1.00 43.40 ? 20   GLY D CA  1 
ATOM   7845  C  C   . GLY D 1 20  ? -44.006 30.433  90.880  1.00 43.91 ? 20   GLY D C   1 
ATOM   7846  O  O   . GLY D 1 20  ? -43.023 30.643  90.139  1.00 46.30 ? 20   GLY D O   1 
ATOM   7847  N  N   . ILE D 1 21  ? -45.248 30.740  90.516  1.00 40.01 ? 21   ILE D N   1 
ATOM   7848  C  CA  . ILE D 1 21  ? -45.446 31.312  89.205  1.00 41.01 ? 21   ILE D CA  1 
ATOM   7849  C  C   . ILE D 1 21  ? -44.951 32.753  89.162  1.00 43.72 ? 21   ILE D C   1 
ATOM   7850  O  O   . ILE D 1 21  ? -44.499 33.225  88.116  1.00 45.23 ? 21   ILE D O   1 
ATOM   7851  C  CB  . ILE D 1 21  ? -46.907 31.222  88.748  1.00 37.34 ? 21   ILE D CB  1 
ATOM   7852  C  CG1 . ILE D 1 21  ? -47.823 32.043  89.649  1.00 35.10 ? 21   ILE D CG1 1 
ATOM   7853  C  CG2 . ILE D 1 21  ? -47.329 29.760  88.705  1.00 36.98 ? 21   ILE D CG2 1 
ATOM   7854  C  CD1 . ILE D 1 21  ? -49.274 31.964  89.218  1.00 26.80 ? 21   ILE D CD1 1 
ATOM   7855  N  N   . GLN D 1 22  ? -45.009 33.448  90.298  1.00 42.34 ? 22   GLN D N   1 
ATOM   7856  C  CA  . GLN D 1 22  ? -44.519 34.812  90.329  1.00 39.81 ? 22   GLN D CA  1 
ATOM   7857  C  C   . GLN D 1 22  ? -43.028 34.803  90.038  1.00 42.14 ? 22   GLN D C   1 
ATOM   7858  O  O   . GLN D 1 22  ? -42.492 35.735  89.408  1.00 43.28 ? 22   GLN D O   1 
ATOM   7859  C  CB  . GLN D 1 22  ? -44.743 35.469  91.682  1.00 34.88 ? 22   GLN D CB  1 
ATOM   7860  C  CG  . GLN D 1 22  ? -44.215 36.899  91.716  1.00 32.12 ? 22   GLN D CG  1 
ATOM   7861  C  CD  . GLN D 1 22  ? -44.646 37.650  92.957  1.00 36.72 ? 22   GLN D CD  1 
ATOM   7862  O  OE1 . GLN D 1 22  ? -45.563 37.219  93.660  1.00 37.65 ? 22   GLN D OE1 1 
ATOM   7863  N  NE2 . GLN D 1 22  ? -43.990 38.789  93.236  1.00 35.26 ? 22   GLN D NE2 1 
ATOM   7864  N  N   . VAL D 1 23  ? -42.354 33.748  90.488  1.00 40.86 ? 23   VAL D N   1 
ATOM   7865  C  CA  . VAL D 1 23  ? -40.930 33.665  90.249  1.00 40.43 ? 23   VAL D CA  1 
ATOM   7866  C  C   . VAL D 1 23  ? -40.673 33.380  88.790  1.00 40.39 ? 23   VAL D C   1 
ATOM   7867  O  O   . VAL D 1 23  ? -39.757 33.946  88.204  1.00 42.42 ? 23   VAL D O   1 
ATOM   7868  C  CB  . VAL D 1 23  ? -40.247 32.602  91.133  1.00 38.73 ? 23   VAL D CB  1 
ATOM   7869  C  CG1 . VAL D 1 23  ? -38.789 32.507  90.773  1.00 32.40 ? 23   VAL D CG1 1 
ATOM   7870  C  CG2 . VAL D 1 23  ? -40.357 33.011  92.608  1.00 33.34 ? 23   VAL D CG2 1 
ATOM   7871  N  N   . LEU D 1 24  ? -41.486 32.529  88.185  1.00 39.37 ? 24   LEU D N   1 
ATOM   7872  C  CA  . LEU D 1 24  ? -41.279 32.253  86.775  1.00 41.57 ? 24   LEU D CA  1 
ATOM   7873  C  C   . LEU D 1 24  ? -41.408 33.564  85.975  1.00 43.27 ? 24   LEU D C   1 
ATOM   7874  O  O   . LEU D 1 24  ? -40.581 33.888  85.103  1.00 46.08 ? 24   LEU D O   1 
ATOM   7875  C  CB  . LEU D 1 24  ? -42.297 31.199  86.294  1.00 39.27 ? 24   LEU D CB  1 
ATOM   7876  C  CG  . LEU D 1 24  ? -42.092 29.780  86.885  1.00 39.39 ? 24   LEU D CG  1 
ATOM   7877  C  CD1 . LEU D 1 24  ? -43.102 28.812  86.301  1.00 36.70 ? 24   LEU D CD1 1 
ATOM   7878  C  CD2 . LEU D 1 24  ? -40.669 29.278  86.582  1.00 32.82 ? 24   LEU D CD2 1 
ATOM   7879  N  N   . MET D 1 25  ? -42.436 34.335  86.309  1.00 43.79 ? 25   MET D N   1 
ATOM   7880  C  CA  . MET D 1 25  ? -42.722 35.588  85.623  1.00 44.78 ? 25   MET D CA  1 
ATOM   7881  C  C   . MET D 1 25  ? -41.610 36.606  85.781  1.00 44.57 ? 25   MET D C   1 
ATOM   7882  O  O   . MET D 1 25  ? -41.159 37.208  84.803  1.00 43.87 ? 25   MET D O   1 
ATOM   7883  C  CB  . MET D 1 25  ? -44.043 36.172  86.135  1.00 46.15 ? 25   MET D CB  1 
ATOM   7884  C  CG  . MET D 1 25  ? -44.513 37.400  85.382  1.00 42.93 ? 25   MET D CG  1 
ATOM   7885  S  SD  . MET D 1 25  ? -45.868 38.236  86.228  1.00 42.24 ? 25   MET D SD  1 
ATOM   7886  C  CE  . MET D 1 25  ? -44.992 38.940  87.669  1.00 41.77 ? 25   MET D CE  1 
ATOM   7887  N  N   . GLU D 1 26  ? -41.171 36.806  87.016  1.00 45.49 ? 26   GLU D N   1 
ATOM   7888  C  CA  . GLU D 1 26  ? -40.101 37.746  87.265  1.00 46.49 ? 26   GLU D CA  1 
ATOM   7889  C  C   . GLU D 1 26  ? -38.801 37.313  86.578  1.00 47.79 ? 26   GLU D C   1 
ATOM   7890  O  O   . GLU D 1 26  ? -38.091 38.139  85.977  1.00 46.88 ? 26   GLU D O   1 
ATOM   7891  C  CB  . GLU D 1 26  ? -39.899 37.903  88.757  1.00 46.32 ? 26   GLU D CB  1 
ATOM   7892  C  CG  . GLU D 1 26  ? -41.034 38.650  89.414  1.00 47.99 ? 26   GLU D CG  1 
ATOM   7893  C  CD  . GLU D 1 26  ? -40.747 38.972  90.864  1.00 52.03 ? 26   GLU D CD  1 
ATOM   7894  O  OE1 . GLU D 1 26  ? -39.644 38.612  91.332  1.00 56.09 ? 26   GLU D OE1 1 
ATOM   7895  O  OE2 . GLU D 1 26  ? -41.607 39.582  91.539  1.00 53.14 ? 26   GLU D OE2 1 
ATOM   7896  N  N   . ASN D 1 27  ? -38.504 36.021  86.637  1.00 47.29 ? 27   ASN D N   1 
ATOM   7897  C  CA  . ASN D 1 27  ? -37.295 35.497  86.005  1.00 48.69 ? 27   ASN D CA  1 
ATOM   7898  C  C   . ASN D 1 27  ? -37.177 35.887  84.543  1.00 47.53 ? 27   ASN D C   1 
ATOM   7899  O  O   . ASN D 1 27  ? -36.065 36.101  84.062  1.00 50.03 ? 27   ASN D O   1 
ATOM   7900  C  CB  . ASN D 1 27  ? -37.232 33.964  86.092  1.00 47.46 ? 27   ASN D CB  1 
ATOM   7901  C  CG  . ASN D 1 27  ? -36.824 33.455  87.472  1.00 50.92 ? 27   ASN D CG  1 
ATOM   7902  O  OD1 . ASN D 1 27  ? -36.798 32.246  87.679  1.00 57.55 ? 27   ASN D OD1 1 
ATOM   7903  N  ND2 . ASN D 1 27  ? -36.511 34.361  88.417  1.00 42.88 ? 27   ASN D ND2 1 
ATOM   7904  N  N   . SER D 1 28  ? -38.307 35.978  83.841  1.00 46.15 ? 28   SER D N   1 
ATOM   7905  C  CA  . SER D 1 28  ? -38.300 36.314  82.410  1.00 45.14 ? 28   SER D CA  1 
ATOM   7906  C  C   . SER D 1 28  ? -37.868 37.765  82.078  1.00 43.60 ? 28   SER D C   1 
ATOM   7907  O  O   . SER D 1 28  ? -37.600 38.097  80.928  1.00 42.16 ? 28   SER D O   1 
ATOM   7908  C  CB  . SER D 1 28  ? -39.680 36.008  81.799  1.00 41.63 ? 28   SER D CB  1 
ATOM   7909  O  OG  . SER D 1 28  ? -40.557 37.105  81.933  1.00 38.95 ? 28   SER D OG  1 
ATOM   7910  N  N   . VAL D 1 29  ? -37.782 38.615  83.088  1.00 43.78 ? 29   VAL D N   1 
ATOM   7911  C  CA  . VAL D 1 29  ? -37.371 39.996  82.872  1.00 47.62 ? 29   VAL D CA  1 
ATOM   7912  C  C   . VAL D 1 29  ? -35.844 40.058  82.683  1.00 49.99 ? 29   VAL D C   1 
ATOM   7913  O  O   . VAL D 1 29  ? -35.087 39.673  83.569  1.00 50.57 ? 29   VAL D O   1 
ATOM   7914  C  CB  . VAL D 1 29  ? -37.802 40.855  84.085  1.00 47.87 ? 29   VAL D CB  1 
ATOM   7915  C  CG1 . VAL D 1 29  ? -37.447 42.313  83.859  1.00 45.20 ? 29   VAL D CG1 1 
ATOM   7916  C  CG2 . VAL D 1 29  ? -39.308 40.676  84.321  1.00 43.99 ? 29   VAL D CG2 1 
ATOM   7917  N  N   . THR D 1 30  ? -35.390 40.534  81.530  1.00 53.86 ? 30   THR D N   1 
ATOM   7918  C  CA  . THR D 1 30  ? -33.951 40.609  81.249  1.00 59.52 ? 30   THR D CA  1 
ATOM   7919  C  C   . THR D 1 30  ? -33.685 41.741  80.248  1.00 65.18 ? 30   THR D C   1 
ATOM   7920  O  O   . THR D 1 30  ? -34.596 42.178  79.535  1.00 66.73 ? 30   THR D O   1 
ATOM   7921  C  CB  . THR D 1 30  ? -33.387 39.248  80.657  1.00 58.54 ? 30   THR D CB  1 
ATOM   7922  O  OG1 . THR D 1 30  ? -33.931 38.993  79.349  1.00 57.98 ? 30   THR D OG1 1 
ATOM   7923  C  CG2 . THR D 1 30  ? -33.745 38.082  81.553  1.00 55.84 ? 30   THR D CG2 1 
ATOM   7924  N  N   . SER D 1 31  ? -32.441 42.211  80.188  1.00 69.51 ? 31   SER D N   1 
ATOM   7925  C  CA  . SER D 1 31  ? -32.065 43.301  79.277  1.00 72.80 ? 31   SER D CA  1 
ATOM   7926  C  C   . SER D 1 31  ? -32.531 43.105  77.827  1.00 73.52 ? 31   SER D C   1 
ATOM   7927  O  O   . SER D 1 31  ? -32.928 44.062  77.154  1.00 76.06 ? 31   SER D O   1 
ATOM   7928  C  CB  . SER D 1 31  ? -30.546 43.491  79.299  1.00 74.28 ? 31   SER D CB  1 
ATOM   7929  O  OG  . SER D 1 31  ? -30.093 43.780  80.614  1.00 77.90 ? 31   SER D OG  1 
ATOM   7930  N  N   . SER D 1 32  ? -32.481 41.866  77.356  1.00 72.46 ? 32   SER D N   1 
ATOM   7931  C  CA  . SER D 1 32  ? -32.882 41.537  75.995  1.00 72.94 ? 32   SER D CA  1 
ATOM   7932  C  C   . SER D 1 32  ? -34.381 41.218  75.828  1.00 73.87 ? 32   SER D C   1 
ATOM   7933  O  O   . SER D 1 32  ? -34.948 41.414  74.743  1.00 74.58 ? 32   SER D O   1 
ATOM   7934  C  CB  . SER D 1 32  ? -32.037 40.363  75.514  1.00 73.56 ? 32   SER D CB  1 
ATOM   7935  O  OG  . SER D 1 32  ? -31.911 39.398  76.548  1.00 73.98 ? 32   SER D OG  1 
ATOM   7936  N  N   . ALA D 1 33  ? -35.025 40.714  76.880  1.00 71.24 ? 33   ALA D N   1 
ATOM   7937  C  CA  . ALA D 1 33  ? -36.441 40.410  76.782  1.00 68.39 ? 33   ALA D CA  1 
ATOM   7938  C  C   . ALA D 1 33  ? -37.163 41.715  76.463  1.00 68.89 ? 33   ALA D C   1 
ATOM   7939  O  O   . ALA D 1 33  ? -36.780 42.783  76.965  1.00 70.58 ? 33   ALA D O   1 
ATOM   7940  C  CB  . ALA D 1 33  ? -36.943 39.847  78.093  1.00 65.57 ? 33   ALA D CB  1 
ATOM   7941  N  N   . TYR D 1 34  ? -38.182 41.644  75.611  1.00 68.04 ? 34   TYR D N   1 
ATOM   7942  C  CA  . TYR D 1 34  ? -38.965 42.833  75.274  1.00 65.06 ? 34   TYR D CA  1 
ATOM   7943  C  C   . TYR D 1 34  ? -39.794 43.167  76.536  1.00 58.06 ? 34   TYR D C   1 
ATOM   7944  O  O   . TYR D 1 34  ? -40.435 42.285  77.119  1.00 58.89 ? 34   TYR D O   1 
ATOM   7945  C  CB  . TYR D 1 34  ? -39.871 42.531  74.078  1.00 72.55 ? 34   TYR D CB  1 
ATOM   7946  C  CG  . TYR D 1 34  ? -40.645 43.723  73.546  1.00 81.13 ? 34   TYR D CG  1 
ATOM   7947  C  CD1 . TYR D 1 34  ? -39.994 44.781  72.895  1.00 81.71 ? 34   TYR D CD1 1 
ATOM   7948  C  CD2 . TYR D 1 34  ? -42.046 43.781  73.679  1.00 83.97 ? 34   TYR D CD2 1 
ATOM   7949  C  CE1 . TYR D 1 34  ? -40.724 45.873  72.386  1.00 87.67 ? 34   TYR D CE1 1 
ATOM   7950  C  CE2 . TYR D 1 34  ? -42.788 44.860  73.174  1.00 87.51 ? 34   TYR D CE2 1 
ATOM   7951  C  CZ  . TYR D 1 34  ? -42.128 45.905  72.526  1.00 89.69 ? 34   TYR D CZ  1 
ATOM   7952  O  OH  . TYR D 1 34  ? -42.883 46.950  72.004  1.00 90.22 ? 34   TYR D OH  1 
ATOM   7953  N  N   . PRO D 1 35  ? -39.799 44.445  76.959  1.00 49.83 ? 35   PRO D N   1 
ATOM   7954  C  CA  . PRO D 1 35  ? -40.514 44.942  78.144  1.00 44.83 ? 35   PRO D CA  1 
ATOM   7955  C  C   . PRO D 1 35  ? -42.021 44.697  78.168  1.00 42.05 ? 35   PRO D C   1 
ATOM   7956  O  O   . PRO D 1 35  ? -42.757 45.282  77.370  1.00 36.71 ? 35   PRO D O   1 
ATOM   7957  C  CB  . PRO D 1 35  ? -40.215 46.449  78.148  1.00 45.40 ? 35   PRO D CB  1 
ATOM   7958  C  CG  . PRO D 1 35  ? -39.257 46.675  76.995  1.00 49.25 ? 35   PRO D CG  1 
ATOM   7959  C  CD  . PRO D 1 35  ? -39.493 45.558  76.048  1.00 49.12 ? 35   PRO D CD  1 
ATOM   7960  N  N   . ASN D 1 36  ? -42.480 43.865  79.104  1.00 39.68 ? 36   ASN D N   1 
ATOM   7961  C  CA  . ASN D 1 36  ? -43.898 43.585  79.224  1.00 39.29 ? 36   ASN D CA  1 
ATOM   7962  C  C   . ASN D 1 36  ? -44.525 44.364  80.388  1.00 41.04 ? 36   ASN D C   1 
ATOM   7963  O  O   . ASN D 1 36  ? -44.391 43.982  81.568  1.00 44.58 ? 36   ASN D O   1 
ATOM   7964  C  CB  . ASN D 1 36  ? -44.139 42.092  79.401  1.00 36.95 ? 36   ASN D CB  1 
ATOM   7965  C  CG  . ASN D 1 36  ? -45.613 41.739  79.324  1.00 42.01 ? 36   ASN D CG  1 
ATOM   7966  O  OD1 . ASN D 1 36  ? -45.985 40.590  79.049  1.00 41.90 ? 36   ASN D OD1 1 
ATOM   7967  N  ND2 . ASN D 1 36  ? -46.471 42.738  79.571  1.00 42.13 ? 36   ASN D ND2 1 
ATOM   7968  N  N   . PRO D 1 37  ? -45.257 45.448  80.068  1.00 38.01 ? 37   PRO D N   1 
ATOM   7969  C  CA  . PRO D 1 37  ? -45.886 46.259  81.118  1.00 34.40 ? 37   PRO D CA  1 
ATOM   7970  C  C   . PRO D 1 37  ? -46.861 45.484  82.002  1.00 34.44 ? 37   PRO D C   1 
ATOM   7971  O  O   . PRO D 1 37  ? -46.984 45.760  83.194  1.00 33.24 ? 37   PRO D O   1 
ATOM   7972  C  CB  . PRO D 1 37  ? -46.524 47.414  80.331  1.00 32.43 ? 37   PRO D CB  1 
ATOM   7973  C  CG  . PRO D 1 37  ? -46.844 46.786  79.016  1.00 31.61 ? 37   PRO D CG  1 
ATOM   7974  C  CD  . PRO D 1 37  ? -45.636 45.918  78.724  1.00 29.07 ? 37   PRO D CD  1 
ATOM   7975  N  N   . SER D 1 38  ? -47.548 44.499  81.429  1.00 37.94 ? 38   SER D N   1 
ATOM   7976  C  CA  . SER D 1 38  ? -48.492 43.700  82.223  1.00 37.15 ? 38   SER D CA  1 
ATOM   7977  C  C   . SER D 1 38  ? -47.748 43.020  83.375  1.00 37.39 ? 38   SER D C   1 
ATOM   7978  O  O   . SER D 1 38  ? -48.259 42.920  84.486  1.00 37.89 ? 38   SER D O   1 
ATOM   7979  C  CB  . SER D 1 38  ? -49.168 42.648  81.346  1.00 37.05 ? 38   SER D CB  1 
ATOM   7980  O  OG  . SER D 1 38  ? -49.983 43.264  80.375  1.00 34.99 ? 38   SER D OG  1 
ATOM   7981  N  N   . ILE D 1 39  ? -46.531 42.558  83.099  1.00 38.76 ? 39   ILE D N   1 
ATOM   7982  C  CA  . ILE D 1 39  ? -45.704 41.925  84.117  1.00 39.34 ? 39   ILE D CA  1 
ATOM   7983  C  C   . ILE D 1 39  ? -45.327 42.917  85.231  1.00 41.79 ? 39   ILE D C   1 
ATOM   7984  O  O   . ILE D 1 39  ? -45.434 42.606  86.438  1.00 39.73 ? 39   ILE D O   1 
ATOM   7985  C  CB  . ILE D 1 39  ? -44.421 41.388  83.511  1.00 40.77 ? 39   ILE D CB  1 
ATOM   7986  C  CG1 . ILE D 1 39  ? -44.751 40.325  82.468  1.00 38.82 ? 39   ILE D CG1 1 
ATOM   7987  C  CG2 . ILE D 1 39  ? -43.560 40.778  84.591  1.00 37.97 ? 39   ILE D CG2 1 
ATOM   7988  C  CD1 . ILE D 1 39  ? -43.543 39.566  82.011  1.00 31.89 ? 39   ILE D CD1 1 
ATOM   7989  N  N   . LEU D 1 40  ? -44.879 44.108  84.829  1.00 39.77 ? 40   LEU D N   1 
ATOM   7990  C  CA  . LEU D 1 40  ? -44.532 45.119  85.813  1.00 39.45 ? 40   LEU D CA  1 
ATOM   7991  C  C   . LEU D 1 40  ? -45.750 45.410  86.699  1.00 39.72 ? 40   LEU D C   1 
ATOM   7992  O  O   . LEU D 1 40  ? -45.632 45.528  87.916  1.00 37.51 ? 40   LEU D O   1 
ATOM   7993  C  CB  . LEU D 1 40  ? -44.075 46.404  85.139  1.00 39.56 ? 40   LEU D CB  1 
ATOM   7994  C  CG  . LEU D 1 40  ? -43.714 47.493  86.158  1.00 38.56 ? 40   LEU D CG  1 
ATOM   7995  C  CD1 . LEU D 1 40  ? -42.840 46.924  87.292  1.00 33.55 ? 40   LEU D CD1 1 
ATOM   7996  C  CD2 . LEU D 1 40  ? -42.988 48.611  85.425  1.00 34.32 ? 40   LEU D CD2 1 
ATOM   7997  N  N   . ILE D 1 41  ? -46.924 45.511  86.089  1.00 38.49 ? 41   ILE D N   1 
ATOM   7998  C  CA  . ILE D 1 41  ? -48.121 45.760  86.870  1.00 36.93 ? 41   ILE D CA  1 
ATOM   7999  C  C   . ILE D 1 41  ? -48.371 44.587  87.808  1.00 39.61 ? 41   ILE D C   1 
ATOM   8000  O  O   . ILE D 1 41  ? -48.756 44.774  88.981  1.00 40.73 ? 41   ILE D O   1 
ATOM   8001  C  CB  . ILE D 1 41  ? -49.350 45.957  85.966  1.00 33.02 ? 41   ILE D CB  1 
ATOM   8002  C  CG1 . ILE D 1 41  ? -49.248 47.294  85.260  1.00 30.26 ? 41   ILE D CG1 1 
ATOM   8003  C  CG2 . ILE D 1 41  ? -50.640 45.914  86.787  1.00 32.46 ? 41   ILE D CG2 1 
ATOM   8004  C  CD1 . ILE D 1 41  ? -50.283 47.474  84.173  1.00 26.33 ? 41   ILE D CD1 1 
ATOM   8005  N  N   . ALA D 1 42  ? -48.149 43.375  87.309  1.00 37.79 ? 42   ALA D N   1 
ATOM   8006  C  CA  . ALA D 1 42  ? -48.375 42.212  88.155  1.00 39.08 ? 42   ALA D CA  1 
ATOM   8007  C  C   . ALA D 1 42  ? -47.454 42.239  89.374  1.00 39.49 ? 42   ALA D C   1 
ATOM   8008  O  O   . ALA D 1 42  ? -47.916 42.155  90.508  1.00 36.06 ? 42   ALA D O   1 
ATOM   8009  C  CB  . ALA D 1 42  ? -48.172 40.925  87.359  1.00 43.75 ? 42   ALA D CB  1 
ATOM   8010  N  N   . MET D 1 43  ? -46.151 42.389  89.163  1.00 41.50 ? 43   MET D N   1 
ATOM   8011  C  CA  . MET D 1 43  ? -45.285 42.405  90.322  1.00 43.36 ? 43   MET D CA  1 
ATOM   8012  C  C   . MET D 1 43  ? -45.498 43.571  91.273  1.00 43.18 ? 43   MET D C   1 
ATOM   8013  O  O   . MET D 1 43  ? -45.349 43.404  92.477  1.00 47.61 ? 43   MET D O   1 
ATOM   8014  C  CB  . MET D 1 43  ? -43.813 42.291  89.925  1.00 44.91 ? 43   MET D CB  1 
ATOM   8015  C  CG  . MET D 1 43  ? -43.387 43.109  88.748  1.00 51.43 ? 43   MET D CG  1 
ATOM   8016  S  SD  . MET D 1 43  ? -41.782 42.496  88.091  1.00 56.62 ? 43   MET D SD  1 
ATOM   8017  C  CE  . MET D 1 43  ? -40.699 42.872  89.449  1.00 50.84 ? 43   MET D CE  1 
ATOM   8018  N  N   . ASN D 1 44  ? -45.880 44.738  90.780  1.00 40.69 ? 44   ASN D N   1 
ATOM   8019  C  CA  . ASN D 1 44  ? -46.081 45.864  91.692  1.00 38.69 ? 44   ASN D CA  1 
ATOM   8020  C  C   . ASN D 1 44  ? -47.336 45.650  92.526  1.00 39.64 ? 44   ASN D C   1 
ATOM   8021  O  O   . ASN D 1 44  ? -47.409 46.033  93.682  1.00 41.19 ? 44   ASN D O   1 
ATOM   8022  C  CB  . ASN D 1 44  ? -46.164 47.196  90.919  1.00 33.44 ? 44   ASN D CB  1 
ATOM   8023  C  CG  . ASN D 1 44  ? -44.816 47.604  90.352  1.00 36.90 ? 44   ASN D CG  1 
ATOM   8024  O  OD1 . ASN D 1 44  ? -43.784 47.176  90.881  1.00 38.40 ? 44   ASN D OD1 1 
ATOM   8025  N  ND2 . ASN D 1 44  ? -44.801 48.428  89.291  1.00 25.92 ? 44   ASN D ND2 1 
ATOM   8026  N  N   . LEU D 1 45  ? -48.324 45.018  91.927  1.00 40.54 ? 45   LEU D N   1 
ATOM   8027  C  CA  . LEU D 1 45  ? -49.573 44.766  92.601  1.00 40.75 ? 45   LEU D CA  1 
ATOM   8028  C  C   . LEU D 1 45  ? -49.407 43.597  93.602  1.00 44.44 ? 45   LEU D C   1 
ATOM   8029  O  O   . LEU D 1 45  ? -50.145 43.466  94.588  1.00 42.71 ? 45   LEU D O   1 
ATOM   8030  C  CB  . LEU D 1 45  ? -50.622 44.441  91.527  1.00 38.48 ? 45   LEU D CB  1 
ATOM   8031  C  CG  . LEU D 1 45  ? -51.923 45.244  91.412  1.00 42.08 ? 45   LEU D CG  1 
ATOM   8032  C  CD1 . LEU D 1 45  ? -51.685 46.722  91.706  1.00 42.90 ? 45   LEU D CD1 1 
ATOM   8033  C  CD2 . LEU D 1 45  ? -52.500 45.074  90.030  1.00 35.68 ? 45   LEU D CD2 1 
ATOM   8034  N  N   . ALA D 1 46  ? -48.429 42.741  93.343  1.00 46.29 ? 46   ALA D N   1 
ATOM   8035  C  CA  . ALA D 1 46  ? -48.216 41.594  94.203  1.00 47.07 ? 46   ALA D CA  1 
ATOM   8036  C  C   . ALA D 1 46  ? -47.136 41.823  95.239  1.00 46.64 ? 46   ALA D C   1 
ATOM   8037  O  O   . ALA D 1 46  ? -47.112 41.144  96.263  1.00 44.70 ? 46   ALA D O   1 
ATOM   8038  C  CB  . ALA D 1 46  ? -47.862 40.397  93.362  1.00 47.57 ? 46   ALA D CB  1 
ATOM   8039  N  N   . GLY D 1 47  ? -46.266 42.793  94.980  1.00 44.82 ? 47   GLY D N   1 
ATOM   8040  C  CA  . GLY D 1 47  ? -45.160 43.048  95.879  1.00 44.39 ? 47   GLY D CA  1 
ATOM   8041  C  C   . GLY D 1 47  ? -44.077 42.228  95.225  1.00 46.01 ? 47   GLY D C   1 
ATOM   8042  O  O   . GLY D 1 47  ? -44.113 40.990  95.271  1.00 46.23 ? 47   GLY D O   1 
ATOM   8043  N  N   . ALA D 1 48  ? -43.128 42.913  94.600  1.00 45.85 ? 48   ALA D N   1 
ATOM   8044  C  CA  . ALA D 1 48  ? -42.058 42.246  93.872  1.00 49.31 ? 48   ALA D CA  1 
ATOM   8045  C  C   . ALA D 1 48  ? -41.009 41.524  94.699  1.00 49.72 ? 48   ALA D C   1 
ATOM   8046  O  O   . ALA D 1 48  ? -40.647 41.969  95.794  1.00 49.22 ? 48   ALA D O   1 
ATOM   8047  C  CB  . ALA D 1 48  ? -41.370 43.262  92.928  1.00 51.24 ? 48   ALA D CB  1 
ATOM   8048  N  N   . TYR D 1 49  ? -40.519 40.412  94.146  1.00 50.38 ? 49   TYR D N   1 
ATOM   8049  C  CA  . TYR D 1 49  ? -39.471 39.610  94.781  1.00 50.95 ? 49   TYR D CA  1 
ATOM   8050  C  C   . TYR D 1 49  ? -38.103 40.083  94.290  1.00 50.70 ? 49   TYR D C   1 
ATOM   8051  O  O   . TYR D 1 49  ? -37.245 40.505  95.060  1.00 54.71 ? 49   TYR D O   1 
ATOM   8052  C  CB  . TYR D 1 49  ? -39.608 38.119  94.435  1.00 47.79 ? 49   TYR D CB  1 
ATOM   8053  C  CG  . TYR D 1 49  ? -40.842 37.418  94.986  1.00 49.56 ? 49   TYR D CG  1 
ATOM   8054  C  CD1 . TYR D 1 49  ? -41.445 37.841  96.171  1.00 47.77 ? 49   TYR D CD1 1 
ATOM   8055  C  CD2 . TYR D 1 49  ? -41.381 36.302  94.333  1.00 46.80 ? 49   TYR D CD2 1 
ATOM   8056  C  CE1 . TYR D 1 49  ? -42.550 37.173  96.688  1.00 50.33 ? 49   TYR D CE1 1 
ATOM   8057  C  CE2 . TYR D 1 49  ? -42.481 35.631  94.839  1.00 45.86 ? 49   TYR D CE2 1 
ATOM   8058  C  CZ  . TYR D 1 49  ? -43.067 36.065  96.014  1.00 50.64 ? 49   TYR D CZ  1 
ATOM   8059  O  OH  . TYR D 1 49  ? -44.170 35.384  96.518  1.00 51.08 ? 49   TYR D OH  1 
ATOM   8060  N  N   . ASN D 1 50  ? -37.908 40.018  92.990  1.00 49.18 ? 50   ASN D N   1 
ATOM   8061  C  CA  . ASN D 1 50  ? -36.642 40.404  92.406  1.00 48.88 ? 50   ASN D CA  1 
ATOM   8062  C  C   . ASN D 1 50  ? -36.613 41.907  92.166  1.00 50.48 ? 50   ASN D C   1 
ATOM   8063  O  O   . ASN D 1 50  ? -37.066 42.396  91.114  1.00 50.25 ? 50   ASN D O   1 
ATOM   8064  C  CB  . ASN D 1 50  ? -36.470 39.634  91.102  1.00 48.18 ? 50   ASN D CB  1 
ATOM   8065  C  CG  . ASN D 1 50  ? -35.142 39.877  90.440  1.00 50.99 ? 50   ASN D CG  1 
ATOM   8066  O  OD1 . ASN D 1 50  ? -34.731 39.083  89.593  1.00 53.45 ? 50   ASN D OD1 1 
ATOM   8067  N  ND2 . ASN D 1 50  ? -34.466 40.974  90.795  1.00 47.14 ? 50   ASN D ND2 1 
ATOM   8068  N  N   . LEU D 1 51  ? -36.067 42.645  93.131  1.00 47.68 ? 51   LEU D N   1 
ATOM   8069  C  CA  . LEU D 1 51  ? -36.004 44.092  93.001  1.00 45.54 ? 51   LEU D CA  1 
ATOM   8070  C  C   . LEU D 1 51  ? -35.193 44.629  91.815  1.00 48.29 ? 51   LEU D C   1 
ATOM   8071  O  O   . LEU D 1 51  ? -35.476 45.725  91.309  1.00 50.60 ? 51   LEU D O   1 
ATOM   8072  C  CB  . LEU D 1 51  ? -35.491 44.695  94.302  1.00 43.99 ? 51   LEU D CB  1 
ATOM   8073  C  CG  . LEU D 1 51  ? -36.394 44.420  95.503  1.00 45.51 ? 51   LEU D CG  1 
ATOM   8074  C  CD1 . LEU D 1 51  ? -36.173 45.463  96.549  1.00 42.65 ? 51   LEU D CD1 1 
ATOM   8075  C  CD2 . LEU D 1 51  ? -37.852 44.469  95.073  1.00 46.14 ? 51   LEU D CD2 1 
ATOM   8076  N  N   . LYS D 1 52  ? -34.295 43.921  91.367  1.00 50.31 ? 52   LYS D N   1 
ATOM   8077  C  CA  . LYS D 1 52  ? -33.404 44.370  90.265  1.00 51.58 ? 52   LYS D CA  1 
ATOM   8078  C  C   . LYS D 1 52  ? -34.232 44.183  88.977  1.00 50.00 ? 52   LYS D C   1 
ATOM   8079  O  O   . LYS D 1 52  ? -33.949 44.955  88.035  1.00 48.00 ? 52   LYS D O   1 
ATOM   8080  C  CB  . LYS D 1 52  ? -32.218 43.415  90.238  1.00 55.19 ? 52   LYS D CB  1 
ATOM   8081  C  CG  . LYS D 1 52  ? -30.989 44.033  89.685  1.00 59.63 ? 52   LYS D CG  1 
ATOM   8082  C  CD  . LYS D 1 52  ? -29.841 43.078  89.300  1.00 64.38 ? 52   LYS D CD  1 
ATOM   8083  C  CE  . LYS D 1 52  ? -28.825 42.859  90.533  1.00 65.94 ? 52   LYS D CE  1 
ATOM   8084  N  NZ  . LYS D 1 52  ? -28.023 41.596  90.681  1.00 67.24 ? 52   LYS D NZ  1 
ATOM   8085  N  N   . ALA D 1 53  ? -35.021 43.192  88.898  1.00 48.06 ? 53   ALA D N   1 
ATOM   8086  C  CA  . ALA D 1 53  ? -35.849 42.977  87.725  1.00 48.33 ? 53   ALA D CA  1 
ATOM   8087  C  C   . ALA D 1 53  ? -36.867 44.118  87.660  1.00 46.35 ? 53   ALA D C   1 
ATOM   8088  O  O   . ALA D 1 53  ? -37.101 44.726  86.593  1.00 44.21 ? 53   ALA D O   1 
ATOM   8089  C  CB  . ALA D 1 53  ? -36.558 41.628  87.830  1.00 50.12 ? 53   ALA D CB  1 
ATOM   8090  N  N   . GLN D 1 54  ? -37.447 44.425  88.817  1.00 43.05 ? 54   GLN D N   1 
ATOM   8091  C  CA  . GLN D 1 54  ? -38.443 45.490  88.909  1.00 42.53 ? 54   GLN D CA  1 
ATOM   8092  C  C   . GLN D 1 54  ? -37.896 46.823  88.429  1.00 41.22 ? 54   GLN D C   1 
ATOM   8093  O  O   . GLN D 1 54  ? -38.556 47.577  87.716  1.00 40.44 ? 54   GLN D O   1 
ATOM   8094  C  CB  . GLN D 1 54  ? -38.923 45.647  90.343  1.00 41.40 ? 54   GLN D CB  1 
ATOM   8095  C  CG  . GLN D 1 54  ? -39.820 46.846  90.533  1.00 44.16 ? 54   GLN D CG  1 
ATOM   8096  C  CD  . GLN D 1 54  ? -40.188 47.067  91.978  1.00 43.37 ? 54   GLN D CD  1 
ATOM   8097  O  OE1 . GLN D 1 54  ? -41.363 47.139  92.323  1.00 47.55 ? 54   GLN D OE1 1 
ATOM   8098  N  NE2 . GLN D 1 54  ? -39.185 47.180  92.831  1.00 44.31 ? 54   GLN D NE2 1 
ATOM   8099  N  N   . LYS D 1 55  ? -36.676 47.111  88.838  1.00 41.19 ? 55   LYS D N   1 
ATOM   8100  C  CA  . LYS D 1 55  ? -36.048 48.350  88.447  1.00 43.64 ? 55   LYS D CA  1 
ATOM   8101  C  C   . LYS D 1 55  ? -35.779 48.376  86.935  1.00 41.14 ? 55   LYS D C   1 
ATOM   8102  O  O   . LYS D 1 55  ? -36.076 49.360  86.227  1.00 38.11 ? 55   LYS D O   1 
ATOM   8103  C  CB  . LYS D 1 55  ? -34.740 48.536  89.238  1.00 46.29 ? 55   LYS D CB  1 
ATOM   8104  C  CG  . LYS D 1 55  ? -33.971 49.788  88.814  1.00 55.53 ? 55   LYS D CG  1 
ATOM   8105  C  CD  . LYS D 1 55  ? -32.908 50.224  89.810  1.00 63.09 ? 55   LYS D CD  1 
ATOM   8106  C  CE  . LYS D 1 55  ? -32.220 51.498  89.312  1.00 65.71 ? 55   LYS D CE  1 
ATOM   8107  N  NZ  . LYS D 1 55  ? -31.286 52.087  90.328  1.00 73.97 ? 55   LYS D NZ  1 
ATOM   8108  N  N   . LEU D 1 56  ? -35.216 47.277  86.456  1.00 39.13 ? 56   LEU D N   1 
ATOM   8109  C  CA  . LEU D 1 56  ? -34.870 47.136  85.064  1.00 38.06 ? 56   LEU D CA  1 
ATOM   8110  C  C   . LEU D 1 56  ? -36.105 47.305  84.193  1.00 36.48 ? 56   LEU D C   1 
ATOM   8111  O  O   . LEU D 1 56  ? -36.095 48.059  83.216  1.00 34.66 ? 56   LEU D O   1 
ATOM   8112  C  CB  . LEU D 1 56  ? -34.208 45.768  84.839  1.00 40.89 ? 56   LEU D CB  1 
ATOM   8113  C  CG  . LEU D 1 56  ? -33.964 45.396  83.373  1.00 44.75 ? 56   LEU D CG  1 
ATOM   8114  C  CD1 . LEU D 1 56  ? -33.209 46.515  82.654  1.00 41.00 ? 56   LEU D CD1 1 
ATOM   8115  C  CD2 . LEU D 1 56  ? -33.230 44.066  83.322  1.00 43.27 ? 56   LEU D CD2 1 
ATOM   8116  N  N   . LEU D 1 57  ? -37.181 46.617  84.551  1.00 35.73 ? 57   LEU D N   1 
ATOM   8117  C  CA  . LEU D 1 57  ? -38.402 46.723  83.762  1.00 37.46 ? 57   LEU D CA  1 
ATOM   8118  C  C   . LEU D 1 57  ? -38.989 48.145  83.811  1.00 39.11 ? 57   LEU D C   1 
ATOM   8119  O  O   . LEU D 1 57  ? -39.450 48.667  82.796  1.00 40.09 ? 57   LEU D O   1 
ATOM   8120  C  CB  . LEU D 1 57  ? -39.415 45.699  84.256  1.00 38.67 ? 57   LEU D CB  1 
ATOM   8121  C  CG  . LEU D 1 57  ? -40.680 45.538  83.425  1.00 37.63 ? 57   LEU D CG  1 
ATOM   8122  C  CD1 . LEU D 1 57  ? -40.350 45.496  81.934  1.00 38.61 ? 57   LEU D CD1 1 
ATOM   8123  C  CD2 . LEU D 1 57  ? -41.361 44.249  83.863  1.00 38.59 ? 57   LEU D CD2 1 
ATOM   8124  N  N   . THR D 1 58  ? -38.965 48.773  84.985  1.00 38.52 ? 58   THR D N   1 
ATOM   8125  C  CA  . THR D 1 58  ? -39.470 50.127  85.118  1.00 38.97 ? 58   THR D CA  1 
ATOM   8126  C  C   . THR D 1 58  ? -38.667 51.007  84.169  1.00 42.46 ? 58   THR D C   1 
ATOM   8127  O  O   . THR D 1 58  ? -39.228 51.779  83.401  1.00 44.17 ? 58   THR D O   1 
ATOM   8128  C  CB  . THR D 1 58  ? -39.307 50.663  86.568  1.00 39.46 ? 58   THR D CB  1 
ATOM   8129  O  OG1 . THR D 1 58  ? -40.094 49.876  87.470  1.00 42.61 ? 58   THR D OG1 1 
ATOM   8130  C  CG2 . THR D 1 58  ? -39.774 52.113  86.666  1.00 40.28 ? 58   THR D CG2 1 
ATOM   8131  N  N   . TYR D 1 59  ? -37.345 50.883  84.213  1.00 45.81 ? 59   TYR D N   1 
ATOM   8132  C  CA  . TYR D 1 59  ? -36.483 51.685  83.347  1.00 49.07 ? 59   TYR D CA  1 
ATOM   8133  C  C   . TYR D 1 59  ? -36.730 51.419  81.853  1.00 49.23 ? 59   TYR D C   1 
ATOM   8134  O  O   . TYR D 1 59  ? -36.834 52.355  81.062  1.00 44.66 ? 59   TYR D O   1 
ATOM   8135  C  CB  . TYR D 1 59  ? -35.008 51.441  83.702  1.00 53.47 ? 59   TYR D CB  1 
ATOM   8136  C  CG  . TYR D 1 59  ? -34.566 52.178  84.948  1.00 62.21 ? 59   TYR D CG  1 
ATOM   8137  C  CD1 . TYR D 1 59  ? -35.425 52.339  86.033  1.00 66.68 ? 59   TYR D CD1 1 
ATOM   8138  C  CD2 . TYR D 1 59  ? -33.296 52.732  85.041  1.00 66.18 ? 59   TYR D CD2 1 
ATOM   8139  C  CE1 . TYR D 1 59  ? -35.028 53.041  87.176  1.00 67.31 ? 59   TYR D CE1 1 
ATOM   8140  C  CE2 . TYR D 1 59  ? -32.893 53.434  86.182  1.00 68.67 ? 59   TYR D CE2 1 
ATOM   8141  C  CZ  . TYR D 1 59  ? -33.766 53.581  87.237  1.00 67.95 ? 59   TYR D CZ  1 
ATOM   8142  O  OH  . TYR D 1 59  ? -33.364 54.273  88.352  1.00 71.80 ? 59   TYR D OH  1 
ATOM   8143  N  N   . GLN D 1 60  ? -36.810 50.152  81.454  1.00 48.31 ? 60   GLN D N   1 
ATOM   8144  C  CA  . GLN D 1 60  ? -37.066 49.877  80.053  1.00 48.31 ? 60   GLN D CA  1 
ATOM   8145  C  C   . GLN D 1 60  ? -38.409 50.501  79.666  1.00 45.36 ? 60   GLN D C   1 
ATOM   8146  O  O   . GLN D 1 60  ? -38.544 51.038  78.572  1.00 41.76 ? 60   GLN D O   1 
ATOM   8147  C  CB  . GLN D 1 60  ? -37.110 48.372  79.778  1.00 49.83 ? 60   GLN D CB  1 
ATOM   8148  C  CG  . GLN D 1 60  ? -35.838 47.637  80.113  1.00 58.73 ? 60   GLN D CG  1 
ATOM   8149  C  CD  . GLN D 1 60  ? -35.980 46.124  79.980  1.00 62.49 ? 60   GLN D CD  1 
ATOM   8150  O  OE1 . GLN D 1 60  ? -36.871 45.507  80.578  1.00 61.18 ? 60   GLN D OE1 1 
ATOM   8151  N  NE2 . GLN D 1 60  ? -35.093 45.518  79.196  1.00 66.17 ? 60   GLN D NE2 1 
ATOM   8152  N  N   . LEU D 1 61  ? -39.399 50.437  80.556  1.00 42.85 ? 61   LEU D N   1 
ATOM   8153  C  CA  . LEU D 1 61  ? -40.703 50.992  80.230  1.00 44.89 ? 61   LEU D CA  1 
ATOM   8154  C  C   . LEU D 1 61  ? -40.656 52.507  80.087  1.00 46.85 ? 61   LEU D C   1 
ATOM   8155  O  O   . LEU D 1 61  ? -41.317 53.070  79.223  1.00 49.07 ? 61   LEU D O   1 
ATOM   8156  C  CB  . LEU D 1 61  ? -41.739 50.552  81.258  1.00 44.43 ? 61   LEU D CB  1 
ATOM   8157  C  CG  . LEU D 1 61  ? -42.685 49.388  80.873  1.00 45.58 ? 61   LEU D CG  1 
ATOM   8158  C  CD1 . LEU D 1 61  ? -42.343 48.767  79.540  1.00 38.65 ? 61   LEU D CD1 1 
ATOM   8159  C  CD2 . LEU D 1 61  ? -42.656 48.362  81.980  1.00 42.69 ? 61   LEU D CD2 1 
ATOM   8160  N  N   . MET D 1 62  ? -39.884 53.176  80.933  1.00 48.58 ? 62   MET D N   1 
ATOM   8161  C  CA  . MET D 1 62  ? -39.723 54.619  80.800  1.00 51.55 ? 62   MET D CA  1 
ATOM   8162  C  C   . MET D 1 62  ? -38.944 54.734  79.493  1.00 56.29 ? 62   MET D C   1 
ATOM   8163  O  O   . MET D 1 62  ? -38.237 53.809  79.122  1.00 60.15 ? 62   MET D O   1 
ATOM   8164  C  CB  . MET D 1 62  ? -38.854 55.169  81.936  1.00 48.38 ? 62   MET D CB  1 
ATOM   8165  C  CG  . MET D 1 62  ? -39.515 55.241  83.293  1.00 47.12 ? 62   MET D CG  1 
ATOM   8166  S  SD  . MET D 1 62  ? -38.276 55.197  84.612  1.00 50.26 ? 62   MET D SD  1 
ATOM   8167  C  CE  . MET D 1 62  ? -37.483 56.784  84.449  1.00 46.21 ? 62   MET D CE  1 
ATOM   8168  N  N   . SER D 1 63  ? -39.063 55.831  78.768  1.00 61.97 ? 63   SER D N   1 
ATOM   8169  C  CA  . SER D 1 63  ? -38.266 55.947  77.535  1.00 69.05 ? 63   SER D CA  1 
ATOM   8170  C  C   . SER D 1 63  ? -38.670 55.113  76.329  1.00 71.60 ? 63   SER D C   1 
ATOM   8171  O  O   . SER D 1 63  ? -38.088 55.290  75.253  1.00 71.72 ? 63   SER D O   1 
ATOM   8172  C  CB  . SER D 1 63  ? -36.807 55.569  77.793  1.00 70.66 ? 63   SER D CB  1 
ATOM   8173  O  OG  . SER D 1 63  ? -36.617 54.194  77.447  1.00 62.28 ? 63   SER D OG  1 
ATOM   8174  N  N   . SER D 1 64  ? -39.602 54.182  76.502  1.00 74.15 ? 64   SER D N   1 
ATOM   8175  C  CA  . SER D 1 64  ? -40.023 53.345  75.385  1.00 76.28 ? 64   SER D CA  1 
ATOM   8176  C  C   . SER D 1 64  ? -40.765 54.136  74.292  1.00 80.09 ? 64   SER D C   1 
ATOM   8177  O  O   . SER D 1 64  ? -41.997 54.193  74.302  1.00 82.80 ? 64   SER D O   1 
ATOM   8178  C  CB  . SER D 1 64  ? -40.908 52.204  75.897  1.00 73.27 ? 64   SER D CB  1 
ATOM   8179  O  OG  . SER D 1 64  ? -42.084 52.698  76.507  1.00 67.13 ? 64   SER D OG  1 
ATOM   8180  N  N   . ASP D 1 65  ? -40.008 54.734  73.366  1.00 82.13 ? 65   ASP D N   1 
ATOM   8181  C  CA  . ASP D 1 65  ? -40.541 55.521  72.239  1.00 84.90 ? 65   ASP D CA  1 
ATOM   8182  C  C   . ASP D 1 65  ? -42.063 55.492  72.211  1.00 83.52 ? 65   ASP D C   1 
ATOM   8183  O  O   . ASP D 1 65  ? -42.654 54.520  71.747  1.00 84.95 ? 65   ASP D O   1 
ATOM   8184  C  CB  . ASP D 1 65  ? -40.005 54.955  70.912  1.00 90.23 ? 65   ASP D CB  1 
ATOM   8185  C  CG  . ASP D 1 65  ? -40.127 55.941  69.748  1.00 92.93 ? 65   ASP D CG  1 
ATOM   8186  O  OD1 . ASP D 1 65  ? -41.048 56.785  69.776  1.00 94.65 ? 65   ASP D OD1 1 
ATOM   8187  O  OD2 . ASP D 1 65  ? -39.307 55.861  68.800  1.00 95.37 ? 65   ASP D OD2 1 
ATOM   8188  N  N   . ASN D 1 66  ? -42.692 56.562  72.682  1.00 81.76 ? 66   ASN D N   1 
ATOM   8189  C  CA  . ASN D 1 66  ? -44.151 56.632  72.751  1.00 80.82 ? 66   ASN D CA  1 
ATOM   8190  C  C   . ASN D 1 66  ? -44.893 56.530  71.428  1.00 79.79 ? 66   ASN D C   1 
ATOM   8191  O  O   . ASN D 1 66  ? -46.115 56.507  71.413  1.00 78.04 ? 66   ASN D O   1 
ATOM   8192  C  CB  . ASN D 1 66  ? -44.578 57.921  73.440  1.00 81.45 ? 66   ASN D CB  1 
ATOM   8193  C  CG  . ASN D 1 66  ? -43.745 58.236  74.672  1.00 81.13 ? 66   ASN D CG  1 
ATOM   8194  O  OD1 . ASN D 1 66  ? -43.472 57.368  75.506  1.00 79.29 ? 66   ASN D OD1 1 
ATOM   8195  N  ND2 . ASN D 1 66  ? -43.351 59.494  74.796  1.00 82.91 ? 66   ASN D ND2 1 
ATOM   8196  N  N   . ASN D 1 67  ? -44.162 56.469  70.322  1.00 80.98 ? 67   ASN D N   1 
ATOM   8197  C  CA  . ASN D 1 67  ? -44.791 56.380  69.008  1.00 81.05 ? 67   ASN D CA  1 
ATOM   8198  C  C   . ASN D 1 67  ? -44.917 54.961  68.485  1.00 79.36 ? 67   ASN D C   1 
ATOM   8199  O  O   . ASN D 1 67  ? -45.728 54.691  67.603  1.00 80.63 ? 67   ASN D O   1 
ATOM   8200  C  CB  . ASN D 1 67  ? -44.015 57.215  67.986  1.00 84.11 ? 67   ASN D CB  1 
ATOM   8201  C  CG  . ASN D 1 67  ? -44.021 58.692  68.319  1.00 87.40 ? 67   ASN D CG  1 
ATOM   8202  O  OD1 . ASN D 1 67  ? -43.426 59.495  67.604  1.00 89.79 ? 67   ASN D OD1 1 
ATOM   8203  N  ND2 . ASN D 1 67  ? -44.694 59.059  69.410  1.00 89.40 ? 67   ASN D ND2 1 
ATOM   8204  N  N   . ASP D 1 68  ? -44.120 54.050  69.019  1.00 76.20 ? 68   ASP D N   1 
ATOM   8205  C  CA  . ASP D 1 68  ? -44.176 52.674  68.549  1.00 74.70 ? 68   ASP D CA  1 
ATOM   8206  C  C   . ASP D 1 68  ? -45.256 51.891  69.286  1.00 70.80 ? 68   ASP D C   1 
ATOM   8207  O  O   . ASP D 1 68  ? -45.497 50.708  68.991  1.00 69.95 ? 68   ASP D O   1 
ATOM   8208  C  CB  . ASP D 1 68  ? -42.827 51.983  68.770  1.00 78.47 ? 68   ASP D CB  1 
ATOM   8209  C  CG  . ASP D 1 68  ? -41.647 52.860  68.383  1.00 84.44 ? 68   ASP D CG  1 
ATOM   8210  O  OD1 . ASP D 1 68  ? -41.869 53.924  67.756  1.00 88.36 ? 68   ASP D OD1 1 
ATOM   8211  O  OD2 . ASP D 1 68  ? -40.492 52.481  68.701  1.00 86.46 ? 68   ASP D OD2 1 
ATOM   8212  N  N   . LEU D 1 69  ? -45.912 52.550  70.236  1.00 62.52 ? 69   LEU D N   1 
ATOM   8213  C  CA  . LEU D 1 69  ? -46.913 51.870  71.038  1.00 53.72 ? 69   LEU D CA  1 
ATOM   8214  C  C   . LEU D 1 69  ? -48.328 52.030  70.557  1.00 48.17 ? 69   LEU D C   1 
ATOM   8215  O  O   . LEU D 1 69  ? -48.729 53.094  70.120  1.00 47.06 ? 69   LEU D O   1 
ATOM   8216  C  CB  . LEU D 1 69  ? -46.815 52.347  72.479  1.00 53.30 ? 69   LEU D CB  1 
ATOM   8217  C  CG  . LEU D 1 69  ? -45.454 52.175  73.141  1.00 53.53 ? 69   LEU D CG  1 
ATOM   8218  C  CD1 . LEU D 1 69  ? -45.509 52.779  74.546  1.00 52.13 ? 69   LEU D CD1 1 
ATOM   8219  C  CD2 . LEU D 1 69  ? -45.079 50.686  73.159  1.00 47.41 ? 69   LEU D CD2 1 
ATOM   8220  N  N   . THR D 1 70  ? -49.088 50.953  70.654  1.00 46.07 ? 70   THR D N   1 
ATOM   8221  C  CA  . THR D 1 70  ? -50.486 50.982  70.257  1.00 45.02 ? 70   THR D CA  1 
ATOM   8222  C  C   . THR D 1 70  ? -51.279 51.513  71.423  1.00 45.17 ? 70   THR D C   1 
ATOM   8223  O  O   . THR D 1 70  ? -50.822 51.491  72.580  1.00 44.01 ? 70   THR D O   1 
ATOM   8224  C  CB  . THR D 1 70  ? -51.065 49.595  69.989  1.00 45.00 ? 70   THR D CB  1 
ATOM   8225  O  OG1 . THR D 1 70  ? -50.962 48.813  71.189  1.00 44.88 ? 70   THR D OG1 1 
ATOM   8226  C  CG2 . THR D 1 70  ? -50.336 48.903  68.846  1.00 41.50 ? 70   THR D CG2 1 
ATOM   8227  N  N   . ILE D 1 71  ? -52.482 51.961  71.096  1.00 43.15 ? 71   ILE D N   1 
ATOM   8228  C  CA  . ILE D 1 71  ? -53.427 52.491  72.046  1.00 41.79 ? 71   ILE D CA  1 
ATOM   8229  C  C   . ILE D 1 71  ? -53.387 51.635  73.351  1.00 42.15 ? 71   ILE D C   1 
ATOM   8230  O  O   . ILE D 1 71  ? -53.298 52.176  74.466  1.00 40.17 ? 71   ILE D O   1 
ATOM   8231  C  CB  . ILE D 1 71  ? -54.808 52.500  71.340  1.00 44.09 ? 71   ILE D CB  1 
ATOM   8232  C  CG1 . ILE D 1 71  ? -55.301 53.919  71.194  1.00 48.10 ? 71   ILE D CG1 1 
ATOM   8233  C  CG2 . ILE D 1 71  ? -55.833 51.660  72.063  1.00 43.42 ? 71   ILE D CG2 1 
ATOM   8234  C  CD1 . ILE D 1 71  ? -56.700 53.934  70.563  1.00 53.89 ? 71   ILE D CD1 1 
ATOM   8235  N  N   . GLY D 1 72  ? -53.409 50.312  73.192  1.00 40.12 ? 72   GLY D N   1 
ATOM   8236  C  CA  . GLY D 1 72  ? -53.368 49.389  74.317  1.00 40.99 ? 72   GLY D CA  1 
ATOM   8237  C  C   . GLY D 1 72  ? -52.010 49.262  74.996  1.00 44.88 ? 72   GLY D C   1 
ATOM   8238  O  O   . GLY D 1 72  ? -51.953 49.145  76.231  1.00 45.44 ? 72   GLY D O   1 
ATOM   8239  N  N   . HIS D 1 73  ? -50.923 49.264  74.214  1.00 49.63 ? 73   HIS D N   1 
ATOM   8240  C  CA  . HIS D 1 73  ? -49.563 49.186  74.782  1.00 51.88 ? 73   HIS D CA  1 
ATOM   8241  C  C   . HIS D 1 73  ? -49.457 50.381  75.722  1.00 49.45 ? 73   HIS D C   1 
ATOM   8242  O  O   . HIS D 1 73  ? -49.077 50.257  76.892  1.00 48.30 ? 73   HIS D O   1 
ATOM   8243  C  CB  . HIS D 1 73  ? -48.461 49.433  73.749  1.00 61.35 ? 73   HIS D CB  1 
ATOM   8244  C  CG  . HIS D 1 73  ? -48.203 48.311  72.792  1.00 70.79 ? 73   HIS D CG  1 
ATOM   8245  N  ND1 . HIS D 1 73  ? -47.338 48.448  71.720  1.00 72.65 ? 73   HIS D ND1 1 
ATOM   8246  C  CD2 . HIS D 1 73  ? -48.634 47.029  72.766  1.00 74.03 ? 73   HIS D CD2 1 
ATOM   8247  C  CE1 . HIS D 1 73  ? -47.245 47.297  71.080  1.00 73.78 ? 73   HIS D CE1 1 
ATOM   8248  N  NE2 . HIS D 1 73  ? -48.021 46.419  71.692  1.00 77.20 ? 73   HIS D NE2 1 
ATOM   8249  N  N   . LEU D 1 74  ? -49.775 51.547  75.163  1.00 43.71 ? 74   LEU D N   1 
ATOM   8250  C  CA  . LEU D 1 74  ? -49.693 52.791  75.895  1.00 43.38 ? 74   LEU D CA  1 
ATOM   8251  C  C   . LEU D 1 74  ? -50.417 52.739  77.230  1.00 42.82 ? 74   LEU D C   1 
ATOM   8252  O  O   . LEU D 1 74  ? -49.810 52.969  78.276  1.00 42.83 ? 74   LEU D O   1 
ATOM   8253  C  CB  . LEU D 1 74  ? -50.235 53.930  75.037  1.00 42.94 ? 74   LEU D CB  1 
ATOM   8254  C  CG  . LEU D 1 74  ? -49.461 55.252  74.989  1.00 42.99 ? 74   LEU D CG  1 
ATOM   8255  C  CD1 . LEU D 1 74  ? -47.993 55.112  75.380  1.00 43.60 ? 74   LEU D CD1 1 
ATOM   8256  C  CD2 . LEU D 1 74  ? -49.564 55.760  73.584  1.00 43.30 ? 74   LEU D CD2 1 
ATOM   8257  N  N   . GLY D 1 75  ? -51.703 52.421  77.194  1.00 39.11 ? 75   GLY D N   1 
ATOM   8258  C  CA  . GLY D 1 75  ? -52.461 52.366  78.422  1.00 38.81 ? 75   GLY D CA  1 
ATOM   8259  C  C   . GLY D 1 75  ? -51.837 51.481  79.476  1.00 38.29 ? 75   GLY D C   1 
ATOM   8260  O  O   . GLY D 1 75  ? -51.849 51.814  80.649  1.00 38.83 ? 75   GLY D O   1 
ATOM   8261  N  N   . LEU D 1 76  ? -51.301 50.343  79.047  1.00 40.28 ? 76   LEU D N   1 
ATOM   8262  C  CA  . LEU D 1 76  ? -50.687 49.372  79.936  1.00 38.61 ? 76   LEU D CA  1 
ATOM   8263  C  C   . LEU D 1 76  ? -49.365 49.919  80.466  1.00 39.70 ? 76   LEU D C   1 
ATOM   8264  O  O   . LEU D 1 76  ? -48.993 49.699  81.627  1.00 42.36 ? 76   LEU D O   1 
ATOM   8265  C  CB  . LEU D 1 76  ? -50.476 48.059  79.165  1.00 39.98 ? 76   LEU D CB  1 
ATOM   8266  C  CG  . LEU D 1 76  ? -51.213 46.788  79.617  1.00 38.87 ? 76   LEU D CG  1 
ATOM   8267  C  CD1 . LEU D 1 76  ? -52.521 47.105  80.254  1.00 37.38 ? 76   LEU D CD1 1 
ATOM   8268  C  CD2 . LEU D 1 76  ? -51.428 45.898  78.421  1.00 34.49 ? 76   LEU D CD2 1 
ATOM   8269  N  N   . THR D 1 77  ? -48.660 50.652  79.623  1.00 37.42 ? 77   THR D N   1 
ATOM   8270  C  CA  . THR D 1 77  ? -47.395 51.213  80.043  1.00 40.15 ? 77   THR D CA  1 
ATOM   8271  C  C   . THR D 1 77  ? -47.622 52.324  81.071  1.00 40.80 ? 77   THR D C   1 
ATOM   8272  O  O   . THR D 1 77  ? -46.885 52.450  82.053  1.00 41.45 ? 77   THR D O   1 
ATOM   8273  C  CB  . THR D 1 77  ? -46.629 51.752  78.838  1.00 40.86 ? 77   THR D CB  1 
ATOM   8274  O  OG1 . THR D 1 77  ? -46.261 50.656  77.991  1.00 48.67 ? 77   THR D OG1 1 
ATOM   8275  C  CG2 . THR D 1 77  ? -45.378 52.465  79.272  1.00 45.21 ? 77   THR D CG2 1 
ATOM   8276  N  N   . ILE D 1 78  ? -48.653 53.126  80.853  1.00 40.28 ? 78   ILE D N   1 
ATOM   8277  C  CA  . ILE D 1 78  ? -48.954 54.203  81.773  1.00 39.39 ? 78   ILE D CA  1 
ATOM   8278  C  C   . ILE D 1 78  ? -49.289 53.620  83.139  1.00 41.31 ? 78   ILE D C   1 
ATOM   8279  O  O   . ILE D 1 78  ? -48.848 54.149  84.163  1.00 43.03 ? 78   ILE D O   1 
ATOM   8280  C  CB  . ILE D 1 78  ? -50.112 55.065  81.233  1.00 40.07 ? 78   ILE D CB  1 
ATOM   8281  C  CG1 . ILE D 1 78  ? -49.616 55.848  80.001  1.00 42.76 ? 78   ILE D CG1 1 
ATOM   8282  C  CG2 . ILE D 1 78  ? -50.619 55.999  82.311  1.00 33.11 ? 78   ILE D CG2 1 
ATOM   8283  C  CD1 . ILE D 1 78  ? -50.670 56.594  79.251  1.00 42.29 ? 78   ILE D CD1 1 
ATOM   8284  N  N   . MET D 1 79  ? -50.041 52.520  83.162  1.00 38.20 ? 79   MET D N   1 
ATOM   8285  C  CA  . MET D 1 79  ? -50.394 51.913  84.433  1.00 39.02 ? 79   MET D CA  1 
ATOM   8286  C  C   . MET D 1 79  ? -49.183 51.270  85.099  1.00 38.19 ? 79   MET D C   1 
ATOM   8287  O  O   . MET D 1 79  ? -49.018 51.371  86.320  1.00 35.46 ? 79   MET D O   1 
ATOM   8288  C  CB  . MET D 1 79  ? -51.511 50.898  84.248  1.00 36.25 ? 79   MET D CB  1 
ATOM   8289  C  CG  . MET D 1 79  ? -52.750 51.545  83.721  1.00 38.90 ? 79   MET D CG  1 
ATOM   8290  S  SD  . MET D 1 79  ? -54.207 50.529  83.896  1.00 44.18 ? 79   MET D SD  1 
ATOM   8291  C  CE  . MET D 1 79  ? -54.149 49.541  82.436  1.00 39.91 ? 79   MET D CE  1 
ATOM   8292  N  N   . ALA D 1 80  ? -48.334 50.629  84.299  1.00 36.39 ? 80   ALA D N   1 
ATOM   8293  C  CA  . ALA D 1 80  ? -47.124 50.004  84.834  1.00 38.15 ? 80   ALA D CA  1 
ATOM   8294  C  C   . ALA D 1 80  ? -46.238 51.046  85.553  1.00 36.69 ? 80   ALA D C   1 
ATOM   8295  O  O   . ALA D 1 80  ? -45.854 50.845  86.716  1.00 32.83 ? 80   ALA D O   1 
ATOM   8296  C  CB  . ALA D 1 80  ? -46.342 49.316  83.709  1.00 35.34 ? 80   ALA D CB  1 
ATOM   8297  N  N   . LEU D 1 81  ? -45.944 52.155  84.865  1.00 37.30 ? 81   LEU D N   1 
ATOM   8298  C  CA  . LEU D 1 81  ? -45.121 53.235  85.422  1.00 37.96 ? 81   LEU D CA  1 
ATOM   8299  C  C   . LEU D 1 81  ? -45.748 53.794  86.706  1.00 38.26 ? 81   LEU D C   1 
ATOM   8300  O  O   . LEU D 1 81  ? -45.049 54.021  87.703  1.00 38.87 ? 81   LEU D O   1 
ATOM   8301  C  CB  . LEU D 1 81  ? -44.910 54.357  84.381  1.00 35.93 ? 81   LEU D CB  1 
ATOM   8302  C  CG  . LEU D 1 81  ? -44.039 53.870  83.199  1.00 36.71 ? 81   LEU D CG  1 
ATOM   8303  C  CD1 . LEU D 1 81  ? -43.873 54.952  82.139  1.00 38.60 ? 81   LEU D CD1 1 
ATOM   8304  C  CD2 . LEU D 1 81  ? -42.682 53.425  83.713  1.00 37.39 ? 81   LEU D CD2 1 
ATOM   8305  N  N   . THR D 1 82  ? -47.061 53.993  86.679  1.00 35.89 ? 82   THR D N   1 
ATOM   8306  C  CA  . THR D 1 82  ? -47.784 54.490  87.834  1.00 33.12 ? 82   THR D CA  1 
ATOM   8307  C  C   . THR D 1 82  ? -47.624 53.513  89.006  1.00 37.52 ? 82   THR D C   1 
ATOM   8308  O  O   . THR D 1 82  ? -47.407 53.939  90.161  1.00 38.49 ? 82   THR D O   1 
ATOM   8309  C  CB  . THR D 1 82  ? -49.284 54.656  87.500  1.00 30.68 ? 82   THR D CB  1 
ATOM   8310  O  OG1 . THR D 1 82  ? -49.422 55.611  86.448  1.00 33.12 ? 82   THR D OG1 1 
ATOM   8311  C  CG2 . THR D 1 82  ? -50.065 55.158  88.692  1.00 25.98 ? 82   THR D CG2 1 
ATOM   8312  N  N   . SER D 1 83  ? -47.718 52.211  88.733  1.00 35.79 ? 83   SER D N   1 
ATOM   8313  C  CA  . SER D 1 83  ? -47.581 51.232  89.815  1.00 38.07 ? 83   SER D CA  1 
ATOM   8314  C  C   . SER D 1 83  ? -46.134 51.210  90.336  1.00 37.68 ? 83   SER D C   1 
ATOM   8315  O  O   . SER D 1 83  ? -45.830 50.561  91.325  1.00 37.18 ? 83   SER D O   1 
ATOM   8316  C  CB  . SER D 1 83  ? -48.002 49.823  89.346  1.00 37.07 ? 83   SER D CB  1 
ATOM   8317  O  OG  . SER D 1 83  ? -47.105 49.308  88.375  1.00 34.74 ? 83   SER D OG  1 
ATOM   8318  N  N   . SER D 1 84  ? -45.236 51.901  89.649  1.00 38.95 ? 84   SER D N   1 
ATOM   8319  C  CA  . SER D 1 84  ? -43.848 51.963  90.090  1.00 43.85 ? 84   SER D CA  1 
ATOM   8320  C  C   . SER D 1 84  ? -43.606 53.372  90.629  1.00 43.87 ? 84   SER D C   1 
ATOM   8321  O  O   . SER D 1 84  ? -42.462 53.779  90.847  1.00 42.92 ? 84   SER D O   1 
ATOM   8322  C  CB  . SER D 1 84  ? -42.889 51.689  88.915  1.00 46.59 ? 84   SER D CB  1 
ATOM   8323  O  OG  . SER D 1 84  ? -42.611 50.304  88.744  1.00 49.63 ? 84   SER D OG  1 
ATOM   8324  N  N   . CYS D 1 85  ? -44.699 54.099  90.844  1.00 42.90 ? 85   CYS D N   1 
ATOM   8325  C  CA  . CYS D 1 85  ? -44.657 55.481  91.307  1.00 44.65 ? 85   CYS D CA  1 
ATOM   8326  C  C   . CYS D 1 85  ? -43.819 56.351  90.385  1.00 43.46 ? 85   CYS D C   1 
ATOM   8327  O  O   . CYS D 1 85  ? -43.124 57.260  90.834  1.00 43.59 ? 85   CYS D O   1 
ATOM   8328  C  CB  . CYS D 1 85  ? -44.132 55.578  92.735  1.00 45.86 ? 85   CYS D CB  1 
ATOM   8329  S  SG  . CYS D 1 85  ? -45.191 54.652  93.867  1.00 51.35 ? 85   CYS D SG  1 
ATOM   8330  N  N   . ARG D 1 86  ? -43.909 56.074  89.089  1.00 40.85 ? 86   ARG D N   1 
ATOM   8331  C  CA  . ARG D 1 86  ? -43.179 56.836  88.093  1.00 43.10 ? 86   ARG D CA  1 
ATOM   8332  C  C   . ARG D 1 86  ? -44.088 57.716  87.236  1.00 44.53 ? 86   ARG D C   1 
ATOM   8333  O  O   . ARG D 1 86  ? -45.169 57.307  86.815  1.00 45.65 ? 86   ARG D O   1 
ATOM   8334  C  CB  . ARG D 1 86  ? -42.396 55.891  87.203  1.00 40.10 ? 86   ARG D CB  1 
ATOM   8335  C  CG  . ARG D 1 86  ? -41.165 55.377  87.874  1.00 39.61 ? 86   ARG D CG  1 
ATOM   8336  C  CD  . ARG D 1 86  ? -40.126 56.457  87.968  1.00 35.81 ? 86   ARG D CD  1 
ATOM   8337  N  NE  . ARG D 1 86  ? -38.874 55.878  88.430  1.00 44.90 ? 86   ARG D NE  1 
ATOM   8338  C  CZ  . ARG D 1 86  ? -37.712 56.518  88.436  1.00 43.11 ? 86   ARG D CZ  1 
ATOM   8339  N  NH1 . ARG D 1 86  ? -37.646 57.766  88.007  1.00 41.23 ? 86   ARG D NH1 1 
ATOM   8340  N  NH2 . ARG D 1 86  ? -36.620 55.902  88.852  1.00 38.05 ? 86   ARG D NH2 1 
ATOM   8341  N  N   . ASP D 1 87  ? -43.642 58.933  86.968  1.00 44.52 ? 87   ASP D N   1 
ATOM   8342  C  CA  . ASP D 1 87  ? -44.454 59.839  86.167  1.00 44.68 ? 87   ASP D CA  1 
ATOM   8343  C  C   . ASP D 1 87  ? -44.470 59.348  84.725  1.00 41.42 ? 87   ASP D C   1 
ATOM   8344  O  O   . ASP D 1 87  ? -43.484 59.467  84.033  1.00 42.03 ? 87   ASP D O   1 
ATOM   8345  C  CB  . ASP D 1 87  ? -43.894 61.265  86.267  1.00 42.32 ? 87   ASP D CB  1 
ATOM   8346  C  CG  . ASP D 1 87  ? -44.750 62.279  85.536  1.00 48.55 ? 87   ASP D CG  1 
ATOM   8347  O  OD1 . ASP D 1 87  ? -45.803 61.886  84.978  1.00 51.88 ? 87   ASP D OD1 1 
ATOM   8348  O  OD2 . ASP D 1 87  ? -44.369 63.470  85.517  1.00 46.05 ? 87   ASP D OD2 1 
ATOM   8349  N  N   . PRO D 1 88  ? -45.596 58.796  84.260  1.00 43.19 ? 88   PRO D N   1 
ATOM   8350  C  CA  . PRO D 1 88  ? -45.651 58.306  82.877  1.00 47.71 ? 88   PRO D CA  1 
ATOM   8351  C  C   . PRO D 1 88  ? -45.389 59.513  81.993  1.00 52.98 ? 88   PRO D C   1 
ATOM   8352  O  O   . PRO D 1 88  ? -44.907 59.407  80.842  1.00 53.03 ? 88   PRO D O   1 
ATOM   8353  C  CB  . PRO D 1 88  ? -47.093 57.804  82.731  1.00 44.75 ? 88   PRO D CB  1 
ATOM   8354  C  CG  . PRO D 1 88  ? -47.599 57.695  84.164  1.00 46.85 ? 88   PRO D CG  1 
ATOM   8355  C  CD  . PRO D 1 88  ? -46.946 58.854  84.835  1.00 44.57 ? 88   PRO D CD  1 
ATOM   8356  N  N   . GLY D 1 89  ? -45.717 60.668  82.570  1.00 54.69 ? 89   GLY D N   1 
ATOM   8357  C  CA  . GLY D 1 89  ? -45.546 61.931  81.891  1.00 55.51 ? 89   GLY D CA  1 
ATOM   8358  C  C   . GLY D 1 89  ? -46.125 61.967  80.487  1.00 57.81 ? 89   GLY D C   1 
ATOM   8359  O  O   . GLY D 1 89  ? -47.298 61.666  80.252  1.00 61.58 ? 89   GLY D O   1 
ATOM   8360  N  N   . ASP D 1 90  ? -45.270 62.345  79.554  1.00 54.34 ? 90   ASP D N   1 
ATOM   8361  C  CA  . ASP D 1 90  ? -45.592 62.474  78.153  1.00 52.97 ? 90   ASP D CA  1 
ATOM   8362  C  C   . ASP D 1 90  ? -46.516 61.399  77.542  1.00 49.93 ? 90   ASP D C   1 
ATOM   8363  O  O   . ASP D 1 90  ? -47.311 61.683  76.626  1.00 42.79 ? 90   ASP D O   1 
ATOM   8364  C  CB  . ASP D 1 90  ? -44.271 62.508  77.398  1.00 62.12 ? 90   ASP D CB  1 
ATOM   8365  C  CG  . ASP D 1 90  ? -44.357 63.291  76.121  1.00 71.18 ? 90   ASP D CG  1 
ATOM   8366  O  OD1 . ASP D 1 90  ? -45.452 63.839  75.840  1.00 72.39 ? 90   ASP D OD1 1 
ATOM   8367  O  OD2 . ASP D 1 90  ? -43.327 63.359  75.405  1.00 77.81 ? 90   ASP D OD2 1 
ATOM   8368  N  N   . LYS D 1 91  ? -46.412 60.166  78.032  1.00 46.38 ? 91   LYS D N   1 
ATOM   8369  C  CA  . LYS D 1 91  ? -47.228 59.085  77.490  1.00 44.24 ? 91   LYS D CA  1 
ATOM   8370  C  C   . LYS D 1 91  ? -48.733 59.305  77.667  1.00 43.77 ? 91   LYS D C   1 
ATOM   8371  O  O   . LYS D 1 91  ? -49.544 58.811  76.870  1.00 44.87 ? 91   LYS D O   1 
ATOM   8372  C  CB  . LYS D 1 91  ? -46.827 57.748  78.117  1.00 43.96 ? 91   LYS D CB  1 
ATOM   8373  C  CG  . LYS D 1 91  ? -45.449 57.253  77.705  1.00 44.01 ? 91   LYS D CG  1 
ATOM   8374  C  CD  . LYS D 1 91  ? -45.044 56.071  78.529  1.00 44.49 ? 91   LYS D CD  1 
ATOM   8375  C  CE  . LYS D 1 91  ? -43.562 55.827  78.421  1.00 49.51 ? 91   LYS D CE  1 
ATOM   8376  N  NZ  . LYS D 1 91  ? -43.164 55.485  77.051  1.00 51.38 ? 91   LYS D NZ  1 
ATOM   8377  N  N   . VAL D 1 92  ? -49.106 60.069  78.688  1.00 39.93 ? 92   VAL D N   1 
ATOM   8378  C  CA  . VAL D 1 92  ? -50.502 60.308  78.964  1.00 38.14 ? 92   VAL D CA  1 
ATOM   8379  C  C   . VAL D 1 92  ? -51.148 61.245  77.971  1.00 41.36 ? 92   VAL D C   1 
ATOM   8380  O  O   . VAL D 1 92  ? -52.266 60.989  77.513  1.00 45.08 ? 92   VAL D O   1 
ATOM   8381  C  CB  . VAL D 1 92  ? -50.678 60.818  80.401  1.00 41.86 ? 92   VAL D CB  1 
ATOM   8382  C  CG1 . VAL D 1 92  ? -52.141 61.147  80.685  1.00 40.66 ? 92   VAL D CG1 1 
ATOM   8383  C  CG2 . VAL D 1 92  ? -50.191 59.738  81.381  1.00 42.32 ? 92   VAL D CG2 1 
ATOM   8384  N  N   . SER D 1 93  ? -50.466 62.325  77.601  1.00 41.88 ? 93   SER D N   1 
ATOM   8385  C  CA  . SER D 1 93  ? -51.066 63.238  76.633  1.00 42.25 ? 93   SER D CA  1 
ATOM   8386  C  C   . SER D 1 93  ? -51.120 62.583  75.252  1.00 41.61 ? 93   SER D C   1 
ATOM   8387  O  O   . SER D 1 93  ? -52.108 62.703  74.546  1.00 42.15 ? 93   SER D O   1 
ATOM   8388  C  CB  . SER D 1 93  ? -50.302 64.556  76.585  1.00 40.14 ? 93   SER D CB  1 
ATOM   8389  O  OG  . SER D 1 93  ? -48.926 64.312  76.745  1.00 47.28 ? 93   SER D OG  1 
ATOM   8390  N  N   . ILE D 1 94  ? -50.066 61.872  74.879  1.00 42.13 ? 94   ILE D N   1 
ATOM   8391  C  CA  . ILE D 1 94  ? -50.041 61.181  73.604  1.00 43.17 ? 94   ILE D CA  1 
ATOM   8392  C  C   . ILE D 1 94  ? -51.262 60.265  73.501  1.00 43.92 ? 94   ILE D C   1 
ATOM   8393  O  O   . ILE D 1 94  ? -51.953 60.252  72.477  1.00 42.82 ? 94   ILE D O   1 
ATOM   8394  C  CB  . ILE D 1 94  ? -48.760 60.349  73.480  1.00 45.33 ? 94   ILE D CB  1 
ATOM   8395  C  CG1 . ILE D 1 94  ? -47.561 61.293  73.376  1.00 47.02 ? 94   ILE D CG1 1 
ATOM   8396  C  CG2 . ILE D 1 94  ? -48.836 59.439  72.277  1.00 47.11 ? 94   ILE D CG2 1 
ATOM   8397  C  CD1 . ILE D 1 94  ? -46.198 60.619  73.461  1.00 46.96 ? 94   ILE D CD1 1 
ATOM   8398  N  N   . LEU D 1 95  ? -51.538 59.511  74.569  1.00 42.42 ? 95   LEU D N   1 
ATOM   8399  C  CA  . LEU D 1 95  ? -52.693 58.613  74.565  1.00 41.00 ? 95   LEU D CA  1 
ATOM   8400  C  C   . LEU D 1 95  ? -54.008 59.400  74.568  1.00 43.13 ? 95   LEU D C   1 
ATOM   8401  O  O   . LEU D 1 95  ? -54.953 59.073  73.837  1.00 42.59 ? 95   LEU D O   1 
ATOM   8402  C  CB  . LEU D 1 95  ? -52.659 57.679  75.773  1.00 37.25 ? 95   LEU D CB  1 
ATOM   8403  C  CG  . LEU D 1 95  ? -53.814 56.681  75.833  1.00 35.78 ? 95   LEU D CG  1 
ATOM   8404  C  CD1 . LEU D 1 95  ? -53.702 55.719  74.658  1.00 37.66 ? 95   LEU D CD1 1 
ATOM   8405  C  CD2 . LEU D 1 95  ? -53.768 55.908  77.144  1.00 39.38 ? 95   LEU D CD2 1 
ATOM   8406  N  N   . GLN D 1 96  ? -54.063 60.437  75.395  1.00 41.04 ? 96   GLN D N   1 
ATOM   8407  C  CA  . GLN D 1 96  ? -55.251 61.268  75.498  1.00 45.05 ? 96   GLN D CA  1 
ATOM   8408  C  C   . GLN D 1 96  ? -55.646 61.844  74.129  1.00 46.59 ? 96   GLN D C   1 
ATOM   8409  O  O   . GLN D 1 96  ? -56.822 61.791  73.744  1.00 45.07 ? 96   GLN D O   1 
ATOM   8410  C  CB  . GLN D 1 96  ? -54.976 62.382  76.523  1.00 49.97 ? 96   GLN D CB  1 
ATOM   8411  C  CG  . GLN D 1 96  ? -56.075 63.397  76.754  1.00 53.09 ? 96   GLN D CG  1 
ATOM   8412  C  CD  . GLN D 1 96  ? -57.388 62.788  77.206  1.00 60.45 ? 96   GLN D CD  1 
ATOM   8413  O  OE1 . GLN D 1 96  ? -57.413 61.881  78.053  1.00 61.37 ? 96   GLN D OE1 1 
ATOM   8414  N  NE2 . GLN D 1 96  ? -58.501 63.300  76.660  1.00 59.95 ? 96   GLN D NE2 1 
ATOM   8415  N  N   . ARG D 1 97  ? -54.665 62.363  73.377  1.00 46.97 ? 97   ARG D N   1 
ATOM   8416  C  CA  . ARG D 1 97  ? -54.948 62.940  72.060  1.00 46.60 ? 97   ARG D CA  1 
ATOM   8417  C  C   . ARG D 1 97  ? -55.374 61.861  71.064  1.00 45.38 ? 97   ARG D C   1 
ATOM   8418  O  O   . ARG D 1 97  ? -56.227 62.096  70.216  1.00 45.08 ? 97   ARG D O   1 
ATOM   8419  C  CB  . ARG D 1 97  ? -53.736 63.730  71.537  1.00 45.47 ? 97   ARG D CB  1 
ATOM   8420  C  CG  . ARG D 1 97  ? -53.027 64.476  72.656  1.00 49.43 ? 97   ARG D CG  1 
ATOM   8421  C  CD  . ARG D 1 97  ? -52.542 65.862  72.312  1.00 48.28 ? 97   ARG D CD  1 
ATOM   8422  N  NE  . ARG D 1 97  ? -51.421 65.870  71.384  1.00 48.62 ? 97   ARG D NE  1 
ATOM   8423  C  CZ  . ARG D 1 97  ? -50.996 66.976  70.778  1.00 47.64 ? 97   ARG D CZ  1 
ATOM   8424  N  NH1 . ARG D 1 97  ? -51.601 68.120  71.033  1.00 50.35 ? 97   ARG D NH1 1 
ATOM   8425  N  NH2 . ARG D 1 97  ? -50.020 66.947  69.886  1.00 45.63 ? 97   ARG D NH2 1 
ATOM   8426  N  N   . GLN D 1 98  ? -54.787 60.676  71.150  1.00 41.99 ? 98   GLN D N   1 
ATOM   8427  C  CA  . GLN D 1 98  ? -55.212 59.626  70.253  1.00 38.62 ? 98   GLN D CA  1 
ATOM   8428  C  C   . GLN D 1 98  ? -56.669 59.260  70.592  1.00 39.30 ? 98   GLN D C   1 
ATOM   8429  O  O   . GLN D 1 98  ? -57.527 59.217  69.713  1.00 39.33 ? 98   GLN D O   1 
ATOM   8430  C  CB  . GLN D 1 98  ? -54.303 58.409  70.392  1.00 39.00 ? 98   GLN D CB  1 
ATOM   8431  C  CG  . GLN D 1 98  ? -53.192 58.328  69.376  1.00 42.00 ? 98   GLN D CG  1 
ATOM   8432  C  CD  . GLN D 1 98  ? -52.119 57.291  69.745  1.00 45.42 ? 98   GLN D CD  1 
ATOM   8433  O  OE1 . GLN D 1 98  ? -51.169 57.590  70.482  1.00 46.80 ? 98   GLN D OE1 1 
ATOM   8434  N  NE2 . GLN D 1 98  ? -52.276 56.067  69.243  1.00 44.53 ? 98   GLN D NE2 1 
ATOM   8435  N  N   . MET D 1 99  ? -56.980 59.030  71.862  1.00 38.92 ? 99   MET D N   1 
ATOM   8436  C  CA  . MET D 1 99  ? -58.350 58.652  72.185  1.00 39.96 ? 99   MET D CA  1 
ATOM   8437  C  C   . MET D 1 99  ? -59.391 59.720  71.892  1.00 40.73 ? 99   MET D C   1 
ATOM   8438  O  O   . MET D 1 99  ? -60.551 59.407  71.635  1.00 42.31 ? 99   MET D O   1 
ATOM   8439  C  CB  . MET D 1 99  ? -58.462 58.202  73.637  1.00 40.93 ? 99   MET D CB  1 
ATOM   8440  C  CG  . MET D 1 99  ? -57.692 56.935  73.925  1.00 43.24 ? 99   MET D CG  1 
ATOM   8441  S  SD  . MET D 1 99  ? -58.025 55.667  72.684  1.00 41.54 ? 99   MET D SD  1 
ATOM   8442  C  CE  . MET D 1 99  ? -59.706 55.138  73.070  1.00 39.90 ? 99   MET D CE  1 
ATOM   8443  N  N   . GLU D 1 100 ? -59.011 60.988  71.942  1.00 40.76 ? 100  GLU D N   1 
ATOM   8444  C  CA  . GLU D 1 100 ? -59.989 62.014  71.625  1.00 41.98 ? 100  GLU D CA  1 
ATOM   8445  C  C   . GLU D 1 100 ? -60.374 61.847  70.159  1.00 42.03 ? 100  GLU D C   1 
ATOM   8446  O  O   . GLU D 1 100 ? -61.403 62.344  69.707  1.00 44.21 ? 100  GLU D O   1 
ATOM   8447  C  CB  . GLU D 1 100 ? -59.402 63.405  71.851  1.00 46.51 ? 100  GLU D CB  1 
ATOM   8448  C  CG  . GLU D 1 100 ? -59.129 63.708  73.305  1.00 57.65 ? 100  GLU D CG  1 
ATOM   8449  C  CD  . GLU D 1 100 ? -58.460 65.058  73.509  1.00 64.90 ? 100  GLU D CD  1 
ATOM   8450  O  OE1 . GLU D 1 100 ? -57.637 65.458  72.642  1.00 67.11 ? 100  GLU D OE1 1 
ATOM   8451  O  OE2 . GLU D 1 100 ? -58.740 65.705  74.550  1.00 69.07 ? 100  GLU D OE2 1 
ATOM   8452  N  N   . ASN D 1 101 ? -59.545 61.119  69.421  1.00 42.34 ? 101  ASN D N   1 
ATOM   8453  C  CA  . ASN D 1 101 ? -59.761 60.899  68.005  1.00 41.06 ? 101  ASN D CA  1 
ATOM   8454  C  C   . ASN D 1 101 ? -60.233 59.499  67.680  1.00 44.70 ? 101  ASN D C   1 
ATOM   8455  O  O   . ASN D 1 101 ? -60.450 59.158  66.518  1.00 45.30 ? 101  ASN D O   1 
ATOM   8456  C  CB  . ASN D 1 101 ? -58.458 61.186  67.264  1.00 39.47 ? 101  ASN D CB  1 
ATOM   8457  C  CG  . ASN D 1 101 ? -58.316 62.640  66.909  1.00 40.16 ? 101  ASN D CG  1 
ATOM   8458  O  OD1 . ASN D 1 101 ? -58.944 63.107  65.963  1.00 42.68 ? 101  ASN D OD1 1 
ATOM   8459  N  ND2 . ASN D 1 101 ? -57.511 63.378  67.677  1.00 37.56 ? 101  ASN D ND2 1 
ATOM   8460  N  N   . TRP D 1 102 ? -60.383 58.673  68.704  1.00 48.77 ? 102  TRP D N   1 
ATOM   8461  C  CA  . TRP D 1 102 ? -60.790 57.308  68.470  1.00 49.68 ? 102  TRP D CA  1 
ATOM   8462  C  C   . TRP D 1 102 ? -62.276 57.098  68.203  1.00 53.20 ? 102  TRP D C   1 
ATOM   8463  O  O   . TRP D 1 102 ? -63.157 57.666  68.881  1.00 53.75 ? 102  TRP D O   1 
ATOM   8464  C  CB  . TRP D 1 102 ? -60.365 56.427  69.639  1.00 49.80 ? 102  TRP D CB  1 
ATOM   8465  C  CG  . TRP D 1 102 ? -60.631 54.973  69.388  1.00 48.34 ? 102  TRP D CG  1 
ATOM   8466  C  CD1 . TRP D 1 102 ? -59.796 54.080  68.781  1.00 47.96 ? 102  TRP D CD1 1 
ATOM   8467  C  CD2 . TRP D 1 102 ? -61.850 54.267  69.655  1.00 44.58 ? 102  TRP D CD2 1 
ATOM   8468  N  NE1 . TRP D 1 102 ? -60.425 52.860  68.650  1.00 49.15 ? 102  TRP D NE1 1 
ATOM   8469  C  CE2 . TRP D 1 102 ? -61.685 52.953  69.174  1.00 45.56 ? 102  TRP D CE2 1 
ATOM   8470  C  CE3 . TRP D 1 102 ? -63.062 54.622  70.254  1.00 42.42 ? 102  TRP D CE3 1 
ATOM   8471  C  CZ2 . TRP D 1 102 ? -62.683 52.001  69.262  1.00 47.30 ? 102  TRP D CZ2 1 
ATOM   8472  C  CZ3 . TRP D 1 102 ? -64.047 53.685  70.345  1.00 45.95 ? 102  TRP D CZ3 1 
ATOM   8473  C  CH2 . TRP D 1 102 ? -63.860 52.384  69.852  1.00 48.97 ? 102  TRP D CH2 1 
ATOM   8474  N  N   . ALA D 1 103 ? -62.521 56.250  67.203  1.00 56.08 ? 103  ALA D N   1 
ATOM   8475  C  CA  . ALA D 1 103 ? -63.855 55.845  66.773  1.00 57.12 ? 103  ALA D CA  1 
ATOM   8476  C  C   . ALA D 1 103 ? -63.703 54.415  66.290  1.00 59.03 ? 103  ALA D C   1 
ATOM   8477  O  O   . ALA D 1 103 ? -62.603 53.989  65.933  1.00 58.37 ? 103  ALA D O   1 
ATOM   8478  C  CB  . ALA D 1 103 ? -64.345 56.711  65.637  1.00 54.32 ? 103  ALA D CB  1 
ATOM   8479  N  N   . PRO D 1 104 ? -64.801 53.645  66.298  1.00 61.89 ? 104  PRO D N   1 
ATOM   8480  C  CA  . PRO D 1 104 ? -64.789 52.249  65.847  1.00 62.70 ? 104  PRO D CA  1 
ATOM   8481  C  C   . PRO D 1 104 ? -64.824 52.222  64.313  1.00 62.64 ? 104  PRO D C   1 
ATOM   8482  O  O   . PRO D 1 104 ? -65.595 52.957  63.702  1.00 62.60 ? 104  PRO D O   1 
ATOM   8483  C  CB  . PRO D 1 104 ? -66.069 51.694  66.456  1.00 63.88 ? 104  PRO D CB  1 
ATOM   8484  C  CG  . PRO D 1 104 ? -67.011 52.885  66.348  1.00 63.71 ? 104  PRO D CG  1 
ATOM   8485  C  CD  . PRO D 1 104 ? -66.124 54.008  66.849  1.00 64.05 ? 104  PRO D CD  1 
ATOM   8486  N  N   . SER D 1 105 ? -64.011 51.377  63.692  1.00 63.09 ? 105  SER D N   1 
ATOM   8487  C  CA  . SER D 1 105 ? -63.994 51.311  62.234  1.00 65.86 ? 105  SER D CA  1 
ATOM   8488  C  C   . SER D 1 105 ? -65.390 51.218  61.581  1.00 67.99 ? 105  SER D C   1 
ATOM   8489  O  O   . SER D 1 105 ? -65.607 51.778  60.509  1.00 67.36 ? 105  SER D O   1 
ATOM   8490  C  CB  . SER D 1 105 ? -63.119 50.133  61.754  1.00 64.88 ? 105  SER D CB  1 
ATOM   8491  O  OG  . SER D 1 105 ? -63.614 48.868  62.176  1.00 65.63 ? 105  SER D OG  1 
ATOM   8492  N  N   . SER D 1 106 ? -66.330 50.526  62.230  1.00 72.45 ? 106  SER D N   1 
ATOM   8493  C  CA  . SER D 1 106 ? -67.686 50.353  61.706  1.00 74.39 ? 106  SER D CA  1 
ATOM   8494  C  C   . SER D 1 106 ? -68.659 49.905  62.784  1.00 76.64 ? 106  SER D C   1 
ATOM   8495  O  O   . SER D 1 106 ? -68.237 49.347  63.808  1.00 76.97 ? 106  SER D O   1 
ATOM   8496  C  CB  . SER D 1 106 ? -67.686 49.292  60.601  1.00 74.34 ? 106  SER D CB  1 
ATOM   8497  O  OG  . SER D 1 106 ? -69.010 48.880  60.311  1.00 73.56 ? 106  SER D OG  1 
ATOM   8498  N  N   . PRO D 1 107 ? -69.972 50.153  62.566  1.00 74.78 ? 107  PRO D N   1 
ATOM   8499  C  CA  . PRO D 1 107 ? -71.055 49.790  63.492  1.00 75.20 ? 107  PRO D CA  1 
ATOM   8500  C  C   . PRO D 1 107 ? -71.194 48.290  63.508  1.00 75.48 ? 107  PRO D C   1 
ATOM   8501  O  O   . PRO D 1 107 ? -72.285 47.761  63.564  1.00 77.33 ? 107  PRO D O   1 
ATOM   8502  C  CB  . PRO D 1 107 ? -72.311 50.426  62.875  1.00 74.47 ? 107  PRO D CB  1 
ATOM   8503  C  CG  . PRO D 1 107 ? -71.814 51.299  61.749  1.00 74.23 ? 107  PRO D CG  1 
ATOM   8504  C  CD  . PRO D 1 107 ? -70.531 50.652  61.304  1.00 74.32 ? 107  PRO D CD  1 
ATOM   8505  N  N   . ASN D 1 108 ? -70.090 47.578  63.454  1.00 75.44 ? 108  ASN D N   1 
ATOM   8506  C  CA  . ASN D 1 108 ? -70.184 46.115  63.394  1.00 75.54 ? 108  ASN D CA  1 
ATOM   8507  C  C   . ASN D 1 108 ? -68.768 45.589  63.327  1.00 74.02 ? 108  ASN D C   1 
ATOM   8508  O  O   . ASN D 1 108 ? -68.463 44.683  62.561  1.00 73.60 ? 108  ASN D O   1 
ATOM   8509  C  CB  . ASN D 1 108 ? -70.943 45.693  62.113  1.00 78.52 ? 108  ASN D CB  1 
ATOM   8510  C  CG  . ASN D 1 108 ? -72.399 45.302  62.379  1.00 80.62 ? 108  ASN D CG  1 
ATOM   8511  O  OD1 . ASN D 1 108 ? -73.178 45.140  61.409  1.00 81.32 ? 108  ASN D OD1 1 
ATOM   8512  N  ND2 . ASN D 1 108 ? -72.788 45.149  63.700  1.00 80.43 ? 108  ASN D ND2 1 
ATOM   8513  N  N   . ALA D 1 109 ? -67.889 46.168  64.122  1.00 72.17 ? 109  ALA D N   1 
ATOM   8514  C  CA  . ALA D 1 109 ? -66.525 45.703  64.124  1.00 69.43 ? 109  ALA D CA  1 
ATOM   8515  C  C   . ALA D 1 109 ? -66.366 44.561  65.088  1.00 67.75 ? 109  ALA D C   1 
ATOM   8516  O  O   . ALA D 1 109 ? -67.217 44.344  65.955  1.00 67.22 ? 109  ALA D O   1 
ATOM   8517  C  CB  . ALA D 1 109 ? -65.611 46.830  64.494  1.00 69.66 ? 109  ALA D CB  1 
ATOM   8518  N  N   . GLU D 1 110 ? -65.312 43.786  64.886  1.00 62.92 ? 110  GLU D N   1 
ATOM   8519  C  CA  . GLU D 1 110 ? -65.011 42.647  65.735  1.00 63.26 ? 110  GLU D CA  1 
ATOM   8520  C  C   . GLU D 1 110 ? -64.874 43.154  67.190  1.00 61.46 ? 110  GLU D C   1 
ATOM   8521  O  O   . GLU D 1 110 ? -64.155 44.126  67.454  1.00 58.98 ? 110  GLU D O   1 
ATOM   8522  C  CB  . GLU D 1 110 ? -63.696 42.013  65.258  1.00 66.31 ? 110  GLU D CB  1 
ATOM   8523  C  CG  . GLU D 1 110 ? -62.466 42.965  65.349  1.00 73.70 ? 110  GLU D CG  1 
ATOM   8524  C  CD  . GLU D 1 110 ? -62.370 44.069  64.255  1.00 77.09 ? 110  GLU D CD  1 
ATOM   8525  O  OE1 . GLU D 1 110 ? -63.396 44.706  63.905  1.00 78.19 ? 110  GLU D OE1 1 
ATOM   8526  O  OE2 . GLU D 1 110 ? -61.239 44.319  63.764  1.00 80.25 ? 110  GLU D OE2 1 
ATOM   8527  N  N   . ALA D 1 111 ? -65.569 42.520  68.130  1.00 57.32 ? 111  ALA D N   1 
ATOM   8528  C  CA  . ALA D 1 111 ? -65.505 42.948  69.525  1.00 55.73 ? 111  ALA D CA  1 
ATOM   8529  C  C   . ALA D 1 111 ? -64.064 43.132  70.059  1.00 54.57 ? 111  ALA D C   1 
ATOM   8530  O  O   . ALA D 1 111 ? -63.820 43.956  70.926  1.00 54.20 ? 111  ALA D O   1 
ATOM   8531  C  CB  . ALA D 1 111 ? -66.273 41.959  70.400  1.00 55.26 ? 111  ALA D CB  1 
ATOM   8532  N  N   . SER D 1 112 ? -63.113 42.372  69.545  1.00 52.91 ? 112  SER D N   1 
ATOM   8533  C  CA  . SER D 1 112 ? -61.740 42.475  70.010  1.00 52.52 ? 112  SER D CA  1 
ATOM   8534  C  C   . SER D 1 112 ? -61.150 43.847  69.711  1.00 52.20 ? 112  SER D C   1 
ATOM   8535  O  O   . SER D 1 112 ? -60.141 44.247  70.296  1.00 52.23 ? 112  SER D O   1 
ATOM   8536  C  CB  . SER D 1 112 ? -60.889 41.429  69.313  1.00 56.04 ? 112  SER D CB  1 
ATOM   8537  O  OG  . SER D 1 112 ? -60.780 41.755  67.926  1.00 53.99 ? 112  SER D OG  1 
ATOM   8538  N  N   . ALA D 1 113 ? -61.752 44.562  68.775  1.00 49.66 ? 113  ALA D N   1 
ATOM   8539  C  CA  . ALA D 1 113 ? -61.245 45.878  68.433  1.00 48.39 ? 113  ALA D CA  1 
ATOM   8540  C  C   . ALA D 1 113 ? -61.494 46.903  69.529  1.00 47.25 ? 113  ALA D C   1 
ATOM   8541  O  O   . ALA D 1 113 ? -60.994 48.019  69.447  1.00 44.77 ? 113  ALA D O   1 
ATOM   8542  C  CB  . ALA D 1 113 ? -61.874 46.353  67.166  1.00 52.76 ? 113  ALA D CB  1 
ATOM   8543  N  N   . PHE D 1 114 ? -62.289 46.543  70.530  1.00 44.11 ? 114  PHE D N   1 
ATOM   8544  C  CA  . PHE D 1 114 ? -62.561 47.452  71.633  1.00 45.77 ? 114  PHE D CA  1 
ATOM   8545  C  C   . PHE D 1 114 ? -61.675 47.167  72.836  1.00 43.96 ? 114  PHE D C   1 
ATOM   8546  O  O   . PHE D 1 114 ? -61.815 47.815  73.868  1.00 44.49 ? 114  PHE D O   1 
ATOM   8547  C  CB  . PHE D 1 114 ? -64.025 47.379  72.048  1.00 45.82 ? 114  PHE D CB  1 
ATOM   8548  C  CG  . PHE D 1 114 ? -64.971 47.732  70.949  1.00 54.25 ? 114  PHE D CG  1 
ATOM   8549  C  CD1 . PHE D 1 114 ? -64.937 48.991  70.365  1.00 57.10 ? 114  PHE D CD1 1 
ATOM   8550  C  CD2 . PHE D 1 114 ? -65.901 46.803  70.480  1.00 57.42 ? 114  PHE D CD2 1 
ATOM   8551  C  CE1 . PHE D 1 114 ? -65.822 49.326  69.323  1.00 59.31 ? 114  PHE D CE1 1 
ATOM   8552  C  CE2 . PHE D 1 114 ? -66.785 47.130  69.445  1.00 56.19 ? 114  PHE D CE2 1 
ATOM   8553  C  CZ  . PHE D 1 114 ? -66.742 48.391  68.867  1.00 56.89 ? 114  PHE D CZ  1 
ATOM   8554  N  N   . TYR D 1 115 ? -60.752 46.218  72.695  1.00 42.34 ? 115  TYR D N   1 
ATOM   8555  C  CA  . TYR D 1 115 ? -59.850 45.868  73.787  1.00 40.83 ? 115  TYR D CA  1 
ATOM   8556  C  C   . TYR D 1 115 ? -58.837 46.991  74.057  1.00 40.18 ? 115  TYR D C   1 
ATOM   8557  O  O   . TYR D 1 115 ? -58.675 47.453  75.208  1.00 39.57 ? 115  TYR D O   1 
ATOM   8558  C  CB  . TYR D 1 115 ? -59.084 44.589  73.467  1.00 35.69 ? 115  TYR D CB  1 
ATOM   8559  C  CG  . TYR D 1 115 ? -58.341 44.025  74.659  1.00 37.28 ? 115  TYR D CG  1 
ATOM   8560  C  CD1 . TYR D 1 115 ? -59.021 43.346  75.685  1.00 35.28 ? 115  TYR D CD1 1 
ATOM   8561  C  CD2 . TYR D 1 115 ? -56.962 44.167  74.768  1.00 33.59 ? 115  TYR D CD2 1 
ATOM   8562  C  CE1 . TYR D 1 115 ? -58.330 42.831  76.792  1.00 34.77 ? 115  TYR D CE1 1 
ATOM   8563  C  CE2 . TYR D 1 115 ? -56.262 43.650  75.850  1.00 33.94 ? 115  TYR D CE2 1 
ATOM   8564  C  CZ  . TYR D 1 115 ? -56.939 42.990  76.865  1.00 37.09 ? 115  TYR D CZ  1 
ATOM   8565  O  OH  . TYR D 1 115 ? -56.206 42.534  77.954  1.00 35.94 ? 115  TYR D OH  1 
ATOM   8566  N  N   . GLY D 1 116 ? -58.153 47.414  72.997  1.00 36.66 ? 116  GLY D N   1 
ATOM   8567  C  CA  . GLY D 1 116 ? -57.168 48.470  73.135  1.00 38.42 ? 116  GLY D CA  1 
ATOM   8568  C  C   . GLY D 1 116 ? -57.810 49.693  73.766  1.00 37.90 ? 116  GLY D C   1 
ATOM   8569  O  O   . GLY D 1 116 ? -57.295 50.271  74.731  1.00 36.52 ? 116  GLY D O   1 
ATOM   8570  N  N   . PRO D 1 117 ? -58.952 50.114  73.217  1.00 36.33 ? 117  PRO D N   1 
ATOM   8571  C  CA  . PRO D 1 117 ? -59.685 51.273  73.714  1.00 38.17 ? 117  PRO D CA  1 
ATOM   8572  C  C   . PRO D 1 117 ? -60.056 51.146  75.198  1.00 38.99 ? 117  PRO D C   1 
ATOM   8573  O  O   . PRO D 1 117 ? -60.034 52.133  75.943  1.00 37.90 ? 117  PRO D O   1 
ATOM   8574  C  CB  . PRO D 1 117 ? -60.908 51.320  72.779  1.00 40.29 ? 117  PRO D CB  1 
ATOM   8575  C  CG  . PRO D 1 117 ? -60.350 50.828  71.497  1.00 34.42 ? 117  PRO D CG  1 
ATOM   8576  C  CD  . PRO D 1 117 ? -59.514 49.647  71.935  1.00 36.18 ? 117  PRO D CD  1 
ATOM   8577  N  N   . SER D 1 118 ? -60.409 49.937  75.627  1.00 39.00 ? 118  SER D N   1 
ATOM   8578  C  CA  . SER D 1 118 ? -60.763 49.738  77.022  1.00 39.01 ? 118  SER D CA  1 
ATOM   8579  C  C   . SER D 1 118 ? -59.544 49.999  77.894  1.00 39.49 ? 118  SER D C   1 
ATOM   8580  O  O   . SER D 1 118 ? -59.601 50.727  78.863  1.00 40.36 ? 118  SER D O   1 
ATOM   8581  C  CB  . SER D 1 118 ? -61.262 48.321  77.232  1.00 38.92 ? 118  SER D CB  1 
ATOM   8582  O  OG  . SER D 1 118 ? -62.544 48.198  76.676  1.00 39.68 ? 118  SER D OG  1 
ATOM   8583  N  N   . LEU D 1 119 ? -58.435 49.382  77.537  1.00 41.11 ? 119  LEU D N   1 
ATOM   8584  C  CA  . LEU D 1 119 ? -57.192 49.560  78.261  1.00 42.30 ? 119  LEU D CA  1 
ATOM   8585  C  C   . LEU D 1 119 ? -56.836 51.050  78.345  1.00 44.28 ? 119  LEU D C   1 
ATOM   8586  O  O   . LEU D 1 119 ? -56.476 51.564  79.414  1.00 41.88 ? 119  LEU D O   1 
ATOM   8587  C  CB  . LEU D 1 119 ? -56.088 48.812  77.519  1.00 43.05 ? 119  LEU D CB  1 
ATOM   8588  C  CG  . LEU D 1 119 ? -55.239 47.746  78.220  1.00 44.80 ? 119  LEU D CG  1 
ATOM   8589  C  CD1 . LEU D 1 119 ? -55.912 47.234  79.483  1.00 36.28 ? 119  LEU D CD1 1 
ATOM   8590  C  CD2 . LEU D 1 119 ? -54.959 46.631  77.190  1.00 37.99 ? 119  LEU D CD2 1 
ATOM   8591  N  N   . ALA D 1 120 ? -56.930 51.739  77.207  1.00 43.21 ? 120  ALA D N   1 
ATOM   8592  C  CA  . ALA D 1 120 ? -56.612 53.166  77.144  1.00 42.06 ? 120  ALA D CA  1 
ATOM   8593  C  C   . ALA D 1 120 ? -57.536 53.998  78.033  1.00 41.83 ? 120  ALA D C   1 
ATOM   8594  O  O   . ALA D 1 120 ? -57.099 54.862  78.801  1.00 39.76 ? 120  ALA D O   1 
ATOM   8595  C  CB  . ALA D 1 120 ? -56.717 53.652  75.719  1.00 42.51 ? 120  ALA D CB  1 
ATOM   8596  N  N   . ILE D 1 121 ? -58.830 53.747  77.927  1.00 40.86 ? 121  ILE D N   1 
ATOM   8597  C  CA  . ILE D 1 121 ? -59.755 54.508  78.730  1.00 39.03 ? 121  ILE D CA  1 
ATOM   8598  C  C   . ILE D 1 121 ? -59.501 54.239  80.212  1.00 39.15 ? 121  ILE D C   1 
ATOM   8599  O  O   . ILE D 1 121 ? -59.604 55.155  81.015  1.00 42.45 ? 121  ILE D O   1 
ATOM   8600  C  CB  . ILE D 1 121 ? -61.203 54.209  78.303  1.00 37.72 ? 121  ILE D CB  1 
ATOM   8601  C  CG1 . ILE D 1 121 ? -61.419 54.751  76.882  1.00 37.15 ? 121  ILE D CG1 1 
ATOM   8602  C  CG2 . ILE D 1 121 ? -62.191 54.856  79.257  1.00 37.60 ? 121  ILE D CG2 1 
ATOM   8603  C  CD1 . ILE D 1 121 ? -62.753 54.378  76.263  1.00 39.93 ? 121  ILE D CD1 1 
ATOM   8604  N  N   . LEU D 1 122 ? -59.149 53.010  80.581  1.00 36.12 ? 122  LEU D N   1 
ATOM   8605  C  CA  . LEU D 1 122 ? -58.863 52.731  81.982  1.00 37.09 ? 122  LEU D CA  1 
ATOM   8606  C  C   . LEU D 1 122 ? -57.685 53.606  82.449  1.00 36.87 ? 122  LEU D C   1 
ATOM   8607  O  O   . LEU D 1 122 ? -57.764 54.263  83.480  1.00 37.55 ? 122  LEU D O   1 
ATOM   8608  C  CB  . LEU D 1 122 ? -58.528 51.246  82.217  1.00 36.15 ? 122  LEU D CB  1 
ATOM   8609  C  CG  . LEU D 1 122 ? -58.126 50.877  83.662  1.00 37.10 ? 122  LEU D CG  1 
ATOM   8610  C  CD1 . LEU D 1 122 ? -59.159 51.356  84.653  1.00 29.08 ? 122  LEU D CD1 1 
ATOM   8611  C  CD2 . LEU D 1 122 ? -57.974 49.370  83.785  1.00 35.51 ? 122  LEU D CD2 1 
ATOM   8612  N  N   . ALA D 1 123 ? -56.608 53.643  81.680  1.00 35.93 ? 123  ALA D N   1 
ATOM   8613  C  CA  . ALA D 1 123 ? -55.466 54.440  82.080  1.00 36.31 ? 123  ALA D CA  1 
ATOM   8614  C  C   . ALA D 1 123 ? -55.836 55.917  82.177  1.00 37.91 ? 123  ALA D C   1 
ATOM   8615  O  O   . ALA D 1 123 ? -55.581 56.567  83.199  1.00 37.96 ? 123  ALA D O   1 
ATOM   8616  C  CB  . ALA D 1 123 ? -54.301 54.235  81.117  1.00 36.37 ? 123  ALA D CB  1 
ATOM   8617  N  N   . LEU D 1 124 ? -56.446 56.444  81.124  1.00 37.65 ? 124  LEU D N   1 
ATOM   8618  C  CA  . LEU D 1 124 ? -56.859 57.838  81.113  1.00 35.09 ? 124  LEU D CA  1 
ATOM   8619  C  C   . LEU D 1 124 ? -57.802 58.137  82.275  1.00 38.17 ? 124  LEU D C   1 
ATOM   8620  O  O   . LEU D 1 124 ? -57.681 59.163  82.955  1.00 40.59 ? 124  LEU D O   1 
ATOM   8621  C  CB  . LEU D 1 124 ? -57.549 58.154  79.798  1.00 34.54 ? 124  LEU D CB  1 
ATOM   8622  C  CG  . LEU D 1 124 ? -56.784 58.790  78.631  1.00 36.33 ? 124  LEU D CG  1 
ATOM   8623  C  CD1 . LEU D 1 124 ? -55.302 58.618  78.727  1.00 31.02 ? 124  LEU D CD1 1 
ATOM   8624  C  CD2 . LEU D 1 124 ? -57.327 58.192  77.357  1.00 36.53 ? 124  LEU D CD2 1 
ATOM   8625  N  N   . CYS D 1 125 ? -58.750 57.248  82.524  1.00 37.02 ? 125  CYS D N   1 
ATOM   8626  C  CA  . CYS D 1 125 ? -59.677 57.497  83.609  1.00 37.71 ? 125  CYS D CA  1 
ATOM   8627  C  C   . CYS D 1 125 ? -58.931 57.633  84.936  1.00 39.16 ? 125  CYS D C   1 
ATOM   8628  O  O   . CYS D 1 125 ? -59.318 58.386  85.811  1.00 41.25 ? 125  CYS D O   1 
ATOM   8629  C  CB  . CYS D 1 125 ? -60.685 56.372  83.679  1.00 38.89 ? 125  CYS D CB  1 
ATOM   8630  S  SG  . CYS D 1 125 ? -61.744 56.442  85.150  1.00 46.18 ? 125  CYS D SG  1 
ATOM   8631  N  N   . GLN D 1 126 ? -57.838 56.910  85.083  1.00 39.53 ? 126  GLN D N   1 
ATOM   8632  C  CA  . GLN D 1 126 ? -57.072 56.973  86.311  1.00 34.77 ? 126  GLN D CA  1 
ATOM   8633  C  C   . GLN D 1 126 ? -56.320 58.266  86.504  1.00 37.32 ? 126  GLN D C   1 
ATOM   8634  O  O   . GLN D 1 126 ? -56.139 58.704  87.638  1.00 39.78 ? 126  GLN D O   1 
ATOM   8635  C  CB  . GLN D 1 126 ? -56.097 55.815  86.369  1.00 27.57 ? 126  GLN D CB  1 
ATOM   8636  C  CG  . GLN D 1 126 ? -56.768 54.508  86.700  1.00 28.77 ? 126  GLN D CG  1 
ATOM   8637  C  CD  . GLN D 1 126 ? -55.804 53.326  86.653  1.00 32.70 ? 126  GLN D CD  1 
ATOM   8638  O  OE1 . GLN D 1 126 ? -56.147 52.224  87.075  1.00 40.76 ? 126  GLN D OE1 1 
ATOM   8639  N  NE2 . GLN D 1 126 ? -54.598 53.550  86.147  1.00 32.82 ? 126  GLN D NE2 1 
ATOM   8640  N  N   . LYS D 1 127 ? -55.889 58.873  85.401  1.00 37.89 ? 127  LYS D N   1 
ATOM   8641  C  CA  . LYS D 1 127 ? -55.130 60.118  85.434  1.00 36.56 ? 127  LYS D CA  1 
ATOM   8642  C  C   . LYS D 1 127 ? -55.997 61.385  85.462  1.00 36.27 ? 127  LYS D C   1 
ATOM   8643  O  O   . LYS D 1 127 ? -55.613 62.378  86.067  1.00 42.07 ? 127  LYS D O   1 
ATOM   8644  C  CB  . LYS D 1 127 ? -54.175 60.175  84.225  1.00 36.27 ? 127  LYS D CB  1 
ATOM   8645  C  CG  . LYS D 1 127 ? -53.025 59.175  84.261  1.00 39.56 ? 127  LYS D CG  1 
ATOM   8646  C  CD  . LYS D 1 127 ? -51.956 59.568  85.288  1.00 47.83 ? 127  LYS D CD  1 
ATOM   8647  C  CE  . LYS D 1 127 ? -51.047 58.405  85.674  1.00 49.28 ? 127  LYS D CE  1 
ATOM   8648  N  NZ  . LYS D 1 127 ? -51.803 57.324  86.428  1.00 55.93 ? 127  LYS D NZ  1 
ATOM   8649  N  N   . ASN D 1 128 ? -57.156 61.359  84.811  1.00 34.69 ? 128  ASN D N   1 
ATOM   8650  C  CA  . ASN D 1 128 ? -58.037 62.520  84.760  1.00 32.54 ? 128  ASN D CA  1 
ATOM   8651  C  C   . ASN D 1 128 ? -59.394 62.044  84.272  1.00 32.77 ? 128  ASN D C   1 
ATOM   8652  O  O   . ASN D 1 128 ? -59.697 62.073  83.082  1.00 37.04 ? 128  ASN D O   1 
ATOM   8653  C  CB  . ASN D 1 128 ? -57.446 63.574  83.820  1.00 27.09 ? 128  ASN D CB  1 
ATOM   8654  C  CG  . ASN D 1 128 ? -58.301 64.855  83.739  1.00 37.93 ? 128  ASN D CG  1 
ATOM   8655  O  OD1 . ASN D 1 128 ? -57.834 65.882  83.239  1.00 40.39 ? 128  ASN D OD1 1 
ATOM   8656  N  ND2 . ASN D 1 128 ? -59.561 64.789  84.208  1.00 34.02 ? 128  ASN D ND2 1 
ATOM   8657  N  N   . SER D 1 129 ? -60.216 61.599  85.208  1.00 33.32 ? 129  SER D N   1 
ATOM   8658  C  CA  . SER D 1 129 ? -61.527 61.063  84.878  1.00 33.98 ? 129  SER D CA  1 
ATOM   8659  C  C   . SER D 1 129 ? -62.418 62.047  84.128  1.00 35.72 ? 129  SER D C   1 
ATOM   8660  O  O   . SER D 1 129 ? -63.114 61.660  83.199  1.00 35.62 ? 129  SER D O   1 
ATOM   8661  C  CB  . SER D 1 129 ? -62.220 60.540  86.152  1.00 34.85 ? 129  SER D CB  1 
ATOM   8662  O  OG  . SER D 1 129 ? -62.355 61.547  87.156  1.00 42.94 ? 129  SER D OG  1 
ATOM   8663  N  N   . GLU D 1 130 ? -62.401 63.321  84.507  1.00 39.75 ? 130  GLU D N   1 
ATOM   8664  C  CA  . GLU D 1 130 ? -63.250 64.290  83.815  1.00 40.92 ? 130  GLU D CA  1 
ATOM   8665  C  C   . GLU D 1 130 ? -62.826 64.492  82.365  1.00 38.59 ? 130  GLU D C   1 
ATOM   8666  O  O   . GLU D 1 130 ? -63.674 64.573  81.481  1.00 41.56 ? 130  GLU D O   1 
ATOM   8667  C  CB  . GLU D 1 130 ? -63.265 65.637  84.547  1.00 40.92 ? 130  GLU D CB  1 
ATOM   8668  C  CG  . GLU D 1 130 ? -64.298 66.589  84.009  1.00 43.74 ? 130  GLU D CG  1 
ATOM   8669  C  CD  . GLU D 1 130 ? -64.514 67.820  84.880  1.00 49.33 ? 130  GLU D CD  1 
ATOM   8670  O  OE1 . GLU D 1 130 ? -63.786 67.996  85.874  1.00 51.51 ? 130  GLU D OE1 1 
ATOM   8671  O  OE2 . GLU D 1 130 ? -65.420 68.620  84.575  1.00 51.40 ? 130  GLU D OE2 1 
ATOM   8672  N  N   . ALA D 1 131 ? -61.530 64.579  82.112  1.00 37.68 ? 131  ALA D N   1 
ATOM   8673  C  CA  . ALA D 1 131 ? -61.072 64.742  80.734  1.00 39.86 ? 131  ALA D CA  1 
ATOM   8674  C  C   . ALA D 1 131 ? -61.481 63.515  79.900  1.00 40.35 ? 131  ALA D C   1 
ATOM   8675  O  O   . ALA D 1 131 ? -61.706 63.628  78.699  1.00 40.34 ? 131  ALA D O   1 
ATOM   8676  C  CB  . ALA D 1 131 ? -59.543 64.929  80.696  1.00 34.97 ? 131  ALA D CB  1 
ATOM   8677  N  N   . THR D 1 132 ? -61.609 62.363  80.561  1.00 41.34 ? 132  THR D N   1 
ATOM   8678  C  CA  . THR D 1 132 ? -61.958 61.100  79.901  1.00 41.84 ? 132  THR D CA  1 
ATOM   8679  C  C   . THR D 1 132 ? -63.455 60.894  79.621  1.00 39.73 ? 132  THR D C   1 
ATOM   8680  O  O   . THR D 1 132 ? -63.823 60.177  78.692  1.00 41.11 ? 132  THR D O   1 
ATOM   8681  C  CB  . THR D 1 132 ? -61.383 59.895  80.726  1.00 41.68 ? 132  THR D CB  1 
ATOM   8682  O  OG1 . THR D 1 132 ? -59.956 59.980  80.728  1.00 43.63 ? 132  THR D OG1 1 
ATOM   8683  C  CG2 . THR D 1 132 ? -61.771 58.558  80.128  1.00 38.92 ? 132  THR D CG2 1 
ATOM   8684  N  N   . LEU D 1 133 ? -64.312 61.541  80.396  1.00 39.14 ? 133  LEU D N   1 
ATOM   8685  C  CA  . LEU D 1 133 ? -65.769 61.424  80.227  1.00 39.31 ? 133  LEU D CA  1 
ATOM   8686  C  C   . LEU D 1 133 ? -66.292 61.366  78.778  1.00 39.14 ? 133  LEU D C   1 
ATOM   8687  O  O   . LEU D 1 133 ? -66.983 60.420  78.404  1.00 37.47 ? 133  LEU D O   1 
ATOM   8688  C  CB  . LEU D 1 133 ? -66.474 62.572  80.940  1.00 35.93 ? 133  LEU D CB  1 
ATOM   8689  C  CG  . LEU D 1 133 ? -67.447 62.258  82.058  1.00 37.46 ? 133  LEU D CG  1 
ATOM   8690  C  CD1 . LEU D 1 133 ? -68.457 63.388  82.057  1.00 40.25 ? 133  LEU D CD1 1 
ATOM   8691  C  CD2 . LEU D 1 133 ? -68.151 60.914  81.876  1.00 37.29 ? 133  LEU D CD2 1 
ATOM   8692  N  N   . PRO D 1 134 ? -65.993 62.391  77.956  1.00 40.63 ? 134  PRO D N   1 
ATOM   8693  C  CA  . PRO D 1 134 ? -66.450 62.427  76.560  1.00 41.93 ? 134  PRO D CA  1 
ATOM   8694  C  C   . PRO D 1 134 ? -66.084 61.150  75.812  1.00 45.01 ? 134  PRO D C   1 
ATOM   8695  O  O   . PRO D 1 134 ? -66.909 60.558  75.111  1.00 46.80 ? 134  PRO D O   1 
ATOM   8696  C  CB  . PRO D 1 134 ? -65.715 63.631  75.979  1.00 41.78 ? 134  PRO D CB  1 
ATOM   8697  C  CG  . PRO D 1 134 ? -65.536 64.521  77.157  1.00 42.15 ? 134  PRO D CG  1 
ATOM   8698  C  CD  . PRO D 1 134 ? -65.136 63.551  78.252  1.00 41.80 ? 134  PRO D CD  1 
ATOM   8699  N  N   . ILE D 1 135 ? -64.832 60.734  75.962  1.00 43.82 ? 135  ILE D N   1 
ATOM   8700  C  CA  . ILE D 1 135 ? -64.338 59.535  75.306  1.00 42.27 ? 135  ILE D CA  1 
ATOM   8701  C  C   . ILE D 1 135 ? -65.037 58.253  75.754  1.00 40.55 ? 135  ILE D C   1 
ATOM   8702  O  O   . ILE D 1 135 ? -65.358 57.391  74.934  1.00 41.47 ? 135  ILE D O   1 
ATOM   8703  C  CB  . ILE D 1 135 ? -62.831 59.392  75.547  1.00 41.37 ? 135  ILE D CB  1 
ATOM   8704  C  CG1 . ILE D 1 135 ? -62.117 60.577  74.902  1.00 40.84 ? 135  ILE D CG1 1 
ATOM   8705  C  CG2 . ILE D 1 135 ? -62.335 58.058  75.012  1.00 41.31 ? 135  ILE D CG2 1 
ATOM   8706  C  CD1 . ILE D 1 135 ? -60.686 60.739  75.351  1.00 43.37 ? 135  ILE D CD1 1 
ATOM   8707  N  N   . ALA D 1 136 ? -65.258 58.124  77.053  1.00 39.59 ? 136  ALA D N   1 
ATOM   8708  C  CA  . ALA D 1 136 ? -65.911 56.935  77.595  1.00 40.81 ? 136  ALA D CA  1 
ATOM   8709  C  C   . ALA D 1 136 ? -67.397 56.903  77.220  1.00 42.34 ? 136  ALA D C   1 
ATOM   8710  O  O   . ALA D 1 136 ? -67.981 55.838  77.030  1.00 42.79 ? 136  ALA D O   1 
ATOM   8711  C  CB  . ALA D 1 136 ? -65.748 56.881  79.119  1.00 36.83 ? 136  ALA D CB  1 
ATOM   8712  N  N   . VAL D 1 137 ? -68.022 58.063  77.110  1.00 41.37 ? 137  VAL D N   1 
ATOM   8713  C  CA  . VAL D 1 137 ? -69.426 58.071  76.739  1.00 44.59 ? 137  VAL D CA  1 
ATOM   8714  C  C   . VAL D 1 137 ? -69.562 57.558  75.316  1.00 45.09 ? 137  VAL D C   1 
ATOM   8715  O  O   . VAL D 1 137 ? -70.422 56.729  75.001  1.00 44.28 ? 137  VAL D O   1 
ATOM   8716  C  CB  . VAL D 1 137 ? -70.020 59.483  76.819  1.00 44.72 ? 137  VAL D CB  1 
ATOM   8717  C  CG1 . VAL D 1 137 ? -71.313 59.545  76.022  1.00 42.54 ? 137  VAL D CG1 1 
ATOM   8718  C  CG2 . VAL D 1 137 ? -70.276 59.842  78.286  1.00 43.09 ? 137  VAL D CG2 1 
ATOM   8719  N  N   . ARG D 1 138 ? -68.699 58.070  74.459  1.00 44.06 ? 138  ARG D N   1 
ATOM   8720  C  CA  . ARG D 1 138 ? -68.700 57.668  73.081  1.00 47.18 ? 138  ARG D CA  1 
ATOM   8721  C  C   . ARG D 1 138 ? -68.496 56.156  73.071  1.00 48.39 ? 138  ARG D C   1 
ATOM   8722  O  O   . ARG D 1 138 ? -69.263 55.406  72.466  1.00 53.77 ? 138  ARG D O   1 
ATOM   8723  C  CB  . ARG D 1 138 ? -67.557 58.380  72.363  1.00 48.87 ? 138  ARG D CB  1 
ATOM   8724  C  CG  . ARG D 1 138 ? -67.663 58.450  70.856  1.00 52.42 ? 138  ARG D CG  1 
ATOM   8725  C  CD  . ARG D 1 138 ? -66.525 59.297  70.276  1.00 54.68 ? 138  ARG D CD  1 
ATOM   8726  N  NE  . ARG D 1 138 ? -66.467 60.598  70.944  1.00 59.37 ? 138  ARG D NE  1 
ATOM   8727  C  CZ  . ARG D 1 138 ? -65.346 61.139  71.415  1.00 59.49 ? 138  ARG D CZ  1 
ATOM   8728  N  NH1 . ARG D 1 138 ? -64.189 60.485  71.276  1.00 57.40 ? 138  ARG D NH1 1 
ATOM   8729  N  NH2 . ARG D 1 138 ? -65.387 62.309  72.050  1.00 57.14 ? 138  ARG D NH2 1 
ATOM   8730  N  N   . PHE D 1 139 ? -67.473 55.708  73.779  1.00 46.27 ? 139  PHE D N   1 
ATOM   8731  C  CA  . PHE D 1 139 ? -67.134 54.296  73.831  1.00 46.02 ? 139  PHE D CA  1 
ATOM   8732  C  C   . PHE D 1 139 ? -68.324 53.431  74.283  1.00 48.20 ? 139  PHE D C   1 
ATOM   8733  O  O   . PHE D 1 139 ? -68.642 52.408  73.672  1.00 48.24 ? 139  PHE D O   1 
ATOM   8734  C  CB  . PHE D 1 139 ? -65.930 54.136  74.770  1.00 43.36 ? 139  PHE D CB  1 
ATOM   8735  C  CG  . PHE D 1 139 ? -65.483 52.722  74.969  1.00 43.70 ? 139  PHE D CG  1 
ATOM   8736  C  CD1 . PHE D 1 139 ? -64.825 52.027  73.956  1.00 44.37 ? 139  PHE D CD1 1 
ATOM   8737  C  CD2 . PHE D 1 139 ? -65.683 52.085  76.193  1.00 42.96 ? 139  PHE D CD2 1 
ATOM   8738  C  CE1 . PHE D 1 139 ? -64.362 50.704  74.165  1.00 40.87 ? 139  PHE D CE1 1 
ATOM   8739  C  CE2 . PHE D 1 139 ? -65.225 50.767  76.403  1.00 43.35 ? 139  PHE D CE2 1 
ATOM   8740  C  CZ  . PHE D 1 139 ? -64.564 50.084  75.383  1.00 39.03 ? 139  PHE D CZ  1 
ATOM   8741  N  N   . ALA D 1 140 ? -68.986 53.851  75.355  1.00 48.16 ? 140  ALA D N   1 
ATOM   8742  C  CA  . ALA D 1 140 ? -70.115 53.104  75.889  1.00 48.23 ? 140  ALA D CA  1 
ATOM   8743  C  C   . ALA D 1 140 ? -71.197 52.916  74.834  1.00 49.62 ? 140  ALA D C   1 
ATOM   8744  O  O   . ALA D 1 140 ? -71.673 51.807  74.614  1.00 49.57 ? 140  ALA D O   1 
ATOM   8745  C  CB  . ALA D 1 140 ? -70.689 53.821  77.092  1.00 43.77 ? 140  ALA D CB  1 
ATOM   8746  N  N   . LYS D 1 141 ? -71.589 54.011  74.193  1.00 49.58 ? 141  LYS D N   1 
ATOM   8747  C  CA  . LYS D 1 141 ? -72.614 53.955  73.159  1.00 47.48 ? 141  LYS D CA  1 
ATOM   8748  C  C   . LYS D 1 141 ? -72.173 53.012  72.057  1.00 47.49 ? 141  LYS D C   1 
ATOM   8749  O  O   . LYS D 1 141 ? -72.888 52.081  71.688  1.00 44.40 ? 141  LYS D O   1 
ATOM   8750  C  CB  . LYS D 1 141 ? -72.851 55.349  72.595  1.00 45.04 ? 141  LYS D CB  1 
ATOM   8751  C  CG  . LYS D 1 141 ? -73.713 56.185  73.485  1.00 43.65 ? 141  LYS D CG  1 
ATOM   8752  C  CD  . LYS D 1 141 ? -73.749 57.598  73.000  1.00 48.09 ? 141  LYS D CD  1 
ATOM   8753  C  CE  . LYS D 1 141 ? -74.409 58.485  74.043  1.00 52.85 ? 141  LYS D CE  1 
ATOM   8754  N  NZ  . LYS D 1 141 ? -74.369 59.922  73.646  1.00 57.88 ? 141  LYS D NZ  1 
ATOM   8755  N  N   . THR D 1 142 ? -70.973 53.251  71.548  1.00 48.68 ? 142  THR D N   1 
ATOM   8756  C  CA  . THR D 1 142 ? -70.425 52.425  70.491  1.00 48.98 ? 142  THR D CA  1 
ATOM   8757  C  C   . THR D 1 142 ? -70.488 50.971  70.864  1.00 50.83 ? 142  THR D C   1 
ATOM   8758  O  O   . THR D 1 142 ? -70.824 50.127  70.048  1.00 52.94 ? 142  THR D O   1 
ATOM   8759  C  CB  . THR D 1 142 ? -68.978 52.819  70.200  1.00 46.59 ? 142  THR D CB  1 
ATOM   8760  O  OG1 . THR D 1 142 ? -68.976 53.930  69.301  1.00 49.24 ? 142  THR D OG1 1 
ATOM   8761  C  CG2 . THR D 1 142 ? -68.209 51.673  69.579  1.00 46.88 ? 142  THR D CG2 1 
ATOM   8762  N  N   . LEU D 1 143 ? -70.175 50.690  72.115  1.00 55.46 ? 143  LEU D N   1 
ATOM   8763  C  CA  . LEU D 1 143 ? -70.161 49.329  72.630  1.00 57.17 ? 143  LEU D CA  1 
ATOM   8764  C  C   . LEU D 1 143 ? -71.568 48.766  72.712  1.00 56.68 ? 143  LEU D C   1 
ATOM   8765  O  O   . LEU D 1 143 ? -71.813 47.593  72.446  1.00 59.12 ? 143  LEU D O   1 
ATOM   8766  C  CB  . LEU D 1 143 ? -69.519 49.346  74.011  1.00 59.95 ? 143  LEU D CB  1 
ATOM   8767  C  CG  . LEU D 1 143 ? -68.772 48.100  74.448  1.00 57.69 ? 143  LEU D CG  1 
ATOM   8768  C  CD1 . LEU D 1 143 ? -67.955 47.511  73.311  1.00 53.60 ? 143  LEU D CD1 1 
ATOM   8769  C  CD2 . LEU D 1 143 ? -67.892 48.515  75.602  1.00 60.89 ? 143  LEU D CD2 1 
ATOM   8770  N  N   . LEU D 1 144 ? -72.495 49.624  73.085  1.00 57.64 ? 144  LEU D N   1 
ATOM   8771  C  CA  . LEU D 1 144 ? -73.878 49.234  73.209  1.00 59.87 ? 144  LEU D CA  1 
ATOM   8772  C  C   . LEU D 1 144 ? -74.396 48.822  71.833  1.00 61.74 ? 144  LEU D C   1 
ATOM   8773  O  O   . LEU D 1 144 ? -74.875 47.699  71.653  1.00 63.34 ? 144  LEU D O   1 
ATOM   8774  C  CB  . LEU D 1 144 ? -74.679 50.412  73.757  1.00 59.76 ? 144  LEU D CB  1 
ATOM   8775  C  CG  . LEU D 1 144 ? -75.887 50.065  74.618  1.00 59.96 ? 144  LEU D CG  1 
ATOM   8776  C  CD1 . LEU D 1 144 ? -75.464 49.015  75.621  1.00 62.43 ? 144  LEU D CD1 1 
ATOM   8777  C  CD2 . LEU D 1 144 ? -76.433 51.314  75.311  1.00 57.03 ? 144  LEU D CD2 1 
ATOM   8778  N  N   . ALA D 1 145 ? -74.272 49.730  70.866  1.00 61.96 ? 145  ALA D N   1 
ATOM   8779  C  CA  . ALA D 1 145 ? -74.727 49.504  69.489  1.00 62.31 ? 145  ALA D CA  1 
ATOM   8780  C  C   . ALA D 1 145 ? -74.085 48.311  68.769  1.00 62.98 ? 145  ALA D C   1 
ATOM   8781  O  O   . ALA D 1 145 ? -74.703 47.696  67.902  1.00 64.74 ? 145  ALA D O   1 
ATOM   8782  C  CB  . ALA D 1 145 ? -74.511 50.765  68.664  1.00 58.03 ? 145  ALA D CB  1 
ATOM   8783  N  N   . ASN D 1 146 ? -72.847 47.987  69.117  1.00 63.72 ? 146  ASN D N   1 
ATOM   8784  C  CA  . ASN D 1 146 ? -72.159 46.875  68.482  1.00 63.27 ? 146  ASN D CA  1 
ATOM   8785  C  C   . ASN D 1 146 ? -72.961 45.585  68.614  1.00 64.48 ? 146  ASN D C   1 
ATOM   8786  O  O   . ASN D 1 146 ? -73.565 45.320  69.652  1.00 65.49 ? 146  ASN D O   1 
ATOM   8787  C  CB  . ASN D 1 146 ? -70.796 46.688  69.121  1.00 62.44 ? 146  ASN D CB  1 
ATOM   8788  C  CG  . ASN D 1 146 ? -69.938 45.728  68.358  1.00 61.74 ? 146  ASN D CG  1 
ATOM   8789  O  OD1 . ASN D 1 146 ? -69.482 46.049  67.263  1.00 61.03 ? 146  ASN D OD1 1 
ATOM   8790  N  ND2 . ASN D 1 146 ? -69.714 44.533  68.919  1.00 57.67 ? 146  ASN D ND2 1 
ATOM   8791  N  N   . SER D 1 147 ? -72.953 44.778  67.559  1.00 67.77 ? 147  SER D N   1 
ATOM   8792  C  CA  . SER D 1 147 ? -73.698 43.510  67.555  1.00 71.73 ? 147  SER D CA  1 
ATOM   8793  C  C   . SER D 1 147 ? -72.784 42.289  67.518  1.00 69.81 ? 147  SER D C   1 
ATOM   8794  O  O   . SER D 1 147 ? -73.178 41.200  67.939  1.00 70.14 ? 147  SER D O   1 
ATOM   8795  C  CB  . SER D 1 147 ? -74.640 43.450  66.345  1.00 74.34 ? 147  SER D CB  1 
ATOM   8796  O  OG  . SER D 1 147 ? -75.466 44.602  66.279  1.00 78.70 ? 147  SER D OG  1 
ATOM   8797  N  N   . SER D 1 148 ? -71.575 42.488  66.997  1.00 67.40 ? 148  SER D N   1 
ATOM   8798  C  CA  . SER D 1 148 ? -70.569 41.439  66.876  1.00 64.01 ? 148  SER D CA  1 
ATOM   8799  C  C   . SER D 1 148 ? -70.497 40.474  68.079  1.00 62.71 ? 148  SER D C   1 
ATOM   8800  O  O   . SER D 1 148 ? -70.739 40.857  69.229  1.00 62.57 ? 148  SER D O   1 
ATOM   8801  C  CB  . SER D 1 148 ? -69.212 42.094  66.635  1.00 64.65 ? 148  SER D CB  1 
ATOM   8802  O  OG  . SER D 1 148 ? -68.161 41.153  66.741  1.00 74.43 ? 148  SER D OG  1 
ATOM   8803  N  N   . PRO D 1 149 ? -70.169 39.196  67.821  1.00 61.07 ? 149  PRO D N   1 
ATOM   8804  C  CA  . PRO D 1 149 ? -70.067 38.176  68.877  1.00 59.82 ? 149  PRO D CA  1 
ATOM   8805  C  C   . PRO D 1 149 ? -69.271 38.669  70.088  1.00 59.74 ? 149  PRO D C   1 
ATOM   8806  O  O   . PRO D 1 149 ? -68.294 39.402  69.941  1.00 59.62 ? 149  PRO D O   1 
ATOM   8807  C  CB  . PRO D 1 149 ? -69.369 37.015  68.174  1.00 58.61 ? 149  PRO D CB  1 
ATOM   8808  C  CG  . PRO D 1 149 ? -69.836 37.156  66.753  1.00 56.61 ? 149  PRO D CG  1 
ATOM   8809  C  CD  . PRO D 1 149 ? -69.800 38.642  66.504  1.00 58.01 ? 149  PRO D CD  1 
ATOM   8810  N  N   . PHE D 1 150 ? -69.695 38.244  71.275  1.00 58.70 ? 150  PHE D N   1 
ATOM   8811  C  CA  . PHE D 1 150 ? -69.067 38.623  72.539  1.00 56.37 ? 150  PHE D CA  1 
ATOM   8812  C  C   . PHE D 1 150 ? -67.692 37.987  72.820  1.00 56.98 ? 150  PHE D C   1 
ATOM   8813  O  O   . PHE D 1 150 ? -67.500 36.784  72.657  1.00 59.52 ? 150  PHE D O   1 
ATOM   8814  C  CB  . PHE D 1 150 ? -70.014 38.286  73.682  1.00 53.06 ? 150  PHE D CB  1 
ATOM   8815  C  CG  . PHE D 1 150 ? -69.476 38.638  75.035  1.00 55.30 ? 150  PHE D CG  1 
ATOM   8816  C  CD1 . PHE D 1 150 ? -69.375 39.965  75.434  1.00 52.16 ? 150  PHE D CD1 1 
ATOM   8817  C  CD2 . PHE D 1 150 ? -69.074 37.642  75.919  1.00 53.91 ? 150  PHE D CD2 1 
ATOM   8818  C  CE1 . PHE D 1 150 ? -68.881 40.300  76.694  1.00 50.42 ? 150  PHE D CE1 1 
ATOM   8819  C  CE2 . PHE D 1 150 ? -68.581 37.969  77.181  1.00 53.22 ? 150  PHE D CE2 1 
ATOM   8820  C  CZ  . PHE D 1 150 ? -68.489 39.306  77.567  1.00 51.84 ? 150  PHE D CZ  1 
ATOM   8821  N  N   . ASN D 1 151 ? -66.748 38.811  73.262  1.00 57.21 ? 151  ASN D N   1 
ATOM   8822  C  CA  . ASN D 1 151 ? -65.391 38.376  73.596  1.00 56.01 ? 151  ASN D CA  1 
ATOM   8823  C  C   . ASN D 1 151 ? -65.082 38.648  75.094  1.00 57.28 ? 151  ASN D C   1 
ATOM   8824  O  O   . ASN D 1 151 ? -64.933 39.805  75.510  1.00 55.65 ? 151  ASN D O   1 
ATOM   8825  C  CB  . ASN D 1 151 ? -64.392 39.115  72.710  1.00 59.01 ? 151  ASN D CB  1 
ATOM   8826  C  CG  . ASN D 1 151 ? -62.975 38.951  73.185  1.00 64.54 ? 151  ASN D CG  1 
ATOM   8827  O  OD1 . ASN D 1 151 ? -62.566 37.864  73.597  1.00 69.10 ? 151  ASN D OD1 1 
ATOM   8828  N  ND2 . ASN D 1 151 ? -62.210 40.030  73.137  1.00 70.31 ? 151  ASN D ND2 1 
ATOM   8829  N  N   . VAL D 1 152 ? -64.974 37.582  75.888  1.00 54.41 ? 152  VAL D N   1 
ATOM   8830  C  CA  . VAL D 1 152 ? -64.732 37.702  77.321  1.00 51.52 ? 152  VAL D CA  1 
ATOM   8831  C  C   . VAL D 1 152 ? -63.679 38.763  77.664  1.00 51.31 ? 152  VAL D C   1 
ATOM   8832  O  O   . VAL D 1 152 ? -63.909 39.651  78.493  1.00 49.08 ? 152  VAL D O   1 
ATOM   8833  C  CB  . VAL D 1 152 ? -64.287 36.342  77.929  1.00 50.41 ? 152  VAL D CB  1 
ATOM   8834  C  CG1 . VAL D 1 152 ? -64.278 36.406  79.452  1.00 47.62 ? 152  VAL D CG1 1 
ATOM   8835  C  CG2 . VAL D 1 152 ? -65.209 35.264  77.473  1.00 54.54 ? 152  VAL D CG2 1 
ATOM   8836  N  N   . ASP D 1 153 ? -62.519 38.660  77.032  1.00 48.94 ? 153  ASP D N   1 
ATOM   8837  C  CA  . ASP D 1 153 ? -61.442 39.598  77.291  1.00 46.86 ? 153  ASP D CA  1 
ATOM   8838  C  C   . ASP D 1 153 ? -61.892 41.043  77.155  1.00 44.79 ? 153  ASP D C   1 
ATOM   8839  O  O   . ASP D 1 153 ? -61.774 41.824  78.085  1.00 41.13 ? 153  ASP D O   1 
ATOM   8840  C  CB  . ASP D 1 153 ? -60.280 39.314  76.349  1.00 47.21 ? 153  ASP D CB  1 
ATOM   8841  C  CG  . ASP D 1 153 ? -59.541 38.066  76.732  1.00 52.17 ? 153  ASP D CG  1 
ATOM   8842  O  OD1 . ASP D 1 153 ? -59.777 37.569  77.854  1.00 60.15 ? 153  ASP D OD1 1 
ATOM   8843  O  OD2 . ASP D 1 153 ? -58.721 37.581  75.935  1.00 58.06 ? 153  ASP D OD2 1 
ATOM   8844  N  N   . THR D 1 154 ? -62.403 41.399  75.986  1.00 42.22 ? 154  THR D N   1 
ATOM   8845  C  CA  . THR D 1 154 ? -62.862 42.750  75.794  1.00 40.44 ? 154  THR D CA  1 
ATOM   8846  C  C   . THR D 1 154 ? -63.911 43.079  76.845  1.00 39.65 ? 154  THR D C   1 
ATOM   8847  O  O   . THR D 1 154 ? -63.923 44.166  77.415  1.00 43.17 ? 154  THR D O   1 
ATOM   8848  C  CB  . THR D 1 154 ? -63.429 42.922  74.404  1.00 38.23 ? 154  THR D CB  1 
ATOM   8849  O  OG1 . THR D 1 154 ? -62.345 42.953  73.474  1.00 44.01 ? 154  THR D OG1 1 
ATOM   8850  C  CG2 . THR D 1 154 ? -64.196 44.215  74.301  1.00 42.55 ? 154  THR D CG2 1 
ATOM   8851  N  N   . GLY D 1 155 ? -64.786 42.131  77.125  1.00 38.49 ? 155  GLY D N   1 
ATOM   8852  C  CA  . GLY D 1 155 ? -65.812 42.374  78.123  1.00 38.61 ? 155  GLY D CA  1 
ATOM   8853  C  C   . GLY D 1 155 ? -65.250 42.684  79.509  1.00 38.65 ? 155  GLY D C   1 
ATOM   8854  O  O   . GLY D 1 155 ? -65.771 43.533  80.231  1.00 36.55 ? 155  GLY D O   1 
ATOM   8855  N  N   . ALA D 1 156 ? -64.182 41.989  79.871  1.00 34.90 ? 156  ALA D N   1 
ATOM   8856  C  CA  . ALA D 1 156 ? -63.538 42.176  81.139  1.00 32.12 ? 156  ALA D CA  1 
ATOM   8857  C  C   . ALA D 1 156 ? -62.880 43.551  81.182  1.00 35.55 ? 156  ALA D C   1 
ATOM   8858  O  O   . ALA D 1 156 ? -63.109 44.351  82.115  1.00 34.93 ? 156  ALA D O   1 
ATOM   8859  C  CB  . ALA D 1 156 ? -62.499 41.086  81.331  1.00 30.83 ? 156  ALA D CB  1 
ATOM   8860  N  N   . MET D 1 157 ? -62.057 43.842  80.178  1.00 36.42 ? 157  MET D N   1 
ATOM   8861  C  CA  . MET D 1 157 ? -61.367 45.143  80.142  1.00 40.39 ? 157  MET D CA  1 
ATOM   8862  C  C   . MET D 1 157 ? -62.345 46.322  80.077  1.00 39.06 ? 157  MET D C   1 
ATOM   8863  O  O   . MET D 1 157 ? -62.127 47.382  80.683  1.00 40.93 ? 157  MET D O   1 
ATOM   8864  C  CB  . MET D 1 157 ? -60.392 45.228  78.962  1.00 38.82 ? 157  MET D CB  1 
ATOM   8865  C  CG  . MET D 1 157 ? -59.265 46.230  79.216  1.00 44.55 ? 157  MET D CG  1 
ATOM   8866  S  SD  . MET D 1 157 ? -58.390 45.869  80.786  1.00 49.23 ? 157  MET D SD  1 
ATOM   8867  C  CE  . MET D 1 157 ? -57.936 44.155  80.510  1.00 43.57 ? 157  MET D CE  1 
ATOM   8868  N  N   . ALA D 1 158 ? -63.426 46.124  79.336  1.00 33.57 ? 158  ALA D N   1 
ATOM   8869  C  CA  . ALA D 1 158 ? -64.437 47.134  79.219  1.00 30.14 ? 158  ALA D CA  1 
ATOM   8870  C  C   . ALA D 1 158 ? -65.100 47.424  80.571  1.00 29.36 ? 158  ALA D C   1 
ATOM   8871  O  O   . ALA D 1 158 ? -65.335 48.582  80.925  1.00 28.49 ? 158  ALA D O   1 
ATOM   8872  C  CB  . ALA D 1 158 ? -65.459 46.690  78.233  1.00 29.91 ? 158  ALA D CB  1 
ATOM   8873  N  N   . THR D 1 159 ? -65.397 46.391  81.343  1.00 27.79 ? 159  THR D N   1 
ATOM   8874  C  CA  . THR D 1 159 ? -66.047 46.679  82.587  1.00 33.96 ? 159  THR D CA  1 
ATOM   8875  C  C   . THR D 1 159 ? -65.091 47.389  83.538  1.00 35.49 ? 159  THR D C   1 
ATOM   8876  O  O   . THR D 1 159 ? -65.515 48.283  84.282  1.00 37.61 ? 159  THR D O   1 
ATOM   8877  C  CB  . THR D 1 159 ? -66.655 45.424  83.247  1.00 36.16 ? 159  THR D CB  1 
ATOM   8878  O  OG1 . THR D 1 159 ? -65.830 44.993  84.324  1.00 44.11 ? 159  THR D OG1 1 
ATOM   8879  C  CG2 . THR D 1 159 ? -66.794 44.338  82.273  1.00 26.51 ? 159  THR D CG2 1 
ATOM   8880  N  N   . LEU D 1 160 ? -63.813 47.006  83.525  1.00 33.19 ? 160  LEU D N   1 
ATOM   8881  C  CA  . LEU D 1 160 ? -62.848 47.695  84.366  1.00 31.80 ? 160  LEU D CA  1 
ATOM   8882  C  C   . LEU D 1 160 ? -62.782 49.162  83.946  1.00 34.59 ? 160  LEU D C   1 
ATOM   8883  O  O   . LEU D 1 160 ? -62.797 50.050  84.794  1.00 37.12 ? 160  LEU D O   1 
ATOM   8884  C  CB  . LEU D 1 160 ? -61.448 47.103  84.224  1.00 34.68 ? 160  LEU D CB  1 
ATOM   8885  C  CG  . LEU D 1 160 ? -61.205 45.694  84.783  1.00 37.82 ? 160  LEU D CG  1 
ATOM   8886  C  CD1 . LEU D 1 160 ? -59.774 45.255  84.502  1.00 35.98 ? 160  LEU D CD1 1 
ATOM   8887  C  CD2 . LEU D 1 160 ? -61.479 45.671  86.263  1.00 34.53 ? 160  LEU D CD2 1 
ATOM   8888  N  N   . ALA D 1 161 ? -62.707 49.440  82.645  1.00 32.74 ? 161  ALA D N   1 
ATOM   8889  C  CA  . ALA D 1 161 ? -62.625 50.838  82.232  1.00 33.54 ? 161  ALA D CA  1 
ATOM   8890  C  C   . ALA D 1 161 ? -63.899 51.599  82.616  1.00 33.61 ? 161  ALA D C   1 
ATOM   8891  O  O   . ALA D 1 161 ? -63.856 52.651  83.241  1.00 35.27 ? 161  ALA D O   1 
ATOM   8892  C  CB  . ALA D 1 161 ? -62.370 50.932  80.732  1.00 32.05 ? 161  ALA D CB  1 
ATOM   8893  N  N   . LEU D 1 162 ? -65.040 51.041  82.260  1.00 33.84 ? 162  LEU D N   1 
ATOM   8894  C  CA  . LEU D 1 162 ? -66.285 51.675  82.552  1.00 31.38 ? 162  LEU D CA  1 
ATOM   8895  C  C   . LEU D 1 162 ? -66.572 51.748  84.058  1.00 35.60 ? 162  LEU D C   1 
ATOM   8896  O  O   . LEU D 1 162 ? -67.334 52.621  84.500  1.00 35.34 ? 162  LEU D O   1 
ATOM   8897  C  CB  . LEU D 1 162 ? -67.386 50.939  81.778  1.00 30.95 ? 162  LEU D CB  1 
ATOM   8898  C  CG  . LEU D 1 162 ? -67.911 51.584  80.471  1.00 36.05 ? 162  LEU D CG  1 
ATOM   8899  C  CD1 . LEU D 1 162 ? -66.969 52.665  79.956  1.00 38.81 ? 162  LEU D CD1 1 
ATOM   8900  C  CD2 . LEU D 1 162 ? -68.132 50.515  79.432  1.00 31.52 ? 162  LEU D CD2 1 
ATOM   8901  N  N   . THR D 1 163 ? -65.980 50.855  84.858  1.00 33.52 ? 163  THR D N   1 
ATOM   8902  C  CA  . THR D 1 163 ? -66.244 50.908  86.292  1.00 34.85 ? 163  THR D CA  1 
ATOM   8903  C  C   . THR D 1 163 ? -65.460 52.086  86.850  1.00 37.00 ? 163  THR D C   1 
ATOM   8904  O  O   . THR D 1 163 ? -65.966 52.859  87.673  1.00 36.32 ? 163  THR D O   1 
ATOM   8905  C  CB  . THR D 1 163 ? -65.826 49.616  87.028  1.00 35.27 ? 163  THR D CB  1 
ATOM   8906  O  OG1 . THR D 1 163 ? -66.719 48.569  86.672  1.00 35.35 ? 163  THR D OG1 1 
ATOM   8907  C  CG2 . THR D 1 163 ? -65.897 49.804  88.540  1.00 32.26 ? 163  THR D CG2 1 
ATOM   8908  N  N   . CYS D 1 164 ? -64.224 52.225  86.392  1.00 34.78 ? 164  CYS D N   1 
ATOM   8909  C  CA  . CYS D 1 164 ? -63.430 53.357  86.830  1.00 38.22 ? 164  CYS D CA  1 
ATOM   8910  C  C   . CYS D 1 164 ? -64.274 54.618  86.613  1.00 35.32 ? 164  CYS D C   1 
ATOM   8911  O  O   . CYS D 1 164 ? -64.467 55.366  87.552  1.00 35.75 ? 164  CYS D O   1 
ATOM   8912  C  CB  . CYS D 1 164 ? -62.105 53.442  86.044  1.00 40.14 ? 164  CYS D CB  1 
ATOM   8913  S  SG  . CYS D 1 164 ? -61.085 54.907  86.411  1.00 50.51 ? 164  CYS D SG  1 
ATOM   8914  N  N   . MET D 1 165 ? -64.780 54.833  85.394  1.00 32.47 ? 165  MET D N   1 
ATOM   8915  C  CA  . MET D 1 165 ? -65.603 56.002  85.087  1.00 36.52 ? 165  MET D CA  1 
ATOM   8916  C  C   . MET D 1 165 ? -66.877 56.137  85.924  1.00 38.98 ? 165  MET D C   1 
ATOM   8917  O  O   . MET D 1 165 ? -67.211 57.225  86.393  1.00 37.76 ? 165  MET D O   1 
ATOM   8918  C  CB  . MET D 1 165 ? -65.993 55.988  83.615  1.00 38.11 ? 165  MET D CB  1 
ATOM   8919  C  CG  . MET D 1 165 ? -64.812 56.242  82.715  1.00 44.30 ? 165  MET D CG  1 
ATOM   8920  S  SD  . MET D 1 165 ? -64.010 57.813  83.114  1.00 46.38 ? 165  MET D SD  1 
ATOM   8921  C  CE  . MET D 1 165 ? -65.222 58.969  82.521  1.00 45.22 ? 165  MET D CE  1 
ATOM   8922  N  N   . TYR D 1 166 ? -67.583 55.019  86.073  1.00 38.88 ? 166  TYR D N   1 
ATOM   8923  C  CA  . TYR D 1 166 ? -68.827 54.938  86.818  1.00 37.27 ? 166  TYR D CA  1 
ATOM   8924  C  C   . TYR D 1 166 ? -68.677 55.508  88.214  1.00 39.15 ? 166  TYR D C   1 
ATOM   8925  O  O   . TYR D 1 166 ? -69.625 56.029  88.778  1.00 39.93 ? 166  TYR D O   1 
ATOM   8926  C  CB  . TYR D 1 166 ? -69.219 53.485  86.967  1.00 37.47 ? 166  TYR D CB  1 
ATOM   8927  C  CG  . TYR D 1 166 ? -70.526 53.265  87.662  1.00 37.12 ? 166  TYR D CG  1 
ATOM   8928  C  CD1 . TYR D 1 166 ? -71.729 53.343  86.950  1.00 39.09 ? 166  TYR D CD1 1 
ATOM   8929  C  CD2 . TYR D 1 166 ? -70.570 52.902  89.015  1.00 38.22 ? 166  TYR D CD2 1 
ATOM   8930  C  CE1 . TYR D 1 166 ? -72.943 53.046  87.552  1.00 35.61 ? 166  TYR D CE1 1 
ATOM   8931  C  CE2 . TYR D 1 166 ? -71.784 52.607  89.634  1.00 35.68 ? 166  TYR D CE2 1 
ATOM   8932  C  CZ  . TYR D 1 166 ? -72.964 52.674  88.883  1.00 38.09 ? 166  TYR D CZ  1 
ATOM   8933  O  OH  . TYR D 1 166 ? -74.166 52.316  89.433  1.00 40.39 ? 166  TYR D OH  1 
ATOM   8934  N  N   . ASN D 1 167 ? -67.486 55.382  88.783  1.00 38.79 ? 167  ASN D N   1 
ATOM   8935  C  CA  . ASN D 1 167 ? -67.275 55.857  90.129  1.00 39.26 ? 167  ASN D CA  1 
ATOM   8936  C  C   . ASN D 1 167 ? -66.684 57.223  90.200  1.00 41.37 ? 167  ASN D C   1 
ATOM   8937  O  O   . ASN D 1 167 ? -66.499 57.735  91.308  1.00 45.84 ? 167  ASN D O   1 
ATOM   8938  C  CB  . ASN D 1 167 ? -66.393 54.889  90.928  1.00 39.20 ? 167  ASN D CB  1 
ATOM   8939  C  CG  . ASN D 1 167 ? -67.065 53.535  91.149  1.00 40.57 ? 167  ASN D CG  1 
ATOM   8940  O  OD1 . ASN D 1 167 ? -68.290 53.449  91.321  1.00 43.28 ? 167  ASN D OD1 1 
ATOM   8941  N  ND2 . ASN D 1 167 ? -66.268 52.475  91.146  1.00 36.60 ? 167  ASN D ND2 1 
ATOM   8942  N  N   . LYS D 1 168 ? -66.390 57.819  89.042  1.00 37.06 ? 168  LYS D N   1 
ATOM   8943  C  CA  . LYS D 1 168 ? -65.822 59.154  89.021  1.00 33.81 ? 168  LYS D CA  1 
ATOM   8944  C  C   . LYS D 1 168 ? -66.669 60.173  88.271  1.00 36.03 ? 168  LYS D C   1 
ATOM   8945  O  O   . LYS D 1 168 ? -66.112 61.109  87.678  1.00 38.11 ? 168  LYS D O   1 
ATOM   8946  C  CB  . LYS D 1 168 ? -64.415 59.119  88.420  1.00 35.72 ? 168  LYS D CB  1 
ATOM   8947  C  CG  . LYS D 1 168 ? -63.355 58.445  89.284  1.00 38.20 ? 168  LYS D CG  1 
ATOM   8948  C  CD  . LYS D 1 168 ? -63.113 59.176  90.599  1.00 39.07 ? 168  LYS D CD  1 
ATOM   8949  C  CE  . LYS D 1 168 ? -61.956 58.559  91.416  1.00 45.09 ? 168  LYS D CE  1 
ATOM   8950  N  NZ  . LYS D 1 168 ? -61.679 59.273  92.738  1.00 42.62 ? 168  LYS D NZ  1 
ATOM   8951  N  N   . ILE D 1 169 ? -67.991 59.992  88.266  1.00 34.74 ? 169  ILE D N   1 
ATOM   8952  C  CA  . ILE D 1 169 ? -68.878 60.938  87.586  1.00 37.82 ? 169  ILE D CA  1 
ATOM   8953  C  C   . ILE D 1 169 ? -68.701 62.288  88.280  1.00 36.89 ? 169  ILE D C   1 
ATOM   8954  O  O   . ILE D 1 169 ? -68.946 62.398  89.464  1.00 38.38 ? 169  ILE D O   1 
ATOM   8955  C  CB  . ILE D 1 169 ? -70.351 60.558  87.729  1.00 41.13 ? 169  ILE D CB  1 
ATOM   8956  C  CG1 . ILE D 1 169 ? -70.603 59.146  87.172  1.00 41.54 ? 169  ILE D CG1 1 
ATOM   8957  C  CG2 . ILE D 1 169 ? -71.191 61.601  87.046  1.00 37.70 ? 169  ILE D CG2 1 
ATOM   8958  C  CD1 . ILE D 1 169 ? -70.389 58.997  85.692  1.00 40.35 ? 169  ILE D CD1 1 
ATOM   8959  N  N   . PRO D 1 170 ? -68.289 63.332  87.548  1.00 36.93 ? 170  PRO D N   1 
ATOM   8960  C  CA  . PRO D 1 170 ? -68.105 64.631  88.208  1.00 34.62 ? 170  PRO D CA  1 
ATOM   8961  C  C   . PRO D 1 170 ? -69.358 65.117  88.932  1.00 34.82 ? 170  PRO D C   1 
ATOM   8962  O  O   . PRO D 1 170 ? -70.473 65.041  88.406  1.00 34.67 ? 170  PRO D O   1 
ATOM   8963  C  CB  . PRO D 1 170 ? -67.701 65.546  87.058  1.00 35.80 ? 170  PRO D CB  1 
ATOM   8964  C  CG  . PRO D 1 170 ? -66.942 64.558  86.115  1.00 38.03 ? 170  PRO D CG  1 
ATOM   8965  C  CD  . PRO D 1 170 ? -67.885 63.378  86.130  1.00 35.00 ? 170  PRO D CD  1 
ATOM   8966  N  N   . VAL D 1 171 ? -69.182 65.594  90.153  1.00 33.44 ? 171  VAL D N   1 
ATOM   8967  C  CA  . VAL D 1 171 ? -70.312 66.109  90.903  1.00 35.31 ? 171  VAL D CA  1 
ATOM   8968  C  C   . VAL D 1 171 ? -70.962 67.216  90.110  1.00 36.44 ? 171  VAL D C   1 
ATOM   8969  O  O   . VAL D 1 171 ? -70.266 68.117  89.640  1.00 35.44 ? 171  VAL D O   1 
ATOM   8970  C  CB  . VAL D 1 171 ? -69.862 66.707  92.229  1.00 37.23 ? 171  VAL D CB  1 
ATOM   8971  C  CG1 . VAL D 1 171 ? -70.982 67.559  92.834  1.00 31.05 ? 171  VAL D CG1 1 
ATOM   8972  C  CG2 . VAL D 1 171 ? -69.468 65.595  93.187  1.00 34.45 ? 171  VAL D CG2 1 
ATOM   8973  N  N   . GLY D 1 172 ? -72.285 67.141  89.966  1.00 39.15 ? 172  GLY D N   1 
ATOM   8974  C  CA  . GLY D 1 172 ? -73.031 68.155  89.244  1.00 44.47 ? 172  GLY D CA  1 
ATOM   8975  C  C   . GLY D 1 172 ? -73.260 67.944  87.763  1.00 48.97 ? 172  GLY D C   1 
ATOM   8976  O  O   . GLY D 1 172 ? -73.851 68.797  87.114  1.00 52.56 ? 172  GLY D O   1 
ATOM   8977  N  N   . SER D 1 173 ? -72.809 66.828  87.217  1.00 53.46 ? 173  SER D N   1 
ATOM   8978  C  CA  . SER D 1 173 ? -72.993 66.569  85.793  1.00 62.67 ? 173  SER D CA  1 
ATOM   8979  C  C   . SER D 1 173 ? -74.042 65.491  85.649  1.00 68.47 ? 173  SER D C   1 
ATOM   8980  O  O   . SER D 1 173 ? -74.186 64.876  84.601  1.00 72.38 ? 173  SER D O   1 
ATOM   8981  C  CB  . SER D 1 173 ? -71.678 66.071  85.185  1.00 63.68 ? 173  SER D CB  1 
ATOM   8982  O  OG  . SER D 1 173 ? -71.279 64.857  85.792  1.00 58.59 ? 173  SER D OG  1 
ATOM   8983  N  N   . GLU D 1 174 ? -74.792 65.291  86.717  1.00 74.22 ? 174  GLU D N   1 
ATOM   8984  C  CA  . GLU D 1 174 ? -75.780 64.215  86.797  1.00 81.75 ? 174  GLU D CA  1 
ATOM   8985  C  C   . GLU D 1 174 ? -76.772 64.001  85.630  1.00 82.53 ? 174  GLU D C   1 
ATOM   8986  O  O   . GLU D 1 174 ? -77.960 63.666  85.818  1.00 82.76 ? 174  GLU D O   1 
ATOM   8987  C  CB  . GLU D 1 174 ? -76.504 64.314  88.159  1.00 86.49 ? 174  GLU D CB  1 
ATOM   8988  C  CG  . GLU D 1 174 ? -75.794 65.225  89.187  1.00 90.90 ? 174  GLU D CG  1 
ATOM   8989  C  CD  . GLU D 1 174 ? -74.783 64.600  90.174  1.00 92.03 ? 174  GLU D CD  1 
ATOM   8990  O  OE1 . GLU D 1 174 ? -74.968 63.432  90.606  1.00 90.84 ? 174  GLU D OE1 1 
ATOM   8991  O  OE2 . GLU D 1 174 ? -73.825 65.355  90.539  1.00 86.74 ? 174  GLU D OE2 1 
ATOM   8992  N  N   . GLU D 1 175 ? -76.263 64.146  84.417  1.00 80.64 ? 175  GLU D N   1 
ATOM   8993  C  CA  . GLU D 1 175 ? -77.105 63.952  83.268  1.00 80.73 ? 175  GLU D CA  1 
ATOM   8994  C  C   . GLU D 1 175 ? -77.076 62.513  82.725  1.00 78.64 ? 175  GLU D C   1 
ATOM   8995  O  O   . GLU D 1 175 ? -76.774 62.286  81.546  1.00 78.27 ? 175  GLU D O   1 
ATOM   8996  C  CB  . GLU D 1 175 ? -76.753 64.965  82.166  1.00 84.05 ? 175  GLU D CB  1 
ATOM   8997  C  CG  . GLU D 1 175 ? -75.288 65.003  81.719  1.00 90.26 ? 175  GLU D CG  1 
ATOM   8998  C  CD  . GLU D 1 175 ? -75.085 65.841  80.450  1.00 93.69 ? 175  GLU D CD  1 
ATOM   8999  O  OE1 . GLU D 1 175 ? -75.696 66.932  80.354  1.00 94.35 ? 175  GLU D OE1 1 
ATOM   9000  O  OE2 . GLU D 1 175 ? -74.315 65.412  79.554  1.00 96.28 ? 175  GLU D OE2 1 
ATOM   9001  N  N   . GLY D 1 176 ? -77.374 61.542  83.590  1.00 73.22 ? 176  GLY D N   1 
ATOM   9002  C  CA  . GLY D 1 176 ? -77.426 60.159  83.147  1.00 66.22 ? 176  GLY D CA  1 
ATOM   9003  C  C   . GLY D 1 176 ? -76.210 59.496  82.505  1.00 65.29 ? 176  GLY D C   1 
ATOM   9004  O  O   . GLY D 1 176 ? -76.359 58.572  81.687  1.00 64.53 ? 176  GLY D O   1 
ATOM   9005  N  N   . TYR D 1 177 ? -75.010 59.961  82.847  1.00 60.35 ? 177  TYR D N   1 
ATOM   9006  C  CA  . TYR D 1 177 ? -73.790 59.343  82.353  1.00 51.91 ? 177  TYR D CA  1 
ATOM   9007  C  C   . TYR D 1 177 ? -73.728 58.036  83.122  1.00 47.59 ? 177  TYR D C   1 
ATOM   9008  O  O   . TYR D 1 177 ? -73.367 56.985  82.611  1.00 43.78 ? 177  TYR D O   1 
ATOM   9009  C  CB  . TYR D 1 177 ? -72.580 60.184  82.730  1.00 52.69 ? 177  TYR D CB  1 
ATOM   9010  C  CG  . TYR D 1 177 ? -72.338 61.364  81.854  1.00 55.55 ? 177  TYR D CG  1 
ATOM   9011  C  CD1 . TYR D 1 177 ? -72.161 61.213  80.495  1.00 57.70 ? 177  TYR D CD1 1 
ATOM   9012  C  CD2 . TYR D 1 177 ? -72.217 62.630  82.391  1.00 60.82 ? 177  TYR D CD2 1 
ATOM   9013  C  CE1 . TYR D 1 177 ? -71.859 62.294  79.682  1.00 62.05 ? 177  TYR D CE1 1 
ATOM   9014  C  CE2 . TYR D 1 177 ? -71.915 63.728  81.585  1.00 64.39 ? 177  TYR D CE2 1 
ATOM   9015  C  CZ  . TYR D 1 177 ? -71.735 63.548  80.229  1.00 63.80 ? 177  TYR D CZ  1 
ATOM   9016  O  OH  . TYR D 1 177 ? -71.428 64.624  79.422  1.00 67.96 ? 177  TYR D OH  1 
ATOM   9017  N  N   . ARG D 1 178 ? -74.090 58.130  84.381  1.00 45.45 ? 178  ARG D N   1 
ATOM   9018  C  CA  . ARG D 1 178 ? -74.097 56.980  85.258  1.00 52.25 ? 178  ARG D CA  1 
ATOM   9019  C  C   . ARG D 1 178 ? -75.073 55.923  84.741  1.00 53.40 ? 178  ARG D C   1 
ATOM   9020  O  O   . ARG D 1 178 ? -74.819 54.719  84.847  1.00 56.73 ? 178  ARG D O   1 
ATOM   9021  C  CB  . ARG D 1 178 ? -74.512 57.423  86.664  1.00 55.50 ? 178  ARG D CB  1 
ATOM   9022  C  CG  . ARG D 1 178 ? -74.376 56.373  87.735  1.00 60.82 ? 178  ARG D CG  1 
ATOM   9023  C  CD  . ARG D 1 178 ? -75.079 56.849  88.996  1.00 72.44 ? 178  ARG D CD  1 
ATOM   9024  N  NE  . ARG D 1 178 ? -75.061 55.857  90.071  1.00 75.38 ? 178  ARG D NE  1 
ATOM   9025  C  CZ  . ARG D 1 178 ? -73.962 55.435  90.694  1.00 78.74 ? 178  ARG D CZ  1 
ATOM   9026  N  NH1 . ARG D 1 178 ? -72.749 55.910  90.358  1.00 78.23 ? 178  ARG D NH1 1 
ATOM   9027  N  NH2 . ARG D 1 178 ? -74.087 54.539  91.669  1.00 77.92 ? 178  ARG D NH2 1 
ATOM   9028  N  N   . SER D 1 179 ? -76.200 56.372  84.197  1.00 51.58 ? 179  SER D N   1 
ATOM   9029  C  CA  . SER D 1 179 ? -77.199 55.459  83.665  1.00 50.26 ? 179  SER D CA  1 
ATOM   9030  C  C   . SER D 1 179 ? -76.599 54.669  82.499  1.00 49.91 ? 179  SER D C   1 
ATOM   9031  O  O   . SER D 1 179 ? -76.699 53.429  82.438  1.00 50.75 ? 179  SER D O   1 
ATOM   9032  C  CB  . SER D 1 179 ? -78.390 56.243  83.156  1.00 51.40 ? 179  SER D CB  1 
ATOM   9033  O  OG  . SER D 1 179 ? -78.825 57.169  84.123  1.00 65.18 ? 179  SER D OG  1 
ATOM   9034  N  N   . LEU D 1 180 ? -75.989 55.406  81.573  1.00 43.92 ? 180  LEU D N   1 
ATOM   9035  C  CA  . LEU D 1 180 ? -75.364 54.827  80.402  1.00 41.50 ? 180  LEU D CA  1 
ATOM   9036  C  C   . LEU D 1 180 ? -74.329 53.769  80.789  1.00 43.33 ? 180  LEU D C   1 
ATOM   9037  O  O   . LEU D 1 180 ? -74.387 52.637  80.311  1.00 42.73 ? 180  LEU D O   1 
ATOM   9038  C  CB  . LEU D 1 180 ? -74.671 55.916  79.579  1.00 39.57 ? 180  LEU D CB  1 
ATOM   9039  C  CG  . LEU D 1 180 ? -74.501 55.675  78.080  1.00 40.68 ? 180  LEU D CG  1 
ATOM   9040  C  CD1 . LEU D 1 180 ? -73.208 56.324  77.637  1.00 44.64 ? 180  LEU D CD1 1 
ATOM   9041  C  CD2 . LEU D 1 180 ? -74.483 54.198  77.760  1.00 38.73 ? 180  LEU D CD2 1 
ATOM   9042  N  N   . PHE D 1 181 ? -73.388 54.133  81.658  1.00 40.72 ? 181  PHE D N   1 
ATOM   9043  C  CA  . PHE D 1 181 ? -72.348 53.200  82.045  1.00 38.13 ? 181  PHE D CA  1 
ATOM   9044  C  C   . PHE D 1 181 ? -72.934 52.016  82.781  1.00 39.06 ? 181  PHE D C   1 
ATOM   9045  O  O   . PHE D 1 181 ? -72.574 50.867  82.517  1.00 43.70 ? 181  PHE D O   1 
ATOM   9046  C  CB  . PHE D 1 181 ? -71.293 53.886  82.929  1.00 35.51 ? 181  PHE D CB  1 
ATOM   9047  C  CG  . PHE D 1 181 ? -70.599 55.058  82.269  1.00 30.85 ? 181  PHE D CG  1 
ATOM   9048  C  CD1 . PHE D 1 181 ? -70.322 55.041  80.904  1.00 30.00 ? 181  PHE D CD1 1 
ATOM   9049  C  CD2 . PHE D 1 181 ? -70.184 56.157  83.031  1.00 27.12 ? 181  PHE D CD2 1 
ATOM   9050  C  CE1 . PHE D 1 181 ? -69.640 56.099  80.295  1.00 29.11 ? 181  PHE D CE1 1 
ATOM   9051  C  CE2 . PHE D 1 181 ? -69.512 57.213  82.458  1.00 31.45 ? 181  PHE D CE2 1 
ATOM   9052  C  CZ  . PHE D 1 181 ? -69.229 57.193  81.075  1.00 33.34 ? 181  PHE D CZ  1 
ATOM   9053  N  N   . GLY D 1 182 ? -73.840 52.284  83.707  1.00 38.29 ? 182  GLY D N   1 
ATOM   9054  C  CA  . GLY D 1 182 ? -74.419 51.189  84.461  1.00 40.55 ? 182  GLY D CA  1 
ATOM   9055  C  C   . GLY D 1 182 ? -75.046 50.156  83.546  1.00 42.75 ? 182  GLY D C   1 
ATOM   9056  O  O   . GLY D 1 182 ? -74.886 48.937  83.736  1.00 40.29 ? 182  GLY D O   1 
ATOM   9057  N  N   . GLN D 1 183 ? -75.755 50.656  82.534  1.00 41.73 ? 183  GLN D N   1 
ATOM   9058  C  CA  . GLN D 1 183 ? -76.440 49.796  81.588  1.00 43.50 ? 183  GLN D CA  1 
ATOM   9059  C  C   . GLN D 1 183 ? -75.427 48.902  80.848  1.00 45.08 ? 183  GLN D C   1 
ATOM   9060  O  O   . GLN D 1 183 ? -75.503 47.666  80.905  1.00 44.91 ? 183  GLN D O   1 
ATOM   9061  C  CB  . GLN D 1 183 ? -77.243 50.676  80.627  1.00 49.91 ? 183  GLN D CB  1 
ATOM   9062  C  CG  . GLN D 1 183 ? -78.176 49.930  79.673  1.00 61.26 ? 183  GLN D CG  1 
ATOM   9063  C  CD  . GLN D 1 183 ? -79.138 48.997  80.409  1.00 70.51 ? 183  GLN D CD  1 
ATOM   9064  O  OE1 . GLN D 1 183 ? -79.947 49.443  81.242  1.00 73.32 ? 183  GLN D OE1 1 
ATOM   9065  N  NE2 . GLN D 1 183 ? -79.054 47.689  80.109  1.00 69.86 ? 183  GLN D NE2 1 
ATOM   9066  N  N   . VAL D 1 184 ? -74.466 49.524  80.171  1.00 42.93 ? 184  VAL D N   1 
ATOM   9067  C  CA  . VAL D 1 184 ? -73.450 48.786  79.454  1.00 40.31 ? 184  VAL D CA  1 
ATOM   9068  C  C   . VAL D 1 184 ? -72.758 47.789  80.374  1.00 39.32 ? 184  VAL D C   1 
ATOM   9069  O  O   . VAL D 1 184 ? -72.445 46.669  79.977  1.00 38.13 ? 184  VAL D O   1 
ATOM   9070  C  CB  . VAL D 1 184 ? -72.398 49.732  78.894  1.00 41.40 ? 184  VAL D CB  1 
ATOM   9071  C  CG1 . VAL D 1 184 ? -71.256 48.933  78.301  1.00 44.74 ? 184  VAL D CG1 1 
ATOM   9072  C  CG2 . VAL D 1 184 ? -73.022 50.623  77.844  1.00 44.38 ? 184  VAL D CG2 1 
ATOM   9073  N  N   . LEU D 1 185 ? -72.519 48.195  81.613  1.00 38.99 ? 185  LEU D N   1 
ATOM   9074  C  CA  . LEU D 1 185 ? -71.856 47.305  82.549  1.00 39.05 ? 185  LEU D CA  1 
ATOM   9075  C  C   . LEU D 1 185 ? -72.736 46.106  82.864  1.00 39.38 ? 185  LEU D C   1 
ATOM   9076  O  O   . LEU D 1 185 ? -72.250 44.989  82.964  1.00 36.08 ? 185  LEU D O   1 
ATOM   9077  C  CB  . LEU D 1 185 ? -71.490 48.068  83.825  1.00 35.12 ? 185  LEU D CB  1 
ATOM   9078  C  CG  . LEU D 1 185 ? -70.295 49.019  83.711  1.00 35.31 ? 185  LEU D CG  1 
ATOM   9079  C  CD1 . LEU D 1 185 ? -70.361 50.079  84.817  1.00 30.94 ? 185  LEU D CD1 1 
ATOM   9080  C  CD2 . LEU D 1 185 ? -68.978 48.208  83.769  1.00 29.81 ? 185  LEU D CD2 1 
ATOM   9081  N  N   . LYS D 1 186 ? -74.036 46.351  83.004  1.00 43.91 ? 186  LYS D N   1 
ATOM   9082  C  CA  . LYS D 1 186 ? -74.997 45.292  83.297  1.00 46.20 ? 186  LYS D CA  1 
ATOM   9083  C  C   . LYS D 1 186 ? -75.019 44.273  82.140  1.00 46.04 ? 186  LYS D C   1 
ATOM   9084  O  O   . LYS D 1 186 ? -74.982 43.063  82.376  1.00 43.95 ? 186  LYS D O   1 
ATOM   9085  C  CB  . LYS D 1 186 ? -76.396 45.891  83.489  1.00 46.27 ? 186  LYS D CB  1 
ATOM   9086  C  CG  . LYS D 1 186 ? -77.200 45.332  84.627  1.00 48.71 ? 186  LYS D CG  1 
ATOM   9087  C  CD  . LYS D 1 186 ? -77.352 43.829  84.556  1.00 58.87 ? 186  LYS D CD  1 
ATOM   9088  C  CE  . LYS D 1 186 ? -78.132 43.300  85.770  1.00 60.00 ? 186  LYS D CE  1 
ATOM   9089  N  NZ  . LYS D 1 186 ? -78.258 41.821  85.740  1.00 60.65 ? 186  LYS D NZ  1 
ATOM   9090  N  N   . ASP D 1 187 ? -75.068 44.760  80.898  1.00 46.18 ? 187  ASP D N   1 
ATOM   9091  C  CA  . ASP D 1 187 ? -75.102 43.858  79.739  1.00 51.14 ? 187  ASP D CA  1 
ATOM   9092  C  C   . ASP D 1 187 ? -73.892 42.961  79.738  1.00 51.18 ? 187  ASP D C   1 
ATOM   9093  O  O   . ASP D 1 187 ? -73.994 41.746  79.539  1.00 53.69 ? 187  ASP D O   1 
ATOM   9094  C  CB  . ASP D 1 187 ? -75.088 44.626  78.424  1.00 56.56 ? 187  ASP D CB  1 
ATOM   9095  C  CG  . ASP D 1 187 ? -76.345 45.437  78.204  1.00 65.55 ? 187  ASP D CG  1 
ATOM   9096  O  OD1 . ASP D 1 187 ? -77.093 45.682  79.187  1.00 64.54 ? 187  ASP D OD1 1 
ATOM   9097  O  OD2 . ASP D 1 187 ? -76.572 45.843  77.036  1.00 71.00 ? 187  ASP D OD2 1 
ATOM   9098  N  N   . ILE D 1 188 ? -72.739 43.579  79.961  1.00 47.42 ? 188  ILE D N   1 
ATOM   9099  C  CA  . ILE D 1 188 ? -71.497 42.858  79.971  1.00 42.36 ? 188  ILE D CA  1 
ATOM   9100  C  C   . ILE D 1 188 ? -71.422 41.814  81.064  1.00 44.31 ? 188  ILE D C   1 
ATOM   9101  O  O   . ILE D 1 188 ? -70.957 40.718  80.797  1.00 47.74 ? 188  ILE D O   1 
ATOM   9102  C  CB  . ILE D 1 188 ? -70.317 43.827  80.077  1.00 39.26 ? 188  ILE D CB  1 
ATOM   9103  C  CG1 . ILE D 1 188 ? -70.400 44.835  78.931  1.00 38.93 ? 188  ILE D CG1 1 
ATOM   9104  C  CG2 . ILE D 1 188 ? -69.012 43.076  80.018  1.00 27.49 ? 188  ILE D CG2 1 
ATOM   9105  C  CD1 . ILE D 1 188 ? -69.275 45.839  78.899  1.00 40.60 ? 188  ILE D CD1 1 
ATOM   9106  N  N   . VAL D 1 189 ? -71.874 42.103  82.282  1.00 42.44 ? 189  VAL D N   1 
ATOM   9107  C  CA  . VAL D 1 189 ? -71.751 41.066  83.301  1.00 44.26 ? 189  VAL D CA  1 
ATOM   9108  C  C   . VAL D 1 189 ? -72.610 39.897  82.888  1.00 45.80 ? 189  VAL D C   1 
ATOM   9109  O  O   . VAL D 1 189 ? -72.265 38.750  83.158  1.00 49.17 ? 189  VAL D O   1 
ATOM   9110  C  CB  . VAL D 1 189 ? -72.231 41.497  84.713  1.00 44.71 ? 189  VAL D CB  1 
ATOM   9111  C  CG1 . VAL D 1 189 ? -71.179 41.146  85.759  1.00 36.71 ? 189  VAL D CG1 1 
ATOM   9112  C  CG2 . VAL D 1 189 ? -72.576 42.950  84.721  1.00 47.32 ? 189  VAL D CG2 1 
ATOM   9113  N  N   . GLU D 1 190 ? -73.735 40.191  82.245  1.00 45.75 ? 190  GLU D N   1 
ATOM   9114  C  CA  . GLU D 1 190 ? -74.635 39.136  81.822  1.00 50.48 ? 190  GLU D CA  1 
ATOM   9115  C  C   . GLU D 1 190 ? -73.938 38.215  80.857  1.00 49.53 ? 190  GLU D C   1 
ATOM   9116  O  O   . GLU D 1 190 ? -74.010 36.992  81.010  1.00 48.94 ? 190  GLU D O   1 
ATOM   9117  C  CB  . GLU D 1 190 ? -75.905 39.702  81.185  1.00 54.33 ? 190  GLU D CB  1 
ATOM   9118  C  CG  . GLU D 1 190 ? -76.974 40.089  82.200  1.00 57.20 ? 190  GLU D CG  1 
ATOM   9119  C  CD  . GLU D 1 190 ? -77.232 38.979  83.213  1.00 63.04 ? 190  GLU D CD  1 
ATOM   9120  O  OE1 . GLU D 1 190 ? -77.235 37.790  82.793  1.00 65.24 ? 190  GLU D OE1 1 
ATOM   9121  O  OE2 . GLU D 1 190 ? -77.436 39.294  84.416  1.00 62.02 ? 190  GLU D OE2 1 
ATOM   9122  N  N   . LYS D 1 191 ? -73.263 38.808  79.878  1.00 48.91 ? 191  LYS D N   1 
ATOM   9123  C  CA  . LYS D 1 191 ? -72.511 38.038  78.888  1.00 50.13 ? 191  LYS D CA  1 
ATOM   9124  C  C   . LYS D 1 191 ? -71.271 37.422  79.514  1.00 48.95 ? 191  LYS D C   1 
ATOM   9125  O  O   . LYS D 1 191 ? -70.890 36.330  79.127  1.00 51.53 ? 191  LYS D O   1 
ATOM   9126  C  CB  . LYS D 1 191 ? -72.106 38.910  77.686  1.00 46.71 ? 191  LYS D CB  1 
ATOM   9127  C  CG  . LYS D 1 191 ? -73.311 39.505  76.974  1.00 49.95 ? 191  LYS D CG  1 
ATOM   9128  C  CD  . LYS D 1 191 ? -72.935 40.541  75.943  1.00 50.64 ? 191  LYS D CD  1 
ATOM   9129  C  CE  . LYS D 1 191 ? -74.175 41.244  75.435  1.00 49.40 ? 191  LYS D CE  1 
ATOM   9130  N  NZ  . LYS D 1 191 ? -73.791 42.293  74.455  1.00 56.57 ? 191  LYS D NZ  1 
ATOM   9131  N  N   . ILE D 1 192 ? -70.638 38.094  80.478  1.00 50.07 ? 192  ILE D N   1 
ATOM   9132  C  CA  . ILE D 1 192 ? -69.443 37.502  81.073  1.00 52.19 ? 192  ILE D CA  1 
ATOM   9133  C  C   . ILE D 1 192 ? -69.905 36.291  81.836  1.00 54.04 ? 192  ILE D C   1 
ATOM   9134  O  O   . ILE D 1 192 ? -69.292 35.224  81.772  1.00 55.32 ? 192  ILE D O   1 
ATOM   9135  C  CB  . ILE D 1 192 ? -68.678 38.461  82.003  1.00 47.33 ? 192  ILE D CB  1 
ATOM   9136  C  CG1 . ILE D 1 192 ? -68.055 39.583  81.167  1.00 44.75 ? 192  ILE D CG1 1 
ATOM   9137  C  CG2 . ILE D 1 192 ? -67.567 37.691  82.735  1.00 45.10 ? 192  ILE D CG2 1 
ATOM   9138  C  CD1 . ILE D 1 192 ? -67.423 40.704  81.965  1.00 37.71 ? 192  ILE D CD1 1 
ATOM   9139  N  N   . SER D 1 193 ? -70.993 36.461  82.565  1.00 56.64 ? 193  SER D N   1 
ATOM   9140  C  CA  . SER D 1 193 ? -71.571 35.334  83.272  1.00 61.25 ? 193  SER D CA  1 
ATOM   9141  C  C   . SER D 1 193 ? -72.030 34.521  82.070  1.00 61.98 ? 193  SER D C   1 
ATOM   9142  O  O   . SER D 1 193 ? -72.106 35.067  80.974  1.00 65.09 ? 193  SER D O   1 
ATOM   9143  C  CB  . SER D 1 193 ? -72.779 35.794  84.081  1.00 61.17 ? 193  SER D CB  1 
ATOM   9144  O  OG  . SER D 1 193 ? -73.278 34.724  84.857  1.00 67.90 ? 193  SER D OG  1 
ATOM   9145  N  N   . MET D 1 194 ? -72.322 33.243  82.228  1.00 60.42 ? 194  MET D N   1 
ATOM   9146  C  CA  . MET D 1 194 ? -72.777 32.459  81.066  1.00 63.47 ? 194  MET D CA  1 
ATOM   9147  C  C   . MET D 1 194 ? -71.653 32.256  80.047  1.00 59.43 ? 194  MET D C   1 
ATOM   9148  O  O   . MET D 1 194 ? -71.879 32.024  78.864  1.00 59.12 ? 194  MET D O   1 
ATOM   9149  C  CB  . MET D 1 194 ? -74.037 33.100  80.397  1.00 64.97 ? 194  MET D CB  1 
ATOM   9150  C  CG  . MET D 1 194 ? -73.824 34.021  79.186  1.00 66.27 ? 194  MET D CG  1 
ATOM   9151  S  SD  . MET D 1 194 ? -75.415 34.690  78.482  1.00 75.11 ? 194  MET D SD  1 
ATOM   9152  C  CE  . MET D 1 194 ? -75.064 34.730  76.684  1.00 67.85 ? 194  MET D CE  1 
ATOM   9153  N  N   . LYS D 1 195 ? -70.435 32.369  80.547  1.00 57.23 ? 195  LYS D N   1 
ATOM   9154  C  CA  . LYS D 1 195 ? -69.222 32.153  79.783  1.00 54.93 ? 195  LYS D CA  1 
ATOM   9155  C  C   . LYS D 1 195 ? -68.412 31.484  80.887  1.00 54.67 ? 195  LYS D C   1 
ATOM   9156  O  O   . LYS D 1 195 ? -67.263 31.087  80.714  1.00 52.00 ? 195  LYS D O   1 
ATOM   9157  C  CB  . LYS D 1 195 ? -68.599 33.482  79.327  1.00 56.99 ? 195  LYS D CB  1 
ATOM   9158  C  CG  . LYS D 1 195 ? -68.936 33.896  77.872  1.00 57.82 ? 195  LYS D CG  1 
ATOM   9159  C  CD  . LYS D 1 195 ? -68.256 32.980  76.854  1.00 58.86 ? 195  LYS D CD  1 
ATOM   9160  C  CE  . LYS D 1 195 ? -68.948 32.959  75.464  1.00 59.32 ? 195  LYS D CE  1 
ATOM   9161  N  NZ  . LYS D 1 195 ? -68.432 33.942  74.438  1.00 61.62 ? 195  LYS D NZ  1 
ATOM   9162  N  N   . ILE D 1 196 ? -69.071 31.360  82.039  1.00 54.18 ? 196  ILE D N   1 
ATOM   9163  C  CA  . ILE D 1 196 ? -68.504 30.726  83.228  1.00 55.46 ? 196  ILE D CA  1 
ATOM   9164  C  C   . ILE D 1 196 ? -68.874 29.242  83.173  1.00 56.96 ? 196  ILE D C   1 
ATOM   9165  O  O   . ILE D 1 196 ? -70.055 28.897  83.249  1.00 59.04 ? 196  ILE D O   1 
ATOM   9166  C  CB  . ILE D 1 196 ? -69.125 31.310  84.532  1.00 54.47 ? 196  ILE D CB  1 
ATOM   9167  C  CG1 . ILE D 1 196 ? -68.835 32.803  84.659  1.00 54.43 ? 196  ILE D CG1 1 
ATOM   9168  C  CG2 . ILE D 1 196 ? -68.608 30.566  85.731  1.00 51.97 ? 196  ILE D CG2 1 
ATOM   9169  C  CD1 . ILE D 1 196 ? -69.447 33.440  85.885  1.00 49.14 ? 196  ILE D CD1 1 
ATOM   9170  N  N   . LYS D 1 197 ? -67.881 28.374  83.026  1.00 58.25 ? 197  LYS D N   1 
ATOM   9171  C  CA  . LYS D 1 197 ? -68.123 26.936  82.980  1.00 61.08 ? 197  LYS D CA  1 
ATOM   9172  C  C   . LYS D 1 197 ? -68.587 26.559  84.370  1.00 62.68 ? 197  LYS D C   1 
ATOM   9173  O  O   . LYS D 1 197 ? -68.668 27.415  85.248  1.00 64.14 ? 197  LYS D O   1 
ATOM   9174  C  CB  . LYS D 1 197 ? -66.830 26.164  82.680  1.00 63.50 ? 197  LYS D CB  1 
ATOM   9175  C  CG  . LYS D 1 197 ? -66.367 26.138  81.239  1.00 66.96 ? 197  LYS D CG  1 
ATOM   9176  C  CD  . LYS D 1 197 ? -66.114 27.516  80.692  1.00 72.53 ? 197  LYS D CD  1 
ATOM   9177  C  CE  . LYS D 1 197 ? -67.237 27.958  79.750  1.00 75.99 ? 197  LYS D CE  1 
ATOM   9178  N  NZ  . LYS D 1 197 ? -67.326 27.103  78.530  1.00 80.01 ? 197  LYS D NZ  1 
ATOM   9179  N  N   . ASP D 1 198 ? -68.888 25.281  84.577  1.00 64.27 ? 198  ASP D N   1 
ATOM   9180  C  CA  . ASP D 1 198 ? -69.302 24.818  85.893  1.00 63.18 ? 198  ASP D CA  1 
ATOM   9181  C  C   . ASP D 1 198 ? -68.087 24.573  86.754  1.00 59.67 ? 198  ASP D C   1 
ATOM   9182  O  O   . ASP D 1 198 ? -68.161 24.698  87.966  1.00 58.63 ? 198  ASP D O   1 
ATOM   9183  C  CB  . ASP D 1 198 ? -70.085 23.520  85.799  1.00 70.98 ? 198  ASP D CB  1 
ATOM   9184  C  CG  . ASP D 1 198 ? -71.453 23.717  85.214  1.00 77.60 ? 198  ASP D CG  1 
ATOM   9185  O  OD1 . ASP D 1 198 ? -71.540 23.920  83.978  1.00 81.44 ? 198  ASP D OD1 1 
ATOM   9186  O  OD2 . ASP D 1 198 ? -72.434 23.676  85.998  1.00 79.35 ? 198  ASP D OD2 1 
ATOM   9187  N  N   . ASN D 1 199 ? -66.967 24.224  86.132  1.00 56.73 ? 199  ASN D N   1 
ATOM   9188  C  CA  . ASN D 1 199 ? -65.746 23.963  86.885  1.00 57.84 ? 199  ASN D CA  1 
ATOM   9189  C  C   . ASN D 1 199 ? -65.125 25.228  87.506  1.00 57.34 ? 199  ASN D C   1 
ATOM   9190  O  O   . ASN D 1 199 ? -64.169 25.125  88.270  1.00 56.87 ? 199  ASN D O   1 
ATOM   9191  C  CB  . ASN D 1 199 ? -64.723 23.282  85.986  1.00 56.82 ? 199  ASN D CB  1 
ATOM   9192  C  CG  . ASN D 1 199 ? -64.197 24.207  84.924  1.00 60.53 ? 199  ASN D CG  1 
ATOM   9193  O  OD1 . ASN D 1 199 ? -64.926 25.070  84.421  1.00 59.19 ? 199  ASN D OD1 1 
ATOM   9194  N  ND2 . ASN D 1 199 ? -62.928 24.040  84.569  1.00 60.33 ? 199  ASN D ND2 1 
ATOM   9195  N  N   . GLY D 1 200 ? -65.667 26.403  87.176  1.00 56.05 ? 200  GLY D N   1 
ATOM   9196  C  CA  . GLY D 1 200 ? -65.153 27.649  87.728  1.00 55.91 ? 200  GLY D CA  1 
ATOM   9197  C  C   . GLY D 1 200 ? -64.463 28.553  86.710  1.00 55.66 ? 200  GLY D C   1 
ATOM   9198  O  O   . GLY D 1 200 ? -64.313 29.756  86.926  1.00 53.74 ? 200  GLY D O   1 
ATOM   9199  N  N   . ILE D 1 201 ? -64.048 27.970  85.595  1.00 53.97 ? 201  ILE D N   1 
ATOM   9200  C  CA  . ILE D 1 201 ? -63.358 28.702  84.542  1.00 53.43 ? 201  ILE D CA  1 
ATOM   9201  C  C   . ILE D 1 201 ? -64.280 29.681  83.828  1.00 51.93 ? 201  ILE D C   1 
ATOM   9202  O  O   . ILE D 1 201 ? -65.466 29.408  83.663  1.00 50.90 ? 201  ILE D O   1 
ATOM   9203  C  CB  . ILE D 1 201 ? -62.763 27.702  83.509  1.00 53.94 ? 201  ILE D CB  1 
ATOM   9204  C  CG1 . ILE D 1 201 ? -61.505 27.075  84.092  1.00 52.06 ? 201  ILE D CG1 1 
ATOM   9205  C  CG2 . ILE D 1 201 ? -62.518 28.379  82.145  1.00 50.86 ? 201  ILE D CG2 1 
ATOM   9206  C  CD1 . ILE D 1 201 ? -60.992 25.928  83.252  1.00 60.36 ? 201  ILE D CD1 1 
ATOM   9207  N  N   . ILE D 1 202 ? -63.728 30.813  83.395  1.00 48.28 ? 202  ILE D N   1 
ATOM   9208  C  CA  . ILE D 1 202 ? -64.514 31.813  82.682  1.00 46.83 ? 202  ILE D CA  1 
ATOM   9209  C  C   . ILE D 1 202 ? -63.891 32.014  81.309  1.00 48.01 ? 202  ILE D C   1 
ATOM   9210  O  O   . ILE D 1 202 ? -62.803 32.587  81.194  1.00 51.18 ? 202  ILE D O   1 
ATOM   9211  C  CB  . ILE D 1 202 ? -64.503 33.161  83.437  1.00 48.64 ? 202  ILE D CB  1 
ATOM   9212  C  CG1 . ILE D 1 202 ? -64.804 32.933  84.933  1.00 47.09 ? 202  ILE D CG1 1 
ATOM   9213  C  CG2 . ILE D 1 202 ? -65.496 34.121  82.784  1.00 44.76 ? 202  ILE D CG2 1 
ATOM   9214  C  CD1 . ILE D 1 202 ? -64.766 34.196  85.791  1.00 45.56 ? 202  ILE D CD1 1 
ATOM   9215  N  N   . GLY D 1 203 ? -64.576 31.563  80.265  1.00 47.84 ? 203  GLY D N   1 
ATOM   9216  C  CA  . GLY D 1 203 ? -64.036 31.684  78.915  1.00 47.18 ? 203  GLY D CA  1 
ATOM   9217  C  C   . GLY D 1 203 ? -63.087 30.511  78.755  1.00 48.82 ? 203  GLY D C   1 
ATOM   9218  O  O   . GLY D 1 203 ? -63.460 29.453  78.261  1.00 52.17 ? 203  GLY D O   1 
ATOM   9219  N  N   . ASP D 1 204 ? -61.841 30.702  79.159  1.00 48.87 ? 204  ASP D N   1 
ATOM   9220  C  CA  . ASP D 1 204 ? -60.870 29.628  79.138  1.00 50.76 ? 204  ASP D CA  1 
ATOM   9221  C  C   . ASP D 1 204 ? -59.920 29.948  80.287  1.00 52.12 ? 204  ASP D C   1 
ATOM   9222  O  O   . ASP D 1 204 ? -60.078 30.995  80.939  1.00 50.70 ? 204  ASP D O   1 
ATOM   9223  C  CB  . ASP D 1 204 ? -60.191 29.502  77.764  1.00 51.78 ? 204  ASP D CB  1 
ATOM   9224  C  CG  . ASP D 1 204 ? -59.000 30.421  77.579  1.00 59.11 ? 204  ASP D CG  1 
ATOM   9225  O  OD1 . ASP D 1 204 ? -58.698 31.256  78.458  1.00 61.84 ? 204  ASP D OD1 1 
ATOM   9226  O  OD2 . ASP D 1 204 ? -58.349 30.300  76.513  1.00 61.88 ? 204  ASP D OD2 1 
ATOM   9227  N  N   . ILE D 1 205 ? -58.965 29.068  80.577  1.00 51.96 ? 205  ILE D N   1 
ATOM   9228  C  CA  . ILE D 1 205 ? -58.082 29.344  81.702  1.00 53.20 ? 205  ILE D CA  1 
ATOM   9229  C  C   . ILE D 1 205 ? -57.290 30.637  81.587  1.00 49.66 ? 205  ILE D C   1 
ATOM   9230  O  O   . ILE D 1 205 ? -56.987 31.280  82.578  1.00 50.67 ? 205  ILE D O   1 
ATOM   9231  C  CB  . ILE D 1 205 ? -57.119 28.167  81.961  1.00 55.07 ? 205  ILE D CB  1 
ATOM   9232  C  CG1 . ILE D 1 205 ? -56.720 27.510  80.644  1.00 58.34 ? 205  ILE D CG1 1 
ATOM   9233  C  CG2 . ILE D 1 205 ? -57.801 27.134  82.841  1.00 59.76 ? 205  ILE D CG2 1 
ATOM   9234  C  CD1 . ILE D 1 205 ? -56.149 26.067  80.797  1.00 61.61 ? 205  ILE D CD1 1 
ATOM   9235  N  N   . TYR D 1 206 ? -56.999 31.058  80.373  1.00 47.58 ? 206  TYR D N   1 
ATOM   9236  C  CA  . TYR D 1 206 ? -56.185 32.246  80.216  1.00 44.92 ? 206  TYR D CA  1 
ATOM   9237  C  C   . TYR D 1 206 ? -56.893 33.578  80.132  1.00 42.64 ? 206  TYR D C   1 
ATOM   9238  O  O   . TYR D 1 206 ? -56.258 34.609  79.944  1.00 42.67 ? 206  TYR D O   1 
ATOM   9239  C  CB  . TYR D 1 206 ? -55.236 32.014  79.046  1.00 42.25 ? 206  TYR D CB  1 
ATOM   9240  C  CG  . TYR D 1 206 ? -54.452 30.739  79.298  1.00 44.95 ? 206  TYR D CG  1 
ATOM   9241  C  CD1 . TYR D 1 206 ? -53.455 30.693  80.277  1.00 43.75 ? 206  TYR D CD1 1 
ATOM   9242  C  CD2 . TYR D 1 206 ? -54.759 29.554  78.615  1.00 44.37 ? 206  TYR D CD2 1 
ATOM   9243  C  CE1 . TYR D 1 206 ? -52.789 29.507  80.565  1.00 42.45 ? 206  TYR D CE1 1 
ATOM   9244  C  CE2 . TYR D 1 206 ? -54.096 28.364  78.898  1.00 41.49 ? 206  TYR D CE2 1 
ATOM   9245  C  CZ  . TYR D 1 206 ? -53.113 28.350  79.869  1.00 43.63 ? 206  TYR D CZ  1 
ATOM   9246  O  OH  . TYR D 1 206 ? -52.435 27.178  80.132  1.00 47.65 ? 206  TYR D OH  1 
ATOM   9247  N  N   . SER D 1 207 ? -58.204 33.570  80.304  1.00 39.62 ? 207  SER D N   1 
ATOM   9248  C  CA  . SER D 1 207 ? -58.923 34.816  80.277  1.00 38.18 ? 207  SER D CA  1 
ATOM   9249  C  C   . SER D 1 207 ? -59.709 34.918  81.582  1.00 38.55 ? 207  SER D C   1 
ATOM   9250  O  O   . SER D 1 207 ? -60.459 35.880  81.805  1.00 39.90 ? 207  SER D O   1 
ATOM   9251  C  CB  . SER D 1 207 ? -59.842 34.882  79.057  1.00 38.87 ? 207  SER D CB  1 
ATOM   9252  O  OG  . SER D 1 207 ? -60.874 33.947  79.178  1.00 44.02 ? 207  SER D OG  1 
ATOM   9253  N  N   . THR D 1 208 ? -59.502 33.941  82.463  1.00 35.80 ? 208  THR D N   1 
ATOM   9254  C  CA  . THR D 1 208 ? -60.206 33.915  83.737  1.00 36.28 ? 208  THR D CA  1 
ATOM   9255  C  C   . THR D 1 208 ? -59.721 35.019  84.668  1.00 38.43 ? 208  THR D C   1 
ATOM   9256  O  O   . THR D 1 208 ? -60.518 35.598  85.416  1.00 41.20 ? 208  THR D O   1 
ATOM   9257  C  CB  . THR D 1 208 ? -60.042 32.556  84.442  1.00 35.68 ? 208  THR D CB  1 
ATOM   9258  O  OG1 . THR D 1 208 ? -60.761 31.557  83.715  1.00 37.92 ? 208  THR D OG1 1 
ATOM   9259  C  CG2 . THR D 1 208 ? -60.583 32.614  85.868  1.00 38.09 ? 208  THR D CG2 1 
ATOM   9260  N  N   . GLY D 1 209 ? -58.420 35.300  84.632  1.00 36.52 ? 209  GLY D N   1 
ATOM   9261  C  CA  . GLY D 1 209 ? -57.859 36.345  85.476  1.00 35.78 ? 209  GLY D CA  1 
ATOM   9262  C  C   . GLY D 1 209 ? -58.575 37.675  85.284  1.00 37.50 ? 209  GLY D C   1 
ATOM   9263  O  O   . GLY D 1 209 ? -59.124 38.222  86.243  1.00 38.87 ? 209  GLY D O   1 
ATOM   9264  N  N   . LEU D 1 210 ? -58.593 38.191  84.054  1.00 36.22 ? 210  LEU D N   1 
ATOM   9265  C  CA  . LEU D 1 210 ? -59.257 39.448  83.786  1.00 36.52 ? 210  LEU D CA  1 
ATOM   9266  C  C   . LEU D 1 210 ? -60.740 39.318  84.041  1.00 39.50 ? 210  LEU D C   1 
ATOM   9267  O  O   . LEU D 1 210 ? -61.369 40.257  84.522  1.00 42.76 ? 210  LEU D O   1 
ATOM   9268  C  CB  . LEU D 1 210 ? -59.004 39.928  82.350  1.00 39.77 ? 210  LEU D CB  1 
ATOM   9269  C  CG  . LEU D 1 210 ? -57.525 40.168  81.962  1.00 43.65 ? 210  LEU D CG  1 
ATOM   9270  C  CD1 . LEU D 1 210 ? -57.435 40.890  80.626  1.00 43.09 ? 210  LEU D CD1 1 
ATOM   9271  C  CD2 . LEU D 1 210 ? -56.813 40.986  83.030  1.00 42.36 ? 210  LEU D CD2 1 
ATOM   9272  N  N   . ALA D 1 211 ? -61.327 38.167  83.743  1.00 40.00 ? 211  ALA D N   1 
ATOM   9273  C  CA  . ALA D 1 211 ? -62.754 38.043  84.022  1.00 37.32 ? 211  ALA D CA  1 
ATOM   9274  C  C   . ALA D 1 211 ? -62.965 38.195  85.538  1.00 37.53 ? 211  ALA D C   1 
ATOM   9275  O  O   . ALA D 1 211 ? -63.897 38.906  85.976  1.00 36.58 ? 211  ALA D O   1 
ATOM   9276  C  CB  . ALA D 1 211 ? -63.283 36.708  83.551  1.00 38.48 ? 211  ALA D CB  1 
ATOM   9277  N  N   . MET D 1 212 ? -62.102 37.553  86.334  1.00 32.95 ? 212  MET D N   1 
ATOM   9278  C  CA  . MET D 1 212 ? -62.235 37.631  87.792  1.00 38.29 ? 212  MET D CA  1 
ATOM   9279  C  C   . MET D 1 212 ? -62.175 39.084  88.271  1.00 42.00 ? 212  MET D C   1 
ATOM   9280  O  O   . MET D 1 212 ? -62.943 39.504  89.157  1.00 39.08 ? 212  MET D O   1 
ATOM   9281  C  CB  . MET D 1 212 ? -61.138 36.848  88.491  1.00 42.83 ? 212  MET D CB  1 
ATOM   9282  C  CG  . MET D 1 212 ? -61.288 35.345  88.437  1.00 49.70 ? 212  MET D CG  1 
ATOM   9283  S  SD  . MET D 1 212 ? -59.898 34.579  89.287  1.00 51.67 ? 212  MET D SD  1 
ATOM   9284  C  CE  . MET D 1 212 ? -60.488 34.778  91.005  1.00 54.77 ? 212  MET D CE  1 
ATOM   9285  N  N   . GLN D 1 213 ? -61.259 39.850  87.685  1.00 37.35 ? 213  GLN D N   1 
ATOM   9286  C  CA  . GLN D 1 213 ? -61.147 41.239  88.049  1.00 34.39 ? 213  GLN D CA  1 
ATOM   9287  C  C   . GLN D 1 213 ? -62.461 41.970  87.755  1.00 33.10 ? 213  GLN D C   1 
ATOM   9288  O  O   . GLN D 1 213 ? -63.036 42.662  88.602  1.00 33.53 ? 213  GLN D O   1 
ATOM   9289  C  CB  . GLN D 1 213 ? -60.016 41.888  87.265  1.00 34.21 ? 213  GLN D CB  1 
ATOM   9290  C  CG  . GLN D 1 213 ? -58.629 41.435  87.695  1.00 36.38 ? 213  GLN D CG  1 
ATOM   9291  C  CD  . GLN D 1 213 ? -57.559 42.331  87.140  1.00 36.39 ? 213  GLN D CD  1 
ATOM   9292  O  OE1 . GLN D 1 213 ? -56.449 41.900  86.873  1.00 42.94 ? 213  GLN D OE1 1 
ATOM   9293  N  NE2 . GLN D 1 213 ? -57.887 43.598  86.971  1.00 40.63 ? 213  GLN D NE2 1 
ATOM   9294  N  N   . ALA D 1 214 ? -62.944 41.799  86.541  1.00 31.48 ? 214  ALA D N   1 
ATOM   9295  C  CA  . ALA D 1 214 ? -64.151 42.482  86.144  1.00 32.31 ? 214  ALA D CA  1 
ATOM   9296  C  C   . ALA D 1 214 ? -65.300 42.130  87.057  1.00 34.63 ? 214  ALA D C   1 
ATOM   9297  O  O   . ALA D 1 214 ? -66.003 43.024  87.535  1.00 36.04 ? 214  ALA D O   1 
ATOM   9298  C  CB  . ALA D 1 214 ? -64.488 42.172  84.675  1.00 27.65 ? 214  ALA D CB  1 
ATOM   9299  N  N   . LEU D 1 215 ? -65.476 40.838  87.322  1.00 37.69 ? 215  LEU D N   1 
ATOM   9300  C  CA  . LEU D 1 215 ? -66.569 40.396  88.180  1.00 38.21 ? 215  LEU D CA  1 
ATOM   9301  C  C   . LEU D 1 215 ? -66.479 40.953  89.597  1.00 37.49 ? 215  LEU D C   1 
ATOM   9302  O  O   . LEU D 1 215 ? -67.490 41.297  90.207  1.00 35.40 ? 215  LEU D O   1 
ATOM   9303  C  CB  . LEU D 1 215 ? -66.613 38.872  88.216  1.00 40.02 ? 215  LEU D CB  1 
ATOM   9304  C  CG  . LEU D 1 215 ? -67.165 38.227  86.946  1.00 41.43 ? 215  LEU D CG  1 
ATOM   9305  C  CD1 . LEU D 1 215 ? -67.156 36.707  87.105  1.00 39.99 ? 215  LEU D CD1 1 
ATOM   9306  C  CD2 . LEU D 1 215 ? -68.575 38.753  86.677  1.00 40.62 ? 215  LEU D CD2 1 
ATOM   9307  N  N   . SER D 1 216 ? -65.261 41.046  90.109  1.00 37.56 ? 216  SER D N   1 
ATOM   9308  C  CA  . SER D 1 216 ? -65.028 41.563  91.445  1.00 41.26 ? 216  SER D CA  1 
ATOM   9309  C  C   . SER D 1 216 ? -65.318 43.041  91.553  1.00 42.81 ? 216  SER D C   1 
ATOM   9310  O  O   . SER D 1 216 ? -65.578 43.548  92.631  1.00 45.86 ? 216  SER D O   1 
ATOM   9311  C  CB  . SER D 1 216 ? -63.573 41.384  91.830  1.00 42.22 ? 216  SER D CB  1 
ATOM   9312  O  OG  . SER D 1 216 ? -63.200 40.031  91.706  1.00 56.80 ? 216  SER D OG  1 
ATOM   9313  N  N   . VAL D 1 217 ? -65.297 43.729  90.428  1.00 42.28 ? 217  VAL D N   1 
ATOM   9314  C  CA  . VAL D 1 217 ? -65.438 45.167  90.445  1.00 41.86 ? 217  VAL D CA  1 
ATOM   9315  C  C   . VAL D 1 217 ? -66.701 45.840  89.899  1.00 43.10 ? 217  VAL D C   1 
ATOM   9316  O  O   . VAL D 1 217 ? -66.944 46.985  90.239  1.00 43.44 ? 217  VAL D O   1 
ATOM   9317  C  CB  . VAL D 1 217 ? -64.164 45.744  89.761  1.00 40.87 ? 217  VAL D CB  1 
ATOM   9318  C  CG1 . VAL D 1 217 ? -64.466 46.984  88.998  1.00 42.56 ? 217  VAL D CG1 1 
ATOM   9319  C  CG2 . VAL D 1 217 ? -63.100 45.974  90.802  1.00 39.49 ? 217  VAL D CG2 1 
ATOM   9320  N  N   . THR D 1 218 ? -67.497 45.161  89.074  1.00 45.15 ? 218  THR D N   1 
ATOM   9321  C  CA  . THR D 1 218 ? -68.704 45.783  88.495  1.00 49.21 ? 218  THR D CA  1 
ATOM   9322  C  C   . THR D 1 218 ? -69.689 46.213  89.535  1.00 49.49 ? 218  THR D C   1 
ATOM   9323  O  O   . THR D 1 218 ? -69.961 45.472  90.461  1.00 50.92 ? 218  THR D O   1 
ATOM   9324  C  CB  . THR D 1 218 ? -69.520 44.834  87.599  1.00 50.74 ? 218  THR D CB  1 
ATOM   9325  O  OG1 . THR D 1 218 ? -68.777 43.641  87.357  1.00 57.07 ? 218  THR D OG1 1 
ATOM   9326  C  CG2 . THR D 1 218 ? -69.872 45.506  86.275  1.00 51.14 ? 218  THR D CG2 1 
ATOM   9327  N  N   . PRO D 1 219 ? -70.276 47.396  89.372  1.00 51.20 ? 219  PRO D N   1 
ATOM   9328  C  CA  . PRO D 1 219 ? -71.252 47.867  90.350  1.00 55.23 ? 219  PRO D CA  1 
ATOM   9329  C  C   . PRO D 1 219 ? -72.408 46.883  90.553  1.00 60.74 ? 219  PRO D C   1 
ATOM   9330  O  O   . PRO D 1 219 ? -72.760 46.559  91.702  1.00 63.26 ? 219  PRO D O   1 
ATOM   9331  C  CB  . PRO D 1 219 ? -71.697 49.215  89.785  1.00 54.21 ? 219  PRO D CB  1 
ATOM   9332  C  CG  . PRO D 1 219 ? -71.405 49.100  88.317  1.00 56.66 ? 219  PRO D CG  1 
ATOM   9333  C  CD  . PRO D 1 219 ? -70.093 48.368  88.287  1.00 52.06 ? 219  PRO D CD  1 
ATOM   9334  N  N   . GLU D 1 220 ? -73.002 46.390  89.470  1.00 64.95 ? 220  GLU D N   1 
ATOM   9335  C  CA  . GLU D 1 220 ? -74.104 45.438  89.641  1.00 71.59 ? 220  GLU D CA  1 
ATOM   9336  C  C   . GLU D 1 220 ? -73.816 44.053  89.054  1.00 74.88 ? 220  GLU D C   1 
ATOM   9337  O  O   . GLU D 1 220 ? -73.504 43.917  87.865  1.00 72.41 ? 220  GLU D O   1 
ATOM   9338  C  CB  . GLU D 1 220 ? -75.401 45.984  89.050  1.00 72.04 ? 220  GLU D CB  1 
ATOM   9339  C  CG  . GLU D 1 220 ? -76.554 45.015  89.183  1.00 76.23 ? 220  GLU D CG  1 
ATOM   9340  C  CD  . GLU D 1 220 ? -77.876 45.618  88.754  1.00 80.36 ? 220  GLU D CD  1 
ATOM   9341  O  OE1 . GLU D 1 220 ? -77.902 46.287  87.694  1.00 78.64 ? 220  GLU D OE1 1 
ATOM   9342  O  OE2 . GLU D 1 220 ? -78.885 45.413  89.472  1.00 82.94 ? 220  GLU D OE2 1 
ATOM   9343  N  N   . PRO D 1 221 ? -73.931 43.000  89.893  1.00 78.45 ? 221  PRO D N   1 
ATOM   9344  C  CA  . PRO D 1 221 ? -73.688 41.601  89.512  1.00 80.18 ? 221  PRO D CA  1 
ATOM   9345  C  C   . PRO D 1 221 ? -74.770 41.074  88.581  1.00 82.47 ? 221  PRO D C   1 
ATOM   9346  O  O   . PRO D 1 221 ? -75.791 41.733  88.383  1.00 83.29 ? 221  PRO D O   1 
ATOM   9347  C  CB  . PRO D 1 221 ? -73.676 40.878  90.857  1.00 79.20 ? 221  PRO D CB  1 
ATOM   9348  C  CG  . PRO D 1 221 ? -74.725 41.614  91.618  1.00 79.04 ? 221  PRO D CG  1 
ATOM   9349  C  CD  . PRO D 1 221 ? -74.430 43.082  91.283  1.00 78.99 ? 221  PRO D CD  1 
ATOM   9350  N  N   . SER D 1 222 ? -74.547 39.895  88.007  1.00 85.21 ? 222  SER D N   1 
ATOM   9351  C  CA  . SER D 1 222 ? -75.534 39.308  87.102  1.00 89.10 ? 222  SER D CA  1 
ATOM   9352  C  C   . SER D 1 222 ? -76.569 38.486  87.880  1.00 90.24 ? 222  SER D C   1 
ATOM   9353  O  O   . SER D 1 222 ? -76.316 38.091  89.018  1.00 89.59 ? 222  SER D O   1 
ATOM   9354  C  CB  . SER D 1 222 ? -74.838 38.444  86.037  1.00 88.81 ? 222  SER D CB  1 
ATOM   9355  O  OG  . SER D 1 222 ? -73.941 37.517  86.619  1.00 90.49 ? 222  SER D OG  1 
ATOM   9356  N  N   . LYS D 1 223 ? -77.736 38.257  87.273  1.00 92.67 ? 223  LYS D N   1 
ATOM   9357  C  CA  . LYS D 1 223 ? -78.804 37.478  87.911  1.00 95.81 ? 223  LYS D CA  1 
ATOM   9358  C  C   . LYS D 1 223 ? -78.203 36.138  88.314  1.00 96.66 ? 223  LYS D C   1 
ATOM   9359  O  O   . LYS D 1 223 ? -78.320 35.714  89.470  1.00 96.18 ? 223  LYS D O   1 
ATOM   9360  C  CB  . LYS D 1 223 ? -79.979 37.265  86.939  1.00 96.62 ? 223  LYS D CB  1 
ATOM   9361  C  CG  . LYS D 1 223 ? -81.280 36.793  87.606  1.00 98.02 ? 223  LYS D CG  1 
ATOM   9362  C  CD  . LYS D 1 223 ? -81.162 35.375  88.168  1.00 99.45 ? 223  LYS D CD  1 
ATOM   9363  C  CE  . LYS D 1 223 ? -82.456 34.900  88.834  1.00 99.45 ? 223  LYS D CE  1 
ATOM   9364  N  NZ  . LYS D 1 223 ? -82.847 35.702  90.035  1.00 99.45 ? 223  LYS D NZ  1 
ATOM   9365  N  N   . LYS D 1 224 ? -77.580 35.471  87.343  1.00 97.65 ? 224  LYS D N   1 
ATOM   9366  C  CA  . LYS D 1 224 ? -76.894 34.202  87.584  1.00 97.42 ? 224  LYS D CA  1 
ATOM   9367  C  C   . LYS D 1 224 ? -75.702 34.677  88.417  1.00 96.47 ? 224  LYS D C   1 
ATOM   9368  O  O   . LYS D 1 224 ? -74.971 35.569  87.971  1.00 96.78 ? 224  LYS D O   1 
ATOM   9369  C  CB  . LYS D 1 224 ? -76.407 33.614  86.249  1.00 98.79 ? 224  LYS D CB  1 
ATOM   9370  C  CG  . LYS D 1 224 ? -75.628 32.300  86.336  1.00 99.28 ? 224  LYS D CG  1 
ATOM   9371  C  CD  . LYS D 1 224 ? -74.973 31.966  84.986  1.00 99.00 ? 224  LYS D CD  1 
ATOM   9372  C  CE  . LYS D 1 224 ? -74.265 30.611  85.011  1.00 99.45 ? 224  LYS D CE  1 
ATOM   9373  N  NZ  . LYS D 1 224 ? -73.535 30.321  83.742  1.00 99.45 ? 224  LYS D NZ  1 
ATOM   9374  N  N   . GLU D 1 225 ? -75.479 34.125  89.605  1.00 93.48 ? 225  GLU D N   1 
ATOM   9375  C  CA  . GLU D 1 225 ? -74.361 34.647  90.361  1.00 90.85 ? 225  GLU D CA  1 
ATOM   9376  C  C   . GLU D 1 225 ? -73.062 33.866  90.363  1.00 88.17 ? 225  GLU D C   1 
ATOM   9377  O  O   . GLU D 1 225 ? -73.037 32.633  90.276  1.00 88.37 ? 225  GLU D O   1 
ATOM   9378  C  CB  . GLU D 1 225 ? -74.767 34.926  91.783  1.00 92.09 ? 225  GLU D CB  1 
ATOM   9379  C  CG  . GLU D 1 225 ? -74.069 36.147  92.302  1.00 95.68 ? 225  GLU D CG  1 
ATOM   9380  C  CD  . GLU D 1 225 ? -73.751 36.017  93.763  1.00 99.45 ? 225  GLU D CD  1 
ATOM   9381  O  OE1 . GLU D 1 225 ? -74.597 35.454  94.506  1.00 99.45 ? 225  GLU D OE1 1 
ATOM   9382  O  OE2 . GLU D 1 225 ? -72.657 36.478  94.163  1.00 99.44 ? 225  GLU D OE2 1 
ATOM   9383  N  N   . TRP D 1 226 ? -71.980 34.624  90.504  1.00 82.67 ? 226  TRP D N   1 
ATOM   9384  C  CA  . TRP D 1 226 ? -70.636 34.087  90.488  1.00 76.21 ? 226  TRP D CA  1 
ATOM   9385  C  C   . TRP D 1 226 ? -70.098 33.630  91.827  1.00 74.13 ? 226  TRP D C   1 
ATOM   9386  O  O   . TRP D 1 226 ? -70.116 34.355  92.815  1.00 73.79 ? 226  TRP D O   1 
ATOM   9387  C  CB  . TRP D 1 226 ? -69.708 35.135  89.876  1.00 74.19 ? 226  TRP D CB  1 
ATOM   9388  C  CG  . TRP D 1 226 ? -68.246 34.828  89.936  1.00 68.66 ? 226  TRP D CG  1 
ATOM   9389  C  CD1 . TRP D 1 226 ? -67.605 33.713  89.458  1.00 67.37 ? 226  TRP D CD1 1 
ATOM   9390  C  CD2 . TRP D 1 226 ? -67.233 35.687  90.442  1.00 65.27 ? 226  TRP D CD2 1 
ATOM   9391  N  NE1 . TRP D 1 226 ? -66.251 33.836  89.635  1.00 62.72 ? 226  TRP D NE1 1 
ATOM   9392  C  CE2 . TRP D 1 226 ? -65.993 35.038  90.236  1.00 63.65 ? 226  TRP D CE2 1 
ATOM   9393  C  CE3 . TRP D 1 226 ? -67.248 36.951  91.048  1.00 64.04 ? 226  TRP D CE3 1 
ATOM   9394  C  CZ2 . TRP D 1 226 ? -64.780 35.607  90.619  1.00 65.54 ? 226  TRP D CZ2 1 
ATOM   9395  C  CZ3 . TRP D 1 226 ? -66.042 37.519  91.429  1.00 64.84 ? 226  TRP D CZ3 1 
ATOM   9396  C  CH2 . TRP D 1 226 ? -64.822 36.846  91.211  1.00 64.86 ? 226  TRP D CH2 1 
ATOM   9397  N  N   . ASN D 1 227 ? -69.615 32.398  91.826  1.00 72.45 ? 227  ASN D N   1 
ATOM   9398  C  CA  . ASN D 1 227 ? -69.020 31.778  92.993  1.00 70.93 ? 227  ASN D CA  1 
ATOM   9399  C  C   . ASN D 1 227 ? -67.512 32.015  92.840  1.00 69.78 ? 227  ASN D C   1 
ATOM   9400  O  O   . ASN D 1 227 ? -66.829 31.282  92.122  1.00 68.79 ? 227  ASN D O   1 
ATOM   9401  C  CB  . ASN D 1 227 ? -69.348 30.278  92.983  1.00 69.82 ? 227  ASN D CB  1 
ATOM   9402  C  CG  . ASN D 1 227 ? -68.667 29.521  94.097  1.00 68.64 ? 227  ASN D CG  1 
ATOM   9403  O  OD1 . ASN D 1 227 ? -67.844 30.080  94.837  1.00 69.63 ? 227  ASN D OD1 1 
ATOM   9404  N  ND2 . ASN D 1 227 ? -68.995 28.235  94.223  1.00 65.04 ? 227  ASN D ND2 1 
ATOM   9405  N  N   . CYS D 1 228 ? -66.998 33.047  93.503  1.00 69.69 ? 228  CYS D N   1 
ATOM   9406  C  CA  . CYS D 1 228 ? -65.580 33.364  93.398  1.00 69.81 ? 228  CYS D CA  1 
ATOM   9407  C  C   . CYS D 1 228 ? -64.608 32.281  93.883  1.00 67.05 ? 228  CYS D C   1 
ATOM   9408  O  O   . CYS D 1 228 ? -63.647 31.984  93.179  1.00 67.86 ? 228  CYS D O   1 
ATOM   9409  C  CB  . CYS D 1 228 ? -65.273 34.699  94.086  1.00 71.92 ? 228  CYS D CB  1 
ATOM   9410  S  SG  . CYS D 1 228 ? -63.496 35.107  94.029  1.00 81.93 ? 228  CYS D SG  1 
ATOM   9411  N  N   . LYS D 1 229 ? -64.848 31.696  95.059  1.00 65.62 ? 229  LYS D N   1 
ATOM   9412  C  CA  . LYS D 1 229 ? -63.973 30.650  95.605  1.00 64.15 ? 229  LYS D CA  1 
ATOM   9413  C  C   . LYS D 1 229 ? -63.848 29.466  94.650  1.00 61.49 ? 229  LYS D C   1 
ATOM   9414  O  O   . LYS D 1 229 ? -62.793 28.845  94.530  1.00 61.36 ? 229  LYS D O   1 
ATOM   9415  C  CB  . LYS D 1 229 ? -64.496 30.131  96.947  1.00 67.17 ? 229  LYS D CB  1 
ATOM   9416  C  CG  . LYS D 1 229 ? -63.603 29.032  97.546  1.00 71.85 ? 229  LYS D CG  1 
ATOM   9417  C  CD  . LYS D 1 229 ? -64.251 28.295  98.727  1.00 72.08 ? 229  LYS D CD  1 
ATOM   9418  C  CE  . LYS D 1 229 ? -63.369 27.147  99.237  1.00 75.56 ? 229  LYS D CE  1 
ATOM   9419  N  NZ  . LYS D 1 229 ? -61.987 27.559  99.716  1.00 76.28 ? 229  LYS D NZ  1 
ATOM   9420  N  N   . LYS D 1 230 ? -64.935 29.146  93.976  1.00 57.13 ? 230  LYS D N   1 
ATOM   9421  C  CA  . LYS D 1 230 ? -64.918 28.050  93.025  1.00 56.78 ? 230  LYS D CA  1 
ATOM   9422  C  C   . LYS D 1 230 ? -63.852 28.322  91.958  1.00 55.09 ? 230  LYS D C   1 
ATOM   9423  O  O   . LYS D 1 230 ? -62.961 27.495  91.693  1.00 51.82 ? 230  LYS D O   1 
ATOM   9424  C  CB  . LYS D 1 230 ? -66.297 27.938  92.375  1.00 59.99 ? 230  LYS D CB  1 
ATOM   9425  C  CG  . LYS D 1 230 ? -66.463 26.819  91.377  1.00 62.12 ? 230  LYS D CG  1 
ATOM   9426  C  CD  . LYS D 1 230 ? -67.530 25.855  91.847  1.00 66.80 ? 230  LYS D CD  1 
ATOM   9427  C  CE  . LYS D 1 230 ? -68.244 25.178  90.680  1.00 70.17 ? 230  LYS D CE  1 
ATOM   9428  N  NZ  . LYS D 1 230 ? -69.150 24.048  91.110  1.00 73.72 ? 230  LYS D NZ  1 
ATOM   9429  N  N   . THR D 1 231 ? -63.960 29.497  91.348  1.00 52.55 ? 231  THR D N   1 
ATOM   9430  C  CA  . THR D 1 231 ? -63.039 29.898  90.303  1.00 50.11 ? 231  THR D CA  1 
ATOM   9431  C  C   . THR D 1 231 ? -61.599 29.997  90.757  1.00 49.44 ? 231  THR D C   1 
ATOM   9432  O  O   . THR D 1 231 ? -60.694 29.577  90.039  1.00 49.00 ? 231  THR D O   1 
ATOM   9433  C  CB  . THR D 1 231 ? -63.422 31.241  89.711  1.00 46.17 ? 231  THR D CB  1 
ATOM   9434  O  OG1 . THR D 1 231 ? -64.670 31.112  89.035  1.00 47.70 ? 231  THR D OG1 1 
ATOM   9435  C  CG2 . THR D 1 231 ? -62.359 31.714  88.732  1.00 46.54 ? 231  THR D CG2 1 
ATOM   9436  N  N   . THR D 1 232 ? -61.360 30.552  91.935  1.00 49.73 ? 232  THR D N   1 
ATOM   9437  C  CA  . THR D 1 232 ? -59.978 30.669  92.336  1.00 52.02 ? 232  THR D CA  1 
ATOM   9438  C  C   . THR D 1 232 ? -59.407 29.305  92.706  1.00 51.92 ? 232  THR D C   1 
ATOM   9439  O  O   . THR D 1 232 ? -58.239 29.020  92.443  1.00 51.18 ? 232  THR D O   1 
ATOM   9440  C  CB  . THR D 1 232 ? -59.798 31.758  93.437  1.00 50.65 ? 232  THR D CB  1 
ATOM   9441  O  OG1 . THR D 1 232 ? -58.871 31.306  94.433  1.00 50.93 ? 232  THR D OG1 1 
ATOM   9442  C  CG2 . THR D 1 232 ? -61.113 32.123  94.031  1.00 48.50 ? 232  THR D CG2 1 
ATOM   9443  N  N   . ASP D 1 233 ? -60.244 28.436  93.254  1.00 52.79 ? 233  ASP D N   1 
ATOM   9444  C  CA  . ASP D 1 233 ? -59.780 27.102  93.588  1.00 53.38 ? 233  ASP D CA  1 
ATOM   9445  C  C   . ASP D 1 233 ? -59.436 26.358  92.299  1.00 53.56 ? 233  ASP D C   1 
ATOM   9446  O  O   . ASP D 1 233 ? -58.390 25.711  92.195  1.00 51.91 ? 233  ASP D O   1 
ATOM   9447  C  CB  . ASP D 1 233 ? -60.852 26.345  94.368  1.00 56.12 ? 233  ASP D CB  1 
ATOM   9448  C  CG  . ASP D 1 233 ? -60.953 26.802  95.820  1.00 61.50 ? 233  ASP D CG  1 
ATOM   9449  O  OD1 . ASP D 1 233 ? -60.053 27.551  96.292  1.00 63.68 ? 233  ASP D OD1 1 
ATOM   9450  O  OD2 . ASP D 1 233 ? -61.929 26.396  96.488  1.00 62.44 ? 233  ASP D OD2 1 
ATOM   9451  N  N   . MET D 1 234 ? -60.316 26.449  91.309  1.00 54.64 ? 234  MET D N   1 
ATOM   9452  C  CA  . MET D 1 234 ? -60.051 25.799  90.032  1.00 55.75 ? 234  MET D CA  1 
ATOM   9453  C  C   . MET D 1 234 ? -58.740 26.333  89.401  1.00 55.37 ? 234  MET D C   1 
ATOM   9454  O  O   . MET D 1 234 ? -57.993 25.583  88.765  1.00 54.35 ? 234  MET D O   1 
ATOM   9455  C  CB  . MET D 1 234 ? -61.235 26.017  89.086  1.00 58.88 ? 234  MET D CB  1 
ATOM   9456  C  CG  . MET D 1 234 ? -61.203 25.141  87.833  1.00 67.72 ? 234  MET D CG  1 
ATOM   9457  S  SD  . MET D 1 234 ? -60.435 23.490  88.113  1.00 80.71 ? 234  MET D SD  1 
ATOM   9458  C  CE  . MET D 1 234 ? -61.781 22.430  88.459  1.00 79.14 ? 234  MET D CE  1 
ATOM   9459  N  N   . ILE D 1 235 ? -58.457 27.623  89.586  1.00 52.16 ? 235  ILE D N   1 
ATOM   9460  C  CA  . ILE D 1 235 ? -57.243 28.196  89.033  1.00 50.19 ? 235  ILE D CA  1 
ATOM   9461  C  C   . ILE D 1 235 ? -56.046 27.622  89.766  1.00 47.76 ? 235  ILE D C   1 
ATOM   9462  O  O   . ILE D 1 235 ? -55.017 27.362  89.155  1.00 45.88 ? 235  ILE D O   1 
ATOM   9463  C  CB  . ILE D 1 235 ? -57.246 29.773  89.115  1.00 52.34 ? 235  ILE D CB  1 
ATOM   9464  C  CG1 . ILE D 1 235 ? -58.159 30.344  88.032  1.00 49.39 ? 235  ILE D CG1 1 
ATOM   9465  C  CG2 . ILE D 1 235 ? -55.826 30.347  88.891  1.00 50.95 ? 235  ILE D CG2 1 
ATOM   9466  C  CD1 . ILE D 1 235 ? -57.699 30.004  86.606  1.00 50.28 ? 235  ILE D CD1 1 
ATOM   9467  N  N   . LEU D 1 236 ? -56.182 27.410  91.073  1.00 46.82 ? 236  LEU D N   1 
ATOM   9468  C  CA  . LEU D 1 236 ? -55.077 26.852  91.849  1.00 49.84 ? 236  LEU D CA  1 
ATOM   9469  C  C   . LEU D 1 236 ? -54.706 25.432  91.392  1.00 50.87 ? 236  LEU D C   1 
ATOM   9470  O  O   . LEU D 1 236 ? -53.513 25.083  91.340  1.00 49.87 ? 236  LEU D O   1 
ATOM   9471  C  CB  . LEU D 1 236 ? -55.401 26.875  93.352  1.00 47.74 ? 236  LEU D CB  1 
ATOM   9472  C  CG  . LEU D 1 236 ? -55.321 28.255  94.027  1.00 48.63 ? 236  LEU D CG  1 
ATOM   9473  C  CD1 . LEU D 1 236 ? -56.015 28.212  95.379  1.00 47.57 ? 236  LEU D CD1 1 
ATOM   9474  C  CD2 . LEU D 1 236 ? -53.854 28.683  94.160  1.00 45.73 ? 236  LEU D CD2 1 
ATOM   9475  N  N   . ASN D 1 237 ? -55.718 24.627  91.057  1.00 50.45 ? 237  ASN D N   1 
ATOM   9476  C  CA  . ASN D 1 237 ? -55.485 23.263  90.583  1.00 54.07 ? 237  ASN D CA  1 
ATOM   9477  C  C   . ASN D 1 237 ? -54.846 23.355  89.221  1.00 52.54 ? 237  ASN D C   1 
ATOM   9478  O  O   . ASN D 1 237 ? -53.959 22.578  88.883  1.00 51.54 ? 237  ASN D O   1 
ATOM   9479  C  CB  . ASN D 1 237 ? -56.793 22.465  90.462  1.00 59.27 ? 237  ASN D CB  1 
ATOM   9480  C  CG  . ASN D 1 237 ? -57.225 21.840  91.789  1.00 65.05 ? 237  ASN D CG  1 
ATOM   9481  O  OD1 . ASN D 1 237 ? -56.504 21.923  92.805  1.00 64.82 ? 237  ASN D OD1 1 
ATOM   9482  N  ND2 . ASN D 1 237 ? -58.404 21.210  91.789  1.00 63.85 ? 237  ASN D ND2 1 
ATOM   9483  N  N   . GLU D 1 238 ? -55.318 24.325  88.450  1.00 53.12 ? 238  GLU D N   1 
ATOM   9484  C  CA  . GLU D 1 238 ? -54.829 24.580  87.112  1.00 50.41 ? 238  GLU D CA  1 
ATOM   9485  C  C   . GLU D 1 238 ? -53.337 24.857  87.201  1.00 47.54 ? 238  GLU D C   1 
ATOM   9486  O  O   . GLU D 1 238 ? -52.566 24.391  86.365  1.00 45.13 ? 238  GLU D O   1 
ATOM   9487  C  CB  . GLU D 1 238 ? -55.574 25.779  86.538  1.00 54.99 ? 238  GLU D CB  1 
ATOM   9488  C  CG  . GLU D 1 238 ? -56.045 25.621  85.104  1.00 62.87 ? 238  GLU D CG  1 
ATOM   9489  C  CD  . GLU D 1 238 ? -56.784 24.316  84.847  1.00 63.93 ? 238  GLU D CD  1 
ATOM   9490  O  OE1 . GLU D 1 238 ? -56.121 23.250  84.819  1.00 62.05 ? 238  GLU D OE1 1 
ATOM   9491  O  OE2 . GLU D 1 238 ? -58.023 24.370  84.669  1.00 65.50 ? 238  GLU D OE2 1 
ATOM   9492  N  N   . ILE D 1 239 ? -52.919 25.598  88.226  1.00 46.59 ? 239  ILE D N   1 
ATOM   9493  C  CA  . ILE D 1 239 ? -51.495 25.892  88.387  1.00 47.47 ? 239  ILE D CA  1 
ATOM   9494  C  C   . ILE D 1 239 ? -50.760 24.600  88.682  1.00 46.89 ? 239  ILE D C   1 
ATOM   9495  O  O   . ILE D 1 239 ? -49.686 24.343  88.165  1.00 42.19 ? 239  ILE D O   1 
ATOM   9496  C  CB  . ILE D 1 239 ? -51.221 26.846  89.536  1.00 46.11 ? 239  ILE D CB  1 
ATOM   9497  C  CG1 . ILE D 1 239 ? -51.817 28.223  89.234  1.00 43.87 ? 239  ILE D CG1 1 
ATOM   9498  C  CG2 . ILE D 1 239 ? -49.715 26.935  89.747  1.00 43.86 ? 239  ILE D CG2 1 
ATOM   9499  C  CD1 . ILE D 1 239 ? -51.645 29.215  90.384  1.00 37.73 ? 239  ILE D CD1 1 
ATOM   9500  N  N   . LYS D 1 240 ? -51.370 23.794  89.538  1.00 51.54 ? 240  LYS D N   1 
ATOM   9501  C  CA  . LYS D 1 240 ? -50.835 22.498  89.904  1.00 53.34 ? 240  LYS D CA  1 
ATOM   9502  C  C   . LYS D 1 240 ? -50.659 21.596  88.682  1.00 54.66 ? 240  LYS D C   1 
ATOM   9503  O  O   . LYS D 1 240 ? -49.685 20.851  88.591  1.00 53.64 ? 240  LYS D O   1 
ATOM   9504  C  CB  . LYS D 1 240 ? -51.761 21.846  90.920  1.00 55.14 ? 240  LYS D CB  1 
ATOM   9505  C  CG  . LYS D 1 240 ? -51.342 22.169  92.338  1.00 59.22 ? 240  LYS D CG  1 
ATOM   9506  C  CD  . LYS D 1 240 ? -52.269 21.563  93.386  1.00 58.70 ? 240  LYS D CD  1 
ATOM   9507  C  CE  . LYS D 1 240 ? -53.608 22.282  93.443  1.00 55.39 ? 240  LYS D CE  1 
ATOM   9508  N  NZ  . LYS D 1 240 ? -54.212 22.170  94.809  1.00 53.15 ? 240  LYS D NZ  1 
ATOM   9509  N  N   . GLN D 1 241 ? -51.607 21.663  87.749  1.00 56.09 ? 241  GLN D N   1 
ATOM   9510  C  CA  . GLN D 1 241 ? -51.536 20.876  86.530  1.00 55.30 ? 241  GLN D CA  1 
ATOM   9511  C  C   . GLN D 1 241 ? -50.415 21.376  85.627  1.00 54.60 ? 241  GLN D C   1 
ATOM   9512  O  O   . GLN D 1 241 ? -50.146 20.770  84.594  1.00 56.78 ? 241  GLN D O   1 
ATOM   9513  C  CB  . GLN D 1 241 ? -52.863 20.930  85.771  1.00 58.27 ? 241  GLN D CB  1 
ATOM   9514  C  CG  . GLN D 1 241 ? -53.888 19.879  86.208  1.00 63.44 ? 241  GLN D CG  1 
ATOM   9515  C  CD  . GLN D 1 241 ? -53.377 18.449  86.045  1.00 66.34 ? 241  GLN D CD  1 
ATOM   9516  O  OE1 . GLN D 1 241 ? -52.976 18.024  84.946  1.00 63.96 ? 241  GLN D OE1 1 
ATOM   9517  N  NE2 . GLN D 1 241 ? -53.392 17.697  87.142  1.00 68.94 ? 241  GLN D NE2 1 
ATOM   9518  N  N   . GLY D 1 242 ? -49.763 22.471  86.018  1.00 53.38 ? 242  GLY D N   1 
ATOM   9519  C  CA  . GLY D 1 242 ? -48.675 23.029  85.225  1.00 51.42 ? 242  GLY D CA  1 
ATOM   9520  C  C   . GLY D 1 242 ? -49.112 23.915  84.057  1.00 51.01 ? 242  GLY D C   1 
ATOM   9521  O  O   . GLY D 1 242 ? -48.354 24.139  83.106  1.00 52.04 ? 242  GLY D O   1 
ATOM   9522  N  N   . LYS D 1 243 ? -50.333 24.438  84.142  1.00 49.59 ? 243  LYS D N   1 
ATOM   9523  C  CA  . LYS D 1 243 ? -50.910 25.284  83.104  1.00 47.09 ? 243  LYS D CA  1 
ATOM   9524  C  C   . LYS D 1 243 ? -50.387 26.722  83.021  1.00 45.78 ? 243  LYS D C   1 
ATOM   9525  O  O   . LYS D 1 243 ? -50.789 27.484  82.149  1.00 45.24 ? 243  LYS D O   1 
ATOM   9526  C  CB  . LYS D 1 243 ? -52.426 25.304  83.265  1.00 47.61 ? 243  LYS D CB  1 
ATOM   9527  C  CG  . LYS D 1 243 ? -53.074 23.916  83.244  1.00 51.57 ? 243  LYS D CG  1 
ATOM   9528  C  CD  . LYS D 1 243 ? -53.105 23.308  81.853  1.00 54.62 ? 243  LYS D CD  1 
ATOM   9529  C  CE  . LYS D 1 243 ? -53.981 22.061  81.826  1.00 59.22 ? 243  LYS D CE  1 
ATOM   9530  N  NZ  . LYS D 1 243 ? -55.418 22.296  82.271  1.00 62.81 ? 243  LYS D NZ  1 
ATOM   9531  N  N   . PHE D 1 244 ? -49.484 27.090  83.917  1.00 45.06 ? 244  PHE D N   1 
ATOM   9532  C  CA  . PHE D 1 244 ? -48.927 28.431  83.902  1.00 45.19 ? 244  PHE D CA  1 
ATOM   9533  C  C   . PHE D 1 244 ? -47.411 28.501  83.915  1.00 45.36 ? 244  PHE D C   1 
ATOM   9534  O  O   . PHE D 1 244 ? -46.804 28.495  84.978  1.00 43.19 ? 244  PHE D O   1 
ATOM   9535  C  CB  . PHE D 1 244 ? -49.465 29.241  85.080  1.00 41.66 ? 244  PHE D CB  1 
ATOM   9536  C  CG  . PHE D 1 244 ? -50.928 29.524  84.987  1.00 40.80 ? 244  PHE D CG  1 
ATOM   9537  C  CD1 . PHE D 1 244 ? -51.861 28.630  85.494  1.00 44.34 ? 244  PHE D CD1 1 
ATOM   9538  C  CD2 . PHE D 1 244 ? -51.381 30.682  84.386  1.00 37.67 ? 244  PHE D CD2 1 
ATOM   9539  C  CE1 . PHE D 1 244 ? -53.232 28.896  85.397  1.00 39.96 ? 244  PHE D CE1 1 
ATOM   9540  C  CE2 . PHE D 1 244 ? -52.730 30.943  84.287  1.00 37.50 ? 244  PHE D CE2 1 
ATOM   9541  C  CZ  . PHE D 1 244 ? -53.657 30.051  84.795  1.00 38.34 ? 244  PHE D CZ  1 
ATOM   9542  N  N   . HIS D 1 245 ? -46.803 28.593  82.738  1.00 48.33 ? 245  HIS D N   1 
ATOM   9543  C  CA  . HIS D 1 245 ? -45.351 28.694  82.655  1.00 53.43 ? 245  HIS D CA  1 
ATOM   9544  C  C   . HIS D 1 245 ? -45.053 29.989  81.904  1.00 49.97 ? 245  HIS D C   1 
ATOM   9545  O  O   . HIS D 1 245 ? -44.011 30.607  82.090  1.00 46.75 ? 245  HIS D O   1 
ATOM   9546  C  CB  . HIS D 1 245 ? -44.766 27.444  81.940  1.00 62.59 ? 245  HIS D CB  1 
ATOM   9547  C  CG  . HIS D 1 245 ? -44.091 27.723  80.616  1.00 79.55 ? 245  HIS D CG  1 
ATOM   9548  N  ND1 . HIS D 1 245 ? -42.790 28.183  80.513  1.00 85.58 ? 245  HIS D ND1 1 
ATOM   9549  C  CD2 . HIS D 1 245 ? -44.539 27.591  79.339  1.00 82.53 ? 245  HIS D CD2 1 
ATOM   9550  C  CE1 . HIS D 1 245 ? -42.470 28.323  79.236  1.00 86.49 ? 245  HIS D CE1 1 
ATOM   9551  N  NE2 . HIS D 1 245 ? -43.513 27.972  78.503  1.00 85.34 ? 245  HIS D NE2 1 
ATOM   9552  N  N   . ASN D 1 246 ? -46.009 30.409  81.082  1.00 49.15 ? 246  ASN D N   1 
ATOM   9553  C  CA  . ASN D 1 246 ? -45.860 31.610  80.264  1.00 47.15 ? 246  ASN D CA  1 
ATOM   9554  C  C   . ASN D 1 246 ? -45.977 32.928  81.042  1.00 46.86 ? 246  ASN D C   1 
ATOM   9555  O  O   . ASN D 1 246 ? -46.996 33.209  81.665  1.00 45.58 ? 246  ASN D O   1 
ATOM   9556  C  CB  . ASN D 1 246 ? -46.881 31.589  79.138  1.00 45.98 ? 246  ASN D CB  1 
ATOM   9557  C  CG  . ASN D 1 246 ? -46.749 32.790  78.220  1.00 49.05 ? 246  ASN D CG  1 
ATOM   9558  O  OD1 . ASN D 1 246 ? -47.734 33.463  77.905  1.00 51.21 ? 246  ASN D OD1 1 
ATOM   9559  N  ND2 . ASN D 1 246 ? -45.535 33.060  77.779  1.00 46.06 ? 246  ASN D ND2 1 
ATOM   9560  N  N   . PRO D 1 247 ? -44.919 33.752  81.002  1.00 44.92 ? 247  PRO D N   1 
ATOM   9561  C  CA  . PRO D 1 247 ? -44.871 35.038  81.691  1.00 43.49 ? 247  PRO D CA  1 
ATOM   9562  C  C   . PRO D 1 247 ? -46.119 35.907  81.557  1.00 44.15 ? 247  PRO D C   1 
ATOM   9563  O  O   . PRO D 1 247 ? -46.634 36.400  82.564  1.00 47.01 ? 247  PRO D O   1 
ATOM   9564  C  CB  . PRO D 1 247 ? -43.624 35.693  81.096  1.00 42.38 ? 247  PRO D CB  1 
ATOM   9565  C  CG  . PRO D 1 247 ? -42.717 34.516  80.918  1.00 40.39 ? 247  PRO D CG  1 
ATOM   9566  C  CD  . PRO D 1 247 ? -43.632 33.473  80.329  1.00 43.40 ? 247  PRO D CD  1 
ATOM   9567  N  N   . MET D 1 248 ? -46.605 36.099  80.332  1.00 41.69 ? 248  MET D N   1 
ATOM   9568  C  CA  . MET D 1 248 ? -47.776 36.941  80.115  1.00 40.20 ? 248  MET D CA  1 
ATOM   9569  C  C   . MET D 1 248 ? -49.029 36.323  80.761  1.00 41.93 ? 248  MET D C   1 
ATOM   9570  O  O   . MET D 1 248 ? -49.835 37.032  81.375  1.00 41.19 ? 248  MET D O   1 
ATOM   9571  C  CB  . MET D 1 248 ? -47.967 37.168  78.608  1.00 38.89 ? 248  MET D CB  1 
ATOM   9572  C  CG  . MET D 1 248 ? -49.168 38.000  78.237  1.00 40.80 ? 248  MET D CG  1 
ATOM   9573  S  SD  . MET D 1 248 ? -49.241 39.601  79.090  1.00 43.77 ? 248  MET D SD  1 
ATOM   9574  C  CE  . MET D 1 248 ? -48.561 40.675  77.816  1.00 44.71 ? 248  MET D CE  1 
ATOM   9575  N  N   . SER D 1 249 ? -49.180 35.001  80.639  1.00 43.91 ? 249  SER D N   1 
ATOM   9576  C  CA  . SER D 1 249 ? -50.321 34.288  81.220  1.00 42.80 ? 249  SER D CA  1 
ATOM   9577  C  C   . SER D 1 249 ? -50.321 34.440  82.739  1.00 41.69 ? 249  SER D C   1 
ATOM   9578  O  O   . SER D 1 249 ? -51.371 34.586  83.370  1.00 41.49 ? 249  SER D O   1 
ATOM   9579  C  CB  . SER D 1 249 ? -50.271 32.796  80.870  1.00 42.63 ? 249  SER D CB  1 
ATOM   9580  O  OG  . SER D 1 249 ? -50.243 32.581  79.470  1.00 42.49 ? 249  SER D OG  1 
ATOM   9581  N  N   . ILE D 1 250 ? -49.132 34.405  83.326  1.00 42.82 ? 250  ILE D N   1 
ATOM   9582  C  CA  . ILE D 1 250 ? -49.005 34.534  84.771  1.00 41.89 ? 250  ILE D CA  1 
ATOM   9583  C  C   . ILE D 1 250 ? -49.331 35.982  85.183  1.00 42.32 ? 250  ILE D C   1 
ATOM   9584  O  O   . ILE D 1 250 ? -50.023 36.218  86.181  1.00 44.07 ? 250  ILE D O   1 
ATOM   9585  C  CB  . ILE D 1 250 ? -47.579 34.149  85.225  1.00 40.43 ? 250  ILE D CB  1 
ATOM   9586  C  CG1 . ILE D 1 250 ? -47.299 32.691  84.845  1.00 35.96 ? 250  ILE D CG1 1 
ATOM   9587  C  CG2 . ILE D 1 250 ? -47.437 34.315  86.735  1.00 38.06 ? 250  ILE D CG2 1 
ATOM   9588  C  CD1 . ILE D 1 250 ? -45.871 32.277  85.075  1.00 33.21 ? 250  ILE D CD1 1 
ATOM   9589  N  N   . ALA D 1 251 ? -48.853 36.939  84.392  1.00 36.98 ? 251  ALA D N   1 
ATOM   9590  C  CA  . ALA D 1 251 ? -49.081 38.339  84.655  1.00 35.67 ? 251  ALA D CA  1 
ATOM   9591  C  C   . ALA D 1 251 ? -50.567 38.635  84.719  1.00 38.31 ? 251  ALA D C   1 
ATOM   9592  O  O   . ALA D 1 251 ? -51.002 39.565  85.413  1.00 41.00 ? 251  ALA D O   1 
ATOM   9593  C  CB  . ALA D 1 251 ? -48.445 39.171  83.572  1.00 34.97 ? 251  ALA D CB  1 
ATOM   9594  N  N   . GLN D 1 252 ? -51.351 37.838  84.005  1.00 37.08 ? 252  GLN D N   1 
ATOM   9595  C  CA  . GLN D 1 252 ? -52.771 38.054  83.968  1.00 32.57 ? 252  GLN D CA  1 
ATOM   9596  C  C   . GLN D 1 252 ? -53.606 37.329  85.008  1.00 35.22 ? 252  GLN D C   1 
ATOM   9597  O  O   . GLN D 1 252 ? -54.808 37.575  85.110  1.00 34.03 ? 252  GLN D O   1 
ATOM   9598  C  CB  . GLN D 1 252 ? -53.254 37.828  82.547  1.00 32.92 ? 252  GLN D CB  1 
ATOM   9599  C  CG  . GLN D 1 252 ? -52.661 38.907  81.623  1.00 37.34 ? 252  GLN D CG  1 
ATOM   9600  C  CD  . GLN D 1 252 ? -53.211 38.905  80.210  1.00 36.00 ? 252  GLN D CD  1 
ATOM   9601  O  OE1 . GLN D 1 252 ? -53.390 37.855  79.623  1.00 40.80 ? 252  GLN D OE1 1 
ATOM   9602  N  NE2 . GLN D 1 252 ? -53.445 40.091  79.648  1.00 33.76 ? 252  GLN D NE2 1 
ATOM   9603  N  N   . ILE D 1 253 ? -52.999 36.453  85.808  1.00 36.50 ? 253  ILE D N   1 
ATOM   9604  C  CA  . ILE D 1 253 ? -53.774 35.832  86.892  1.00 39.67 ? 253  ILE D CA  1 
ATOM   9605  C  C   . ILE D 1 253 ? -53.228 36.284  88.216  1.00 37.75 ? 253  ILE D C   1 
ATOM   9606  O  O   . ILE D 1 253 ? -53.950 36.291  89.211  1.00 38.47 ? 253  ILE D O   1 
ATOM   9607  C  CB  . ILE D 1 253 ? -53.711 34.256  86.996  1.00 43.05 ? 253  ILE D CB  1 
ATOM   9608  C  CG1 . ILE D 1 253 ? -52.662 33.714  86.060  1.00 44.64 ? 253  ILE D CG1 1 
ATOM   9609  C  CG2 . ILE D 1 253 ? -55.122 33.637  86.862  1.00 45.47 ? 253  ILE D CG2 1 
ATOM   9610  C  CD1 . ILE D 1 253 ? -51.318 33.646  86.704  1.00 49.37 ? 253  ILE D CD1 1 
ATOM   9611  N  N   . LEU D 1 254 ? -51.950 36.640  88.245  1.00 37.65 ? 254  LEU D N   1 
ATOM   9612  C  CA  . LEU D 1 254 ? -51.348 36.995  89.512  1.00 38.02 ? 254  LEU D CA  1 
ATOM   9613  C  C   . LEU D 1 254 ? -52.181 37.989  90.322  1.00 39.13 ? 254  LEU D C   1 
ATOM   9614  O  O   . LEU D 1 254 ? -52.555 37.690  91.468  1.00 41.80 ? 254  LEU D O   1 
ATOM   9615  C  CB  . LEU D 1 254 ? -49.935 37.508  89.304  1.00 38.79 ? 254  LEU D CB  1 
ATOM   9616  C  CG  . LEU D 1 254 ? -48.927 36.959  90.312  1.00 39.18 ? 254  LEU D CG  1 
ATOM   9617  C  CD1 . LEU D 1 254 ? -47.645 37.800  90.307  1.00 38.39 ? 254  LEU D CD1 1 
ATOM   9618  C  CD2 . LEU D 1 254 ? -49.541 36.981  91.679  1.00 39.58 ? 254  LEU D CD2 1 
ATOM   9619  N  N   . PRO D 1 255 ? -52.523 39.153  89.732  1.00 36.48 ? 255  PRO D N   1 
ATOM   9620  C  CA  . PRO D 1 255 ? -53.316 40.183  90.410  1.00 37.02 ? 255  PRO D CA  1 
ATOM   9621  C  C   . PRO D 1 255 ? -54.540 39.618  91.102  1.00 40.93 ? 255  PRO D C   1 
ATOM   9622  O  O   . PRO D 1 255 ? -54.811 39.949  92.273  1.00 39.84 ? 255  PRO D O   1 
ATOM   9623  C  CB  . PRO D 1 255 ? -53.713 41.113  89.285  1.00 35.90 ? 255  PRO D CB  1 
ATOM   9624  C  CG  . PRO D 1 255 ? -52.587 40.986  88.354  1.00 37.42 ? 255  PRO D CG  1 
ATOM   9625  C  CD  . PRO D 1 255 ? -52.335 39.513  88.321  1.00 35.13 ? 255  PRO D CD  1 
ATOM   9626  N  N   . SER D 1 256 ? -55.287 38.785  90.374  1.00 40.17 ? 256  SER D N   1 
ATOM   9627  C  CA  . SER D 1 256 ? -56.483 38.172  90.944  1.00 42.96 ? 256  SER D CA  1 
ATOM   9628  C  C   . SER D 1 256 ? -56.096 37.307  92.132  1.00 43.79 ? 256  SER D C   1 
ATOM   9629  O  O   . SER D 1 256 ? -56.718 37.380  93.178  1.00 46.42 ? 256  SER D O   1 
ATOM   9630  C  CB  . SER D 1 256 ? -57.227 37.304  89.912  1.00 41.67 ? 256  SER D CB  1 
ATOM   9631  O  OG  . SER D 1 256 ? -57.859 38.079  88.909  1.00 41.47 ? 256  SER D OG  1 
ATOM   9632  N  N   . LEU D 1 257 ? -55.049 36.504  91.978  1.00 45.53 ? 257  LEU D N   1 
ATOM   9633  C  CA  . LEU D 1 257 ? -54.637 35.617  93.056  1.00 45.86 ? 257  LEU D CA  1 
ATOM   9634  C  C   . LEU D 1 257 ? -54.161 36.387  94.276  1.00 45.43 ? 257  LEU D C   1 
ATOM   9635  O  O   . LEU D 1 257 ? -53.989 35.805  95.352  1.00 46.76 ? 257  LEU D O   1 
ATOM   9636  C  CB  . LEU D 1 257 ? -53.552 34.648  92.561  1.00 46.37 ? 257  LEU D CB  1 
ATOM   9637  C  CG  . LEU D 1 257 ? -53.997 33.637  91.484  1.00 46.82 ? 257  LEU D CG  1 
ATOM   9638  C  CD1 . LEU D 1 257 ? -52.782 32.862  90.967  1.00 42.44 ? 257  LEU D CD1 1 
ATOM   9639  C  CD2 . LEU D 1 257 ? -55.056 32.687  92.059  1.00 41.78 ? 257  LEU D CD2 1 
ATOM   9640  N  N   . LYS D 1 258 ? -53.965 37.694  94.109  1.00 42.36 ? 258  LYS D N   1 
ATOM   9641  C  CA  . LYS D 1 258 ? -53.506 38.554  95.197  1.00 40.41 ? 258  LYS D CA  1 
ATOM   9642  C  C   . LYS D 1 258 ? -54.597 39.504  95.699  1.00 40.42 ? 258  LYS D C   1 
ATOM   9643  O  O   . LYS D 1 258 ? -54.301 40.443  96.428  1.00 42.26 ? 258  LYS D O   1 
ATOM   9644  C  CB  . LYS D 1 258 ? -52.307 39.372  94.731  1.00 40.41 ? 258  LYS D CB  1 
ATOM   9645  C  CG  . LYS D 1 258 ? -51.060 38.567  94.471  1.00 40.93 ? 258  LYS D CG  1 
ATOM   9646  C  CD  . LYS D 1 258 ? -50.581 37.983  95.793  1.00 48.68 ? 258  LYS D CD  1 
ATOM   9647  C  CE  . LYS D 1 258 ? -49.257 37.279  95.670  1.00 49.83 ? 258  LYS D CE  1 
ATOM   9648  N  NZ  . LYS D 1 258 ? -48.763 36.946  97.017  1.00 53.66 ? 258  LYS D NZ  1 
ATOM   9649  N  N   . GLY D 1 259 ? -55.849 39.261  95.315  1.00 37.58 ? 259  GLY D N   1 
ATOM   9650  C  CA  . GLY D 1 259 ? -56.930 40.140  95.732  1.00 38.83 ? 259  GLY D CA  1 
ATOM   9651  C  C   . GLY D 1 259 ? -56.814 41.549  95.161  1.00 42.41 ? 259  GLY D C   1 
ATOM   9652  O  O   . GLY D 1 259 ? -57.281 42.511  95.756  1.00 45.73 ? 259  GLY D O   1 
ATOM   9653  N  N   . LYS D 1 260 ? -56.197 41.682  93.994  1.00 43.23 ? 260  LYS D N   1 
ATOM   9654  C  CA  . LYS D 1 260 ? -56.026 42.991  93.383  1.00 43.48 ? 260  LYS D CA  1 
ATOM   9655  C  C   . LYS D 1 260 ? -56.625 43.041  91.996  1.00 40.95 ? 260  LYS D C   1 
ATOM   9656  O  O   . LYS D 1 260 ? -56.897 42.010  91.402  1.00 45.33 ? 260  LYS D O   1 
ATOM   9657  C  CB  . LYS D 1 260 ? -54.540 43.298  93.262  1.00 47.21 ? 260  LYS D CB  1 
ATOM   9658  C  CG  . LYS D 1 260 ? -53.782 43.205  94.553  1.00 51.53 ? 260  LYS D CG  1 
ATOM   9659  C  CD  . LYS D 1 260 ? -54.192 44.335  95.460  1.00 56.90 ? 260  LYS D CD  1 
ATOM   9660  C  CE  . LYS D 1 260 ? -53.133 44.630  96.504  1.00 58.27 ? 260  LYS D CE  1 
ATOM   9661  N  NZ  . LYS D 1 260 ? -53.404 45.982  97.092  1.00 65.58 ? 260  LYS D NZ  1 
ATOM   9662  N  N   . THR D 1 261 ? -56.845 44.241  91.485  1.00 38.76 ? 261  THR D N   1 
ATOM   9663  C  CA  . THR D 1 261 ? -57.325 44.405  90.109  1.00 38.38 ? 261  THR D CA  1 
ATOM   9664  C  C   . THR D 1 261 ? -56.512 45.591  89.629  1.00 38.25 ? 261  THR D C   1 
ATOM   9665  O  O   . THR D 1 261 ? -55.828 46.241  90.433  1.00 35.58 ? 261  THR D O   1 
ATOM   9666  C  CB  . THR D 1 261 ? -58.826 44.799  89.973  1.00 36.93 ? 261  THR D CB  1 
ATOM   9667  O  OG1 . THR D 1 261 ? -59.012 46.143  90.446  1.00 36.99 ? 261  THR D OG1 1 
ATOM   9668  C  CG2 . THR D 1 261 ? -59.731 43.824  90.737  1.00 32.54 ? 261  THR D CG2 1 
ATOM   9669  N  N   . TYR D 1 262 ? -56.575 45.864  88.331  1.00 36.24 ? 262  TYR D N   1 
ATOM   9670  C  CA  . TYR D 1 262 ? -55.866 46.990  87.766  1.00 33.44 ? 262  TYR D CA  1 
ATOM   9671  C  C   . TYR D 1 262 ? -56.427 48.301  88.343  1.00 34.26 ? 262  TYR D C   1 
ATOM   9672  O  O   . TYR D 1 262 ? -55.823 49.355  88.198  1.00 34.97 ? 262  TYR D O   1 
ATOM   9673  C  CB  . TYR D 1 262 ? -56.027 47.000  86.254  1.00 33.88 ? 262  TYR D CB  1 
ATOM   9674  C  CG  . TYR D 1 262 ? -55.274 45.918  85.525  1.00 36.22 ? 262  TYR D CG  1 
ATOM   9675  C  CD1 . TYR D 1 262 ? -54.227 45.227  86.137  1.00 35.43 ? 262  TYR D CD1 1 
ATOM   9676  C  CD2 . TYR D 1 262 ? -55.553 45.643  84.178  1.00 34.00 ? 262  TYR D CD2 1 
ATOM   9677  C  CE1 . TYR D 1 262 ? -53.474 44.295  85.422  1.00 34.68 ? 262  TYR D CE1 1 
ATOM   9678  C  CE2 . TYR D 1 262 ? -54.810 44.717  83.453  1.00 29.12 ? 262  TYR D CE2 1 
ATOM   9679  C  CZ  . TYR D 1 262 ? -53.770 44.042  84.071  1.00 30.93 ? 262  TYR D CZ  1 
ATOM   9680  O  OH  . TYR D 1 262 ? -53.033 43.106  83.340  1.00 31.17 ? 262  TYR D OH  1 
ATOM   9681  N  N   . LEU D 1 263 ? -57.596 48.255  88.966  1.00 33.34 ? 263  LEU D N   1 
ATOM   9682  C  CA  . LEU D 1 263 ? -58.133 49.475  89.537  1.00 37.42 ? 263  LEU D CA  1 
ATOM   9683  C  C   . LEU D 1 263 ? -57.322 49.856  90.769  1.00 38.36 ? 263  LEU D C   1 
ATOM   9684  O  O   . LEU D 1 263 ? -57.450 50.971  91.262  1.00 38.93 ? 263  LEU D O   1 
ATOM   9685  C  CB  . LEU D 1 263 ? -59.598 49.315  89.940  1.00 37.02 ? 263  LEU D CB  1 
ATOM   9686  C  CG  . LEU D 1 263 ? -60.624 49.081  88.833  1.00 40.81 ? 263  LEU D CG  1 
ATOM   9687  C  CD1 . LEU D 1 263 ? -62.004 49.284  89.399  1.00 36.82 ? 263  LEU D CD1 1 
ATOM   9688  C  CD2 . LEU D 1 263 ? -60.395 50.035  87.696  1.00 35.94 ? 263  LEU D CD2 1 
ATOM   9689  N  N   . ASP D 1 264 ? -56.474 48.949  91.248  1.00 36.74 ? 264  ASP D N   1 
ATOM   9690  C  CA  . ASP D 1 264 ? -55.684 49.234  92.436  1.00 41.30 ? 264  ASP D CA  1 
ATOM   9691  C  C   . ASP D 1 264 ? -54.366 49.915  92.119  1.00 42.07 ? 264  ASP D C   1 
ATOM   9692  O  O   . ASP D 1 264 ? -53.676 50.399  93.021  1.00 44.24 ? 264  ASP D O   1 
ATOM   9693  C  CB  . ASP D 1 264 ? -55.384 47.956  93.218  1.00 43.79 ? 264  ASP D CB  1 
ATOM   9694  C  CG  . ASP D 1 264 ? -56.616 47.325  93.804  1.00 47.62 ? 264  ASP D CG  1 
ATOM   9695  O  OD1 . ASP D 1 264 ? -57.400 48.063  94.443  1.00 49.16 ? 264  ASP D OD1 1 
ATOM   9696  O  OD2 . ASP D 1 264 ? -56.789 46.088  93.643  1.00 51.54 ? 264  ASP D OD2 1 
ATOM   9697  N  N   . VAL D 1 265 ? -54.017 49.937  90.844  1.00 39.74 ? 265  VAL D N   1 
ATOM   9698  C  CA  . VAL D 1 265 ? -52.789 50.555  90.406  1.00 40.78 ? 265  VAL D CA  1 
ATOM   9699  C  C   . VAL D 1 265 ? -52.538 51.935  91.015  1.00 42.73 ? 265  VAL D C   1 
ATOM   9700  O  O   . VAL D 1 265 ? -51.493 52.159  91.609  1.00 47.59 ? 265  VAL D O   1 
ATOM   9701  C  CB  . VAL D 1 265 ? -52.757 50.619  88.862  1.00 39.94 ? 265  VAL D CB  1 
ATOM   9702  C  CG1 . VAL D 1 265 ? -51.738 51.604  88.383  1.00 39.40 ? 265  VAL D CG1 1 
ATOM   9703  C  CG2 . VAL D 1 265 ? -52.410 49.235  88.324  1.00 41.86 ? 265  VAL D CG2 1 
ATOM   9704  N  N   . PRO D 1 266 ? -53.483 52.880  90.896  1.00 43.30 ? 266  PRO D N   1 
ATOM   9705  C  CA  . PRO D 1 266 ? -53.196 54.193  91.497  1.00 40.81 ? 266  PRO D CA  1 
ATOM   9706  C  C   . PRO D 1 266 ? -52.883 54.170  93.004  1.00 40.84 ? 266  PRO D C   1 
ATOM   9707  O  O   . PRO D 1 266 ? -52.200 55.073  93.496  1.00 42.16 ? 266  PRO D O   1 
ATOM   9708  C  CB  . PRO D 1 266 ? -54.455 54.992  91.198  1.00 37.57 ? 266  PRO D CB  1 
ATOM   9709  C  CG  . PRO D 1 266 ? -54.947 54.390  89.909  1.00 40.20 ? 266  PRO D CG  1 
ATOM   9710  C  CD  . PRO D 1 266 ? -54.772 52.904  90.182  1.00 43.52 ? 266  PRO D CD  1 
ATOM   9711  N  N   . GLN D 1 267 ? -53.350 53.149  93.727  1.00 37.69 ? 267  GLN D N   1 
ATOM   9712  C  CA  . GLN D 1 267 ? -53.133 53.078  95.175  1.00 40.30 ? 267  GLN D CA  1 
ATOM   9713  C  C   . GLN D 1 267 ? -51.888 52.344  95.662  1.00 43.00 ? 267  GLN D C   1 
ATOM   9714  O  O   . GLN D 1 267 ? -51.689 52.188  96.872  1.00 43.52 ? 267  GLN D O   1 
ATOM   9715  C  CB  . GLN D 1 267 ? -54.352 52.462  95.861  1.00 42.24 ? 267  GLN D CB  1 
ATOM   9716  C  CG  . GLN D 1 267 ? -55.526 53.414  96.040  1.00 53.58 ? 267  GLN D CG  1 
ATOM   9717  C  CD  . GLN D 1 267 ? -56.238 53.767  94.718  1.00 62.76 ? 267  GLN D CD  1 
ATOM   9718  O  OE1 . GLN D 1 267 ? -56.863 52.907  94.083  1.00 63.56 ? 267  GLN D OE1 1 
ATOM   9719  N  NE2 . GLN D 1 267 ? -56.143 55.038  94.307  1.00 65.60 ? 267  GLN D NE2 1 
ATOM   9720  N  N   . VAL D 1 268 ? -51.051 51.884  94.741  1.00 41.32 ? 268  VAL D N   1 
ATOM   9721  C  CA  . VAL D 1 268 ? -49.851 51.164  95.117  1.00 41.78 ? 268  VAL D CA  1 
ATOM   9722  C  C   . VAL D 1 268 ? -48.857 52.011  95.905  1.00 45.24 ? 268  VAL D C   1 
ATOM   9723  O  O   . VAL D 1 268 ? -48.559 53.149  95.544  1.00 46.58 ? 268  VAL D O   1 
ATOM   9724  C  CB  . VAL D 1 268 ? -49.114 50.621  93.863  1.00 45.02 ? 268  VAL D CB  1 
ATOM   9725  C  CG1 . VAL D 1 268 ? -47.715 50.107  94.254  1.00 44.82 ? 268  VAL D CG1 1 
ATOM   9726  C  CG2 . VAL D 1 268 ? -49.931 49.511  93.197  1.00 41.87 ? 268  VAL D CG2 1 
ATOM   9727  N  N   . THR D 1 269 ? -48.324 51.431  96.971  1.00 48.12 ? 269  THR D N   1 
ATOM   9728  C  CA  . THR D 1 269 ? -47.324 52.083  97.816  1.00 50.94 ? 269  THR D CA  1 
ATOM   9729  C  C   . THR D 1 269 ? -45.954 51.639  97.315  1.00 53.57 ? 269  THR D C   1 
ATOM   9730  O  O   . THR D 1 269 ? -45.741 50.446  97.083  1.00 56.54 ? 269  THR D O   1 
ATOM   9731  C  CB  . THR D 1 269 ? -47.433 51.610  99.276  1.00 54.85 ? 269  THR D CB  1 
ATOM   9732  O  OG1 . THR D 1 269 ? -48.688 52.022  99.829  1.00 52.74 ? 269  THR D OG1 1 
ATOM   9733  C  CG2 . THR D 1 269 ? -46.281 52.176  100.109 1.00 59.46 ? 269  THR D CG2 1 
ATOM   9734  N  N   . CYS D 1 270 ? -45.013 52.561  97.162  1.00 54.17 ? 270  CYS D N   1 
ATOM   9735  C  CA  . CYS D 1 270 ? -43.700 52.139  96.687  1.00 57.94 ? 270  CYS D CA  1 
ATOM   9736  C  C   . CYS D 1 270 ? -42.643 51.993  97.778  1.00 62.61 ? 270  CYS D C   1 
ATOM   9737  O  O   . CYS D 1 270 ? -42.656 52.698  98.781  1.00 59.90 ? 270  CYS D O   1 
ATOM   9738  C  CB  . CYS D 1 270 ? -43.211 53.051  95.552  1.00 56.76 ? 270  CYS D CB  1 
ATOM   9739  S  SG  . CYS D 1 270 ? -44.200 52.873  94.015  1.00 53.19 ? 270  CYS D SG  1 
ATOM   9740  N  N   . SER D 1 271 ? -41.730 51.052  97.547  1.00 72.73 ? 271  SER D N   1 
ATOM   9741  C  CA  . SER D 1 271 ? -40.648 50.681  98.476  1.00 81.43 ? 271  SER D CA  1 
ATOM   9742  C  C   . SER D 1 271 ? -41.284 50.219  99.772  1.00 86.63 ? 271  SER D C   1 
ATOM   9743  O  O   . SER D 1 271 ? -41.224 50.921  100.793 1.00 84.17 ? 271  SER D O   1 
ATOM   9744  C  CB  . SER D 1 271 ? -39.668 51.826  98.769  1.00 81.57 ? 271  SER D CB  1 
ATOM   9745  O  OG  . SER D 1 271 ? -38.529 51.318  99.464  1.00 78.66 ? 271  SER D OG  1 
ATOM   9746  N  N   . PRO D 1 272 ? -41.914 49.021  99.730  1.00 92.98 ? 272  PRO D N   1 
ATOM   9747  C  CA  . PRO D 1 272 ? -42.618 48.321  100.817 1.00 96.95 ? 272  PRO D CA  1 
ATOM   9748  C  C   . PRO D 1 272 ? -41.919 48.290  102.184 1.00 98.65 ? 272  PRO D C   1 
ATOM   9749  O  O   . PRO D 1 272 ? -40.682 48.302  102.280 1.00 99.45 ? 272  PRO D O   1 
ATOM   9750  C  CB  . PRO D 1 272 ? -42.835 46.917  100.239 1.00 98.11 ? 272  PRO D CB  1 
ATOM   9751  C  CG  . PRO D 1 272 ? -43.074 47.209  98.772  1.00 97.51 ? 272  PRO D CG  1 
ATOM   9752  C  CD  . PRO D 1 272 ? -41.979 48.230  98.479  1.00 94.50 ? 272  PRO D CD  1 
ATOM   9753  N  N   . ASP D 1 273 ? -42.739 48.248  103.234 1.00 99.17 ? 273  ASP D N   1 
ATOM   9754  C  CA  . ASP D 1 273 ? -42.265 48.207  104.615 1.00 99.45 ? 273  ASP D CA  1 
ATOM   9755  C  C   . ASP D 1 273 ? -42.309 46.741  105.082 1.00 99.45 ? 273  ASP D C   1 
ATOM   9756  O  O   . ASP D 1 273 ? -43.088 46.436  106.019 1.00 99.45 ? 273  ASP D O   1 
ATOM   9757  C  CB  . ASP D 1 273 ? -43.169 49.091  105.504 1.00 99.45 ? 273  ASP D CB  1 
ATOM   9758  C  CG  . ASP D 1 273 ? -42.558 49.388  106.874 1.00 99.45 ? 273  ASP D CG  1 
ATOM   9759  O  OD1 . ASP D 1 273 ? -42.287 48.430  107.635 1.00 99.45 ? 273  ASP D OD1 1 
ATOM   9760  O  OD2 . ASP D 1 273 ? -42.354 50.583  107.188 1.00 99.45 ? 273  ASP D OD2 1 
HETATM 9761  C  C1  . NAG E 2 .   ? -14.429 89.753  95.782  1.00 94.22 ? 901  NAG A C1  1 
HETATM 9762  C  C2  . NAG E 2 .   ? -14.892 88.642  94.787  1.00 95.89 ? 901  NAG A C2  1 
HETATM 9763  C  C3  . NAG E 2 .   ? -16.184 89.131  94.100  1.00 97.17 ? 901  NAG A C3  1 
HETATM 9764  C  C4  . NAG E 2 .   ? -17.242 89.352  95.228  1.00 97.06 ? 901  NAG A C4  1 
HETATM 9765  C  C5  . NAG E 2 .   ? -16.717 90.451  96.227  1.00 97.83 ? 901  NAG A C5  1 
HETATM 9766  C  C6  . NAG E 2 .   ? -17.659 90.760  97.404  1.00 99.33 ? 901  NAG A C6  1 
HETATM 9767  C  C7  . NAG E 2 .   ? -13.151 87.267  93.495  1.00 98.67 ? 901  NAG A C7  1 
HETATM 9768  C  C8  . NAG E 2 .   ? -13.380 85.969  94.228  1.00 98.29 ? 901  NAG A C8  1 
HETATM 9769  N  N2  . NAG E 2 .   ? -13.840 88.410  93.774  1.00 96.81 ? 901  NAG A N2  1 
HETATM 9770  O  O3  . NAG E 2 .   ? -16.609 88.118  93.184  1.00 99.45 ? 901  NAG A O3  1 
HETATM 9771  O  O4  . NAG E 2 .   ? -18.461 89.834  94.633  1.00 97.93 ? 901  NAG A O4  1 
HETATM 9772  O  O5  . NAG E 2 .   ? -15.423 90.048  96.788  1.00 96.37 ? 901  NAG A O5  1 
HETATM 9773  O  O6  . NAG E 2 .   ? -17.389 89.932  98.536  1.00 99.00 ? 901  NAG A O6  1 
HETATM 9774  O  O7  . NAG E 2 .   ? -12.291 87.243  92.609  1.00 98.83 ? 901  NAG A O7  1 
HETATM 9775  C  C1  . NAG F 2 .   ? -19.740 89.157  94.997  1.00 98.89 ? 902  NAG A C1  1 
HETATM 9776  C  C2  . NAG F 2 .   ? -20.987 90.060  95.106  1.00 99.18 ? 902  NAG A C2  1 
HETATM 9777  C  C3  . NAG F 2 .   ? -22.260 89.214  95.399  1.00 99.45 ? 902  NAG A C3  1 
HETATM 9778  C  C4  . NAG F 2 .   ? -22.366 87.984  94.455  1.00 99.45 ? 902  NAG A C4  1 
HETATM 9779  C  C5  . NAG F 2 .   ? -20.978 87.216  94.449  1.00 99.45 ? 902  NAG A C5  1 
HETATM 9780  C  C6  . NAG F 2 .   ? -20.965 85.970  93.568  1.00 99.45 ? 902  NAG A C6  1 
HETATM 9781  C  C7  . NAG F 2 .   ? -20.935 92.399  96.117  1.00 99.45 ? 902  NAG A C7  1 
HETATM 9782  C  C8  . NAG F 2 .   ? -20.171 93.256  97.092  1.00 97.55 ? 902  NAG A C8  1 
HETATM 9783  N  N2  . NAG F 2 .   ? -20.715 91.054  96.183  1.00 98.17 ? 902  NAG A N2  1 
HETATM 9784  O  O3  . NAG F 2 .   ? -23.413 89.993  95.163  1.00 99.45 ? 902  NAG A O3  1 
HETATM 9785  O  O4  . NAG F 2 .   ? -23.446 87.147  94.909  1.00 99.45 ? 902  NAG A O4  1 
HETATM 9786  O  O5  . NAG F 2 .   ? -19.932 88.147  93.987  1.00 99.45 ? 902  NAG A O5  1 
HETATM 9787  O  O6  . NAG F 2 .   ? -20.907 84.837  94.435  1.00 99.45 ? 902  NAG A O6  1 
HETATM 9788  O  O7  . NAG F 2 .   ? -21.719 92.948  95.324  1.00 99.45 ? 902  NAG A O7  1 
HETATM 9789  CO CO  . B12 G 3 .   ? -9.144  78.607  106.449 1.00 68.54 ? 1001 B12 A CO  1 
HETATM 9790  N  N21 . B12 G 3 .   ? -7.888  77.291  106.005 1.00 39.72 ? 1001 B12 A N21 1 
HETATM 9791  N  N22 . B12 G 3 .   ? -8.221  79.945  105.297 1.00 41.50 ? 1001 B12 A N22 1 
HETATM 9792  N  N23 . B12 G 3 .   ? -10.601 79.855  107.007 1.00 42.12 ? 1001 B12 A N23 1 
HETATM 9793  N  N24 . B12 G 3 .   ? -10.081 77.163  107.270 1.00 39.53 ? 1001 B12 A N24 1 
HETATM 9794  C  C1  . B12 G 3 .   ? -7.960  75.916  106.739 1.00 35.92 ? 1001 B12 A C1  1 
HETATM 9795  C  C20 . B12 G 3 .   ? -7.268  76.125  108.100 1.00 32.70 ? 1001 B12 A C20 1 
HETATM 9796  C  C2  . B12 G 3 .   ? -7.157  74.891  105.698 1.00 37.17 ? 1001 B12 A C2  1 
HETATM 9797  C  C25 . B12 G 3 .   ? -6.352  73.733  106.380 1.00 33.27 ? 1001 B12 A C25 1 
HETATM 9798  C  C26 . B12 G 3 .   ? -8.162  74.296  104.694 1.00 30.73 ? 1001 B12 A C26 1 
HETATM 9799  C  C27 . B12 G 3 .   ? -7.601  73.332  103.658 1.00 32.58 ? 1001 B12 A C27 1 
HETATM 9800  O  O28 . B12 G 3 .   ? -6.981  73.782  102.724 1.00 36.16 ? 1001 B12 A O28 1 
HETATM 9801  N  N29 . B12 G 3 .   ? -7.838  72.051  103.914 1.00 34.07 ? 1001 B12 A N29 1 
HETATM 9802  C  C3  . B12 G 3 .   ? -6.190  75.928  104.960 1.00 37.66 ? 1001 B12 A C3  1 
HETATM 9803  C  C30 . B12 G 3 .   ? -4.692  76.102  105.573 1.00 39.11 ? 1001 B12 A C30 1 
HETATM 9804  C  C31 . B12 G 3 .   ? -3.608  75.494  104.754 1.00 40.93 ? 1001 B12 A C31 1 
HETATM 9805  C  C32 . B12 G 3 .   ? -2.210  75.902  105.191 1.00 44.83 ? 1001 B12 A C32 1 
HETATM 9806  O  O34 . B12 G 3 .   ? -1.225  75.203  104.909 1.00 44.97 ? 1001 B12 A O34 1 
HETATM 9807  N  N33 . B12 G 3 .   ? -2.128  77.013  105.872 1.00 41.68 ? 1001 B12 A N33 1 
HETATM 9808  C  C4  . B12 G 3 .   ? -6.937  77.298  105.027 1.00 39.95 ? 1001 B12 A C4  1 
HETATM 9809  C  C5  . B12 G 3 .   ? -6.572  78.453  104.198 1.00 42.48 ? 1001 B12 A C5  1 
HETATM 9810  C  C35 . B12 G 3 .   ? -5.450  78.194  103.162 1.00 42.30 ? 1001 B12 A C35 1 
HETATM 9811  C  C6  . B12 G 3 .   ? -7.174  79.730  104.387 1.00 39.48 ? 1001 B12 A C6  1 
HETATM 9812  C  C7  . B12 G 3 .   ? -6.831  81.019  103.640 1.00 39.80 ? 1001 B12 A C7  1 
HETATM 9813  C  C36 . B12 G 3 .   ? -5.298  81.388  103.452 1.00 35.64 ? 1001 B12 A C36 1 
HETATM 9814  C  C37 . B12 G 3 .   ? -7.578  80.963  102.241 1.00 41.80 ? 1001 B12 A C37 1 
HETATM 9815  C  C38 . B12 G 3 .   ? -7.356  82.169  101.303 1.00 41.57 ? 1001 B12 A C38 1 
HETATM 9816  O  O39 . B12 G 3 .   ? -6.771  81.994  100.272 1.00 42.63 ? 1001 B12 A O39 1 
HETATM 9817  N  N40 . B12 G 3 .   ? -7.805  83.375  101.758 1.00 41.77 ? 1001 B12 A N40 1 
HETATM 9818  C  C8  . B12 G 3 .   ? -7.674  82.114  104.330 1.00 42.03 ? 1001 B12 A C8  1 
HETATM 9819  C  C41 . B12 G 3 .   ? -6.633  83.130  105.029 1.00 41.87 ? 1001 B12 A C41 1 
HETATM 9820  C  C42 . B12 G 3 .   ? -7.090  84.337  105.787 1.00 54.15 ? 1001 B12 A C42 1 
HETATM 9821  C  C43 . B12 G 3 .   ? -6.092  85.475  105.863 1.00 56.11 ? 1001 B12 A C43 1 
HETATM 9822  O  O44 . B12 G 3 .   ? -4.948  85.342  106.474 1.00 54.44 ? 1001 B12 A O44 1 
HETATM 9823  N  N45 . B12 G 3 .   ? -6.479  86.581  105.312 1.00 59.07 ? 1001 B12 A N45 1 
HETATM 9824  C  C9  . B12 G 3 .   ? -8.569  81.278  105.245 1.00 42.20 ? 1001 B12 A C9  1 
HETATM 9825  C  C10 . B12 G 3 .   ? -9.649  81.872  105.879 1.00 41.43 ? 1001 B12 A C10 1 
HETATM 9826  C  C11 . B12 G 3 .   ? -10.603 81.260  106.676 1.00 43.20 ? 1001 B12 A C11 1 
HETATM 9827  C  C12 . B12 G 3 .   ? -11.843 81.998  107.274 1.00 42.56 ? 1001 B12 A C12 1 
HETATM 9828  C  C46 . B12 G 3 .   ? -12.759 82.276  106.052 1.00 39.39 ? 1001 B12 A C46 1 
HETATM 9829  C  C47 . B12 G 3 .   ? -11.612 83.389  107.883 1.00 39.23 ? 1001 B12 A C47 1 
HETATM 9830  C  C13 . B12 G 3 .   ? -12.540 80.827  108.027 1.00 44.46 ? 1001 B12 A C13 1 
HETATM 9831  C  C48 . B12 G 3 .   ? -12.471 81.089  109.594 1.00 47.63 ? 1001 B12 A C48 1 
HETATM 9832  C  C49 . B12 G 3 .   ? -13.715 81.553  110.411 1.00 50.07 ? 1001 B12 A C49 1 
HETATM 9833  C  C50 . B12 G 3 .   ? -13.423 81.728  111.845 1.00 52.10 ? 1001 B12 A C50 1 
HETATM 9834  O  O51 . B12 G 3 .   ? -13.889 80.920  112.690 1.00 53.08 ? 1001 B12 A O51 1 
HETATM 9835  N  N52 . B12 G 3 .   ? -12.601 82.804  112.121 1.00 47.95 ? 1001 B12 A N52 1 
HETATM 9836  C  C14 . B12 G 3 .   ? -11.727 79.526  107.781 1.00 40.48 ? 1001 B12 A C14 1 
HETATM 9837  C  C15 . B12 G 3 .   ? -12.073 78.217  108.273 1.00 40.92 ? 1001 B12 A C15 1 
HETATM 9838  C  C53 . B12 G 3 .   ? -13.372 78.088  109.070 1.00 38.12 ? 1001 B12 A C53 1 
HETATM 9839  C  C16 . B12 G 3 .   ? -11.202 77.024  108.021 1.00 39.80 ? 1001 B12 A C16 1 
HETATM 9840  C  C17 . B12 G 3 .   ? -11.442 75.513  108.457 1.00 42.38 ? 1001 B12 A C17 1 
HETATM 9841  C  C54 . B12 G 3 .   ? -12.608 74.895  107.590 1.00 40.27 ? 1001 B12 A C54 1 
HETATM 9842  C  C55 . B12 G 3 .   ? -11.778 75.232  109.982 1.00 41.47 ? 1001 B12 A C55 1 
HETATM 9843  C  C56 . B12 G 3 .   ? -10.935 75.940  111.062 1.00 45.50 ? 1001 B12 A C56 1 
HETATM 9844  C  C57 . B12 G 3 .   ? -11.575 75.832  112.437 1.00 50.05 ? 1001 B12 A C57 1 
HETATM 9845  O  O58 . B12 G 3 .   ? -12.643 76.513  112.653 1.00 50.38 ? 1001 B12 A O58 1 
HETATM 9846  N  N59 . B12 G 3 .   ? -11.011 75.042  113.353 1.00 52.13 ? 1001 B12 A N59 1 
HETATM 9847  C  C18 . B12 G 3 .   ? -10.056 74.868  108.138 1.00 39.72 ? 1001 B12 A C18 1 
HETATM 9848  C  C60 . B12 G 3 .   ? -9.765  73.396  108.055 1.00 36.78 ? 1001 B12 A C60 1 
HETATM 9849  C  C61 . B12 G 3 .   ? -8.607  72.850  108.873 1.00 33.03 ? 1001 B12 A C61 1 
HETATM 9850  O  O63 . B12 G 3 .   ? -8.160  73.426  109.850 1.00 33.37 ? 1001 B12 A O63 1 
HETATM 9851  N  N62 . B12 G 3 .   ? -8.069  71.741  108.492 1.00 35.56 ? 1001 B12 A N62 1 
HETATM 9852  C  C19 . B12 G 3 .   ? -9.522  75.767  106.960 1.00 36.43 ? 1001 B12 A C19 1 
HETATM 9853  C  C1P . B12 G 3 .   ? -11.568 74.889  114.687 1.00 51.59 ? 1001 B12 A C1P 1 
HETATM 9854  C  C2P . B12 G 3 .   ? -11.174 75.981  115.619 1.00 48.55 ? 1001 B12 A C2P 1 
HETATM 9855  C  C3P . B12 G 3 .   ? -11.803 75.788  116.939 1.00 48.71 ? 1001 B12 A C3P 1 
HETATM 9856  O  O3  . B12 G 3 .   ? -9.731  75.886  115.686 1.00 46.23 ? 1001 B12 A O3  1 
HETATM 9857  O  O4  . B12 G 3 .   ? -7.506  76.820  115.746 1.00 42.70 ? 1001 B12 A O4  1 
HETATM 9858  O  O5  . B12 G 3 .   ? -9.374  78.089  116.722 1.00 39.63 ? 1001 B12 A O5  1 
HETATM 9859  P  P   . B12 G 3 .   ? -8.890  77.173  115.649 1.00 43.22 ? 1001 B12 A P   1 
HETATM 9860  O  O2  . B12 G 3 .   ? -9.229  77.718  114.181 1.00 41.70 ? 1001 B12 A O2  1 
HETATM 9861  C  C3R . B12 G 3 .   ? -8.636  78.908  113.794 1.00 40.95 ? 1001 B12 A C3R 1 
HETATM 9862  C  C2R . B12 G 3 .   ? -7.705  78.795  112.687 1.00 41.30 ? 1001 B12 A C2R 1 
HETATM 9863  O  O7R . B12 G 3 .   ? -7.990  77.595  111.974 1.00 41.10 ? 1001 B12 A O7R 1 
HETATM 9864  C  C1R . B12 G 3 .   ? -7.884  80.159  111.871 1.00 39.66 ? 1001 B12 A C1R 1 
HETATM 9865  O  O6R . B12 G 3 .   ? -9.243  80.497  112.062 1.00 45.58 ? 1001 B12 A O6R 1 
HETATM 9866  C  C4R . B12 G 3 .   ? -9.666  79.993  113.425 1.00 44.62 ? 1001 B12 A C4R 1 
HETATM 9867  C  C5R . B12 G 3 .   ? -9.688  81.208  114.339 1.00 40.41 ? 1001 B12 A C5R 1 
HETATM 9868  O  O8R . B12 G 3 .   ? -8.715  81.107  115.388 1.00 46.93 ? 1001 B12 A O8R 1 
HETATM 9869  N  N1B . B12 G 3 .   ? -7.593  79.946  110.435 1.00 38.10 ? 1001 B12 A N1B 1 
HETATM 9870  C  C8B . B12 G 3 .   ? -6.435  80.110  109.784 1.00 35.75 ? 1001 B12 A C8B 1 
HETATM 9871  C  C2B . B12 G 3 .   ? -8.550  79.552  109.477 1.00 39.88 ? 1001 B12 A C2B 1 
HETATM 9872  N  N3B . B12 G 3 .   ? -8.082  79.419  108.240 1.00 40.71 ? 1001 B12 A N3B 1 
HETATM 9873  C  C9B . B12 G 3 .   ? -6.718  79.766  108.406 1.00 38.15 ? 1001 B12 A C9B 1 
HETATM 9874  C  C4B . B12 G 3 .   ? -5.689  79.810  107.447 1.00 38.17 ? 1001 B12 A C4B 1 
HETATM 9875  C  C5B . B12 G 3 .   ? -4.386  80.179  107.748 1.00 41.87 ? 1001 B12 A C5B 1 
HETATM 9876  C  C5M . B12 G 3 .   ? -3.369  80.182  106.642 1.00 41.04 ? 1001 B12 A C5M 1 
HETATM 9877  C  C6B . B12 G 3 .   ? -4.074  80.525  109.175 1.00 41.49 ? 1001 B12 A C6B 1 
HETATM 9878  C  C6M . B12 G 3 .   ? -2.673  80.941  109.596 1.00 39.51 ? 1001 B12 A C6M 1 
HETATM 9879  C  C7B . B12 G 3 .   ? -5.151  80.465  110.145 1.00 35.06 ? 1001 B12 A C7B 1 
HETATM 9880  C  C1  . NAG H 2 .   ? -48.730 92.286  124.005 1.00 87.38 ? 901  NAG C C1  1 
HETATM 9881  C  C2  . NAG H 2 .   ? -48.033 91.197  124.904 1.00 87.41 ? 901  NAG C C2  1 
HETATM 9882  C  C3  . NAG H 2 .   ? -46.649 91.759  125.341 1.00 87.85 ? 901  NAG C C3  1 
HETATM 9883  C  C4  . NAG H 2 .   ? -45.839 92.028  124.033 1.00 89.85 ? 901  NAG C C4  1 
HETATM 9884  C  C5  . NAG H 2 .   ? -46.600 93.100  123.146 1.00 90.48 ? 901  NAG C C5  1 
HETATM 9885  C  C6  . NAG H 2 .   ? -45.910 93.464  121.807 1.00 91.27 ? 901  NAG C C6  1 
HETATM 9886  C  C7  . NAG H 2 .   ? -49.429 89.727  126.532 1.00 87.89 ? 901  NAG C C7  1 
HETATM 9887  C  C8  . NAG H 2 .   ? -49.279 88.431  125.780 1.00 87.20 ? 901  NAG C C8  1 
HETATM 9888  N  N2  . NAG H 2 .   ? -48.868 90.909  126.114 1.00 86.24 ? 901  NAG C N2  1 
HETATM 9889  O  O3  . NAG H 2 .   ? -45.994 90.781  126.159 1.00 86.73 ? 901  NAG C O3  1 
HETATM 9890  O  O4  . NAG H 2 .   ? -44.552 92.564  124.390 1.00 94.35 ? 901  NAG C O4  1 
HETATM 9891  O  O5  . NAG H 2 .   ? -47.959 92.636  122.835 1.00 88.59 ? 901  NAG C O5  1 
HETATM 9892  O  O6  . NAG H 2 .   ? -46.360 92.664  120.710 1.00 89.47 ? 901  NAG C O6  1 
HETATM 9893  O  O7  . NAG H 2 .   ? -50.096 89.663  127.571 1.00 87.40 ? 901  NAG C O7  1 
HETATM 9894  C  C1  . NAG I 2 .   ? -43.346 91.933  123.782 1.00 95.93 ? 902  NAG C C1  1 
HETATM 9895  C  C2  . NAG I 2 .   ? -42.188 92.880  123.453 1.00 97.22 ? 902  NAG C C2  1 
HETATM 9896  C  C3  . NAG I 2 .   ? -40.975 92.089  122.907 1.00 98.60 ? 902  NAG C C3  1 
HETATM 9897  C  C4  . NAG I 2 .   ? -40.635 90.865  123.807 1.00 99.45 ? 902  NAG C C4  1 
HETATM 9898  C  C5  . NAG I 2 .   ? -41.952 90.037  124.074 1.00 98.59 ? 902  NAG C C5  1 
HETATM 9899  C  C6  . NAG I 2 .   ? -41.727 88.799  124.945 1.00 99.45 ? 902  NAG C C6  1 
HETATM 9900  C  C7  . NAG I 2 .   ? -42.530 95.214  122.507 1.00 99.45 ? 902  NAG C C7  1 
HETATM 9901  C  C8  . NAG I 2 .   ? -43.472 96.038  121.664 1.00 98.88 ? 902  NAG C C8  1 
HETATM 9902  N  N2  . NAG I 2 .   ? -42.703 93.863  122.467 1.00 98.80 ? 902  NAG C N2  1 
HETATM 9903  O  O3  . NAG I 2 .   ? -39.844 92.927  122.916 1.00 99.45 ? 902  NAG C O3  1 
HETATM 9904  O  O4  . NAG I 2 .   ? -39.634 90.063  123.159 1.00 99.45 ? 902  NAG C O4  1 
HETATM 9905  O  O5  . NAG I 2 .   ? -42.928 90.929  124.725 1.00 97.27 ? 902  NAG C O5  1 
HETATM 9906  O  O6  . NAG I 2 .   ? -41.909 87.651  124.131 1.00 99.45 ? 902  NAG C O6  1 
HETATM 9907  O  O7  . NAG I 2 .   ? -41.654 95.793  123.176 1.00 99.44 ? 902  NAG C O7  1 
HETATM 9908  CO CO  . B12 J 3 .   ? -55.465 80.967  114.484 1.00 65.00 ? 1002 B12 C CO  1 
HETATM 9909  N  N21 . B12 J 3 .   ? -56.560 79.574  115.114 1.00 45.07 ? 1002 B12 C N21 1 
HETATM 9910  N  N22 . B12 J 3 .   ? -56.183 82.235  115.770 1.00 48.74 ? 1002 B12 C N22 1 
HETATM 9911  N  N23 . B12 J 3 .   ? -54.145 82.254  113.652 1.00 45.76 ? 1002 B12 C N23 1 
HETATM 9912  N  N24 . B12 J 3 .   ? -54.639 79.539  113.440 1.00 37.90 ? 1002 B12 C N24 1 
HETATM 9913  C  C1  . B12 J 3 .   ? -56.558 78.214  114.358 1.00 41.98 ? 1002 B12 C C1  1 
HETATM 9914  C  C20 . B12 J 3 .   ? -57.485 78.392  113.126 1.00 40.75 ? 1002 B12 C C20 1 
HETATM 9915  C  C2  . B12 J 3 .   ? -57.126 77.168  115.473 1.00 42.60 ? 1002 B12 C C2  1 
HETATM 9916  C  C25 . B12 J 3 .   ? -57.977 76.010  114.860 1.00 40.01 ? 1002 B12 C C25 1 
HETATM 9917  C  C26 . B12 J 3 .   ? -55.949 76.563  116.300 1.00 40.35 ? 1002 B12 C C26 1 
HETATM 9918  C  C27 . B12 J 3 .   ? -56.374 75.584  117.400 1.00 38.59 ? 1002 B12 C C27 1 
HETATM 9919  O  O28 . B12 J 3 .   ? -56.890 76.047  118.394 1.00 43.20 ? 1002 B12 C O28 1 
HETATM 9920  N  N29 . B12 J 3 .   ? -56.184 74.295  117.129 1.00 37.60 ? 1002 B12 C N29 1 
HETATM 9921  C  C3  . B12 J 3 .   ? -58.003 78.149  116.394 1.00 41.28 ? 1002 B12 C C3  1 
HETATM 9922  C  C30 . B12 J 3 .   ? -59.605 78.250  116.123 1.00 39.58 ? 1002 B12 C C30 1 
HETATM 9923  C  C31 . B12 J 3 .   ? -60.436 77.398  117.034 1.00 42.10 ? 1002 B12 C C31 1 
HETATM 9924  C  C32 . B12 J 3 .   ? -61.923 77.743  117.061 1.00 45.20 ? 1002 B12 C C32 1 
HETATM 9925  O  O34 . B12 J 3 .   ? -62.752 76.955  117.571 1.00 48.45 ? 1002 B12 C O34 1 
HETATM 9926  N  N33 . B12 J 3 .   ? -62.262 78.887  116.511 1.00 41.73 ? 1002 B12 C N33 1 
HETATM 9927  C  C4  . B12 J 3 .   ? -57.327 79.537  116.226 1.00 43.68 ? 1002 B12 C C4  1 
HETATM 9928  C  C5  . B12 J 3 .   ? -57.599 80.679  117.103 1.00 47.68 ? 1002 B12 C C5  1 
HETATM 9929  C  C35 . B12 J 3 .   ? -58.521 80.383  118.322 1.00 51.65 ? 1002 B12 C C35 1 
HETATM 9930  C  C6  . B12 J 3 .   ? -57.043 81.970  116.852 1.00 46.72 ? 1002 B12 C C6  1 
HETATM 9931  C  C7  . B12 J 3 .   ? -57.293 83.245  117.682 1.00 50.08 ? 1002 B12 C C7  1 
HETATM 9932  C  C36 . B12 J 3 .   ? -58.776 83.609  118.142 1.00 48.60 ? 1002 B12 C C36 1 
HETATM 9933  C  C37 . B12 J 3 .   ? -56.327 83.128  118.950 1.00 51.39 ? 1002 B12 C C37 1 
HETATM 9934  C  C38 . B12 J 3 .   ? -56.375 84.268  119.989 1.00 50.85 ? 1002 B12 C C38 1 
HETATM 9935  O  O39 . B12 J 3 .   ? -56.040 85.383  119.672 1.00 52.31 ? 1002 B12 C O39 1 
HETATM 9936  N  N40 . B12 J 3 .   ? -56.833 83.913  121.206 1.00 48.52 ? 1002 B12 C N40 1 
HETATM 9937  C  C8  . B12 J 3 .   ? -56.589 84.383  116.886 1.00 50.70 ? 1002 B12 C C8  1 
HETATM 9938  C  C41 . B12 J 3 .   ? -57.776 85.403  116.407 1.00 54.78 ? 1002 B12 C C41 1 
HETATM 9939  C  C42 . B12 J 3 .   ? -57.520 86.678  115.626 1.00 61.72 ? 1002 B12 C C42 1 
HETATM 9940  C  C43 . B12 J 3 .   ? -58.701 87.647  115.581 1.00 60.94 ? 1002 B12 C C43 1 
HETATM 9941  O  O44 . B12 J 3 .   ? -59.911 87.212  115.634 1.00 60.22 ? 1002 B12 C O44 1 
HETATM 9942  N  N45 . B12 J 3 .   ? -58.413 88.916  115.458 1.00 60.07 ? 1002 B12 C N45 1 
HETATM 9943  C  C9  . B12 J 3 .   ? -55.857 83.581  115.792 1.00 48.39 ? 1002 B12 C C9  1 
HETATM 9944  C  C10 . B12 J 3 .   ? -54.925 84.210  114.980 1.00 44.84 ? 1002 B12 C C10 1 
HETATM 9945  C  C11 . B12 J 3 .   ? -54.124 83.639  113.992 1.00 45.98 ? 1002 B12 C C11 1 
HETATM 9946  C  C12 . B12 J 3 .   ? -53.047 84.419  113.168 1.00 46.86 ? 1002 B12 C C12 1 
HETATM 9947  C  C46 . B12 J 3 .   ? -51.933 84.774  114.205 1.00 46.11 ? 1002 B12 C C46 1 
HETATM 9948  C  C47 . B12 J 3 .   ? -53.468 85.784  112.567 1.00 43.63 ? 1002 B12 C C47 1 
HETATM 9949  C  C13 . B12 J 3 .   ? -52.472 83.286  112.282 1.00 46.47 ? 1002 B12 C C13 1 
HETATM 9950  C  C48 . B12 J 3 .   ? -52.795 83.594  110.767 1.00 49.46 ? 1002 B12 C C48 1 
HETATM 9951  C  C49 . B12 J 3 .   ? -51.668 84.088  109.829 1.00 56.56 ? 1002 B12 C C49 1 
HETATM 9952  C  C50 . B12 J 3 .   ? -52.109 84.339  108.455 1.00 60.87 ? 1002 B12 C C50 1 
HETATM 9953  O  O51 . B12 J 3 .   ? -51.750 83.577  107.535 1.00 66.62 ? 1002 B12 C O51 1 
HETATM 9954  N  N52 . B12 J 3 .   ? -52.923 85.436  108.320 1.00 58.57 ? 1002 B12 C N52 1 
HETATM 9955  C  C14 . B12 J 3 .   ? -53.187 81.964  112.653 1.00 42.93 ? 1002 B12 C C14 1 
HETATM 9956  C  C15 . B12 J 3 .   ? -52.912 80.654  112.083 1.00 40.38 ? 1002 B12 C C15 1 
HETATM 9957  C  C53 . B12 J 3 .   ? -51.791 80.541  111.043 1.00 41.65 ? 1002 B12 C C53 1 
HETATM 9958  C  C16 . B12 J 3 .   ? -53.691 79.438  112.497 1.00 38.61 ? 1002 B12 C C16 1 
HETATM 9959  C  C17 . B12 J 3 .   ? -53.488 77.949  112.038 1.00 41.05 ? 1002 B12 C C17 1 
HETATM 9960  C  C54 . B12 J 3 .   ? -52.118 77.437  112.653 1.00 37.15 ? 1002 B12 C C54 1 
HETATM 9961  C  C55 . B12 J 3 .   ? -53.470 77.660  110.503 1.00 40.26 ? 1002 B12 C C55 1 
HETATM 9962  C  C56 . B12 J 3 .   ? -54.425 78.449  109.604 1.00 45.28 ? 1002 B12 C C56 1 
HETATM 9963  C  C57 . B12 J 3 .   ? -53.942 78.366  108.196 1.00 49.33 ? 1002 B12 C C57 1 
HETATM 9964  O  O58 . B12 J 3 .   ? -52.792 78.890  107.932 1.00 47.42 ? 1002 B12 C O58 1 
HETATM 9965  N  N59 . B12 J 3 .   ? -54.721 77.744  107.324 1.00 51.12 ? 1002 B12 C N59 1 
HETATM 9966  C  C18 . B12 J 3 .   ? -54.736 77.230  112.624 1.00 39.49 ? 1002 B12 C C18 1 
HETATM 9967  C  C60 . B12 J 3 .   ? -54.934 75.723  112.790 1.00 44.60 ? 1002 B12 C C60 1 
HETATM 9968  C  C61 . B12 J 3 .   ? -56.140 75.014  112.111 1.00 45.34 ? 1002 B12 C C61 1 
HETATM 9969  O  O63 . B12 J 3 .   ? -56.883 75.599  111.307 1.00 46.72 ? 1002 B12 C O63 1 
HETATM 9970  N  N62 . B12 J 3 .   ? -56.381 73.752  112.426 1.00 38.28 ? 1002 B12 C N62 1 
HETATM 9971  C  C19 . B12 J 3 .   ? -55.060 78.121  113.864 1.00 41.48 ? 1002 B12 C C19 1 
HETATM 9972  C  C1P . B12 J 3 .   ? -54.387 77.565  105.940 1.00 48.13 ? 1002 B12 C C1P 1 
HETATM 9973  C  C2P . B12 J 3 .   ? -55.017 78.524  105.032 1.00 43.65 ? 1002 B12 C C2P 1 
HETATM 9974  C  C3P . B12 J 3 .   ? -54.584 78.245  103.661 1.00 46.55 ? 1002 B12 C C3P 1 
HETATM 9975  O  O3  . B12 J 3 .   ? -56.449 78.338  105.166 1.00 47.59 ? 1002 B12 C O3  1 
HETATM 9976  O  O4  . B12 J 3 .   ? -58.700 79.190  105.419 1.00 44.96 ? 1002 B12 C O4  1 
HETATM 9977  O  O5  . B12 J 3 .   ? -57.032 80.555  104.267 1.00 40.87 ? 1002 B12 C O5  1 
HETATM 9978  P  P   . B12 J 3 .   ? -57.327 79.597  105.343 1.00 44.82 ? 1002 B12 C P   1 
HETATM 9979  O  O2  . B12 J 3 .   ? -56.770 80.094  106.770 1.00 49.58 ? 1002 B12 C O2  1 
HETATM 9980  C  C3R . B12 J 3 .   ? -57.262 81.269  107.335 1.00 47.62 ? 1002 B12 C C3R 1 
HETATM 9981  C  C2R . B12 J 3 .   ? -57.990 81.084  108.575 1.00 47.82 ? 1002 B12 C C2R 1 
HETATM 9982  O  O7R . B12 J 3 .   ? -57.514 79.880  109.152 1.00 42.63 ? 1002 B12 C O7R 1 
HETATM 9983  C  C1R . B12 J 3 .   ? -57.665 82.366  109.402 1.00 48.48 ? 1002 B12 C C1R 1 
HETATM 9984  O  O6R . B12 J 3 .   ? -56.334 82.629  109.053 1.00 48.63 ? 1002 B12 C O6R 1 
HETATM 9985  C  C4R . B12 J 3 .   ? -56.137 82.264  107.635 1.00 48.98 ? 1002 B12 C C4R 1 
HETATM 9986  C  C5R . B12 J 3 .   ? -56.121 83.585  106.850 1.00 49.19 ? 1002 B12 C C5R 1 
HETATM 9987  O  O8R . B12 J 3 .   ? -57.194 83.689  105.934 1.00 59.76 ? 1002 B12 C O8R 1 
HETATM 9988  N  N1B . B12 J 3 .   ? -57.744 82.137  110.862 1.00 50.46 ? 1002 B12 C N1B 1 
HETATM 9989  C  C8B . B12 J 3 .   ? -58.819 82.241  111.692 1.00 50.93 ? 1002 B12 C C8B 1 
HETATM 9990  C  C2B . B12 J 3 .   ? -56.677 81.718  111.642 1.00 48.37 ? 1002 B12 C C2B 1 
HETATM 9991  N  N3B . B12 J 3 .   ? -56.964 81.556  112.942 1.00 51.74 ? 1002 B12 C N3B 1 
HETATM 9992  C  C9B . B12 J 3 .   ? -58.321 81.896  113.003 1.00 50.31 ? 1002 B12 C C9B 1 
HETATM 9993  C  C4B . B12 J 3 .   ? -59.192 81.902  114.117 1.00 49.28 ? 1002 B12 C C4B 1 
HETATM 9994  C  C5B . B12 J 3 .   ? -60.525 82.261  114.038 1.00 49.98 ? 1002 B12 C C5B 1 
HETATM 9995  C  C5M . B12 J 3 .   ? -61.335 82.236  115.293 1.00 51.14 ? 1002 B12 C C5M 1 
HETATM 9996  C  C6B . B12 J 3 .   ? -61.074 82.639  112.701 1.00 50.36 ? 1002 B12 C C6B 1 
HETATM 9997  C  C6M . B12 J 3 .   ? -62.525 83.036  112.559 1.00 49.12 ? 1002 B12 C C6M 1 
HETATM 9998  C  C7B . B12 J 3 .   ? -60.172 82.628  111.556 1.00 49.79 ? 1002 B12 C C7B 1 
HETATM 9999  O  O   . HOH K 4 .   ? -6.957  69.255  114.689 1.00 27.18 ? 1002 HOH A O   1 
HETATM 10000 O  O   . HOH K 4 .   ? 1.525   76.630  113.387 1.00 32.54 ? 1003 HOH A O   1 
HETATM 10001 O  O   . HOH K 4 .   ? -24.413 66.773  104.885 1.00 42.65 ? 1004 HOH A O   1 
HETATM 10002 O  O   . HOH K 4 .   ? -18.286 57.969  126.981 1.00 53.31 ? 1005 HOH A O   1 
HETATM 10003 O  O   . HOH K 4 .   ? -4.243  70.238  107.577 1.00 30.03 ? 1006 HOH A O   1 
HETATM 10004 O  O   . HOH K 4 .   ? 7.110   68.267  104.435 1.00 39.80 ? 1007 HOH A O   1 
HETATM 10005 O  O   . HOH K 4 .   ? 3.178   72.972  105.473 1.00 40.41 ? 1008 HOH A O   1 
HETATM 10006 O  O   . HOH K 4 .   ? -8.699  73.040  132.941 1.00 43.85 ? 1009 HOH A O   1 
HETATM 10007 O  O   . HOH K 4 .   ? -23.613 79.242  112.424 1.00 55.51 ? 1010 HOH A O   1 
HETATM 10008 O  O   . HOH K 4 .   ? 7.341   57.428  98.938  1.00 56.60 ? 1011 HOH A O   1 
HETATM 10009 O  O   . HOH K 4 .   ? 0.417   50.989  126.609 1.00 51.63 ? 1012 HOH A O   1 
HETATM 10010 O  O   . HOH K 4 .   ? -2.209  78.290  95.570  1.00 67.82 ? 1013 HOH A O   1 
HETATM 10011 O  O   . HOH K 4 .   ? -24.497 56.540  125.308 1.00 27.90 ? 1014 HOH A O   1 
HETATM 10012 O  O   . HOH K 4 .   ? 10.662  66.210  119.699 1.00 57.45 ? 1015 HOH A O   1 
HETATM 10013 O  O   . HOH K 4 .   ? -10.608 73.948  133.613 1.00 53.60 ? 1016 HOH A O   1 
HETATM 10014 O  O   . HOH K 4 .   ? -6.724  71.738  133.945 1.00 48.46 ? 1017 HOH A O   1 
HETATM 10015 O  O   . HOH K 4 .   ? -23.626 50.550  117.085 1.00 54.68 ? 1018 HOH A O   1 
HETATM 10016 O  O   . HOH K 4 .   ? -20.779 55.536  107.026 1.00 34.45 ? 1019 HOH A O   1 
HETATM 10017 O  O   . HOH K 4 .   ? -8.124  74.814  112.216 1.00 27.76 ? 1020 HOH A O   1 
HETATM 10018 O  O   . HOH K 4 .   ? -1.852  56.122  120.773 1.00 38.14 ? 1021 HOH A O   1 
HETATM 10019 O  O   . HOH K 4 .   ? -4.645  62.454  110.623 1.00 37.99 ? 1022 HOH A O   1 
HETATM 10020 O  O   . HOH K 4 .   ? -20.106 75.899  102.174 1.00 39.41 ? 1023 HOH A O   1 
HETATM 10021 O  O   . HOH K 4 .   ? 3.015   82.224  110.653 1.00 55.57 ? 1024 HOH A O   1 
HETATM 10022 O  O   . HOH K 4 .   ? -3.774  66.552  105.323 1.00 33.24 ? 1025 HOH A O   1 
HETATM 10023 O  O   . HOH K 4 .   ? -6.208  67.258  107.102 1.00 32.12 ? 1026 HOH A O   1 
HETATM 10024 O  O   . HOH K 4 .   ? -3.870  66.786  115.755 1.00 36.92 ? 1027 HOH A O   1 
HETATM 10025 O  O   . HOH K 4 .   ? 15.201  69.000  121.016 1.00 39.00 ? 1028 HOH A O   1 
HETATM 10026 O  O   . HOH K 4 .   ? -9.730  55.235  115.601 1.00 35.99 ? 1029 HOH A O   1 
HETATM 10027 O  O   . HOH K 4 .   ? -23.126 54.974  107.991 1.00 33.40 ? 1030 HOH A O   1 
HETATM 10028 O  O   . HOH K 4 .   ? 0.448   80.379  108.019 1.00 40.86 ? 1031 HOH A O   1 
HETATM 10029 O  O   . HOH K 4 .   ? -11.821 78.902  117.068 1.00 63.78 ? 1032 HOH A O   1 
HETATM 10030 O  O   . HOH K 4 .   ? -2.437  83.981  106.303 1.00 32.74 ? 1033 HOH A O   1 
HETATM 10031 O  O   . HOH K 4 .   ? -32.143 56.694  107.402 1.00 42.93 ? 1034 HOH A O   1 
HETATM 10032 O  O   . HOH K 4 .   ? -7.707  73.868  114.838 1.00 28.50 ? 1035 HOH A O   1 
HETATM 10033 O  O   . HOH K 4 .   ? 1.898   75.125  120.676 1.00 42.51 ? 1036 HOH A O   1 
HETATM 10034 O  O   . HOH K 4 .   ? -2.298  68.175  106.977 1.00 37.07 ? 1037 HOH A O   1 
HETATM 10035 O  O   . HOH K 4 .   ? 0.377   53.580  109.299 1.00 54.18 ? 1038 HOH A O   1 
HETATM 10036 O  O   . HOH K 4 .   ? 3.531   75.586  118.065 1.00 52.45 ? 1039 HOH A O   1 
HETATM 10037 O  O   . HOH K 4 .   ? 10.185  87.837  88.793  1.00 61.04 ? 1040 HOH A O   1 
HETATM 10038 O  O   . HOH K 4 .   ? 8.708   71.084  129.965 1.00 50.92 ? 1041 HOH A O   1 
HETATM 10039 O  O   . HOH K 4 .   ? 3.687   75.979  122.497 1.00 32.26 ? 1042 HOH A O   1 
HETATM 10040 O  O   . HOH K 4 .   ? -8.834  71.622  114.229 1.00 32.27 ? 1043 HOH A O   1 
HETATM 10041 O  O   . HOH K 4 .   ? -17.347 76.538  104.323 1.00 43.99 ? 1044 HOH A O   1 
HETATM 10042 O  O   . HOH K 4 .   ? -29.282 73.515  108.972 1.00 44.23 ? 1045 HOH A O   1 
HETATM 10043 O  O   . HOH K 4 .   ? -13.079 64.064  125.530 1.00 50.10 ? 1046 HOH A O   1 
HETATM 10044 O  O   . HOH K 4 .   ? -8.874  62.784  131.815 1.00 41.17 ? 1047 HOH A O   1 
HETATM 10045 O  O   . HOH K 4 .   ? -12.902 67.781  137.593 1.00 42.47 ? 1048 HOH A O   1 
HETATM 10046 O  O   . HOH K 4 .   ? -31.561 73.637  103.414 1.00 49.58 ? 1049 HOH A O   1 
HETATM 10047 O  O   . HOH K 4 .   ? -6.190  57.706  110.048 1.00 51.94 ? 1050 HOH A O   1 
HETATM 10048 O  O   . HOH K 4 .   ? -23.622 80.077  115.554 1.00 56.32 ? 1051 HOH A O   1 
HETATM 10049 O  O   . HOH K 4 .   ? -33.236 63.731  121.778 1.00 35.61 ? 1052 HOH A O   1 
HETATM 10050 O  O   . HOH K 4 .   ? 7.669   56.345  132.140 1.00 52.59 ? 1053 HOH A O   1 
HETATM 10051 O  O   . HOH K 4 .   ? -1.286  75.158  134.775 1.00 57.72 ? 1054 HOH A O   1 
HETATM 10052 O  O   . HOH K 4 .   ? -15.133 83.285  100.893 1.00 68.65 ? 1055 HOH A O   1 
HETATM 10053 O  O   . HOH K 4 .   ? -14.432 56.081  96.892  1.00 43.26 ? 1056 HOH A O   1 
HETATM 10054 O  O   . HOH K 4 .   ? -14.827 67.424  133.594 1.00 49.47 ? 1057 HOH A O   1 
HETATM 10055 O  O   . HOH K 4 .   ? 3.068   80.095  113.611 1.00 62.65 ? 1058 HOH A O   1 
HETATM 10056 O  O   . HOH K 4 .   ? -19.771 78.467  101.792 1.00 61.81 ? 1059 HOH A O   1 
HETATM 10057 O  O   . HOH K 4 .   ? -11.505 85.401  110.515 1.00 44.32 ? 1060 HOH A O   1 
HETATM 10058 O  O   . HOH K 4 .   ? 1.327   78.961  115.471 1.00 43.36 ? 1061 HOH A O   1 
HETATM 10059 O  O   . HOH K 4 .   ? 4.039   64.675  95.405  1.00 42.86 ? 1062 HOH A O   1 
HETATM 10060 O  O   . HOH K 4 .   ? 1.390   75.617  115.875 1.00 49.30 ? 1063 HOH A O   1 
HETATM 10061 O  O   . HOH K 4 .   ? -30.914 53.460  118.006 1.00 45.46 ? 1064 HOH A O   1 
HETATM 10062 O  O   . HOH K 4 .   ? -4.343  78.230  122.591 1.00 52.07 ? 1065 HOH A O   1 
HETATM 10063 O  O   . HOH K 4 .   ? -6.664  85.658  129.515 1.00 56.02 ? 1066 HOH A O   1 
HETATM 10064 O  O   . HOH K 4 .   ? -17.514 79.189  120.114 1.00 44.05 ? 1067 HOH A O   1 
HETATM 10065 O  O   . HOH K 4 .   ? -6.422  52.905  127.799 1.00 64.07 ? 1068 HOH A O   1 
HETATM 10066 O  O   . HOH K 4 .   ? -17.205 78.927  109.251 1.00 64.44 ? 1069 HOH A O   1 
HETATM 10067 O  O   . HOH K 4 .   ? -4.621  55.549  121.566 1.00 51.34 ? 1070 HOH A O   1 
HETATM 10068 O  O   . HOH K 4 .   ? 13.673  69.902  114.786 1.00 40.96 ? 1071 HOH A O   1 
HETATM 10069 O  O   . HOH K 4 .   ? 3.152   79.823  117.565 1.00 48.54 ? 1072 HOH A O   1 
HETATM 10070 O  O   . HOH K 4 .   ? 1.686   73.773  99.693  1.00 56.31 ? 1073 HOH A O   1 
HETATM 10071 O  O   . HOH K 4 .   ? -29.938 66.496  103.101 1.00 75.36 ? 1074 HOH A O   1 
HETATM 10072 O  O   . HOH K 4 .   ? -14.068 83.151  122.748 1.00 52.35 ? 1075 HOH A O   1 
HETATM 10073 O  O   . HOH K 4 .   ? 5.178   75.380  101.208 1.00 53.93 ? 1076 HOH A O   1 
HETATM 10074 O  O   . HOH K 4 .   ? -16.008 86.023  97.114  1.00 59.43 ? 1077 HOH A O   1 
HETATM 10075 O  O   . HOH K 4 .   ? -3.609  50.174  95.559  1.00 54.31 ? 1078 HOH A O   1 
HETATM 10076 O  O   . HOH K 4 .   ? 0.258   78.527  106.532 1.00 37.66 ? 1079 HOH A O   1 
HETATM 10077 O  O   . HOH K 4 .   ? 1.070   67.192  138.863 1.00 56.49 ? 1080 HOH A O   1 
HETATM 10078 O  O   . HOH K 4 .   ? -0.845  55.673  123.812 1.00 55.59 ? 1081 HOH A O   1 
HETATM 10079 O  O   . HOH K 4 .   ? 5.426   76.794  108.603 1.00 58.55 ? 1082 HOH A O   1 
HETATM 10080 O  O   . HOH K 4 .   ? 8.127   47.944  105.293 1.00 88.51 ? 1083 HOH A O   1 
HETATM 10081 O  O   . HOH K 4 .   ? -6.669  63.610  89.959  1.00 57.23 ? 1084 HOH A O   1 
HETATM 10082 O  O   . HOH K 4 .   ? -6.476  52.644  116.295 1.00 55.26 ? 1085 HOH A O   1 
HETATM 10083 O  O   . HOH K 4 .   ? -18.532 66.234  97.725  1.00 45.70 ? 1086 HOH A O   1 
HETATM 10084 O  O   . HOH K 4 .   ? -25.520 75.268  98.517  1.00 72.50 ? 1087 HOH A O   1 
HETATM 10085 O  O   . HOH K 4 .   ? -15.290 76.900  116.908 1.00 42.13 ? 1088 HOH A O   1 
HETATM 10086 O  O   . HOH K 4 .   ? -23.387 78.328  122.292 1.00 55.53 ? 1089 HOH A O   1 
HETATM 10087 O  O   . HOH K 4 .   ? -1.671  49.250  127.230 1.00 63.51 ? 1090 HOH A O   1 
HETATM 10088 O  O   . HOH K 4 .   ? -15.907 78.623  111.756 1.00 58.73 ? 1091 HOH A O   1 
HETATM 10089 O  O   . HOH K 4 .   ? -2.429  87.555  117.799 1.00 52.40 ? 1092 HOH A O   1 
HETATM 10090 O  O   . HOH K 4 .   ? -16.995 75.994  112.928 1.00 42.73 ? 1093 HOH A O   1 
HETATM 10091 O  O   . HOH K 4 .   ? -9.157  97.268  88.496  1.00 62.98 ? 1094 HOH A O   1 
HETATM 10092 O  O   . HOH K 4 .   ? -27.456 52.682  94.957  1.00 57.85 ? 1095 HOH A O   1 
HETATM 10093 O  O   . HOH K 4 .   ? 2.983   79.781  109.124 1.00 54.97 ? 1096 HOH A O   1 
HETATM 10094 O  O   . HOH K 4 .   ? 12.759  73.200  121.299 1.00 46.80 ? 1097 HOH A O   1 
HETATM 10095 O  O   . HOH K 4 .   ? -4.399  51.659  117.944 1.00 60.35 ? 1098 HOH A O   1 
HETATM 10096 O  O   . HOH K 4 .   ? -23.853 47.808  93.680  1.00 69.14 ? 1099 HOH A O   1 
HETATM 10097 O  O   . HOH K 4 .   ? 15.618  68.353  115.596 1.00 41.64 ? 1100 HOH A O   1 
HETATM 10098 O  O   . HOH K 4 .   ? 1.013   83.725  92.622  1.00 67.27 ? 1101 HOH A O   1 
HETATM 10099 O  O   . HOH K 4 .   ? -29.779 69.031  125.285 1.00 93.85 ? 1102 HOH A O   1 
HETATM 10100 O  O   . HOH K 4 .   ? 2.914   84.360  93.694  1.00 52.04 ? 1103 HOH A O   1 
HETATM 10101 O  O   . HOH K 4 .   ? 15.871  91.810  90.168  1.00 72.75 ? 1104 HOH A O   1 
HETATM 10102 O  O   . HOH K 4 .   ? -8.172  77.237  134.223 1.00 63.80 ? 1105 HOH A O   1 
HETATM 10103 O  O   . HOH K 4 .   ? -30.763 58.803  132.634 1.00 61.14 ? 1106 HOH A O   1 
HETATM 10104 O  O   . HOH K 4 .   ? -5.090  76.692  135.889 1.00 73.03 ? 1107 HOH A O   1 
HETATM 10105 O  O   . HOH K 4 .   ? -6.675  76.673  121.952 1.00 66.95 ? 1108 HOH A O   1 
HETATM 10106 O  O   . HOH K 4 .   ? -8.304  53.048  106.802 1.00 63.55 ? 1109 HOH A O   1 
HETATM 10107 O  O   . HOH K 4 .   ? -21.679 81.055  127.688 1.00 70.97 ? 1110 HOH A O   1 
HETATM 10108 O  O   . HOH K 4 .   ? 3.863   106.811 99.164  1.00 61.36 ? 1111 HOH A O   1 
HETATM 10109 O  O   . HOH K 4 .   ? -2.887  56.851  89.636  1.00 56.22 ? 1112 HOH A O   1 
HETATM 10110 O  O   . HOH K 4 .   ? -10.223 79.339  132.975 1.00 54.56 ? 1113 HOH A O   1 
HETATM 10111 O  O   . HOH K 4 .   ? 0.434   60.665  126.815 1.00 50.09 ? 1114 HOH A O   1 
HETATM 10112 O  O   . HOH K 4 .   ? -23.744 80.590  125.101 1.00 74.22 ? 1115 HOH A O   1 
HETATM 10113 O  O   . HOH K 4 .   ? 3.522   60.320  125.369 1.00 54.33 ? 1116 HOH A O   1 
HETATM 10114 O  O   . HOH K 4 .   ? -8.042  77.263  95.857  1.00 82.31 ? 1117 HOH A O   1 
HETATM 10115 O  O   . HOH K 4 .   ? -27.637 49.719  122.313 1.00 62.32 ? 1118 HOH A O   1 
HETATM 10116 O  O   . HOH K 4 .   ? -8.668  88.492  107.403 1.00 44.39 ? 1119 HOH A O   1 
HETATM 10117 O  O   . HOH K 4 .   ? -7.599  60.379  83.686  1.00 59.69 ? 1120 HOH A O   1 
HETATM 10118 O  O   . HOH K 4 .   ? -0.328  58.137  95.197  1.00 57.61 ? 1121 HOH A O   1 
HETATM 10119 O  O   . HOH K 4 .   ? -27.089 65.296  101.375 1.00 56.91 ? 1122 HOH A O   1 
HETATM 10120 O  O   . HOH K 4 .   ? -24.669 81.472  122.326 1.00 62.14 ? 1123 HOH A O   1 
HETATM 10121 O  O   . HOH K 4 .   ? 1.854   102.442 106.541 1.00 94.56 ? 1124 HOH A O   1 
HETATM 10122 O  O   . HOH K 4 .   ? -11.871 66.663  94.405  1.00 70.64 ? 1125 HOH A O   1 
HETATM 10123 O  O   . HOH K 4 .   ? 8.360   74.646  111.271 1.00 46.46 ? 1126 HOH A O   1 
HETATM 10124 O  O   . HOH K 4 .   ? -0.992  86.852  88.944  1.00 65.41 ? 1127 HOH A O   1 
HETATM 10125 O  O   . HOH K 4 .   ? -12.627 53.388  115.877 1.00 51.06 ? 1128 HOH A O   1 
HETATM 10126 O  O   . HOH K 4 .   ? -14.344 105.146 98.567  1.00 75.83 ? 1129 HOH A O   1 
HETATM 10127 O  O   . HOH K 4 .   ? -17.396 81.599  112.559 1.00 61.32 ? 1130 HOH A O   1 
HETATM 10128 O  O   . HOH K 4 .   ? 1.031   73.160  137.145 1.00 65.25 ? 1131 HOH A O   1 
HETATM 10129 O  O   . HOH K 4 .   ? -20.728 55.370  127.760 1.00 67.55 ? 1132 HOH A O   1 
HETATM 10130 O  O   . HOH K 4 .   ? 10.795  57.056  133.087 1.00 60.54 ? 1133 HOH A O   1 
HETATM 10131 O  O   . HOH K 4 .   ? 12.858  91.597  99.782  1.00 57.32 ? 1134 HOH A O   1 
HETATM 10132 O  O   . HOH K 4 .   ? -11.613 80.745  101.818 1.00 56.29 ? 1135 HOH A O   1 
HETATM 10133 O  O   . HOH K 4 .   ? 12.563  72.601  115.546 1.00 68.72 ? 1136 HOH A O   1 
HETATM 10134 O  O   . HOH L 4 .   ? -20.561 23.670  133.341 1.00 32.49 ? 400  HOH B O   1 
HETATM 10135 O  O   . HOH L 4 .   ? -15.872 64.085  149.404 1.00 51.34 ? 401  HOH B O   1 
HETATM 10136 O  O   . HOH L 4 .   ? -17.591 40.458  139.266 1.00 41.21 ? 402  HOH B O   1 
HETATM 10137 O  O   . HOH L 4 .   ? -18.199 31.728  141.935 1.00 33.65 ? 403  HOH B O   1 
HETATM 10138 O  O   . HOH L 4 .   ? -13.272 31.435  137.260 1.00 33.45 ? 404  HOH B O   1 
HETATM 10139 O  O   . HOH L 4 .   ? -15.810 31.639  137.875 1.00 28.11 ? 405  HOH B O   1 
HETATM 10140 O  O   . HOH L 4 .   ? -23.179 33.231  143.932 1.00 40.93 ? 406  HOH B O   1 
HETATM 10141 O  O   . HOH L 4 .   ? -15.836 66.773  149.621 1.00 40.11 ? 407  HOH B O   1 
HETATM 10142 O  O   . HOH L 4 .   ? -28.135 47.409  116.351 1.00 50.96 ? 408  HOH B O   1 
HETATM 10143 O  O   . HOH L 4 .   ? -24.366 42.939  123.731 1.00 45.28 ? 409  HOH B O   1 
HETATM 10144 O  O   . HOH L 4 .   ? -18.529 39.682  135.036 1.00 32.68 ? 410  HOH B O   1 
HETATM 10145 O  O   . HOH L 4 .   ? -4.751  60.270  135.172 1.00 43.87 ? 411  HOH B O   1 
HETATM 10146 O  O   . HOH L 4 .   ? -21.852 41.351  141.073 1.00 36.35 ? 412  HOH B O   1 
HETATM 10147 O  O   . HOH L 4 .   ? -12.584 18.239  134.921 1.00 45.06 ? 413  HOH B O   1 
HETATM 10148 O  O   . HOH L 4 .   ? -8.263  44.129  128.413 1.00 36.78 ? 414  HOH B O   1 
HETATM 10149 O  O   . HOH L 4 .   ? -16.348 32.892  140.299 1.00 37.27 ? 415  HOH B O   1 
HETATM 10150 O  O   . HOH L 4 .   ? -10.027 50.046  131.715 1.00 45.10 ? 416  HOH B O   1 
HETATM 10151 O  O   . HOH L 4 .   ? 2.484   44.438  160.440 1.00 48.77 ? 417  HOH B O   1 
HETATM 10152 O  O   . HOH L 4 .   ? -28.091 27.247  135.645 1.00 43.64 ? 418  HOH B O   1 
HETATM 10153 O  O   . HOH L 4 .   ? -18.342 46.075  122.163 1.00 40.88 ? 419  HOH B O   1 
HETATM 10154 O  O   . HOH L 4 .   ? -8.561  62.409  134.461 1.00 42.44 ? 420  HOH B O   1 
HETATM 10155 O  O   . HOH L 4 .   ? 3.782   44.232  136.883 1.00 55.79 ? 421  HOH B O   1 
HETATM 10156 O  O   . HOH L 4 .   ? -17.169 46.179  148.975 1.00 42.86 ? 422  HOH B O   1 
HETATM 10157 O  O   . HOH L 4 .   ? -18.689 49.297  151.320 1.00 46.67 ? 423  HOH B O   1 
HETATM 10158 O  O   . HOH L 4 .   ? -25.033 33.420  141.031 1.00 52.94 ? 424  HOH B O   1 
HETATM 10159 O  O   . HOH L 4 .   ? -16.781 40.843  142.029 1.00 45.29 ? 425  HOH B O   1 
HETATM 10160 O  O   . HOH L 4 .   ? -28.919 54.660  138.591 1.00 63.58 ? 426  HOH B O   1 
HETATM 10161 O  O   . HOH L 4 .   ? -16.575 44.411  123.844 1.00 50.01 ? 427  HOH B O   1 
HETATM 10162 O  O   . HOH L 4 .   ? -32.124 40.714  136.955 1.00 45.77 ? 428  HOH B O   1 
HETATM 10163 O  O   . HOH L 4 .   ? 4.855   58.683  137.865 1.00 60.07 ? 429  HOH B O   1 
HETATM 10164 O  O   . HOH L 4 .   ? -36.737 43.791  128.828 1.00 50.26 ? 430  HOH B O   1 
HETATM 10165 O  O   . HOH L 4 .   ? -34.078 38.573  123.108 1.00 53.37 ? 431  HOH B O   1 
HETATM 10166 O  O   . HOH L 4 .   ? -24.718 48.789  108.412 1.00 67.84 ? 432  HOH B O   1 
HETATM 10167 O  O   . HOH L 4 .   ? -8.842  55.922  132.346 1.00 57.15 ? 433  HOH B O   1 
HETATM 10168 O  O   . HOH L 4 .   ? -0.201  28.829  147.234 1.00 63.97 ? 434  HOH B O   1 
HETATM 10169 O  O   . HOH L 4 .   ? 1.809   42.630  150.571 1.00 63.93 ? 435  HOH B O   1 
HETATM 10170 O  O   . HOH L 4 .   ? -27.070 56.471  138.720 1.00 82.09 ? 436  HOH B O   1 
HETATM 10171 O  O   . HOH L 4 .   ? -9.619  45.331  161.581 1.00 80.70 ? 437  HOH B O   1 
HETATM 10172 O  O   . HOH L 4 .   ? -29.629 40.300  137.451 1.00 51.58 ? 438  HOH B O   1 
HETATM 10173 O  O   . HOH L 4 .   ? -33.621 36.003  131.311 1.00 45.92 ? 439  HOH B O   1 
HETATM 10174 O  O   . HOH L 4 .   ? -12.502 50.180  156.081 1.00 46.38 ? 440  HOH B O   1 
HETATM 10175 O  O   . HOH L 4 .   ? -13.677 44.607  150.390 1.00 54.64 ? 441  HOH B O   1 
HETATM 10176 O  O   . HOH L 4 .   ? -6.491  35.003  130.248 1.00 65.57 ? 442  HOH B O   1 
HETATM 10177 O  O   . HOH L 4 .   ? 1.740   41.930  147.277 1.00 56.35 ? 443  HOH B O   1 
HETATM 10178 O  O   . HOH L 4 .   ? -27.297 61.055  145.025 1.00 55.76 ? 444  HOH B O   1 
HETATM 10179 O  O   . HOH L 4 .   ? -3.741  39.597  148.661 1.00 48.82 ? 445  HOH B O   1 
HETATM 10180 O  O   . HOH L 4 .   ? -38.555 51.550  127.502 1.00 72.36 ? 446  HOH B O   1 
HETATM 10181 O  O   . HOH L 4 .   ? -3.511  46.886  155.900 1.00 50.67 ? 447  HOH B O   1 
HETATM 10182 O  O   . HOH L 4 .   ? -23.081 24.379  132.183 1.00 46.64 ? 448  HOH B O   1 
HETATM 10183 O  O   . HOH L 4 .   ? -29.587 33.424  126.724 1.00 53.60 ? 449  HOH B O   1 
HETATM 10184 O  O   . HOH L 4 .   ? -9.164  42.883  125.224 1.00 47.78 ? 450  HOH B O   1 
HETATM 10185 O  O   . HOH L 4 .   ? -9.942  52.611  129.936 1.00 61.57 ? 451  HOH B O   1 
HETATM 10186 O  O   . HOH L 4 .   ? -12.019 47.833  153.280 1.00 58.31 ? 452  HOH B O   1 
HETATM 10187 O  O   . HOH L 4 .   ? -22.816 56.885  150.667 1.00 56.58 ? 453  HOH B O   1 
HETATM 10188 O  O   . HOH L 4 .   ? 4.385   35.549  133.112 1.00 70.99 ? 454  HOH B O   1 
HETATM 10189 O  O   . HOH L 4 .   ? -25.621 32.717  144.059 1.00 60.93 ? 455  HOH B O   1 
HETATM 10190 O  O   . HOH L 4 .   ? -35.253 50.750  143.985 1.00 75.24 ? 456  HOH B O   1 
HETATM 10191 O  O   . HOH L 4 .   ? -4.910  68.577  136.449 1.00 57.80 ? 457  HOH B O   1 
HETATM 10192 O  O   . HOH L 4 .   ? -19.624 43.180  121.610 1.00 66.24 ? 458  HOH B O   1 
HETATM 10193 O  O   . HOH L 4 .   ? -22.880 43.390  143.396 1.00 52.93 ? 459  HOH B O   1 
HETATM 10194 O  O   . HOH L 4 .   ? -7.920  61.902  149.051 1.00 67.65 ? 460  HOH B O   1 
HETATM 10195 O  O   . HOH L 4 .   ? -8.500  63.966  147.887 1.00 55.17 ? 461  HOH B O   1 
HETATM 10196 O  O   . HOH L 4 .   ? -0.806  42.174  149.238 1.00 61.73 ? 462  HOH B O   1 
HETATM 10197 O  O   . HOH L 4 .   ? 9.446   62.409  131.946 1.00 49.84 ? 463  HOH B O   1 
HETATM 10198 O  O   . HOH L 4 .   ? 1.697   38.054  132.525 1.00 55.06 ? 464  HOH B O   1 
HETATM 10199 O  O   . HOH L 4 .   ? -2.598  18.357  135.521 1.00 53.19 ? 465  HOH B O   1 
HETATM 10200 O  O   . HOH L 4 .   ? -28.080 61.279  138.656 1.00 59.34 ? 466  HOH B O   1 
HETATM 10201 O  O   . HOH L 4 .   ? -40.333 40.531  141.322 1.00 66.86 ? 467  HOH B O   1 
HETATM 10202 O  O   . HOH L 4 .   ? -1.707  62.549  143.843 1.00 92.43 ? 468  HOH B O   1 
HETATM 10203 O  O   . HOH L 4 .   ? -31.183 53.993  151.538 1.00 65.31 ? 469  HOH B O   1 
HETATM 10204 O  O   . HOH L 4 .   ? -10.070 35.775  141.144 1.00 52.12 ? 470  HOH B O   1 
HETATM 10205 O  O   . HOH L 4 .   ? -32.168 56.483  136.343 1.00 70.12 ? 471  HOH B O   1 
HETATM 10206 O  O   . HOH L 4 .   ? -1.455  62.509  146.402 1.00 74.49 ? 472  HOH B O   1 
HETATM 10207 O  O   . HOH L 4 .   ? 0.736   31.182  127.209 1.00 86.11 ? 473  HOH B O   1 
HETATM 10208 O  O   . HOH L 4 .   ? 9.409   60.561  134.521 1.00 90.02 ? 474  HOH B O   1 
HETATM 10209 O  O   . HOH L 4 .   ? 3.725   29.010  136.103 1.00 84.48 ? 475  HOH B O   1 
HETATM 10210 O  O   . HOH L 4 .   ? 3.029   39.563  159.973 1.00 76.78 ? 476  HOH B O   1 
HETATM 10211 O  O   . HOH L 4 .   ? -35.056 52.925  142.460 1.00 99.45 ? 477  HOH B O   1 
HETATM 10212 O  O   . HOH L 4 .   ? -24.502 45.252  151.460 1.00 72.69 ? 478  HOH B O   1 
HETATM 10213 O  O   . HOH L 4 .   ? -10.622 47.683  156.225 1.00 72.89 ? 479  HOH B O   1 
HETATM 10214 O  O   . HOH L 4 .   ? -34.340 46.044  124.432 1.00 78.84 ? 480  HOH B O   1 
HETATM 10215 O  O   . HOH L 4 .   ? -31.220 27.583  127.753 1.00 57.26 ? 481  HOH B O   1 
HETATM 10216 O  O   . HOH L 4 .   ? -16.161 55.381  130.887 1.00 66.15 ? 482  HOH B O   1 
HETATM 10217 O  O   . HOH L 4 .   ? -6.427  32.783  147.673 1.00 73.36 ? 483  HOH B O   1 
HETATM 10218 O  O   . HOH L 4 .   ? -24.707 22.902  135.537 1.00 34.27 ? 484  HOH B O   1 
HETATM 10219 O  O   . HOH L 4 .   ? -31.829 53.817  154.295 1.00 73.75 ? 485  HOH B O   1 
HETATM 10220 O  O   . HOH L 4 .   ? -1.214  24.362  126.022 1.00 65.28 ? 486  HOH B O   1 
HETATM 10221 O  O   . HOH L 4 .   ? 7.601   55.497  145.150 1.00 66.57 ? 487  HOH B O   1 
HETATM 10222 O  O   . HOH L 4 .   ? 2.660   41.298  162.958 1.00 57.73 ? 488  HOH B O   1 
HETATM 10223 O  O   . HOH L 4 .   ? 6.979   33.229  139.781 1.00 75.91 ? 489  HOH B O   1 
HETATM 10224 O  O   . HOH L 4 .   ? -18.301 43.133  145.652 1.00 62.42 ? 490  HOH B O   1 
HETATM 10225 O  O   . HOH L 4 .   ? -23.659 27.253  119.932 1.00 71.28 ? 491  HOH B O   1 
HETATM 10226 O  O   . HOH L 4 .   ? -10.032 58.725  132.355 1.00 62.40 ? 492  HOH B O   1 
HETATM 10227 O  O   . HOH L 4 .   ? -34.345 53.297  144.885 1.00 85.78 ? 493  HOH B O   1 
HETATM 10228 O  O   . HOH L 4 .   ? -20.578 27.290  116.480 1.00 67.17 ? 494  HOH B O   1 
HETATM 10229 O  O   . HOH L 4 .   ? -23.645 23.390  125.763 1.00 60.09 ? 495  HOH B O   1 
HETATM 10230 O  O   . HOH L 4 .   ? -24.414 49.505  152.703 1.00 71.92 ? 496  HOH B O   1 
HETATM 10231 O  O   . HOH L 4 .   ? 0.626   36.190  156.290 1.00 65.55 ? 497  HOH B O   1 
HETATM 10232 O  O   . HOH L 4 .   ? -33.042 56.370  142.637 1.00 55.74 ? 498  HOH B O   1 
HETATM 10233 O  O   . HOH L 4 .   ? -35.461 33.010  130.408 1.00 62.69 ? 499  HOH B O   1 
HETATM 10234 O  O   . HOH M 4 .   ? -76.294 73.837  117.580 1.00 69.18 ? 1094 HOH C O   1 
HETATM 10235 O  O   . HOH M 4 .   ? -79.185 68.144  89.499  1.00 99.45 ? 1095 HOH C O   1 
HETATM 10236 O  O   . HOH M 4 .   ? -34.913 77.326  110.150 1.00 39.58 ? 1096 HOH C O   1 
HETATM 10237 O  O   . HOH M 4 .   ? -53.255 60.880  98.959  1.00 33.04 ? 1097 HOH C O   1 
HETATM 10238 O  O   . HOH M 4 .   ? -58.760 71.672  106.725 1.00 33.62 ? 1098 HOH C O   1 
HETATM 10239 O  O   . HOH M 4 .   ? -59.853 77.933  102.943 1.00 39.51 ? 1099 HOH C O   1 
HETATM 10240 O  O   . HOH M 4 .   ? -39.935 71.134  113.292 1.00 50.42 ? 1100 HOH C O   1 
HETATM 10241 O  O   . HOH M 4 .   ? -81.022 69.499  106.335 1.00 40.59 ? 1101 HOH C O   1 
HETATM 10242 O  O   . HOH M 4 .   ? -75.064 66.903  119.594 1.00 31.99 ? 1102 HOH C O   1 
HETATM 10243 O  O   . HOH M 4 .   ? -60.399 72.376  114.055 1.00 40.03 ? 1103 HOH C O   1 
HETATM 10244 O  O   . HOH M 4 .   ? -60.696 75.730  104.420 1.00 33.02 ? 1104 HOH C O   1 
HETATM 10245 O  O   . HOH M 4 .   ? -46.676 78.942  115.030 1.00 37.82 ? 1105 HOH C O   1 
HETATM 10246 O  O   . HOH M 4 .   ? -72.293 61.326  109.759 1.00 44.50 ? 1106 HOH C O   1 
HETATM 10247 O  O   . HOH M 4 .   ? -37.685 76.534  98.548  1.00 54.89 ? 1107 HOH C O   1 
HETATM 10248 O  O   . HOH M 4 .   ? -70.173 69.800  119.530 1.00 47.03 ? 1108 HOH C O   1 
HETATM 10249 O  O   . HOH M 4 .   ? -60.219 81.250  105.007 1.00 50.33 ? 1109 HOH C O   1 
HETATM 10250 O  O   . HOH M 4 .   ? -76.752 68.195  88.217  1.00 79.64 ? 1110 HOH C O   1 
HETATM 10251 O  O   . HOH M 4 .   ? -68.938 83.954  101.665 1.00 42.77 ? 1111 HOH C O   1 
HETATM 10252 O  O   . HOH M 4 .   ? -44.016 79.011  116.184 1.00 39.76 ? 1112 HOH C O   1 
HETATM 10253 O  O   . HOH M 4 .   ? -54.747 81.675  103.686 1.00 46.64 ? 1113 HOH C O   1 
HETATM 10254 O  O   . HOH M 4 .   ? -68.773 76.443  102.356 1.00 42.40 ? 1114 HOH C O   1 
HETATM 10255 O  O   . HOH M 4 .   ? -64.571 79.984  116.423 1.00 41.75 ? 1115 HOH C O   1 
HETATM 10256 O  O   . HOH M 4 .   ? -55.678 57.738  105.397 1.00 54.96 ? 1116 HOH C O   1 
HETATM 10257 O  O   . HOH M 4 .   ? -56.934 73.846  106.969 1.00 40.68 ? 1117 HOH C O   1 
HETATM 10258 O  O   . HOH M 4 .   ? -74.252 66.090  117.082 1.00 35.83 ? 1118 HOH C O   1 
HETATM 10259 O  O   . HOH M 4 .   ? -35.856 68.857  116.106 1.00 47.93 ? 1119 HOH C O   1 
HETATM 10260 O  O   . HOH M 4 .   ? -66.527 78.260  109.952 1.00 45.12 ? 1120 HOH C O   1 
HETATM 10261 O  O   . HOH M 4 .   ? -50.739 69.566  125.029 1.00 46.38 ? 1121 HOH C O   1 
HETATM 10262 O  O   . HOH M 4 .   ? -57.264 77.225  108.858 1.00 37.90 ? 1122 HOH C O   1 
HETATM 10263 O  O   . HOH M 4 .   ? -60.035 64.278  110.927 1.00 42.70 ? 1123 HOH C O   1 
HETATM 10264 O  O   . HOH M 4 .   ? -56.566 90.309  133.763 1.00 81.69 ? 1124 HOH C O   1 
HETATM 10265 O  O   . HOH M 4 .   ? -59.296 82.269  88.365  1.00 48.04 ? 1125 HOH C O   1 
HETATM 10266 O  O   . HOH M 4 .   ? -61.385 68.580  82.274  1.00 45.67 ? 1126 HOH C O   1 
HETATM 10267 O  O   . HOH M 4 .   ? -45.526 73.048  114.119 1.00 42.73 ? 1127 HOH C O   1 
HETATM 10268 O  O   . HOH M 4 .   ? -60.281 79.163  100.488 1.00 48.46 ? 1128 HOH C O   1 
HETATM 10269 O  O   . HOH M 4 .   ? -58.090 69.299  114.483 1.00 44.83 ? 1129 HOH C O   1 
HETATM 10270 O  O   . HOH M 4 .   ? -70.610 77.594  100.615 1.00 41.27 ? 1130 HOH C O   1 
HETATM 10271 O  O   . HOH M 4 .   ? -66.446 75.287  117.855 1.00 50.58 ? 1131 HOH C O   1 
HETATM 10272 O  O   . HOH M 4 .   ? -73.677 57.936  107.770 1.00 57.96 ? 1132 HOH C O   1 
HETATM 10273 O  O   . HOH M 4 .   ? -43.128 58.491  111.542 1.00 50.95 ? 1133 HOH C O   1 
HETATM 10274 O  O   . HOH M 4 .   ? -61.719 70.355  115.071 1.00 51.42 ? 1134 HOH C O   1 
HETATM 10275 O  O   . HOH M 4 .   ? -46.184 74.788  122.017 1.00 61.62 ? 1135 HOH C O   1 
HETATM 10276 O  O   . HOH M 4 .   ? -63.013 80.404  99.361  1.00 39.62 ? 1136 HOH C O   1 
HETATM 10277 O  O   . HOH M 4 .   ? -47.854 88.166  121.740 1.00 76.95 ? 1137 HOH C O   1 
HETATM 10278 O  O   . HOH M 4 .   ? -66.007 57.524  98.533  1.00 46.05 ? 1138 HOH C O   1 
HETATM 10279 O  O   . HOH M 4 .   ? -76.796 64.907  119.868 1.00 44.35 ? 1139 HOH C O   1 
HETATM 10280 O  O   . HOH M 4 .   ? -77.773 78.873  98.713  1.00 60.54 ? 1140 HOH C O   1 
HETATM 10281 O  O   . HOH M 4 .   ? -75.915 58.191  92.073  1.00 50.03 ? 1141 HOH C O   1 
HETATM 10282 O  O   . HOH M 4 .   ? -74.584 59.647  124.170 1.00 77.50 ? 1142 HOH C O   1 
HETATM 10283 O  O   . HOH M 4 .   ? -49.458 82.332  99.698  1.00 48.48 ? 1143 HOH C O   1 
HETATM 10284 O  O   . HOH M 4 .   ? -49.602 74.561  119.042 1.00 60.08 ? 1144 HOH C O   1 
HETATM 10285 O  O   . HOH M 4 .   ? -70.687 62.429  94.948  1.00 61.00 ? 1145 HOH C O   1 
HETATM 10286 O  O   . HOH M 4 .   ? -73.446 61.934  127.627 1.00 63.73 ? 1146 HOH C O   1 
HETATM 10287 O  O   . HOH M 4 .   ? -70.761 78.651  115.552 1.00 70.33 ? 1147 HOH C O   1 
HETATM 10288 O  O   . HOH M 4 .   ? -77.534 67.697  105.500 1.00 55.10 ? 1148 HOH C O   1 
HETATM 10289 O  O   . HOH M 4 .   ? -62.197 56.587  114.491 1.00 54.96 ? 1149 HOH C O   1 
HETATM 10290 O  O   . HOH M 4 .   ? -45.874 60.597  89.785  1.00 56.45 ? 1150 HOH C O   1 
HETATM 10291 O  O   . HOH M 4 .   ? -62.540 100.674 125.078 1.00 66.74 ? 1151 HOH C O   1 
HETATM 10292 O  O   . HOH M 4 .   ? -48.450 81.739  110.397 1.00 51.07 ? 1152 HOH C O   1 
HETATM 10293 O  O   . HOH M 4 .   ? -49.043 78.895  106.397 1.00 41.41 ? 1153 HOH C O   1 
HETATM 10294 O  O   . HOH M 4 .   ? -36.135 77.220  107.676 1.00 43.83 ? 1154 HOH C O   1 
HETATM 10295 O  O   . HOH M 4 .   ? -73.456 59.344  103.377 1.00 53.76 ? 1155 HOH C O   1 
HETATM 10296 O  O   . HOH M 4 .   ? -40.968 73.190  114.487 1.00 48.00 ? 1156 HOH C O   1 
HETATM 10297 O  O   . HOH M 4 .   ? -79.859 73.038  103.834 1.00 56.66 ? 1157 HOH C O   1 
HETATM 10298 O  O   . HOH M 4 .   ? -63.914 60.314  127.615 1.00 60.09 ? 1158 HOH C O   1 
HETATM 10299 O  O   . HOH M 4 .   ? -65.517 81.597  114.520 1.00 49.61 ? 1159 HOH C O   1 
HETATM 10300 O  O   . HOH M 4 .   ? -75.759 59.309  121.366 1.00 63.35 ? 1160 HOH C O   1 
HETATM 10301 O  O   . HOH M 4 .   ? -58.169 59.336  110.946 1.00 42.43 ? 1161 HOH C O   1 
HETATM 10302 O  O   . HOH M 4 .   ? -69.026 82.421  136.535 1.00 68.85 ? 1162 HOH C O   1 
HETATM 10303 O  O   . HOH M 4 .   ? -57.281 70.056  82.790  1.00 53.08 ? 1163 HOH C O   1 
HETATM 10304 O  O   . HOH M 4 .   ? -64.976 90.005  104.386 1.00 56.06 ? 1164 HOH C O   1 
HETATM 10305 O  O   . HOH M 4 .   ? -52.135 65.562  130.762 1.00 51.15 ? 1165 HOH C O   1 
HETATM 10306 O  O   . HOH M 4 .   ? -58.213 76.308  106.415 1.00 48.99 ? 1166 HOH C O   1 
HETATM 10307 O  O   . HOH M 4 .   ? -68.507 77.537  122.247 1.00 55.80 ? 1167 HOH C O   1 
HETATM 10308 O  O   . HOH M 4 .   ? -73.743 80.188  95.120  1.00 66.66 ? 1168 HOH C O   1 
HETATM 10309 O  O   . HOH M 4 .   ? -55.550 63.007  92.298  1.00 54.14 ? 1169 HOH C O   1 
HETATM 10310 O  O   . HOH M 4 .   ? -76.714 73.900  103.099 1.00 50.08 ? 1170 HOH C O   1 
HETATM 10311 O  O   . HOH M 4 .   ? -67.848 62.684  96.059  1.00 41.63 ? 1171 HOH C O   1 
HETATM 10312 O  O   . HOH M 4 .   ? -31.395 64.935  96.517  1.00 48.55 ? 1172 HOH C O   1 
HETATM 10313 O  O   . HOH M 4 .   ? -68.074 56.459  111.847 1.00 47.82 ? 1173 HOH C O   1 
HETATM 10314 O  O   . HOH M 4 .   ? -49.253 72.513  82.975  1.00 62.33 ? 1174 HOH C O   1 
HETATM 10315 O  O   . HOH M 4 .   ? -58.938 84.283  104.191 1.00 63.45 ? 1175 HOH C O   1 
HETATM 10316 O  O   . HOH M 4 .   ? -73.583 55.914  110.406 1.00 49.12 ? 1176 HOH C O   1 
HETATM 10317 O  O   . HOH M 4 .   ? -31.875 62.507  97.432  1.00 71.48 ? 1177 HOH C O   1 
HETATM 10318 O  O   . HOH M 4 .   ? -58.856 79.159  126.781 1.00 76.08 ? 1178 HOH C O   1 
HETATM 10319 O  O   . HOH M 4 .   ? -61.798 63.419  127.855 1.00 86.26 ? 1179 HOH C O   1 
HETATM 10320 O  O   . HOH M 4 .   ? -81.032 68.569  90.909  1.00 78.80 ? 1180 HOH C O   1 
HETATM 10321 O  O   . HOH M 4 .   ? -73.390 62.120  94.876  1.00 72.80 ? 1181 HOH C O   1 
HETATM 10322 O  O   . HOH M 4 .   ? -35.226 79.436  106.023 1.00 51.00 ? 1182 HOH C O   1 
HETATM 10323 O  O   . HOH M 4 .   ? -53.385 85.791  97.485  1.00 54.53 ? 1183 HOH C O   1 
HETATM 10324 O  O   . HOH M 4 .   ? -43.040 82.716  106.312 1.00 57.98 ? 1184 HOH C O   1 
HETATM 10325 O  O   . HOH M 4 .   ? -61.955 78.897  97.289  1.00 63.32 ? 1185 HOH C O   1 
HETATM 10326 O  O   . HOH M 4 .   ? -72.944 73.948  119.895 1.00 61.45 ? 1186 HOH C O   1 
HETATM 10327 O  O   . HOH M 4 .   ? -67.822 95.641  137.318 1.00 71.48 ? 1187 HOH C O   1 
HETATM 10328 O  O   . HOH M 4 .   ? -71.246 80.323  119.848 1.00 76.29 ? 1188 HOH C O   1 
HETATM 10329 O  O   . HOH M 4 .   ? -37.976 78.607  109.221 1.00 58.75 ? 1189 HOH C O   1 
HETATM 10330 O  O   . HOH M 4 .   ? -61.943 74.660  87.686  1.00 37.47 ? 1190 HOH C O   1 
HETATM 10331 O  O   . HOH M 4 .   ? -71.037 53.009  94.143  1.00 56.24 ? 1191 HOH C O   1 
HETATM 10332 O  O   . HOH M 4 .   ? -61.950 69.446  127.139 1.00 72.12 ? 1192 HOH C O   1 
HETATM 10333 O  O   . HOH M 4 .   ? -48.891 60.753  92.156  1.00 53.92 ? 1193 HOH C O   1 
HETATM 10334 O  O   . HOH M 4 .   ? -76.428 96.927  135.943 1.00 64.53 ? 1194 HOH C O   1 
HETATM 10335 O  O   . HOH M 4 .   ? -59.484 67.535  131.930 1.00 99.12 ? 1195 HOH C O   1 
HETATM 10336 O  O   . HOH M 4 .   ? -49.495 65.832  130.900 1.00 66.51 ? 1196 HOH C O   1 
HETATM 10337 O  O   . HOH M 4 .   ? -63.808 74.890  123.811 1.00 59.65 ? 1197 HOH C O   1 
HETATM 10338 O  O   . HOH M 4 .   ? -52.917 58.686  97.245  1.00 67.20 ? 1198 HOH C O   1 
HETATM 10339 O  O   . HOH M 4 .   ? -33.139 56.585  101.573 1.00 53.86 ? 1199 HOH C O   1 
HETATM 10340 O  O   . HOH M 4 .   ? -76.522 86.404  102.841 1.00 73.89 ? 1200 HOH C O   1 
HETATM 10341 O  O   . HOH M 4 .   ? -67.855 81.080  133.910 1.00 81.99 ? 1201 HOH C O   1 
HETATM 10342 O  O   . HOH M 4 .   ? -70.919 78.919  91.544  1.00 47.47 ? 1202 HOH C O   1 
HETATM 10343 O  O   . HOH M 4 .   ? -74.490 72.133  118.194 1.00 79.58 ? 1203 HOH C O   1 
HETATM 10344 O  O   . HOH M 4 .   ? -53.952 73.957  125.105 1.00 47.14 ? 1204 HOH C O   1 
HETATM 10345 O  O   . HOH M 4 .   ? -72.024 49.923  96.306  1.00 62.21 ? 1205 HOH C O   1 
HETATM 10346 O  O   . HOH M 4 .   ? -67.005 54.725  107.674 1.00 58.37 ? 1206 HOH C O   1 
HETATM 10347 O  O   . HOH M 4 .   ? -75.586 92.026  118.109 1.00 68.89 ? 1207 HOH C O   1 
HETATM 10348 O  O   . HOH M 4 .   ? -71.942 80.467  117.143 1.00 64.30 ? 1208 HOH C O   1 
HETATM 10349 O  O   . HOH M 4 .   ? -55.171 79.417  82.862  1.00 49.94 ? 1209 HOH C O   1 
HETATM 10350 O  O   . HOH M 4 .   ? -32.361 77.039  114.231 1.00 55.88 ? 1210 HOH C O   1 
HETATM 10351 O  O   . HOH M 4 .   ? -60.116 54.243  126.546 1.00 89.38 ? 1211 HOH C O   1 
HETATM 10352 O  O   . HOH M 4 .   ? -54.251 79.240  125.031 1.00 72.00 ? 1212 HOH C O   1 
HETATM 10353 O  O   . HOH M 4 .   ? -39.711 53.661  111.021 1.00 69.45 ? 1213 HOH C O   1 
HETATM 10354 O  O   . HOH M 4 .   ? -76.068 60.169  94.678  1.00 57.87 ? 1214 HOH C O   1 
HETATM 10355 O  O   . HOH M 4 .   ? -67.608 80.962  86.503  1.00 81.20 ? 1215 HOH C O   1 
HETATM 10356 O  O   . HOH M 4 .   ? -50.959 89.614  123.567 1.00 87.68 ? 1216 HOH C O   1 
HETATM 10357 O  O   . HOH M 4 .   ? -54.179 53.122  111.117 1.00 75.17 ? 1217 HOH C O   1 
HETATM 10358 O  O   . HOH M 4 .   ? -48.511 95.896  103.387 1.00 85.68 ? 1218 HOH C O   1 
HETATM 10359 O  O   . HOH M 4 .   ? -49.770 83.197  90.471  1.00 53.67 ? 1219 HOH C O   1 
HETATM 10360 O  O   . HOH M 4 .   ? -48.539 95.304  126.099 1.00 65.85 ? 1220 HOH C O   1 
HETATM 10361 O  O   . HOH M 4 .   ? -71.283 89.300  135.811 1.00 91.11 ? 1221 HOH C O   1 
HETATM 10362 O  O   . HOH M 4 .   ? -76.626 93.178  124.929 1.00 63.25 ? 1222 HOH C O   1 
HETATM 10363 O  O   . HOH N 4 .   ? -52.715 42.458  80.561  1.00 27.67 ? 400  HOH D O   1 
HETATM 10364 O  O   . HOH N 4 .   ? -50.894 69.855  69.331  1.00 45.62 ? 401  HOH D O   1 
HETATM 10365 O  O   . HOH N 4 .   ? -50.779 42.096  84.755  1.00 33.02 ? 402  HOH D O   1 
HETATM 10366 O  O   . HOH N 4 .   ? -46.151 38.320  96.291  1.00 41.77 ? 403  HOH D O   1 
HETATM 10367 O  O   . HOH N 4 .   ? -48.767 43.729  78.231  1.00 33.74 ? 404  HOH D O   1 
HETATM 10368 O  O   . HOH N 4 .   ? -64.284 62.992  87.243  1.00 52.04 ? 405  HOH D O   1 
HETATM 10369 O  O   . HOH N 4 .   ? -71.694 44.504  73.753  1.00 49.04 ? 406  HOH D O   1 
HETATM 10370 O  O   . HOH N 4 .   ? -41.839 54.911  98.122  1.00 67.66 ? 407  HOH D O   1 
HETATM 10371 O  O   . HOH N 4 .   ? -52.215 33.858  77.995  1.00 33.49 ? 408  HOH D O   1 
HETATM 10372 O  O   . HOH N 4 .   ? -48.746 26.003  86.335  1.00 36.85 ? 409  HOH D O   1 
HETATM 10373 O  O   . HOH N 4 .   ? -41.248 30.989  79.207  1.00 60.01 ? 410  HOH D O   1 
HETATM 10374 O  O   . HOH N 4 .   ? -53.980 56.318  67.356  1.00 43.62 ? 411  HOH D O   1 
HETATM 10375 O  O   . HOH N 4 .   ? -59.374 43.826  66.165  1.00 46.64 ? 412  HOH D O   1 
HETATM 10376 O  O   . HOH N 4 .   ? -53.776 43.053  77.954  1.00 51.38 ? 413  HOH D O   1 
HETATM 10377 O  O   . HOH N 4 .   ? -53.586 51.546  68.495  1.00 40.99 ? 414  HOH D O   1 
HETATM 10378 O  O   . HOH N 4 .   ? -72.571 45.831  86.630  1.00 44.18 ? 415  HOH D O   1 
HETATM 10379 O  O   . HOH N 4 .   ? -55.790 39.191  87.442  1.00 29.48 ? 416  HOH D O   1 
HETATM 10380 O  O   . HOH N 4 .   ? -35.488 38.491  85.701  1.00 46.28 ? 417  HOH D O   1 
HETATM 10381 O  O   . HOH N 4 .   ? -60.150 46.651  93.045  1.00 39.19 ? 418  HOH D O   1 
HETATM 10382 O  O   . HOH N 4 .   ? -58.137 46.229  70.485  1.00 48.94 ? 419  HOH D O   1 
HETATM 10383 O  O   . HOH N 4 .   ? -42.423 63.485  79.632  1.00 46.31 ? 420  HOH D O   1 
HETATM 10384 O  O   . HOH N 4 .   ? -74.747 60.701  85.705  1.00 68.18 ? 421  HOH D O   1 
HETATM 10385 O  O   . HOH N 4 .   ? -75.698 52.477  71.966  1.00 65.80 ? 422  HOH D O   1 
HETATM 10386 O  O   . HOH N 4 .   ? -48.108 35.148  75.315  1.00 58.35 ? 423  HOH D O   1 
HETATM 10387 O  O   . HOH N 4 .   ? -45.340 47.607  95.023  1.00 55.31 ? 424  HOH D O   1 
HETATM 10388 O  O   . HOH N 4 .   ? -58.763 53.429  89.350  1.00 58.01 ? 425  HOH D O   1 
HETATM 10389 O  O   . HOH N 4 .   ? -31.637 46.840  80.043  1.00 50.13 ? 426  HOH D O   1 
HETATM 10390 O  O   . HOH N 4 .   ? -69.615 42.771  71.508  1.00 63.48 ? 427  HOH D O   1 
HETATM 10391 O  O   . HOH N 4 .   ? -72.361 38.733  88.922  1.00 51.24 ? 428  HOH D O   1 
HETATM 10392 O  O   . HOH N 4 .   ? -45.389 36.888  98.477  1.00 56.03 ? 429  HOH D O   1 
HETATM 10393 O  O   . HOH N 4 .   ? -40.902 56.000  66.060  1.00 66.61 ? 430  HOH D O   1 
HETATM 10394 O  O   . HOH N 4 .   ? -69.965 24.552  82.075  1.00 54.28 ? 431  HOH D O   1 
HETATM 10395 O  O   . HOH N 4 .   ? -62.148 55.529  89.322  1.00 49.22 ? 432  HOH D O   1 
HETATM 10396 O  O   . HOH N 4 .   ? -45.866 26.544  86.610  1.00 56.44 ? 433  HOH D O   1 
HETATM 10397 O  O   . HOH N 4 .   ? -67.781 41.875  73.405  1.00 48.24 ? 434  HOH D O   1 
HETATM 10398 O  O   . HOH N 4 .   ? -54.555 48.870  70.809  1.00 38.20 ? 435  HOH D O   1 
HETATM 10399 O  O   . HOH N 4 .   ? -60.372 64.348  87.048  1.00 47.60 ? 436  HOH D O   1 
HETATM 10400 O  O   . HOH N 4 .   ? -64.212 70.834  86.679  1.00 45.91 ? 437  HOH D O   1 
HETATM 10401 O  O   . HOH N 4 .   ? -37.895 43.061  80.506  1.00 51.43 ? 438  HOH D O   1 
HETATM 10402 O  O   . HOH N 4 .   ? -60.034 49.983  67.717  1.00 59.27 ? 439  HOH D O   1 
HETATM 10403 O  O   . HOH N 4 .   ? -53.771 34.035  82.580  1.00 25.52 ? 440  HOH D O   1 
HETATM 10404 O  O   . HOH N 4 .   ? -31.997 50.854  92.943  1.00 81.43 ? 441  HOH D O   1 
HETATM 10405 O  O   . HOH N 4 .   ? -59.181 40.081  91.399  1.00 51.53 ? 442  HOH D O   1 
HETATM 10406 O  O   . HOH N 4 .   ? -76.575 30.319  93.390  1.00 58.42 ? 443  HOH D O   1 
HETATM 10407 O  O   . HOH N 4 .   ? -40.502 42.486  80.348  1.00 43.99 ? 444  HOH D O   1 
HETATM 10408 O  O   . HOH N 4 .   ? -56.345 46.760  98.075  1.00 54.88 ? 445  HOH D O   1 
HETATM 10409 O  O   . HOH N 4 .   ? -29.935 53.029  93.341  1.00 63.35 ? 446  HOH D O   1 
HETATM 10410 O  O   . HOH N 4 .   ? -47.357 43.624  72.167  1.00 64.66 ? 447  HOH D O   1 
HETATM 10411 O  O   . HOH N 4 .   ? -41.253 28.740  82.705  1.00 56.35 ? 448  HOH D O   1 
HETATM 10412 O  O   . HOH N 4 .   ? -56.740 20.610  86.363  1.00 57.14 ? 449  HOH D O   1 
HETATM 10413 O  O   . HOH N 4 .   ? -69.269 61.862  74.833  1.00 44.52 ? 450  HOH D O   1 
HETATM 10414 O  O   . HOH N 4 .   ? -53.760 35.283  80.105  1.00 30.61 ? 451  HOH D O   1 
HETATM 10415 O  O   . HOH N 4 .   ? -32.039 39.243  88.343  1.00 52.33 ? 452  HOH D O   1 
HETATM 10416 O  O   . HOH N 4 .   ? -52.845 48.552  95.880  1.00 41.02 ? 453  HOH D O   1 
HETATM 10417 O  O   . HOH N 4 .   ? -47.574 58.724  88.905  1.00 58.47 ? 454  HOH D O   1 
HETATM 10418 O  O   . HOH N 4 .   ? -50.770 33.332  76.302  1.00 49.28 ? 455  HOH D O   1 
HETATM 10419 O  O   . HOH N 4 .   ? -70.519 49.353  57.778  1.00 46.42 ? 456  HOH D O   1 
HETATM 10420 O  O   . HOH N 4 .   ? -74.479 48.021  86.806  1.00 49.45 ? 457  HOH D O   1 
HETATM 10421 O  O   . HOH N 4 .   ? -31.696 39.899  91.150  1.00 42.74 ? 458  HOH D O   1 
HETATM 10422 O  O   . HOH N 4 .   ? -61.010 22.877  92.173  1.00 63.79 ? 459  HOH D O   1 
HETATM 10423 O  O   . HOH N 4 .   ? -71.073 62.625  90.576  1.00 51.25 ? 460  HOH D O   1 
HETATM 10424 O  O   . HOH N 4 .   ? -42.131 58.515  80.177  1.00 51.08 ? 461  HOH D O   1 
HETATM 10425 O  O   . HOH N 4 .   ? -58.216 45.241  96.265  1.00 59.86 ? 462  HOH D O   1 
HETATM 10426 O  O   . HOH N 4 .   ? -39.353 47.133  99.086  1.00 85.74 ? 463  HOH D O   1 
HETATM 10427 O  O   . HOH N 4 .   ? -37.701 30.649  85.046  1.00 55.36 ? 464  HOH D O   1 
HETATM 10428 O  O   . HOH N 4 .   ? -44.899 25.261  83.634  1.00 33.35 ? 465  HOH D O   1 
HETATM 10429 O  O   . HOH N 4 .   ? -66.803 36.428  95.650  1.00 93.17 ? 466  HOH D O   1 
HETATM 10430 O  O   . HOH N 4 .   ? -71.528 31.152  87.995  1.00 71.43 ? 467  HOH D O   1 
HETATM 10431 O  O   . HOH N 4 .   ? -45.228 45.206  69.021  1.00 52.44 ? 468  HOH D O   1 
HETATM 10432 O  O   . HOH N 4 .   ? -76.683 37.716  91.350  1.00 70.85 ? 469  HOH D O   1 
HETATM 10433 O  O   . HOH N 4 .   ? -33.138 49.996  81.118  1.00 60.44 ? 470  HOH D O   1 
HETATM 10434 O  O   . HOH N 4 .   ? -58.939 54.975  91.676  1.00 51.69 ? 471  HOH D O   1 
HETATM 10435 O  O   . HOH N 4 .   ? -35.608 47.059  76.068  1.00 53.09 ? 472  HOH D O   1 
HETATM 10436 O  O   . HOH N 4 .   ? -55.339 48.804  96.667  1.00 68.22 ? 473  HOH D O   1 
HETATM 10437 O  O   . HOH N 4 .   ? -42.853 46.191  95.371  1.00 56.63 ? 474  HOH D O   1 
HETATM 10438 O  O   . HOH N 4 .   ? -68.901 43.295  92.580  1.00 71.92 ? 475  HOH D O   1 
HETATM 10439 O  O   . HOH N 4 .   ? -69.396 64.193  76.762  1.00 73.53 ? 476  HOH D O   1 
HETATM 10440 O  O   . HOH N 4 .   ? -58.431 26.095  78.677  1.00 56.59 ? 477  HOH D O   1 
HETATM 10441 O  O   . HOH N 4 .   ? -37.406 52.392  72.730  1.00 57.33 ? 478  HOH D O   1 
HETATM 10442 O  O   . HOH N 4 .   ? -33.921 41.332  95.061  1.00 57.11 ? 479  HOH D O   1 
HETATM 10443 O  O   . HOH N 4 .   ? -45.098 36.093  77.504  1.00 56.20 ? 480  HOH D O   1 
HETATM 10444 O  O   . HOH N 4 .   ? -56.316 33.749  83.475  1.00 63.44 ? 481  HOH D O   1 
HETATM 10445 O  O   . HOH N 4 .   ? -68.901 35.715  94.649  1.00 68.35 ? 482  HOH D O   1 
HETATM 10446 O  O   . HOH N 4 .   ? -56.687 45.414  102.202 1.00 66.01 ? 483  HOH D O   1 
HETATM 10447 O  O   . HOH N 4 .   ? -77.484 28.752  85.462  1.00 74.80 ? 484  HOH D O   1 
HETATM 10448 O  O   . HOH N 4 .   ? -47.978 22.558  81.128  1.00 70.24 ? 485  HOH D O   1 
HETATM 10449 O  O   . HOH N 4 .   ? -50.939 57.699  91.336  1.00 45.31 ? 486  HOH D O   1 
HETATM 10450 O  O   . HOH N 4 .   ? -49.321 45.175  75.011  1.00 60.07 ? 487  HOH D O   1 
HETATM 10451 O  O   . HOH N 4 .   ? -72.258 28.261  86.889  1.00 87.55 ? 488  HOH D O   1 
HETATM 10452 O  O   . HOH N 4 .   ? -34.018 58.013  88.095  1.00 75.08 ? 489  HOH D O   1 
HETATM 10453 O  O   . HOH N 4 .   ? -79.141 30.350  90.734  1.00 67.19 ? 490  HOH D O   1 
HETATM 10454 O  O   . HOH N 4 .   ? -55.833 47.606  100.510 1.00 70.39 ? 491  HOH D O   1 
HETATM 10455 O  O   . HOH N 4 .   ? -36.871 50.107  76.097  1.00 50.77 ? 492  HOH D O   1 
HETATM 10456 O  O   . HOH N 4 .   ? -58.247 49.666  99.386  1.00 73.95 ? 493  HOH D O   1 
HETATM 10457 O  O   . HOH N 4 .   ? -56.747 51.641  67.230  1.00 60.93 ? 494  HOH D 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   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   THR 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   SER 6   6   ?   ?   ?   A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   CYS 8   8   8   CYS CYS A . n 
A 1 9   SER 9   9   9   SER SER A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  MET 25  25  25  MET MET A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  ASN 36  36  36  ASN ASN A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  MET 43  43  43  MET MET A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  MET 62  62  62  MET MET A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  HIS 73  73  73  HIS HIS A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  MET 79  79  79  MET MET A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  PRO 88  88  88  PRO PRO A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  MET 99  99  99  MET MET A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 TRP 102 102 102 TRP TRP A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 PRO 107 107 107 PRO PRO A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 CYS 125 125 125 CYS CYS A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 PRO 134 134 134 PRO PRO A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 ARG 138 138 138 ARG ARG A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 LYS 141 141 141 LYS LYS A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 THR 159 159 159 THR THR A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 CYS 164 164 164 CYS CYS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 SER 173 173 173 SER SER A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 TYR 177 177 177 TYR TYR A . n 
A 1 178 ARG 178 178 178 ARG ARG A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 GLN 183 183 183 GLN GLN A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 LYS 186 186 186 LYS LYS A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 GLU 190 190 190 GLU GLU A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 MET 194 194 194 MET MET A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 LYS 197 197 197 LYS LYS A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 ASN 199 199 199 ASN ASN A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 ASP 204 204 204 ASP ASP A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 MET 212 212 212 MET MET A . n 
A 1 213 GLN 213 213 213 GLN GLN A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 PRO 221 221 221 PRO PRO A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 TRP 226 226 226 TRP TRP A . n 
A 1 227 ASN 227 227 227 ASN ASN A . n 
A 1 228 CYS 228 228 228 CYS CYS A . n 
A 1 229 LYS 229 229 229 LYS LYS A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 ASP 233 233 233 ASP ASP A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 ILE 239 239 239 ILE ILE A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 GLN 241 241 241 GLN GLN A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 HIS 245 245 245 HIS HIS A . n 
A 1 246 ASN 246 246 246 ASN ASN A . n 
A 1 247 PRO 247 247 247 PRO PRO A . n 
A 1 248 MET 248 248 248 MET MET A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 GLN 252 252 252 GLN GLN A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
A 1 261 THR 261 261 261 THR THR A . n 
A 1 262 TYR 262 262 262 TYR TYR A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 PRO 266 266 266 PRO PRO A . n 
A 1 267 GLN 267 267 267 GLN GLN A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 CYS 270 270 270 CYS CYS A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 PRO 272 272 272 PRO PRO A . n 
A 1 273 ASP 273 273 273 ASP ASP A . n 
A 1 274 HIS 274 274 ?   ?   ?   A . n 
A 1 275 GLU 275 275 ?   ?   ?   A . n 
A 1 276 VAL 276 276 ?   ?   ?   A . n 
A 1 277 GLN 277 277 ?   ?   ?   A . n 
A 1 278 PRO 278 278 ?   ?   ?   A . n 
A 1 279 THR 279 279 ?   ?   ?   A . n 
A 1 280 LEU 280 280 ?   ?   ?   A . n 
A 1 281 PRO 281 281 ?   ?   ?   A . n 
A 1 282 SER 282 282 ?   ?   ?   A . n 
A 1 283 ASN 283 283 ?   ?   ?   A . n 
A 1 284 PRO 284 284 ?   ?   ?   A . n 
A 1 285 GLY 285 285 ?   ?   ?   A . n 
A 1 286 PRO 286 286 ?   ?   ?   A . n 
A 1 287 GLY 287 287 ?   ?   ?   A . n 
A 1 288 PRO 288 288 ?   ?   ?   A . n 
A 1 289 THR 289 289 289 THR THR A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 SER 292 292 292 SER SER A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 ILE 294 294 294 ILE ILE A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 ILE 297 297 297 ILE ILE A . n 
A 1 298 TYR 298 298 298 TYR TYR A . n 
A 1 299 THR 299 299 299 THR THR A . n 
A 1 300 ILE 300 300 300 ILE ILE A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 ASN 302 302 302 ASN ASN A . n 
A 1 303 GLN 303 303 303 GLN GLN A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 ARG 305 305 305 ARG ARG A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 VAL 307 307 307 VAL VAL A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 PHE 311 311 311 PHE PHE A . n 
A 1 312 ASN 312 312 312 ASN ASN A . n 
A 1 313 GLU 313 313 313 GLU GLU A . n 
A 1 314 THR 314 314 314 THR THR A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 ASN 316 316 316 ASN ASN A . n 
A 1 317 VAL 317 317 317 VAL VAL A . n 
A 1 318 SER 318 318 318 SER SER A . n 
A 1 319 VAL 319 319 319 VAL VAL A . n 
A 1 320 LYS 320 320 320 LYS LYS A . n 
A 1 321 SER 321 321 321 SER SER A . n 
A 1 322 GLY 322 322 322 GLY GLY A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 LEU 325 325 325 LEU LEU A . n 
A 1 326 LEU 326 326 326 LEU LEU A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 VAL 328 328 328 VAL VAL A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 GLU 331 331 331 GLU GLU A . n 
A 1 332 ALA 332 332 332 ALA ALA A . n 
A 1 333 GLN 333 333 333 GLN GLN A . n 
A 1 334 ARG 334 334 334 ARG ARG A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 ASN 336 336 336 ASN ASN A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 MET 338 338 338 MET MET A . n 
A 1 339 PHE 339 339 339 PHE PHE A . n 
A 1 340 LYS 340 340 340 LYS LYS A . n 
A 1 341 PHE 341 341 341 PHE PHE A . n 
A 1 342 GLU 342 342 342 GLU GLU A . n 
A 1 343 THR 343 343 343 THR THR A . n 
A 1 344 THR 344 344 344 THR THR A . n 
A 1 345 MET 345 345 345 MET MET A . n 
A 1 346 THR 346 346 346 THR THR A . n 
A 1 347 SER 347 347 347 SER SER A . n 
A 1 348 TRP 348 348 348 TRP TRP A . n 
A 1 349 GLY 349 349 349 GLY GLY A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 VAL 352 352 352 VAL VAL A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 SER 354 354 354 SER SER A . n 
A 1 355 ILE 355 355 355 ILE ILE A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 ASN 357 357 357 ASN ASN A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 GLU 360 360 360 GLU GLU A . n 
A 1 361 ASN 361 361 361 ASN ASN A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 HIS 364 364 364 HIS HIS A . n 
A 1 365 LYS 365 365 365 LYS LYS A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 TYR 367 367 367 TYR TYR A . n 
A 1 368 TRP 368 368 368 TRP TRP A . n 
A 1 369 GLN 369 369 369 GLN GLN A . n 
A 1 370 PHE 370 370 370 PHE PHE A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 SER 372 372 372 SER SER A . n 
A 1 373 GLY 373 373 373 GLY GLY A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 THR 375 375 375 THR THR A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 ASN 378 378 378 ASN ASN A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 ALA 382 382 382 ALA ALA A . n 
A 1 383 ASP 383 383 383 ASP ASP A . n 
A 1 384 TYR 384 384 384 TYR TYR A . n 
A 1 385 ILE 385 385 385 ILE ILE A . n 
A 1 386 PRO 386 386 386 PRO PRO A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 ASN 388 388 388 ASN ASN A . n 
A 1 389 HIS 389 389 389 HIS HIS A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 HIS 391 391 391 HIS HIS A . n 
A 1 392 ILE 392 392 392 ILE ILE A . n 
A 1 393 THR 393 393 393 THR THR A . n 
A 1 394 ALA 394 394 394 ALA ALA A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 PHE 396 396 396 PHE PHE A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 GLN 398 398 398 GLN GLN A . n 
A 1 399 TYR 399 399 399 TYR TYR A . n 
B 1 1   SER 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   GLN 3   3   ?   ?   ?   B . n 
B 1 4   THR 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   SER 6   6   ?   ?   ?   B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   CYS 8   8   8   CYS CYS B . n 
B 1 9   SER 9   9   9   SER SER B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  PRO 11  11  11  PRO PRO B . n 
B 1 12  SER 12  12  12  SER SER B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  GLN 14  14  14  GLN GLN B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  PRO 16  16  16  PRO PRO B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  GLY 20  20  20  GLY GLY B . n 
B 1 21  ILE 21  21  21  ILE ILE B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  VAL 23  23  23  VAL VAL B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  MET 25  25  25  MET MET B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ASN 27  27  27  ASN ASN B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  THR 30  30  30  THR THR B . n 
B 1 31  SER 31  31  31  SER SER B . n 
B 1 32  SER 32  32  32  SER SER B . n 
B 1 33  ALA 33  33  33  ALA ALA B . n 
B 1 34  TYR 34  34  34  TYR TYR B . n 
B 1 35  PRO 35  35  35  PRO PRO B . n 
B 1 36  ASN 36  36  36  ASN ASN B . n 
B 1 37  PRO 37  37  37  PRO PRO B . n 
B 1 38  SER 38  38  38  SER SER B . n 
B 1 39  ILE 39  39  39  ILE ILE B . n 
B 1 40  LEU 40  40  40  LEU LEU B . n 
B 1 41  ILE 41  41  41  ILE ILE B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  MET 43  43  43  MET MET B . n 
B 1 44  ASN 44  44  44  ASN ASN B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  ALA 46  46  46  ALA ALA B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  TYR 49  49  49  TYR TYR B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  ALA 53  53  53  ALA ALA B . n 
B 1 54  GLN 54  54  54  GLN GLN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  TYR 59  59  59  TYR TYR B . n 
B 1 60  GLN 60  60  60  GLN GLN B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  MET 62  62  62  MET MET B . n 
B 1 63  SER 63  63  63  SER SER B . n 
B 1 64  SER 64  64  64  SER SER B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  THR 70  70  70  THR THR B . n 
B 1 71  ILE 71  71  71  ILE ILE B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  HIS 73  73  73  HIS HIS B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  THR 77  77  77  THR THR B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  MET 79  79  79  MET MET B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  THR 82  82  82  THR THR B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  ARG 86  86  86  ARG ARG B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  PRO 88  88  88  PRO PRO B . n 
B 1 89  GLY 89  89  89  GLY GLY B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  GLN 96  96  96  GLN GLN B . n 
B 1 97  ARG 97  97  97  ARG ARG B . n 
B 1 98  GLN 98  98  98  GLN GLN B . n 
B 1 99  MET 99  99  99  MET MET B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 TRP 102 102 102 TRP TRP B . n 
B 1 103 ALA 103 103 103 ALA ALA B . n 
B 1 104 PRO 104 104 104 PRO PRO B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 PRO 107 107 107 PRO PRO B . n 
B 1 108 ASN 108 108 108 ASN ASN B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 GLU 110 110 110 GLU GLU B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 PHE 114 114 114 PHE PHE B . n 
B 1 115 TYR 115 115 115 TYR TYR B . n 
B 1 116 GLY 116 116 116 GLY GLY B . n 
B 1 117 PRO 117 117 117 PRO PRO B . n 
B 1 118 SER 118 118 118 SER SER B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 ILE 121 121 121 ILE ILE B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 CYS 125 125 125 CYS CYS B . n 
B 1 126 GLN 126 126 126 GLN GLN B . n 
B 1 127 LYS 127 127 127 LYS LYS B . n 
B 1 128 ASN 128 128 128 ASN ASN B . n 
B 1 129 SER 129 129 129 SER SER B . n 
B 1 130 GLU 130 130 130 GLU GLU B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 PRO 134 134 134 PRO PRO B . n 
B 1 135 ILE 135 135 135 ILE ILE B . n 
B 1 136 ALA 136 136 136 ALA ALA B . n 
B 1 137 VAL 137 137 137 VAL VAL B . n 
B 1 138 ARG 138 138 138 ARG ARG B . n 
B 1 139 PHE 139 139 139 PHE PHE B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 LYS 141 141 141 LYS LYS B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 ASN 146 146 146 ASN ASN B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 SER 148 148 148 SER SER B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 THR 154 154 154 THR THR B . n 
B 1 155 GLY 155 155 155 GLY GLY B . n 
B 1 156 ALA 156 156 156 ALA ALA B . n 
B 1 157 MET 157 157 157 MET MET B . n 
B 1 158 ALA 158 158 158 ALA ALA B . n 
B 1 159 THR 159 159 159 THR THR B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 ALA 161 161 161 ALA ALA B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 THR 163 163 163 THR THR B . n 
B 1 164 CYS 164 164 164 CYS CYS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 TYR 166 166 166 TYR TYR B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 GLY 172 172 172 GLY GLY B . n 
B 1 173 SER 173 173 173 SER SER B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 GLU 175 175 175 GLU GLU B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 TYR 177 177 177 TYR TYR B . n 
B 1 178 ARG 178 178 178 ARG ARG B . n 
B 1 179 SER 179 179 179 SER SER B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 GLY 182 182 182 GLY GLY B . n 
B 1 183 GLN 183 183 183 GLN GLN B . n 
B 1 184 VAL 184 184 184 VAL VAL B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 LYS 186 186 186 LYS LYS B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ILE 188 188 188 ILE ILE B . n 
B 1 189 VAL 189 189 189 VAL VAL B . n 
B 1 190 GLU 190 190 190 GLU GLU B . n 
B 1 191 LYS 191 191 191 LYS LYS B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 MET 194 194 194 MET MET B . n 
B 1 195 LYS 195 195 195 LYS LYS B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 LYS 197 197 197 LYS LYS B . n 
B 1 198 ASP 198 198 198 ASP ASP B . n 
B 1 199 ASN 199 199 199 ASN ASN B . n 
B 1 200 GLY 200 200 200 GLY GLY B . n 
B 1 201 ILE 201 201 201 ILE ILE B . n 
B 1 202 ILE 202 202 202 ILE ILE B . n 
B 1 203 GLY 203 203 203 GLY GLY B . n 
B 1 204 ASP 204 204 204 ASP ASP B . n 
B 1 205 ILE 205 205 205 ILE ILE B . n 
B 1 206 TYR 206 206 206 TYR TYR B . n 
B 1 207 SER 207 207 207 SER SER B . n 
B 1 208 THR 208 208 208 THR THR B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 MET 212 212 212 MET MET B . n 
B 1 213 GLN 213 213 213 GLN GLN B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 LEU 215 215 215 LEU LEU B . n 
B 1 216 SER 216 216 216 SER SER B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 THR 218 218 218 THR THR B . n 
B 1 219 PRO 219 219 219 PRO PRO B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 PRO 221 221 221 PRO PRO B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 LYS 223 223 223 LYS LYS B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 GLU 225 225 225 GLU GLU B . n 
B 1 226 TRP 226 226 226 TRP TRP B . n 
B 1 227 ASN 227 227 227 ASN ASN B . n 
B 1 228 CYS 228 228 228 CYS CYS B . n 
B 1 229 LYS 229 229 229 LYS LYS B . n 
B 1 230 LYS 230 230 230 LYS LYS B . n 
B 1 231 THR 231 231 231 THR THR B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 ASP 233 233 233 ASP ASP B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ILE 235 235 235 ILE ILE B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 ASN 237 237 237 ASN ASN B . n 
B 1 238 GLU 238 238 238 GLU GLU B . n 
B 1 239 ILE 239 239 239 ILE ILE B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 GLN 241 241 241 GLN GLN B . n 
B 1 242 GLY 242 242 242 GLY GLY B . n 
B 1 243 LYS 243 243 243 LYS LYS B . n 
B 1 244 PHE 244 244 244 PHE PHE B . n 
B 1 245 HIS 245 245 245 HIS HIS B . n 
B 1 246 ASN 246 246 246 ASN ASN B . n 
B 1 247 PRO 247 247 247 PRO PRO B . n 
B 1 248 MET 248 248 248 MET MET B . n 
B 1 249 SER 249 249 249 SER SER B . n 
B 1 250 ILE 250 250 250 ILE ILE B . n 
B 1 251 ALA 251 251 251 ALA ALA B . n 
B 1 252 GLN 252 252 252 GLN GLN B . n 
B 1 253 ILE 253 253 253 ILE ILE B . n 
B 1 254 LEU 254 254 254 LEU LEU B . n 
B 1 255 PRO 255 255 255 PRO PRO B . n 
B 1 256 SER 256 256 256 SER SER B . n 
B 1 257 LEU 257 257 257 LEU LEU B . n 
B 1 258 LYS 258 258 258 LYS LYS B . n 
B 1 259 GLY 259 259 259 GLY GLY B . n 
B 1 260 LYS 260 260 260 LYS LYS B . n 
B 1 261 THR 261 261 261 THR THR B . n 
B 1 262 TYR 262 262 262 TYR TYR B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 ASP 264 264 264 ASP ASP B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 PRO 266 266 266 PRO PRO B . n 
B 1 267 GLN 267 267 267 GLN GLN B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 THR 269 269 269 THR THR B . n 
B 1 270 CYS 270 270 270 CYS CYS B . n 
B 1 271 SER 271 271 271 SER SER B . n 
B 1 272 PRO 272 272 272 PRO PRO B . n 
B 1 273 ASP 273 273 273 ASP ASP B . n 
B 1 274 HIS 274 274 ?   ?   ?   B . n 
B 1 275 GLU 275 275 ?   ?   ?   B . n 
B 1 276 VAL 276 276 ?   ?   ?   B . n 
B 1 277 GLN 277 277 ?   ?   ?   B . n 
B 1 278 PRO 278 278 ?   ?   ?   B . n 
B 1 279 THR 279 279 ?   ?   ?   B . n 
B 1 280 LEU 280 280 ?   ?   ?   B . n 
B 1 281 PRO 281 281 ?   ?   ?   B . n 
B 1 282 SER 282 282 ?   ?   ?   B . n 
B 1 283 ASN 283 283 ?   ?   ?   B . n 
B 1 284 PRO 284 284 ?   ?   ?   B . n 
B 1 285 GLY 285 285 ?   ?   ?   B . n 
B 1 286 PRO 286 286 ?   ?   ?   B . n 
B 1 287 GLY 287 287 ?   ?   ?   B . n 
B 1 288 PRO 288 288 ?   ?   ?   B . n 
B 1 289 THR 289 289 ?   ?   ?   B . n 
B 1 290 SER 290 290 ?   ?   ?   B . n 
B 1 291 ALA 291 291 ?   ?   ?   B . n 
B 1 292 SER 292 292 ?   ?   ?   B . n 
B 1 293 ASN 293 293 ?   ?   ?   B . n 
B 1 294 ILE 294 294 ?   ?   ?   B . n 
B 1 295 THR 295 295 ?   ?   ?   B . n 
B 1 296 VAL 296 296 ?   ?   ?   B . n 
B 1 297 ILE 297 297 ?   ?   ?   B . n 
B 1 298 TYR 298 298 ?   ?   ?   B . n 
B 1 299 THR 299 299 ?   ?   ?   B . n 
B 1 300 ILE 300 300 ?   ?   ?   B . n 
B 1 301 ASN 301 301 ?   ?   ?   B . n 
B 1 302 ASN 302 302 ?   ?   ?   B . n 
B 1 303 GLN 303 303 ?   ?   ?   B . n 
B 1 304 LEU 304 304 ?   ?   ?   B . n 
B 1 305 ARG 305 305 ?   ?   ?   B . n 
B 1 306 GLY 306 306 ?   ?   ?   B . n 
B 1 307 VAL 307 307 ?   ?   ?   B . n 
B 1 308 GLU 308 308 ?   ?   ?   B . n 
B 1 309 LEU 309 309 ?   ?   ?   B . n 
B 1 310 LEU 310 310 ?   ?   ?   B . n 
B 1 311 PHE 311 311 ?   ?   ?   B . n 
B 1 312 ASN 312 312 ?   ?   ?   B . n 
B 1 313 GLU 313 313 ?   ?   ?   B . n 
B 1 314 THR 314 314 ?   ?   ?   B . n 
B 1 315 ILE 315 315 ?   ?   ?   B . n 
B 1 316 ASN 316 316 ?   ?   ?   B . n 
B 1 317 VAL 317 317 ?   ?   ?   B . n 
B 1 318 SER 318 318 ?   ?   ?   B . n 
B 1 319 VAL 319 319 ?   ?   ?   B . n 
B 1 320 LYS 320 320 ?   ?   ?   B . n 
B 1 321 SER 321 321 ?   ?   ?   B . n 
B 1 322 GLY 322 322 ?   ?   ?   B . n 
B 1 323 SER 323 323 ?   ?   ?   B . n 
B 1 324 VAL 324 324 ?   ?   ?   B . n 
B 1 325 LEU 325 325 ?   ?   ?   B . n 
B 1 326 LEU 326 326 ?   ?   ?   B . n 
B 1 327 VAL 327 327 ?   ?   ?   B . n 
B 1 328 VAL 328 328 ?   ?   ?   B . n 
B 1 329 LEU 329 329 ?   ?   ?   B . n 
B 1 330 GLU 330 330 ?   ?   ?   B . n 
B 1 331 GLU 331 331 ?   ?   ?   B . n 
B 1 332 ALA 332 332 ?   ?   ?   B . n 
B 1 333 GLN 333 333 ?   ?   ?   B . n 
B 1 334 ARG 334 334 ?   ?   ?   B . n 
B 1 335 LYS 335 335 ?   ?   ?   B . n 
B 1 336 ASN 336 336 ?   ?   ?   B . n 
B 1 337 PRO 337 337 ?   ?   ?   B . n 
B 1 338 MET 338 338 ?   ?   ?   B . n 
B 1 339 PHE 339 339 ?   ?   ?   B . n 
B 1 340 LYS 340 340 ?   ?   ?   B . n 
B 1 341 PHE 341 341 ?   ?   ?   B . n 
B 1 342 GLU 342 342 ?   ?   ?   B . n 
B 1 343 THR 343 343 ?   ?   ?   B . n 
B 1 344 THR 344 344 ?   ?   ?   B . n 
B 1 345 MET 345 345 ?   ?   ?   B . n 
B 1 346 THR 346 346 ?   ?   ?   B . n 
B 1 347 SER 347 347 ?   ?   ?   B . n 
B 1 348 TRP 348 348 ?   ?   ?   B . n 
B 1 349 GLY 349 349 ?   ?   ?   B . n 
B 1 350 LEU 350 350 ?   ?   ?   B . n 
B 1 351 VAL 351 351 ?   ?   ?   B . n 
B 1 352 VAL 352 352 ?   ?   ?   B . n 
B 1 353 SER 353 353 ?   ?   ?   B . n 
B 1 354 SER 354 354 ?   ?   ?   B . n 
B 1 355 ILE 355 355 ?   ?   ?   B . n 
B 1 356 ASN 356 356 ?   ?   ?   B . n 
B 1 357 ASN 357 357 ?   ?   ?   B . n 
B 1 358 ILE 358 358 ?   ?   ?   B . n 
B 1 359 ALA 359 359 ?   ?   ?   B . n 
B 1 360 GLU 360 360 ?   ?   ?   B . n 
B 1 361 ASN 361 361 ?   ?   ?   B . n 
B 1 362 VAL 362 362 ?   ?   ?   B . n 
B 1 363 ASN 363 363 ?   ?   ?   B . n 
B 1 364 HIS 364 364 ?   ?   ?   B . n 
B 1 365 LYS 365 365 ?   ?   ?   B . n 
B 1 366 THR 366 366 ?   ?   ?   B . n 
B 1 367 TYR 367 367 ?   ?   ?   B . n 
B 1 368 TRP 368 368 ?   ?   ?   B . n 
B 1 369 GLN 369 369 ?   ?   ?   B . n 
B 1 370 PHE 370 370 ?   ?   ?   B . n 
B 1 371 LEU 371 371 ?   ?   ?   B . n 
B 1 372 SER 372 372 ?   ?   ?   B . n 
B 1 373 GLY 373 373 ?   ?   ?   B . n 
B 1 374 VAL 374 374 ?   ?   ?   B . n 
B 1 375 THR 375 375 ?   ?   ?   B . n 
B 1 376 PRO 376 376 ?   ?   ?   B . n 
B 1 377 LEU 377 377 ?   ?   ?   B . n 
B 1 378 ASN 378 378 ?   ?   ?   B . n 
B 1 379 GLU 379 379 ?   ?   ?   B . n 
B 1 380 GLY 380 380 ?   ?   ?   B . n 
B 1 381 VAL 381 381 ?   ?   ?   B . n 
B 1 382 ALA 382 382 ?   ?   ?   B . n 
B 1 383 ASP 383 383 ?   ?   ?   B . n 
B 1 384 TYR 384 384 ?   ?   ?   B . n 
B 1 385 ILE 385 385 ?   ?   ?   B . n 
B 1 386 PRO 386 386 ?   ?   ?   B . n 
B 1 387 PHE 387 387 ?   ?   ?   B . n 
B 1 388 ASN 388 388 ?   ?   ?   B . n 
B 1 389 HIS 389 389 ?   ?   ?   B . n 
B 1 390 GLU 390 390 ?   ?   ?   B . n 
B 1 391 HIS 391 391 ?   ?   ?   B . n 
B 1 392 ILE 392 392 ?   ?   ?   B . n 
B 1 393 THR 393 393 ?   ?   ?   B . n 
B 1 394 ALA 394 394 ?   ?   ?   B . n 
B 1 395 ASN 395 395 ?   ?   ?   B . n 
B 1 396 PHE 396 396 ?   ?   ?   B . n 
B 1 397 THR 397 397 ?   ?   ?   B . n 
B 1 398 GLN 398 398 ?   ?   ?   B . n 
B 1 399 TYR 399 399 ?   ?   ?   B . n 
C 1 1   SER 1   1   ?   ?   ?   C . n 
C 1 2   THR 2   2   ?   ?   ?   C . n 
C 1 3   GLN 3   3   ?   ?   ?   C . n 
C 1 4   THR 4   4   ?   ?   ?   C . n 
C 1 5   GLN 5   5   ?   ?   ?   C . n 
C 1 6   SER 6   6   ?   ?   ?   C . n 
C 1 7   SER 7   7   7   SER SER C . n 
C 1 8   CYS 8   8   8   CYS CYS C . n 
C 1 9   SER 9   9   9   SER SER C . n 
C 1 10  VAL 10  10  10  VAL VAL C . n 
C 1 11  PRO 11  11  11  PRO PRO C . n 
C 1 12  SER 12  12  12  SER SER C . n 
C 1 13  ALA 13  13  13  ALA ALA C . n 
C 1 14  GLN 14  14  14  GLN GLN C . n 
C 1 15  GLU 15  15  15  GLU GLU C . n 
C 1 16  PRO 16  16  16  PRO PRO C . n 
C 1 17  LEU 17  17  17  LEU LEU C . n 
C 1 18  VAL 18  18  18  VAL VAL C . n 
C 1 19  ASN 19  19  19  ASN ASN C . n 
C 1 20  GLY 20  20  20  GLY GLY C . n 
C 1 21  ILE 21  21  21  ILE ILE C . n 
C 1 22  GLN 22  22  22  GLN GLN C . n 
C 1 23  VAL 23  23  23  VAL VAL C . n 
C 1 24  LEU 24  24  24  LEU LEU C . n 
C 1 25  MET 25  25  25  MET MET C . n 
C 1 26  GLU 26  26  26  GLU GLU C . n 
C 1 27  ASN 27  27  27  ASN ASN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  THR 30  30  30  THR THR C . n 
C 1 31  SER 31  31  31  SER SER C . n 
C 1 32  SER 32  32  32  SER SER C . n 
C 1 33  ALA 33  33  33  ALA ALA C . n 
C 1 34  TYR 34  34  34  TYR TYR C . n 
C 1 35  PRO 35  35  35  PRO PRO C . n 
C 1 36  ASN 36  36  36  ASN ASN C . n 
C 1 37  PRO 37  37  37  PRO PRO C . n 
C 1 38  SER 38  38  38  SER SER C . n 
C 1 39  ILE 39  39  39  ILE ILE C . n 
C 1 40  LEU 40  40  40  LEU LEU C . n 
C 1 41  ILE 41  41  41  ILE ILE C . n 
C 1 42  ALA 42  42  42  ALA ALA C . n 
C 1 43  MET 43  43  43  MET MET C . n 
C 1 44  ASN 44  44  44  ASN ASN C . n 
C 1 45  LEU 45  45  45  LEU LEU C . n 
C 1 46  ALA 46  46  46  ALA ALA C . n 
C 1 47  GLY 47  47  47  GLY GLY C . n 
C 1 48  ALA 48  48  48  ALA ALA C . n 
C 1 49  TYR 49  49  49  TYR TYR C . n 
C 1 50  ASN 50  50  50  ASN ASN C . n 
C 1 51  LEU 51  51  51  LEU LEU C . n 
C 1 52  LYS 52  52  52  LYS LYS C . n 
C 1 53  ALA 53  53  53  ALA ALA C . n 
C 1 54  GLN 54  54  54  GLN GLN C . n 
C 1 55  LYS 55  55  55  LYS LYS C . n 
C 1 56  LEU 56  56  56  LEU LEU C . n 
C 1 57  LEU 57  57  57  LEU LEU C . n 
C 1 58  THR 58  58  58  THR THR C . n 
C 1 59  TYR 59  59  59  TYR TYR C . n 
C 1 60  GLN 60  60  60  GLN GLN C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  MET 62  62  62  MET MET C . n 
C 1 63  SER 63  63  63  SER SER C . n 
C 1 64  SER 64  64  64  SER SER C . n 
C 1 65  ASP 65  65  65  ASP ASP C . n 
C 1 66  ASN 66  66  66  ASN ASN C . n 
C 1 67  ASN 67  67  67  ASN ASN C . n 
C 1 68  ASP 68  68  68  ASP ASP C . n 
C 1 69  LEU 69  69  69  LEU LEU C . n 
C 1 70  THR 70  70  70  THR THR C . n 
C 1 71  ILE 71  71  71  ILE ILE C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  HIS 73  73  73  HIS HIS C . n 
C 1 74  LEU 74  74  74  LEU LEU C . n 
C 1 75  GLY 75  75  75  GLY GLY C . n 
C 1 76  LEU 76  76  76  LEU LEU C . n 
C 1 77  THR 77  77  77  THR THR C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  MET 79  79  79  MET MET C . n 
C 1 80  ALA 80  80  80  ALA ALA C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  THR 82  82  82  THR THR C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  SER 84  84  84  SER SER C . n 
C 1 85  CYS 85  85  85  CYS CYS C . n 
C 1 86  ARG 86  86  86  ARG ARG C . n 
C 1 87  ASP 87  87  87  ASP ASP C . n 
C 1 88  PRO 88  88  88  PRO PRO C . n 
C 1 89  GLY 89  89  89  GLY GLY C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  LYS 91  91  91  LYS LYS C . n 
C 1 92  VAL 92  92  92  VAL VAL C . n 
C 1 93  SER 93  93  93  SER SER C . n 
C 1 94  ILE 94  94  94  ILE ILE C . n 
C 1 95  LEU 95  95  95  LEU LEU C . n 
C 1 96  GLN 96  96  96  GLN GLN C . n 
C 1 97  ARG 97  97  97  ARG ARG C . n 
C 1 98  GLN 98  98  98  GLN GLN C . n 
C 1 99  MET 99  99  99  MET MET C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ASN 101 101 101 ASN ASN C . n 
C 1 102 TRP 102 102 102 TRP TRP C . n 
C 1 103 ALA 103 103 103 ALA ALA C . n 
C 1 104 PRO 104 104 104 PRO PRO C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 SER 106 106 106 SER SER C . n 
C 1 107 PRO 107 107 107 PRO PRO C . n 
C 1 108 ASN 108 108 108 ASN ASN C . n 
C 1 109 ALA 109 109 109 ALA ALA C . n 
C 1 110 GLU 110 110 110 GLU GLU C . n 
C 1 111 ALA 111 111 111 ALA ALA C . n 
C 1 112 SER 112 112 112 SER SER C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 PHE 114 114 114 PHE PHE C . n 
C 1 115 TYR 115 115 115 TYR TYR C . n 
C 1 116 GLY 116 116 116 GLY GLY C . n 
C 1 117 PRO 117 117 117 PRO PRO C . n 
C 1 118 SER 118 118 118 SER SER C . n 
C 1 119 LEU 119 119 119 LEU LEU C . n 
C 1 120 ALA 120 120 120 ALA ALA C . n 
C 1 121 ILE 121 121 121 ILE ILE C . n 
C 1 122 LEU 122 122 122 LEU LEU C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 LEU 124 124 124 LEU LEU C . n 
C 1 125 CYS 125 125 125 CYS CYS C . n 
C 1 126 GLN 126 126 126 GLN GLN C . n 
C 1 127 LYS 127 127 127 LYS LYS C . n 
C 1 128 ASN 128 128 128 ASN ASN C . n 
C 1 129 SER 129 129 129 SER SER C . n 
C 1 130 GLU 130 130 130 GLU GLU C . n 
C 1 131 ALA 131 131 131 ALA ALA C . n 
C 1 132 THR 132 132 132 THR THR C . n 
C 1 133 LEU 133 133 133 LEU LEU C . n 
C 1 134 PRO 134 134 134 PRO PRO C . n 
C 1 135 ILE 135 135 135 ILE ILE C . n 
C 1 136 ALA 136 136 136 ALA ALA C . n 
C 1 137 VAL 137 137 137 VAL VAL C . n 
C 1 138 ARG 138 138 138 ARG ARG C . n 
C 1 139 PHE 139 139 139 PHE PHE C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 LYS 141 141 141 LYS LYS C . n 
C 1 142 THR 142 142 142 THR THR C . n 
C 1 143 LEU 143 143 143 LEU LEU C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 ASN 146 146 146 ASN ASN C . n 
C 1 147 SER 147 147 147 SER SER C . n 
C 1 148 SER 148 148 148 SER SER C . n 
C 1 149 PRO 149 149 149 PRO PRO C . n 
C 1 150 PHE 150 150 150 PHE PHE C . n 
C 1 151 ASN 151 151 151 ASN ASN C . n 
C 1 152 VAL 152 152 152 VAL VAL C . n 
C 1 153 ASP 153 153 153 ASP ASP C . n 
C 1 154 THR 154 154 154 THR THR C . n 
C 1 155 GLY 155 155 155 GLY GLY C . n 
C 1 156 ALA 156 156 156 ALA ALA C . n 
C 1 157 MET 157 157 157 MET MET C . n 
C 1 158 ALA 158 158 158 ALA ALA C . n 
C 1 159 THR 159 159 159 THR THR C . n 
C 1 160 LEU 160 160 160 LEU LEU C . n 
C 1 161 ALA 161 161 161 ALA ALA C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 THR 163 163 163 THR THR C . n 
C 1 164 CYS 164 164 164 CYS CYS C . n 
C 1 165 MET 165 165 165 MET MET C . n 
C 1 166 TYR 166 166 166 TYR TYR C . n 
C 1 167 ASN 167 167 167 ASN ASN C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 ILE 169 169 169 ILE ILE C . n 
C 1 170 PRO 170 170 170 PRO PRO C . n 
C 1 171 VAL 171 171 171 VAL VAL C . n 
C 1 172 GLY 172 172 172 GLY GLY C . n 
C 1 173 SER 173 173 173 SER SER C . n 
C 1 174 GLU 174 174 174 GLU GLU C . n 
C 1 175 GLU 175 175 175 GLU GLU C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 TYR 177 177 177 TYR TYR C . n 
C 1 178 ARG 178 178 178 ARG ARG C . n 
C 1 179 SER 179 179 179 SER SER C . n 
C 1 180 LEU 180 180 180 LEU LEU C . n 
C 1 181 PHE 181 181 181 PHE PHE C . n 
C 1 182 GLY 182 182 182 GLY GLY C . n 
C 1 183 GLN 183 183 183 GLN GLN C . n 
C 1 184 VAL 184 184 184 VAL VAL C . n 
C 1 185 LEU 185 185 185 LEU LEU C . n 
C 1 186 LYS 186 186 186 LYS LYS C . n 
C 1 187 ASP 187 187 187 ASP ASP C . n 
C 1 188 ILE 188 188 188 ILE ILE C . n 
C 1 189 VAL 189 189 189 VAL VAL C . n 
C 1 190 GLU 190 190 190 GLU GLU C . n 
C 1 191 LYS 191 191 191 LYS LYS C . n 
C 1 192 ILE 192 192 192 ILE ILE C . n 
C 1 193 SER 193 193 193 SER SER C . n 
C 1 194 MET 194 194 194 MET MET C . n 
C 1 195 LYS 195 195 195 LYS LYS C . n 
C 1 196 ILE 196 196 196 ILE ILE C . n 
C 1 197 LYS 197 197 197 LYS LYS C . n 
C 1 198 ASP 198 198 198 ASP ASP C . n 
C 1 199 ASN 199 199 199 ASN ASN C . n 
C 1 200 GLY 200 200 200 GLY GLY C . n 
C 1 201 ILE 201 201 201 ILE ILE C . n 
C 1 202 ILE 202 202 202 ILE ILE C . n 
C 1 203 GLY 203 203 203 GLY GLY C . n 
C 1 204 ASP 204 204 204 ASP ASP C . n 
C 1 205 ILE 205 205 205 ILE ILE C . n 
C 1 206 TYR 206 206 206 TYR TYR C . n 
C 1 207 SER 207 207 207 SER SER C . n 
C 1 208 THR 208 208 208 THR THR C . n 
C 1 209 GLY 209 209 209 GLY GLY C . n 
C 1 210 LEU 210 210 210 LEU LEU C . n 
C 1 211 ALA 211 211 211 ALA ALA C . n 
C 1 212 MET 212 212 212 MET MET C . n 
C 1 213 GLN 213 213 213 GLN GLN C . n 
C 1 214 ALA 214 214 214 ALA ALA C . n 
C 1 215 LEU 215 215 215 LEU LEU C . n 
C 1 216 SER 216 216 216 SER SER C . n 
C 1 217 VAL 217 217 217 VAL VAL C . n 
C 1 218 THR 218 218 218 THR THR C . n 
C 1 219 PRO 219 219 219 PRO PRO C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 PRO 221 221 221 PRO PRO C . n 
C 1 222 SER 222 222 222 SER SER C . n 
C 1 223 LYS 223 223 223 LYS LYS C . n 
C 1 224 LYS 224 224 224 LYS LYS C . n 
C 1 225 GLU 225 225 225 GLU GLU C . n 
C 1 226 TRP 226 226 226 TRP TRP C . n 
C 1 227 ASN 227 227 227 ASN ASN C . n 
C 1 228 CYS 228 228 228 CYS CYS C . n 
C 1 229 LYS 229 229 229 LYS LYS C . n 
C 1 230 LYS 230 230 230 LYS LYS C . n 
C 1 231 THR 231 231 231 THR THR C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 ASP 233 233 233 ASP ASP C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ILE 235 235 235 ILE ILE C . n 
C 1 236 LEU 236 236 236 LEU LEU C . n 
C 1 237 ASN 237 237 237 ASN ASN C . n 
C 1 238 GLU 238 238 238 GLU GLU C . n 
C 1 239 ILE 239 239 239 ILE ILE C . n 
C 1 240 LYS 240 240 240 LYS LYS C . n 
C 1 241 GLN 241 241 241 GLN GLN C . n 
C 1 242 GLY 242 242 242 GLY GLY C . n 
C 1 243 LYS 243 243 243 LYS LYS C . n 
C 1 244 PHE 244 244 244 PHE PHE C . n 
C 1 245 HIS 245 245 245 HIS HIS C . n 
C 1 246 ASN 246 246 246 ASN ASN C . n 
C 1 247 PRO 247 247 247 PRO PRO C . n 
C 1 248 MET 248 248 248 MET MET C . n 
C 1 249 SER 249 249 249 SER SER C . n 
C 1 250 ILE 250 250 250 ILE ILE C . n 
C 1 251 ALA 251 251 251 ALA ALA C . n 
C 1 252 GLN 252 252 252 GLN GLN C . n 
C 1 253 ILE 253 253 253 ILE ILE C . n 
C 1 254 LEU 254 254 254 LEU LEU C . n 
C 1 255 PRO 255 255 255 PRO PRO C . n 
C 1 256 SER 256 256 256 SER SER C . n 
C 1 257 LEU 257 257 257 LEU LEU C . n 
C 1 258 LYS 258 258 258 LYS LYS C . n 
C 1 259 GLY 259 259 259 GLY GLY C . n 
C 1 260 LYS 260 260 260 LYS LYS C . n 
C 1 261 THR 261 261 261 THR THR C . n 
C 1 262 TYR 262 262 262 TYR TYR C . n 
C 1 263 LEU 263 263 263 LEU LEU C . n 
C 1 264 ASP 264 264 264 ASP ASP C . n 
C 1 265 VAL 265 265 265 VAL VAL C . n 
C 1 266 PRO 266 266 266 PRO PRO C . n 
C 1 267 GLN 267 267 267 GLN GLN C . n 
C 1 268 VAL 268 268 268 VAL VAL C . n 
C 1 269 THR 269 269 269 THR THR C . n 
C 1 270 CYS 270 270 270 CYS CYS C . n 
C 1 271 SER 271 271 271 SER SER C . n 
C 1 272 PRO 272 272 272 PRO PRO C . n 
C 1 273 ASP 273 273 273 ASP ASP C . n 
C 1 274 HIS 274 274 ?   ?   ?   C . n 
C 1 275 GLU 275 275 ?   ?   ?   C . n 
C 1 276 VAL 276 276 ?   ?   ?   C . n 
C 1 277 GLN 277 277 ?   ?   ?   C . n 
C 1 278 PRO 278 278 ?   ?   ?   C . n 
C 1 279 THR 279 279 ?   ?   ?   C . n 
C 1 280 LEU 280 280 ?   ?   ?   C . n 
C 1 281 PRO 281 281 ?   ?   ?   C . n 
C 1 282 SER 282 282 ?   ?   ?   C . n 
C 1 283 ASN 283 283 ?   ?   ?   C . n 
C 1 284 PRO 284 284 ?   ?   ?   C . n 
C 1 285 GLY 285 285 ?   ?   ?   C . n 
C 1 286 PRO 286 286 ?   ?   ?   C . n 
C 1 287 GLY 287 287 ?   ?   ?   C . n 
C 1 288 PRO 288 288 ?   ?   ?   C . n 
C 1 289 THR 289 289 289 THR THR C . n 
C 1 290 SER 290 290 290 SER SER C . n 
C 1 291 ALA 291 291 291 ALA ALA C . n 
C 1 292 SER 292 292 292 SER SER C . n 
C 1 293 ASN 293 293 293 ASN ASN C . n 
C 1 294 ILE 294 294 294 ILE ILE C . n 
C 1 295 THR 295 295 295 THR THR C . n 
C 1 296 VAL 296 296 296 VAL VAL C . n 
C 1 297 ILE 297 297 297 ILE ILE C . n 
C 1 298 TYR 298 298 298 TYR TYR C . n 
C 1 299 THR 299 299 299 THR THR C . n 
C 1 300 ILE 300 300 300 ILE ILE C . n 
C 1 301 ASN 301 301 301 ASN ASN C . n 
C 1 302 ASN 302 302 302 ASN ASN C . n 
C 1 303 GLN 303 303 303 GLN GLN C . n 
C 1 304 LEU 304 304 304 LEU LEU C . n 
C 1 305 ARG 305 305 305 ARG ARG C . n 
C 1 306 GLY 306 306 306 GLY GLY C . n 
C 1 307 VAL 307 307 307 VAL VAL C . n 
C 1 308 GLU 308 308 308 GLU GLU C . n 
C 1 309 LEU 309 309 309 LEU LEU C . n 
C 1 310 LEU 310 310 310 LEU LEU C . n 
C 1 311 PHE 311 311 311 PHE PHE C . n 
C 1 312 ASN 312 312 312 ASN ASN C . n 
C 1 313 GLU 313 313 313 GLU GLU C . n 
C 1 314 THR 314 314 314 THR THR C . n 
C 1 315 ILE 315 315 315 ILE ILE C . n 
C 1 316 ASN 316 316 316 ASN ASN C . n 
C 1 317 VAL 317 317 317 VAL VAL C . n 
C 1 318 SER 318 318 318 SER SER C . n 
C 1 319 VAL 319 319 319 VAL VAL C . n 
C 1 320 LYS 320 320 320 LYS LYS C . n 
C 1 321 SER 321 321 321 SER SER C . n 
C 1 322 GLY 322 322 322 GLY GLY C . n 
C 1 323 SER 323 323 323 SER SER C . n 
C 1 324 VAL 324 324 324 VAL VAL C . n 
C 1 325 LEU 325 325 325 LEU LEU C . n 
C 1 326 LEU 326 326 326 LEU LEU C . n 
C 1 327 VAL 327 327 327 VAL VAL C . n 
C 1 328 VAL 328 328 328 VAL VAL C . n 
C 1 329 LEU 329 329 329 LEU LEU C . n 
C 1 330 GLU 330 330 330 GLU GLU C . n 
C 1 331 GLU 331 331 331 GLU GLU C . n 
C 1 332 ALA 332 332 332 ALA ALA C . n 
C 1 333 GLN 333 333 333 GLN GLN C . n 
C 1 334 ARG 334 334 334 ARG ARG C . n 
C 1 335 LYS 335 335 335 LYS LYS C . n 
C 1 336 ASN 336 336 336 ASN ASN C . n 
C 1 337 PRO 337 337 337 PRO PRO C . n 
C 1 338 MET 338 338 338 MET MET C . n 
C 1 339 PHE 339 339 339 PHE PHE C . n 
C 1 340 LYS 340 340 340 LYS LYS C . n 
C 1 341 PHE 341 341 341 PHE PHE C . n 
C 1 342 GLU 342 342 342 GLU GLU C . n 
C 1 343 THR 343 343 343 THR THR C . n 
C 1 344 THR 344 344 344 THR THR C . n 
C 1 345 MET 345 345 345 MET MET C . n 
C 1 346 THR 346 346 346 THR THR C . n 
C 1 347 SER 347 347 347 SER SER C . n 
C 1 348 TRP 348 348 348 TRP TRP C . n 
C 1 349 GLY 349 349 349 GLY GLY C . n 
C 1 350 LEU 350 350 350 LEU LEU C . n 
C 1 351 VAL 351 351 351 VAL VAL C . n 
C 1 352 VAL 352 352 352 VAL VAL C . n 
C 1 353 SER 353 353 353 SER SER C . n 
C 1 354 SER 354 354 354 SER SER C . n 
C 1 355 ILE 355 355 355 ILE ILE C . n 
C 1 356 ASN 356 356 356 ASN ASN C . n 
C 1 357 ASN 357 357 357 ASN ASN C . n 
C 1 358 ILE 358 358 358 ILE ILE C . n 
C 1 359 ALA 359 359 359 ALA ALA C . n 
C 1 360 GLU 360 360 360 GLU GLU C . n 
C 1 361 ASN 361 361 361 ASN ASN C . n 
C 1 362 VAL 362 362 362 VAL VAL C . n 
C 1 363 ASN 363 363 363 ASN ASN C . n 
C 1 364 HIS 364 364 364 HIS HIS C . n 
C 1 365 LYS 365 365 365 LYS LYS C . n 
C 1 366 THR 366 366 366 THR THR C . n 
C 1 367 TYR 367 367 367 TYR TYR C . n 
C 1 368 TRP 368 368 368 TRP TRP C . n 
C 1 369 GLN 369 369 369 GLN GLN C . n 
C 1 370 PHE 370 370 370 PHE PHE C . n 
C 1 371 LEU 371 371 371 LEU LEU C . n 
C 1 372 SER 372 372 372 SER SER C . n 
C 1 373 GLY 373 373 373 GLY GLY C . n 
C 1 374 VAL 374 374 374 VAL VAL C . n 
C 1 375 THR 375 375 375 THR THR C . n 
C 1 376 PRO 376 376 376 PRO PRO C . n 
C 1 377 LEU 377 377 377 LEU LEU C . n 
C 1 378 ASN 378 378 378 ASN ASN C . n 
C 1 379 GLU 379 379 379 GLU GLU C . n 
C 1 380 GLY 380 380 380 GLY GLY C . n 
C 1 381 VAL 381 381 381 VAL VAL C . n 
C 1 382 ALA 382 382 382 ALA ALA C . n 
C 1 383 ASP 383 383 383 ASP ASP C . n 
C 1 384 TYR 384 384 384 TYR TYR C . n 
C 1 385 ILE 385 385 385 ILE ILE C . n 
C 1 386 PRO 386 386 386 PRO PRO C . n 
C 1 387 PHE 387 387 387 PHE PHE C . n 
C 1 388 ASN 388 388 388 ASN ASN C . n 
C 1 389 HIS 389 389 389 HIS HIS C . n 
C 1 390 GLU 390 390 390 GLU GLU C . n 
C 1 391 HIS 391 391 391 HIS HIS C . n 
C 1 392 ILE 392 392 392 ILE ILE C . n 
C 1 393 THR 393 393 393 THR THR C . n 
C 1 394 ALA 394 394 394 ALA ALA C . n 
C 1 395 ASN 395 395 395 ASN ASN C . n 
C 1 396 PHE 396 396 396 PHE PHE C . n 
C 1 397 THR 397 397 397 THR THR C . n 
C 1 398 GLN 398 398 398 GLN GLN C . n 
C 1 399 TYR 399 399 399 TYR TYR C . n 
D 1 1   SER 1   1   ?   ?   ?   D . n 
D 1 2   THR 2   2   ?   ?   ?   D . n 
D 1 3   GLN 3   3   ?   ?   ?   D . n 
D 1 4   THR 4   4   ?   ?   ?   D . n 
D 1 5   GLN 5   5   ?   ?   ?   D . n 
D 1 6   SER 6   6   ?   ?   ?   D . n 
D 1 7   SER 7   7   7   SER SER D . n 
D 1 8   CYS 8   8   8   CYS CYS D . n 
D 1 9   SER 9   9   9   SER SER D . n 
D 1 10  VAL 10  10  10  VAL VAL D . n 
D 1 11  PRO 11  11  11  PRO PRO D . n 
D 1 12  SER 12  12  12  SER SER D . n 
D 1 13  ALA 13  13  13  ALA ALA D . n 
D 1 14  GLN 14  14  14  GLN GLN D . n 
D 1 15  GLU 15  15  15  GLU GLU D . n 
D 1 16  PRO 16  16  16  PRO PRO D . n 
D 1 17  LEU 17  17  17  LEU LEU D . n 
D 1 18  VAL 18  18  18  VAL VAL D . n 
D 1 19  ASN 19  19  19  ASN ASN D . n 
D 1 20  GLY 20  20  20  GLY GLY D . n 
D 1 21  ILE 21  21  21  ILE ILE D . n 
D 1 22  GLN 22  22  22  GLN GLN D . n 
D 1 23  VAL 23  23  23  VAL VAL D . n 
D 1 24  LEU 24  24  24  LEU LEU D . n 
D 1 25  MET 25  25  25  MET MET D . n 
D 1 26  GLU 26  26  26  GLU GLU D . n 
D 1 27  ASN 27  27  27  ASN ASN D . n 
D 1 28  SER 28  28  28  SER SER D . n 
D 1 29  VAL 29  29  29  VAL VAL D . n 
D 1 30  THR 30  30  30  THR THR D . n 
D 1 31  SER 31  31  31  SER SER D . n 
D 1 32  SER 32  32  32  SER SER D . n 
D 1 33  ALA 33  33  33  ALA ALA D . n 
D 1 34  TYR 34  34  34  TYR TYR D . n 
D 1 35  PRO 35  35  35  PRO PRO D . n 
D 1 36  ASN 36  36  36  ASN ASN D . n 
D 1 37  PRO 37  37  37  PRO PRO D . n 
D 1 38  SER 38  38  38  SER SER D . n 
D 1 39  ILE 39  39  39  ILE ILE D . n 
D 1 40  LEU 40  40  40  LEU LEU D . n 
D 1 41  ILE 41  41  41  ILE ILE D . n 
D 1 42  ALA 42  42  42  ALA ALA D . n 
D 1 43  MET 43  43  43  MET MET D . n 
D 1 44  ASN 44  44  44  ASN ASN D . n 
D 1 45  LEU 45  45  45  LEU LEU D . n 
D 1 46  ALA 46  46  46  ALA ALA D . n 
D 1 47  GLY 47  47  47  GLY GLY D . n 
D 1 48  ALA 48  48  48  ALA ALA D . n 
D 1 49  TYR 49  49  49  TYR TYR D . n 
D 1 50  ASN 50  50  50  ASN ASN D . n 
D 1 51  LEU 51  51  51  LEU LEU D . n 
D 1 52  LYS 52  52  52  LYS LYS D . n 
D 1 53  ALA 53  53  53  ALA ALA D . n 
D 1 54  GLN 54  54  54  GLN GLN D . n 
D 1 55  LYS 55  55  55  LYS LYS D . n 
D 1 56  LEU 56  56  56  LEU LEU D . n 
D 1 57  LEU 57  57  57  LEU LEU D . n 
D 1 58  THR 58  58  58  THR THR D . n 
D 1 59  TYR 59  59  59  TYR TYR D . n 
D 1 60  GLN 60  60  60  GLN GLN D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  MET 62  62  62  MET MET D . n 
D 1 63  SER 63  63  63  SER SER D . n 
D 1 64  SER 64  64  64  SER SER D . n 
D 1 65  ASP 65  65  65  ASP ASP D . n 
D 1 66  ASN 66  66  66  ASN ASN D . n 
D 1 67  ASN 67  67  67  ASN ASN D . n 
D 1 68  ASP 68  68  68  ASP ASP D . n 
D 1 69  LEU 69  69  69  LEU LEU D . n 
D 1 70  THR 70  70  70  THR THR D . n 
D 1 71  ILE 71  71  71  ILE ILE D . n 
D 1 72  GLY 72  72  72  GLY GLY D . n 
D 1 73  HIS 73  73  73  HIS HIS D . n 
D 1 74  LEU 74  74  74  LEU LEU D . n 
D 1 75  GLY 75  75  75  GLY GLY D . n 
D 1 76  LEU 76  76  76  LEU LEU D . n 
D 1 77  THR 77  77  77  THR THR D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  MET 79  79  79  MET MET D . n 
D 1 80  ALA 80  80  80  ALA ALA D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  THR 82  82  82  THR THR D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  SER 84  84  84  SER SER D . n 
D 1 85  CYS 85  85  85  CYS CYS D . n 
D 1 86  ARG 86  86  86  ARG ARG D . n 
D 1 87  ASP 87  87  87  ASP ASP D . n 
D 1 88  PRO 88  88  88  PRO PRO D . n 
D 1 89  GLY 89  89  89  GLY GLY D . n 
D 1 90  ASP 90  90  90  ASP ASP D . n 
D 1 91  LYS 91  91  91  LYS LYS D . n 
D 1 92  VAL 92  92  92  VAL VAL D . n 
D 1 93  SER 93  93  93  SER SER D . n 
D 1 94  ILE 94  94  94  ILE ILE D . n 
D 1 95  LEU 95  95  95  LEU LEU D . n 
D 1 96  GLN 96  96  96  GLN GLN D . n 
D 1 97  ARG 97  97  97  ARG ARG D . n 
D 1 98  GLN 98  98  98  GLN GLN D . n 
D 1 99  MET 99  99  99  MET MET D . n 
D 1 100 GLU 100 100 100 GLU GLU D . n 
D 1 101 ASN 101 101 101 ASN ASN D . n 
D 1 102 TRP 102 102 102 TRP TRP D . n 
D 1 103 ALA 103 103 103 ALA ALA D . n 
D 1 104 PRO 104 104 104 PRO PRO D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 SER 106 106 106 SER SER D . n 
D 1 107 PRO 107 107 107 PRO PRO D . n 
D 1 108 ASN 108 108 108 ASN ASN D . n 
D 1 109 ALA 109 109 109 ALA ALA D . n 
D 1 110 GLU 110 110 110 GLU GLU D . n 
D 1 111 ALA 111 111 111 ALA ALA D . n 
D 1 112 SER 112 112 112 SER SER D . n 
D 1 113 ALA 113 113 113 ALA ALA D . n 
D 1 114 PHE 114 114 114 PHE PHE D . n 
D 1 115 TYR 115 115 115 TYR TYR D . n 
D 1 116 GLY 116 116 116 GLY GLY D . n 
D 1 117 PRO 117 117 117 PRO PRO D . n 
D 1 118 SER 118 118 118 SER SER D . n 
D 1 119 LEU 119 119 119 LEU LEU D . n 
D 1 120 ALA 120 120 120 ALA ALA D . n 
D 1 121 ILE 121 121 121 ILE ILE D . n 
D 1 122 LEU 122 122 122 LEU LEU D . n 
D 1 123 ALA 123 123 123 ALA ALA D . n 
D 1 124 LEU 124 124 124 LEU LEU D . n 
D 1 125 CYS 125 125 125 CYS CYS D . n 
D 1 126 GLN 126 126 126 GLN GLN D . n 
D 1 127 LYS 127 127 127 LYS LYS D . n 
D 1 128 ASN 128 128 128 ASN ASN D . n 
D 1 129 SER 129 129 129 SER SER D . n 
D 1 130 GLU 130 130 130 GLU GLU D . n 
D 1 131 ALA 131 131 131 ALA ALA D . n 
D 1 132 THR 132 132 132 THR THR D . n 
D 1 133 LEU 133 133 133 LEU LEU D . n 
D 1 134 PRO 134 134 134 PRO PRO D . n 
D 1 135 ILE 135 135 135 ILE ILE D . n 
D 1 136 ALA 136 136 136 ALA ALA D . n 
D 1 137 VAL 137 137 137 VAL VAL D . n 
D 1 138 ARG 138 138 138 ARG ARG D . n 
D 1 139 PHE 139 139 139 PHE PHE D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 LYS 141 141 141 LYS LYS D . n 
D 1 142 THR 142 142 142 THR THR D . n 
D 1 143 LEU 143 143 143 LEU LEU D . n 
D 1 144 LEU 144 144 144 LEU LEU D . n 
D 1 145 ALA 145 145 145 ALA ALA D . n 
D 1 146 ASN 146 146 146 ASN ASN D . n 
D 1 147 SER 147 147 147 SER SER D . n 
D 1 148 SER 148 148 148 SER SER D . n 
D 1 149 PRO 149 149 149 PRO PRO D . n 
D 1 150 PHE 150 150 150 PHE PHE D . n 
D 1 151 ASN 151 151 151 ASN ASN D . n 
D 1 152 VAL 152 152 152 VAL VAL D . n 
D 1 153 ASP 153 153 153 ASP ASP D . n 
D 1 154 THR 154 154 154 THR THR D . n 
D 1 155 GLY 155 155 155 GLY GLY D . n 
D 1 156 ALA 156 156 156 ALA ALA D . n 
D 1 157 MET 157 157 157 MET MET D . n 
D 1 158 ALA 158 158 158 ALA ALA D . n 
D 1 159 THR 159 159 159 THR THR D . n 
D 1 160 LEU 160 160 160 LEU LEU D . n 
D 1 161 ALA 161 161 161 ALA ALA D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 THR 163 163 163 THR THR D . n 
D 1 164 CYS 164 164 164 CYS CYS D . n 
D 1 165 MET 165 165 165 MET MET D . n 
D 1 166 TYR 166 166 166 TYR TYR D . n 
D 1 167 ASN 167 167 167 ASN ASN D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 ILE 169 169 169 ILE ILE D . n 
D 1 170 PRO 170 170 170 PRO PRO D . n 
D 1 171 VAL 171 171 171 VAL VAL D . n 
D 1 172 GLY 172 172 172 GLY GLY D . n 
D 1 173 SER 173 173 173 SER SER D . n 
D 1 174 GLU 174 174 174 GLU GLU D . n 
D 1 175 GLU 175 175 175 GLU GLU D . n 
D 1 176 GLY 176 176 176 GLY GLY D . n 
D 1 177 TYR 177 177 177 TYR TYR D . n 
D 1 178 ARG 178 178 178 ARG ARG D . n 
D 1 179 SER 179 179 179 SER SER D . n 
D 1 180 LEU 180 180 180 LEU LEU D . n 
D 1 181 PHE 181 181 181 PHE PHE D . n 
D 1 182 GLY 182 182 182 GLY GLY D . n 
D 1 183 GLN 183 183 183 GLN GLN D . n 
D 1 184 VAL 184 184 184 VAL VAL D . n 
D 1 185 LEU 185 185 185 LEU LEU D . n 
D 1 186 LYS 186 186 186 LYS LYS D . n 
D 1 187 ASP 187 187 187 ASP ASP D . n 
D 1 188 ILE 188 188 188 ILE ILE D . n 
D 1 189 VAL 189 189 189 VAL VAL D . n 
D 1 190 GLU 190 190 190 GLU GLU D . n 
D 1 191 LYS 191 191 191 LYS LYS D . n 
D 1 192 ILE 192 192 192 ILE ILE D . n 
D 1 193 SER 193 193 193 SER SER D . n 
D 1 194 MET 194 194 194 MET MET D . n 
D 1 195 LYS 195 195 195 LYS LYS D . n 
D 1 196 ILE 196 196 196 ILE ILE D . n 
D 1 197 LYS 197 197 197 LYS LYS D . n 
D 1 198 ASP 198 198 198 ASP ASP D . n 
D 1 199 ASN 199 199 199 ASN ASN D . n 
D 1 200 GLY 200 200 200 GLY GLY D . n 
D 1 201 ILE 201 201 201 ILE ILE D . n 
D 1 202 ILE 202 202 202 ILE ILE D . n 
D 1 203 GLY 203 203 203 GLY GLY D . n 
D 1 204 ASP 204 204 204 ASP ASP D . n 
D 1 205 ILE 205 205 205 ILE ILE D . n 
D 1 206 TYR 206 206 206 TYR TYR D . n 
D 1 207 SER 207 207 207 SER SER D . n 
D 1 208 THR 208 208 208 THR THR D . n 
D 1 209 GLY 209 209 209 GLY GLY D . n 
D 1 210 LEU 210 210 210 LEU LEU D . n 
D 1 211 ALA 211 211 211 ALA ALA D . n 
D 1 212 MET 212 212 212 MET MET D . n 
D 1 213 GLN 213 213 213 GLN GLN D . n 
D 1 214 ALA 214 214 214 ALA ALA D . n 
D 1 215 LEU 215 215 215 LEU LEU D . n 
D 1 216 SER 216 216 216 SER SER D . n 
D 1 217 VAL 217 217 217 VAL VAL D . n 
D 1 218 THR 218 218 218 THR THR D . n 
D 1 219 PRO 219 219 219 PRO PRO D . n 
D 1 220 GLU 220 220 220 GLU GLU D . n 
D 1 221 PRO 221 221 221 PRO PRO D . n 
D 1 222 SER 222 222 222 SER SER D . n 
D 1 223 LYS 223 223 223 LYS LYS D . n 
D 1 224 LYS 224 224 224 LYS LYS D . n 
D 1 225 GLU 225 225 225 GLU GLU D . n 
D 1 226 TRP 226 226 226 TRP TRP D . n 
D 1 227 ASN 227 227 227 ASN ASN D . n 
D 1 228 CYS 228 228 228 CYS CYS D . n 
D 1 229 LYS 229 229 229 LYS LYS D . n 
D 1 230 LYS 230 230 230 LYS LYS D . n 
D 1 231 THR 231 231 231 THR THR D . n 
D 1 232 THR 232 232 232 THR THR D . n 
D 1 233 ASP 233 233 233 ASP ASP D . n 
D 1 234 MET 234 234 234 MET MET D . n 
D 1 235 ILE 235 235 235 ILE ILE D . n 
D 1 236 LEU 236 236 236 LEU LEU D . n 
D 1 237 ASN 237 237 237 ASN ASN D . n 
D 1 238 GLU 238 238 238 GLU GLU D . n 
D 1 239 ILE 239 239 239 ILE ILE D . n 
D 1 240 LYS 240 240 240 LYS LYS D . n 
D 1 241 GLN 241 241 241 GLN GLN D . n 
D 1 242 GLY 242 242 242 GLY GLY D . n 
D 1 243 LYS 243 243 243 LYS LYS D . n 
D 1 244 PHE 244 244 244 PHE PHE D . n 
D 1 245 HIS 245 245 245 HIS HIS D . n 
D 1 246 ASN 246 246 246 ASN ASN D . n 
D 1 247 PRO 247 247 247 PRO PRO D . n 
D 1 248 MET 248 248 248 MET MET D . n 
D 1 249 SER 249 249 249 SER SER D . n 
D 1 250 ILE 250 250 250 ILE ILE D . n 
D 1 251 ALA 251 251 251 ALA ALA D . n 
D 1 252 GLN 252 252 252 GLN GLN D . n 
D 1 253 ILE 253 253 253 ILE ILE D . n 
D 1 254 LEU 254 254 254 LEU LEU D . n 
D 1 255 PRO 255 255 255 PRO PRO D . n 
D 1 256 SER 256 256 256 SER SER D . n 
D 1 257 LEU 257 257 257 LEU LEU D . n 
D 1 258 LYS 258 258 258 LYS LYS D . n 
D 1 259 GLY 259 259 259 GLY GLY D . n 
D 1 260 LYS 260 260 260 LYS LYS D . n 
D 1 261 THR 261 261 261 THR THR D . n 
D 1 262 TYR 262 262 262 TYR TYR D . n 
D 1 263 LEU 263 263 263 LEU LEU D . n 
D 1 264 ASP 264 264 264 ASP ASP D . n 
D 1 265 VAL 265 265 265 VAL VAL D . n 
D 1 266 PRO 266 266 266 PRO PRO D . n 
D 1 267 GLN 267 267 267 GLN GLN D . n 
D 1 268 VAL 268 268 268 VAL VAL D . n 
D 1 269 THR 269 269 269 THR THR D . n 
D 1 270 CYS 270 270 270 CYS CYS D . n 
D 1 271 SER 271 271 271 SER SER D . n 
D 1 272 PRO 272 272 272 PRO PRO D . n 
D 1 273 ASP 273 273 273 ASP ASP D . n 
D 1 274 HIS 274 274 ?   ?   ?   D . n 
D 1 275 GLU 275 275 ?   ?   ?   D . n 
D 1 276 VAL 276 276 ?   ?   ?   D . n 
D 1 277 GLN 277 277 ?   ?   ?   D . n 
D 1 278 PRO 278 278 ?   ?   ?   D . n 
D 1 279 THR 279 279 ?   ?   ?   D . n 
D 1 280 LEU 280 280 ?   ?   ?   D . n 
D 1 281 PRO 281 281 ?   ?   ?   D . n 
D 1 282 SER 282 282 ?   ?   ?   D . n 
D 1 283 ASN 283 283 ?   ?   ?   D . n 
D 1 284 PRO 284 284 ?   ?   ?   D . n 
D 1 285 GLY 285 285 ?   ?   ?   D . n 
D 1 286 PRO 286 286 ?   ?   ?   D . n 
D 1 287 GLY 287 287 ?   ?   ?   D . n 
D 1 288 PRO 288 288 ?   ?   ?   D . n 
D 1 289 THR 289 289 ?   ?   ?   D . n 
D 1 290 SER 290 290 ?   ?   ?   D . n 
D 1 291 ALA 291 291 ?   ?   ?   D . n 
D 1 292 SER 292 292 ?   ?   ?   D . n 
D 1 293 ASN 293 293 ?   ?   ?   D . n 
D 1 294 ILE 294 294 ?   ?   ?   D . n 
D 1 295 THR 295 295 ?   ?   ?   D . n 
D 1 296 VAL 296 296 ?   ?   ?   D . n 
D 1 297 ILE 297 297 ?   ?   ?   D . n 
D 1 298 TYR 298 298 ?   ?   ?   D . n 
D 1 299 THR 299 299 ?   ?   ?   D . n 
D 1 300 ILE 300 300 ?   ?   ?   D . n 
D 1 301 ASN 301 301 ?   ?   ?   D . n 
D 1 302 ASN 302 302 ?   ?   ?   D . n 
D 1 303 GLN 303 303 ?   ?   ?   D . n 
D 1 304 LEU 304 304 ?   ?   ?   D . n 
D 1 305 ARG 305 305 ?   ?   ?   D . n 
D 1 306 GLY 306 306 ?   ?   ?   D . n 
D 1 307 VAL 307 307 ?   ?   ?   D . n 
D 1 308 GLU 308 308 ?   ?   ?   D . n 
D 1 309 LEU 309 309 ?   ?   ?   D . n 
D 1 310 LEU 310 310 ?   ?   ?   D . n 
D 1 311 PHE 311 311 ?   ?   ?   D . n 
D 1 312 ASN 312 312 ?   ?   ?   D . n 
D 1 313 GLU 313 313 ?   ?   ?   D . n 
D 1 314 THR 314 314 ?   ?   ?   D . n 
D 1 315 ILE 315 315 ?   ?   ?   D . n 
D 1 316 ASN 316 316 ?   ?   ?   D . n 
D 1 317 VAL 317 317 ?   ?   ?   D . n 
D 1 318 SER 318 318 ?   ?   ?   D . n 
D 1 319 VAL 319 319 ?   ?   ?   D . n 
D 1 320 LYS 320 320 ?   ?   ?   D . n 
D 1 321 SER 321 321 ?   ?   ?   D . n 
D 1 322 GLY 322 322 ?   ?   ?   D . n 
D 1 323 SER 323 323 ?   ?   ?   D . n 
D 1 324 VAL 324 324 ?   ?   ?   D . n 
D 1 325 LEU 325 325 ?   ?   ?   D . n 
D 1 326 LEU 326 326 ?   ?   ?   D . n 
D 1 327 VAL 327 327 ?   ?   ?   D . n 
D 1 328 VAL 328 328 ?   ?   ?   D . n 
D 1 329 LEU 329 329 ?   ?   ?   D . n 
D 1 330 GLU 330 330 ?   ?   ?   D . n 
D 1 331 GLU 331 331 ?   ?   ?   D . n 
D 1 332 ALA 332 332 ?   ?   ?   D . n 
D 1 333 GLN 333 333 ?   ?   ?   D . n 
D 1 334 ARG 334 334 ?   ?   ?   D . n 
D 1 335 LYS 335 335 ?   ?   ?   D . n 
D 1 336 ASN 336 336 ?   ?   ?   D . n 
D 1 337 PRO 337 337 ?   ?   ?   D . n 
D 1 338 MET 338 338 ?   ?   ?   D . n 
D 1 339 PHE 339 339 ?   ?   ?   D . n 
D 1 340 LYS 340 340 ?   ?   ?   D . n 
D 1 341 PHE 341 341 ?   ?   ?   D . n 
D 1 342 GLU 342 342 ?   ?   ?   D . n 
D 1 343 THR 343 343 ?   ?   ?   D . n 
D 1 344 THR 344 344 ?   ?   ?   D . n 
D 1 345 MET 345 345 ?   ?   ?   D . n 
D 1 346 THR 346 346 ?   ?   ?   D . n 
D 1 347 SER 347 347 ?   ?   ?   D . n 
D 1 348 TRP 348 348 ?   ?   ?   D . n 
D 1 349 GLY 349 349 ?   ?   ?   D . n 
D 1 350 LEU 350 350 ?   ?   ?   D . n 
D 1 351 VAL 351 351 ?   ?   ?   D . n 
D 1 352 VAL 352 352 ?   ?   ?   D . n 
D 1 353 SER 353 353 ?   ?   ?   D . n 
D 1 354 SER 354 354 ?   ?   ?   D . n 
D 1 355 ILE 355 355 ?   ?   ?   D . n 
D 1 356 ASN 356 356 ?   ?   ?   D . n 
D 1 357 ASN 357 357 ?   ?   ?   D . n 
D 1 358 ILE 358 358 ?   ?   ?   D . n 
D 1 359 ALA 359 359 ?   ?   ?   D . n 
D 1 360 GLU 360 360 ?   ?   ?   D . n 
D 1 361 ASN 361 361 ?   ?   ?   D . n 
D 1 362 VAL 362 362 ?   ?   ?   D . n 
D 1 363 ASN 363 363 ?   ?   ?   D . n 
D 1 364 HIS 364 364 ?   ?   ?   D . n 
D 1 365 LYS 365 365 ?   ?   ?   D . n 
D 1 366 THR 366 366 ?   ?   ?   D . n 
D 1 367 TYR 367 367 ?   ?   ?   D . n 
D 1 368 TRP 368 368 ?   ?   ?   D . n 
D 1 369 GLN 369 369 ?   ?   ?   D . n 
D 1 370 PHE 370 370 ?   ?   ?   D . n 
D 1 371 LEU 371 371 ?   ?   ?   D . n 
D 1 372 SER 372 372 ?   ?   ?   D . n 
D 1 373 GLY 373 373 ?   ?   ?   D . n 
D 1 374 VAL 374 374 ?   ?   ?   D . n 
D 1 375 THR 375 375 ?   ?   ?   D . n 
D 1 376 PRO 376 376 ?   ?   ?   D . n 
D 1 377 LEU 377 377 ?   ?   ?   D . n 
D 1 378 ASN 378 378 ?   ?   ?   D . n 
D 1 379 GLU 379 379 ?   ?   ?   D . n 
D 1 380 GLY 380 380 ?   ?   ?   D . n 
D 1 381 VAL 381 381 ?   ?   ?   D . n 
D 1 382 ALA 382 382 ?   ?   ?   D . n 
D 1 383 ASP 383 383 ?   ?   ?   D . n 
D 1 384 TYR 384 384 ?   ?   ?   D . n 
D 1 385 ILE 385 385 ?   ?   ?   D . n 
D 1 386 PRO 386 386 ?   ?   ?   D . n 
D 1 387 PHE 387 387 ?   ?   ?   D . n 
D 1 388 ASN 388 388 ?   ?   ?   D . n 
D 1 389 HIS 389 389 ?   ?   ?   D . n 
D 1 390 GLU 390 390 ?   ?   ?   D . n 
D 1 391 HIS 391 391 ?   ?   ?   D . n 
D 1 392 ILE 392 392 ?   ?   ?   D . n 
D 1 393 THR 393 393 ?   ?   ?   D . n 
D 1 394 ALA 394 394 ?   ?   ?   D . n 
D 1 395 ASN 395 395 ?   ?   ?   D . n 
D 1 396 PHE 396 396 ?   ?   ?   D . n 
D 1 397 THR 397 397 ?   ?   ?   D . n 
D 1 398 GLN 398 398 ?   ?   ?   D . n 
D 1 399 TYR 399 399 ?   ?   ?   D . 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 
E 2 NAG 1   901  901  NAG NAG A . 
F 2 NAG 2   902  902  NAG NAG A . 
G 3 B12 1   1001 1001 B12 B12 A . 
H 2 NAG 1   901  901  NAG NAG C . 
I 2 NAG 2   902  902  NAG NAG C . 
J 3 B12 1   1002 1002 B12 B12 C . 
K 4 HOH 1   1002 1002 HOH HOH A . 
K 4 HOH 2   1003 1003 HOH HOH A . 
K 4 HOH 3   1004 1004 HOH HOH A . 
K 4 HOH 4   1005 1005 HOH HOH A . 
K 4 HOH 5   1006 1006 HOH HOH A . 
K 4 HOH 6   1007 1007 HOH HOH A . 
K 4 HOH 7   1008 1008 HOH HOH A . 
K 4 HOH 8   1009 1009 HOH HOH A . 
K 4 HOH 9   1010 1010 HOH HOH A . 
K 4 HOH 10  1011 1011 HOH HOH A . 
K 4 HOH 11  1012 1012 HOH HOH A . 
K 4 HOH 12  1013 1013 HOH HOH A . 
K 4 HOH 13  1014 1014 HOH HOH A . 
K 4 HOH 14  1015 1015 HOH HOH A . 
K 4 HOH 15  1016 1016 HOH HOH A . 
K 4 HOH 16  1017 1017 HOH HOH A . 
K 4 HOH 17  1018 1018 HOH HOH A . 
K 4 HOH 18  1019 1019 HOH HOH A . 
K 4 HOH 19  1020 1020 HOH HOH A . 
K 4 HOH 20  1021 1021 HOH HOH A . 
K 4 HOH 21  1022 1022 HOH HOH A . 
K 4 HOH 22  1023 1023 HOH HOH A . 
K 4 HOH 23  1024 1024 HOH HOH A . 
K 4 HOH 24  1025 1025 HOH HOH A . 
K 4 HOH 25  1026 1026 HOH HOH A . 
K 4 HOH 26  1027 1027 HOH HOH A . 
K 4 HOH 27  1028 1028 HOH HOH A . 
K 4 HOH 28  1029 1029 HOH HOH A . 
K 4 HOH 29  1030 1030 HOH HOH A . 
K 4 HOH 30  1031 1031 HOH HOH A . 
K 4 HOH 31  1032 1032 HOH HOH A . 
K 4 HOH 32  1033 1033 HOH HOH A . 
K 4 HOH 33  1034 1034 HOH HOH A . 
K 4 HOH 34  1035 1035 HOH HOH A . 
K 4 HOH 35  1036 1036 HOH HOH A . 
K 4 HOH 36  1037 1037 HOH HOH A . 
K 4 HOH 37  1038 1038 HOH HOH A . 
K 4 HOH 38  1039 1039 HOH HOH A . 
K 4 HOH 39  1040 1040 HOH HOH A . 
K 4 HOH 40  1041 1041 HOH HOH A . 
K 4 HOH 41  1042 1042 HOH HOH A . 
K 4 HOH 42  1043 1043 HOH HOH A . 
K 4 HOH 43  1044 1044 HOH HOH A . 
K 4 HOH 44  1045 1045 HOH HOH A . 
K 4 HOH 45  1046 1046 HOH HOH A . 
K 4 HOH 46  1047 1047 HOH HOH A . 
K 4 HOH 47  1048 1048 HOH HOH A . 
K 4 HOH 48  1049 1049 HOH HOH A . 
K 4 HOH 49  1050 1050 HOH HOH A . 
K 4 HOH 50  1051 1051 HOH HOH A . 
K 4 HOH 51  1052 1052 HOH HOH A . 
K 4 HOH 52  1053 1053 HOH HOH A . 
K 4 HOH 53  1054 1054 HOH HOH A . 
K 4 HOH 54  1055 1055 HOH HOH A . 
K 4 HOH 55  1056 1056 HOH HOH A . 
K 4 HOH 56  1057 1057 HOH HOH A . 
K 4 HOH 57  1058 1058 HOH HOH A . 
K 4 HOH 58  1059 1059 HOH HOH A . 
K 4 HOH 59  1060 1060 HOH HOH A . 
K 4 HOH 60  1061 1061 HOH HOH A . 
K 4 HOH 61  1062 1062 HOH HOH A . 
K 4 HOH 62  1063 1063 HOH HOH A . 
K 4 HOH 63  1064 1064 HOH HOH A . 
K 4 HOH 64  1065 1065 HOH HOH A . 
K 4 HOH 65  1066 1066 HOH HOH A . 
K 4 HOH 66  1067 1067 HOH HOH A . 
K 4 HOH 67  1068 1068 HOH HOH A . 
K 4 HOH 68  1069 1069 HOH HOH A . 
K 4 HOH 69  1070 1070 HOH HOH A . 
K 4 HOH 70  1071 1071 HOH HOH A . 
K 4 HOH 71  1072 1072 HOH HOH A . 
K 4 HOH 72  1073 1073 HOH HOH A . 
K 4 HOH 73  1074 1074 HOH HOH A . 
K 4 HOH 74  1075 1075 HOH HOH A . 
K 4 HOH 75  1076 1076 HOH HOH A . 
K 4 HOH 76  1077 1077 HOH HOH A . 
K 4 HOH 77  1078 1078 HOH HOH A . 
K 4 HOH 78  1079 1079 HOH HOH A . 
K 4 HOH 79  1080 1080 HOH HOH A . 
K 4 HOH 80  1081 1081 HOH HOH A . 
K 4 HOH 81  1082 1082 HOH HOH A . 
K 4 HOH 82  1083 1083 HOH HOH A . 
K 4 HOH 83  1084 1084 HOH HOH A . 
K 4 HOH 84  1085 1085 HOH HOH A . 
K 4 HOH 85  1086 1086 HOH HOH A . 
K 4 HOH 86  1087 1087 HOH HOH A . 
K 4 HOH 87  1088 1088 HOH HOH A . 
K 4 HOH 88  1089 1089 HOH HOH A . 
K 4 HOH 89  1090 1090 HOH HOH A . 
K 4 HOH 90  1091 1091 HOH HOH A . 
K 4 HOH 91  1092 1092 HOH HOH A . 
K 4 HOH 92  1093 1093 HOH HOH A . 
K 4 HOH 93  1094 1095 HOH HOH A . 
K 4 HOH 94  1095 1096 HOH HOH A . 
K 4 HOH 95  1096 1097 HOH HOH A . 
K 4 HOH 96  1097 1098 HOH HOH A . 
K 4 HOH 97  1098 1099 HOH HOH A . 
K 4 HOH 98  1099 1100 HOH HOH A . 
K 4 HOH 99  1100 1102 HOH HOH A . 
K 4 HOH 100 1101 1103 HOH HOH A . 
K 4 HOH 101 1102 1104 HOH HOH A . 
K 4 HOH 102 1103 1105 HOH HOH A . 
K 4 HOH 103 1104 1106 HOH HOH A . 
K 4 HOH 104 1105 1107 HOH HOH A . 
K 4 HOH 105 1106 1108 HOH HOH A . 
K 4 HOH 106 1107 1109 HOH HOH A . 
K 4 HOH 107 1108 1110 HOH HOH A . 
K 4 HOH 108 1109 1111 HOH HOH A . 
K 4 HOH 109 1110 1112 HOH HOH A . 
K 4 HOH 110 1111 1113 HOH HOH A . 
K 4 HOH 111 1112 1114 HOH HOH A . 
K 4 HOH 112 1113 1115 HOH HOH A . 
K 4 HOH 113 1114 1116 HOH HOH A . 
K 4 HOH 114 1115 1117 HOH HOH A . 
K 4 HOH 115 1116 1118 HOH HOH A . 
K 4 HOH 116 1117 1119 HOH HOH A . 
K 4 HOH 117 1118 1120 HOH HOH A . 
K 4 HOH 118 1119 1121 HOH HOH A . 
K 4 HOH 119 1120 1122 HOH HOH A . 
K 4 HOH 120 1121 1123 HOH HOH A . 
K 4 HOH 121 1122 1124 HOH HOH A . 
K 4 HOH 122 1123 1125 HOH HOH A . 
K 4 HOH 123 1124 1126 HOH HOH A . 
K 4 HOH 124 1125 1127 HOH HOH A . 
K 4 HOH 125 1126 1128 HOH HOH A . 
K 4 HOH 126 1127 1129 HOH HOH A . 
K 4 HOH 127 1128 1130 HOH HOH A . 
K 4 HOH 128 1129 1131 HOH HOH A . 
K 4 HOH 129 1130 1132 HOH HOH A . 
K 4 HOH 130 1131 1133 HOH HOH A . 
K 4 HOH 131 1132 1134 HOH HOH A . 
K 4 HOH 132 1133 1135 HOH HOH A . 
K 4 HOH 133 1134 1136 HOH HOH A . 
K 4 HOH 134 1135 1137 HOH HOH A . 
K 4 HOH 135 1136 1062 HOH HOH A . 
L 4 HOH 1   400  274  HOH HOH B . 
L 4 HOH 2   401  275  HOH HOH B . 
L 4 HOH 3   402  276  HOH HOH B . 
L 4 HOH 4   403  277  HOH HOH B . 
L 4 HOH 5   404  278  HOH HOH B . 
L 4 HOH 6   405  279  HOH HOH B . 
L 4 HOH 7   406  280  HOH HOH B . 
L 4 HOH 8   407  281  HOH HOH B . 
L 4 HOH 9   408  282  HOH HOH B . 
L 4 HOH 10  409  283  HOH HOH B . 
L 4 HOH 11  410  284  HOH HOH B . 
L 4 HOH 12  411  285  HOH HOH B . 
L 4 HOH 13  412  286  HOH HOH B . 
L 4 HOH 14  413  287  HOH HOH B . 
L 4 HOH 15  414  288  HOH HOH B . 
L 4 HOH 16  415  289  HOH HOH B . 
L 4 HOH 17  416  290  HOH HOH B . 
L 4 HOH 18  417  291  HOH HOH B . 
L 4 HOH 19  418  292  HOH HOH B . 
L 4 HOH 20  419  293  HOH HOH B . 
L 4 HOH 21  420  294  HOH HOH B . 
L 4 HOH 22  421  295  HOH HOH B . 
L 4 HOH 23  422  296  HOH HOH B . 
L 4 HOH 24  423  297  HOH HOH B . 
L 4 HOH 25  424  298  HOH HOH B . 
L 4 HOH 26  425  299  HOH HOH B . 
L 4 HOH 27  426  300  HOH HOH B . 
L 4 HOH 28  427  301  HOH HOH B . 
L 4 HOH 29  428  302  HOH HOH B . 
L 4 HOH 30  429  303  HOH HOH B . 
L 4 HOH 31  430  304  HOH HOH B . 
L 4 HOH 32  431  305  HOH HOH B . 
L 4 HOH 33  432  306  HOH HOH B . 
L 4 HOH 34  433  307  HOH HOH B . 
L 4 HOH 35  434  308  HOH HOH B . 
L 4 HOH 36  435  309  HOH HOH B . 
L 4 HOH 37  436  310  HOH HOH B . 
L 4 HOH 38  437  311  HOH HOH B . 
L 4 HOH 39  438  312  HOH HOH B . 
L 4 HOH 40  439  313  HOH HOH B . 
L 4 HOH 41  440  314  HOH HOH B . 
L 4 HOH 42  441  315  HOH HOH B . 
L 4 HOH 43  442  316  HOH HOH B . 
L 4 HOH 44  443  317  HOH HOH B . 
L 4 HOH 45  444  318  HOH HOH B . 
L 4 HOH 46  445  319  HOH HOH B . 
L 4 HOH 47  446  320  HOH HOH B . 
L 4 HOH 48  447  321  HOH HOH B . 
L 4 HOH 49  448  322  HOH HOH B . 
L 4 HOH 50  449  323  HOH HOH B . 
L 4 HOH 51  450  324  HOH HOH B . 
L 4 HOH 52  451  325  HOH HOH B . 
L 4 HOH 53  452  326  HOH HOH B . 
L 4 HOH 54  453  327  HOH HOH B . 
L 4 HOH 55  454  328  HOH HOH B . 
L 4 HOH 56  455  329  HOH HOH B . 
L 4 HOH 57  456  330  HOH HOH B . 
L 4 HOH 58  457  331  HOH HOH B . 
L 4 HOH 59  458  332  HOH HOH B . 
L 4 HOH 60  459  333  HOH HOH B . 
L 4 HOH 61  460  334  HOH HOH B . 
L 4 HOH 62  461  335  HOH HOH B . 
L 4 HOH 63  462  336  HOH HOH B . 
L 4 HOH 64  463  337  HOH HOH B . 
L 4 HOH 65  464  338  HOH HOH B . 
L 4 HOH 66  465  339  HOH HOH B . 
L 4 HOH 67  466  340  HOH HOH B . 
L 4 HOH 68  467  341  HOH HOH B . 
L 4 HOH 69  468  342  HOH HOH B . 
L 4 HOH 70  469  343  HOH HOH B . 
L 4 HOH 71  470  344  HOH HOH B . 
L 4 HOH 72  471  345  HOH HOH B . 
L 4 HOH 73  472  346  HOH HOH B . 
L 4 HOH 74  473  347  HOH HOH B . 
L 4 HOH 75  474  348  HOH HOH B . 
L 4 HOH 76  475  349  HOH HOH B . 
L 4 HOH 77  476  350  HOH HOH B . 
L 4 HOH 78  477  351  HOH HOH B . 
L 4 HOH 79  478  352  HOH HOH B . 
L 4 HOH 80  479  353  HOH HOH B . 
L 4 HOH 81  480  354  HOH HOH B . 
L 4 HOH 82  481  355  HOH HOH B . 
L 4 HOH 83  482  356  HOH HOH B . 
L 4 HOH 84  483  357  HOH HOH B . 
L 4 HOH 85  484  358  HOH HOH B . 
L 4 HOH 86  485  359  HOH HOH B . 
L 4 HOH 87  486  360  HOH HOH B . 
L 4 HOH 88  487  361  HOH HOH B . 
L 4 HOH 89  488  362  HOH HOH B . 
L 4 HOH 90  489  363  HOH HOH B . 
L 4 HOH 91  490  364  HOH HOH B . 
L 4 HOH 92  491  365  HOH HOH B . 
L 4 HOH 93  492  366  HOH HOH B . 
L 4 HOH 94  493  367  HOH HOH B . 
L 4 HOH 95  494  368  HOH HOH B . 
L 4 HOH 96  495  369  HOH HOH B . 
L 4 HOH 97  496  370  HOH HOH B . 
L 4 HOH 98  497  371  HOH HOH B . 
L 4 HOH 99  498  372  HOH HOH B . 
L 4 HOH 100 499  373  HOH HOH B . 
M 4 HOH 1   1094 1094 HOH HOH C . 
M 4 HOH 2   1095 1101 HOH HOH C . 
M 4 HOH 3   1096 1003 HOH HOH C . 
M 4 HOH 4   1097 1004 HOH HOH C . 
M 4 HOH 5   1098 1005 HOH HOH C . 
M 4 HOH 6   1099 1006 HOH HOH C . 
M 4 HOH 7   1100 1007 HOH HOH C . 
M 4 HOH 8   1101 1008 HOH HOH C . 
M 4 HOH 9   1102 1009 HOH HOH C . 
M 4 HOH 10  1103 1010 HOH HOH C . 
M 4 HOH 11  1104 1011 HOH HOH C . 
M 4 HOH 12  1105 1012 HOH HOH C . 
M 4 HOH 13  1106 1013 HOH HOH C . 
M 4 HOH 14  1107 1014 HOH HOH C . 
M 4 HOH 15  1108 1015 HOH HOH C . 
M 4 HOH 16  1109 1016 HOH HOH C . 
M 4 HOH 17  1110 1017 HOH HOH C . 
M 4 HOH 18  1111 1018 HOH HOH C . 
M 4 HOH 19  1112 1019 HOH HOH C . 
M 4 HOH 20  1113 1020 HOH HOH C . 
M 4 HOH 21  1114 1021 HOH HOH C . 
M 4 HOH 22  1115 1022 HOH HOH C . 
M 4 HOH 23  1116 1023 HOH HOH C . 
M 4 HOH 24  1117 1024 HOH HOH C . 
M 4 HOH 25  1118 1025 HOH HOH C . 
M 4 HOH 26  1119 1026 HOH HOH C . 
M 4 HOH 27  1120 1027 HOH HOH C . 
M 4 HOH 28  1121 1028 HOH HOH C . 
M 4 HOH 29  1122 1029 HOH HOH C . 
M 4 HOH 30  1123 1030 HOH HOH C . 
M 4 HOH 31  1124 1031 HOH HOH C . 
M 4 HOH 32  1125 1032 HOH HOH C . 
M 4 HOH 33  1126 1033 HOH HOH C . 
M 4 HOH 34  1127 1034 HOH HOH C . 
M 4 HOH 35  1128 1035 HOH HOH C . 
M 4 HOH 36  1129 1036 HOH HOH C . 
M 4 HOH 37  1130 1037 HOH HOH C . 
M 4 HOH 38  1131 1038 HOH HOH C . 
M 4 HOH 39  1132 1039 HOH HOH C . 
M 4 HOH 40  1133 1040 HOH HOH C . 
M 4 HOH 41  1134 1041 HOH HOH C . 
M 4 HOH 42  1135 1042 HOH HOH C . 
M 4 HOH 43  1136 1043 HOH HOH C . 
M 4 HOH 44  1137 1044 HOH HOH C . 
M 4 HOH 45  1138 1045 HOH HOH C . 
M 4 HOH 46  1139 1046 HOH HOH C . 
M 4 HOH 47  1140 1047 HOH HOH C . 
M 4 HOH 48  1141 1048 HOH HOH C . 
M 4 HOH 49  1142 1049 HOH HOH C . 
M 4 HOH 50  1143 1050 HOH HOH C . 
M 4 HOH 51  1144 1051 HOH HOH C . 
M 4 HOH 52  1145 1052 HOH HOH C . 
M 4 HOH 53  1146 1053 HOH HOH C . 
M 4 HOH 54  1147 1054 HOH HOH C . 
M 4 HOH 55  1148 1055 HOH HOH C . 
M 4 HOH 56  1149 1056 HOH HOH C . 
M 4 HOH 57  1150 1057 HOH HOH C . 
M 4 HOH 58  1151 1058 HOH HOH C . 
M 4 HOH 59  1152 1059 HOH HOH C . 
M 4 HOH 60  1153 1060 HOH HOH C . 
M 4 HOH 61  1154 1061 HOH HOH C . 
M 4 HOH 62  1155 1063 HOH HOH C . 
M 4 HOH 63  1156 1064 HOH HOH C . 
M 4 HOH 64  1157 1065 HOH HOH C . 
M 4 HOH 65  1158 1066 HOH HOH C . 
M 4 HOH 66  1159 1067 HOH HOH C . 
M 4 HOH 67  1160 1068 HOH HOH C . 
M 4 HOH 68  1161 1069 HOH HOH C . 
M 4 HOH 69  1162 1070 HOH HOH C . 
M 4 HOH 70  1163 1071 HOH HOH C . 
M 4 HOH 71  1164 1072 HOH HOH C . 
M 4 HOH 72  1165 1073 HOH HOH C . 
M 4 HOH 73  1166 1074 HOH HOH C . 
M 4 HOH 74  1167 1075 HOH HOH C . 
M 4 HOH 75  1168 1076 HOH HOH C . 
M 4 HOH 76  1169 1077 HOH HOH C . 
M 4 HOH 77  1170 1078 HOH HOH C . 
M 4 HOH 78  1171 1079 HOH HOH C . 
M 4 HOH 79  1172 1080 HOH HOH C . 
M 4 HOH 80  1173 1081 HOH HOH C . 
M 4 HOH 81  1174 1082 HOH HOH C . 
M 4 HOH 82  1175 1083 HOH HOH C . 
M 4 HOH 83  1176 1084 HOH HOH C . 
M 4 HOH 84  1177 1085 HOH HOH C . 
M 4 HOH 85  1178 1086 HOH HOH C . 
M 4 HOH 86  1179 1087 HOH HOH C . 
M 4 HOH 87  1180 1088 HOH HOH C . 
M 4 HOH 88  1181 1089 HOH HOH C . 
M 4 HOH 89  1182 1090 HOH HOH C . 
M 4 HOH 90  1183 1091 HOH HOH C . 
M 4 HOH 91  1184 1092 HOH HOH C . 
M 4 HOH 92  1185 1093 HOH HOH C . 
M 4 HOH 93  1186 1094 HOH HOH C . 
M 4 HOH 94  1187 1095 HOH HOH C . 
M 4 HOH 95  1188 1096 HOH HOH C . 
M 4 HOH 96  1189 1097 HOH HOH C . 
M 4 HOH 97  1190 1098 HOH HOH C . 
M 4 HOH 98  1191 1099 HOH HOH C . 
M 4 HOH 99  1192 1100 HOH HOH C . 
M 4 HOH 100 1193 1101 HOH HOH C . 
M 4 HOH 101 1194 1102 HOH HOH C . 
M 4 HOH 102 1195 1103 HOH HOH C . 
M 4 HOH 103 1196 1104 HOH HOH C . 
M 4 HOH 104 1197 1105 HOH HOH C . 
M 4 HOH 105 1198 1106 HOH HOH C . 
M 4 HOH 106 1199 1107 HOH HOH C . 
M 4 HOH 107 1200 1108 HOH HOH C . 
M 4 HOH 108 1201 1109 HOH HOH C . 
M 4 HOH 109 1202 1110 HOH HOH C . 
M 4 HOH 110 1203 1111 HOH HOH C . 
M 4 HOH 111 1204 1112 HOH HOH C . 
M 4 HOH 112 1205 1113 HOH HOH C . 
M 4 HOH 113 1206 1114 HOH HOH C . 
M 4 HOH 114 1207 1115 HOH HOH C . 
M 4 HOH 115 1208 1116 HOH HOH C . 
M 4 HOH 116 1209 1117 HOH HOH C . 
M 4 HOH 117 1210 1118 HOH HOH C . 
M 4 HOH 118 1211 1119 HOH HOH C . 
M 4 HOH 119 1212 1120 HOH HOH C . 
M 4 HOH 120 1213 1121 HOH HOH C . 
M 4 HOH 121 1214 1122 HOH HOH C . 
M 4 HOH 122 1215 1123 HOH HOH C . 
M 4 HOH 123 1216 1124 HOH HOH C . 
M 4 HOH 124 1217 1125 HOH HOH C . 
M 4 HOH 125 1218 1126 HOH HOH C . 
M 4 HOH 126 1219 1127 HOH HOH C . 
M 4 HOH 127 1220 1128 HOH HOH C . 
M 4 HOH 128 1221 1129 HOH HOH C . 
M 4 HOH 129 1222 1130 HOH HOH C . 
N 4 HOH 1   400  274  HOH HOH D . 
N 4 HOH 2   401  275  HOH HOH D . 
N 4 HOH 3   402  276  HOH HOH D . 
N 4 HOH 4   403  277  HOH HOH D . 
N 4 HOH 5   404  278  HOH HOH D . 
N 4 HOH 6   405  279  HOH HOH D . 
N 4 HOH 7   406  280  HOH HOH D . 
N 4 HOH 8   407  281  HOH HOH D . 
N 4 HOH 9   408  282  HOH HOH D . 
N 4 HOH 10  409  283  HOH HOH D . 
N 4 HOH 11  410  284  HOH HOH D . 
N 4 HOH 12  411  285  HOH HOH D . 
N 4 HOH 13  412  286  HOH HOH D . 
N 4 HOH 14  413  287  HOH HOH D . 
N 4 HOH 15  414  288  HOH HOH D . 
N 4 HOH 16  415  289  HOH HOH D . 
N 4 HOH 17  416  290  HOH HOH D . 
N 4 HOH 18  417  291  HOH HOH D . 
N 4 HOH 19  418  292  HOH HOH D . 
N 4 HOH 20  419  293  HOH HOH D . 
N 4 HOH 21  420  294  HOH HOH D . 
N 4 HOH 22  421  295  HOH HOH D . 
N 4 HOH 23  422  296  HOH HOH D . 
N 4 HOH 24  423  297  HOH HOH D . 
N 4 HOH 25  424  298  HOH HOH D . 
N 4 HOH 26  425  299  HOH HOH D . 
N 4 HOH 27  426  300  HOH HOH D . 
N 4 HOH 28  427  301  HOH HOH D . 
N 4 HOH 29  428  302  HOH HOH D . 
N 4 HOH 30  429  303  HOH HOH D . 
N 4 HOH 31  430  304  HOH HOH D . 
N 4 HOH 32  431  305  HOH HOH D . 
N 4 HOH 33  432  306  HOH HOH D . 
N 4 HOH 34  433  307  HOH HOH D . 
N 4 HOH 35  434  308  HOH HOH D . 
N 4 HOH 36  435  309  HOH HOH D . 
N 4 HOH 37  436  310  HOH HOH D . 
N 4 HOH 38  437  311  HOH HOH D . 
N 4 HOH 39  438  312  HOH HOH D . 
N 4 HOH 40  439  313  HOH HOH D . 
N 4 HOH 41  440  314  HOH HOH D . 
N 4 HOH 42  441  315  HOH HOH D . 
N 4 HOH 43  442  316  HOH HOH D . 
N 4 HOH 44  443  317  HOH HOH D . 
N 4 HOH 45  444  318  HOH HOH D . 
N 4 HOH 46  445  319  HOH HOH D . 
N 4 HOH 47  446  320  HOH HOH D . 
N 4 HOH 48  447  321  HOH HOH D . 
N 4 HOH 49  448  322  HOH HOH D . 
N 4 HOH 50  449  323  HOH HOH D . 
N 4 HOH 51  450  324  HOH HOH D . 
N 4 HOH 52  451  325  HOH HOH D . 
N 4 HOH 53  452  326  HOH HOH D . 
N 4 HOH 54  453  327  HOH HOH D . 
N 4 HOH 55  454  328  HOH HOH D . 
N 4 HOH 56  455  329  HOH HOH D . 
N 4 HOH 57  456  330  HOH HOH D . 
N 4 HOH 58  457  331  HOH HOH D . 
N 4 HOH 59  458  332  HOH HOH D . 
N 4 HOH 60  459  333  HOH HOH D . 
N 4 HOH 61  460  334  HOH HOH D . 
N 4 HOH 62  461  335  HOH HOH D . 
N 4 HOH 63  462  336  HOH HOH D . 
N 4 HOH 64  463  337  HOH HOH D . 
N 4 HOH 65  464  338  HOH HOH D . 
N 4 HOH 66  465  339  HOH HOH D . 
N 4 HOH 67  466  340  HOH HOH D . 
N 4 HOH 68  467  341  HOH HOH D . 
N 4 HOH 69  468  342  HOH HOH D . 
N 4 HOH 70  469  343  HOH HOH D . 
N 4 HOH 71  470  344  HOH HOH D . 
N 4 HOH 72  471  345  HOH HOH D . 
N 4 HOH 73  472  346  HOH HOH D . 
N 4 HOH 74  473  347  HOH HOH D . 
N 4 HOH 75  474  348  HOH HOH D . 
N 4 HOH 76  475  349  HOH HOH D . 
N 4 HOH 77  476  350  HOH HOH D . 
N 4 HOH 78  477  351  HOH HOH D . 
N 4 HOH 79  478  352  HOH HOH D . 
N 4 HOH 80  479  353  HOH HOH D . 
N 4 HOH 81  480  354  HOH HOH D . 
N 4 HOH 82  481  355  HOH HOH D . 
N 4 HOH 83  482  356  HOH HOH D . 
N 4 HOH 84  483  357  HOH HOH D . 
N 4 HOH 85  484  358  HOH HOH D . 
N 4 HOH 86  485  359  HOH HOH D . 
N 4 HOH 87  486  360  HOH HOH D . 
N 4 HOH 88  487  361  HOH HOH D . 
N 4 HOH 89  488  362  HOH HOH D . 
N 4 HOH 90  489  363  HOH HOH D . 
N 4 HOH 91  490  364  HOH HOH D . 
N 4 HOH 92  491  365  HOH HOH D . 
N 4 HOH 93  492  366  HOH HOH D . 
N 4 HOH 94  493  367  HOH HOH D . 
N 4 HOH 95  494  368  HOH HOH D . 
# 
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 C ASN 395 C ASN 395 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 395 A ASN 395 ? 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 
3 author_and_software_defined_assembly PISA monomeric 1 
4 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,E,F,G,K 
2 1 B,L       
3 1 C,H,I,J,M 
4 1 D,N       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2007-10-30 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2012-10-24 
# 
_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_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Non-polymer description'   
2 2 'Structure model' 'Version format compliance' 
3 3 'Structure model' 'Non-polymer description'   
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNS      refinement        1.1     ? 1 
ADSC     'data collection' Quantum ? 2 
HKL-2000 'data reduction'  .       ? 3 
HKL-2000 'data scaling'    .       ? 4 
SHELXD   phasing           .       ? 5 
SOLVE    phasing           .       ? 6 
# 
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   C ARG 305 ? ? N   C VAL 307  ? ? 1.80 
2 1 O   A ARG 305 ? ? N   A VAL 307  ? ? 1.85 
3 1 OE1 A GLU 175 ? ? CE1 A TYR 177  ? ? 1.89 
4 1 NH1 A ARG 178 ? ? O   A HOH 1018 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLN 
_pdbx_validate_symm_contact.auth_seq_id_1     241 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    NZ 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    LYS 
_pdbx_validate_symm_contact.auth_seq_id_2     52 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_655 
_pdbx_validate_symm_contact.dist              1.87 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A GLU 175 ? ? CG  A GLU 175 ? ? 1.349 1.517 -0.168 0.019 N 
2 1 CD A GLU 308 ? ? OE1 A GLU 308 ? ? 1.179 1.252 -0.073 0.011 N 
3 1 CB C LYS 52  ? ? CG  C LYS 52  ? ? 1.288 1.521 -0.233 0.027 N 
4 1 CG C LYS 52  ? ? CD  C LYS 52  ? ? 1.305 1.520 -0.215 0.034 N 
5 1 CD C GLU 308 ? ? OE1 C GLU 308 ? ? 1.180 1.252 -0.072 0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CD A LYS 52  ? ? CE A LYS 52  ? ? NZ  A LYS 52  ? ? 82.66  111.70 -29.04 2.30 N 
2  1 O  A GLU 174 ? ? C  A GLU 174 ? ? N   A GLU 175 ? ? 109.84 122.70 -12.86 1.60 Y 
3  1 N  A GLU 175 ? ? CA A GLU 175 ? ? CB  A GLU 175 ? ? 87.12  110.60 -23.48 1.80 N 
4  1 CA A GLU 175 ? ? CB A GLU 175 ? ? CG  A GLU 175 ? ? 135.76 113.40 22.36  2.20 N 
5  1 C  A SER 271 ? ? N  A PRO 272 ? ? CA  A PRO 272 ? ? 128.80 119.30 9.50   1.50 Y 
6  1 N  A SER 290 ? ? CA A SER 290 ? ? C   A SER 290 ? ? 138.40 111.00 27.40  2.70 N 
7  1 CA A LEU 304 ? ? CB A LEU 304 ? ? CG  A LEU 304 ? ? 94.12  115.30 -21.18 2.30 N 
8  1 CB A LEU 304 ? ? CG A LEU 304 ? ? CD1 A LEU 304 ? ? 100.36 111.00 -10.64 1.70 N 
9  1 N  A LEU 304 ? ? CA A LEU 304 ? ? C   A LEU 304 ? ? 141.36 111.00 30.36  2.70 N 
10 1 N  A SER 321 ? ? CA A SER 321 ? ? C   A SER 321 ? ? 78.97  111.00 -32.03 2.70 N 
11 1 CB C LYS 52  ? ? CA C LYS 52  ? ? C   C LYS 52  ? ? 95.76  110.40 -14.64 2.00 N 
12 1 CB C LYS 52  ? ? CG C LYS 52  ? ? CD  C LYS 52  ? ? 93.70  111.60 -17.90 2.60 N 
13 1 CD C LYS 52  ? ? CE C LYS 52  ? ? NZ  C LYS 52  ? ? 82.11  111.70 -29.59 2.30 N 
14 1 C  C SER 271 ? ? N  C PRO 272 ? ? CA  C PRO 272 ? ? 128.41 119.30 9.11   1.50 Y 
15 1 N  C SER 290 ? ? CA C SER 290 ? ? C   C SER 290 ? ? 138.17 111.00 27.17  2.70 N 
16 1 CA C LEU 304 ? ? CB C LEU 304 ? ? CG  C LEU 304 ? ? 92.38  115.30 -22.92 2.30 N 
17 1 N  C LEU 304 ? ? CA C LEU 304 ? ? C   C LEU 304 ? ? 142.05 111.00 31.05  2.70 N 
18 1 N  C SER 321 ? ? CA C SER 321 ? ? C   C SER 321 ? ? 82.29  111.00 -28.71 2.70 N 
19 1 N  C GLY 322 ? ? CA C GLY 322 ? ? C   C GLY 322 ? ? 89.47  113.10 -23.63 2.50 N 
20 1 C  D SER 271 ? ? N  D PRO 272 ? ? CA  D PRO 272 ? ? 128.33 119.30 9.03   1.50 Y 
# 
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 CYS A 8   ? ? -155.80 53.10   
2  1 SER A 12  ? ? -65.67  89.35   
3  1 ALA A 13  ? ? 170.16  -23.39  
4  1 ASP A 90  ? ? -25.35  -52.87  
5  1 ASN A 128 ? ? -164.74 87.28   
6  1 SER A 148 ? ? -42.57  156.45  
7  1 GLU A 174 ? ? -102.12 52.19   
8  1 GLU A 175 ? ? -113.73 67.80   
9  1 PHE A 244 ? ? -108.80 52.76   
10 1 SER A 290 ? ? -118.95 -129.31 
11 1 ALA A 291 ? ? -13.03  166.68  
12 1 SER A 292 ? ? -166.57 -83.55  
13 1 ASN A 293 ? ? -153.31 -10.93  
14 1 ASN A 302 ? ? -177.85 149.63  
15 1 ARG A 305 ? ? -78.23  -112.52 
16 1 VAL A 307 ? ? 36.49   -143.40 
17 1 GLU A 308 ? ? 70.13   52.83   
18 1 PHE A 311 ? ? 158.36  90.30   
19 1 THR A 314 ? ? 175.32  162.83  
20 1 VAL A 319 ? ? -55.34  176.62  
21 1 LYS A 320 ? ? -3.17   -55.46  
22 1 SER A 321 ? ? 148.70  167.96  
23 1 SER A 323 ? ? -3.53   90.24   
24 1 VAL A 324 ? ? -41.58  167.52  
25 1 PRO A 337 ? ? -64.47  37.94   
26 1 MET A 338 ? ? 57.47   -12.09  
27 1 ASN A 361 ? ? 52.15   98.16   
28 1 ASN A 388 ? ? -23.31  -86.26  
29 1 THR A 397 ? ? -104.73 -167.70 
30 1 CYS B 8   ? ? -67.19  13.95   
31 1 SER B 12  ? ? -54.93  84.65   
32 1 ALA B 13  ? ? 178.17  -29.65  
33 1 TYR B 49  ? ? -92.26  -60.69  
34 1 SER B 63  ? ? 73.52   -10.26  
35 1 SER B 64  ? ? -65.08  85.29   
36 1 ASP B 65  ? ? -3.20   100.46  
37 1 PRO B 107 ? ? -72.56  41.10   
38 1 ASN B 108 ? ? 179.02  41.45   
39 1 ASN B 128 ? ? -163.07 91.72   
40 1 SER B 148 ? ? -37.21  146.84  
41 1 GLU B 174 ? ? -42.64  39.10   
42 1 GLU B 175 ? ? -94.41  54.86   
43 1 SER B 271 ? ? 60.90   68.50   
44 1 PRO B 272 ? ? -42.47  151.48  
45 1 CYS C 8   ? ? -155.63 51.61   
46 1 SER C 12  ? ? -63.91  86.21   
47 1 ALA C 13  ? ? 171.45  -19.18  
48 1 PRO C 35  ? ? -57.33  101.95  
49 1 ASP C 90  ? ? -25.03  -53.83  
50 1 ASN C 128 ? ? -162.80 85.92   
51 1 SER C 148 ? ? -44.71  155.74  
52 1 PHE C 244 ? ? -110.08 58.61   
53 1 SER C 290 ? ? -119.16 -129.34 
54 1 ALA C 291 ? ? -11.65  166.33  
55 1 SER C 292 ? ? -166.47 -82.24  
56 1 ASN C 293 ? ? -149.76 -13.43  
57 1 LEU C 304 ? ? -163.11 -157.38 
58 1 ARG C 305 ? ? -71.41  -116.96 
59 1 VAL C 307 ? ? 34.18   -141.90 
60 1 PHE C 311 ? ? 157.06  93.38   
61 1 THR C 314 ? ? 175.87  163.11  
62 1 VAL C 319 ? ? -56.92  177.40  
63 1 LYS C 320 ? ? -1.04   -55.87  
64 1 SER C 321 ? ? 143.52  151.07  
65 1 SER C 323 ? ? -8.33   90.60   
66 1 VAL C 324 ? ? -38.39  168.72  
67 1 PRO C 337 ? ? -64.56  38.18   
68 1 MET C 338 ? ? 57.58   -12.91  
69 1 ASN C 361 ? ? 53.35   96.65   
70 1 ASN C 388 ? ? -21.29  -85.96  
71 1 THR C 397 ? ? -100.46 -167.95 
72 1 CYS D 8   ? ? -68.44  15.34   
73 1 SER D 12  ? ? -55.52  86.42   
74 1 ALA D 13  ? ? 176.24  -29.15  
75 1 SER D 63  ? ? 73.19   -9.38   
76 1 SER D 64  ? ? -67.03  85.56   
77 1 ASP D 65  ? ? -3.68   101.48  
78 1 ASP D 90  ? ? -39.56  -33.25  
79 1 PRO D 107 ? ? -69.23  38.43   
80 1 ASN D 108 ? ? 179.44  42.39   
81 1 ASN D 128 ? ? -165.31 86.81   
82 1 SER D 148 ? ? -39.40  146.92  
83 1 GLU D 174 ? ? -47.87  39.88   
84 1 GLU D 175 ? ? -92.34  55.31   
85 1 SER D 271 ? ? 59.45   71.36   
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             GLU 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              174 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -12.00 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A ASN 312 ? CG  ? A ASN 312 CG  
2  1 Y 0 A ASN 312 ? OD1 ? A ASN 312 OD1 
3  1 Y 0 A ASN 312 ? ND2 ? A ASN 312 ND2 
4  1 Y 1 A THR 314 ? OG1 ? A THR 314 OG1 
5  1 Y 1 A THR 314 ? CG2 ? A THR 314 CG2 
6  1 Y 1 A ILE 315 ? CG1 ? A ILE 315 CG1 
7  1 Y 1 A ILE 315 ? CG2 ? A ILE 315 CG2 
8  1 Y 1 A ILE 315 ? CD1 ? A ILE 315 CD1 
9  1 Y 1 A ASN 316 ? CG  ? A ASN 316 CG  
10 1 Y 1 A ASN 316 ? OD1 ? A ASN 316 OD1 
11 1 Y 1 A ASN 316 ? ND2 ? A ASN 316 ND2 
12 1 Y 1 A VAL 317 ? CG1 ? A VAL 317 CG1 
13 1 Y 1 A VAL 317 ? CG2 ? A VAL 317 CG2 
14 1 Y 1 A LYS 320 ? CG  ? A LYS 320 CG  
15 1 Y 1 A LYS 320 ? CD  ? A LYS 320 CD  
16 1 Y 1 A LYS 320 ? CE  ? A LYS 320 CE  
17 1 Y 1 A LYS 320 ? NZ  ? A LYS 320 NZ  
18 1 Y 1 A SER 321 ? OG  ? A SER 321 OG  
19 1 Y 1 A ASN 336 ? CG  ? A ASN 336 CG  
20 1 Y 1 A ASN 336 ? OD1 ? A ASN 336 OD1 
21 1 Y 1 A ASN 336 ? ND2 ? A ASN 336 ND2 
22 1 Y 1 A GLU 390 ? CG  ? A GLU 390 CG  
23 1 Y 1 A GLU 390 ? CD  ? A GLU 390 CD  
24 1 Y 1 A GLU 390 ? OE1 ? A GLU 390 OE1 
25 1 Y 1 A GLU 390 ? OE2 ? A GLU 390 OE2 
26 1 Y 0 C THR 289 ? OG1 ? C THR 289 OG1 
27 1 Y 0 C THR 289 ? CG2 ? C THR 289 CG2 
28 1 Y 0 C ILE 297 ? CG1 ? C ILE 297 CG1 
29 1 Y 0 C ILE 297 ? CG2 ? C ILE 297 CG2 
30 1 Y 0 C ILE 297 ? CD1 ? C ILE 297 CD1 
31 1 Y 1 C THR 314 ? OG1 ? C THR 314 OG1 
32 1 Y 1 C THR 314 ? CG2 ? C THR 314 CG2 
33 1 Y 1 C ILE 315 ? CG1 ? C ILE 315 CG1 
34 1 Y 1 C ILE 315 ? CG2 ? C ILE 315 CG2 
35 1 Y 1 C ILE 315 ? CD1 ? C ILE 315 CD1 
36 1 Y 1 C ASN 316 ? CG  ? C ASN 316 CG  
37 1 Y 1 C ASN 316 ? OD1 ? C ASN 316 OD1 
38 1 Y 1 C ASN 316 ? ND2 ? C ASN 316 ND2 
39 1 Y 1 C VAL 317 ? CG1 ? C VAL 317 CG1 
40 1 Y 1 C VAL 317 ? CG2 ? C VAL 317 CG2 
41 1 Y 1 C LYS 320 ? CG  ? C LYS 320 CG  
42 1 Y 1 C LYS 320 ? CD  ? C LYS 320 CD  
43 1 Y 1 C LYS 320 ? CE  ? C LYS 320 CE  
44 1 Y 1 C LYS 320 ? NZ  ? C LYS 320 NZ  
45 1 Y 1 C SER 321 ? OG  ? C SER 321 OG  
46 1 Y 1 C ASN 336 ? CG  ? C ASN 336 CG  
47 1 Y 1 C ASN 336 ? OD1 ? C ASN 336 OD1 
48 1 Y 1 C ASN 336 ? ND2 ? C ASN 336 ND2 
49 1 Y 1 C GLU 390 ? CG  ? C GLU 390 CG  
50 1 Y 1 C GLU 390 ? CD  ? C GLU 390 CD  
51 1 Y 1 C GLU 390 ? OE1 ? C GLU 390 OE1 
52 1 Y 1 C GLU 390 ? OE2 ? C GLU 390 OE2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A SER 1   ? A SER 1   
2   1 Y 1 A THR 2   ? A THR 2   
3   1 Y 1 A GLN 3   ? A GLN 3   
4   1 Y 1 A THR 4   ? A THR 4   
5   1 Y 1 A GLN 5   ? A GLN 5   
6   1 Y 1 A SER 6   ? A SER 6   
7   1 Y 1 A HIS 274 ? A HIS 274 
8   1 Y 1 A GLU 275 ? A GLU 275 
9   1 Y 1 A VAL 276 ? A VAL 276 
10  1 Y 1 A GLN 277 ? A GLN 277 
11  1 Y 1 A PRO 278 ? A PRO 278 
12  1 Y 1 A THR 279 ? A THR 279 
13  1 Y 1 A LEU 280 ? A LEU 280 
14  1 Y 1 A PRO 281 ? A PRO 281 
15  1 Y 1 A SER 282 ? A SER 282 
16  1 Y 1 A ASN 283 ? A ASN 283 
17  1 Y 1 A PRO 284 ? A PRO 284 
18  1 Y 1 A GLY 285 ? A GLY 285 
19  1 Y 1 A PRO 286 ? A PRO 286 
20  1 Y 1 A GLY 287 ? A GLY 287 
21  1 Y 1 A PRO 288 ? A PRO 288 
22  1 Y 1 B SER 1   ? B SER 1   
23  1 Y 1 B THR 2   ? B THR 2   
24  1 Y 1 B GLN 3   ? B GLN 3   
25  1 Y 1 B THR 4   ? B THR 4   
26  1 Y 1 B GLN 5   ? B GLN 5   
27  1 Y 1 B SER 6   ? B SER 6   
28  1 Y 1 B HIS 274 ? B HIS 274 
29  1 Y 1 B GLU 275 ? B GLU 275 
30  1 Y 1 B VAL 276 ? B VAL 276 
31  1 Y 1 B GLN 277 ? B GLN 277 
32  1 Y 1 B PRO 278 ? B PRO 278 
33  1 Y 1 B THR 279 ? B THR 279 
34  1 Y 1 B LEU 280 ? B LEU 280 
35  1 Y 1 B PRO 281 ? B PRO 281 
36  1 Y 1 B SER 282 ? B SER 282 
37  1 Y 1 B ASN 283 ? B ASN 283 
38  1 Y 1 B PRO 284 ? B PRO 284 
39  1 Y 1 B GLY 285 ? B GLY 285 
40  1 Y 1 B PRO 286 ? B PRO 286 
41  1 Y 1 B GLY 287 ? B GLY 287 
42  1 Y 1 B PRO 288 ? B PRO 288 
43  1 Y 1 B THR 289 ? B THR 289 
44  1 Y 1 B SER 290 ? B SER 290 
45  1 Y 1 B ALA 291 ? B ALA 291 
46  1 Y 1 B SER 292 ? B SER 292 
47  1 Y 1 B ASN 293 ? B ASN 293 
48  1 Y 1 B ILE 294 ? B ILE 294 
49  1 Y 1 B THR 295 ? B THR 295 
50  1 Y 1 B VAL 296 ? B VAL 296 
51  1 Y 1 B ILE 297 ? B ILE 297 
52  1 Y 1 B TYR 298 ? B TYR 298 
53  1 Y 1 B THR 299 ? B THR 299 
54  1 Y 1 B ILE 300 ? B ILE 300 
55  1 Y 1 B ASN 301 ? B ASN 301 
56  1 Y 1 B ASN 302 ? B ASN 302 
57  1 Y 1 B GLN 303 ? B GLN 303 
58  1 Y 1 B LEU 304 ? B LEU 304 
59  1 Y 1 B ARG 305 ? B ARG 305 
60  1 Y 1 B GLY 306 ? B GLY 306 
61  1 Y 1 B VAL 307 ? B VAL 307 
62  1 Y 1 B GLU 308 ? B GLU 308 
63  1 Y 1 B LEU 309 ? B LEU 309 
64  1 Y 1 B LEU 310 ? B LEU 310 
65  1 Y 1 B PHE 311 ? B PHE 311 
66  1 Y 1 B ASN 312 ? B ASN 312 
67  1 Y 1 B GLU 313 ? B GLU 313 
68  1 Y 1 B THR 314 ? B THR 314 
69  1 Y 1 B ILE 315 ? B ILE 315 
70  1 Y 1 B ASN 316 ? B ASN 316 
71  1 Y 1 B VAL 317 ? B VAL 317 
72  1 Y 1 B SER 318 ? B SER 318 
73  1 Y 1 B VAL 319 ? B VAL 319 
74  1 Y 1 B LYS 320 ? B LYS 320 
75  1 Y 1 B SER 321 ? B SER 321 
76  1 Y 1 B GLY 322 ? B GLY 322 
77  1 Y 1 B SER 323 ? B SER 323 
78  1 Y 1 B VAL 324 ? B VAL 324 
79  1 Y 1 B LEU 325 ? B LEU 325 
80  1 Y 1 B LEU 326 ? B LEU 326 
81  1 Y 1 B VAL 327 ? B VAL 327 
82  1 Y 1 B VAL 328 ? B VAL 328 
83  1 Y 1 B LEU 329 ? B LEU 329 
84  1 Y 1 B GLU 330 ? B GLU 330 
85  1 Y 1 B GLU 331 ? B GLU 331 
86  1 Y 1 B ALA 332 ? B ALA 332 
87  1 Y 1 B GLN 333 ? B GLN 333 
88  1 Y 1 B ARG 334 ? B ARG 334 
89  1 Y 1 B LYS 335 ? B LYS 335 
90  1 Y 1 B ASN 336 ? B ASN 336 
91  1 Y 1 B PRO 337 ? B PRO 337 
92  1 Y 1 B MET 338 ? B MET 338 
93  1 Y 1 B PHE 339 ? B PHE 339 
94  1 Y 1 B LYS 340 ? B LYS 340 
95  1 Y 1 B PHE 341 ? B PHE 341 
96  1 Y 1 B GLU 342 ? B GLU 342 
97  1 Y 1 B THR 343 ? B THR 343 
98  1 Y 1 B THR 344 ? B THR 344 
99  1 Y 1 B MET 345 ? B MET 345 
100 1 Y 1 B THR 346 ? B THR 346 
101 1 Y 1 B SER 347 ? B SER 347 
102 1 Y 1 B TRP 348 ? B TRP 348 
103 1 Y 1 B GLY 349 ? B GLY 349 
104 1 Y 1 B LEU 350 ? B LEU 350 
105 1 Y 1 B VAL 351 ? B VAL 351 
106 1 Y 1 B VAL 352 ? B VAL 352 
107 1 Y 1 B SER 353 ? B SER 353 
108 1 Y 1 B SER 354 ? B SER 354 
109 1 Y 1 B ILE 355 ? B ILE 355 
110 1 Y 1 B ASN 356 ? B ASN 356 
111 1 Y 1 B ASN 357 ? B ASN 357 
112 1 Y 1 B ILE 358 ? B ILE 358 
113 1 Y 1 B ALA 359 ? B ALA 359 
114 1 Y 1 B GLU 360 ? B GLU 360 
115 1 Y 1 B ASN 361 ? B ASN 361 
116 1 Y 1 B VAL 362 ? B VAL 362 
117 1 Y 1 B ASN 363 ? B ASN 363 
118 1 Y 1 B HIS 364 ? B HIS 364 
119 1 Y 1 B LYS 365 ? B LYS 365 
120 1 Y 1 B THR 366 ? B THR 366 
121 1 Y 1 B TYR 367 ? B TYR 367 
122 1 Y 1 B TRP 368 ? B TRP 368 
123 1 Y 1 B GLN 369 ? B GLN 369 
124 1 Y 1 B PHE 370 ? B PHE 370 
125 1 Y 1 B LEU 371 ? B LEU 371 
126 1 Y 1 B SER 372 ? B SER 372 
127 1 Y 1 B GLY 373 ? B GLY 373 
128 1 Y 1 B VAL 374 ? B VAL 374 
129 1 Y 1 B THR 375 ? B THR 375 
130 1 Y 1 B PRO 376 ? B PRO 376 
131 1 Y 1 B LEU 377 ? B LEU 377 
132 1 Y 1 B ASN 378 ? B ASN 378 
133 1 Y 1 B GLU 379 ? B GLU 379 
134 1 Y 1 B GLY 380 ? B GLY 380 
135 1 Y 1 B VAL 381 ? B VAL 381 
136 1 Y 1 B ALA 382 ? B ALA 382 
137 1 Y 1 B ASP 383 ? B ASP 383 
138 1 Y 1 B TYR 384 ? B TYR 384 
139 1 Y 1 B ILE 385 ? B ILE 385 
140 1 Y 1 B PRO 386 ? B PRO 386 
141 1 Y 1 B PHE 387 ? B PHE 387 
142 1 Y 1 B ASN 388 ? B ASN 388 
143 1 Y 1 B HIS 389 ? B HIS 389 
144 1 Y 1 B GLU 390 ? B GLU 390 
145 1 Y 1 B HIS 391 ? B HIS 391 
146 1 Y 1 B ILE 392 ? B ILE 392 
147 1 Y 1 B THR 393 ? B THR 393 
148 1 Y 1 B ALA 394 ? B ALA 394 
149 1 Y 1 B ASN 395 ? B ASN 395 
150 1 Y 1 B PHE 396 ? B PHE 396 
151 1 Y 1 B THR 397 ? B THR 397 
152 1 Y 1 B GLN 398 ? B GLN 398 
153 1 Y 1 B TYR 399 ? B TYR 399 
154 1 Y 1 C SER 1   ? C SER 1   
155 1 Y 1 C THR 2   ? C THR 2   
156 1 Y 1 C GLN 3   ? C GLN 3   
157 1 Y 1 C THR 4   ? C THR 4   
158 1 Y 1 C GLN 5   ? C GLN 5   
159 1 Y 1 C SER 6   ? C SER 6   
160 1 Y 1 C HIS 274 ? C HIS 274 
161 1 Y 1 C GLU 275 ? C GLU 275 
162 1 Y 1 C VAL 276 ? C VAL 276 
163 1 Y 1 C GLN 277 ? C GLN 277 
164 1 Y 1 C PRO 278 ? C PRO 278 
165 1 Y 1 C THR 279 ? C THR 279 
166 1 Y 1 C LEU 280 ? C LEU 280 
167 1 Y 1 C PRO 281 ? C PRO 281 
168 1 Y 1 C SER 282 ? C SER 282 
169 1 Y 1 C ASN 283 ? C ASN 283 
170 1 Y 1 C PRO 284 ? C PRO 284 
171 1 Y 1 C GLY 285 ? C GLY 285 
172 1 Y 1 C PRO 286 ? C PRO 286 
173 1 Y 1 C GLY 287 ? C GLY 287 
174 1 Y 1 C PRO 288 ? C PRO 288 
175 1 Y 1 D SER 1   ? D SER 1   
176 1 Y 1 D THR 2   ? D THR 2   
177 1 Y 1 D GLN 3   ? D GLN 3   
178 1 Y 1 D THR 4   ? D THR 4   
179 1 Y 1 D GLN 5   ? D GLN 5   
180 1 Y 1 D SER 6   ? D SER 6   
181 1 Y 1 D HIS 274 ? D HIS 274 
182 1 Y 1 D GLU 275 ? D GLU 275 
183 1 Y 1 D VAL 276 ? D VAL 276 
184 1 Y 1 D GLN 277 ? D GLN 277 
185 1 Y 1 D PRO 278 ? D PRO 278 
186 1 Y 1 D THR 279 ? D THR 279 
187 1 Y 1 D LEU 280 ? D LEU 280 
188 1 Y 1 D PRO 281 ? D PRO 281 
189 1 Y 1 D SER 282 ? D SER 282 
190 1 Y 1 D ASN 283 ? D ASN 283 
191 1 Y 1 D PRO 284 ? D PRO 284 
192 1 Y 1 D GLY 285 ? D GLY 285 
193 1 Y 1 D PRO 286 ? D PRO 286 
194 1 Y 1 D GLY 287 ? D GLY 287 
195 1 Y 1 D PRO 288 ? D PRO 288 
196 1 Y 1 D THR 289 ? D THR 289 
197 1 Y 1 D SER 290 ? D SER 290 
198 1 Y 1 D ALA 291 ? D ALA 291 
199 1 Y 1 D SER 292 ? D SER 292 
200 1 Y 1 D ASN 293 ? D ASN 293 
201 1 Y 1 D ILE 294 ? D ILE 294 
202 1 Y 1 D THR 295 ? D THR 295 
203 1 Y 1 D VAL 296 ? D VAL 296 
204 1 Y 1 D ILE 297 ? D ILE 297 
205 1 Y 1 D TYR 298 ? D TYR 298 
206 1 Y 1 D THR 299 ? D THR 299 
207 1 Y 1 D ILE 300 ? D ILE 300 
208 1 Y 1 D ASN 301 ? D ASN 301 
209 1 Y 1 D ASN 302 ? D ASN 302 
210 1 Y 1 D GLN 303 ? D GLN 303 
211 1 Y 1 D LEU 304 ? D LEU 304 
212 1 Y 1 D ARG 305 ? D ARG 305 
213 1 Y 1 D GLY 306 ? D GLY 306 
214 1 Y 1 D VAL 307 ? D VAL 307 
215 1 Y 1 D GLU 308 ? D GLU 308 
216 1 Y 1 D LEU 309 ? D LEU 309 
217 1 Y 1 D LEU 310 ? D LEU 310 
218 1 Y 1 D PHE 311 ? D PHE 311 
219 1 Y 1 D ASN 312 ? D ASN 312 
220 1 Y 1 D GLU 313 ? D GLU 313 
221 1 Y 1 D THR 314 ? D THR 314 
222 1 Y 1 D ILE 315 ? D ILE 315 
223 1 Y 1 D ASN 316 ? D ASN 316 
224 1 Y 1 D VAL 317 ? D VAL 317 
225 1 Y 1 D SER 318 ? D SER 318 
226 1 Y 1 D VAL 319 ? D VAL 319 
227 1 Y 1 D LYS 320 ? D LYS 320 
228 1 Y 1 D SER 321 ? D SER 321 
229 1 Y 1 D GLY 322 ? D GLY 322 
230 1 Y 1 D SER 323 ? D SER 323 
231 1 Y 1 D VAL 324 ? D VAL 324 
232 1 Y 1 D LEU 325 ? D LEU 325 
233 1 Y 1 D LEU 326 ? D LEU 326 
234 1 Y 1 D VAL 327 ? D VAL 327 
235 1 Y 1 D VAL 328 ? D VAL 328 
236 1 Y 1 D LEU 329 ? D LEU 329 
237 1 Y 1 D GLU 330 ? D GLU 330 
238 1 Y 1 D GLU 331 ? D GLU 331 
239 1 Y 1 D ALA 332 ? D ALA 332 
240 1 Y 1 D GLN 333 ? D GLN 333 
241 1 Y 1 D ARG 334 ? D ARG 334 
242 1 Y 1 D LYS 335 ? D LYS 335 
243 1 Y 1 D ASN 336 ? D ASN 336 
244 1 Y 1 D PRO 337 ? D PRO 337 
245 1 Y 1 D MET 338 ? D MET 338 
246 1 Y 1 D PHE 339 ? D PHE 339 
247 1 Y 1 D LYS 340 ? D LYS 340 
248 1 Y 1 D PHE 341 ? D PHE 341 
249 1 Y 1 D GLU 342 ? D GLU 342 
250 1 Y 1 D THR 343 ? D THR 343 
251 1 Y 1 D THR 344 ? D THR 344 
252 1 Y 1 D MET 345 ? D MET 345 
253 1 Y 1 D THR 346 ? D THR 346 
254 1 Y 1 D SER 347 ? D SER 347 
255 1 Y 1 D TRP 348 ? D TRP 348 
256 1 Y 1 D GLY 349 ? D GLY 349 
257 1 Y 1 D LEU 350 ? D LEU 350 
258 1 Y 1 D VAL 351 ? D VAL 351 
259 1 Y 1 D VAL 352 ? D VAL 352 
260 1 Y 1 D SER 353 ? D SER 353 
261 1 Y 1 D SER 354 ? D SER 354 
262 1 Y 1 D ILE 355 ? D ILE 355 
263 1 Y 1 D ASN 356 ? D ASN 356 
264 1 Y 1 D ASN 357 ? D ASN 357 
265 1 Y 1 D ILE 358 ? D ILE 358 
266 1 Y 1 D ALA 359 ? D ALA 359 
267 1 Y 1 D GLU 360 ? D GLU 360 
268 1 Y 1 D ASN 361 ? D ASN 361 
269 1 Y 1 D VAL 362 ? D VAL 362 
270 1 Y 1 D ASN 363 ? D ASN 363 
271 1 Y 1 D HIS 364 ? D HIS 364 
272 1 Y 1 D LYS 365 ? D LYS 365 
273 1 Y 1 D THR 366 ? D THR 366 
274 1 Y 1 D TYR 367 ? D TYR 367 
275 1 Y 1 D TRP 368 ? D TRP 368 
276 1 Y 1 D GLN 369 ? D GLN 369 
277 1 Y 1 D PHE 370 ? D PHE 370 
278 1 Y 1 D LEU 371 ? D LEU 371 
279 1 Y 1 D SER 372 ? D SER 372 
280 1 Y 1 D GLY 373 ? D GLY 373 
281 1 Y 1 D VAL 374 ? D VAL 374 
282 1 Y 1 D THR 375 ? D THR 375 
283 1 Y 1 D PRO 376 ? D PRO 376 
284 1 Y 1 D LEU 377 ? D LEU 377 
285 1 Y 1 D ASN 378 ? D ASN 378 
286 1 Y 1 D GLU 379 ? D GLU 379 
287 1 Y 1 D GLY 380 ? D GLY 380 
288 1 Y 1 D VAL 381 ? D VAL 381 
289 1 Y 1 D ALA 382 ? D ALA 382 
290 1 Y 1 D ASP 383 ? D ASP 383 
291 1 Y 1 D TYR 384 ? D TYR 384 
292 1 Y 1 D ILE 385 ? D ILE 385 
293 1 Y 1 D PRO 386 ? D PRO 386 
294 1 Y 1 D PHE 387 ? D PHE 387 
295 1 Y 1 D ASN 388 ? D ASN 388 
296 1 Y 1 D HIS 389 ? D HIS 389 
297 1 Y 1 D GLU 390 ? D GLU 390 
298 1 Y 1 D HIS 391 ? D HIS 391 
299 1 Y 1 D ILE 392 ? D ILE 392 
300 1 Y 1 D THR 393 ? D THR 393 
301 1 Y 1 D ALA 394 ? D ALA 394 
302 1 Y 1 D ASN 395 ? D ASN 395 
303 1 Y 1 D PHE 396 ? D PHE 396 
304 1 Y 1 D THR 397 ? D THR 397 
305 1 Y 1 D GLN 398 ? D GLN 398 
306 1 Y 1 D TYR 399 ? D TYR 399 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 COBALAMIN              B12 
4 water                  HOH 
# 
