data_3P3Y
# 
_entry.id   3P3Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3P3Y         
RCSB  RCSB061925   
WWPDB D_1000061925 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          3P40 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3P3Y 
_pdbx_database_status.recvd_initial_deposition_date   2010-10-05 
_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 
'Liu, H.' 1 
'He, X.'  2 
# 
_citation.id                        primary 
_citation.title                     
'Homophilic adhesion mechanism of neurofascin, a member of the l1 family of neural cell adhesion molecules.' 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_volume            286 
_citation.page_first                797 
_citation.page_last                 805 
_citation.year                      2011 
_citation.journal_id_ASTM           JBCHA3 
_citation.country                   US 
_citation.journal_id_ISSN           0021-9258 
_citation.journal_id_CSD            0071 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   21047790 
_citation.pdbx_database_id_DOI      10.1074/jbc.M110.180281 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Liu, H.'     1 
primary 'Focia, P.J.' 2 
primary 'He, X.'      3 
# 
_cell.entry_id           3P3Y 
_cell.length_a           171.425 
_cell.length_b           171.425 
_cell.length_c           87.792 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              12 
_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                         3P3Y 
_symmetry.space_group_name_H-M             'P 65 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                179 
_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 Neurofascin            45285.199 1   ? ? 'N-terminal four Ig domains (UNP residues 25-428)' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   1   ? ? ?                                                  ? 
3 water       nat water                  18.015    495 ? ? ?                                                  ? 
# 
_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       
;IEIPMDPSIQNELTQPPTITKQSAKDHIVDPRDNILIECEAKGNPAPSFHWTRNSRFFNIAKDPRVSMRRRSGTLVIDFR
SGGRPEEYEGEYQCFARNKFGTALSNRIRLQVSKSPLWPKENLDPVVVQEGAPLTLQCNPPPGLPSPVIFWMSSSMEPIT
QDKRVSQGHNGDLYFSNVMLQDMQTDYSCNARFHFTHTIQQKNPFTLKVLTTRGVAERTPSFMYPQGTASSQMVLRGMDL
LLECIASGVPTPDIAWYKKGGDLPSDKAKFENFNKALRITNVSEEDSGEYFCLASNKMGSIRHTISVRVKAAPYWLDEPK
NLILAPGEDGRLVCRANGNPKPTVQWMVNGEPLQSAPPNPNREVAGDTIIFRDTQISSRAVYQCNTSNEHGYLLANAFVS
VLDV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IEIPMDPSIQNELTQPPTITKQSAKDHIVDPRDNILIECEAKGNPAPSFHWTRNSRFFNIAKDPRVSMRRRSGTLVIDFR
SGGRPEEYEGEYQCFARNKFGTALSNRIRLQVSKSPLWPKENLDPVVVQEGAPLTLQCNPPPGLPSPVIFWMSSSMEPIT
QDKRVSQGHNGDLYFSNVMLQDMQTDYSCNARFHFTHTIQQKNPFTLKVLTTRGVAERTPSFMYPQGTASSQMVLRGMDL
LLECIASGVPTPDIAWYKKGGDLPSDKAKFENFNKALRITNVSEEDSGEYFCLASNKMGSIRHTISVRVKAAPYWLDEPK
NLILAPGEDGRLVCRANGNPKPTVQWMVNGEPLQSAPPNPNREVAGDTIIFRDTQISSRAVYQCNTSNEHGYLLANAFVS
VLDV
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ILE n 
1 2   GLU n 
1 3   ILE n 
1 4   PRO n 
1 5   MET n 
1 6   ASP n 
1 7   PRO n 
1 8   SER n 
1 9   ILE n 
1 10  GLN n 
1 11  ASN n 
1 12  GLU n 
1 13  LEU n 
1 14  THR n 
1 15  GLN n 
1 16  PRO n 
1 17  PRO n 
1 18  THR n 
1 19  ILE n 
1 20  THR n 
1 21  LYS n 
1 22  GLN n 
1 23  SER n 
1 24  ALA n 
1 25  LYS n 
1 26  ASP n 
1 27  HIS n 
1 28  ILE n 
1 29  VAL n 
1 30  ASP n 
1 31  PRO n 
1 32  ARG n 
1 33  ASP n 
1 34  ASN n 
1 35  ILE n 
1 36  LEU n 
1 37  ILE n 
1 38  GLU n 
1 39  CYS n 
1 40  GLU n 
1 41  ALA n 
1 42  LYS n 
1 43  GLY n 
1 44  ASN n 
1 45  PRO n 
1 46  ALA n 
1 47  PRO n 
1 48  SER n 
1 49  PHE n 
1 50  HIS n 
1 51  TRP n 
1 52  THR n 
1 53  ARG n 
1 54  ASN n 
1 55  SER n 
1 56  ARG n 
1 57  PHE n 
1 58  PHE n 
1 59  ASN n 
1 60  ILE n 
1 61  ALA n 
1 62  LYS n 
1 63  ASP n 
1 64  PRO n 
1 65  ARG n 
1 66  VAL n 
1 67  SER n 
1 68  MET n 
1 69  ARG n 
1 70  ARG n 
1 71  ARG n 
1 72  SER n 
1 73  GLY n 
1 74  THR n 
1 75  LEU n 
1 76  VAL n 
1 77  ILE n 
1 78  ASP n 
1 79  PHE n 
1 80  ARG n 
1 81  SER n 
1 82  GLY n 
1 83  GLY n 
1 84  ARG n 
1 85  PRO n 
1 86  GLU n 
1 87  GLU n 
1 88  TYR n 
1 89  GLU n 
1 90  GLY n 
1 91  GLU n 
1 92  TYR n 
1 93  GLN n 
1 94  CYS n 
1 95  PHE n 
1 96  ALA n 
1 97  ARG n 
1 98  ASN n 
1 99  LYS n 
1 100 PHE n 
1 101 GLY n 
1 102 THR n 
1 103 ALA n 
1 104 LEU n 
1 105 SER n 
1 106 ASN n 
1 107 ARG n 
1 108 ILE n 
1 109 ARG n 
1 110 LEU n 
1 111 GLN n 
1 112 VAL n 
1 113 SER n 
1 114 LYS n 
1 115 SER n 
1 116 PRO n 
1 117 LEU n 
1 118 TRP n 
1 119 PRO n 
1 120 LYS n 
1 121 GLU n 
1 122 ASN n 
1 123 LEU n 
1 124 ASP n 
1 125 PRO n 
1 126 VAL n 
1 127 VAL n 
1 128 VAL n 
1 129 GLN n 
1 130 GLU n 
1 131 GLY n 
1 132 ALA n 
1 133 PRO n 
1 134 LEU n 
1 135 THR n 
1 136 LEU n 
1 137 GLN n 
1 138 CYS n 
1 139 ASN n 
1 140 PRO n 
1 141 PRO n 
1 142 PRO n 
1 143 GLY n 
1 144 LEU n 
1 145 PRO n 
1 146 SER n 
1 147 PRO n 
1 148 VAL n 
1 149 ILE n 
1 150 PHE n 
1 151 TRP n 
1 152 MET n 
1 153 SER n 
1 154 SER n 
1 155 SER n 
1 156 MET n 
1 157 GLU n 
1 158 PRO n 
1 159 ILE n 
1 160 THR n 
1 161 GLN n 
1 162 ASP n 
1 163 LYS n 
1 164 ARG n 
1 165 VAL n 
1 166 SER n 
1 167 GLN n 
1 168 GLY n 
1 169 HIS n 
1 170 ASN n 
1 171 GLY n 
1 172 ASP n 
1 173 LEU n 
1 174 TYR n 
1 175 PHE n 
1 176 SER n 
1 177 ASN n 
1 178 VAL n 
1 179 MET n 
1 180 LEU n 
1 181 GLN n 
1 182 ASP n 
1 183 MET n 
1 184 GLN n 
1 185 THR n 
1 186 ASP n 
1 187 TYR n 
1 188 SER n 
1 189 CYS n 
1 190 ASN n 
1 191 ALA n 
1 192 ARG n 
1 193 PHE n 
1 194 HIS n 
1 195 PHE n 
1 196 THR n 
1 197 HIS n 
1 198 THR n 
1 199 ILE n 
1 200 GLN n 
1 201 GLN n 
1 202 LYS n 
1 203 ASN n 
1 204 PRO n 
1 205 PHE n 
1 206 THR n 
1 207 LEU n 
1 208 LYS n 
1 209 VAL n 
1 210 LEU n 
1 211 THR n 
1 212 THR n 
1 213 ARG n 
1 214 GLY n 
1 215 VAL n 
1 216 ALA n 
1 217 GLU n 
1 218 ARG n 
1 219 THR n 
1 220 PRO n 
1 221 SER n 
1 222 PHE n 
1 223 MET n 
1 224 TYR n 
1 225 PRO n 
1 226 GLN n 
1 227 GLY n 
1 228 THR n 
1 229 ALA n 
1 230 SER n 
1 231 SER n 
1 232 GLN n 
1 233 MET n 
1 234 VAL n 
1 235 LEU n 
1 236 ARG n 
1 237 GLY n 
1 238 MET n 
1 239 ASP n 
1 240 LEU n 
1 241 LEU n 
1 242 LEU n 
1 243 GLU n 
1 244 CYS n 
1 245 ILE n 
1 246 ALA n 
1 247 SER n 
1 248 GLY n 
1 249 VAL n 
1 250 PRO n 
1 251 THR n 
1 252 PRO n 
1 253 ASP n 
1 254 ILE n 
1 255 ALA n 
1 256 TRP n 
1 257 TYR n 
1 258 LYS n 
1 259 LYS n 
1 260 GLY n 
1 261 GLY n 
1 262 ASP n 
1 263 LEU n 
1 264 PRO n 
1 265 SER n 
1 266 ASP n 
1 267 LYS n 
1 268 ALA n 
1 269 LYS n 
1 270 PHE n 
1 271 GLU n 
1 272 ASN n 
1 273 PHE n 
1 274 ASN n 
1 275 LYS n 
1 276 ALA n 
1 277 LEU n 
1 278 ARG n 
1 279 ILE n 
1 280 THR n 
1 281 ASN n 
1 282 VAL n 
1 283 SER n 
1 284 GLU n 
1 285 GLU n 
1 286 ASP n 
1 287 SER n 
1 288 GLY n 
1 289 GLU n 
1 290 TYR n 
1 291 PHE n 
1 292 CYS n 
1 293 LEU n 
1 294 ALA n 
1 295 SER n 
1 296 ASN n 
1 297 LYS n 
1 298 MET n 
1 299 GLY n 
1 300 SER n 
1 301 ILE n 
1 302 ARG n 
1 303 HIS n 
1 304 THR n 
1 305 ILE n 
1 306 SER n 
1 307 VAL n 
1 308 ARG n 
1 309 VAL n 
1 310 LYS n 
1 311 ALA n 
1 312 ALA n 
1 313 PRO n 
1 314 TYR n 
1 315 TRP n 
1 316 LEU n 
1 317 ASP n 
1 318 GLU n 
1 319 PRO n 
1 320 LYS n 
1 321 ASN n 
1 322 LEU n 
1 323 ILE n 
1 324 LEU n 
1 325 ALA n 
1 326 PRO n 
1 327 GLY n 
1 328 GLU n 
1 329 ASP n 
1 330 GLY n 
1 331 ARG n 
1 332 LEU n 
1 333 VAL n 
1 334 CYS n 
1 335 ARG n 
1 336 ALA n 
1 337 ASN n 
1 338 GLY n 
1 339 ASN n 
1 340 PRO n 
1 341 LYS n 
1 342 PRO n 
1 343 THR n 
1 344 VAL n 
1 345 GLN n 
1 346 TRP n 
1 347 MET n 
1 348 VAL n 
1 349 ASN n 
1 350 GLY n 
1 351 GLU n 
1 352 PRO n 
1 353 LEU n 
1 354 GLN n 
1 355 SER n 
1 356 ALA n 
1 357 PRO n 
1 358 PRO n 
1 359 ASN n 
1 360 PRO n 
1 361 ASN n 
1 362 ARG n 
1 363 GLU n 
1 364 VAL n 
1 365 ALA n 
1 366 GLY n 
1 367 ASP n 
1 368 THR n 
1 369 ILE n 
1 370 ILE n 
1 371 PHE n 
1 372 ARG n 
1 373 ASP n 
1 374 THR n 
1 375 GLN n 
1 376 ILE n 
1 377 SER n 
1 378 SER n 
1 379 ARG n 
1 380 ALA n 
1 381 VAL n 
1 382 TYR n 
1 383 GLN n 
1 384 CYS n 
1 385 ASN n 
1 386 THR n 
1 387 SER n 
1 388 ASN n 
1 389 GLU n 
1 390 HIS n 
1 391 GLY n 
1 392 TYR n 
1 393 LEU n 
1 394 LEU n 
1 395 ALA n 
1 396 ASN n 
1 397 ALA n 
1 398 PHE n 
1 399 VAL n 
1 400 SER n 
1 401 VAL n 
1 402 LEU n 
1 403 ASP n 
1 404 VAL 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                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'NFASC, KIAA0756' 
_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               'cabbage looper' 
_entity_src_gen.pdbx_host_org_scientific_name      'Trichoplusia ni' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7111 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            Hi5 
_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                    NFASC_HUMAN 
_struct_ref.pdbx_db_accession          O94856 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;IEIPMDPSIQNELTQPPTITKQSAKDHIVDPRDNILIECEAKGNPAPSFHWTRNSRFFNIAKDPRVSMRRRSGTLVIDFR
SGGRPEEYEGEYQCFARNKFGTALSNRIRLQVSKSPLWPKENLDPVVVQEGAPLTLQCNPPPGLPSPVIFWMSSSMEPIT
QDKRVSQGHNGDLYFSNVMLQDMQTDYSCNARFHFTHTIQQKNPFTLKVLTTRGVAERTPSFMYPQGTASSQMVLRGMDL
LLECIASGVPTPDIAWYKKGGDLPSDKAKFENFNKALRITNVSEEDSGEYFCLASNKMGSIRHTISVRVKAAPYWLDEPK
NLILAPGEDGRLVCRANGNPKPTVQWMVNGEPLQSAPPNPNREVAGDTIIFRDTQISSRAVYQCNTSNEHGYLLANAFVS
VLDV
;
_struct_ref.pdbx_align_begin           25 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3P3Y 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 404 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O94856 
_struct_ref_seq.db_align_beg                  25 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  428 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       25 
_struct_ref_seq.pdbx_auth_seq_align_end       428 
# 
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 
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          3P3Y 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      4.11 
_exptl_crystal.density_percent_sol   70.08 
_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            293.15 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_details    
'1.4 ammonium sulfate, 0.1 M cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K' 
_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               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR scanner 300 mm plate' 
_diffrn_detector.pdbx_collection_date   2008-08-14 
_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                    'Si(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54981 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 21-ID-D' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.54981 
# 
_reflns.entry_id                     3P3Y 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   0.0 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            2.6 
_reflns.number_obs                   23568 
_reflns.number_all                   23854 
_reflns.percent_possible_obs         98.8 
_reflns.pdbx_Rmerge_I_obs            0.050 
_reflns.pdbx_Rsym_value              0.054 
_reflns.pdbx_netI_over_sigmaI        19.9 
_reflns.B_iso_Wilson_estimate        42.6 
_reflns.pdbx_redundancy              5.8 
_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_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.6 
_reflns_shell.d_res_low              2.7 
_reflns_shell.percent_possible_all   96.4 
_reflns_shell.Rmerge_I_obs           0.487 
_reflns_shell.pdbx_Rsym_value        0.427 
_reflns_shell.meanI_over_sigI_obs    2.4 
_reflns_shell.pdbx_redundancy        3.9 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      2390 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3P3Y 
_refine.ls_number_reflns_obs                     23508 
_refine.ls_number_reflns_all                     23769 
_refine.pdbx_ls_sigma_I                          0.0 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               3482001.70 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.71 
_refine.ls_d_res_high                            2.60 
_refine.ls_percent_reflns_obs                    98.9 
_refine.ls_R_factor_obs                          0.258 
_refine.ls_R_factor_all                          0.274 
_refine.ls_R_factor_R_work                       0.258 
_refine.ls_R_factor_R_free                       0.288 
_refine.ls_R_factor_R_free_error                 0.009 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_number_reflns_R_free                  1131 
_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                               89.0 
_refine.aniso_B[1][1]                            -4.32 
_refine.aniso_B[2][2]                            -4.32 
_refine.aniso_B[3][3]                            8.65 
_refine.aniso_B[1][2]                            -2.33 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.24541 
_refine.solvent_model_param_bsol                 45.1788 
_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                                  'BULK SOLVENT MODEL USED' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          SIRAS 
_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_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_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_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_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                        3P3Y 
_refine_analyze.Luzzati_coordinate_error_obs    0.43 
_refine_analyze.Luzzati_sigma_a_obs             0.54 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.50 
_refine_analyze.Luzzati_sigma_a_free            0.56 
_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        3068 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         14 
_refine_hist.number_atoms_solvent             495 
_refine_hist.number_atoms_total               3577 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        19.71 
# 
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           0.010 ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        1.5   ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d 28.0  ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d 1.25  ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_restr_ncs.pdbx_refine_id      'X-RAY DIFFRACTION' 
_refine_ls_restr_ncs.dom_id              1 
_refine_ls_restr_ncs.ncs_model_details   NONE 
_refine_ls_restr_ncs.rms_dev_position    ? 
_refine_ls_restr_ncs.weight_position     ? 
_refine_ls_restr_ncs.rms_dev_B_iso       ? 
_refine_ls_restr_ncs.weight_B_iso        ? 
_refine_ls_restr_ncs.pdbx_ordinal        1 
_refine_ls_restr_ncs.pdbx_type           . 
_refine_ls_restr_ncs.pdbx_auth_asym_id   . 
_refine_ls_restr_ncs.pdbx_ens_id         1 
_refine_ls_restr_ncs.pdbx_number         ? 
# 
_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             3547 
_refine_ls_shell.R_factor_R_work                  0.366 
_refine_ls_shell.percent_reflns_obs               95.6 
_refine_ls_shell.R_factor_R_free                  0.401 
_refine_ls_shell.R_factor_R_free_error            0.032 
_refine_ls_shell.percent_reflns_R_free            4.4 
_refine_ls_shell.number_reflns_R_free             162 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                3547 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 protein_rep.param  protein.top      'X-RAY DIFFRACTION' 
2 water_rep.param    water.top        'X-RAY DIFFRACTION' 
3 carbohydrate.param carbohydrate.top 'X-RAY DIFFRACTION' 
4 ion.param          ion.top          'X-RAY DIFFRACTION' 
# 
_struct_ncs_dom.id            1 
_struct_ncs_dom.details       ? 
_struct_ncs_dom.pdbx_ens_id   1 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                  3P3Y 
_struct.title                     'Crystal structure of neurofascin homophilic adhesion complex in space group p6522' 
_struct.pdbx_descriptor           Neurofascin 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3P3Y 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
_struct_keywords.text            'Ig domains, cell adhesion' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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 ASN A 59  ? ASP A 63  ? ASN A 83  ASP A 87  5 ? 5 
HELX_P HELX_P2 2 LEU A 180 ? GLN A 184 ? LEU A 204 GLN A 208 5 ? 5 
HELX_P HELX_P3 3 ASN A 272 ? ASN A 274 ? ASN A 296 ASN A 298 5 ? 3 
HELX_P HELX_P4 4 SER A 283 ? SER A 287 ? SER A 307 SER A 311 5 ? 5 
HELX_P HELX_P5 5 GLN A 354 ? ALA A 356 ? GLN A 378 ALA A 380 5 ? 3 
# 
_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 39  SG  ? ? ? 1_555 A CYS 94  SG ? ? A CYS 63  A CYS 118 1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf2 disulf ? ? A CYS 138 SG  ? ? ? 1_555 A CYS 189 SG ? ? A CYS 162 A CYS 213 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf3 disulf ? ? A CYS 244 SG  ? ? ? 1_555 A CYS 292 SG ? ? A CYS 268 A CYS 316 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf4 disulf ? ? A CYS 334 SG  ? ? ? 1_555 A CYS 384 SG ? ? A CYS 358 A CYS 408 1_555 ? ? ? ? ? ? ? 2.021 ? 
covale1 covale ? ? A ASN 385 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 409 A NAG 1   1_555 ? ? ? ? ? ? ? 1.294 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 144 A . ? LEU 168 A PRO 145 A ? PRO 169 A 1 -3.57 
2 ASN 339 A . ? ASN 363 A PRO 340 A ? PRO 364 A 1 5.21  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2 ? 
B ? 5 ? 
C ? 2 ? 
D ? 3 ? 
E ? 3 ? 
F ? 4 ? 
G ? 3 ? 
H ? 3 ? 
I ? 5 ? 
J ? 3 ? 
# 
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 
B 1 2 ? parallel      
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
C 1 2 ? parallel      
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
F 1 2 ? parallel      
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? parallel      
G 2 3 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
I 1 2 ? parallel      
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
I 4 5 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? 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 ILE A 19  ? GLN A 22  ? ILE A 43  GLN A 46  
A 2 CYS A 39  ? ALA A 41  ? CYS A 63  ALA A 65  
B 1 ILE A 28  ? VAL A 29  ? ILE A 52  VAL A 53  
B 2 THR A 102 ? VAL A 112 ? THR A 126 VAL A 136 
B 3 GLY A 90  ? ARG A 97  ? GLY A 114 ARG A 121 
B 4 SER A 48  ? ARG A 53  ? SER A 72  ARG A 77  
B 5 ARG A 56  ? PHE A 57  ? ARG A 80  PHE A 81  
C 1 VAL A 126 ? GLN A 129 ? VAL A 150 GLN A 153 
C 2 LEU A 207 ? LEU A 210 ? LEU A 231 LEU A 234 
D 1 LEU A 134 ? LEU A 136 ? LEU A 158 LEU A 160 
D 2 LEU A 173 ? PHE A 175 ? LEU A 197 PHE A 199 
D 3 VAL A 165 ? GLN A 167 ? VAL A 189 GLN A 191 
E 1 VAL A 148 ? MET A 152 ? VAL A 172 MET A 176 
E 2 SER A 188 ? ARG A 192 ? SER A 212 ARG A 216 
E 3 ILE A 199 ? GLN A 201 ? ILE A 223 GLN A 225 
F 1 ALA A 229 ? LEU A 235 ? ALA A 253 LEU A 259 
F 2 SER A 300 ? ASP A 317 ? SER A 324 ASP A 341 
F 3 GLY A 288 ? SER A 295 ? GLY A 312 SER A 319 
F 4 ASP A 253 ? LYS A 258 ? ASP A 277 LYS A 282 
G 1 ALA A 229 ? LEU A 235 ? ALA A 253 LEU A 259 
G 2 SER A 300 ? ASP A 317 ? SER A 324 ASP A 341 
G 3 ARG A 335 ? ASN A 339 ? ARG A 359 ASN A 363 
H 1 LEU A 240 ? GLU A 243 ? LEU A 264 GLU A 267 
H 2 ALA A 276 ? ILE A 279 ? ALA A 300 ILE A 303 
H 3 ALA A 268 ? GLU A 271 ? ALA A 292 GLU A 295 
I 1 LEU A 322 ? LEU A 324 ? LEU A 346 LEU A 348 
I 2 GLY A 391 ? VAL A 401 ? GLY A 415 VAL A 425 
I 3 VAL A 381 ? ASN A 388 ? VAL A 405 ASN A 412 
I 4 THR A 343 ? VAL A 348 ? THR A 367 VAL A 372 
I 5 GLU A 351 ? PRO A 352 ? GLU A 375 PRO A 376 
J 1 GLY A 330 ? VAL A 333 ? GLY A 354 VAL A 357 
J 2 THR A 368 ? PHE A 371 ? THR A 392 PHE A 395 
J 3 ARG A 362 ? ALA A 365 ? ARG A 386 ALA A 389 
# 
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 N THR A 20  ? N THR A 44  O GLU A 40  ? O GLU A 64  
B 1 2 N VAL A 29  ? N VAL A 53  O GLN A 111 ? O GLN A 135 
B 2 3 O ALA A 103 ? O ALA A 127 N ALA A 96  ? N ALA A 120 
B 3 4 O ARG A 97  ? O ARG A 121 N SER A 48  ? N SER A 72  
B 4 5 N ARG A 53  ? N ARG A 77  O ARG A 56  ? O ARG A 80  
C 1 2 N VAL A 126 ? N VAL A 150 O LYS A 208 ? O LYS A 232 
D 1 2 N LEU A 136 ? N LEU A 160 O LEU A 173 ? O LEU A 197 
D 2 3 O TYR A 174 ? O TYR A 198 N SER A 166 ? N SER A 190 
E 1 2 N VAL A 148 ? N VAL A 172 O ARG A 192 ? O ARG A 216 
E 2 3 N ALA A 191 ? N ALA A 215 O GLN A 200 ? O GLN A 224 
F 1 2 N SER A 230 ? N SER A 254 O SER A 306 ? O SER A 330 
F 2 3 O ILE A 305 ? O ILE A 329 N TYR A 290 ? N TYR A 314 
F 3 4 O PHE A 291 ? O PHE A 315 N TYR A 257 ? N TYR A 281 
G 1 2 N SER A 230 ? N SER A 254 O SER A 306 ? O SER A 330 
G 2 3 N ASP A 317 ? N ASP A 341 O ARG A 335 ? O ARG A 359 
H 1 2 N LEU A 242 ? N LEU A 266 O LEU A 277 ? O LEU A 301 
H 2 3 O ARG A 278 ? O ARG A 302 N LYS A 269 ? N LYS A 293 
I 1 2 N LEU A 322 ? N LEU A 346 O PHE A 398 ? O PHE A 422 
I 2 3 O GLY A 391 ? O GLY A 415 N ASN A 388 ? N ASN A 412 
I 3 4 O GLN A 383 ? O GLN A 407 N MET A 347 ? N MET A 371 
I 4 5 N VAL A 348 ? N VAL A 372 O GLU A 351 ? O GLU A 375 
J 1 2 N LEU A 332 ? N LEU A 356 O ILE A 369 ? O ILE A 393 
J 2 3 O THR A 368 ? O THR A 392 N ALA A 365 ? N ALA A 389 
# 
_struct_site.id                   AC1 
_struct_site.pdbx_evidence_code   Software 
_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    8 
_struct_site.details              'BINDING SITE FOR RESIDUE NAG A 1' 
# 
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 8 ARG A 107 ? ARG A 131 . ? 1_555  ? 
2 AC1 8 GLN A 226 ? GLN A 250 . ? 10_666 ? 
3 AC1 8 GLN A 345 ? GLN A 369 . ? 1_555  ? 
4 AC1 8 ASN A 385 ? ASN A 409 . ? 1_555  ? 
5 AC1 8 SER A 387 ? SER A 411 . ? 1_555  ? 
6 AC1 8 TYR A 392 ? TYR A 416 . ? 1_555  ? 
7 AC1 8 HOH C .   ? HOH A 737 . ? 1_555  ? 
8 AC1 8 HOH C .   ? HOH A 872 . ? 1_555  ? 
# 
_database_PDB_matrix.entry_id          3P3Y 
_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                    3P3Y 
_atom_sites.fract_transf_matrix[1][1]   0.005833 
_atom_sites.fract_transf_matrix[1][2]   0.003368 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006736 
_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]   0.011391 
_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 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU A 1 13  ? 20.872 67.182  5.944  1.00 164.73 ? 37  LEU A N   1 
ATOM   2    C CA  . LEU A 1 13  ? 19.404 66.981  5.989  1.00 164.73 ? 37  LEU A CA  1 
ATOM   3    C C   . LEU A 1 13  ? 18.912 66.527  7.371  1.00 164.65 ? 37  LEU A C   1 
ATOM   4    O O   . LEU A 1 13  ? 18.615 67.368  8.226  1.00 164.69 ? 37  LEU A O   1 
ATOM   5    C CB  . LEU A 1 13  ? 18.959 65.965  4.910  1.00 121.08 ? 37  LEU A CB  1 
ATOM   6    C CG  . LEU A 1 13  ? 17.483 66.006  4.461  1.00 121.49 ? 37  LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 13  ? 17.302 66.967  3.278  1.00 121.61 ? 37  LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 13  ? 17.011 64.610  4.081  1.00 121.78 ? 37  LEU A CD2 1 
ATOM   9    N N   . THR A 1 14  ? 18.879 65.209  7.599  1.00 193.19 ? 38  THR A N   1 
ATOM   10   C CA  . THR A 1 14  ? 18.318 64.637  8.827  1.00 192.91 ? 38  THR A CA  1 
ATOM   11   C C   . THR A 1 14  ? 19.069 64.847  10.144 1.00 192.71 ? 38  THR A C   1 
ATOM   12   O O   . THR A 1 14  ? 19.720 63.936  10.667 1.00 192.74 ? 38  THR A O   1 
ATOM   13   C CB  . THR A 1 14  ? 17.983 63.104  8.622  1.00 116.75 ? 38  THR A CB  1 
ATOM   14   O OG1 . THR A 1 14  ? 17.543 62.526  9.862  1.00 116.63 ? 38  THR A OG1 1 
ATOM   15   C CG2 . THR A 1 14  ? 19.197 62.339  8.087  1.00 116.63 ? 38  THR A CG2 1 
ATOM   16   N N   . GLN A 1 15  ? 18.968 66.063  10.680 1.00 159.04 ? 39  GLN A N   1 
ATOM   17   C CA  . GLN A 1 15  ? 19.589 66.374  11.962 1.00 158.60 ? 39  GLN A CA  1 
ATOM   18   C C   . GLN A 1 15  ? 18.617 67.026  12.963 1.00 158.06 ? 39  GLN A C   1 
ATOM   19   O O   . GLN A 1 15  ? 17.853 67.934  12.602 1.00 158.01 ? 39  GLN A O   1 
ATOM   20   C CB  . GLN A 1 15  ? 20.849 67.262  11.782 1.00 138.55 ? 39  GLN A CB  1 
ATOM   21   C CG  . GLN A 1 15  ? 20.648 68.583  11.028 1.00 139.00 ? 39  GLN A CG  1 
ATOM   22   C CD  . GLN A 1 15  ? 21.954 69.346  10.791 1.00 139.64 ? 39  GLN A CD  1 
ATOM   23   O OE1 . GLN A 1 15  ? 22.779 69.500  11.699 1.00 139.72 ? 39  GLN A OE1 1 
ATOM   24   N NE2 . GLN A 1 15  ? 22.137 69.836  9.568  1.00 139.60 ? 39  GLN A NE2 1 
ATOM   25   N N   . PRO A 1 16  ? 18.605 66.520  14.226 1.00 151.68 ? 40  PRO A N   1 
ATOM   26   C CA  . PRO A 1 16  ? 17.767 67.003  15.337 1.00 145.05 ? 40  PRO A CA  1 
ATOM   27   C C   . PRO A 1 16  ? 18.035 68.493  15.632 1.00 135.55 ? 40  PRO A C   1 
ATOM   28   O O   . PRO A 1 16  ? 18.988 69.075  15.097 1.00 147.70 ? 40  PRO A O   1 
ATOM   29   C CB  . PRO A 1 16  ? 18.174 66.106  16.500 1.00 117.28 ? 40  PRO A CB  1 
ATOM   30   C CG  . PRO A 1 16  ? 18.523 64.820  15.848 1.00 115.65 ? 40  PRO A CG  1 
ATOM   31   C CD  . PRO A 1 16  ? 19.246 65.234  14.581 1.00 122.17 ? 40  PRO A CD  1 
ATOM   32   N N   . PRO A 1 17  ? 17.221 69.112  16.515 1.00 92.44  ? 41  PRO A N   1 
ATOM   33   C CA  . PRO A 1 17  ? 17.387 70.536  16.845 1.00 83.99  ? 41  PRO A CA  1 
ATOM   34   C C   . PRO A 1 17  ? 18.694 70.914  17.520 1.00 83.89  ? 41  PRO A C   1 
ATOM   35   O O   . PRO A 1 17  ? 19.234 70.149  18.324 1.00 82.58  ? 41  PRO A O   1 
ATOM   36   C CB  . PRO A 1 17  ? 16.187 70.846  17.752 1.00 58.31  ? 41  PRO A CB  1 
ATOM   37   C CG  . PRO A 1 17  ? 15.254 69.687  17.584 1.00 53.40  ? 41  PRO A CG  1 
ATOM   38   C CD  . PRO A 1 17  ? 16.135 68.511  17.316 1.00 65.11  ? 41  PRO A CD  1 
ATOM   39   N N   . THR A 1 18  ? 19.192 72.101  17.189 1.00 82.05  ? 42  THR A N   1 
ATOM   40   C CA  . THR A 1 18  ? 20.418 72.609  17.778 1.00 85.78  ? 42  THR A CA  1 
ATOM   41   C C   . THR A 1 18  ? 20.283 74.124  17.911 1.00 83.88  ? 42  THR A C   1 
ATOM   42   O O   . THR A 1 18  ? 20.050 74.815  16.916 1.00 82.47  ? 42  THR A O   1 
ATOM   43   C CB  . THR A 1 18  ? 21.649 72.241  16.909 1.00 93.61  ? 42  THR A CB  1 
ATOM   44   O OG1 . THR A 1 18  ? 21.793 70.813  16.872 1.00 97.63  ? 42  THR A OG1 1 
ATOM   45   C CG2 . THR A 1 18  ? 22.924 72.849  17.481 1.00 98.12  ? 42  THR A CG2 1 
ATOM   46   N N   . ILE A 1 19  ? 20.412 74.629  19.142 1.00 80.91  ? 43  ILE A N   1 
ATOM   47   C CA  . ILE A 1 19  ? 20.290 76.067  19.411 1.00 80.09  ? 43  ILE A CA  1 
ATOM   48   C C   . ILE A 1 19  ? 21.355 76.855  18.640 1.00 82.86  ? 43  ILE A C   1 
ATOM   49   O O   . ILE A 1 19  ? 22.550 76.563  18.707 1.00 80.16  ? 43  ILE A O   1 
ATOM   50   C CB  . ILE A 1 19  ? 20.333 76.368  20.951 1.00 87.23  ? 43  ILE A CB  1 
ATOM   51   C CG1 . ILE A 1 19  ? 18.945 76.152  21.562 1.00 86.07  ? 43  ILE A CG1 1 
ATOM   52   C CG2 . ILE A 1 19  ? 20.760 77.809  21.215 1.00 88.19  ? 43  ILE A CG2 1 
ATOM   53   C CD1 . ILE A 1 19  ? 18.969 75.838  23.018 1.00 85.06  ? 43  ILE A CD1 1 
ATOM   54   N N   . THR A 1 20  ? 20.884 77.851  17.896 1.00 89.37  ? 44  THR A N   1 
ATOM   55   C CA  . THR A 1 20  ? 21.711 78.670  17.018 1.00 95.65  ? 44  THR A CA  1 
ATOM   56   C C   . THR A 1 20  ? 22.135 79.952  17.704 1.00 88.03  ? 44  THR A C   1 
ATOM   57   O O   . THR A 1 20  ? 23.295 80.364  17.614 1.00 81.75  ? 44  THR A O   1 
ATOM   58   C CB  . THR A 1 20  ? 20.911 79.001  15.712 1.00 127.40 ? 44  THR A CB  1 
ATOM   59   O OG1 . THR A 1 20  ? 20.754 77.806  14.932 1.00 145.53 ? 44  THR A OG1 1 
ATOM   60   C CG2 . THR A 1 20  ? 21.610 80.073  14.876 1.00 146.02 ? 44  THR A CG2 1 
ATOM   61   N N   . LYS A 1 21  ? 21.181 80.563  18.394 1.00 85.90  ? 45  LYS A N   1 
ATOM   62   C CA  . LYS A 1 21  ? 21.396 81.806  19.108 1.00 82.86  ? 45  LYS A CA  1 
ATOM   63   C C   . LYS A 1 21  ? 20.466 81.803  20.317 1.00 80.07  ? 45  LYS A C   1 
ATOM   64   O O   . LYS A 1 21  ? 19.475 81.069  20.339 1.00 81.81  ? 45  LYS A O   1 
ATOM   65   C CB  . LYS A 1 21  ? 21.044 82.993  18.194 1.00 81.87  ? 45  LYS A CB  1 
ATOM   66   C CG  . LYS A 1 21  ? 21.497 84.352  18.709 1.00 84.59  ? 45  LYS A CG  1 
ATOM   67   C CD  . LYS A 1 21  ? 20.762 85.510  18.031 1.00 85.45  ? 45  LYS A CD  1 
ATOM   68   C CE  . LYS A 1 21  ? 21.414 85.933  16.724 1.00 86.21  ? 45  LYS A CE  1 
ATOM   69   N NZ  . LYS A 1 21  ? 20.815 87.194  16.199 1.00 86.23  ? 45  LYS A NZ  1 
ATOM   70   N N   . GLN A 1 22  ? 20.809 82.599  21.328 1.00 75.40  ? 46  GLN A N   1 
ATOM   71   C CA  . GLN A 1 22  ? 19.978 82.765  22.520 1.00 71.60  ? 46  GLN A CA  1 
ATOM   72   C C   . GLN A 1 22  ? 20.416 83.976  23.327 1.00 71.59  ? 46  GLN A C   1 
ATOM   73   O O   . GLN A 1 22  ? 21.584 84.375  23.275 1.00 71.67  ? 46  GLN A O   1 
ATOM   74   C CB  . GLN A 1 22  ? 20.020 81.523  23.418 1.00 64.91  ? 46  GLN A CB  1 
ATOM   75   C CG  . GLN A 1 22  ? 21.403 81.071  23.848 1.00 60.46  ? 46  GLN A CG  1 
ATOM   76   C CD  . GLN A 1 22  ? 21.362 79.815  24.703 1.00 59.15  ? 46  GLN A CD  1 
ATOM   77   O OE1 . GLN A 1 22  ? 21.862 78.761  24.307 1.00 58.54  ? 46  GLN A OE1 1 
ATOM   78   N NE2 . GLN A 1 22  ? 20.757 79.918  25.883 1.00 58.48  ? 46  GLN A NE2 1 
ATOM   79   N N   . SER A 1 23  ? 19.467 84.575  24.048 1.00 71.18  ? 47  SER A N   1 
ATOM   80   C CA  . SER A 1 23  ? 19.760 85.707  24.930 1.00 74.35  ? 47  SER A CA  1 
ATOM   81   C C   . SER A 1 23  ? 20.775 85.277  25.989 1.00 76.57  ? 47  SER A C   1 
ATOM   82   O O   . SER A 1 23  ? 20.877 84.096  26.326 1.00 76.24  ? 47  SER A O   1 
ATOM   83   C CB  . SER A 1 23  ? 18.486 86.202  25.619 1.00 69.13  ? 47  SER A CB  1 
ATOM   84   O OG  . SER A 1 23  ? 17.823 87.158  24.814 1.00 70.56  ? 47  SER A OG  1 
ATOM   85   N N   . ALA A 1 24  ? 21.527 86.240  26.506 1.00 79.92  ? 48  ALA A N   1 
ATOM   86   C CA  . ALA A 1 24  ? 22.544 85.951  27.507 1.00 80.16  ? 48  ALA A CA  1 
ATOM   87   C C   . ALA A 1 24  ? 21.943 85.353  28.776 1.00 78.47  ? 48  ALA A C   1 
ATOM   88   O O   . ALA A 1 24  ? 20.804 85.647  29.132 1.00 83.10  ? 48  ALA A O   1 
ATOM   89   C CB  . ALA A 1 24  ? 23.314 87.231  27.850 1.00 67.26  ? 48  ALA A CB  1 
ATOM   90   N N   . LYS A 1 25  ? 22.718 84.491  29.433 1.00 75.71  ? 49  LYS A N   1 
ATOM   91   C CA  . LYS A 1 25  ? 22.337 83.866  30.703 1.00 72.10  ? 49  LYS A CA  1 
ATOM   92   C C   . LYS A 1 25  ? 21.807 84.935  31.670 1.00 71.55  ? 49  LYS A C   1 
ATOM   93   O O   . LYS A 1 25  ? 20.807 84.723  32.356 1.00 67.63  ? 49  LYS A O   1 
ATOM   94   C CB  . LYS A 1 25  ? 23.558 83.179  31.326 1.00 72.55  ? 49  LYS A CB  1 
ATOM   95   C CG  . LYS A 1 25  ? 23.236 81.981  32.191 1.00 70.73  ? 49  LYS A CG  1 
ATOM   96   C CD  . LYS A 1 25  ? 23.667 80.683  31.528 1.00 70.85  ? 49  LYS A CD  1 
ATOM   97   C CE  . LYS A 1 25  ? 25.075 80.286  31.934 1.00 71.41  ? 49  LYS A CE  1 
ATOM   98   N NZ  . LYS A 1 25  ? 25.372 78.871  31.559 1.00 72.66  ? 49  LYS A NZ  1 
ATOM   99   N N   . ASP A 1 26  ? 22.496 86.073  31.723 1.00 73.83  ? 50  ASP A N   1 
ATOM   100  C CA  . ASP A 1 26  ? 22.084 87.198  32.567 1.00 82.98  ? 50  ASP A CA  1 
ATOM   101  C C   . ASP A 1 26  ? 21.635 88.329  31.630 1.00 88.78  ? 50  ASP A C   1 
ATOM   102  O O   . ASP A 1 26  ? 22.398 89.251  31.332 1.00 86.28  ? 50  ASP A O   1 
ATOM   103  C CB  . ASP A 1 26  ? 23.252 87.651  33.445 1.00 92.53  ? 50  ASP A CB  1 
ATOM   104  C CG  . ASP A 1 26  ? 22.817 88.595  34.547 1.00 93.98  ? 50  ASP A CG  1 
ATOM   105  O OD1 . ASP A 1 26  ? 21.807 88.303  35.229 1.00 94.67  ? 50  ASP A OD1 1 
ATOM   106  O OD2 . ASP A 1 26  ? 23.496 89.625  34.742 1.00 93.41  ? 50  ASP A OD2 1 
ATOM   107  N N   . HIS A 1 27  ? 20.383 88.247  31.176 1.00 95.03  ? 51  HIS A N   1 
ATOM   108  C CA  . HIS A 1 27  ? 19.852 89.208  30.208 1.00 98.27  ? 51  HIS A CA  1 
ATOM   109  C C   . HIS A 1 27  ? 19.214 90.418  30.867 1.00 101.17 ? 51  HIS A C   1 
ATOM   110  O O   . HIS A 1 27  ? 18.063 90.385  31.314 1.00 102.33 ? 51  HIS A O   1 
ATOM   111  C CB  . HIS A 1 27  ? 18.870 88.510  29.260 1.00 99.05  ? 51  HIS A CB  1 
ATOM   112  C CG  . HIS A 1 27  ? 18.879 89.073  27.873 1.00 98.74  ? 51  HIS A CG  1 
ATOM   113  N ND1 . HIS A 1 27  ? 17.752 89.595  27.276 1.00 98.56  ? 51  HIS A ND1 1 
ATOM   114  C CD2 . HIS A 1 27  ? 19.881 89.204  26.969 1.00 98.98  ? 51  HIS A CD2 1 
ATOM   115  C CE1 . HIS A 1 27  ? 18.058 90.022  26.064 1.00 99.38  ? 51  HIS A CE1 1 
ATOM   116  N NE2 . HIS A 1 27  ? 19.343 89.796  25.852 1.00 99.98  ? 51  HIS A NE2 1 
ATOM   117  N N   . ILE A 1 28  ? 19.995 91.495  30.913 1.00 95.39  ? 52  ILE A N   1 
ATOM   118  C CA  . ILE A 1 28  ? 19.587 92.742  31.556 1.00 95.25  ? 52  ILE A CA  1 
ATOM   119  C C   . ILE A 1 28  ? 19.110 93.772  30.540 1.00 89.80  ? 52  ILE A C   1 
ATOM   120  O O   . ILE A 1 28  ? 19.736 93.960  29.493 1.00 88.08  ? 52  ILE A O   1 
ATOM   121  C CB  . ILE A 1 28  ? 20.756 93.320  32.408 1.00 103.32 ? 52  ILE A CB  1 
ATOM   122  C CG1 . ILE A 1 28  ? 22.080 93.227  31.636 1.00 109.26 ? 52  ILE A CG1 1 
ATOM   123  C CG2 . ILE A 1 28  ? 20.859 92.573  33.734 1.00 113.04 ? 52  ILE A CG2 1 
ATOM   124  C CD1 . ILE A 1 28  ? 22.309 94.345  30.640 1.00 102.44 ? 52  ILE A CD1 1 
ATOM   125  N N   . VAL A 1 29  ? 17.995 94.428  30.852 1.00 100.87 ? 53  VAL A N   1 
ATOM   126  C CA  . VAL A 1 29  ? 17.410 95.413  29.945 1.00 106.28 ? 53  VAL A CA  1 
ATOM   127  C C   . VAL A 1 29  ? 16.815 96.661  30.615 1.00 114.15 ? 53  VAL A C   1 
ATOM   128  O O   . VAL A 1 29  ? 16.315 96.601  31.748 1.00 115.17 ? 53  VAL A O   1 
ATOM   129  C CB  . VAL A 1 29  ? 16.266 94.774  29.057 1.00 96.92  ? 53  VAL A CB  1 
ATOM   130  C CG1 . VAL A 1 29  ? 16.867 93.928  27.932 1.00 90.57  ? 53  VAL A CG1 1 
ATOM   131  C CG2 . VAL A 1 29  ? 15.308 93.952  29.925 1.00 90.07  ? 53  VAL A CG2 1 
ATOM   132  N N   . ASP A 1 30  ? 16.906 97.788  29.903 1.00 154.68 ? 54  ASP A N   1 
ATOM   133  C CA  . ASP A 1 30  ? 16.297 99.051  30.331 1.00 170.06 ? 54  ASP A CA  1 
ATOM   134  C C   . ASP A 1 30  ? 14.834 99.065  29.868 1.00 177.20 ? 54  ASP A C   1 
ATOM   135  O O   . ASP A 1 30  ? 14.517 98.542  28.794 1.00 194.36 ? 54  ASP A O   1 
ATOM   136  C CB  . ASP A 1 30  ? 17.028 100.267 29.732 1.00 131.20 ? 54  ASP A CB  1 
ATOM   137  C CG  . ASP A 1 30  ? 17.315 100.131 28.230 1.00 112.06 ? 54  ASP A CG  1 
ATOM   138  O OD1 . ASP A 1 30  ? 17.875 101.093 27.652 1.00 99.79  ? 54  ASP A OD1 1 
ATOM   139  O OD2 . ASP A 1 30  ? 17.000 99.079  27.627 1.00 100.48 ? 54  ASP A OD2 1 
ATOM   140  N N   . PRO A 1 31  ? 13.923 99.647  30.681 1.00 171.49 ? 55  PRO A N   1 
ATOM   141  C CA  . PRO A 1 31  ? 12.493 99.711  30.323 1.00 176.14 ? 55  PRO A CA  1 
ATOM   142  C C   . PRO A 1 31  ? 12.216 100.438 28.995 1.00 185.65 ? 55  PRO A C   1 
ATOM   143  O O   . PRO A 1 31  ? 11.052 100.605 28.612 1.00 194.36 ? 55  PRO A O   1 
ATOM   144  C CB  . PRO A 1 31  ? 11.863 100.461 31.502 1.00 100.13 ? 55  PRO A CB  1 
ATOM   145  C CG  . PRO A 1 31  ? 12.768 100.152 32.652 1.00 81.40  ? 55  PRO A CG  1 
ATOM   146  C CD  . PRO A 1 31  ? 14.157 100.140 32.055 1.00 99.63  ? 55  PRO A CD  1 
ATOM   147  N N   . ARG A 1 32  ? 13.286 100.849 28.306 1.00 143.46 ? 56  ARG A N   1 
ATOM   148  C CA  . ARG A 1 32  ? 13.205 101.591 27.042 1.00 126.42 ? 56  ARG A CA  1 
ATOM   149  C C   . ARG A 1 32  ? 12.638 100.744 25.895 1.00 124.23 ? 56  ARG A C   1 
ATOM   150  O O   . ARG A 1 32  ? 11.437 100.444 25.892 1.00 120.52 ? 56  ARG A O   1 
ATOM   151  C CB  . ARG A 1 32  ? 14.593 102.144 26.685 1.00 123.27 ? 56  ARG A CB  1 
ATOM   152  C CG  . ARG A 1 32  ? 14.569 103.347 25.758 1.00 113.35 ? 56  ARG A CG  1 
ATOM   153  C CD  . ARG A 1 32  ? 15.975 103.779 25.388 1.00 109.75 ? 56  ARG A CD  1 
ATOM   154  N NE  . ARG A 1 32  ? 16.647 104.476 26.482 1.00 108.93 ? 56  ARG A NE  1 
ATOM   155  C CZ  . ARG A 1 32  ? 17.909 104.903 26.445 1.00 109.11 ? 56  ARG A CZ  1 
ATOM   156  N NH1 . ARG A 1 32  ? 18.660 104.707 25.364 1.00 109.46 ? 56  ARG A NH1 1 
ATOM   157  N NH2 . ARG A 1 32  ? 18.422 105.535 27.493 1.00 109.25 ? 56  ARG A NH2 1 
ATOM   158  N N   . ASP A 1 33  ? 13.475 100.366 24.922 1.00 135.15 ? 57  ASP A N   1 
ATOM   159  C CA  . ASP A 1 33  ? 12.989 99.537  23.809 1.00 145.01 ? 57  ASP A CA  1 
ATOM   160  C C   . ASP A 1 33  ? 12.635 98.153  24.349 1.00 144.18 ? 57  ASP A C   1 
ATOM   161  O O   . ASP A 1 33  ? 13.435 97.505  25.029 1.00 147.03 ? 57  ASP A O   1 
ATOM   162  C CB  . ASP A 1 33  ? 14.008 99.437  22.670 1.00 168.61 ? 57  ASP A CB  1 
ATOM   163  C CG  . ASP A 1 33  ? 13.427 98.754  21.421 1.00 171.22 ? 57  ASP A CG  1 
ATOM   164  O OD1 . ASP A 1 33  ? 14.211 98.417  20.507 1.00 171.74 ? 57  ASP A OD1 1 
ATOM   165  O OD2 . ASP A 1 33  ? 12.191 98.552  21.349 1.00 171.63 ? 57  ASP A OD2 1 
ATOM   166  N N   . ASN A 1 34  ? 11.415 97.724  24.026 1.00 165.76 ? 58  ASN A N   1 
ATOM   167  C CA  . ASN A 1 34  ? 10.834 96.486  24.535 1.00 159.82 ? 58  ASN A CA  1 
ATOM   168  C C   . ASN A 1 34  ? 11.721 95.251  24.412 1.00 153.96 ? 58  ASN A C   1 
ATOM   169  O O   . ASN A 1 34  ? 12.486 95.105  23.451 1.00 158.87 ? 58  ASN A O   1 
ATOM   170  C CB  . ASN A 1 34  ? 9.453  96.264  23.908 1.00 139.94 ? 58  ASN A CB  1 
ATOM   171  C CG  . ASN A 1 34  ? 8.491  97.431  24.159 1.00 135.85 ? 58  ASN A CG  1 
ATOM   172  O OD1 . ASN A 1 34  ? 8.110  97.713  25.297 1.00 133.15 ? 58  ASN A OD1 1 
ATOM   173  N ND2 . ASN A 1 34  ? 8.094  98.107  23.085 1.00 132.87 ? 58  ASN A ND2 1 
ATOM   174  N N   . ILE A 1 35  ? 11.586 94.367  25.402 1.00 110.25 ? 59  ILE A N   1 
ATOM   175  C CA  . ILE A 1 35  ? 12.407 93.165  25.560 1.00 98.69  ? 59  ILE A CA  1 
ATOM   176  C C   . ILE A 1 35  ? 12.456 92.231  24.358 1.00 99.47  ? 59  ILE A C   1 
ATOM   177  O O   . ILE A 1 35  ? 11.504 92.148  23.592 1.00 91.88  ? 59  ILE A O   1 
ATOM   178  C CB  . ILE A 1 35  ? 11.932 92.381  26.829 1.00 85.42  ? 59  ILE A CB  1 
ATOM   179  C CG1 . ILE A 1 35  ? 11.982 93.290  28.071 1.00 78.14  ? 59  ILE A CG1 1 
ATOM   180  C CG2 . ILE A 1 35  ? 12.781 91.138  27.048 1.00 79.26  ? 59  ILE A CG2 1 
ATOM   181  C CD1 . ILE A 1 35  ? 11.089 94.502  28.090 1.00 74.01  ? 59  ILE A CD1 1 
ATOM   182  N N   . LEU A 1 36  ? 13.585 91.548  24.185 1.00 102.73 ? 60  LEU A N   1 
ATOM   183  C CA  . LEU A 1 36  ? 13.733 90.575  23.107 1.00 104.57 ? 60  LEU A CA  1 
ATOM   184  C C   . LEU A 1 36  ? 14.454 89.293  23.580 1.00 105.89 ? 60  LEU A C   1 
ATOM   185  O O   . LEU A 1 36  ? 15.653 89.115  23.347 1.00 112.51 ? 60  LEU A O   1 
ATOM   186  C CB  . LEU A 1 36  ? 14.474 91.185  21.911 1.00 109.52 ? 60  LEU A CB  1 
ATOM   187  C CG  . LEU A 1 36  ? 14.233 90.523  20.542 1.00 106.76 ? 60  LEU A CG  1 
ATOM   188  C CD1 . LEU A 1 36  ? 12.959 91.085  19.910 1.00 105.41 ? 60  LEU A CD1 1 
ATOM   189  C CD2 . LEU A 1 36  ? 15.427 90.762  19.619 1.00 105.42 ? 60  LEU A CD2 1 
ATOM   190  N N   . ILE A 1 37  ? 13.710 88.414  24.259 1.00 87.91  ? 61  ILE A N   1 
ATOM   191  C CA  . ILE A 1 37  ? 14.237 87.126  24.732 1.00 72.83  ? 61  ILE A CA  1 
ATOM   192  C C   . ILE A 1 37  ? 14.461 86.252  23.498 1.00 72.81  ? 61  ILE A C   1 
ATOM   193  O O   . ILE A 1 37  ? 13.527 85.667  22.959 1.00 74.54  ? 61  ILE A O   1 
ATOM   194  C CB  . ILE A 1 37  ? 13.235 86.393  25.657 1.00 65.09  ? 61  ILE A CB  1 
ATOM   195  C CG1 . ILE A 1 37  ? 12.489 87.382  26.571 1.00 56.27  ? 61  ILE A CG1 1 
ATOM   196  C CG2 . ILE A 1 37  ? 13.981 85.321  26.446 1.00 56.81  ? 61  ILE A CG2 1 
ATOM   197  C CD1 . ILE A 1 37  ? 13.320 88.049  27.677 1.00 60.69  ? 61  ILE A CD1 1 
ATOM   198  N N   . GLU A 1 38  ? 15.708 86.151  23.070 1.00 74.14  ? 62  GLU A N   1 
ATOM   199  C CA  . GLU A 1 38  ? 16.034 85.429  21.852 1.00 74.54  ? 62  GLU A CA  1 
ATOM   200  C C   . GLU A 1 38  ? 16.213 83.938  22.032 1.00 70.18  ? 62  GLU A C   1 
ATOM   201  O O   . GLU A 1 38  ? 16.628 83.487  23.087 1.00 64.24  ? 62  GLU A O   1 
ATOM   202  C CB  . GLU A 1 38  ? 17.308 86.043  21.223 1.00 100.49 ? 62  GLU A CB  1 
ATOM   203  C CG  . GLU A 1 38  ? 17.093 87.450  20.641 1.00 117.78 ? 62  GLU A CG  1 
ATOM   204  C CD  . GLU A 1 38  ? 18.384 88.228  20.401 1.00 125.17 ? 62  GLU A CD  1 
ATOM   205  O OE1 . GLU A 1 38  ? 19.381 87.632  19.927 1.00 126.95 ? 62  GLU A OE1 1 
ATOM   206  O OE2 . GLU A 1 38  ? 18.391 89.449  20.676 1.00 127.12 ? 62  GLU A OE2 1 
ATOM   207  N N   . CYS A 1 39  ? 15.839 83.184  21.001 1.00 74.66  ? 63  CYS A N   1 
ATOM   208  C CA  . CYS A 1 39  ? 16.044 81.737  20.931 1.00 74.99  ? 63  CYS A CA  1 
ATOM   209  C C   . CYS A 1 39  ? 15.783 81.251  19.510 1.00 77.03  ? 63  CYS A C   1 
ATOM   210  O O   . CYS A 1 39  ? 14.666 81.362  19.004 1.00 79.76  ? 63  CYS A O   1 
ATOM   211  C CB  . CYS A 1 39  ? 15.151 80.960  21.894 1.00 67.14  ? 63  CYS A CB  1 
ATOM   212  S SG  . CYS A 1 39  ? 15.410 79.157  21.799 1.00 67.47  ? 63  CYS A SG  1 
ATOM   213  N N   . GLU A 1 40  ? 16.825 80.723  18.870 1.00 75.83  ? 64  GLU A N   1 
ATOM   214  C CA  . GLU A 1 40  ? 16.731 80.213  17.507 1.00 76.50  ? 64  GLU A CA  1 
ATOM   215  C C   . GLU A 1 40  ? 17.374 78.840  17.439 1.00 75.32  ? 64  GLU A C   1 
ATOM   216  O O   . GLU A 1 40  ? 18.199 78.501  18.285 1.00 74.93  ? 64  GLU A O   1 
ATOM   217  C CB  . GLU A 1 40  ? 17.416 81.177  16.525 1.00 89.15  ? 64  GLU A CB  1 
ATOM   218  C CG  . GLU A 1 40  ? 16.678 82.506  16.355 1.00 93.96  ? 64  GLU A CG  1 
ATOM   219  C CD  . GLU A 1 40  ? 17.488 83.560  15.610 1.00 95.87  ? 64  GLU A CD  1 
ATOM   220  O OE1 . GLU A 1 40  ? 18.477 83.194  14.936 1.00 96.23  ? 64  GLU A OE1 1 
ATOM   221  O OE2 . GLU A 1 40  ? 17.124 84.757  15.697 1.00 94.97  ? 64  GLU A OE2 1 
ATOM   222  N N   . ALA A 1 41  ? 16.999 78.054  16.434 1.00 79.56  ? 65  ALA A N   1 
ATOM   223  C CA  . ALA A 1 41  ? 17.529 76.705  16.283 1.00 79.35  ? 65  ALA A CA  1 
ATOM   224  C C   . ALA A 1 41  ? 17.477 76.171  14.859 1.00 79.98  ? 65  ALA A C   1 
ATOM   225  O O   . ALA A 1 41  ? 16.671 76.620  14.043 1.00 85.62  ? 65  ALA A O   1 
ATOM   226  C CB  . ALA A 1 41  ? 16.752 75.736  17.205 1.00 65.55  ? 65  ALA A CB  1 
ATOM   227  N N   . LYS A 1 42  ? 18.367 75.224  14.574 1.00 93.90  ? 66  LYS A N   1 
ATOM   228  C CA  . LYS A 1 42  ? 18.384 74.511  13.297 1.00 99.71  ? 66  LYS A CA  1 
ATOM   229  C C   . LYS A 1 42  ? 17.472 73.272  13.452 1.00 99.64  ? 66  LYS A C   1 
ATOM   230  O O   . LYS A 1 42  ? 16.681 73.196  14.394 1.00 97.72  ? 66  LYS A O   1 
ATOM   231  C CB  . LYS A 1 42  ? 19.801 74.053  12.939 1.00 98.04  ? 66  LYS A CB  1 
ATOM   232  C CG  . LYS A 1 42  ? 20.806 75.180  12.713 1.00 105.10 ? 66  LYS A CG  1 
ATOM   233  C CD  . LYS A 1 42  ? 22.220 74.607  12.643 1.00 108.23 ? 66  LYS A CD  1 
ATOM   234  C CE  . LYS A 1 42  ? 23.235 75.609  12.113 1.00 108.24 ? 66  LYS A CE  1 
ATOM   235  N NZ  . LYS A 1 42  ? 24.572 74.972  11.934 1.00 107.93 ? 66  LYS A NZ  1 
ATOM   236  N N   . GLY A 1 43  ? 17.597 72.314  12.529 1.00 107.48 ? 67  GLY A N   1 
ATOM   237  C CA  . GLY A 1 43  ? 16.785 71.099  12.547 1.00 118.42 ? 67  GLY A CA  1 
ATOM   238  C C   . GLY A 1 43  ? 16.260 70.744  11.158 1.00 126.37 ? 67  GLY A C   1 
ATOM   239  O O   . GLY A 1 43  ? 15.961 71.651  10.369 1.00 123.95 ? 67  GLY A O   1 
ATOM   240  N N   . ASN A 1 44  ? 16.152 69.437  10.851 1.00 130.52 ? 68  ASN A N   1 
ATOM   241  C CA  . ASN A 1 44  ? 15.669 68.967  9.519  1.00 131.30 ? 68  ASN A CA  1 
ATOM   242  C C   . ASN A 1 44  ? 14.253 69.527  9.375  1.00 125.50 ? 68  ASN A C   1 
ATOM   243  O O   . ASN A 1 44  ? 13.975 70.244  8.392  1.00 134.69 ? 68  ASN A O   1 
ATOM   244  C CB  . ASN A 1 44  ? 15.779 67.456  9.398  1.00 115.76 ? 68  ASN A CB  1 
ATOM   245  C CG  . ASN A 1 44  ? 15.650 66.992  7.951  1.00 113.95 ? 68  ASN A CG  1 
ATOM   246  O OD1 . ASN A 1 44  ? 15.458 65.810  7.691  1.00 112.65 ? 68  ASN A OD1 1 
ATOM   247  N ND2 . ASN A 1 44  ? 15.759 67.931  7.000  1.00 113.11 ? 68  ASN A ND2 1 
ATOM   248  N N   . PRO A 1 45  ? 13.315 69.085  10.249 1.00 106.45 ? 69  PRO A N   1 
ATOM   249  C CA  . PRO A 1 45  ? 12.005 69.731  10.130 1.00 98.79  ? 69  PRO A CA  1 
ATOM   250  C C   . PRO A 1 45  ? 12.222 71.024  11.010 1.00 99.44  ? 69  PRO A C   1 
ATOM   251  O O   . PRO A 1 45  ? 12.877 70.978  12.069 1.00 95.51  ? 69  PRO A O   1 
ATOM   252  C CB  . PRO A 1 45  ? 11.052 68.803  10.876 1.00 78.99  ? 69  PRO A CB  1 
ATOM   253  C CG  . PRO A 1 45  ? 11.736 67.465  10.877 1.00 76.55  ? 69  PRO A CG  1 
ATOM   254  C CD  . PRO A 1 45  ? 13.201 67.790  10.965 1.00 81.84  ? 69  PRO A CD  1 
ATOM   255  N N   . ALA A 1 46  ? 11.685 72.159  10.559 1.00 129.26 ? 70  ALA A N   1 
ATOM   256  C CA  . ALA A 1 46  ? 11.756 73.426  11.309 1.00 139.19 ? 70  ALA A CA  1 
ATOM   257  C C   . ALA A 1 46  ? 11.146 73.163  12.694 1.00 144.18 ? 70  ALA A C   1 
ATOM   258  O O   . ALA A 1 46  ? 9.974  72.780  12.819 1.00 152.17 ? 70  ALA A O   1 
ATOM   259  C CB  . ALA A 1 46  ? 11.009 74.523  10.564 1.00 113.57 ? 70  ALA A CB  1 
ATOM   260  N N   . PRO A 1 47  ? 11.938 73.402  13.753 1.00 110.86 ? 71  PRO A N   1 
ATOM   261  C CA  . PRO A 1 47  ? 11.483 73.157  15.121 1.00 108.41 ? 71  PRO A CA  1 
ATOM   262  C C   . PRO A 1 47  ? 10.398 74.055  15.647 1.00 103.42 ? 71  PRO A C   1 
ATOM   263  O O   . PRO A 1 47  ? 10.302 75.201  15.225 1.00 98.69  ? 71  PRO A O   1 
ATOM   264  C CB  . PRO A 1 47  ? 12.774 73.277  15.939 1.00 109.21 ? 71  PRO A CB  1 
ATOM   265  C CG  . PRO A 1 47  ? 13.561 74.306  15.206 1.00 111.32 ? 71  PRO A CG  1 
ATOM   266  C CD  . PRO A 1 47  ? 13.221 74.141  13.739 1.00 114.44 ? 71  PRO A CD  1 
ATOM   267  N N   . SER A 1 48  ? 9.577  73.522  16.556 1.00 91.76  ? 72  SER A N   1 
ATOM   268  C CA  . SER A 1 48  ? 8.533  74.313  17.216 1.00 87.18  ? 72  SER A CA  1 
ATOM   269  C C   . SER A 1 48  ? 9.052  74.689  18.607 1.00 81.58  ? 72  SER A C   1 
ATOM   270  O O   . SER A 1 48  ? 9.804  73.933  19.226 1.00 80.57  ? 72  SER A O   1 
ATOM   271  C CB  . SER A 1 48  ? 7.219  73.540  17.309 1.00 106.40 ? 72  SER A CB  1 
ATOM   272  O OG  . SER A 1 48  ? 7.345  72.368  18.095 1.00 109.65 ? 72  SER A OG  1 
ATOM   273  N N   . PHE A 1 49  ? 8.626  75.845  19.092 1.00 80.08  ? 73  PHE A N   1 
ATOM   274  C CA  . PHE A 1 49  ? 9.142  76.390  20.338 1.00 73.55  ? 73  PHE A CA  1 
ATOM   275  C C   . PHE A 1 49  ? 8.112  76.662  21.411 1.00 69.94  ? 73  PHE A C   1 
ATOM   276  O O   . PHE A 1 49  ? 6.973  77.017  21.114 1.00 66.76  ? 73  PHE A O   1 
ATOM   277  C CB  . PHE A 1 49  ? 9.850  77.738  20.051 1.00 81.58  ? 73  PHE A CB  1 
ATOM   278  C CG  . PHE A 1 49  ? 10.965 77.654  19.046 1.00 88.17  ? 73  PHE A CG  1 
ATOM   279  C CD1 . PHE A 1 49  ? 10.697 77.651  17.677 1.00 91.66  ? 73  PHE A CD1 1 
ATOM   280  C CD2 . PHE A 1 49  ? 12.288 77.585  19.474 1.00 91.52  ? 73  PHE A CD2 1 
ATOM   281  C CE1 . PHE A 1 49  ? 11.733 77.574  16.745 1.00 93.38  ? 73  PHE A CE1 1 
ATOM   282  C CE2 . PHE A 1 49  ? 13.336 77.506  18.555 1.00 93.23  ? 73  PHE A CE2 1 
ATOM   283  C CZ  . PHE A 1 49  ? 13.058 77.504  17.186 1.00 93.78  ? 73  PHE A CZ  1 
ATOM   284  N N   . HIS A 1 50  ? 8.523  76.456  22.660 1.00 61.41  ? 74  HIS A N   1 
ATOM   285  C CA  . HIS A 1 50  ? 7.720  76.850  23.809 1.00 58.68  ? 74  HIS A CA  1 
ATOM   286  C C   . HIS A 1 50  ? 8.665  77.273  24.941 1.00 57.63  ? 74  HIS A C   1 
ATOM   287  O O   . HIS A 1 50  ? 9.860  76.969  24.918 1.00 52.95  ? 74  HIS A O   1 
ATOM   288  C CB  . HIS A 1 50  ? 6.729  75.788  24.252 1.00 69.28  ? 74  HIS A CB  1 
ATOM   289  C CG  . HIS A 1 50  ? 7.356  74.575  24.845 1.00 74.59  ? 74  HIS A CG  1 
ATOM   290  N ND1 . HIS A 1 50  ? 7.719  73.480  24.090 1.00 77.60  ? 74  HIS A ND1 1 
ATOM   291  C CD2 . HIS A 1 50  ? 7.670  74.275  26.127 1.00 76.19  ? 74  HIS A CD2 1 
ATOM   292  C CE1 . HIS A 1 50  ? 8.229  72.555  24.884 1.00 78.33  ? 74  HIS A CE1 1 
ATOM   293  N NE2 . HIS A 1 50  ? 8.211  73.013  26.125 1.00 77.07  ? 74  HIS A NE2 1 
ATOM   294  N N   . TRP A 1 51  ? 8.111  77.959  25.930 1.00 59.31  ? 75  TRP A N   1 
ATOM   295  C CA  . TRP A 1 51  ? 8.896  78.540  26.993 1.00 59.71  ? 75  TRP A CA  1 
ATOM   296  C C   . TRP A 1 51  ? 8.401  78.248  28.382 1.00 57.81  ? 75  TRP A C   1 
ATOM   297  O O   . TRP A 1 51  ? 7.229  77.935  28.571 1.00 57.43  ? 75  TRP A O   1 
ATOM   298  C CB  . TRP A 1 51  ? 8.880  80.070  26.816 1.00 69.69  ? 75  TRP A CB  1 
ATOM   299  C CG  . TRP A 1 51  ? 9.726  80.546  25.706 1.00 76.40  ? 75  TRP A CG  1 
ATOM   300  C CD1 . TRP A 1 51  ? 9.418  80.548  24.382 1.00 78.68  ? 75  TRP A CD1 1 
ATOM   301  C CD2 . TRP A 1 51  ? 11.049 81.069  25.815 1.00 79.73  ? 75  TRP A CD2 1 
ATOM   302  N NE1 . TRP A 1 51  ? 10.467 81.041  23.653 1.00 79.96  ? 75  TRP A NE1 1 
ATOM   303  C CE2 . TRP A 1 51  ? 11.485 81.368  24.507 1.00 80.97  ? 75  TRP A CE2 1 
ATOM   304  C CE3 . TRP A 1 51  ? 11.913 81.312  26.891 1.00 80.53  ? 75  TRP A CE3 1 
ATOM   305  C CZ2 . TRP A 1 51  ? 12.752 81.906  24.242 1.00 80.67  ? 75  TRP A CZ2 1 
ATOM   306  C CZ3 . TRP A 1 51  ? 13.168 81.846  26.627 1.00 81.17  ? 75  TRP A CZ3 1 
ATOM   307  C CH2 . TRP A 1 51  ? 13.575 82.136  25.311 1.00 81.02  ? 75  TRP A CH2 1 
ATOM   308  N N   . THR A 1 52  ? 9.318  78.315  29.343 1.00 55.90  ? 76  THR A N   1 
ATOM   309  C CA  . THR A 1 52  ? 8.929  78.246  30.737 1.00 58.27  ? 76  THR A CA  1 
ATOM   310  C C   . THR A 1 52  ? 9.319  79.569  31.388 1.00 61.45  ? 76  THR A C   1 
ATOM   311  O O   . THR A 1 52  ? 10.317 80.197  31.012 1.00 60.35  ? 76  THR A O   1 
ATOM   312  C CB  . THR A 1 52  ? 9.624  77.121  31.559 1.00 61.95  ? 76  THR A CB  1 
ATOM   313  O OG1 . THR A 1 52  ? 11.040 77.343  31.613 1.00 61.76  ? 76  THR A OG1 1 
ATOM   314  C CG2 . THR A 1 52  ? 9.313  75.766  30.963 1.00 59.77  ? 76  THR A CG2 1 
ATOM   315  N N   . ARG A 1 53  ? 8.493  80.004  32.335 1.00 57.00  ? 77  ARG A N   1 
ATOM   316  C CA  . ARG A 1 53  ? 8.804  81.185  33.131 1.00 58.80  ? 77  ARG A CA  1 
ATOM   317  C C   . ARG A 1 53  ? 8.721  80.679  34.572 1.00 57.77  ? 77  ARG A C   1 
ATOM   318  O O   . ARG A 1 53  ? 7.680  80.208  35.011 1.00 53.63  ? 77  ARG A O   1 
ATOM   319  C CB  . ARG A 1 53  ? 7.814  82.313  32.887 1.00 81.67  ? 77  ARG A CB  1 
ATOM   320  C CG  . ARG A 1 53  ? 8.327  83.678  33.330 1.00 95.85  ? 77  ARG A CG  1 
ATOM   321  C CD  . ARG A 1 53  ? 7.210  84.717  33.355 1.00 103.19 ? 77  ARG A CD  1 
ATOM   322  N NE  . ARG A 1 53  ? 6.137  84.353  34.284 1.00 106.67 ? 77  ARG A NE  1 
ATOM   323  C CZ  . ARG A 1 53  ? 5.990  84.847  35.512 1.00 107.36 ? 77  ARG A CZ  1 
ATOM   324  N NH1 . ARG A 1 53  ? 6.846  85.745  35.991 1.00 107.20 ? 77  ARG A NH1 1 
ATOM   325  N NH2 . ARG A 1 53  ? 4.973  84.442  36.263 1.00 108.03 ? 77  ARG A NH2 1 
ATOM   326  N N   . ASN A 1 54  ? 9.840  80.771  35.284 1.00 70.21  ? 78  ASN A N   1 
ATOM   327  C CA  . ASN A 1 54  ? 9.961  80.267  36.647 1.00 73.54  ? 78  ASN A CA  1 
ATOM   328  C C   . ASN A 1 54  ? 9.451  78.824  36.801 1.00 74.16  ? 78  ASN A C   1 
ATOM   329  O O   . ASN A 1 54  ? 8.648  78.527  37.690 1.00 75.00  ? 78  ASN A O   1 
ATOM   330  C CB  . ASN A 1 54  ? 9.287  81.207  37.655 1.00 76.90  ? 78  ASN A CB  1 
ATOM   331  C CG  . ASN A 1 54  ? 9.890  82.604  37.632 1.00 79.51  ? 78  ASN A CG  1 
ATOM   332  O OD1 . ASN A 1 54  ? 9.270  83.548  37.140 1.00 80.28  ? 78  ASN A OD1 1 
ATOM   333  N ND2 . ASN A 1 54  ? 11.112 82.738  38.148 1.00 79.62  ? 78  ASN A ND2 1 
ATOM   334  N N   . SER A 1 55  ? 9.931  77.948  35.907 1.00 66.86  ? 79  SER A N   1 
ATOM   335  C CA  . SER A 1 55  ? 9.622  76.502  35.916 1.00 66.70  ? 79  SER A CA  1 
ATOM   336  C C   . SER A 1 55  ? 8.223  76.044  35.561 1.00 66.65  ? 79  SER A C   1 
ATOM   337  O O   . SER A 1 55  ? 7.942  74.842  35.621 1.00 62.92  ? 79  SER A O   1 
ATOM   338  C CB  . SER A 1 55  ? 9.838  75.886  37.293 1.00 76.33  ? 79  SER A CB  1 
ATOM   339  O OG  . SER A 1 55  ? 11.202 75.718  37.596 1.00 81.71  ? 79  SER A OG  1 
ATOM   340  N N   . ARG A 1 56  ? 7.326  76.971  35.259 1.00 70.51  ? 80  ARG A N   1 
ATOM   341  C CA  . ARG A 1 56  ? 5.963  76.587  34.902 1.00 73.32  ? 80  ARG A CA  1 
ATOM   342  C C   . ARG A 1 56  ? 5.807  77.042  33.471 1.00 67.75  ? 80  ARG A C   1 
ATOM   343  O O   . ARG A 1 56  ? 6.468  77.986  33.042 1.00 62.39  ? 80  ARG A O   1 
ATOM   344  C CB  . ARG A 1 56  ? 4.859  77.209  35.790 1.00 111.37 ? 80  ARG A CB  1 
ATOM   345  C CG  . ARG A 1 56  ? 4.501  76.339  36.992 1.00 135.24 ? 80  ARG A CG  1 
ATOM   346  C CD  . ARG A 1 56  ? 3.330  76.906  37.786 1.00 147.06 ? 80  ARG A CD  1 
ATOM   347  N NE  . ARG A 1 56  ? 2.983  76.034  38.908 1.00 150.95 ? 80  ARG A NE  1 
ATOM   348  C CZ  . ARG A 1 56  ? 2.244  76.398  39.955 1.00 152.09 ? 80  ARG A CZ  1 
ATOM   349  N NH1 . ARG A 1 56  ? 1.758  77.634  40.046 1.00 152.13 ? 80  ARG A NH1 1 
ATOM   350  N NH2 . ARG A 1 56  ? 1.994  75.519  40.918 1.00 152.18 ? 80  ARG A NH2 1 
ATOM   351  N N   . PHE A 1 57  ? 4.959  76.336  32.727 1.00 71.89  ? 81  PHE A N   1 
ATOM   352  C CA  . PHE A 1 57  ? 4.702  76.634  31.320 1.00 71.12  ? 81  PHE A CA  1 
ATOM   353  C C   . PHE A 1 57  ? 4.275  78.087  31.131 1.00 69.63  ? 81  PHE A C   1 
ATOM   354  O O   . PHE A 1 57  ? 3.319  78.563  31.760 1.00 69.74  ? 81  PHE A O   1 
ATOM   355  C CB  . PHE A 1 57  ? 3.632  75.679  30.763 1.00 73.64  ? 81  PHE A CB  1 
ATOM   356  C CG  . PHE A 1 57  ? 3.190  76.007  29.357 1.00 76.32  ? 81  PHE A CG  1 
ATOM   357  C CD1 . PHE A 1 57  ? 4.074  75.898  28.282 1.00 77.70  ? 81  PHE A CD1 1 
ATOM   358  C CD2 . PHE A 1 57  ? 1.886  76.427  29.108 1.00 77.48  ? 81  PHE A CD2 1 
ATOM   359  C CE1 . PHE A 1 57  ? 3.666  76.207  26.982 1.00 77.41  ? 81  PHE A CE1 1 
ATOM   360  C CE2 . PHE A 1 57  ? 1.471  76.740  27.809 1.00 76.96  ? 81  PHE A CE2 1 
ATOM   361  C CZ  . PHE A 1 57  ? 2.360  76.628  26.748 1.00 76.31  ? 81  PHE A CZ  1 
ATOM   362  N N   . PHE A 1 58  ? 5.003  78.790  30.270 1.00 63.53  ? 82  PHE A N   1 
ATOM   363  C CA  . PHE A 1 58  ? 4.724  80.195  30.007 1.00 70.91  ? 82  PHE A CA  1 
ATOM   364  C C   . PHE A 1 58  ? 3.728  80.314  28.855 1.00 78.01  ? 82  PHE A C   1 
ATOM   365  O O   . PHE A 1 58  ? 4.080  80.158  27.678 1.00 68.91  ? 82  PHE A O   1 
ATOM   366  C CB  . PHE A 1 58  ? 6.026  80.953  29.703 1.00 78.43  ? 82  PHE A CB  1 
ATOM   367  C CG  . PHE A 1 58  ? 5.854  82.447  29.603 1.00 81.91  ? 82  PHE A CG  1 
ATOM   368  C CD1 . PHE A 1 58  ? 6.406  83.148  28.532 1.00 83.80  ? 82  PHE A CD1 1 
ATOM   369  C CD2 . PHE A 1 58  ? 5.147  83.156  30.575 1.00 82.88  ? 82  PHE A CD2 1 
ATOM   370  C CE1 . PHE A 1 58  ? 6.257  84.532  28.426 1.00 82.73  ? 82  PHE A CE1 1 
ATOM   371  C CE2 . PHE A 1 58  ? 4.995  84.537  30.475 1.00 82.64  ? 82  PHE A CE2 1 
ATOM   372  C CZ  . PHE A 1 58  ? 5.553  85.223  29.398 1.00 82.05  ? 82  PHE A CZ  1 
ATOM   373  N N   . ASN A 1 59  ? 2.476  80.593  29.225 1.00 101.62 ? 83  ASN A N   1 
ATOM   374  C CA  . ASN A 1 59  ? 1.363  80.695  28.280 1.00 111.37 ? 83  ASN A CA  1 
ATOM   375  C C   . ASN A 1 59  ? 1.401  82.003  27.481 1.00 115.72 ? 83  ASN A C   1 
ATOM   376  O O   . ASN A 1 59  ? 1.016  83.061  27.991 1.00 128.19 ? 83  ASN A O   1 
ATOM   377  C CB  . ASN A 1 59  ? 0.041  80.582  29.052 1.00 102.65 ? 83  ASN A CB  1 
ATOM   378  C CG  . ASN A 1 59  ? -1.017 79.792  28.299 1.00 94.66  ? 83  ASN A CG  1 
ATOM   379  O OD1 . ASN A 1 59  ? -1.035 79.763  27.064 1.00 89.84  ? 83  ASN A OD1 1 
ATOM   380  N ND2 . ASN A 1 59  ? -1.916 79.157  29.047 1.00 90.68  ? 83  ASN A ND2 1 
ATOM   381  N N   . ILE A 1 60  ? 1.870  81.921  26.231 1.00 110.79 ? 84  ILE A N   1 
ATOM   382  C CA  . ILE A 1 60  ? 1.991  83.102  25.357 1.00 105.47 ? 84  ILE A CA  1 
ATOM   383  C C   . ILE A 1 60  ? 0.596  83.650  25.067 1.00 101.71 ? 84  ILE A C   1 
ATOM   384  O O   . ILE A 1 60  ? 0.326  84.828  25.312 1.00 95.28  ? 84  ILE A O   1 
ATOM   385  C CB  . ILE A 1 60  ? 2.738  82.773  24.036 1.00 99.17  ? 84  ILE A CB  1 
ATOM   386  C CG1 . ILE A 1 60  ? 4.138  82.202  24.334 1.00 103.60 ? 84  ILE A CG1 1 
ATOM   387  C CG2 . ILE A 1 60  ? 2.822  84.025  23.156 1.00 105.44 ? 84  ILE A CG2 1 
ATOM   388  C CD1 . ILE A 1 60  ? 5.120  83.115  25.109 1.00 101.61 ? 84  ILE A CD1 1 
ATOM   389  N N   . ALA A 1 61  ? -0.276 82.796  24.535 1.00 108.46 ? 85  ALA A N   1 
ATOM   390  C CA  . ALA A 1 61  ? -1.665 83.186  24.310 1.00 116.87 ? 85  ALA A CA  1 
ATOM   391  C C   . ALA A 1 61  ? -2.619 84.048  25.190 1.00 120.33 ? 85  ALA A C   1 
ATOM   392  O O   . ALA A 1 61  ? -3.449 84.762  24.618 1.00 131.97 ? 85  ALA A O   1 
ATOM   393  C CB  . ALA A 1 61  ? -2.420 81.985  23.711 1.00 105.33 ? 85  ALA A CB  1 
ATOM   394  N N   . LYS A 1 62  ? -2.433 84.080  26.492 1.00 102.49 ? 86  LYS A N   1 
ATOM   395  C CA  . LYS A 1 62  ? -3.279 84.751  27.455 1.00 93.11  ? 86  LYS A CA  1 
ATOM   396  C C   . LYS A 1 62  ? -2.516 86.043  27.850 1.00 91.56  ? 86  LYS A C   1 
ATOM   397  O O   . LYS A 1 62  ? -2.986 86.864  28.647 1.00 94.79  ? 86  LYS A O   1 
ATOM   398  C CB  . LYS A 1 62  ? -3.347 83.645  28.488 1.00 94.24  ? 86  LYS A CB  1 
ATOM   399  C CG  . LYS A 1 62  ? -4.624 82.809  28.447 1.00 86.25  ? 86  LYS A CG  1 
ATOM   400  C CD  . LYS A 1 62  ? -4.522 81.563  29.317 1.00 81.67  ? 86  LYS A CD  1 
ATOM   401  C CE  . LYS A 1 62  ? -5.827 80.773  29.295 1.00 81.39  ? 86  LYS A CE  1 
ATOM   402  N NZ  . LYS A 1 62  ? -5.774 79.528  30.115 1.00 81.58  ? 86  LYS A NZ  1 
ATOM   403  N N   . ASP A 1 63  ? -1.315 86.182  27.278 1.00 105.70 ? 87  ASP A N   1 
ATOM   404  C CA  . ASP A 1 63  ? -0.492 87.389  27.440 1.00 103.35 ? 87  ASP A CA  1 
ATOM   405  C C   . ASP A 1 63  ? -0.498 88.215  26.126 1.00 98.25  ? 87  ASP A C   1 
ATOM   406  O O   . ASP A 1 63  ? -0.063 87.737  25.070 1.00 94.61  ? 87  ASP A O   1 
ATOM   407  C CB  . ASP A 1 63  ? 0.917  86.984  27.827 1.00 115.85 ? 87  ASP A CB  1 
ATOM   408  C CG  . ASP A 1 63  ? 1.753  88.154  28.318 1.00 124.80 ? 87  ASP A CG  1 
ATOM   409  O OD1 . ASP A 1 63  ? 1.818  89.188  27.614 1.00 128.67 ? 87  ASP A OD1 1 
ATOM   410  O OD2 . ASP A 1 63  ? 2.360  88.033  29.404 1.00 128.14 ? 87  ASP A OD2 1 
ATOM   411  N N   . PRO A 1 64  ? -0.973 89.475  26.198 1.00 101.23 ? 88  PRO A N   1 
ATOM   412  C CA  . PRO A 1 64  ? -1.057 90.364  25.033 1.00 103.38 ? 88  PRO A CA  1 
ATOM   413  C C   . PRO A 1 64  ? 0.248  90.954  24.570 1.00 107.51 ? 88  PRO A C   1 
ATOM   414  O O   . PRO A 1 64  ? 0.409  91.291  23.396 1.00 111.05 ? 88  PRO A O   1 
ATOM   415  C CB  . PRO A 1 64  ? -2.001 91.485  25.498 1.00 75.48  ? 88  PRO A CB  1 
ATOM   416  C CG  . PRO A 1 64  ? -2.396 91.140  26.925 1.00 71.63  ? 88  PRO A CG  1 
ATOM   417  C CD  . PRO A 1 64  ? -1.374 90.179  27.430 1.00 76.76  ? 88  PRO A CD  1 
ATOM   418  N N   . ARG A 1 65  ? 1.173  91.067  25.514 1.00 87.28  ? 89  ARG A N   1 
ATOM   419  C CA  . ARG A 1 65  ? 2.448  91.722  25.285 1.00 85.71  ? 89  ARG A CA  1 
ATOM   420  C C   . ARG A 1 65  ? 3.438  90.924  24.448 1.00 83.47  ? 89  ARG A C   1 
ATOM   421  O O   . ARG A 1 65  ? 4.086  91.465  23.543 1.00 76.87  ? 89  ARG A O   1 
ATOM   422  C CB  . ARG A 1 65  ? 3.086  92.058  26.650 1.00 98.74  ? 89  ARG A CB  1 
ATOM   423  C CG  . ARG A 1 65  ? 2.102  92.566  27.727 1.00 107.10 ? 89  ARG A CG  1 
ATOM   424  C CD  . ARG A 1 65  ? 2.029  94.096  27.772 1.00 111.34 ? 89  ARG A CD  1 
ATOM   425  N NE  . ARG A 1 65  ? 1.113  94.662  28.775 1.00 113.09 ? 89  ARG A NE  1 
ATOM   426  C CZ  . ARG A 1 65  ? 0.880  94.179  30.000 1.00 113.53 ? 89  ARG A CZ  1 
ATOM   427  N NH1 . ARG A 1 65  ? 1.482  93.078  30.436 1.00 113.70 ? 89  ARG A NH1 1 
ATOM   428  N NH2 . ARG A 1 65  ? 0.032  94.815  30.802 1.00 113.53 ? 89  ARG A NH2 1 
ATOM   429  N N   . VAL A 1 66  ? 3.512  89.624  24.727 1.00 78.58  ? 90  VAL A N   1 
ATOM   430  C CA  . VAL A 1 66  ? 4.508  88.757  24.103 1.00 78.63  ? 90  VAL A CA  1 
ATOM   431  C C   . VAL A 1 66  ? 4.041  88.079  22.825 1.00 76.45  ? 90  VAL A C   1 
ATOM   432  O O   . VAL A 1 66  ? 2.854  87.822  22.659 1.00 72.82  ? 90  VAL A O   1 
ATOM   433  C CB  . VAL A 1 66  ? 4.987  87.679  25.129 1.00 86.36  ? 90  VAL A CB  1 
ATOM   434  C CG1 . VAL A 1 66  ? 6.398  87.226  24.801 1.00 93.71  ? 90  VAL A CG1 1 
ATOM   435  C CG2 . VAL A 1 66  ? 4.935  88.232  26.547 1.00 93.36  ? 90  VAL A CG2 1 
ATOM   436  N N   . SER A 1 67  ? 4.985  87.804  21.926 1.00 81.43  ? 91  SER A N   1 
ATOM   437  C CA  . SER A 1 67  ? 4.694  87.160  20.644 1.00 83.44  ? 91  SER A CA  1 
ATOM   438  C C   . SER A 1 67  ? 5.923  86.446  20.070 1.00 82.75  ? 91  SER A C   1 
ATOM   439  O O   . SER A 1 67  ? 7.055  86.856  20.315 1.00 81.19  ? 91  SER A O   1 
ATOM   440  C CB  . SER A 1 67  ? 4.186  88.198  19.629 1.00 90.67  ? 91  SER A CB  1 
ATOM   441  O OG  . SER A 1 67  ? 5.176  89.172  19.334 1.00 95.81  ? 91  SER A OG  1 
ATOM   442  N N   . MET A 1 68  ? 5.693  85.379  19.305 1.00 84.40  ? 92  MET A N   1 
ATOM   443  C CA  . MET A 1 68  ? 6.780  84.621  18.700 1.00 84.10  ? 92  MET A CA  1 
ATOM   444  C C   . MET A 1 68  ? 7.178  85.187  17.340 1.00 84.73  ? 92  MET A C   1 
ATOM   445  O O   . MET A 1 68  ? 6.591  86.158  16.877 1.00 82.19  ? 92  MET A O   1 
ATOM   446  C CB  . MET A 1 68  ? 6.459  83.125  18.657 1.00 87.35  ? 92  MET A CB  1 
ATOM   447  C CG  . MET A 1 68  ? 7.661  82.243  18.988 1.00 93.31  ? 92  MET A CG  1 
ATOM   448  S SD  . MET A 1 68  ? 7.250  80.559  19.463 1.00 95.32  ? 92  MET A SD  1 
ATOM   449  C CE  . MET A 1 68  ? 7.253  79.728  17.867 1.00 96.50  ? 92  MET A CE  1 
ATOM   450  N N   . ARG A 1 69  ? 8.143  84.550  16.691 1.00 74.44  ? 93  ARG A N   1 
ATOM   451  C CA  . ARG A 1 69  ? 8.785  85.135  15.516 1.00 82.94  ? 93  ARG A CA  1 
ATOM   452  C C   . ARG A 1 69  ? 8.651  84.361  14.216 1.00 87.80  ? 93  ARG A C   1 
ATOM   453  O O   . ARG A 1 69  ? 8.012  83.312  14.169 1.00 80.38  ? 93  ARG A O   1 
ATOM   454  C CB  . ARG A 1 69  ? 10.296 85.284  15.865 1.00 111.05 ? 93  ARG A CB  1 
ATOM   455  C CG  . ARG A 1 69  ? 10.987 86.546  15.347 1.00 121.40 ? 93  ARG A CG  1 
ATOM   456  C CD  . ARG A 1 69  ? 11.083 87.635  16.418 1.00 126.37 ? 93  ARG A CD  1 
ATOM   457  N NE  . ARG A 1 69  ? 11.382 88.956  15.859 1.00 128.19 ? 93  ARG A NE  1 
ATOM   458  C CZ  . ARG A 1 69  ? 12.587 89.374  15.473 1.00 128.75 ? 93  ARG A CZ  1 
ATOM   459  N NH1 . ARG A 1 69  ? 13.649 88.581  15.579 1.00 128.56 ? 93  ARG A NH1 1 
ATOM   460  N NH2 . ARG A 1 69  ? 12.730 90.598  14.976 1.00 128.56 ? 93  ARG A NH2 1 
ATOM   461  N N   . ARG A 1 70  ? 9.241  84.916  13.158 1.00 129.30 ? 94  ARG A N   1 
ATOM   462  C CA  . ARG A 1 70  ? 9.302  84.259  11.862 1.00 142.04 ? 94  ARG A CA  1 
ATOM   463  C C   . ARG A 1 70  ? 10.153 82.990  12.009 1.00 148.97 ? 94  ARG A C   1 
ATOM   464  O O   . ARG A 1 70  ? 11.364 83.072  12.232 1.00 162.94 ? 94  ARG A O   1 
ATOM   465  C CB  . ARG A 1 70  ? 9.995  85.151  10.811 1.00 125.08 ? 94  ARG A CB  1 
ATOM   466  C CG  . ARG A 1 70  ? 9.437  86.559  10.635 1.00 115.31 ? 94  ARG A CG  1 
ATOM   467  C CD  . ARG A 1 70  ? 10.269 87.587  11.391 1.00 109.64 ? 94  ARG A CD  1 
ATOM   468  N NE  . ARG A 1 70  ? 9.692  87.923  12.691 1.00 107.45 ? 94  ARG A NE  1 
ATOM   469  C CZ  . ARG A 1 70  ? 8.875  88.951  12.913 1.00 107.18 ? 94  ARG A CZ  1 
ATOM   470  N NH1 . ARG A 1 70  ? 8.529  89.763  11.921 1.00 108.10 ? 94  ARG A NH1 1 
ATOM   471  N NH2 . ARG A 1 70  ? 8.404  89.171  14.133 1.00 106.77 ? 94  ARG A NH2 1 
ATOM   472  N N   . ARG A 1 71  ? 9.510  81.830  11.915 1.00 123.43 ? 95  ARG A N   1 
ATOM   473  C CA  . ARG A 1 71  ? 10.197 80.532  11.930 1.00 118.46 ? 95  ARG A CA  1 
ATOM   474  C C   . ARG A 1 71  ? 11.152 80.279  13.110 1.00 115.74 ? 95  ARG A C   1 
ATOM   475  O O   . ARG A 1 71  ? 11.994 79.373  13.050 1.00 111.31 ? 95  ARG A O   1 
ATOM   476  C CB  . ARG A 1 71  ? 10.972 80.352  10.603 1.00 148.93 ? 95  ARG A CB  1 
ATOM   477  C CG  . ARG A 1 71  ? 10.218 80.752  9.332  1.00 150.13 ? 95  ARG A CG  1 
ATOM   478  C CD  . ARG A 1 71  ? 11.192 81.237  8.256  1.00 151.31 ? 95  ARG A CD  1 
ATOM   479  N NE  . ARG A 1 71  ? 12.022 80.157  7.721  1.00 152.29 ? 95  ARG A NE  1 
ATOM   480  C CZ  . ARG A 1 71  ? 13.260 80.310  7.252  1.00 152.48 ? 95  ARG A CZ  1 
ATOM   481  N NH1 . ARG A 1 71  ? 13.839 81.506  7.248  1.00 152.31 ? 95  ARG A NH1 1 
ATOM   482  N NH2 . ARG A 1 71  ? 13.923 79.259  6.785  1.00 152.60 ? 95  ARG A NH2 1 
ATOM   483  N N   . SER A 1 72  ? 11.026 81.076  14.173 1.00 150.37 ? 96  SER A N   1 
ATOM   484  C CA  . SER A 1 72  ? 11.862 80.903  15.365 1.00 146.36 ? 96  SER A CA  1 
ATOM   485  C C   . SER A 1 72  ? 11.065 81.057  16.675 1.00 144.25 ? 96  SER A C   1 
ATOM   486  O O   . SER A 1 72  ? 9.862  81.344  16.655 1.00 158.14 ? 96  SER A O   1 
ATOM   487  C CB  . SER A 1 72  ? 13.052 81.879  15.346 1.00 105.18 ? 96  SER A CB  1 
ATOM   488  O OG  . SER A 1 72  ? 12.755 83.088  16.024 1.00 88.85  ? 96  SER A OG  1 
ATOM   489  N N   . GLY A 1 73  ? 11.752 80.848  17.803 1.00 99.43  ? 97  GLY A N   1 
ATOM   490  C CA  . GLY A 1 73  ? 11.143 80.941  19.122 1.00 80.18  ? 97  GLY A CA  1 
ATOM   491  C C   . GLY A 1 73  ? 11.491 82.215  19.862 1.00 74.41  ? 97  GLY A C   1 
ATOM   492  O O   . GLY A 1 73  ? 11.096 82.401  21.017 1.00 65.99  ? 97  GLY A O   1 
ATOM   493  N N   . THR A 1 74  ? 12.248 83.085  19.197 1.00 81.54  ? 98  THR A N   1 
ATOM   494  C CA  . THR A 1 74  ? 12.619 84.383  19.750 1.00 85.52  ? 98  THR A CA  1 
ATOM   495  C C   . THR A 1 74  ? 11.347 85.124  20.132 1.00 85.85  ? 98  THR A C   1 
ATOM   496  O O   . THR A 1 74  ? 10.441 85.282  19.320 1.00 88.79  ? 98  THR A O   1 
ATOM   497  C CB  . THR A 1 74  ? 13.400 85.216  18.711 1.00 82.91  ? 98  THR A CB  1 
ATOM   498  O OG1 . THR A 1 74  ? 14.625 84.546  18.404 1.00 84.09  ? 98  THR A OG1 1 
ATOM   499  C CG2 . THR A 1 74  ? 13.704 86.610  19.242 1.00 81.88  ? 98  THR A CG2 1 
ATOM   500  N N   . LEU A 1 75  ? 11.278 85.558  21.381 1.00 77.97  ? 99  LEU A N   1 
ATOM   501  C CA  . LEU A 1 75  ? 10.113 86.274  21.862 1.00 78.36  ? 99  LEU A CA  1 
ATOM   502  C C   . LEU A 1 75  ? 10.323 87.775  21.763 1.00 81.51  ? 99  LEU A C   1 
ATOM   503  O O   . LEU A 1 75  ? 11.449 88.246  21.583 1.00 75.11  ? 99  LEU A O   1 
ATOM   504  C CB  . LEU A 1 75  ? 9.825  85.902  23.327 1.00 82.42  ? 99  LEU A CB  1 
ATOM   505  C CG  . LEU A 1 75  ? 9.614  84.415  23.667 1.00 84.97  ? 99  LEU A CG  1 
ATOM   506  C CD1 . LEU A 1 75  ? 9.260  84.284  25.144 1.00 86.07  ? 99  LEU A CD1 1 
ATOM   507  C CD2 . LEU A 1 75  ? 8.529  83.787  22.797 1.00 85.18  ? 99  LEU A CD2 1 
ATOM   508  N N   . VAL A 1 76  ? 9.216  88.512  21.833 1.00 104.09 ? 100 VAL A N   1 
ATOM   509  C CA  . VAL A 1 76  ? 9.224  89.974  21.864 1.00 106.69 ? 100 VAL A CA  1 
ATOM   510  C C   . VAL A 1 76  ? 8.041  90.484  22.681 1.00 110.76 ? 100 VAL A C   1 
ATOM   511  O O   . VAL A 1 76  ? 6.891  90.150  22.409 1.00 122.99 ? 100 VAL A O   1 
ATOM   512  C CB  . VAL A 1 76  ? 9.252  90.626  20.432 1.00 92.10  ? 100 VAL A CB  1 
ATOM   513  C CG1 . VAL A 1 76  ? 8.354  89.883  19.471 1.00 83.90  ? 100 VAL A CG1 1 
ATOM   514  C CG2 . VAL A 1 76  ? 8.878  92.111  20.512 1.00 82.54  ? 100 VAL A CG2 1 
ATOM   515  N N   . ILE A 1 77  ? 8.347  91.261  23.715 1.00 88.84  ? 101 ILE A N   1 
ATOM   516  C CA  . ILE A 1 77  ? 7.322  91.839  24.574 1.00 85.78  ? 101 ILE A CA  1 
ATOM   517  C C   . ILE A 1 77  ? 7.040  93.273  24.074 1.00 91.67  ? 101 ILE A C   1 
ATOM   518  O O   . ILE A 1 77  ? 7.805  93.808  23.266 1.00 83.04  ? 101 ILE A O   1 
ATOM   519  C CB  . ILE A 1 77  ? 7.790  91.824  26.065 1.00 93.09  ? 101 ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 77  ? 8.428  90.464  26.383 1.00 93.30  ? 101 ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 77  ? 6.607  92.084  27.006 1.00 95.41  ? 101 ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 77  ? 9.236  90.420  27.678 1.00 87.61  ? 101 ILE A CD1 1 
ATOM   523  N N   . ASP A 1 78  ? 5.922  93.863  24.510 1.00 125.25 ? 102 ASP A N   1 
ATOM   524  C CA  . ASP A 1 78  ? 5.529  95.235  24.117 1.00 141.28 ? 102 ASP A CA  1 
ATOM   525  C C   . ASP A 1 78  ? 4.701  95.929  25.211 1.00 149.54 ? 102 ASP A C   1 
ATOM   526  O O   . ASP A 1 78  ? 3.605  95.480  25.562 1.00 160.11 ? 102 ASP A O   1 
ATOM   527  C CB  . ASP A 1 78  ? 4.752  95.222  22.791 1.00 151.77 ? 102 ASP A CB  1 
ATOM   528  C CG  . ASP A 1 78  ? 5.624  95.588  21.595 1.00 147.78 ? 102 ASP A CG  1 
ATOM   529  O OD1 . ASP A 1 78  ? 5.203  95.311  20.453 1.00 145.42 ? 102 ASP A OD1 1 
ATOM   530  O OD2 . ASP A 1 78  ? 6.719  96.162  21.791 1.00 145.62 ? 102 ASP A OD2 1 
ATOM   531  N N   . PHE A 1 79  ? 5.229  97.040  25.725 1.00 152.87 ? 103 PHE A N   1 
ATOM   532  C CA  . PHE A 1 79  ? 4.597  97.765  26.832 1.00 148.56 ? 103 PHE A CA  1 
ATOM   533  C C   . PHE A 1 79  ? 3.857  99.030  26.405 1.00 144.56 ? 103 PHE A C   1 
ATOM   534  O O   . PHE A 1 79  ? 3.394  99.801  27.253 1.00 144.86 ? 103 PHE A O   1 
ATOM   535  C CB  . PHE A 1 79  ? 5.668  98.106  27.891 1.00 152.82 ? 103 PHE A CB  1 
ATOM   536  C CG  . PHE A 1 79  ? 6.363  96.897  28.473 1.00 156.91 ? 103 PHE A CG  1 
ATOM   537  C CD1 . PHE A 1 79  ? 5.847  96.254  29.595 1.00 158.29 ? 103 PHE A CD1 1 
ATOM   538  C CD2 . PHE A 1 79  ? 7.528  96.395  27.888 1.00 158.29 ? 103 PHE A CD2 1 
ATOM   539  C CE1 . PHE A 1 79  ? 6.480  95.131  30.127 1.00 158.95 ? 103 PHE A CE1 1 
ATOM   540  C CE2 . PHE A 1 79  ? 8.166  95.274  28.411 1.00 159.00 ? 103 PHE A CE2 1 
ATOM   541  C CZ  . PHE A 1 79  ? 7.642  94.639  29.534 1.00 159.20 ? 103 PHE A CZ  1 
ATOM   542  N N   . ARG A 1 80  ? 3.727  99.217  25.091 1.00 144.37 ? 104 ARG A N   1 
ATOM   543  C CA  . ARG A 1 80  ? 3.063  100.388 24.505 1.00 144.48 ? 104 ARG A CA  1 
ATOM   544  C C   . ARG A 1 80  ? 1.586  100.520 24.891 1.00 147.84 ? 104 ARG A C   1 
ATOM   545  O O   . ARG A 1 80  ? 0.917  101.469 24.468 1.00 147.41 ? 104 ARG A O   1 
ATOM   546  C CB  . ARG A 1 80  ? 3.172  100.342 22.966 1.00 140.42 ? 104 ARG A CB  1 
ATOM   547  C CG  . ARG A 1 80  ? 4.576  100.532 22.410 1.00 132.12 ? 104 ARG A CG  1 
ATOM   548  C CD  . ARG A 1 80  ? 4.639  100.181 20.926 1.00 128.58 ? 104 ARG A CD  1 
ATOM   549  N NE  . ARG A 1 80  ? 5.983  100.360 20.371 1.00 128.26 ? 104 ARG A NE  1 
ATOM   550  C CZ  . ARG A 1 80  ? 6.389  99.900  19.185 1.00 128.25 ? 104 ARG A CZ  1 
ATOM   551  N NH1 . ARG A 1 80  ? 5.558  99.218  18.401 1.00 127.80 ? 104 ARG A NH1 1 
ATOM   552  N NH2 . ARG A 1 80  ? 7.636  100.121 18.780 1.00 127.63 ? 104 ARG A NH2 1 
ATOM   553  N N   . SER A 1 81  ? 1.094  99.587  25.707 1.00 176.39 ? 105 SER A N   1 
ATOM   554  C CA  . SER A 1 81  ? -0.316 99.557  26.098 1.00 181.80 ? 105 SER A CA  1 
ATOM   555  C C   . SER A 1 81  ? -0.564 99.327  27.600 1.00 187.28 ? 105 SER A C   1 
ATOM   556  O O   . SER A 1 81  ? -1.326 98.436  27.991 1.00 194.36 ? 105 SER A O   1 
ATOM   557  C CB  . SER A 1 81  ? -1.049 98.488  25.260 1.00 136.83 ? 105 SER A CB  1 
ATOM   558  O OG  . SER A 1 81  ? -2.450 98.533  25.469 1.00 118.74 ? 105 SER A OG  1 
ATOM   559  N N   . GLY A 1 82  ? 0.089  100.145 28.427 1.00 176.03 ? 106 GLY A N   1 
ATOM   560  C CA  . GLY A 1 82  ? -0.074 100.082 29.875 1.00 168.28 ? 106 GLY A CA  1 
ATOM   561  C C   . GLY A 1 82  ? 0.492  98.835  30.529 1.00 164.20 ? 106 GLY A C   1 
ATOM   562  O O   . GLY A 1 82  ? -0.262 97.974  30.984 1.00 163.32 ? 106 GLY A O   1 
ATOM   563  N N   . GLY A 1 83  ? 1.821  98.747  30.578 1.00 148.86 ? 107 GLY A N   1 
ATOM   564  C CA  . GLY A 1 83  ? 2.496  97.595  31.164 1.00 148.17 ? 107 GLY A CA  1 
ATOM   565  C C   . GLY A 1 83  ? 3.875  97.925  31.718 1.00 149.56 ? 107 GLY A C   1 
ATOM   566  O O   . GLY A 1 83  ? 4.533  98.857  31.246 1.00 144.73 ? 107 GLY A O   1 
ATOM   567  N N   . ARG A 1 84  ? 4.322  97.150  32.709 1.00 163.38 ? 108 ARG A N   1 
ATOM   568  C CA  . ARG A 1 84  ? 5.615  97.390  33.359 1.00 162.39 ? 108 ARG A CA  1 
ATOM   569  C C   . ARG A 1 84  ? 6.485  96.134  33.484 1.00 148.98 ? 108 ARG A C   1 
ATOM   570  O O   . ARG A 1 84  ? 6.044  95.107  34.010 1.00 162.10 ? 108 ARG A O   1 
ATOM   571  C CB  . ARG A 1 84  ? 5.392  98.069  34.729 1.00 177.24 ? 108 ARG A CB  1 
ATOM   572  C CG  . ARG A 1 84  ? 4.269  97.494  35.593 1.00 181.41 ? 108 ARG A CG  1 
ATOM   573  C CD  . ARG A 1 84  ? 3.881  98.477  36.707 1.00 182.55 ? 108 ARG A CD  1 
ATOM   574  N NE  . ARG A 1 84  ? 2.986  97.887  37.705 1.00 183.38 ? 108 ARG A NE  1 
ATOM   575  C CZ  . ARG A 1 84  ? 2.587  98.499  38.822 1.00 183.89 ? 108 ARG A CZ  1 
ATOM   576  N NH1 . ARG A 1 84  ? 2.999  99.732  39.097 1.00 184.24 ? 108 ARG A NH1 1 
ATOM   577  N NH2 . ARG A 1 84  ? 1.775  97.875  39.670 1.00 183.94 ? 108 ARG A NH2 1 
ATOM   578  N N   . PRO A 1 85  ? 7.749  96.215  33.000 1.00 98.81  ? 109 PRO A N   1 
ATOM   579  C CA  . PRO A 1 85  ? 8.713  95.102  33.025 1.00 87.00  ? 109 PRO A CA  1 
ATOM   580  C C   . PRO A 1 85  ? 9.107  94.598  34.403 1.00 84.47  ? 109 PRO A C   1 
ATOM   581  O O   . PRO A 1 85  ? 9.734  93.553  34.515 1.00 77.03  ? 109 PRO A O   1 
ATOM   582  C CB  . PRO A 1 85  ? 9.927  95.644  32.259 1.00 76.82  ? 109 PRO A CB  1 
ATOM   583  C CG  . PRO A 1 85  ? 9.445  96.886  31.567 1.00 75.08  ? 109 PRO A CG  1 
ATOM   584  C CD  . PRO A 1 85  ? 8.368  97.439  32.448 1.00 86.25  ? 109 PRO A CD  1 
ATOM   585  N N   . GLU A 1 86  ? 8.751  95.353  35.442 1.00 97.58  ? 110 GLU A N   1 
ATOM   586  C CA  . GLU A 1 86  ? 9.049  94.983  36.832 1.00 113.29 ? 110 GLU A CA  1 
ATOM   587  C C   . GLU A 1 86  ? 8.263  93.749  37.287 1.00 116.68 ? 110 GLU A C   1 
ATOM   588  O O   . GLU A 1 86  ? 8.657  93.074  38.242 1.00 111.76 ? 110 GLU A O   1 
ATOM   589  C CB  . GLU A 1 86  ? 8.793  96.171  37.769 1.00 148.72 ? 110 GLU A CB  1 
ATOM   590  C CG  . GLU A 1 86  ? 7.422  96.831  37.604 1.00 162.86 ? 110 GLU A CG  1 
ATOM   591  C CD  . GLU A 1 86  ? 7.374  98.249  38.159 1.00 168.45 ? 110 GLU A CD  1 
ATOM   592  O OE1 . GLU A 1 86  ? 7.726  98.441  39.344 1.00 169.94 ? 110 GLU A OE1 1 
ATOM   593  O OE2 . GLU A 1 86  ? 6.977  99.168  37.406 1.00 169.66 ? 110 GLU A OE2 1 
ATOM   594  N N   . GLU A 1 87  ? 7.153  93.467  36.604 1.00 148.98 ? 111 GLU A N   1 
ATOM   595  C CA  . GLU A 1 87  ? 6.350  92.270  36.870 1.00 156.04 ? 111 GLU A CA  1 
ATOM   596  C C   . GLU A 1 87  ? 6.877  91.098  36.017 1.00 153.89 ? 111 GLU A C   1 
ATOM   597  O O   . GLU A 1 87  ? 6.621  89.930  36.328 1.00 156.45 ? 111 GLU A O   1 
ATOM   598  C CB  . GLU A 1 87  ? 4.878  92.505  36.481 1.00 169.22 ? 111 GLU A CB  1 
ATOM   599  C CG  . GLU A 1 87  ? 4.191  93.661  37.201 1.00 175.15 ? 111 GLU A CG  1 
ATOM   600  C CD  . GLU A 1 87  ? 2.916  94.133  36.496 1.00 176.86 ? 111 GLU A CD  1 
ATOM   601  O OE1 . GLU A 1 87  ? 2.014  94.660  37.187 1.00 177.03 ? 111 GLU A OE1 1 
ATOM   602  O OE2 . GLU A 1 87  ? 2.816  93.993  35.255 1.00 176.84 ? 111 GLU A OE2 1 
ATOM   603  N N   . TYR A 1 88  ? 7.623  91.432  34.961 1.00 121.26 ? 112 TYR A N   1 
ATOM   604  C CA  . TYR A 1 88  ? 8.124  90.458  33.988 1.00 109.88 ? 112 TYR A CA  1 
ATOM   605  C C   . TYR A 1 88  ? 9.539  89.946  34.241 1.00 100.98 ? 112 TYR A C   1 
ATOM   606  O O   . TYR A 1 88  ? 10.230 89.497  33.323 1.00 95.41  ? 112 TYR A O   1 
ATOM   607  C CB  . TYR A 1 88  ? 8.001  91.061  32.574 1.00 117.34 ? 112 TYR A CB  1 
ATOM   608  C CG  . TYR A 1 88  ? 6.621  90.918  31.957 1.00 124.61 ? 112 TYR A CG  1 
ATOM   609  C CD1 . TYR A 1 88  ? 5.465  91.069  32.732 1.00 128.10 ? 112 TYR A CD1 1 
ATOM   610  C CD2 . TYR A 1 88  ? 6.470  90.622  30.601 1.00 128.17 ? 112 TYR A CD2 1 
ATOM   611  C CE1 . TYR A 1 88  ? 4.200  90.923  32.178 1.00 129.66 ? 112 TYR A CE1 1 
ATOM   612  C CE2 . TYR A 1 88  ? 5.207  90.480  30.036 1.00 129.92 ? 112 TYR A CE2 1 
ATOM   613  C CZ  . TYR A 1 88  ? 4.079  90.630  30.834 1.00 130.43 ? 112 TYR A CZ  1 
ATOM   614  O OH  . TYR A 1 88  ? 2.825  90.489  30.289 1.00 131.51 ? 112 TYR A OH  1 
ATOM   615  N N   . GLU A 1 89  ? 9.959  90.013  35.499 1.00 92.02  ? 113 GLU A N   1 
ATOM   616  C CA  . GLU A 1 89  ? 11.269 89.532  35.897 1.00 90.30  ? 113 GLU A CA  1 
ATOM   617  C C   . GLU A 1 89  ? 11.168 88.066  36.323 1.00 85.98  ? 113 GLU A C   1 
ATOM   618  O O   . GLU A 1 89  ? 10.347 87.714  37.178 1.00 82.76  ? 113 GLU A O   1 
ATOM   619  C CB  . GLU A 1 89  ? 11.832 90.370  37.061 1.00 104.97 ? 113 GLU A CB  1 
ATOM   620  C CG  . GLU A 1 89  ? 12.099 91.834  36.716 1.00 111.13 ? 113 GLU A CG  1 
ATOM   621  C CD  . GLU A 1 89  ? 13.056 92.512  37.688 1.00 113.91 ? 113 GLU A CD  1 
ATOM   622  O OE1 . GLU A 1 89  ? 12.790 92.509  38.911 1.00 113.95 ? 113 GLU A OE1 1 
ATOM   623  O OE2 . GLU A 1 89  ? 14.080 93.055  37.220 1.00 114.43 ? 113 GLU A OE2 1 
ATOM   624  N N   . GLY A 1 90  ? 12.001 87.220  35.711 1.00 86.82  ? 114 GLY A N   1 
ATOM   625  C CA  . GLY A 1 90  ? 12.017 85.808  36.048 1.00 81.89  ? 114 GLY A CA  1 
ATOM   626  C C   . GLY A 1 90  ? 12.947 84.960  35.200 1.00 77.38  ? 114 GLY A C   1 
ATOM   627  O O   . GLY A 1 90  ? 13.608 85.463  34.289 1.00 77.19  ? 114 GLY A O   1 
ATOM   628  N N   . GLU A 1 91  ? 12.973 83.662  35.508 1.00 71.03  ? 115 GLU A N   1 
ATOM   629  C CA  . GLU A 1 91  ? 13.810 82.683  34.821 1.00 68.50  ? 115 GLU A CA  1 
ATOM   630  C C   . GLU A 1 91  ? 13.099 82.109  33.593 1.00 62.90  ? 115 GLU A C   1 
ATOM   631  O O   . GLU A 1 91  ? 12.046 81.481  33.713 1.00 54.34  ? 115 GLU A O   1 
ATOM   632  C CB  . GLU A 1 91  ? 14.157 81.560  35.797 1.00 81.15  ? 115 GLU A CB  1 
ATOM   633  C CG  . GLU A 1 91  ? 15.368 80.731  35.416 1.00 94.95  ? 115 GLU A CG  1 
ATOM   634  C CD  . GLU A 1 91  ? 15.596 79.561  36.363 1.00 100.79 ? 115 GLU A CD  1 
ATOM   635  O OE1 . GLU A 1 91  ? 14.824 78.579  36.296 1.00 102.60 ? 115 GLU A OE1 1 
ATOM   636  O OE2 . GLU A 1 91  ? 16.544 79.623  37.174 1.00 101.45 ? 115 GLU A OE2 1 
ATOM   637  N N   . TYR A 1 92  ? 13.677 82.327  32.418 1.00 56.45  ? 116 TYR A N   1 
ATOM   638  C CA  . TYR A 1 92  ? 13.100 81.848  31.165 1.00 57.40  ? 116 TYR A CA  1 
ATOM   639  C C   . TYR A 1 92  ? 13.927 80.716  30.579 1.00 55.35  ? 116 TYR A C   1 
ATOM   640  O O   . TYR A 1 92  ? 15.146 80.699  30.738 1.00 53.03  ? 116 TYR A O   1 
ATOM   641  C CB  . TYR A 1 92  ? 13.035 82.978  30.125 1.00 79.94  ? 116 TYR A CB  1 
ATOM   642  C CG  . TYR A 1 92  ? 12.047 84.087  30.429 1.00 91.57  ? 116 TYR A CG  1 
ATOM   643  C CD1 . TYR A 1 92  ? 12.353 85.092  31.346 1.00 96.35  ? 116 TYR A CD1 1 
ATOM   644  C CD2 . TYR A 1 92  ? 10.804 84.132  29.795 1.00 95.87  ? 116 TYR A CD2 1 
ATOM   645  C CE1 . TYR A 1 92  ? 11.451 86.113  31.623 1.00 97.93  ? 116 TYR A CE1 1 
ATOM   646  C CE2 . TYR A 1 92  ? 9.896  85.149  30.066 1.00 97.16  ? 116 TYR A CE2 1 
ATOM   647  C CZ  . TYR A 1 92  ? 10.227 86.135  30.981 1.00 97.93  ? 116 TYR A CZ  1 
ATOM   648  O OH  . TYR A 1 92  ? 9.340  87.148  31.264 1.00 98.33  ? 116 TYR A OH  1 
ATOM   649  N N   . GLN A 1 93  ? 13.272 79.768  29.911 1.00 55.54  ? 117 GLN A N   1 
ATOM   650  C CA  . GLN A 1 93  ? 13.985 78.669  29.261 1.00 56.30  ? 117 GLN A CA  1 
ATOM   651  C C   . GLN A 1 93  ? 13.269 78.253  27.981 1.00 58.57  ? 117 GLN A C   1 
ATOM   652  O O   . GLN A 1 93  ? 12.072 77.967  27.979 1.00 58.79  ? 117 GLN A O   1 
ATOM   653  C CB  . GLN A 1 93  ? 14.161 77.469  30.200 1.00 56.36  ? 117 GLN A CB  1 
ATOM   654  C CG  . GLN A 1 93  ? 15.188 76.447  29.708 1.00 56.54  ? 117 GLN A CG  1 
ATOM   655  C CD  . GLN A 1 93  ? 15.495 75.348  30.724 1.00 58.23  ? 117 GLN A CD  1 
ATOM   656  O OE1 . GLN A 1 93  ? 14.838 75.226  31.753 1.00 58.95  ? 117 GLN A OE1 1 
ATOM   657  N NE2 . GLN A 1 93  ? 16.502 74.539  30.424 1.00 58.77  ? 117 GLN A NE2 1 
ATOM   658  N N   . CYS A 1 94  ? 14.027 78.230  26.892 1.00 70.27  ? 118 CYS A N   1 
ATOM   659  C CA  . CYS A 1 94  ? 13.507 77.902  25.575 1.00 73.48  ? 118 CYS A CA  1 
ATOM   660  C C   . CYS A 1 94  ? 13.626 76.415  25.282 1.00 73.32  ? 118 CYS A C   1 
ATOM   661  O O   . CYS A 1 94  ? 14.594 75.773  25.676 1.00 74.75  ? 118 CYS A O   1 
ATOM   662  C CB  . CYS A 1 94  ? 14.264 78.715  24.536 1.00 75.45  ? 118 CYS A CB  1 
ATOM   663  S SG  . CYS A 1 94  ? 13.831 78.376  22.813 1.00 77.19  ? 118 CYS A SG  1 
ATOM   664  N N   . PHE A 1 95  ? 12.631 75.877  24.591 1.00 68.82  ? 119 PHE A N   1 
ATOM   665  C CA  . PHE A 1 95  ? 12.595 74.463  24.257 1.00 66.35  ? 119 PHE A CA  1 
ATOM   666  C C   . PHE A 1 95  ? 12.402 74.268  22.754 1.00 68.27  ? 119 PHE A C   1 
ATOM   667  O O   . PHE A 1 95  ? 11.359 74.624  22.203 1.00 70.33  ? 119 PHE A O   1 
ATOM   668  C CB  . PHE A 1 95  ? 11.457 73.770  25.023 1.00 61.46  ? 119 PHE A CB  1 
ATOM   669  C CG  . PHE A 1 95  ? 11.721 73.607  26.493 1.00 56.85  ? 119 PHE A CG  1 
ATOM   670  C CD1 . PHE A 1 95  ? 11.661 74.695  27.359 1.00 54.78  ? 119 PHE A CD1 1 
ATOM   671  C CD2 . PHE A 1 95  ? 12.019 72.351  27.019 1.00 54.38  ? 119 PHE A CD2 1 
ATOM   672  C CE1 . PHE A 1 95  ? 11.900 74.536  28.722 1.00 53.46  ? 119 PHE A CE1 1 
ATOM   673  C CE2 . PHE A 1 95  ? 12.262 72.182  28.382 1.00 53.08  ? 119 PHE A CE2 1 
ATOM   674  C CZ  . PHE A 1 95  ? 12.198 73.276  29.233 1.00 53.46  ? 119 PHE A CZ  1 
ATOM   675  N N   . ALA A 1 96  ? 13.413 73.711  22.094 1.00 66.85  ? 120 ALA A N   1 
ATOM   676  C CA  . ALA A 1 96  ? 13.351 73.473  20.655 1.00 69.26  ? 120 ALA A CA  1 
ATOM   677  C C   . ALA A 1 96  ? 13.118 71.993  20.367 1.00 73.94  ? 120 ALA A C   1 
ATOM   678  O O   . ALA A 1 96  ? 13.976 71.151  20.633 1.00 76.40  ? 120 ALA A O   1 
ATOM   679  C CB  . ALA A 1 96  ? 14.629 73.957  19.985 1.00 48.93  ? 120 ALA A CB  1 
ATOM   680  N N   . ARG A 1 97  ? 11.946 71.689  19.818 1.00 93.41  ? 121 ARG A N   1 
ATOM   681  C CA  . ARG A 1 97  ? 11.562 70.317  19.537 1.00 99.69  ? 121 ARG A CA  1 
ATOM   682  C C   . ARG A 1 97  ? 11.255 70.040  18.070 1.00 96.77  ? 121 ARG A C   1 
ATOM   683  O O   . ARG A 1 97  ? 10.647 70.868  17.379 1.00 99.41  ? 121 ARG A O   1 
ATOM   684  C CB  . ARG A 1 97  ? 10.308 69.953  20.377 1.00 108.32 ? 121 ARG A CB  1 
ATOM   685  C CG  . ARG A 1 97  ? 9.621  68.644  19.994 1.00 117.13 ? 121 ARG A CG  1 
ATOM   686  C CD  . ARG A 1 97  ? 8.270  68.488  20.679 1.00 121.27 ? 121 ARG A CD  1 
ATOM   687  N NE  . ARG A 1 97  ? 7.353  67.677  19.879 1.00 122.98 ? 121 ARG A NE  1 
ATOM   688  C CZ  . ARG A 1 97  ? 6.151  67.265  20.284 1.00 123.81 ? 121 ARG A CZ  1 
ATOM   689  N NH1 . ARG A 1 97  ? 5.699  67.579  21.496 1.00 124.08 ? 121 ARG A NH1 1 
ATOM   690  N NH2 . ARG A 1 97  ? 5.393  66.537  19.469 1.00 123.78 ? 121 ARG A NH2 1 
ATOM   691  N N   . ASN A 1 98  ? 11.733 68.892  17.592 1.00 81.07  ? 122 ASN A N   1 
ATOM   692  C CA  . ASN A 1 98  ? 11.341 68.410  16.274 1.00 80.45  ? 122 ASN A CA  1 
ATOM   693  C C   . ASN A 1 98  ? 10.896 66.939  16.404 1.00 77.37  ? 122 ASN A C   1 
ATOM   694  O O   . ASN A 1 98  ? 10.731 66.429  17.527 1.00 62.50  ? 122 ASN A O   1 
ATOM   695  C CB  . ASN A 1 98  ? 12.417 68.607  15.192 1.00 118.63 ? 122 ASN A CB  1 
ATOM   696  C CG  . ASN A 1 98  ? 13.519 67.556  15.216 1.00 136.13 ? 122 ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 98  ? 13.507 66.617  16.014 1.00 145.20 ? 122 ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 98  ? 14.490 67.717  14.314 1.00 145.00 ? 122 ASN A ND2 1 
ATOM   699  N N   . LYS A 1 99  ? 10.686 66.275  15.267 1.00 98.02  ? 123 LYS A N   1 
ATOM   700  C CA  . LYS A 1 99  ? 10.209 64.893  15.239 1.00 114.40 ? 123 LYS A CA  1 
ATOM   701  C C   . LYS A 1 99  ? 11.101 63.903  15.994 1.00 121.64 ? 123 LYS A C   1 
ATOM   702  O O   . LYS A 1 99  ? 10.603 62.930  16.576 1.00 118.86 ? 123 LYS A O   1 
ATOM   703  C CB  . LYS A 1 99  ? 10.002 64.441  13.777 1.00 129.76 ? 123 LYS A CB  1 
ATOM   704  C CG  . LYS A 1 99  ? 8.733  65.010  13.115 1.00 138.81 ? 123 LYS A CG  1 
ATOM   705  C CD  . LYS A 1 99  ? 7.474  64.215  13.509 1.00 143.06 ? 123 LYS A CD  1 
ATOM   706  C CE  . LYS A 1 99  ? 6.183  64.958  13.172 1.00 144.37 ? 123 LYS A CE  1 
ATOM   707  N NZ  . LYS A 1 99  ? 5.925  65.050  11.706 1.00 145.29 ? 123 LYS A NZ  1 
ATOM   708  N N   . PHE A 1 100 ? 12.408 64.166  16.003 1.00 124.91 ? 124 PHE A N   1 
ATOM   709  C CA  . PHE A 1 100 ? 13.364 63.294  16.680 1.00 126.55 ? 124 PHE A CA  1 
ATOM   710  C C   . PHE A 1 100 ? 13.452 63.553  18.191 1.00 128.28 ? 124 PHE A C   1 
ATOM   711  O O   . PHE A 1 100 ? 13.303 62.623  18.989 1.00 135.37 ? 124 PHE A O   1 
ATOM   712  C CB  . PHE A 1 100 ? 14.778 63.441  16.068 1.00 121.54 ? 124 PHE A CB  1 
ATOM   713  C CG  . PHE A 1 100 ? 14.807 63.423  14.559 1.00 118.34 ? 124 PHE A CG  1 
ATOM   714  C CD1 . PHE A 1 100 ? 15.470 64.432  13.860 1.00 116.78 ? 124 PHE A CD1 1 
ATOM   715  C CD2 . PHE A 1 100 ? 14.177 62.407  13.836 1.00 116.89 ? 124 PHE A CD2 1 
ATOM   716  C CE1 . PHE A 1 100 ? 15.506 64.433  12.461 1.00 117.25 ? 124 PHE A CE1 1 
ATOM   717  C CE2 . PHE A 1 100 ? 14.210 62.400  12.435 1.00 117.32 ? 124 PHE A CE2 1 
ATOM   718  C CZ  . PHE A 1 100 ? 14.875 63.415  11.749 1.00 117.08 ? 124 PHE A CZ  1 
ATOM   719  N N   . GLY A 1 101 ? 13.687 64.811  18.574 1.00 117.48 ? 125 GLY A N   1 
ATOM   720  C CA  . GLY A 1 101 ? 13.852 65.152  19.978 1.00 103.66 ? 125 GLY A CA  1 
ATOM   721  C C   . GLY A 1 101 ? 13.727 66.625  20.323 1.00 93.26  ? 125 GLY A C   1 
ATOM   722  O O   . GLY A 1 101 ? 13.202 67.411  19.531 1.00 96.53  ? 125 GLY A O   1 
ATOM   723  N N   . THR A 1 102 ? 14.234 66.994  21.502 1.00 81.03  ? 126 THR A N   1 
ATOM   724  C CA  . THR A 1 102 ? 14.117 68.359  22.026 1.00 71.13  ? 126 THR A CA  1 
ATOM   725  C C   . THR A 1 102 ? 15.412 68.858  22.667 1.00 66.53  ? 126 THR A C   1 
ATOM   726  O O   . THR A 1 102 ? 16.046 68.149  23.448 1.00 64.02  ? 126 THR A O   1 
ATOM   727  C CB  . THR A 1 102 ? 12.961 68.422  23.102 1.00 68.72  ? 126 THR A CB  1 
ATOM   728  O OG1 . THR A 1 102 ? 11.754 67.878  22.547 1.00 67.31  ? 126 THR A OG1 1 
ATOM   729  C CG2 . THR A 1 102 ? 12.699 69.857  23.558 1.00 66.37  ? 126 THR A CG2 1 
ATOM   730  N N   . ALA A 1 103 ? 15.799 70.080  22.314 1.00 65.99  ? 127 ALA A N   1 
ATOM   731  C CA  . ALA A 1 103 ? 16.997 70.723  22.851 1.00 66.26  ? 127 ALA A CA  1 
ATOM   732  C C   . ALA A 1 103 ? 16.587 71.948  23.667 1.00 65.93  ? 127 ALA A C   1 
ATOM   733  O O   . ALA A 1 103 ? 15.638 72.645  23.308 1.00 67.07  ? 127 ALA A O   1 
ATOM   734  C CB  . ALA A 1 103 ? 17.930 71.135  21.729 1.00 62.26  ? 127 ALA A CB  1 
ATOM   735  N N   . LEU A 1 104 ? 17.319 72.216  24.752 1.00 63.20  ? 128 LEU A N   1 
ATOM   736  C CA  . LEU A 1 104 ? 16.974 73.325  25.640 1.00 60.48  ? 128 LEU A CA  1 
ATOM   737  C C   . LEU A 1 104 ? 18.012 74.425  25.632 1.00 59.99  ? 128 LEU A C   1 
ATOM   738  O O   . LEU A 1 104 ? 19.184 74.185  25.372 1.00 60.83  ? 128 LEU A O   1 
ATOM   739  C CB  . LEU A 1 104 ? 16.807 72.828  27.098 1.00 55.06  ? 128 LEU A CB  1 
ATOM   740  C CG  . LEU A 1 104 ? 16.463 71.362  27.432 1.00 55.75  ? 128 LEU A CG  1 
ATOM   741  C CD1 . LEU A 1 104 ? 16.404 71.183  28.940 1.00 53.42  ? 128 LEU A CD1 1 
ATOM   742  C CD2 . LEU A 1 104 ? 15.145 70.915  26.794 1.00 55.13  ? 128 LEU A CD2 1 
ATOM   743  N N   . SER A 1 105 ? 17.565 75.642  25.901 1.00 57.90  ? 129 SER A N   1 
ATOM   744  C CA  . SER A 1 105 ? 18.462 76.776  26.013 1.00 57.81  ? 129 SER A CA  1 
ATOM   745  C C   . SER A 1 105 ? 18.838 76.896  27.486 1.00 56.17  ? 129 SER A C   1 
ATOM   746  O O   . SER A 1 105 ? 18.348 76.140  28.327 1.00 54.88  ? 129 SER A O   1 
ATOM   747  C CB  . SER A 1 105 ? 17.759 78.064  25.598 1.00 65.19  ? 129 SER A CB  1 
ATOM   748  O OG  . SER A 1 105 ? 16.837 78.488  26.591 1.00 67.58  ? 129 SER A OG  1 
ATOM   749  N N   . ASN A 1 106 ? 19.725 77.841  27.779 1.00 55.22  ? 130 ASN A N   1 
ATOM   750  C CA  . ASN A 1 106 ? 20.106 78.122  29.146 1.00 54.99  ? 130 ASN A CA  1 
ATOM   751  C C   . ASN A 1 106 ? 18.899 78.728  29.882 1.00 54.30  ? 130 ASN A C   1 
ATOM   752  O O   . ASN A 1 106 ? 17.857 79.006  29.275 1.00 52.54  ? 130 ASN A O   1 
ATOM   753  C CB  . ASN A 1 106 ? 21.269 79.123  29.176 1.00 62.30  ? 130 ASN A CB  1 
ATOM   754  C CG  . ASN A 1 106 ? 22.588 78.510  28.691 1.00 66.22  ? 130 ASN A CG  1 
ATOM   755  O OD1 . ASN A 1 106 ? 22.969 77.410  29.107 1.00 67.03  ? 130 ASN A OD1 1 
ATOM   756  N ND2 . ASN A 1 106 ? 23.295 79.231  27.826 1.00 65.49  ? 130 ASN A ND2 1 
ATOM   757  N N   . ARG A 1 107 ? 19.035 78.896  31.196 1.00 57.10  ? 131 ARG A N   1 
ATOM   758  C CA  . ARG A 1 107 ? 17.995 79.523  32.005 1.00 59.34  ? 131 ARG A CA  1 
ATOM   759  C C   . ARG A 1 107 ? 18.253 81.023  32.040 1.00 57.58  ? 131 ARG A C   1 
ATOM   760  O O   . ARG A 1 107 ? 19.075 81.511  32.816 1.00 60.20  ? 131 ARG A O   1 
ATOM   761  C CB  . ARG A 1 107 ? 17.964 78.923  33.414 1.00 71.44  ? 131 ARG A CB  1 
ATOM   762  C CG  . ARG A 1 107 ? 17.160 77.629  33.467 1.00 75.56  ? 131 ARG A CG  1 
ATOM   763  C CD  . ARG A 1 107 ? 17.301 76.881  34.776 1.00 77.01  ? 131 ARG A CD  1 
ATOM   764  N NE  . ARG A 1 107 ? 16.641 75.578  34.695 1.00 76.13  ? 131 ARG A NE  1 
ATOM   765  C CZ  . ARG A 1 107 ? 16.552 74.705  35.700 1.00 76.66  ? 131 ARG A CZ  1 
ATOM   766  N NH1 . ARG A 1 107 ? 17.081 74.983  36.891 1.00 75.77  ? 131 ARG A NH1 1 
ATOM   767  N NH2 . ARG A 1 107 ? 15.926 73.545  35.513 1.00 76.63  ? 131 ARG A NH2 1 
ATOM   768  N N   . ILE A 1 108 ? 17.528 81.736  31.179 1.00 55.14  ? 132 ILE A N   1 
ATOM   769  C CA  . ILE A 1 108 ? 17.670 83.177  31.022 1.00 53.96  ? 132 ILE A CA  1 
ATOM   770  C C   . ILE A 1 108 ? 17.016 83.949  32.164 1.00 56.72  ? 132 ILE A C   1 
ATOM   771  O O   . ILE A 1 108 ? 15.793 84.043  32.231 1.00 52.51  ? 132 ILE A O   1 
ATOM   772  C CB  . ILE A 1 108 ? 17.028 83.672  29.673 1.00 54.18  ? 132 ILE A CB  1 
ATOM   773  C CG1 . ILE A 1 108 ? 17.258 82.668  28.529 1.00 55.19  ? 132 ILE A CG1 1 
ATOM   774  C CG2 . ILE A 1 108 ? 17.537 85.057  29.318 1.00 53.63  ? 132 ILE A CG2 1 
ATOM   775  C CD1 . ILE A 1 108 ? 18.715 82.364  28.155 1.00 64.64  ? 132 ILE A CD1 1 
ATOM   776  N N   . ARG A 1 109 ? 17.834 84.475  33.073 1.00 71.11  ? 133 ARG A N   1 
ATOM   777  C CA  . ARG A 1 109 ? 17.327 85.303  34.165 1.00 83.46  ? 133 ARG A CA  1 
ATOM   778  C C   . ARG A 1 109 ? 17.250 86.759  33.677 1.00 88.02  ? 133 ARG A C   1 
ATOM   779  O O   . ARG A 1 109 ? 18.242 87.493  33.689 1.00 84.89  ? 133 ARG A O   1 
ATOM   780  C CB  . ARG A 1 109 ? 18.224 85.209  35.404 1.00 113.54 ? 133 ARG A CB  1 
ATOM   781  C CG  . ARG A 1 109 ? 18.143 83.868  36.141 1.00 130.09 ? 133 ARG A CG  1 
ATOM   782  C CD  . ARG A 1 109 ? 16.910 83.782  37.046 1.00 138.02 ? 133 ARG A CD  1 
ATOM   783  N NE  . ARG A 1 109 ? 16.862 82.548  37.835 1.00 140.96 ? 133 ARG A NE  1 
ATOM   784  C CZ  . ARG A 1 109 ? 17.429 82.383  39.032 1.00 142.50 ? 133 ARG A CZ  1 
ATOM   785  N NH1 . ARG A 1 109 ? 18.102 83.378  39.605 1.00 142.56 ? 133 ARG A NH1 1 
ATOM   786  N NH2 . ARG A 1 109 ? 17.320 81.218  39.667 1.00 143.33 ? 133 ARG A NH2 1 
ATOM   787  N N   . LEU A 1 110 ? 16.057 87.153  33.227 1.00 100.25 ? 134 LEU A N   1 
ATOM   788  C CA  . LEU A 1 110 ? 15.808 88.509  32.739 1.00 104.60 ? 134 LEU A CA  1 
ATOM   789  C C   . LEU A 1 110 ? 15.556 89.438  33.922 1.00 101.71 ? 134 LEU A C   1 
ATOM   790  O O   . LEU A 1 110 ? 14.714 89.157  34.784 1.00 108.18 ? 134 LEU A O   1 
ATOM   791  C CB  . LEU A 1 110 ? 14.609 88.525  31.781 1.00 98.95  ? 134 LEU A CB  1 
ATOM   792  C CG  . LEU A 1 110 ? 14.189 89.891  31.217 1.00 99.60  ? 134 LEU A CG  1 
ATOM   793  C CD1 . LEU A 1 110 ? 14.971 90.223  29.945 1.00 99.03  ? 134 LEU A CD1 1 
ATOM   794  C CD2 . LEU A 1 110 ? 12.695 89.885  30.937 1.00 98.85  ? 134 LEU A CD2 1 
ATOM   795  N N   . GLN A 1 111 ? 16.293 90.547  33.943 1.00 87.34  ? 135 GLN A N   1 
ATOM   796  C CA  . GLN A 1 111 ? 16.209 91.513  35.037 1.00 82.11  ? 135 GLN A CA  1 
ATOM   797  C C   . GLN A 1 111 ? 16.241 92.947  34.498 1.00 80.06  ? 135 GLN A C   1 
ATOM   798  O O   . GLN A 1 111 ? 16.908 93.223  33.493 1.00 72.66  ? 135 GLN A O   1 
ATOM   799  C CB  . GLN A 1 111 ? 17.373 91.266  36.008 1.00 81.54  ? 135 GLN A CB  1 
ATOM   800  C CG  . GLN A 1 111 ? 17.042 91.504  37.480 1.00 83.58  ? 135 GLN A CG  1 
ATOM   801  C CD  . GLN A 1 111 ? 18.118 90.960  38.420 1.00 85.33  ? 135 GLN A CD  1 
ATOM   802  O OE1 . GLN A 1 111 ? 19.240 90.656  38.001 1.00 85.18  ? 135 GLN A OE1 1 
ATOM   803  N NE2 . GLN A 1 111 ? 17.778 90.840  39.699 1.00 85.38  ? 135 GLN A NE2 1 
ATOM   804  N N   . VAL A 1 112 ? 15.513 93.851  35.159 1.00 92.09  ? 136 VAL A N   1 
ATOM   805  C CA  . VAL A 1 112 ? 15.459 95.244  34.721 1.00 97.56  ? 136 VAL A CA  1 
ATOM   806  C C   . VAL A 1 112 ? 16.621 96.088  35.236 1.00 101.88 ? 136 VAL A C   1 
ATOM   807  O O   . VAL A 1 112 ? 16.948 96.052  36.425 1.00 108.00 ? 136 VAL A O   1 
ATOM   808  C CB  . VAL A 1 112 ? 14.107 95.955  35.122 1.00 98.25  ? 136 VAL A CB  1 
ATOM   809  C CG1 . VAL A 1 112 ? 12.938 95.293  34.407 1.00 94.71  ? 136 VAL A CG1 1 
ATOM   810  C CG2 . VAL A 1 112 ? 13.905 95.958  36.640 1.00 94.22  ? 136 VAL A CG2 1 
ATOM   811  N N   . SER A 1 113 ? 17.251 96.828  34.320 1.00 93.81  ? 137 SER A N   1 
ATOM   812  C CA  . SER A 1 113 ? 18.356 97.730  34.659 1.00 89.54  ? 137 SER A CA  1 
ATOM   813  C C   . SER A 1 113 ? 17.842 98.901  35.492 1.00 84.37  ? 137 SER A C   1 
ATOM   814  O O   . SER A 1 113 ? 17.365 99.905  34.962 1.00 79.15  ? 137 SER A O   1 
ATOM   815  C CB  . SER A 1 113 ? 19.036 98.263  33.390 1.00 105.55 ? 137 SER A CB  1 
ATOM   816  O OG  . SER A 1 113 ? 20.023 97.363  32.922 1.00 112.51 ? 137 SER A OG  1 
ATOM   817  N N   . LYS A 1 114 ? 17.940 98.759  36.804 1.00 85.77  ? 138 LYS A N   1 
ATOM   818  C CA  . LYS A 1 114 ? 17.487 99.800  37.693 1.00 91.77  ? 138 LYS A CA  1 
ATOM   819  C C   . LYS A 1 114 ? 18.535 100.891 37.932 1.00 92.61  ? 138 LYS A C   1 
ATOM   820  O O   . LYS A 1 114 ? 19.734 100.613 38.042 1.00 87.00  ? 138 LYS A O   1 
ATOM   821  C CB  . LYS A 1 114 ? 17.072 99.188  39.048 1.00 114.75 ? 138 LYS A CB  1 
ATOM   822  C CG  . LYS A 1 114 ? 15.586 98.828  39.148 1.00 124.68 ? 138 LYS A CG  1 
ATOM   823  C CD  . LYS A 1 114 ? 14.761 99.981  39.729 1.00 129.09 ? 138 LYS A CD  1 
ATOM   824  C CE  . LYS A 1 114 ? 13.303 99.582  39.956 1.00 130.36 ? 138 LYS A CE  1 
ATOM   825  N NZ  . LYS A 1 114 ? 13.132 98.597  41.064 1.00 130.89 ? 138 LYS A NZ  1 
ATOM   826  N N   . SER A 1 115 ? 18.075 102.140 37.956 1.00 106.55 ? 139 SER A N   1 
ATOM   827  C CA  . SER A 1 115 ? 18.921 103.287 38.342 1.00 110.97 ? 139 SER A CA  1 
ATOM   828  C C   . SER A 1 115 ? 18.045 104.038 39.364 1.00 115.14 ? 139 SER A C   1 
ATOM   829  O O   . SER A 1 115 ? 17.613 105.172 39.127 1.00 118.34 ? 139 SER A O   1 
ATOM   830  C CB  . SER A 1 115 ? 19.254 104.157 37.135 1.00 91.53  ? 139 SER A CB  1 
ATOM   831  O OG  . SER A 1 115 ? 18.109 104.487 36.373 1.00 85.42  ? 139 SER A OG  1 
ATOM   832  N N   . PRO A 1 116 ? 17.846 103.429 40.553 1.00 100.55 ? 140 PRO A N   1 
ATOM   833  C CA  . PRO A 1 116 ? 17.002 104.003 41.602 1.00 96.28  ? 140 PRO A CA  1 
ATOM   834  C C   . PRO A 1 116 ? 17.507 105.203 42.352 1.00 88.90  ? 140 PRO A C   1 
ATOM   835  O O   . PRO A 1 116 ? 18.705 105.453 42.375 1.00 78.68  ? 140 PRO A O   1 
ATOM   836  C CB  . PRO A 1 116 ? 16.732 102.805 42.527 1.00 109.23 ? 140 PRO A CB  1 
ATOM   837  C CG  . PRO A 1 116 ? 17.591 101.658 41.979 1.00 116.65 ? 140 PRO A CG  1 
ATOM   838  C CD  . PRO A 1 116 ? 18.616 102.300 41.106 1.00 112.00 ? 140 PRO A CD  1 
ATOM   839  N N   . LEU A 1 117 ? 16.584 105.925 42.985 1.00 92.65  ? 141 LEU A N   1 
ATOM   840  C CA  . LEU A 1 117 ? 16.916 107.129 43.735 1.00 93.87  ? 141 LEU A CA  1 
ATOM   841  C C   . LEU A 1 117 ? 17.446 106.859 45.131 1.00 91.49  ? 141 LEU A C   1 
ATOM   842  O O   . LEU A 1 117 ? 17.271 105.772 45.685 1.00 94.05  ? 141 LEU A O   1 
ATOM   843  C CB  . LEU A 1 117 ? 15.674 108.023 43.849 1.00 102.35 ? 141 LEU A CB  1 
ATOM   844  C CG  . LEU A 1 117 ? 15.368 108.926 42.650 1.00 105.18 ? 141 LEU A CG  1 
ATOM   845  C CD1 . LEU A 1 117 ? 13.881 109.255 42.595 1.00 105.84 ? 141 LEU A CD1 1 
ATOM   846  C CD2 . LEU A 1 117 ? 16.215 110.188 42.734 1.00 106.34 ? 141 LEU A CD2 1 
ATOM   847  N N   . TRP A 1 118 ? 18.104 107.861 45.689 1.00 83.12  ? 142 TRP A N   1 
ATOM   848  C CA  . TRP A 1 118 ? 18.599 107.771 47.047 1.00 84.48  ? 142 TRP A CA  1 
ATOM   849  C C   . TRP A 1 118 ? 17.474 108.024 48.045 1.00 92.03  ? 142 TRP A C   1 
ATOM   850  O O   . TRP A 1 118 ? 16.576 108.839 47.788 1.00 85.36  ? 142 TRP A O   1 
ATOM   851  C CB  . TRP A 1 118 ? 19.671 108.830 47.300 1.00 86.05  ? 142 TRP A CB  1 
ATOM   852  C CG  . TRP A 1 118 ? 20.983 108.521 46.672 1.00 85.11  ? 142 TRP A CG  1 
ATOM   853  C CD1 . TRP A 1 118 ? 21.310 108.619 45.348 1.00 85.97  ? 142 TRP A CD1 1 
ATOM   854  C CD2 . TRP A 1 118 ? 22.156 108.056 47.339 1.00 84.54  ? 142 TRP A CD2 1 
ATOM   855  N NE1 . TRP A 1 118 ? 22.622 108.246 45.151 1.00 85.14  ? 142 TRP A NE1 1 
ATOM   856  C CE2 . TRP A 1 118 ? 23.164 107.895 46.357 1.00 84.59  ? 142 TRP A CE2 1 
ATOM   857  C CE3 . TRP A 1 118 ? 22.456 107.759 48.673 1.00 84.34  ? 142 TRP A CE3 1 
ATOM   858  C CZ2 . TRP A 1 118 ? 24.444 107.452 46.666 1.00 83.94  ? 142 TRP A CZ2 1 
ATOM   859  C CZ3 . TRP A 1 118 ? 23.727 107.319 48.982 1.00 84.77  ? 142 TRP A CZ3 1 
ATOM   860  C CH2 . TRP A 1 118 ? 24.708 107.169 47.982 1.00 85.33  ? 142 TRP A CH2 1 
ATOM   861  N N   . PRO A 1 119 ? 17.487 107.291 49.178 1.00 110.03 ? 143 PRO A N   1 
ATOM   862  C CA  . PRO A 1 119 ? 16.470 107.474 50.220 1.00 119.85 ? 143 PRO A CA  1 
ATOM   863  C C   . PRO A 1 119 ? 16.590 108.921 50.738 1.00 124.92 ? 143 PRO A C   1 
ATOM   864  O O   . PRO A 1 119 ? 17.704 109.440 50.920 1.00 130.43 ? 143 PRO A O   1 
ATOM   865  C CB  . PRO A 1 119 ? 16.896 106.494 51.306 1.00 125.52 ? 143 PRO A CB  1 
ATOM   866  C CG  . PRO A 1 119 ? 17.591 105.402 50.564 1.00 123.72 ? 143 PRO A CG  1 
ATOM   867  C CD  . PRO A 1 119 ? 18.330 106.107 49.454 1.00 119.79 ? 143 PRO A CD  1 
ATOM   868  N N   . LYS A 1 120 ? 15.441 109.555 50.964 1.00 129.78 ? 144 LYS A N   1 
ATOM   869  C CA  . LYS A 1 120 ? 15.382 110.928 51.463 1.00 125.27 ? 144 LYS A CA  1 
ATOM   870  C C   . LYS A 1 120 ? 16.024 111.033 52.842 1.00 121.79 ? 144 LYS A C   1 
ATOM   871  O O   . LYS A 1 120 ? 15.617 110.350 53.787 1.00 119.58 ? 144 LYS A O   1 
ATOM   872  C CB  . LYS A 1 120 ? 13.924 111.434 51.492 1.00 135.51 ? 144 LYS A CB  1 
ATOM   873  C CG  . LYS A 1 120 ? 12.834 110.345 51.496 1.00 144.52 ? 144 LYS A CG  1 
ATOM   874  C CD  . LYS A 1 120 ? 12.576 109.743 52.878 1.00 149.14 ? 144 LYS A CD  1 
ATOM   875  C CE  . LYS A 1 120 ? 11.600 108.572 52.799 1.00 150.64 ? 144 LYS A CE  1 
ATOM   876  N NZ  . LYS A 1 120 ? 11.258 108.021 54.142 1.00 151.15 ? 144 LYS A NZ  1 
ATOM   877  N N   . GLU A 1 121 ? 17.044 111.880 52.948 1.00 118.75 ? 145 GLU A N   1 
ATOM   878  C CA  . GLU A 1 121 ? 17.755 112.038 54.208 1.00 121.19 ? 145 GLU A CA  1 
ATOM   879  C C   . GLU A 1 121 ? 18.305 113.439 54.442 1.00 120.53 ? 145 GLU A C   1 
ATOM   880  O O   . GLU A 1 121 ? 18.934 114.036 53.562 1.00 118.50 ? 145 GLU A O   1 
ATOM   881  C CB  . GLU A 1 121 ? 18.904 111.001 54.308 1.00 133.47 ? 145 GLU A CB  1 
ATOM   882  C CG  . GLU A 1 121 ? 19.827 110.909 53.081 1.00 139.30 ? 145 GLU A CG  1 
ATOM   883  C CD  . GLU A 1 121 ? 20.815 109.750 53.157 1.00 141.35 ? 145 GLU A CD  1 
ATOM   884  O OE1 . GLU A 1 121 ? 20.381 108.605 53.404 1.00 142.16 ? 145 GLU A OE1 1 
ATOM   885  O OE2 . GLU A 1 121 ? 22.026 109.984 52.960 1.00 141.47 ? 145 GLU A OE2 1 
ATOM   886  N N   . ASN A 1 122 ? 18.022 113.970 55.631 1.00 135.60 ? 146 ASN A N   1 
ATOM   887  C CA  . ASN A 1 122 ? 18.548 115.272 56.041 1.00 137.31 ? 146 ASN A CA  1 
ATOM   888  C C   . ASN A 1 122 ? 19.879 115.002 56.765 1.00 135.29 ? 146 ASN A C   1 
ATOM   889  O O   . ASN A 1 122 ? 19.911 114.610 57.937 1.00 146.75 ? 146 ASN A O   1 
ATOM   890  C CB  . ASN A 1 122 ? 17.557 115.995 56.956 1.00 119.72 ? 146 ASN A CB  1 
ATOM   891  C CG  . ASN A 1 122 ? 17.856 117.487 57.069 1.00 112.91 ? 146 ASN A CG  1 
ATOM   892  O OD1 . ASN A 1 122 ? 18.754 118.010 56.402 1.00 109.38 ? 146 ASN A OD1 1 
ATOM   893  N ND2 . ASN A 1 122 ? 17.097 118.177 57.910 1.00 108.79 ? 146 ASN A ND2 1 
ATOM   894  N N   . LEU A 1 123 ? 20.976 115.223 56.042 1.00 106.96 ? 147 LEU A N   1 
ATOM   895  C CA  . LEU A 1 123 ? 22.308 114.928 56.553 1.00 103.42 ? 147 LEU A CA  1 
ATOM   896  C C   . LEU A 1 123 ? 22.812 115.875 57.622 1.00 107.58 ? 147 LEU A C   1 
ATOM   897  O O   . LEU A 1 123 ? 22.496 117.064 57.619 1.00 99.87  ? 147 LEU A O   1 
ATOM   898  C CB  . LEU A 1 123 ? 23.328 114.878 55.390 1.00 87.70  ? 147 LEU A CB  1 
ATOM   899  C CG  . LEU A 1 123 ? 23.290 113.665 54.439 1.00 80.24  ? 147 LEU A CG  1 
ATOM   900  C CD1 . LEU A 1 123 ? 24.227 113.896 53.273 1.00 75.49  ? 147 LEU A CD1 1 
ATOM   901  C CD2 . LEU A 1 123 ? 23.658 112.374 55.172 1.00 75.84  ? 147 LEU A CD2 1 
ATOM   902  N N   . ASP A 1 124 ? 23.583 115.325 58.551 1.00 142.58 ? 148 ASP A N   1 
ATOM   903  C CA  . ASP A 1 124 ? 24.203 116.116 59.596 1.00 151.66 ? 148 ASP A CA  1 
ATOM   904  C C   . ASP A 1 124 ? 25.417 116.872 59.054 1.00 148.56 ? 148 ASP A C   1 
ATOM   905  O O   . ASP A 1 124 ? 26.170 116.341 58.227 1.00 157.53 ? 148 ASP A O   1 
ATOM   906  C CB  . ASP A 1 124 ? 24.713 115.208 60.735 1.00 139.82 ? 148 ASP A CB  1 
ATOM   907  C CG  . ASP A 1 124 ? 23.597 114.677 61.623 1.00 141.53 ? 148 ASP A CG  1 
ATOM   908  O OD1 . ASP A 1 124 ? 23.780 113.599 62.234 1.00 141.87 ? 148 ASP A OD1 1 
ATOM   909  O OD2 . ASP A 1 124 ? 22.541 115.340 61.723 1.00 142.15 ? 148 ASP A OD2 1 
ATOM   910  N N   . PRO A 1 125 ? 25.576 118.149 59.457 1.00 115.06 ? 149 PRO A N   1 
ATOM   911  C CA  . PRO A 1 125 ? 26.740 118.933 59.019 1.00 106.14 ? 149 PRO A CA  1 
ATOM   912  C C   . PRO A 1 125 ? 27.954 118.220 59.654 1.00 101.15 ? 149 PRO A C   1 
ATOM   913  O O   . PRO A 1 125 ? 27.929 117.863 60.842 1.00 108.25 ? 149 PRO A O   1 
ATOM   914  C CB  . PRO A 1 125 ? 26.511 120.303 59.644 1.00 93.24  ? 149 PRO A CB  1 
ATOM   915  C CG  . PRO A 1 125 ? 25.481 120.081 60.713 1.00 90.01  ? 149 PRO A CG  1 
ATOM   916  C CD  . PRO A 1 125 ? 24.607 118.991 60.179 1.00 98.35  ? 149 PRO A CD  1 
ATOM   917  N N   . VAL A 1 126 ? 29.011 118.025 58.874 1.00 106.59 ? 150 VAL A N   1 
ATOM   918  C CA  . VAL A 1 126 ? 30.156 117.278 59.367 1.00 102.75 ? 150 VAL A CA  1 
ATOM   919  C C   . VAL A 1 126 ? 31.201 118.143 60.034 1.00 99.96  ? 150 VAL A C   1 
ATOM   920  O O   . VAL A 1 126 ? 31.779 119.038 59.415 1.00 95.41  ? 150 VAL A O   1 
ATOM   921  C CB  . VAL A 1 126 ? 30.800 116.427 58.228 1.00 104.84 ? 150 VAL A CB  1 
ATOM   922  C CG1 . VAL A 1 126 ? 31.987 115.643 58.769 1.00 106.27 ? 150 VAL A CG1 1 
ATOM   923  C CG2 . VAL A 1 126 ? 29.767 115.466 57.641 1.00 106.37 ? 150 VAL A CG2 1 
ATOM   924  N N   . VAL A 1 127 ? 31.411 117.878 61.321 1.00 111.36 ? 151 VAL A N   1 
ATOM   925  C CA  . VAL A 1 127 ? 32.397 118.602 62.110 1.00 118.94 ? 151 VAL A CA  1 
ATOM   926  C C   . VAL A 1 127 ? 33.478 117.626 62.581 1.00 123.78 ? 151 VAL A C   1 
ATOM   927  O O   . VAL A 1 127 ? 33.190 116.638 63.266 1.00 132.10 ? 151 VAL A O   1 
ATOM   928  C CB  . VAL A 1 127 ? 31.753 119.296 63.349 1.00 106.08 ? 151 VAL A CB  1 
ATOM   929  C CG1 . VAL A 1 127 ? 32.789 120.152 64.070 1.00 99.00  ? 151 VAL A CG1 1 
ATOM   930  C CG2 . VAL A 1 127 ? 30.568 120.156 62.922 1.00 98.85  ? 151 VAL A CG2 1 
ATOM   931  N N   . VAL A 1 128 ? 34.720 117.904 62.188 1.00 113.45 ? 152 VAL A N   1 
ATOM   932  C CA  . VAL A 1 128 ? 35.855 117.077 62.572 1.00 116.12 ? 152 VAL A CA  1 
ATOM   933  C C   . VAL A 1 128 ? 37.068 117.941 62.925 1.00 114.86 ? 152 VAL A C   1 
ATOM   934  O O   . VAL A 1 128 ? 37.286 119.000 62.321 1.00 113.94 ? 152 VAL A O   1 
ATOM   935  C CB  . VAL A 1 128 ? 36.221 116.056 61.431 1.00 107.55 ? 152 VAL A CB  1 
ATOM   936  C CG1 . VAL A 1 128 ? 36.752 116.778 60.190 1.00 104.46 ? 152 VAL A CG1 1 
ATOM   937  C CG2 . VAL A 1 128 ? 37.226 115.026 61.941 1.00 104.99 ? 152 VAL A CG2 1 
ATOM   938  N N   . GLN A 1 129 ? 37.832 117.501 63.926 1.00 123.68 ? 153 GLN A N   1 
ATOM   939  C CA  . GLN A 1 129 ? 39.045 118.209 64.338 1.00 124.46 ? 153 GLN A CA  1 
ATOM   940  C C   . GLN A 1 129 ? 40.093 118.153 63.220 1.00 118.42 ? 153 GLN A C   1 
ATOM   941  O O   . GLN A 1 129 ? 40.223 117.144 62.525 1.00 121.79 ? 153 GLN A O   1 
ATOM   942  C CB  . GLN A 1 129 ? 39.612 117.601 65.628 1.00 126.45 ? 153 GLN A CB  1 
ATOM   943  C CG  . GLN A 1 129 ? 38.806 117.941 66.875 1.00 131.20 ? 153 GLN A CG  1 
ATOM   944  C CD  . GLN A 1 129 ? 39.346 117.271 68.130 1.00 133.24 ? 153 GLN A CD  1 
ATOM   945  O OE1 . GLN A 1 129 ? 40.559 117.235 68.363 1.00 133.65 ? 153 GLN A OE1 1 
ATOM   946  N NE2 . GLN A 1 129 ? 38.443 116.749 68.956 1.00 133.85 ? 153 GLN A NE2 1 
ATOM   947  N N   . GLU A 1 130 ? 40.821 119.253 63.044 1.00 113.86 ? 154 GLU A N   1 
ATOM   948  C CA  . GLU A 1 130 ? 41.848 119.352 62.011 1.00 110.26 ? 154 GLU A CA  1 
ATOM   949  C C   . GLU A 1 130 ? 42.938 118.322 62.261 1.00 109.91 ? 154 GLU A C   1 
ATOM   950  O O   . GLU A 1 130 ? 43.300 118.067 63.411 1.00 99.82  ? 154 GLU A O   1 
ATOM   951  C CB  . GLU A 1 130 ? 42.445 120.758 61.997 1.00 102.79 ? 154 GLU A CB  1 
ATOM   952  C CG  . GLU A 1 130 ? 43.352 121.041 60.813 1.00 108.66 ? 154 GLU A CG  1 
ATOM   953  C CD  . GLU A 1 130 ? 44.103 122.352 60.955 1.00 111.86 ? 154 GLU A CD  1 
ATOM   954  O OE1 . GLU A 1 130 ? 43.858 123.086 61.941 1.00 112.22 ? 154 GLU A OE1 1 
ATOM   955  O OE2 . GLU A 1 130 ? 44.939 122.648 60.076 1.00 113.02 ? 154 GLU A OE2 1 
ATOM   956  N N   . GLY A 1 131 ? 43.443 117.729 61.177 1.00 104.46 ? 155 GLY A N   1 
ATOM   957  C CA  . GLY A 1 131 ? 44.475 116.703 61.264 1.00 115.67 ? 155 GLY A CA  1 
ATOM   958  C C   . GLY A 1 131 ? 43.932 115.307 61.555 1.00 118.53 ? 155 GLY A C   1 
ATOM   959  O O   . GLY A 1 131 ? 44.584 114.303 61.248 1.00 122.06 ? 155 GLY A O   1 
ATOM   960  N N   . ALA A 1 132 ? 42.746 115.250 62.163 1.00 110.75 ? 156 ALA A N   1 
ATOM   961  C CA  . ALA A 1 132 ? 42.088 113.984 62.486 1.00 107.65 ? 156 ALA A CA  1 
ATOM   962  C C   . ALA A 1 132 ? 41.518 113.329 61.216 1.00 109.21 ? 156 ALA A C   1 
ATOM   963  O O   . ALA A 1 132 ? 41.320 113.995 60.198 1.00 107.47 ? 156 ALA A O   1 
ATOM   964  C CB  . ALA A 1 132 ? 40.982 114.216 63.523 1.00 109.13 ? 156 ALA A CB  1 
ATOM   965  N N   . PRO A 1 133 ? 41.263 112.008 61.260 1.00 107.05 ? 157 PRO A N   1 
ATOM   966  C CA  . PRO A 1 133 ? 40.724 111.293 60.099 1.00 104.33 ? 157 PRO A CA  1 
ATOM   967  C C   . PRO A 1 133 ? 39.207 111.362 59.961 1.00 96.67  ? 157 PRO A C   1 
ATOM   968  O O   . PRO A 1 133 ? 38.507 111.604 60.941 1.00 90.48  ? 157 PRO A O   1 
ATOM   969  C CB  . PRO A 1 133 ? 41.189 109.860 60.331 1.00 128.70 ? 157 PRO A CB  1 
ATOM   970  C CG  . PRO A 1 133 ? 41.204 109.726 61.820 1.00 135.47 ? 157 PRO A CG  1 
ATOM   971  C CD  . PRO A 1 133 ? 41.566 111.084 62.373 1.00 130.71 ? 157 PRO A CD  1 
ATOM   972  N N   . LEU A 1 134 ? 38.712 111.132 58.743 1.00 95.69  ? 158 LEU A N   1 
ATOM   973  C CA  . LEU A 1 134 ? 37.274 111.118 58.464 1.00 91.58  ? 158 LEU A CA  1 
ATOM   974  C C   . LEU A 1 134 ? 36.927 110.276 57.233 1.00 89.59  ? 158 LEU A C   1 
ATOM   975  O O   . LEU A 1 134 ? 37.660 110.262 56.238 1.00 86.81  ? 158 LEU A O   1 
ATOM   976  C CB  . LEU A 1 134 ? 36.745 112.545 58.255 1.00 106.06 ? 158 LEU A CB  1 
ATOM   977  C CG  . LEU A 1 134 ? 35.243 112.742 57.976 1.00 106.26 ? 158 LEU A CG  1 
ATOM   978  C CD1 . LEU A 1 134 ? 34.406 112.487 59.222 1.00 106.56 ? 158 LEU A CD1 1 
ATOM   979  C CD2 . LEU A 1 134 ? 35.009 114.153 57.466 1.00 106.99 ? 158 LEU A CD2 1 
ATOM   980  N N   . THR A 1 135 ? 35.803 109.570 57.321 1.00 86.12  ? 159 THR A N   1 
ATOM   981  C CA  . THR A 1 135 ? 35.312 108.767 56.218 1.00 81.74  ? 159 THR A CA  1 
ATOM   982  C C   . THR A 1 135 ? 33.901 109.196 55.821 1.00 82.42  ? 159 THR A C   1 
ATOM   983  O O   . THR A 1 135 ? 32.946 109.005 56.579 1.00 85.79  ? 159 THR A O   1 
ATOM   984  C CB  . THR A 1 135 ? 35.284 107.260 56.574 1.00 76.01  ? 159 THR A CB  1 
ATOM   985  O OG1 . THR A 1 135 ? 36.594 106.846 56.979 1.00 71.16  ? 159 THR A OG1 1 
ATOM   986  C CG2 . THR A 1 135 ? 34.844 106.427 55.375 1.00 69.34  ? 159 THR A CG2 1 
ATOM   987  N N   . LEU A 1 136 ? 33.782 109.809 54.646 1.00 79.86  ? 160 LEU A N   1 
ATOM   988  C CA  . LEU A 1 136 ? 32.468 110.171 54.124 1.00 76.40  ? 160 LEU A CA  1 
ATOM   989  C C   . LEU A 1 136 ? 31.925 108.944 53.398 1.00 76.54  ? 160 LEU A C   1 
ATOM   990  O O   . LEU A 1 136 ? 32.261 108.678 52.239 1.00 76.14  ? 160 LEU A O   1 
ATOM   991  C CB  . LEU A 1 136 ? 32.542 111.364 53.159 1.00 71.69  ? 160 LEU A CB  1 
ATOM   992  C CG  . LEU A 1 136 ? 32.821 112.748 53.765 1.00 69.90  ? 160 LEU A CG  1 
ATOM   993  C CD1 . LEU A 1 136 ? 32.942 113.770 52.651 1.00 70.45  ? 160 LEU A CD1 1 
ATOM   994  C CD2 . LEU A 1 136 ? 31.732 113.149 54.744 1.00 69.13  ? 160 LEU A CD2 1 
ATOM   995  N N   . GLN A 1 137 ? 31.094 108.189 54.108 1.00 76.40  ? 161 GLN A N   1 
ATOM   996  C CA  . GLN A 1 137 ? 30.497 106.980 53.560 1.00 81.11  ? 161 GLN A CA  1 
ATOM   997  C C   . GLN A 1 137 ? 29.423 107.309 52.532 1.00 79.92  ? 161 GLN A C   1 
ATOM   998  O O   . GLN A 1 137 ? 28.524 108.112 52.790 1.00 78.46  ? 161 GLN A O   1 
ATOM   999  C CB  . GLN A 1 137 ? 29.930 106.108 54.692 1.00 99.39  ? 161 GLN A CB  1 
ATOM   1000 C CG  . GLN A 1 137 ? 29.197 106.877 55.779 1.00 106.59 ? 161 GLN A CG  1 
ATOM   1001 C CD  . GLN A 1 137 ? 29.494 106.345 57.171 1.00 109.58 ? 161 GLN A CD  1 
ATOM   1002 O OE1 . GLN A 1 137 ? 29.526 105.134 57.395 1.00 109.50 ? 161 GLN A OE1 1 
ATOM   1003 N NE2 . GLN A 1 137 ? 29.708 107.255 58.115 1.00 110.12 ? 161 GLN A NE2 1 
ATOM   1004 N N   . CYS A 1 138 ? 29.541 106.699 51.355 1.00 80.67  ? 162 CYS A N   1 
ATOM   1005 C CA  . CYS A 1 138 ? 28.588 106.924 50.283 1.00 81.12  ? 162 CYS A CA  1 
ATOM   1006 C C   . CYS A 1 138 ? 27.352 106.046 50.473 1.00 82.79  ? 162 CYS A C   1 
ATOM   1007 O O   . CYS A 1 138 ? 26.250 106.562 50.657 1.00 81.89  ? 162 CYS A O   1 
ATOM   1008 C CB  . CYS A 1 138 ? 29.238 106.646 48.915 1.00 85.96  ? 162 CYS A CB  1 
ATOM   1009 S SG  . CYS A 1 138 ? 28.158 106.931 47.474 1.00 85.25  ? 162 CYS A SG  1 
ATOM   1010 N N   . ASN A 1 139 ? 27.551 104.728 50.474 1.00 93.10  ? 163 ASN A N   1 
ATOM   1011 C CA  . ASN A 1 139 ? 26.470 103.734 50.594 1.00 96.78  ? 163 ASN A CA  1 
ATOM   1012 C C   . ASN A 1 139 ? 25.371 103.975 49.554 1.00 95.43  ? 163 ASN A C   1 
ATOM   1013 O O   . ASN A 1 139 ? 24.277 104.438 49.868 1.00 93.89  ? 163 ASN A O   1 
ATOM   1014 C CB  . ASN A 1 139 ? 25.886 103.707 52.018 1.00 104.64 ? 163 ASN A CB  1 
ATOM   1015 C CG  . ASN A 1 139 ? 26.852 103.099 53.034 1.00 114.57 ? 163 ASN A CG  1 
ATOM   1016 O OD1 . ASN A 1 139 ? 27.973 102.707 52.691 1.00 119.33 ? 163 ASN A OD1 1 
ATOM   1017 N ND2 . ASN A 1 139 ? 26.421 103.020 54.289 1.00 119.02 ? 163 ASN A ND2 1 
ATOM   1018 N N   . PRO A 1 140 ? 25.653 103.626 48.294 1.00 92.21  ? 164 PRO A N   1 
ATOM   1019 C CA  . PRO A 1 140 ? 24.688 103.815 47.213 1.00 93.11  ? 164 PRO A CA  1 
ATOM   1020 C C   . PRO A 1 140 ? 23.568 102.796 47.161 1.00 96.91  ? 164 PRO A C   1 
ATOM   1021 O O   . PRO A 1 140 ? 23.646 101.758 47.822 1.00 88.40  ? 164 PRO A O   1 
ATOM   1022 C CB  . PRO A 1 140 ? 25.556 103.648 45.954 1.00 96.89  ? 164 PRO A CB  1 
ATOM   1023 C CG  . PRO A 1 140 ? 26.578 102.641 46.361 1.00 98.02  ? 164 PRO A CG  1 
ATOM   1024 C CD  . PRO A 1 140 ? 26.889 102.974 47.803 1.00 96.31  ? 164 PRO A CD  1 
ATOM   1025 N N   . PRO A 1 141 ? 22.477 103.121 46.424 1.00 121.85 ? 165 PRO A N   1 
ATOM   1026 C CA  . PRO A 1 141 ? 21.366 102.174 46.254 1.00 126.97 ? 165 PRO A CA  1 
ATOM   1027 C C   . PRO A 1 141 ? 21.949 101.158 45.220 1.00 124.55 ? 165 PRO A C   1 
ATOM   1028 O O   . PRO A 1 141 ? 22.795 101.526 44.382 1.00 135.09 ? 165 PRO A O   1 
ATOM   1029 C CB  . PRO A 1 141 ? 20.256 103.014 45.645 1.00 125.48 ? 165 PRO A CB  1 
ATOM   1030 C CG  . PRO A 1 141 ? 20.950 104.179 45.029 1.00 125.81 ? 165 PRO A CG  1 
ATOM   1031 C CD  . PRO A 1 141 ? 22.097 104.472 45.956 1.00 119.26 ? 165 PRO A CD  1 
ATOM   1032 N N   . PRO A 1 142 ? 21.461 99.899  45.239 1.00 120.44 ? 166 PRO A N   1 
ATOM   1033 C CA  . PRO A 1 142 ? 21.940 98.842  44.346 1.00 109.65 ? 166 PRO A CA  1 
ATOM   1034 C C   . PRO A 1 142 ? 22.131 99.156  42.875 1.00 96.94  ? 166 PRO A C   1 
ATOM   1035 O O   . PRO A 1 142 ? 23.170 99.684  42.484 1.00 90.90  ? 166 PRO A O   1 
ATOM   1036 C CB  . PRO A 1 142 ? 20.956 97.694  44.581 1.00 128.39 ? 166 PRO A CB  1 
ATOM   1037 C CG  . PRO A 1 142 ? 20.451 97.928  45.965 1.00 134.82 ? 166 PRO A CG  1 
ATOM   1038 C CD  . PRO A 1 142 ? 20.321 99.428  46.049 1.00 134.58 ? 166 PRO A CD  1 
ATOM   1039 N N   . GLY A 1 143 ? 21.126 98.844  42.066 1.00 87.43  ? 167 GLY A N   1 
ATOM   1040 C CA  . GLY A 1 143 ? 21.243 99.032  40.625 1.00 85.91  ? 167 GLY A CA  1 
ATOM   1041 C C   . GLY A 1 143 ? 22.090 97.920  40.006 1.00 89.46  ? 167 GLY A C   1 
ATOM   1042 O O   . GLY A 1 143 ? 23.054 97.445  40.621 1.00 80.71  ? 167 GLY A O   1 
ATOM   1043 N N   . LEU A 1 144 ? 21.748 97.517  38.784 1.00 94.10  ? 168 LEU A N   1 
ATOM   1044 C CA  . LEU A 1 144 ? 22.446 96.412  38.120 1.00 102.58 ? 168 LEU A CA  1 
ATOM   1045 C C   . LEU A 1 144 ? 22.844 96.755  36.685 1.00 102.73 ? 168 LEU A C   1 
ATOM   1046 O O   . LEU A 1 144 ? 22.025 97.221  35.902 1.00 105.61 ? 168 LEU A O   1 
ATOM   1047 C CB  . LEU A 1 144 ? 21.566 95.145  38.139 1.00 119.08 ? 168 LEU A CB  1 
ATOM   1048 C CG  . LEU A 1 144 ? 21.086 94.600  39.502 1.00 121.73 ? 168 LEU A CG  1 
ATOM   1049 C CD1 . LEU A 1 144 ? 19.675 95.098  39.821 1.00 122.82 ? 168 LEU A CD1 1 
ATOM   1050 C CD2 . LEU A 1 144 ? 21.117 93.072  39.505 1.00 122.99 ? 168 LEU A CD2 1 
ATOM   1051 N N   . PRO A 1 145 ? 24.137 96.575  36.346 1.00 94.86  ? 169 PRO A N   1 
ATOM   1052 C CA  . PRO A 1 145 ? 25.176 96.147  37.291 1.00 88.26  ? 169 PRO A CA  1 
ATOM   1053 C C   . PRO A 1 145 ? 25.608 97.342  38.124 1.00 81.88  ? 169 PRO A C   1 
ATOM   1054 O O   . PRO A 1 145 ? 25.076 98.440  37.951 1.00 79.23  ? 169 PRO A O   1 
ATOM   1055 C CB  . PRO A 1 145 ? 26.291 95.639  36.382 1.00 89.22  ? 169 PRO A CB  1 
ATOM   1056 C CG  . PRO A 1 145 ? 26.159 96.466  35.156 1.00 93.06  ? 169 PRO A CG  1 
ATOM   1057 C CD  . PRO A 1 145 ? 24.678 96.763  34.991 1.00 92.65  ? 169 PRO A CD  1 
ATOM   1058 N N   . SER A 1 146 ? 26.583 97.137  39.007 1.00 73.61  ? 170 SER A N   1 
ATOM   1059 C CA  . SER A 1 146 ? 27.043 98.194  39.894 1.00 68.81  ? 170 SER A CA  1 
ATOM   1060 C C   . SER A 1 146 ? 27.346 99.498  39.184 1.00 65.61  ? 170 SER A C   1 
ATOM   1061 O O   . SER A 1 146 ? 27.975 99.511  38.130 1.00 62.50  ? 170 SER A O   1 
ATOM   1062 C CB  . SER A 1 146 ? 28.274 97.731  40.681 1.00 71.36  ? 170 SER A CB  1 
ATOM   1063 O OG  . SER A 1 146 ? 27.894 96.819  41.696 1.00 75.38  ? 170 SER A OG  1 
ATOM   1064 N N   . PRO A 1 147 ? 26.862 100.611 39.743 1.00 68.44  ? 171 PRO A N   1 
ATOM   1065 C CA  . PRO A 1 147 ? 27.090 101.937 39.175 1.00 69.78  ? 171 PRO A CA  1 
ATOM   1066 C C   . PRO A 1 147 ? 28.523 102.410 39.409 1.00 70.10  ? 171 PRO A C   1 
ATOM   1067 O O   . PRO A 1 147 ? 29.102 102.136 40.459 1.00 73.16  ? 171 PRO A O   1 
ATOM   1068 C CB  . PRO A 1 147 ? 26.117 102.830 39.960 1.00 58.10  ? 171 PRO A CB  1 
ATOM   1069 C CG  . PRO A 1 147 ? 25.936 102.126 41.259 1.00 54.77  ? 171 PRO A CG  1 
ATOM   1070 C CD  . PRO A 1 147 ? 25.941 100.671 40.896 1.00 57.86  ? 171 PRO A CD  1 
ATOM   1071 N N   . VAL A 1 148 ? 29.086 103.108 38.424 1.00 59.22  ? 172 VAL A N   1 
ATOM   1072 C CA  . VAL A 1 148 ? 30.396 103.745 38.575 1.00 55.65  ? 172 VAL A CA  1 
ATOM   1073 C C   . VAL A 1 148 ? 30.163 104.956 39.500 1.00 55.22  ? 172 VAL A C   1 
ATOM   1074 O O   . VAL A 1 148 ? 29.184 105.696 39.356 1.00 56.14  ? 172 VAL A O   1 
ATOM   1075 C CB  . VAL A 1 148 ? 30.971 104.205 37.207 1.00 49.23  ? 172 VAL A CB  1 
ATOM   1076 C CG1 . VAL A 1 148 ? 32.246 105.026 37.396 1.00 45.63  ? 172 VAL A CG1 1 
ATOM   1077 C CG2 . VAL A 1 148 ? 31.262 102.981 36.339 1.00 47.99  ? 172 VAL A CG2 1 
ATOM   1078 N N   . ILE A 1 149 ? 31.062 105.143 40.457 1.00 54.82  ? 173 ILE A N   1 
ATOM   1079 C CA  . ILE A 1 149 ? 30.914 106.194 41.445 1.00 57.21  ? 173 ILE A CA  1 
ATOM   1080 C C   . ILE A 1 149 ? 32.049 107.201 41.426 1.00 57.08  ? 173 ILE A C   1 
ATOM   1081 O O   . ILE A 1 149 ? 33.197 106.856 41.129 1.00 56.21  ? 173 ILE A O   1 
ATOM   1082 C CB  . ILE A 1 149 ? 30.805 105.560 42.879 1.00 62.26  ? 173 ILE A CB  1 
ATOM   1083 C CG1 . ILE A 1 149 ? 29.488 104.782 42.997 1.00 65.07  ? 173 ILE A CG1 1 
ATOM   1084 C CG2 . ILE A 1 149 ? 30.919 106.637 43.968 1.00 61.63  ? 173 ILE A CG2 1 
ATOM   1085 C CD1 . ILE A 1 149 ? 29.401 103.845 44.196 1.00 75.83  ? 173 ILE A CD1 1 
ATOM   1086 N N   . PHE A 1 150 ? 31.700 108.460 41.688 1.00 61.20  ? 174 PHE A N   1 
ATOM   1087 C CA  . PHE A 1 150 ? 32.672 109.543 41.817 1.00 65.51  ? 174 PHE A CA  1 
ATOM   1088 C C   . PHE A 1 150 ? 32.096 110.650 42.682 1.00 65.60  ? 174 PHE A C   1 
ATOM   1089 O O   . PHE A 1 150 ? 30.893 110.685 42.944 1.00 61.41  ? 174 PHE A O   1 
ATOM   1090 C CB  . PHE A 1 150 ? 33.120 110.101 40.469 1.00 76.19  ? 174 PHE A CB  1 
ATOM   1091 C CG  . PHE A 1 150 ? 32.017 110.248 39.478 1.00 86.50  ? 174 PHE A CG  1 
ATOM   1092 C CD1 . PHE A 1 150 ? 31.122 111.308 39.561 1.00 90.94  ? 174 PHE A CD1 1 
ATOM   1093 C CD2 . PHE A 1 150 ? 31.870 109.318 38.455 1.00 90.68  ? 174 PHE A CD2 1 
ATOM   1094 C CE1 . PHE A 1 150 ? 30.089 111.442 38.636 1.00 92.61  ? 174 PHE A CE1 1 
ATOM   1095 C CE2 . PHE A 1 150 ? 30.847 109.438 37.529 1.00 92.83  ? 174 PHE A CE2 1 
ATOM   1096 C CZ  . PHE A 1 150 ? 29.951 110.506 37.618 1.00 93.17  ? 174 PHE A CZ  1 
ATOM   1097 N N   . TRP A 1 151 ? 32.967 111.551 43.126 1.00 70.28  ? 175 TRP A N   1 
ATOM   1098 C CA  . TRP A 1 151 ? 32.568 112.642 43.995 1.00 72.45  ? 175 TRP A CA  1 
ATOM   1099 C C   . TRP A 1 151 ? 32.726 113.977 43.290 1.00 75.02  ? 175 TRP A C   1 
ATOM   1100 O O   . TRP A 1 151 ? 33.707 114.218 42.584 1.00 73.62  ? 175 TRP A O   1 
ATOM   1101 C CB  . TRP A 1 151 ? 33.388 112.603 45.295 1.00 69.46  ? 175 TRP A CB  1 
ATOM   1102 C CG  . TRP A 1 151 ? 33.105 111.390 46.160 1.00 69.50  ? 175 TRP A CG  1 
ATOM   1103 C CD1 . TRP A 1 151 ? 33.585 110.124 45.981 1.00 70.39  ? 175 TRP A CD1 1 
ATOM   1104 C CD2 . TRP A 1 151 ? 32.272 111.339 47.330 1.00 68.98  ? 175 TRP A CD2 1 
ATOM   1105 N NE1 . TRP A 1 151 ? 33.105 109.289 46.966 1.00 70.34  ? 175 TRP A NE1 1 
ATOM   1106 C CE2 . TRP A 1 151 ? 32.298 110.009 47.805 1.00 69.61  ? 175 TRP A CE2 1 
ATOM   1107 C CE3 . TRP A 1 151 ? 31.506 112.289 48.021 1.00 68.71  ? 175 TRP A CE3 1 
ATOM   1108 C CZ2 . TRP A 1 151 ? 31.592 109.604 48.940 1.00 70.14  ? 175 TRP A CZ2 1 
ATOM   1109 C CZ3 . TRP A 1 151 ? 30.803 111.887 49.150 1.00 69.16  ? 175 TRP A CZ3 1 
ATOM   1110 C CH2 . TRP A 1 151 ? 30.852 110.555 49.598 1.00 70.41  ? 175 TRP A CH2 1 
ATOM   1111 N N   . MET A 1 152 ? 31.728 114.833 43.474 1.00 77.67  ? 176 MET A N   1 
ATOM   1112 C CA  . MET A 1 152 ? 31.707 116.153 42.860 1.00 79.84  ? 176 MET A CA  1 
ATOM   1113 C C   . MET A 1 152 ? 31.159 117.170 43.851 1.00 82.29  ? 176 MET A C   1 
ATOM   1114 O O   . MET A 1 152 ? 30.441 116.810 44.790 1.00 80.87  ? 176 MET A O   1 
ATOM   1115 C CB  . MET A 1 152 ? 30.768 116.148 41.641 1.00 87.03  ? 176 MET A CB  1 
ATOM   1116 C CG  . MET A 1 152 ? 31.026 115.040 40.646 1.00 91.35  ? 176 MET A CG  1 
ATOM   1117 S SD  . MET A 1 152 ? 32.326 115.461 39.486 1.00 94.55  ? 176 MET A SD  1 
ATOM   1118 C CE  . MET A 1 152 ? 31.351 115.926 38.072 1.00 95.72  ? 176 MET A CE  1 
ATOM   1119 N N   . SER A 1 153 ? 31.536 118.431 43.653 1.00 88.61  ? 177 SER A N   1 
ATOM   1120 C CA  . SER A 1 153 ? 30.949 119.530 44.415 1.00 91.35  ? 177 SER A CA  1 
ATOM   1121 C C   . SER A 1 153 ? 29.472 119.618 43.951 1.00 88.63  ? 177 SER A C   1 
ATOM   1122 O O   . SER A 1 153 ? 29.145 119.233 42.823 1.00 88.91  ? 177 SER A O   1 
ATOM   1123 C CB  . SER A 1 153 ? 31.662 120.843 44.088 1.00 110.99 ? 177 SER A CB  1 
ATOM   1124 O OG  . SER A 1 153 ? 31.023 121.947 44.714 1.00 120.09 ? 177 SER A OG  1 
ATOM   1125 N N   . SER A 1 154 ? 28.590 120.116 44.818 1.00 85.23  ? 178 SER A N   1 
ATOM   1126 C CA  . SER A 1 154 ? 27.165 120.219 44.492 1.00 81.39  ? 178 SER A CA  1 
ATOM   1127 C C   . SER A 1 154 ? 26.897 121.108 43.282 1.00 80.62  ? 178 SER A C   1 
ATOM   1128 O O   . SER A 1 154 ? 25.811 121.068 42.710 1.00 79.58  ? 178 SER A O   1 
ATOM   1129 C CB  . SER A 1 154 ? 26.365 120.718 45.700 1.00 85.18  ? 178 SER A CB  1 
ATOM   1130 O OG  . SER A 1 154 ? 26.719 122.046 46.041 1.00 86.26  ? 178 SER A OG  1 
ATOM   1131 N N   . SER A 1 155 ? 27.893 121.907 42.906 1.00 78.97  ? 179 SER A N   1 
ATOM   1132 C CA  . SER A 1 155 ? 27.807 122.771 41.738 1.00 87.50  ? 179 SER A CA  1 
ATOM   1133 C C   . SER A 1 155 ? 28.606 122.196 40.554 1.00 88.68  ? 179 SER A C   1 
ATOM   1134 O O   . SER A 1 155 ? 29.024 122.926 39.652 1.00 80.76  ? 179 SER A O   1 
ATOM   1135 C CB  . SER A 1 155 ? 28.274 124.185 42.076 1.00 97.81  ? 179 SER A CB  1 
ATOM   1136 O OG  . SER A 1 155 ? 29.547 124.168 42.689 1.00 108.97 ? 179 SER A OG  1 
ATOM   1137 N N   . MET A 1 156 ? 28.821 120.880 40.591 1.00 104.28 ? 180 MET A N   1 
ATOM   1138 C CA  . MET A 1 156 ? 29.463 120.100 39.522 1.00 109.31 ? 180 MET A CA  1 
ATOM   1139 C C   . MET A 1 156 ? 30.957 120.258 39.262 1.00 110.69 ? 180 MET A C   1 
ATOM   1140 O O   . MET A 1 156 ? 31.440 119.973 38.157 1.00 116.17 ? 180 MET A O   1 
ATOM   1141 C CB  . MET A 1 156 ? 28.660 120.247 38.208 1.00 105.99 ? 180 MET A CB  1 
ATOM   1142 C CG  . MET A 1 156 ? 27.250 119.643 38.254 1.00 106.97 ? 180 MET A CG  1 
ATOM   1143 S SD  . MET A 1 156 ? 27.210 117.836 38.140 1.00 107.06 ? 180 MET A SD  1 
ATOM   1144 C CE  . MET A 1 156 ? 27.240 117.366 39.876 1.00 107.15 ? 180 MET A CE  1 
ATOM   1145 N N   . GLU A 1 157 ? 31.690 120.712 40.278 1.00 95.38  ? 181 GLU A N   1 
ATOM   1146 C CA  . GLU A 1 157 ? 33.145 120.782 40.166 1.00 90.68  ? 181 GLU A CA  1 
ATOM   1147 C C   . GLU A 1 157 ? 33.728 119.444 40.631 1.00 81.64  ? 181 GLU A C   1 
ATOM   1148 O O   . GLU A 1 157 ? 33.324 118.903 41.671 1.00 69.05  ? 181 GLU A O   1 
ATOM   1149 C CB  . GLU A 1 157 ? 33.739 121.904 41.018 1.00 132.52 ? 181 GLU A CB  1 
ATOM   1150 C CG  . GLU A 1 157 ? 33.411 123.305 40.536 1.00 159.83 ? 181 GLU A CG  1 
ATOM   1151 C CD  . GLU A 1 157 ? 32.247 123.917 41.292 1.00 171.91 ? 181 GLU A CD  1 
ATOM   1152 O OE1 . GLU A 1 157 ? 32.268 123.891 42.546 1.00 175.27 ? 181 GLU A OE1 1 
ATOM   1153 O OE2 . GLU A 1 157 ? 31.317 124.431 40.633 1.00 175.61 ? 181 GLU A OE2 1 
ATOM   1154 N N   . PRO A 1 158 ? 34.685 118.891 39.859 1.00 90.16  ? 182 PRO A N   1 
ATOM   1155 C CA  . PRO A 1 158 ? 35.317 117.611 40.208 1.00 88.98  ? 182 PRO A CA  1 
ATOM   1156 C C   . PRO A 1 158 ? 36.232 117.732 41.422 1.00 84.77  ? 182 PRO A C   1 
ATOM   1157 O O   . PRO A 1 158 ? 37.073 118.631 41.480 1.00 86.02  ? 182 PRO A O   1 
ATOM   1158 C CB  . PRO A 1 158 ? 36.089 117.235 38.946 1.00 106.83 ? 182 PRO A CB  1 
ATOM   1159 C CG  . PRO A 1 158 ? 36.395 118.543 38.300 1.00 110.24 ? 182 PRO A CG  1 
ATOM   1160 C CD  . PRO A 1 158 ? 35.228 119.446 38.602 1.00 105.50 ? 182 PRO A CD  1 
ATOM   1161 N N   . ILE A 1 159 ? 36.057 116.831 42.391 1.00 88.22  ? 183 ILE A N   1 
ATOM   1162 C CA  . ILE A 1 159 ? 36.878 116.822 43.606 1.00 88.50  ? 183 ILE A CA  1 
ATOM   1163 C C   . ILE A 1 159 ? 38.190 116.107 43.295 1.00 87.63  ? 183 ILE A C   1 
ATOM   1164 O O   . ILE A 1 159 ? 38.203 114.935 42.910 1.00 86.05  ? 183 ILE A O   1 
ATOM   1165 C CB  . ILE A 1 159 ? 36.155 116.100 44.777 1.00 81.12  ? 183 ILE A CB  1 
ATOM   1166 C CG1 . ILE A 1 159 ? 34.774 116.727 45.028 1.00 79.17  ? 183 ILE A CG1 1 
ATOM   1167 C CG2 . ILE A 1 159 ? 37.020 116.126 46.032 1.00 80.39  ? 183 ILE A CG2 1 
ATOM   1168 C CD1 . ILE A 1 159 ? 34.745 118.217 45.435 1.00 80.04  ? 183 ILE A CD1 1 
ATOM   1169 N N   . THR A 1 160 ? 39.294 116.830 43.451 1.00 88.62  ? 184 THR A N   1 
ATOM   1170 C CA  . THR A 1 160 ? 40.619 116.285 43.153 1.00 101.10 ? 184 THR A CA  1 
ATOM   1171 C C   . THR A 1 160 ? 41.071 115.304 44.225 1.00 101.33 ? 184 THR A C   1 
ATOM   1172 O O   . THR A 1 160 ? 40.900 115.541 45.426 1.00 97.36  ? 184 THR A O   1 
ATOM   1173 C CB  . THR A 1 160 ? 41.662 117.411 42.968 1.00 110.99 ? 184 THR A CB  1 
ATOM   1174 O OG1 . THR A 1 160 ? 41.396 118.466 43.898 1.00 118.04 ? 184 THR A OG1 1 
ATOM   1175 C CG2 . THR A 1 160 ? 41.605 117.967 41.545 1.00 117.68 ? 184 THR A CG2 1 
ATOM   1176 N N   . GLN A 1 161 ? 41.642 114.193 43.773 1.00 120.87 ? 185 GLN A N   1 
ATOM   1177 C CA  . GLN A 1 161 ? 42.063 113.129 44.670 1.00 122.98 ? 185 GLN A CA  1 
ATOM   1178 C C   . GLN A 1 161 ? 43.576 112.975 44.719 1.00 125.62 ? 185 GLN A C   1 
ATOM   1179 O O   . GLN A 1 161 ? 44.265 113.228 43.730 1.00 131.89 ? 185 GLN A O   1 
ATOM   1180 C CB  . GLN A 1 161 ? 41.401 111.803 44.245 1.00 103.42 ? 185 GLN A CB  1 
ATOM   1181 C CG  . GLN A 1 161 ? 39.867 111.831 44.263 1.00 93.42  ? 185 GLN A CG  1 
ATOM   1182 C CD  . GLN A 1 161 ? 39.235 110.440 44.297 1.00 89.97  ? 185 GLN A CD  1 
ATOM   1183 O OE1 . GLN A 1 161 ? 39.814 109.459 43.817 1.00 89.11  ? 185 GLN A OE1 1 
ATOM   1184 N NE2 . GLN A 1 161 ? 38.032 110.354 44.857 1.00 88.25  ? 185 GLN A NE2 1 
ATOM   1185 N N   . ASP A 1 162 ? 44.085 112.582 45.885 1.00 104.40 ? 186 ASP A N   1 
ATOM   1186 C CA  . ASP A 1 162 ? 45.520 112.379 46.086 1.00 98.45  ? 186 ASP A CA  1 
ATOM   1187 C C   . ASP A 1 162 ? 45.771 111.281 47.118 1.00 96.30  ? 186 ASP A C   1 
ATOM   1188 O O   . ASP A 1 162 ? 44.832 110.601 47.537 1.00 89.47  ? 186 ASP A O   1 
ATOM   1189 C CB  . ASP A 1 162 ? 46.201 113.697 46.516 1.00 103.77 ? 186 ASP A CB  1 
ATOM   1190 C CG  . ASP A 1 162 ? 45.432 114.445 47.599 1.00 108.29 ? 186 ASP A CG  1 
ATOM   1191 O OD1 . ASP A 1 162 ? 45.604 115.684 47.700 1.00 111.11 ? 186 ASP A OD1 1 
ATOM   1192 O OD2 . ASP A 1 162 ? 44.665 113.803 48.350 1.00 111.12 ? 186 ASP A OD2 1 
ATOM   1193 N N   . LYS A 1 163 ? 47.036 111.097 47.504 1.00 106.66 ? 187 LYS A N   1 
ATOM   1194 C CA  . LYS A 1 163 ? 47.411 110.101 48.512 1.00 106.21 ? 187 LYS A CA  1 
ATOM   1195 C C   . LYS A 1 163 ? 46.732 110.379 49.860 1.00 103.76 ? 187 LYS A C   1 
ATOM   1196 O O   . LYS A 1 163 ? 46.509 109.460 50.654 1.00 107.64 ? 187 LYS A O   1 
ATOM   1197 C CB  . LYS A 1 163 ? 48.940 110.046 48.695 1.00 114.77 ? 187 LYS A CB  1 
ATOM   1198 C CG  . LYS A 1 163 ? 49.695 109.462 47.494 1.00 118.97 ? 187 LYS A CG  1 
ATOM   1199 C CD  . LYS A 1 163 ? 51.055 108.856 47.881 1.00 121.26 ? 187 LYS A CD  1 
ATOM   1200 C CE  . LYS A 1 163 ? 50.929 107.389 48.326 1.00 122.28 ? 187 LYS A CE  1 
ATOM   1201 N NZ  . LYS A 1 163 ? 52.247 106.703 48.521 1.00 121.74 ? 187 LYS A NZ  1 
ATOM   1202 N N   . ARG A 1 164 ? 46.394 111.640 50.110 1.00 88.41  ? 188 ARG A N   1 
ATOM   1203 C CA  . ARG A 1 164 ? 45.728 112.016 51.347 1.00 82.97  ? 188 ARG A CA  1 
ATOM   1204 C C   . ARG A 1 164 ? 44.225 111.720 51.283 1.00 80.94  ? 188 ARG A C   1 
ATOM   1205 O O   . ARG A 1 164 ? 43.668 111.125 52.210 1.00 77.20  ? 188 ARG A O   1 
ATOM   1206 C CB  . ARG A 1 164 ? 45.960 113.512 51.631 1.00 83.84  ? 188 ARG A CB  1 
ATOM   1207 C CG  . ARG A 1 164 ? 45.469 113.998 52.994 1.00 87.10  ? 188 ARG A CG  1 
ATOM   1208 C CD  . ARG A 1 164 ? 45.696 115.498 53.154 1.00 90.03  ? 188 ARG A CD  1 
ATOM   1209 N NE  . ARG A 1 164 ? 44.956 116.274 52.157 1.00 92.10  ? 188 ARG A NE  1 
ATOM   1210 C CZ  . ARG A 1 164 ? 43.745 116.801 52.350 1.00 92.86  ? 188 ARG A CZ  1 
ATOM   1211 N NH1 . ARG A 1 164 ? 43.116 116.650 53.513 1.00 91.97  ? 188 ARG A NH1 1 
ATOM   1212 N NH2 . ARG A 1 164 ? 43.157 117.481 51.370 1.00 92.95  ? 188 ARG A NH2 1 
ATOM   1213 N N   . VAL A 1 165 ? 43.586 112.116 50.178 1.00 84.57  ? 189 VAL A N   1 
ATOM   1214 C CA  . VAL A 1 165 ? 42.136 111.968 50.005 1.00 87.74  ? 189 VAL A CA  1 
ATOM   1215 C C   . VAL A 1 165 ? 41.786 111.206 48.730 1.00 86.58  ? 189 VAL A C   1 
ATOM   1216 O O   . VAL A 1 165 ? 42.107 111.638 47.621 1.00 88.71  ? 189 VAL A O   1 
ATOM   1217 C CB  . VAL A 1 165 ? 41.445 113.362 49.969 1.00 90.41  ? 189 VAL A CB  1 
ATOM   1218 C CG1 . VAL A 1 165 ? 39.944 113.207 49.799 1.00 91.97  ? 189 VAL A CG1 1 
ATOM   1219 C CG2 . VAL A 1 165 ? 41.743 114.133 51.244 1.00 92.43  ? 189 VAL A CG2 1 
ATOM   1220 N N   . SER A 1 166 ? 41.120 110.069 48.903 1.00 79.84  ? 190 SER A N   1 
ATOM   1221 C CA  . SER A 1 166 ? 40.750 109.218 47.784 1.00 73.62  ? 190 SER A CA  1 
ATOM   1222 C C   . SER A 1 166 ? 39.538 108.361 48.133 1.00 70.67  ? 190 SER A C   1 
ATOM   1223 O O   . SER A 1 166 ? 39.182 108.219 49.308 1.00 67.39  ? 190 SER A O   1 
ATOM   1224 C CB  . SER A 1 166 ? 41.935 108.314 47.412 1.00 75.66  ? 190 SER A CB  1 
ATOM   1225 O OG  . SER A 1 166 ? 41.668 107.585 46.228 1.00 79.44  ? 190 SER A OG  1 
ATOM   1226 N N   . GLN A 1 167 ? 38.899 107.795 47.110 1.00 68.28  ? 191 GLN A N   1 
ATOM   1227 C CA  . GLN A 1 167 ? 37.745 106.948 47.343 1.00 67.01  ? 191 GLN A CA  1 
ATOM   1228 C C   . GLN A 1 167 ? 38.072 105.462 47.255 1.00 67.82  ? 191 GLN A C   1 
ATOM   1229 O O   . GLN A 1 167 ? 38.931 105.039 46.472 1.00 69.44  ? 191 GLN A O   1 
ATOM   1230 C CB  . GLN A 1 167 ? 36.613 107.269 46.343 1.00 64.69  ? 191 GLN A CB  1 
ATOM   1231 C CG  . GLN A 1 167 ? 36.807 106.727 44.934 1.00 61.88  ? 191 GLN A CG  1 
ATOM   1232 C CD  . GLN A 1 167 ? 35.628 107.024 44.022 1.00 60.49  ? 191 GLN A CD  1 
ATOM   1233 O OE1 . GLN A 1 167 ? 35.345 108.178 43.709 1.00 60.92  ? 191 GLN A OE1 1 
ATOM   1234 N NE2 . GLN A 1 167 ? 34.938 105.980 43.593 1.00 59.87  ? 191 GLN A NE2 1 
ATOM   1235 N N   . GLY A 1 168 ? 37.394 104.687 48.099 1.00 65.89  ? 192 GLY A N   1 
ATOM   1236 C CA  . GLY A 1 168 ? 37.513 103.241 48.054 1.00 62.76  ? 192 GLY A CA  1 
ATOM   1237 C C   . GLY A 1 168 ? 36.588 102.688 46.971 1.00 60.94  ? 192 GLY A C   1 
ATOM   1238 O O   . GLY A 1 168 ? 35.726 103.405 46.449 1.00 62.21  ? 192 GLY A O   1 
ATOM   1239 N N   . HIS A 1 169 ? 36.761 101.410 46.640 1.00 54.92  ? 193 HIS A N   1 
ATOM   1240 C CA  . HIS A 1 169 ? 35.976 100.759 45.599 1.00 56.99  ? 193 HIS A CA  1 
ATOM   1241 C C   . HIS A 1 169 ? 34.494 100.662 45.947 1.00 58.54  ? 193 HIS A C   1 
ATOM   1242 O O   . HIS A 1 169 ? 33.658 100.478 45.067 1.00 54.59  ? 193 HIS A O   1 
ATOM   1243 C CB  . HIS A 1 169 ? 36.556 99.383  45.289 1.00 65.21  ? 193 HIS A CB  1 
ATOM   1244 C CG  . HIS A 1 169 ? 35.990 98.758  44.055 1.00 69.75  ? 193 HIS A CG  1 
ATOM   1245 N ND1 . HIS A 1 169 ? 35.005 97.794  44.093 1.00 70.82  ? 193 HIS A ND1 1 
ATOM   1246 C CD2 . HIS A 1 169 ? 36.267 98.963  42.744 1.00 71.68  ? 193 HIS A CD2 1 
ATOM   1247 C CE1 . HIS A 1 169 ? 34.705 97.427  42.860 1.00 72.07  ? 193 HIS A CE1 1 
ATOM   1248 N NE2 . HIS A 1 169 ? 35.456 98.121  42.023 1.00 73.67  ? 193 HIS A NE2 1 
ATOM   1249 N N   . ASN A 1 170 ? 34.179 100.782 47.233 1.00 77.29  ? 194 ASN A N   1 
ATOM   1250 C CA  . ASN A 1 170 ? 32.790 100.775 47.694 1.00 84.19  ? 194 ASN A CA  1 
ATOM   1251 C C   . ASN A 1 170 ? 32.151 102.162 47.526 1.00 86.34  ? 194 ASN A C   1 
ATOM   1252 O O   . ASN A 1 170 ? 30.945 102.329 47.738 1.00 92.13  ? 194 ASN A O   1 
ATOM   1253 C CB  . ASN A 1 170 ? 32.715 100.343 49.161 1.00 79.78  ? 194 ASN A CB  1 
ATOM   1254 C CG  . ASN A 1 170 ? 33.397 101.321 50.103 1.00 77.96  ? 194 ASN A CG  1 
ATOM   1255 O OD1 . ASN A 1 170 ? 34.423 101.925 49.773 1.00 76.09  ? 194 ASN A OD1 1 
ATOM   1256 N ND2 . ASN A 1 170 ? 32.838 101.464 51.295 1.00 77.52  ? 194 ASN A ND2 1 
ATOM   1257 N N   . GLY A 1 171 ? 32.977 103.146 47.162 1.00 78.84  ? 195 GLY A N   1 
ATOM   1258 C CA  . GLY A 1 171 ? 32.502 104.503 46.931 1.00 71.58  ? 195 GLY A CA  1 
ATOM   1259 C C   . GLY A 1 171 ? 32.720 105.499 48.052 1.00 66.70  ? 195 GLY A C   1 
ATOM   1260 O O   . GLY A 1 171 ? 32.559 106.707 47.852 1.00 67.26  ? 195 GLY A O   1 
ATOM   1261 N N   . ASP A 1 172 ? 33.069 105.001 49.236 1.00 64.13  ? 196 ASP A N   1 
ATOM   1262 C CA  . ASP A 1 172 ? 33.324 105.865 50.394 1.00 62.85  ? 196 ASP A CA  1 
ATOM   1263 C C   . ASP A 1 172 ? 34.537 106.750 50.135 1.00 59.69  ? 196 ASP A C   1 
ATOM   1264 O O   . ASP A 1 172 ? 35.485 106.341 49.451 1.00 56.23  ? 196 ASP A O   1 
ATOM   1265 C CB  . ASP A 1 172 ? 33.556 105.022 51.652 1.00 75.35  ? 196 ASP A CB  1 
ATOM   1266 C CG  . ASP A 1 172 ? 32.298 104.302 52.116 1.00 84.55  ? 196 ASP A CG  1 
ATOM   1267 O OD1 . ASP A 1 172 ? 32.380 103.538 53.104 1.00 88.00  ? 196 ASP A OD1 1 
ATOM   1268 O OD2 . ASP A 1 172 ? 31.226 104.497 51.496 1.00 88.62  ? 196 ASP A OD2 1 
ATOM   1269 N N   . LEU A 1 173 ? 34.498 107.968 50.672 1.00 59.90  ? 197 LEU A N   1 
ATOM   1270 C CA  . LEU A 1 173 ? 35.595 108.925 50.492 1.00 65.49  ? 197 LEU A CA  1 
ATOM   1271 C C   . LEU A 1 173 ? 36.440 108.952 51.753 1.00 69.92  ? 197 LEU A C   1 
ATOM   1272 O O   . LEU A 1 173 ? 35.931 109.206 52.850 1.00 70.69  ? 197 LEU A O   1 
ATOM   1273 C CB  . LEU A 1 173 ? 35.040 110.319 50.171 1.00 68.53  ? 197 LEU A CB  1 
ATOM   1274 C CG  . LEU A 1 173 ? 36.035 111.421 49.771 1.00 66.00  ? 197 LEU A CG  1 
ATOM   1275 C CD1 . LEU A 1 173 ? 36.657 111.137 48.410 1.00 63.75  ? 197 LEU A CD1 1 
ATOM   1276 C CD2 . LEU A 1 173 ? 35.323 112.759 49.760 1.00 65.05  ? 197 LEU A CD2 1 
ATOM   1277 N N   . TYR A 1 174 ? 37.734 108.712 51.581 1.00 74.50  ? 198 TYR A N   1 
ATOM   1278 C CA  . TYR A 1 174 ? 38.648 108.591 52.708 1.00 78.25  ? 198 TYR A CA  1 
ATOM   1279 C C   . TYR A 1 174 ? 39.633 109.724 52.920 1.00 82.81  ? 198 TYR A C   1 
ATOM   1280 O O   . TYR A 1 174 ? 40.478 110.002 52.058 1.00 85.65  ? 198 TYR A O   1 
ATOM   1281 C CB  . TYR A 1 174 ? 39.435 107.267 52.592 1.00 78.37  ? 198 TYR A CB  1 
ATOM   1282 C CG  . TYR A 1 174 ? 38.591 106.017 52.733 1.00 73.60  ? 198 TYR A CG  1 
ATOM   1283 C CD1 . TYR A 1 174 ? 38.037 105.393 51.618 1.00 71.95  ? 198 TYR A CD1 1 
ATOM   1284 C CD2 . TYR A 1 174 ? 38.350 105.460 53.989 1.00 71.51  ? 198 TYR A CD2 1 
ATOM   1285 C CE1 . TYR A 1 174 ? 37.267 104.246 51.748 1.00 71.83  ? 198 TYR A CE1 1 
ATOM   1286 C CE2 . TYR A 1 174 ? 37.580 104.312 54.132 1.00 71.76  ? 198 TYR A CE2 1 
ATOM   1287 C CZ  . TYR A 1 174 ? 37.042 103.710 53.009 1.00 71.92  ? 198 TYR A CZ  1 
ATOM   1288 O OH  . TYR A 1 174 ? 36.280 102.575 53.144 1.00 72.14  ? 198 TYR A OH  1 
ATOM   1289 N N   . PHE A 1 175 ? 39.498 110.381 54.071 1.00 85.58  ? 199 PHE A N   1 
ATOM   1290 C CA  . PHE A 1 175 ? 40.416 111.434 54.470 1.00 88.60  ? 199 PHE A CA  1 
ATOM   1291 C C   . PHE A 1 175 ? 41.420 110.850 55.469 1.00 89.54  ? 199 PHE A C   1 
ATOM   1292 O O   . PHE A 1 175 ? 41.051 110.516 56.602 1.00 85.03  ? 199 PHE A O   1 
ATOM   1293 C CB  . PHE A 1 175 ? 39.683 112.598 55.147 1.00 98.86  ? 199 PHE A CB  1 
ATOM   1294 C CG  . PHE A 1 175 ? 38.693 113.296 54.258 1.00 107.57 ? 199 PHE A CG  1 
ATOM   1295 C CD1 . PHE A 1 175 ? 37.363 112.887 54.218 1.00 111.28 ? 199 PHE A CD1 1 
ATOM   1296 C CD2 . PHE A 1 175 ? 39.088 114.367 53.463 1.00 110.89 ? 199 PHE A CD2 1 
ATOM   1297 C CE1 . PHE A 1 175 ? 36.441 113.533 53.394 1.00 112.44 ? 199 PHE A CE1 1 
ATOM   1298 C CE2 . PHE A 1 175 ? 38.173 115.018 52.634 1.00 112.25 ? 199 PHE A CE2 1 
ATOM   1299 C CZ  . PHE A 1 175 ? 36.847 114.602 52.603 1.00 112.32 ? 199 PHE A CZ  1 
ATOM   1300 N N   . SER A 1 176 ? 42.675 110.710 55.038 1.00 92.25  ? 200 SER A N   1 
ATOM   1301 C CA  . SER A 1 176 ? 43.750 110.228 55.920 1.00 95.96  ? 200 SER A CA  1 
ATOM   1302 C C   . SER A 1 176 ? 43.840 111.220 57.086 1.00 95.37  ? 200 SER A C   1 
ATOM   1303 O O   . SER A 1 176 ? 43.692 110.839 58.254 1.00 96.08  ? 200 SER A O   1 
ATOM   1304 C CB  . SER A 1 176 ? 45.066 110.157 55.156 1.00 110.14 ? 200 SER A CB  1 
ATOM   1305 O OG  . SER A 1 176 ? 44.981 109.208 54.108 1.00 114.48 ? 200 SER A OG  1 
ATOM   1306 N N   . ASN A 1 177 ? 44.103 112.483 56.749 1.00 109.73 ? 201 ASN A N   1 
ATOM   1307 C CA  . ASN A 1 177 ? 44.058 113.579 57.714 1.00 108.89 ? 201 ASN A CA  1 
ATOM   1308 C C   . ASN A 1 177 ? 43.302 114.759 57.076 1.00 109.31 ? 201 ASN A C   1 
ATOM   1309 O O   . ASN A 1 177 ? 43.535 115.114 55.914 1.00 110.94 ? 201 ASN A O   1 
ATOM   1310 C CB  . ASN A 1 177 ? 45.445 114.019 58.173 1.00 99.65  ? 201 ASN A CB  1 
ATOM   1311 C CG  . ASN A 1 177 ? 46.382 114.323 57.023 1.00 99.40  ? 201 ASN A CG  1 
ATOM   1312 O OD1 . ASN A 1 177 ? 47.017 113.422 56.465 1.00 98.65  ? 201 ASN A OD1 1 
ATOM   1313 N ND2 . ASN A 1 177 ? 46.475 115.598 56.659 1.00 99.65  ? 201 ASN A ND2 1 
ATOM   1314 N N   . VAL A 1 178 ? 42.383 115.346 57.838 1.00 115.91 ? 202 VAL A N   1 
ATOM   1315 C CA  . VAL A 1 178 ? 41.589 116.468 57.352 1.00 116.98 ? 202 VAL A CA  1 
ATOM   1316 C C   . VAL A 1 178 ? 42.336 117.794 57.506 1.00 123.31 ? 202 VAL A C   1 
ATOM   1317 O O   . VAL A 1 178 ? 42.660 118.218 58.621 1.00 131.10 ? 202 VAL A O   1 
ATOM   1318 C CB  . VAL A 1 178 ? 40.219 116.552 58.097 1.00 97.35  ? 202 VAL A CB  1 
ATOM   1319 C CG1 . VAL A 1 178 ? 39.459 117.798 57.672 1.00 88.55  ? 202 VAL A CG1 1 
ATOM   1320 C CG2 . VAL A 1 178 ? 39.388 115.304 57.813 1.00 89.11  ? 202 VAL A CG2 1 
ATOM   1321 N N   . MET A 1 179 ? 42.623 118.429 56.370 1.00 119.35 ? 203 MET A N   1 
ATOM   1322 C CA  . MET A 1 179 ? 43.304 119.722 56.353 1.00 119.90 ? 203 MET A CA  1 
ATOM   1323 C C   . MET A 1 179 ? 42.282 120.859 56.459 1.00 118.56 ? 203 MET A C   1 
ATOM   1324 O O   . MET A 1 179 ? 41.098 120.623 56.724 1.00 118.32 ? 203 MET A O   1 
ATOM   1325 C CB  . MET A 1 179 ? 44.127 119.883 55.064 1.00 114.15 ? 203 MET A CB  1 
ATOM   1326 C CG  . MET A 1 179 ? 45.297 118.910 54.940 1.00 113.68 ? 203 MET A CG  1 
ATOM   1327 S SD  . MET A 1 179 ? 46.254 119.150 53.424 1.00 113.87 ? 203 MET A SD  1 
ATOM   1328 C CE  . MET A 1 179 ? 47.418 120.420 53.949 1.00 113.93 ? 203 MET A CE  1 
ATOM   1329 N N   . LEU A 1 180 ? 42.753 122.091 56.274 1.00 126.33 ? 204 LEU A N   1 
ATOM   1330 C CA  . LEU A 1 180 ? 41.883 123.262 56.321 1.00 121.70 ? 204 LEU A CA  1 
ATOM   1331 C C   . LEU A 1 180 ? 41.190 123.520 54.975 1.00 118.63 ? 204 LEU A C   1 
ATOM   1332 O O   . LEU A 1 180 ? 40.013 123.903 54.940 1.00 121.70 ? 204 LEU A O   1 
ATOM   1333 C CB  . LEU A 1 180 ? 42.676 124.512 56.770 1.00 127.39 ? 204 LEU A CB  1 
ATOM   1334 C CG  . LEU A 1 180 ? 44.204 124.590 56.557 1.00 123.69 ? 204 LEU A CG  1 
ATOM   1335 C CD1 . LEU A 1 180 ? 44.569 124.876 55.099 1.00 121.31 ? 204 LEU A CD1 1 
ATOM   1336 C CD2 . LEU A 1 180 ? 44.792 125.664 57.473 1.00 121.98 ? 204 LEU A CD2 1 
ATOM   1337 N N   . GLN A 1 181 ? 41.912 123.273 53.879 1.00 96.24  ? 205 GLN A N   1 
ATOM   1338 C CA  . GLN A 1 181 ? 41.394 123.503 52.529 1.00 95.15  ? 205 GLN A CA  1 
ATOM   1339 C C   . GLN A 1 181 ? 40.201 122.614 52.159 1.00 93.55  ? 205 GLN A C   1 
ATOM   1340 O O   . GLN A 1 181 ? 39.508 122.873 51.174 1.00 86.36  ? 205 GLN A O   1 
ATOM   1341 C CB  . GLN A 1 181 ? 42.517 123.339 51.490 1.00 96.89  ? 205 GLN A CB  1 
ATOM   1342 C CG  . GLN A 1 181 ? 42.993 121.907 51.278 1.00 101.29 ? 205 GLN A CG  1 
ATOM   1343 C CD  . GLN A 1 181 ? 43.786 121.735 49.990 1.00 103.50 ? 205 GLN A CD  1 
ATOM   1344 O OE1 . GLN A 1 181 ? 44.827 122.364 49.796 1.00 103.57 ? 205 GLN A OE1 1 
ATOM   1345 N NE2 . GLN A 1 181 ? 43.293 120.876 49.102 1.00 103.51 ? 205 GLN A NE2 1 
ATOM   1346 N N   . ASP A 1 182 ? 39.960 121.579 52.961 1.00 108.68 ? 206 ASP A N   1 
ATOM   1347 C CA  . ASP A 1 182 ? 38.854 120.651 52.725 1.00 117.05 ? 206 ASP A CA  1 
ATOM   1348 C C   . ASP A 1 182 ? 37.486 121.317 52.900 1.00 118.11 ? 206 ASP A C   1 
ATOM   1349 O O   . ASP A 1 182 ? 36.441 120.664 52.809 1.00 125.02 ? 206 ASP A O   1 
ATOM   1350 C CB  . ASP A 1 182 ? 38.994 119.418 53.623 1.00 126.71 ? 206 ASP A CB  1 
ATOM   1351 C CG  . ASP A 1 182 ? 40.236 118.590 53.291 1.00 126.55 ? 206 ASP A CG  1 
ATOM   1352 O OD1 . ASP A 1 182 ? 40.664 117.795 54.159 1.00 125.58 ? 206 ASP A OD1 1 
ATOM   1353 O OD2 . ASP A 1 182 ? 40.779 118.731 52.167 1.00 125.68 ? 206 ASP A OD2 1 
ATOM   1354 N N   . MET A 1 183 ? 37.509 122.624 53.159 1.00 117.57 ? 207 MET A N   1 
ATOM   1355 C CA  . MET A 1 183 ? 36.282 123.405 53.241 1.00 115.26 ? 207 MET A CA  1 
ATOM   1356 C C   . MET A 1 183 ? 36.128 124.286 51.990 1.00 111.27 ? 207 MET A C   1 
ATOM   1357 O O   . MET A 1 183 ? 35.207 125.102 51.908 1.00 100.24 ? 207 MET A O   1 
ATOM   1358 C CB  . MET A 1 183 ? 36.239 124.242 54.519 1.00 124.27 ? 207 MET A CB  1 
ATOM   1359 C CG  . MET A 1 183 ? 35.907 123.413 55.753 1.00 137.65 ? 207 MET A CG  1 
ATOM   1360 S SD  . MET A 1 183 ? 35.599 124.375 57.248 1.00 144.80 ? 207 MET A SD  1 
ATOM   1361 C CE  . MET A 1 183 ? 34.170 125.370 56.761 1.00 146.56 ? 207 MET A CE  1 
ATOM   1362 N N   . GLN A 1 184 ? 37.027 124.095 51.019 1.00 119.23 ? 208 GLN A N   1 
ATOM   1363 C CA  . GLN A 1 184 ? 36.982 124.816 49.742 1.00 123.84 ? 208 GLN A CA  1 
ATOM   1364 C C   . GLN A 1 184 ? 35.974 124.186 48.764 1.00 122.56 ? 208 GLN A C   1 
ATOM   1365 O O   . GLN A 1 184 ? 36.001 124.470 47.563 1.00 127.33 ? 208 GLN A O   1 
ATOM   1366 C CB  . GLN A 1 184 ? 38.372 124.868 49.086 1.00 126.05 ? 208 GLN A CB  1 
ATOM   1367 C CG  . GLN A 1 184 ? 39.322 125.885 49.714 1.00 127.09 ? 208 GLN A CG  1 
ATOM   1368 C CD  . GLN A 1 184 ? 40.689 125.930 49.040 1.00 128.06 ? 208 GLN A CD  1 
ATOM   1369 O OE1 . GLN A 1 184 ? 40.998 125.115 48.164 1.00 128.58 ? 208 GLN A OE1 1 
ATOM   1370 N NE2 . GLN A 1 184 ? 41.517 126.883 49.454 1.00 128.58 ? 208 GLN A NE2 1 
ATOM   1371 N N   . THR A 1 185 ? 35.095 123.338 49.297 1.00 99.74  ? 209 THR A N   1 
ATOM   1372 C CA  . THR A 1 185 ? 34.038 122.671 48.534 1.00 92.80  ? 209 THR A CA  1 
ATOM   1373 C C   . THR A 1 185 ? 33.173 121.790 49.433 1.00 88.41  ? 209 THR A C   1 
ATOM   1374 O O   . THR A 1 185 ? 33.580 121.437 50.543 1.00 88.73  ? 209 THR A O   1 
ATOM   1375 C CB  . THR A 1 185 ? 34.621 121.756 47.391 1.00 92.71  ? 209 THR A CB  1 
ATOM   1376 O OG1 . THR A 1 185 ? 33.579 120.923 46.866 1.00 89.77  ? 209 THR A OG1 1 
ATOM   1377 C CG2 . THR A 1 185 ? 35.757 120.875 47.899 1.00 89.87  ? 209 THR A CG2 1 
ATOM   1378 N N   . ASP A 1 186 ? 31.955 121.497 48.972 1.00 83.56  ? 210 ASP A N   1 
ATOM   1379 C CA  . ASP A 1 186 ? 31.100 120.527 49.655 1.00 82.49  ? 210 ASP A CA  1 
ATOM   1380 C C   . ASP A 1 186 ? 31.241 119.197 48.885 1.00 82.19  ? 210 ASP A C   1 
ATOM   1381 O O   . ASP A 1 186 ? 31.814 119.166 47.787 1.00 78.01  ? 210 ASP A O   1 
ATOM   1382 C CB  . ASP A 1 186 ? 29.642 120.976 49.761 1.00 95.45  ? 210 ASP A CB  1 
ATOM   1383 C CG  . ASP A 1 186 ? 28.990 121.244 48.417 1.00 99.47  ? 210 ASP A CG  1 
ATOM   1384 O OD1 . ASP A 1 186 ? 27.763 121.493 48.418 1.00 100.61 ? 210 ASP A OD1 1 
ATOM   1385 O OD2 . ASP A 1 186 ? 29.674 121.217 47.367 1.00 101.80 ? 210 ASP A OD2 1 
ATOM   1386 N N   . TYR A 1 187 ? 30.722 118.110 49.451 1.00 83.74  ? 211 TYR A N   1 
ATOM   1387 C CA  . TYR A 1 187 ? 30.943 116.795 48.855 1.00 83.05  ? 211 TYR A CA  1 
ATOM   1388 C C   . TYR A 1 187 ? 29.695 115.951 48.664 1.00 83.06  ? 211 TYR A C   1 
ATOM   1389 O O   . TYR A 1 187 ? 28.992 115.626 49.623 1.00 80.02  ? 211 TYR A O   1 
ATOM   1390 C CB  . TYR A 1 187 ? 31.977 116.037 49.713 1.00 81.79  ? 211 TYR A CB  1 
ATOM   1391 C CG  . TYR A 1 187 ? 33.259 116.814 49.950 1.00 84.87  ? 211 TYR A CG  1 
ATOM   1392 C CD1 . TYR A 1 187 ? 33.374 117.701 51.022 1.00 85.72  ? 211 TYR A CD1 1 
ATOM   1393 C CD2 . TYR A 1 187 ? 34.351 116.672 49.089 1.00 86.18  ? 211 TYR A CD2 1 
ATOM   1394 C CE1 . TYR A 1 187 ? 34.539 118.426 51.232 1.00 86.94  ? 211 TYR A CE1 1 
ATOM   1395 C CE2 . TYR A 1 187 ? 35.524 117.395 49.295 1.00 87.41  ? 211 TYR A CE2 1 
ATOM   1396 C CZ  . TYR A 1 187 ? 35.610 118.270 50.370 1.00 87.40  ? 211 TYR A CZ  1 
ATOM   1397 O OH  . TYR A 1 187 ? 36.769 118.986 50.583 1.00 88.15  ? 211 TYR A OH  1 
ATOM   1398 N N   . SER A 1 188 ? 29.423 115.609 47.407 1.00 76.01  ? 212 SER A N   1 
ATOM   1399 C CA  . SER A 1 188 ? 28.256 114.806 47.068 1.00 78.44  ? 212 SER A CA  1 
ATOM   1400 C C   . SER A 1 188 ? 28.650 113.560 46.289 1.00 74.03  ? 212 SER A C   1 
ATOM   1401 O O   . SER A 1 188 ? 29.386 113.641 45.304 1.00 71.30  ? 212 SER A O   1 
ATOM   1402 C CB  . SER A 1 188 ? 27.258 115.635 46.247 1.00 95.97  ? 212 SER A CB  1 
ATOM   1403 O OG  . SER A 1 188 ? 27.842 116.075 45.034 1.00 106.47 ? 212 SER A OG  1 
ATOM   1404 N N   . CYS A 1 189 ? 28.168 112.407 46.749 1.00 76.64  ? 213 CYS A N   1 
ATOM   1405 C CA  . CYS A 1 189 ? 28.448 111.146 46.078 1.00 73.68  ? 213 CYS A CA  1 
ATOM   1406 C C   . CYS A 1 189 ? 27.537 110.985 44.866 1.00 73.75  ? 213 CYS A C   1 
ATOM   1407 O O   . CYS A 1 189 ? 26.317 111.140 44.963 1.00 73.66  ? 213 CYS A O   1 
ATOM   1408 C CB  . CYS A 1 189 ? 28.256 109.966 47.036 1.00 70.87  ? 213 CYS A CB  1 
ATOM   1409 S SG  . CYS A 1 189 ? 29.051 108.445 46.434 1.00 73.59  ? 213 CYS A SG  1 
ATOM   1410 N N   . ASN A 1 190 ? 28.149 110.692 43.724 1.00 72.86  ? 214 ASN A N   1 
ATOM   1411 C CA  . ASN A 1 190 ? 27.429 110.497 42.470 1.00 71.58  ? 214 ASN A CA  1 
ATOM   1412 C C   . ASN A 1 190 ? 27.555 109.063 41.977 1.00 69.21  ? 214 ASN A C   1 
ATOM   1413 O O   . ASN A 1 190 ? 28.611 108.439 42.120 1.00 67.75  ? 214 ASN A O   1 
ATOM   1414 C CB  . ASN A 1 190 ? 27.974 111.435 41.390 1.00 77.50  ? 214 ASN A CB  1 
ATOM   1415 C CG  . ASN A 1 190 ? 27.443 112.845 41.517 1.00 82.48  ? 214 ASN A CG  1 
ATOM   1416 O OD1 . ASN A 1 190 ? 26.807 113.360 40.597 1.00 84.65  ? 214 ASN A OD1 1 
ATOM   1417 N ND2 . ASN A 1 190 ? 27.704 113.482 42.655 1.00 85.02  ? 214 ASN A ND2 1 
ATOM   1418 N N   . ALA A 1 191 ? 26.476 108.550 41.390 1.00 58.60  ? 215 ALA A N   1 
ATOM   1419 C CA  . ALA A 1 191 ? 26.478 107.197 40.860 1.00 54.85  ? 215 ALA A CA  1 
ATOM   1420 C C   . ALA A 1 191 ? 26.012 107.154 39.408 1.00 55.94  ? 215 ALA A C   1 
ATOM   1421 O O   . ALA A 1 191 ? 24.822 107.303 39.117 1.00 56.55  ? 215 ALA A O   1 
ATOM   1422 C CB  . ALA A 1 191 ? 25.603 106.296 41.722 1.00 40.91  ? 215 ALA A CB  1 
ATOM   1423 N N   . ARG A 1 192 ? 26.960 106.961 38.496 1.00 63.26  ? 216 ARG A N   1 
ATOM   1424 C CA  . ARG A 1 192 ? 26.652 106.870 37.069 1.00 67.20  ? 216 ARG A CA  1 
ATOM   1425 C C   . ARG A 1 192 ? 26.378 105.410 36.701 1.00 64.84  ? 216 ARG A C   1 
ATOM   1426 O O   . ARG A 1 192 ? 27.184 104.527 36.976 1.00 64.13  ? 216 ARG A O   1 
ATOM   1427 C CB  . ARG A 1 192 ? 27.804 107.435 36.228 1.00 83.41  ? 216 ARG A CB  1 
ATOM   1428 C CG  . ARG A 1 192 ? 27.598 107.332 34.722 1.00 94.60  ? 216 ARG A CG  1 
ATOM   1429 C CD  . ARG A 1 192 ? 28.838 107.794 33.967 1.00 100.30 ? 216 ARG A CD  1 
ATOM   1430 N NE  . ARG A 1 192 ? 28.937 107.185 32.642 1.00 102.62 ? 216 ARG A NE  1 
ATOM   1431 C CZ  . ARG A 1 192 ? 29.584 106.050 32.372 1.00 103.92 ? 216 ARG A CZ  1 
ATOM   1432 N NH1 . ARG A 1 192 ? 30.210 105.378 33.337 1.00 103.41 ? 216 ARG A NH1 1 
ATOM   1433 N NH2 . ARG A 1 192 ? 29.608 105.581 31.128 1.00 104.60 ? 216 ARG A NH2 1 
ATOM   1434 N N   . PHE A 1 193 ? 25.229 105.176 36.073 1.00 60.28  ? 217 PHE A N   1 
ATOM   1435 C CA  . PHE A 1 193 ? 24.798 103.834 35.706 1.00 67.63  ? 217 PHE A CA  1 
ATOM   1436 C C   . PHE A 1 193 ? 25.243 103.453 34.304 1.00 78.91  ? 217 PHE A C   1 
ATOM   1437 O O   . PHE A 1 193 ? 25.330 104.304 33.427 1.00 73.97  ? 217 PHE A O   1 
ATOM   1438 C CB  . PHE A 1 193 ? 23.304 103.704 35.922 1.00 67.39  ? 217 PHE A CB  1 
ATOM   1439 C CG  . PHE A 1 193 ? 22.903 103.774 37.368 1.00 62.80  ? 217 PHE A CG  1 
ATOM   1440 C CD1 . PHE A 1 193 ? 22.666 104.997 37.980 1.00 62.41  ? 217 PHE A CD1 1 
ATOM   1441 C CD2 . PHE A 1 193 ? 22.770 102.614 38.123 1.00 62.42  ? 217 PHE A CD2 1 
ATOM   1442 C CE1 . PHE A 1 193 ? 22.294 105.068 39.329 1.00 62.34  ? 217 PHE A CE1 1 
ATOM   1443 C CE2 . PHE A 1 193 ? 22.401 102.673 39.468 1.00 62.85  ? 217 PHE A CE2 1 
ATOM   1444 C CZ  . PHE A 1 193 ? 22.164 103.907 40.074 1.00 61.91  ? 217 PHE A CZ  1 
ATOM   1445 N N   . HIS A 1 194 ? 25.488 102.160 34.102 1.00 127.28 ? 218 HIS A N   1 
ATOM   1446 C CA  . HIS A 1 194 ? 26.152 101.698 32.888 1.00 149.44 ? 218 HIS A CA  1 
ATOM   1447 C C   . HIS A 1 194 ? 25.550 101.925 31.522 1.00 161.18 ? 218 HIS A C   1 
ATOM   1448 O O   . HIS A 1 194 ? 26.214 102.479 30.632 1.00 178.77 ? 218 HIS A O   1 
ATOM   1449 C CB  . HIS A 1 194 ? 26.550 100.205 33.034 1.00 125.30 ? 218 HIS A CB  1 
ATOM   1450 C CG  . HIS A 1 194 ? 27.876 99.983  33.707 1.00 114.07 ? 218 HIS A CG  1 
ATOM   1451 N ND1 . HIS A 1 194 ? 28.003 99.311  34.906 1.00 108.23 ? 218 HIS A ND1 1 
ATOM   1452 C CD2 . HIS A 1 194 ? 29.130 100.346 33.347 1.00 108.66 ? 218 HIS A CD2 1 
ATOM   1453 C CE1 . HIS A 1 194 ? 29.278 99.273  35.255 1.00 106.63 ? 218 HIS A CE1 1 
ATOM   1454 N NE2 . HIS A 1 194 ? 29.983 99.894  34.326 1.00 107.03 ? 218 HIS A NE2 1 
ATOM   1455 N N   . PHE A 1 195 ? 24.292 101.532 31.359 1.00 140.90 ? 219 PHE A N   1 
ATOM   1456 C CA  . PHE A 1 195 ? 23.665 101.595 30.043 1.00 132.96 ? 219 PHE A CA  1 
ATOM   1457 C C   . PHE A 1 195 ? 22.604 102.674 29.884 1.00 121.01 ? 219 PHE A C   1 
ATOM   1458 O O   . PHE A 1 195 ? 22.332 103.118 28.762 1.00 116.25 ? 219 PHE A O   1 
ATOM   1459 C CB  . PHE A 1 195 ? 23.131 100.198 29.678 1.00 169.75 ? 219 PHE A CB  1 
ATOM   1460 C CG  . PHE A 1 195 ? 24.177 99.107  29.768 1.00 179.10 ? 219 PHE A CG  1 
ATOM   1461 C CD1 . PHE A 1 195 ? 25.302 99.121  28.939 1.00 182.85 ? 219 PHE A CD1 1 
ATOM   1462 C CD2 . PHE A 1 195 ? 24.039 98.071  30.689 1.00 183.09 ? 219 PHE A CD2 1 
ATOM   1463 C CE1 . PHE A 1 195 ? 26.274 98.120  29.024 1.00 183.90 ? 219 PHE A CE1 1 
ATOM   1464 C CE2 . PHE A 1 195 ? 25.009 97.061  30.784 1.00 184.25 ? 219 PHE A CE2 1 
ATOM   1465 C CZ  . PHE A 1 195 ? 26.127 97.088  29.949 1.00 184.38 ? 219 PHE A CZ  1 
ATOM   1466 N N   . THR A 1 196 ? 22.013 103.093 31.006 1.00 114.24 ? 220 THR A N   1 
ATOM   1467 C CA  . THR A 1 196 ? 21.052 104.197 30.991 1.00 102.89 ? 220 THR A CA  1 
ATOM   1468 C C   . THR A 1 196 ? 21.772 105.558 31.068 1.00 98.04  ? 220 THR A C   1 
ATOM   1469 O O   . THR A 1 196 ? 21.239 106.575 30.629 1.00 96.43  ? 220 THR A O   1 
ATOM   1470 C CB  . THR A 1 196 ? 20.016 104.106 32.162 1.00 89.37  ? 220 THR A CB  1 
ATOM   1471 O OG1 . THR A 1 196 ? 19.539 105.418 32.477 1.00 87.01  ? 220 THR A OG1 1 
ATOM   1472 C CG2 . THR A 1 196 ? 20.623 103.489 33.411 1.00 86.92  ? 220 THR A CG2 1 
ATOM   1473 N N   . HIS A 1 197 ? 22.991 105.553 31.603 1.00 82.26  ? 221 HIS A N   1 
ATOM   1474 C CA  . HIS A 1 197 ? 23.812 106.757 31.789 1.00 78.21  ? 221 HIS A CA  1 
ATOM   1475 C C   . HIS A 1 197 ? 23.191 107.782 32.755 1.00 69.70  ? 221 HIS A C   1 
ATOM   1476 O O   . HIS A 1 197 ? 23.647 108.918 32.850 1.00 62.70  ? 221 HIS A O   1 
ATOM   1477 C CB  . HIS A 1 197 ? 24.180 107.397 30.440 1.00 106.23 ? 221 HIS A CB  1 
ATOM   1478 C CG  . HIS A 1 197 ? 24.872 106.460 29.491 1.00 122.75 ? 221 HIS A CG  1 
ATOM   1479 N ND1 . HIS A 1 197 ? 26.166 106.017 29.678 1.00 129.43 ? 221 HIS A ND1 1 
ATOM   1480 C CD2 . HIS A 1 197 ? 24.441 105.882 28.344 1.00 129.27 ? 221 HIS A CD2 1 
ATOM   1481 C CE1 . HIS A 1 197 ? 26.500 105.208 28.688 1.00 131.50 ? 221 HIS A CE1 1 
ATOM   1482 N NE2 . HIS A 1 197 ? 25.471 105.109 27.865 1.00 131.32 ? 221 HIS A NE2 1 
ATOM   1483 N N   . THR A 1 198 ? 22.151 107.361 33.468 1.00 67.21  ? 222 THR A N   1 
ATOM   1484 C CA  . THR A 1 198 ? 21.538 108.184 34.498 1.00 61.68  ? 222 THR A CA  1 
ATOM   1485 C C   . THR A 1 198 ? 22.529 108.337 35.667 1.00 60.89  ? 222 THR A C   1 
ATOM   1486 O O   . THR A 1 198 ? 23.226 107.396 36.043 1.00 58.76  ? 222 THR A O   1 
ATOM   1487 C CB  . THR A 1 198 ? 20.232 107.523 35.040 1.00 59.70  ? 222 THR A CB  1 
ATOM   1488 O OG1 . THR A 1 198 ? 19.229 107.575 34.028 1.00 61.51  ? 222 THR A OG1 1 
ATOM   1489 C CG2 . THR A 1 198 ? 19.714 108.236 36.270 1.00 61.05  ? 222 THR A CG2 1 
ATOM   1490 N N   . ILE A 1 199 ? 22.619 109.548 36.200 1.00 58.27  ? 223 ILE A N   1 
ATOM   1491 C CA  . ILE A 1 199 ? 23.441 109.800 37.360 1.00 59.08  ? 223 ILE A CA  1 
ATOM   1492 C C   . ILE A 1 199 ? 22.510 110.187 38.508 1.00 60.13  ? 223 ILE A C   1 
ATOM   1493 O O   . ILE A 1 199 ? 21.574 110.959 38.330 1.00 63.52  ? 223 ILE A O   1 
ATOM   1494 C CB  . ILE A 1 199 ? 24.475 110.937 37.120 1.00 58.90  ? 223 ILE A CB  1 
ATOM   1495 C CG1 . ILE A 1 199 ? 25.458 110.505 36.023 1.00 59.30  ? 223 ILE A CG1 1 
ATOM   1496 C CG2 . ILE A 1 199 ? 25.229 111.262 38.416 1.00 54.66  ? 223 ILE A CG2 1 
ATOM   1497 C CD1 . ILE A 1 199 ? 26.306 111.633 35.439 1.00 66.55  ? 223 ILE A CD1 1 
ATOM   1498 N N   . GLN A 1 200 ? 22.743 109.599 39.677 1.00 62.42  ? 224 GLN A N   1 
ATOM   1499 C CA  . GLN A 1 200 ? 21.966 109.940 40.858 1.00 64.20  ? 224 GLN A CA  1 
ATOM   1500 C C   . GLN A 1 200 ? 22.901 110.589 41.872 1.00 65.58  ? 224 GLN A C   1 
ATOM   1501 O O   . GLN A 1 200 ? 24.012 110.107 42.120 1.00 66.19  ? 224 GLN A O   1 
ATOM   1502 C CB  . GLN A 1 200 ? 21.291 108.709 41.458 1.00 65.12  ? 224 GLN A CB  1 
ATOM   1503 C CG  . GLN A 1 200 ? 20.311 108.003 40.527 1.00 64.14  ? 224 GLN A CG  1 
ATOM   1504 C CD  . GLN A 1 200 ? 19.046 108.800 40.264 1.00 66.04  ? 224 GLN A CD  1 
ATOM   1505 O OE1 . GLN A 1 200 ? 18.147 108.221 39.471 1.00 62.97  ? 224 GLN A OE1 1 
ATOM   1506 N NE2 . GLN A 1 200 ? 18.874 109.920 40.769 1.00 65.51  ? 224 GLN A NE2 1 
ATOM   1507 N N   . GLN A 1 201 ? 22.441 111.695 42.440 1.00 66.31  ? 225 GLN A N   1 
ATOM   1508 C CA  . GLN A 1 201 ? 23.212 112.459 43.401 1.00 69.19  ? 225 GLN A CA  1 
ATOM   1509 C C   . GLN A 1 201 ? 22.692 112.296 44.808 1.00 66.71  ? 225 GLN A C   1 
ATOM   1510 O O   . GLN A 1 201 ? 21.478 112.323 45.033 1.00 62.60  ? 225 GLN A O   1 
ATOM   1511 C CB  . GLN A 1 201 ? 23.161 113.958 43.063 1.00 98.30  ? 225 GLN A CB  1 
ATOM   1512 C CG  . GLN A 1 201 ? 24.166 114.426 42.037 1.00 111.33 ? 225 GLN A CG  1 
ATOM   1513 C CD  . GLN A 1 201 ? 24.332 115.939 42.041 1.00 116.69 ? 225 GLN A CD  1 
ATOM   1514 O OE1 . GLN A 1 201 ? 25.326 116.463 42.552 1.00 118.46 ? 225 GLN A OE1 1 
ATOM   1515 N NE2 . GLN A 1 201 ? 23.352 116.649 41.482 1.00 117.35 ? 225 GLN A NE2 1 
ATOM   1516 N N   . LYS A 1 202 ? 23.611 112.099 45.749 1.00 66.45  ? 226 LYS A N   1 
ATOM   1517 C CA  . LYS A 1 202 ? 23.215 112.066 47.145 1.00 70.67  ? 226 LYS A CA  1 
ATOM   1518 C C   . LYS A 1 202 ? 23.505 113.458 47.714 1.00 74.84  ? 226 LYS A C   1 
ATOM   1519 O O   . LYS A 1 202 ? 24.404 114.167 47.240 1.00 70.60  ? 226 LYS A O   1 
ATOM   1520 C CB  . LYS A 1 202 ? 23.961 110.984 47.935 1.00 74.75  ? 226 LYS A CB  1 
ATOM   1521 C CG  . LYS A 1 202 ? 25.213 111.428 48.680 1.00 79.31  ? 226 LYS A CG  1 
ATOM   1522 C CD  . LYS A 1 202 ? 25.600 110.407 49.756 1.00 82.00  ? 226 LYS A CD  1 
ATOM   1523 C CE  . LYS A 1 202 ? 24.594 110.376 50.907 1.00 81.42  ? 226 LYS A CE  1 
ATOM   1524 N NZ  . LYS A 1 202 ? 24.927 109.332 51.915 1.00 80.45  ? 226 LYS A NZ  1 
ATOM   1525 N N   . ASN A 1 203 ? 22.725 113.845 48.719 1.00 98.10  ? 227 ASN A N   1 
ATOM   1526 C CA  . ASN A 1 203 ? 22.864 115.151 49.350 1.00 108.78 ? 227 ASN A CA  1 
ATOM   1527 C C   . ASN A 1 203 ? 24.316 115.483 49.681 1.00 109.77 ? 227 ASN A C   1 
ATOM   1528 O O   . ASN A 1 203 ? 25.075 114.624 50.124 1.00 111.75 ? 227 ASN A O   1 
ATOM   1529 C CB  . ASN A 1 203 ? 21.986 115.219 50.606 1.00 115.83 ? 227 ASN A CB  1 
ATOM   1530 C CG  . ASN A 1 203 ? 20.509 115.002 50.294 1.00 123.62 ? 227 ASN A CG  1 
ATOM   1531 O OD1 . ASN A 1 203 ? 19.900 114.031 50.753 1.00 127.48 ? 227 ASN A OD1 1 
ATOM   1532 N ND2 . ASN A 1 203 ? 19.930 115.904 49.503 1.00 126.94 ? 227 ASN A ND2 1 
ATOM   1533 N N   . PRO A 1 204 ? 24.725 116.736 49.432 1.00 103.38 ? 228 PRO A N   1 
ATOM   1534 C CA  . PRO A 1 204 ? 26.090 117.190 49.703 1.00 102.36 ? 228 PRO A CA  1 
ATOM   1535 C C   . PRO A 1 204 ? 26.429 117.175 51.185 1.00 104.95 ? 228 PRO A C   1 
ATOM   1536 O O   . PRO A 1 204 ? 25.592 117.533 52.011 1.00 106.39 ? 228 PRO A O   1 
ATOM   1537 C CB  . PRO A 1 204 ? 26.096 118.639 49.203 1.00 104.64 ? 228 PRO A CB  1 
ATOM   1538 C CG  . PRO A 1 204 ? 24.961 118.722 48.252 1.00 104.20 ? 228 PRO A CG  1 
ATOM   1539 C CD  . PRO A 1 204 ? 23.922 117.797 48.799 1.00 105.53 ? 228 PRO A CD  1 
ATOM   1540 N N   . PHE A 1 205 ? 27.648 116.746 51.508 1.00 96.15  ? 229 PHE A N   1 
ATOM   1541 C CA  . PHE A 1 205 ? 28.156 116.815 52.875 1.00 92.03  ? 229 PHE A CA  1 
ATOM   1542 C C   . PHE A 1 205 ? 28.855 118.175 53.040 1.00 93.91  ? 229 PHE A C   1 
ATOM   1543 O O   . PHE A 1 205 ? 29.663 118.578 52.191 1.00 95.30  ? 229 PHE A O   1 
ATOM   1544 C CB  . PHE A 1 205 ? 29.193 115.719 53.155 1.00 86.05  ? 229 PHE A CB  1 
ATOM   1545 C CG  . PHE A 1 205 ? 28.596 114.365 53.418 1.00 79.09  ? 229 PHE A CG  1 
ATOM   1546 C CD1 . PHE A 1 205 ? 28.660 113.364 52.455 1.00 76.51  ? 229 PHE A CD1 1 
ATOM   1547 C CD2 . PHE A 1 205 ? 27.981 114.088 54.633 1.00 76.23  ? 229 PHE A CD2 1 
ATOM   1548 C CE1 . PHE A 1 205 ? 28.115 112.105 52.696 1.00 76.80  ? 229 PHE A CE1 1 
ATOM   1549 C CE2 . PHE A 1 205 ? 27.432 112.832 54.884 1.00 76.59  ? 229 PHE A CE2 1 
ATOM   1550 C CZ  . PHE A 1 205 ? 27.502 111.836 53.913 1.00 76.90  ? 229 PHE A CZ  1 
ATOM   1551 N N   . THR A 1 206 ? 28.526 118.885 54.116 1.00 96.99  ? 230 THR A N   1 
ATOM   1552 C CA  . THR A 1 206 ? 29.187 120.155 54.405 1.00 106.95 ? 230 THR A CA  1 
ATOM   1553 C C   . THR A 1 206 ? 30.186 119.939 55.539 1.00 103.42 ? 230 THR A C   1 
ATOM   1554 O O   . THR A 1 206 ? 29.824 119.528 56.648 1.00 100.84 ? 230 THR A O   1 
ATOM   1555 C CB  . THR A 1 206 ? 28.196 121.270 54.808 1.00 125.10 ? 230 THR A CB  1 
ATOM   1556 O OG1 . THR A 1 206 ? 27.059 121.239 53.936 1.00 132.90 ? 230 THR A OG1 1 
ATOM   1557 C CG2 . THR A 1 206 ? 28.874 122.640 54.695 1.00 133.02 ? 230 THR A CG2 1 
ATOM   1558 N N   . LEU A 1 207 ? 31.450 120.201 55.238 1.00 112.73 ? 231 LEU A N   1 
ATOM   1559 C CA  . LEU A 1 207 ? 32.492 120.039 56.222 1.00 114.75 ? 231 LEU A CA  1 
ATOM   1560 C C   . LEU A 1 207 ? 32.751 121.328 56.977 1.00 120.59 ? 231 LEU A C   1 
ATOM   1561 O O   . LEU A 1 207 ? 32.955 122.384 56.368 1.00 126.85 ? 231 LEU A O   1 
ATOM   1562 C CB  . LEU A 1 207 ? 33.815 119.593 55.564 1.00 100.72 ? 231 LEU A CB  1 
ATOM   1563 C CG  . LEU A 1 207 ? 33.921 118.273 54.778 1.00 89.92  ? 231 LEU A CG  1 
ATOM   1564 C CD1 . LEU A 1 207 ? 35.396 117.963 54.583 1.00 84.90  ? 231 LEU A CD1 1 
ATOM   1565 C CD2 . LEU A 1 207 ? 33.237 117.114 55.492 1.00 84.69  ? 231 LEU A CD2 1 
ATOM   1566 N N   . LYS A 1 208 ? 32.691 121.238 58.303 1.00 131.05 ? 232 LYS A N   1 
ATOM   1567 C CA  . LYS A 1 208 ? 33.073 122.351 59.166 1.00 132.21 ? 232 LYS A CA  1 
ATOM   1568 C C   . LYS A 1 208 ? 34.250 121.842 60.026 1.00 125.79 ? 232 LYS A C   1 
ATOM   1569 O O   . LYS A 1 208 ? 34.049 121.230 61.082 1.00 125.52 ? 232 LYS A O   1 
ATOM   1570 C CB  . LYS A 1 208 ? 31.915 122.821 60.054 1.00 145.00 ? 232 LYS A CB  1 
ATOM   1571 C CG  . LYS A 1 208 ? 32.178 124.150 60.771 1.00 152.32 ? 232 LYS A CG  1 
ATOM   1572 C CD  . LYS A 1 208 ? 30.995 124.559 61.645 1.00 155.43 ? 232 LYS A CD  1 
ATOM   1573 C CE  . LYS A 1 208 ? 31.270 125.873 62.371 1.00 155.91 ? 232 LYS A CE  1 
ATOM   1574 N NZ  . LYS A 1 208 ? 30.082 126.360 63.131 1.00 155.85 ? 232 LYS A NZ  1 
ATOM   1575 N N   . VAL A 1 209 ? 35.474 122.076 59.546 1.00 126.53 ? 233 VAL A N   1 
ATOM   1576 C CA  . VAL A 1 209 ? 36.665 121.648 60.272 1.00 128.23 ? 233 VAL A CA  1 
ATOM   1577 C C   . VAL A 1 209 ? 36.931 122.571 61.463 1.00 130.82 ? 233 VAL A C   1 
ATOM   1578 O O   . VAL A 1 209 ? 36.544 123.746 61.457 1.00 129.95 ? 233 VAL A O   1 
ATOM   1579 C CB  . VAL A 1 209 ? 37.950 121.588 59.348 1.00 124.27 ? 233 VAL A CB  1 
ATOM   1580 C CG1 . VAL A 1 209 ? 37.626 120.880 58.046 1.00 120.20 ? 233 VAL A CG1 1 
ATOM   1581 C CG2 . VAL A 1 209 ? 38.519 122.979 59.077 1.00 120.44 ? 233 VAL A CG2 1 
ATOM   1582 N N   . LEU A 1 210 ? 37.553 122.019 62.500 1.00 140.74 ? 234 LEU A N   1 
ATOM   1583 C CA  . LEU A 1 210 ? 37.900 122.797 63.683 1.00 152.01 ? 234 LEU A CA  1 
ATOM   1584 C C   . LEU A 1 210 ? 39.409 122.824 63.914 1.00 159.14 ? 234 LEU A C   1 
ATOM   1585 O O   . LEU A 1 210 ? 40.050 121.776 64.050 1.00 171.07 ? 234 LEU A O   1 
ATOM   1586 C CB  . LEU A 1 210 ? 37.195 122.248 64.937 1.00 120.92 ? 234 LEU A CB  1 
ATOM   1587 C CG  . LEU A 1 210 ? 35.877 122.919 65.358 1.00 106.11 ? 234 LEU A CG  1 
ATOM   1588 C CD1 . LEU A 1 210 ? 35.162 122.046 66.382 1.00 98.00  ? 234 LEU A CD1 1 
ATOM   1589 C CD2 . LEU A 1 210 ? 36.135 124.322 65.922 1.00 98.12  ? 234 LEU A CD2 1 
ATOM   1590 N N   . THR A 1 211 ? 39.968 124.033 63.927 1.00 162.95 ? 235 THR A N   1 
ATOM   1591 C CA  . THR A 1 211 ? 41.392 124.215 64.202 1.00 162.79 ? 235 THR A CA  1 
ATOM   1592 C C   . THR A 1 211 ? 41.631 124.062 65.715 1.00 162.12 ? 235 THR A C   1 
ATOM   1593 O O   . THR A 1 211 ? 41.052 124.784 66.539 1.00 158.63 ? 235 THR A O   1 
ATOM   1594 C CB  . THR A 1 211 ? 41.923 125.589 63.663 1.00 152.71 ? 235 THR A CB  1 
ATOM   1595 O OG1 . THR A 1 211 ? 43.242 125.826 64.171 1.00 150.99 ? 235 THR A OG1 1 
ATOM   1596 C CG2 . THR A 1 211 ? 40.996 126.752 64.034 1.00 151.07 ? 235 THR A CG2 1 
ATOM   1597 N N   . THR A 1 212 ? 42.477 123.092 66.064 1.00 146.37 ? 236 THR A N   1 
ATOM   1598 C CA  . THR A 1 212 ? 42.766 122.780 67.462 1.00 151.31 ? 236 THR A CA  1 
ATOM   1599 C C   . THR A 1 212 ? 44.208 123.097 67.874 1.00 150.14 ? 236 THR A C   1 
ATOM   1600 O O   . THR A 1 212 ? 44.676 122.671 68.932 1.00 147.48 ? 236 THR A O   1 
ATOM   1601 C CB  . THR A 1 212 ? 42.418 121.277 67.769 1.00 158.81 ? 236 THR A CB  1 
ATOM   1602 O OG1 . THR A 1 212 ? 42.642 121.004 69.160 1.00 163.57 ? 236 THR A OG1 1 
ATOM   1603 C CG2 . THR A 1 212 ? 43.252 120.321 66.911 1.00 163.55 ? 236 THR A CG2 1 
ATOM   1604 N N   . ARG A 1 213 ? 44.889 123.875 67.033 1.00 166.38 ? 237 ARG A N   1 
ATOM   1605 C CA  . ARG A 1 213 ? 46.275 124.304 67.254 1.00 167.01 ? 237 ARG A CA  1 
ATOM   1606 C C   . ARG A 1 213 ? 47.183 123.135 67.649 1.00 161.67 ? 237 ARG A C   1 
ATOM   1607 O O   . ARG A 1 213 ? 47.636 123.020 68.792 1.00 165.28 ? 237 ARG A O   1 
ATOM   1608 C CB  . ARG A 1 213 ? 46.323 125.447 68.295 1.00 165.89 ? 237 ARG A CB  1 
ATOM   1609 C CG  . ARG A 1 213 ? 47.704 126.080 68.477 1.00 169.39 ? 237 ARG A CG  1 
ATOM   1610 C CD  . ARG A 1 213 ? 47.613 127.553 68.856 1.00 170.74 ? 237 ARG A CD  1 
ATOM   1611 N NE  . ARG A 1 213 ? 47.338 128.400 67.696 1.00 171.21 ? 237 ARG A NE  1 
ATOM   1612 C CZ  . ARG A 1 213 ? 48.256 128.816 66.824 1.00 171.45 ? 237 ARG A CZ  1 
ATOM   1613 N NH1 . ARG A 1 213 ? 49.529 128.471 66.967 1.00 171.53 ? 237 ARG A NH1 1 
ATOM   1614 N NH2 . ARG A 1 213 ? 47.897 129.585 65.801 1.00 171.74 ? 237 ARG A NH2 1 
ATOM   1615 N N   . GLY A 1 214 ? 47.435 122.270 66.668 1.00 139.16 ? 238 GLY A N   1 
ATOM   1616 C CA  . GLY A 1 214 ? 48.271 121.104 66.875 1.00 133.87 ? 238 GLY A CA  1 
ATOM   1617 C C   . GLY A 1 214 ? 48.469 120.266 65.626 1.00 134.50 ? 238 GLY A C   1 
ATOM   1618 O O   . GLY A 1 214 ? 47.502 119.818 65.002 1.00 128.87 ? 238 GLY A O   1 
ATOM   1619 N N   . VAL A 1 215 ? 49.734 120.077 65.254 1.00 154.18 ? 239 VAL A N   1 
ATOM   1620 C CA  . VAL A 1 215 ? 50.093 119.238 64.114 1.00 162.72 ? 239 VAL A CA  1 
ATOM   1621 C C   . VAL A 1 215 ? 50.245 117.783 64.622 1.00 168.33 ? 239 VAL A C   1 
ATOM   1622 O O   . VAL A 1 215 ? 50.537 116.873 63.837 1.00 177.85 ? 239 VAL A O   1 
ATOM   1623 C CB  . VAL A 1 215 ? 51.448 119.703 63.468 1.00 149.30 ? 239 VAL A CB  1 
ATOM   1624 C CG1 . VAL A 1 215 ? 51.571 119.153 62.046 1.00 138.96 ? 239 VAL A CG1 1 
ATOM   1625 C CG2 . VAL A 1 215 ? 51.545 121.233 63.460 1.00 139.11 ? 239 VAL A CG2 1 
ATOM   1626 N N   . ALA A 1 216 ? 50.008 117.593 65.930 1.00 175.11 ? 240 ALA A N   1 
ATOM   1627 C CA  . ALA A 1 216 ? 50.158 116.313 66.626 1.00 170.12 ? 240 ALA A CA  1 
ATOM   1628 C C   . ALA A 1 216 ? 50.320 115.222 65.562 1.00 168.31 ? 240 ALA A C   1 
ATOM   1629 O O   . ALA A 1 216 ? 49.374 114.856 64.861 1.00 176.33 ? 240 ALA A O   1 
ATOM   1630 C CB  . ALA A 1 216 ? 48.966 116.086 67.594 1.00 117.21 ? 240 ALA A CB  1 
ATOM   1631 N N   . GLU A 1 217 ? 51.566 114.746 65.426 1.00 145.47 ? 241 GLU A N   1 
ATOM   1632 C CA  . GLU A 1 217 ? 51.929 113.726 64.426 1.00 137.73 ? 241 GLU A CA  1 
ATOM   1633 C C   . GLU A 1 217 ? 51.633 112.389 65.092 1.00 138.15 ? 241 GLU A C   1 
ATOM   1634 O O   . GLU A 1 217 ? 52.129 112.102 66.185 1.00 142.01 ? 241 GLU A O   1 
ATOM   1635 C CB  . GLU A 1 217 ? 53.403 113.850 64.010 1.00 122.51 ? 241 GLU A CB  1 
ATOM   1636 C CG  . GLU A 1 217 ? 53.739 115.163 63.302 1.00 110.29 ? 241 GLU A CG  1 
ATOM   1637 C CD  . GLU A 1 217 ? 55.232 115.354 63.049 1.00 105.86 ? 241 GLU A CD  1 
ATOM   1638 O OE1 . GLU A 1 217 ? 55.623 116.485 62.687 1.00 105.00 ? 241 GLU A OE1 1 
ATOM   1639 O OE2 . GLU A 1 217 ? 56.014 114.388 63.204 1.00 104.01 ? 241 GLU A OE2 1 
ATOM   1640 N N   . ARG A 1 218 ? 50.835 111.571 64.411 1.00 135.73 ? 242 ARG A N   1 
ATOM   1641 C CA  . ARG A 1 218 ? 50.314 110.330 64.983 1.00 136.22 ? 242 ARG A CA  1 
ATOM   1642 C C   . ARG A 1 218 ? 50.700 109.085 64.216 1.00 134.19 ? 242 ARG A C   1 
ATOM   1643 O O   . ARG A 1 218 ? 51.108 109.166 63.058 1.00 133.20 ? 242 ARG A O   1 
ATOM   1644 C CB  . ARG A 1 218 ? 48.773 110.434 65.014 1.00 127.43 ? 242 ARG A CB  1 
ATOM   1645 C CG  . ARG A 1 218 ? 48.085 109.856 66.244 1.00 130.74 ? 242 ARG A CG  1 
ATOM   1646 C CD  . ARG A 1 218 ? 46.622 110.292 66.289 1.00 132.63 ? 242 ARG A CD  1 
ATOM   1647 N NE  . ARG A 1 218 ? 45.996 109.950 67.569 1.00 133.80 ? 242 ARG A NE  1 
ATOM   1648 C CZ  . ARG A 1 218 ? 44.957 110.591 68.108 1.00 134.36 ? 242 ARG A CZ  1 
ATOM   1649 N NH1 . ARG A 1 218 ? 44.399 111.628 67.488 1.00 134.67 ? 242 ARG A NH1 1 
ATOM   1650 N NH2 . ARG A 1 218 ? 44.476 110.194 69.282 1.00 134.63 ? 242 ARG A NH2 1 
ATOM   1651 N N   . THR A 1 219 ? 50.576 107.934 64.880 1.00 131.39 ? 243 THR A N   1 
ATOM   1652 C CA  . THR A 1 219 ? 50.842 106.636 64.257 1.00 121.68 ? 243 THR A CA  1 
ATOM   1653 C C   . THR A 1 219 ? 49.714 106.323 63.256 1.00 116.51 ? 243 THR A C   1 
ATOM   1654 O O   . THR A 1 219 ? 48.575 106.752 63.445 1.00 129.66 ? 243 THR A O   1 
ATOM   1655 C CB  . THR A 1 219 ? 50.935 105.504 65.321 1.00 112.23 ? 243 THR A CB  1 
ATOM   1656 O OG1 . THR A 1 219 ? 49.783 105.532 66.175 1.00 102.69 ? 243 THR A OG1 1 
ATOM   1657 C CG2 . THR A 1 219 ? 52.190 105.678 66.166 1.00 102.24 ? 243 THR A CG2 1 
ATOM   1658 N N   . PRO A 1 220 ? 50.021 105.577 62.175 1.00 98.41  ? 244 PRO A N   1 
ATOM   1659 C CA  . PRO A 1 220 ? 48.999 105.245 61.174 1.00 92.14  ? 244 PRO A CA  1 
ATOM   1660 C C   . PRO A 1 220 ? 47.967 104.239 61.661 1.00 93.23  ? 244 PRO A C   1 
ATOM   1661 O O   . PRO A 1 220 ? 48.229 103.481 62.591 1.00 96.71  ? 244 PRO A O   1 
ATOM   1662 C CB  . PRO A 1 220 ? 49.815 104.692 60.007 1.00 75.46  ? 244 PRO A CB  1 
ATOM   1663 C CG  . PRO A 1 220 ? 50.978 104.061 60.665 1.00 71.61  ? 244 PRO A CG  1 
ATOM   1664 C CD  . PRO A 1 220 ? 51.315 104.949 61.844 1.00 80.27  ? 244 PRO A CD  1 
ATOM   1665 N N   . SER A 1 221 ? 46.800 104.234 61.026 1.00 88.22  ? 245 SER A N   1 
ATOM   1666 C CA  . SER A 1 221 ? 45.738 103.292 61.373 1.00 86.40  ? 245 SER A CA  1 
ATOM   1667 C C   . SER A 1 221 ? 45.040 102.795 60.096 1.00 80.74  ? 245 SER A C   1 
ATOM   1668 O O   . SER A 1 221 ? 45.222 103.371 59.022 1.00 78.25  ? 245 SER A O   1 
ATOM   1669 C CB  . SER A 1 221 ? 44.731 103.955 62.321 1.00 100.20 ? 245 SER A CB  1 
ATOM   1670 O OG  . SER A 1 221 ? 43.758 103.027 62.767 1.00 104.03 ? 245 SER A OG  1 
ATOM   1671 N N   . PHE A 1 222 ? 44.268 101.716 60.201 1.00 78.36  ? 246 PHE A N   1 
ATOM   1672 C CA  . PHE A 1 222 ? 43.573 101.201 59.026 1.00 71.66  ? 246 PHE A CA  1 
ATOM   1673 C C   . PHE A 1 222 ? 42.125 101.657 58.941 1.00 68.40  ? 246 PHE A C   1 
ATOM   1674 O O   . PHE A 1 222 ? 41.283 101.307 59.773 1.00 67.83  ? 246 PHE A O   1 
ATOM   1675 C CB  . PHE A 1 222 ? 43.695 99.678  58.937 1.00 74.35  ? 246 PHE A CB  1 
ATOM   1676 C CG  . PHE A 1 222 ? 44.998 99.225  58.341 1.00 74.71  ? 246 PHE A CG  1 
ATOM   1677 C CD1 . PHE A 1 222 ? 45.820 98.337  59.021 1.00 75.39  ? 246 PHE A CD1 1 
ATOM   1678 C CD2 . PHE A 1 222 ? 45.414 99.706  57.096 1.00 74.62  ? 246 PHE A CD2 1 
ATOM   1679 C CE1 . PHE A 1 222 ? 47.033 97.927  58.475 1.00 75.59  ? 246 PHE A CE1 1 
ATOM   1680 C CE2 . PHE A 1 222 ? 46.626 99.301  56.541 1.00 74.42  ? 246 PHE A CE2 1 
ATOM   1681 C CZ  . PHE A 1 222 ? 47.436 98.414  57.231 1.00 74.94  ? 246 PHE A CZ  1 
ATOM   1682 N N   . MET A 1 223 ? 41.849 102.452 57.909 1.00 58.26  ? 247 MET A N   1 
ATOM   1683 C CA  . MET A 1 223 ? 40.530 103.017 57.724 1.00 64.81  ? 247 MET A CA  1 
ATOM   1684 C C   . MET A 1 223 ? 39.561 102.017 57.128 1.00 69.92  ? 247 MET A C   1 
ATOM   1685 O O   . MET A 1 223 ? 38.637 101.592 57.818 1.00 62.65  ? 247 MET A O   1 
ATOM   1686 C CB  . MET A 1 223 ? 40.609 104.287 56.868 1.00 79.38  ? 247 MET A CB  1 
ATOM   1687 C CG  . MET A 1 223 ? 41.606 105.314 57.390 1.00 87.35  ? 247 MET A CG  1 
ATOM   1688 S SD  . MET A 1 223 ? 41.322 106.986 56.761 1.00 91.56  ? 247 MET A SD  1 
ATOM   1689 C CE  . MET A 1 223 ? 39.885 107.465 57.729 1.00 92.70  ? 247 MET A CE  1 
ATOM   1690 N N   . TYR A 1 224 ? 39.769 101.616 55.874 1.00 107.02 ? 248 TYR A N   1 
ATOM   1691 C CA  . TYR A 1 224 ? 38.835 100.681 55.267 1.00 116.80 ? 248 TYR A CA  1 
ATOM   1692 C C   . TYR A 1 224 ? 38.945 99.250  55.750 1.00 117.05 ? 248 TYR A C   1 
ATOM   1693 O O   . TYR A 1 224 ? 38.065 98.779  56.488 1.00 146.25 ? 248 TYR A O   1 
ATOM   1694 C CB  . TYR A 1 224 ? 38.893 100.688 53.726 1.00 87.80  ? 248 TYR A CB  1 
ATOM   1695 C CG  . TYR A 1 224 ? 38.280 99.436  53.106 1.00 65.79  ? 248 TYR A CG  1 
ATOM   1696 C CD1 . TYR A 1 224 ? 37.001 99.006  53.473 1.00 54.85  ? 248 TYR A CD1 1 
ATOM   1697 C CD2 . TYR A 1 224 ? 38.987 98.677  52.179 1.00 54.77  ? 248 TYR A CD2 1 
ATOM   1698 C CE1 . TYR A 1 224 ? 36.445 97.856  52.938 1.00 51.39  ? 248 TYR A CE1 1 
ATOM   1699 C CE2 . TYR A 1 224 ? 38.434 97.521  51.636 1.00 52.95  ? 248 TYR A CE2 1 
ATOM   1700 C CZ  . TYR A 1 224 ? 37.160 97.120  52.023 1.00 52.36  ? 248 TYR A CZ  1 
ATOM   1701 O OH  . TYR A 1 224 ? 36.595 95.985  51.490 1.00 54.77  ? 248 TYR A OH  1 
ATOM   1702 N N   . PRO A 1 225 ? 40.025 98.538  55.374 1.00 75.70  ? 249 PRO A N   1 
ATOM   1703 C CA  . PRO A 1 225 ? 40.008 97.160  55.885 1.00 63.38  ? 249 PRO A CA  1 
ATOM   1704 C C   . PRO A 1 225 ? 40.163 97.239  57.391 1.00 59.74  ? 249 PRO A C   1 
ATOM   1705 O O   . PRO A 1 225 ? 41.203 97.648  57.889 1.00 54.78  ? 249 PRO A O   1 
ATOM   1706 C CB  . PRO A 1 225 ? 41.167 96.493  55.148 1.00 44.99  ? 249 PRO A CB  1 
ATOM   1707 C CG  . PRO A 1 225 ? 41.777 97.564  54.267 1.00 41.67  ? 249 PRO A CG  1 
ATOM   1708 C CD  . PRO A 1 225 ? 41.335 98.888  54.794 1.00 54.09  ? 249 PRO A CD  1 
ATOM   1709 N N   . GLN A 1 226 ? 39.108 96.866  58.109 1.00 61.31  ? 250 GLN A N   1 
ATOM   1710 C CA  . GLN A 1 226 ? 39.097 97.025  59.553 1.00 64.13  ? 250 GLN A CA  1 
ATOM   1711 C C   . GLN A 1 226 ? 40.094 96.153  60.268 1.00 66.85  ? 250 GLN A C   1 
ATOM   1712 O O   . GLN A 1 226 ? 40.147 94.947  60.030 1.00 63.01  ? 250 GLN A O   1 
ATOM   1713 C CB  . GLN A 1 226 ? 37.695 96.745  60.126 1.00 73.42  ? 250 GLN A CB  1 
ATOM   1714 C CG  . GLN A 1 226 ? 36.546 97.448  59.428 1.00 76.82  ? 250 GLN A CG  1 
ATOM   1715 C CD  . GLN A 1 226 ? 35.387 97.734  60.373 1.00 79.03  ? 250 GLN A CD  1 
ATOM   1716 O OE1 . GLN A 1 226 ? 35.393 98.738  61.095 1.00 79.89  ? 250 GLN A OE1 1 
ATOM   1717 N NE2 . GLN A 1 226 ? 34.395 96.850  60.381 1.00 78.86  ? 250 GLN A NE2 1 
ATOM   1718 N N   . GLY A 1 227 ? 40.906 96.794  61.108 1.00 81.14  ? 251 GLY A N   1 
ATOM   1719 C CA  . GLY A 1 227 ? 41.824 96.077  61.954 1.00 82.92  ? 251 GLY A CA  1 
ATOM   1720 C C   . GLY A 1 227 ? 43.012 95.389  61.346 1.00 80.83  ? 251 GLY A C   1 
ATOM   1721 O O   . GLY A 1 227 ? 43.676 95.935  60.470 1.00 86.09  ? 251 GLY A O   1 
ATOM   1722 N N   . THR A 1 228 ? 43.223 94.154  61.784 1.00 63.90  ? 252 THR A N   1 
ATOM   1723 C CA  . THR A 1 228 ? 44.412 93.390  61.459 1.00 57.23  ? 252 THR A CA  1 
ATOM   1724 C C   . THR A 1 228 ? 44.408 92.607  60.170 1.00 54.07  ? 252 THR A C   1 
ATOM   1725 O O   . THR A 1 228 ? 45.321 92.735  59.362 1.00 50.84  ? 252 THR A O   1 
ATOM   1726 C CB  . THR A 1 228 ? 44.742 92.442  62.691 1.00 57.30  ? 252 THR A CB  1 
ATOM   1727 O OG1 . THR A 1 228 ? 45.567 93.152  63.628 1.00 57.13  ? 252 THR A OG1 1 
ATOM   1728 C CG2 . THR A 1 228 ? 45.441 91.163  62.268 1.00 57.28  ? 252 THR A CG2 1 
ATOM   1729 N N   . ALA A 1 229 ? 43.358 91.824  59.963 1.00 54.86  ? 253 ALA A N   1 
ATOM   1730 C CA  . ALA A 1 229 ? 43.275 90.959  58.802 1.00 55.52  ? 253 ALA A CA  1 
ATOM   1731 C C   . ALA A 1 229 ? 41.923 91.027  58.090 1.00 56.97  ? 253 ALA A C   1 
ATOM   1732 O O   . ALA A 1 229 ? 40.997 91.698  58.547 1.00 58.88  ? 253 ALA A O   1 
ATOM   1733 C CB  . ALA A 1 229 ? 43.538 89.511  59.257 1.00 48.17  ? 253 ALA A CB  1 
ATOM   1734 N N   . SER A 1 230 ? 41.842 90.346  56.945 1.00 55.89  ? 254 SER A N   1 
ATOM   1735 C CA  . SER A 1 230 ? 40.605 90.222  56.183 1.00 56.31  ? 254 SER A CA  1 
ATOM   1736 C C   . SER A 1 230 ? 40.742 89.081  55.185 1.00 59.63  ? 254 SER A C   1 
ATOM   1737 O O   . SER A 1 230 ? 41.842 88.753  54.745 1.00 58.73  ? 254 SER A O   1 
ATOM   1738 C CB  . SER A 1 230 ? 40.229 91.520  55.455 1.00 52.98  ? 254 SER A CB  1 
ATOM   1739 O OG  . SER A 1 230 ? 41.244 91.953  54.561 1.00 52.41  ? 254 SER A OG  1 
ATOM   1740 N N   . SER A 1 231 ? 39.617 88.464  54.849 1.00 64.08  ? 255 SER A N   1 
ATOM   1741 C CA  . SER A 1 231 ? 39.604 87.375  53.909 1.00 64.30  ? 255 SER A CA  1 
ATOM   1742 C C   . SER A 1 231 ? 38.849 87.809  52.653 1.00 60.50  ? 255 SER A C   1 
ATOM   1743 O O   . SER A 1 231 ? 38.050 88.741  52.701 1.00 61.40  ? 255 SER A O   1 
ATOM   1744 C CB  . SER A 1 231 ? 38.921 86.161  54.528 1.00 70.00  ? 255 SER A CB  1 
ATOM   1745 O OG  . SER A 1 231 ? 39.031 85.031  53.674 1.00 78.45  ? 255 SER A OG  1 
ATOM   1746 N N   . GLN A 1 232 ? 39.124 87.135  51.531 1.00 47.00  ? 256 GLN A N   1 
ATOM   1747 C CA  . GLN A 1 232 ? 38.462 87.427  50.279 1.00 40.55  ? 256 GLN A CA  1 
ATOM   1748 C C   . GLN A 1 232 ? 38.391 86.202  49.421 1.00 39.87  ? 256 GLN A C   1 
ATOM   1749 O O   . GLN A 1 232 ? 39.387 85.521  49.213 1.00 37.50  ? 256 GLN A O   1 
ATOM   1750 C CB  . GLN A 1 232 ? 39.200 88.523  49.482 1.00 49.84  ? 256 GLN A CB  1 
ATOM   1751 C CG  . GLN A 1 232 ? 38.801 89.943  49.817 1.00 54.60  ? 256 GLN A CG  1 
ATOM   1752 C CD  . GLN A 1 232 ? 39.398 90.958  48.861 1.00 58.47  ? 256 GLN A CD  1 
ATOM   1753 O OE1 . GLN A 1 232 ? 39.368 90.766  47.648 1.00 58.84  ? 256 GLN A OE1 1 
ATOM   1754 N NE2 . GLN A 1 232 ? 39.929 92.059  49.407 1.00 59.63  ? 256 GLN A NE2 1 
ATOM   1755 N N   . MET A 1 233 ? 37.195 85.901  48.945 1.00 55.79  ? 257 MET A N   1 
ATOM   1756 C CA  . MET A 1 233 ? 37.028 84.825  47.992 1.00 62.45  ? 257 MET A CA  1 
ATOM   1757 C C   . MET A 1 233 ? 36.950 85.518  46.612 1.00 65.69  ? 257 MET A C   1 
ATOM   1758 O O   . MET A 1 233 ? 36.478 86.657  46.511 1.00 69.61  ? 257 MET A O   1 
ATOM   1759 C CB  . MET A 1 233 ? 35.764 84.033  48.287 1.00 62.78  ? 257 MET A CB  1 
ATOM   1760 C CG  . MET A 1 233 ? 35.605 82.796  47.438 1.00 65.83  ? 257 MET A CG  1 
ATOM   1761 S SD  . MET A 1 233 ? 35.068 83.232  45.777 1.00 70.06  ? 257 MET A SD  1 
ATOM   1762 C CE  . MET A 1 233 ? 33.383 83.797  46.109 1.00 69.16  ? 257 MET A CE  1 
ATOM   1763 N N   . VAL A 1 234 ? 37.442 84.842  45.570 1.00 62.75  ? 258 VAL A N   1 
ATOM   1764 C CA  . VAL A 1 234 ? 37.442 85.396  44.207 1.00 60.00  ? 258 VAL A CA  1 
ATOM   1765 C C   . VAL A 1 234 ? 37.332 84.295  43.148 1.00 56.92  ? 258 VAL A C   1 
ATOM   1766 O O   . VAL A 1 234 ? 37.933 83.216  43.286 1.00 56.87  ? 258 VAL A O   1 
ATOM   1767 C CB  . VAL A 1 234 ? 38.693 86.299  43.971 1.00 56.73  ? 258 VAL A CB  1 
ATOM   1768 C CG1 . VAL A 1 234 ? 39.884 85.496  43.482 1.00 56.00  ? 258 VAL A CG1 1 
ATOM   1769 C CG2 . VAL A 1 234 ? 38.350 87.403  43.002 1.00 58.14  ? 258 VAL A CG2 1 
ATOM   1770 N N   . LEU A 1 235 ? 36.548 84.561  42.103 1.00 50.49  ? 259 LEU A N   1 
ATOM   1771 C CA  . LEU A 1 235 ? 36.304 83.544  41.086 1.00 50.60  ? 259 LEU A CA  1 
ATOM   1772 C C   . LEU A 1 235 ? 37.394 83.469  40.031 1.00 51.30  ? 259 LEU A C   1 
ATOM   1773 O O   . LEU A 1 235 ? 37.921 84.490  39.588 1.00 46.39  ? 259 LEU A O   1 
ATOM   1774 C CB  . LEU A 1 235 ? 34.943 83.770  40.391 1.00 54.18  ? 259 LEU A CB  1 
ATOM   1775 C CG  . LEU A 1 235 ? 33.644 83.555  41.189 1.00 56.82  ? 259 LEU A CG  1 
ATOM   1776 C CD1 . LEU A 1 235 ? 32.453 83.852  40.311 1.00 57.48  ? 259 LEU A CD1 1 
ATOM   1777 C CD2 . LEU A 1 235 ? 33.557 82.135  41.724 1.00 58.63  ? 259 LEU A CD2 1 
ATOM   1778 N N   . ARG A 1 236 ? 37.745 82.245  39.655 1.00 61.46  ? 260 ARG A N   1 
ATOM   1779 C CA  . ARG A 1 236 ? 38.726 82.017  38.615 1.00 64.86  ? 260 ARG A CA  1 
ATOM   1780 C C   . ARG A 1 236 ? 38.354 82.838  37.387 1.00 67.82  ? 260 ARG A C   1 
ATOM   1781 O O   . ARG A 1 236 ? 37.213 82.777  36.922 1.00 71.94  ? 260 ARG A O   1 
ATOM   1782 C CB  . ARG A 1 236 ? 38.734 80.543  38.232 1.00 63.14  ? 260 ARG A CB  1 
ATOM   1783 C CG  . ARG A 1 236 ? 39.640 80.215  37.075 1.00 62.71  ? 260 ARG A CG  1 
ATOM   1784 C CD  . ARG A 1 236 ? 39.648 78.732  36.789 1.00 64.63  ? 260 ARG A CD  1 
ATOM   1785 N NE  . ARG A 1 236 ? 40.728 78.392  35.875 1.00 68.17  ? 260 ARG A NE  1 
ATOM   1786 C CZ  . ARG A 1 236 ? 40.606 78.319  34.552 1.00 70.36  ? 260 ARG A CZ  1 
ATOM   1787 N NH1 . ARG A 1 236 ? 39.434 78.555  33.971 1.00 69.39  ? 260 ARG A NH1 1 
ATOM   1788 N NH2 . ARG A 1 236 ? 41.668 78.014  33.808 1.00 72.53  ? 260 ARG A NH2 1 
ATOM   1789 N N   . GLY A 1 237 ? 39.312 83.613  36.877 1.00 65.37  ? 261 GLY A N   1 
ATOM   1790 C CA  . GLY A 1 237 ? 39.084 84.413  35.682 1.00 65.03  ? 261 GLY A CA  1 
ATOM   1791 C C   . GLY A 1 237 ? 38.713 85.863  35.941 1.00 63.88  ? 261 GLY A C   1 
ATOM   1792 O O   . GLY A 1 237 ? 38.921 86.725  35.082 1.00 66.80  ? 261 GLY A O   1 
ATOM   1793 N N   . MET A 1 238 ? 38.168 86.135  37.127 1.00 54.66  ? 262 MET A N   1 
ATOM   1794 C CA  . MET A 1 238 ? 37.762 87.485  37.494 1.00 52.06  ? 262 MET A CA  1 
ATOM   1795 C C   . MET A 1 238 ? 38.953 88.274  37.997 1.00 51.18  ? 262 MET A C   1 
ATOM   1796 O O   . MET A 1 238 ? 40.058 87.746  38.073 1.00 46.61  ? 262 MET A O   1 
ATOM   1797 C CB  . MET A 1 238 ? 36.670 87.445  38.574 1.00 60.25  ? 262 MET A CB  1 
ATOM   1798 C CG  . MET A 1 238 ? 35.396 86.706  38.162 1.00 64.88  ? 262 MET A CG  1 
ATOM   1799 S SD  . MET A 1 238 ? 34.585 87.388  36.694 1.00 71.08  ? 262 MET A SD  1 
ATOM   1800 C CE  . MET A 1 238 ? 33.806 88.878  37.390 1.00 70.53  ? 262 MET A CE  1 
ATOM   1801 N N   . ASP A 1 239 ? 38.730 89.546  38.312 1.00 56.07  ? 263 ASP A N   1 
ATOM   1802 C CA  . ASP A 1 239 ? 39.785 90.395  38.857 1.00 57.16  ? 263 ASP A CA  1 
ATOM   1803 C C   . ASP A 1 239 ? 39.797 90.310  40.386 1.00 54.61  ? 263 ASP A C   1 
ATOM   1804 O O   . ASP A 1 239 ? 38.772 90.027  41.015 1.00 53.72  ? 263 ASP A O   1 
ATOM   1805 C CB  . ASP A 1 239 ? 39.577 91.862  38.450 1.00 72.18  ? 263 ASP A CB  1 
ATOM   1806 C CG  . ASP A 1 239 ? 39.791 92.101  36.964 1.00 79.18  ? 263 ASP A CG  1 
ATOM   1807 O OD1 . ASP A 1 239 ? 40.017 91.119  36.205 1.00 82.46  ? 263 ASP A OD1 1 
ATOM   1808 O OD2 . ASP A 1 239 ? 39.727 93.286  36.557 1.00 82.33  ? 263 ASP A OD2 1 
ATOM   1809 N N   . LEU A 1 240 ? 40.969 90.558  40.974 1.00 52.11  ? 264 LEU A N   1 
ATOM   1810 C CA  . LEU A 1 240 ? 41.116 90.559  42.418 1.00 48.92  ? 264 LEU A CA  1 
ATOM   1811 C C   . LEU A 1 240 ? 41.537 91.955  42.832 1.00 48.75  ? 264 LEU A C   1 
ATOM   1812 O O   . LEU A 1 240 ? 42.545 92.471  42.356 1.00 49.29  ? 264 LEU A O   1 
ATOM   1813 C CB  . LEU A 1 240 ? 42.150 89.512  42.838 1.00 53.75  ? 264 LEU A CB  1 
ATOM   1814 C CG  . LEU A 1 240 ? 42.614 89.196  44.292 1.00 53.19  ? 264 LEU A CG  1 
ATOM   1815 C CD1 . LEU A 1 240 ? 43.950 89.847  44.552 1.00 50.79  ? 264 LEU A CD1 1 
ATOM   1816 C CD2 . LEU A 1 240 ? 41.586 89.562  45.356 1.00 51.91  ? 264 LEU A CD2 1 
ATOM   1817 N N   . LEU A 1 241 ? 40.752 92.568  43.712 1.00 54.46  ? 265 LEU A N   1 
ATOM   1818 C CA  . LEU A 1 241 ? 41.033 93.925  44.165 1.00 59.26  ? 265 LEU A CA  1 
ATOM   1819 C C   . LEU A 1 241 ? 41.347 93.977  45.650 1.00 60.03  ? 265 LEU A C   1 
ATOM   1820 O O   . LEU A 1 241 ? 40.518 93.625  46.483 1.00 62.66  ? 265 LEU A O   1 
ATOM   1821 C CB  . LEU A 1 241 ? 39.841 94.840  43.860 1.00 59.44  ? 265 LEU A CB  1 
ATOM   1822 C CG  . LEU A 1 241 ? 40.100 96.251  43.280 1.00 61.12  ? 265 LEU A CG  1 
ATOM   1823 C CD1 . LEU A 1 241 ? 40.642 97.215  44.321 1.00 59.65  ? 265 LEU A CD1 1 
ATOM   1824 C CD2 . LEU A 1 241 ? 41.053 96.158  42.083 1.00 61.46  ? 265 LEU A CD2 1 
ATOM   1825 N N   . LEU A 1 242 ? 42.557 94.412  45.970 1.00 54.22  ? 266 LEU A N   1 
ATOM   1826 C CA  . LEU A 1 242 ? 42.992 94.529  47.347 1.00 53.62  ? 266 LEU A CA  1 
ATOM   1827 C C   . LEU A 1 242 ? 43.148 96.007  47.668 1.00 54.61  ? 266 LEU A C   1 
ATOM   1828 O O   . LEU A 1 242 ? 43.706 96.760  46.867 1.00 53.22  ? 266 LEU A O   1 
ATOM   1829 C CB  . LEU A 1 242 ? 44.334 93.824  47.539 1.00 56.87  ? 266 LEU A CB  1 
ATOM   1830 C CG  . LEU A 1 242 ? 44.467 92.413  46.968 1.00 58.13  ? 266 LEU A CG  1 
ATOM   1831 C CD1 . LEU A 1 242 ? 45.922 92.152  46.628 1.00 59.49  ? 266 LEU A CD1 1 
ATOM   1832 C CD2 . LEU A 1 242 ? 43.925 91.382  47.951 1.00 58.35  ? 266 LEU A CD2 1 
ATOM   1833 N N   . GLU A 1 243 ? 42.670 96.414  48.842 1.00 54.98  ? 267 GLU A N   1 
ATOM   1834 C CA  . GLU A 1 243 ? 42.739 97.814  49.237 1.00 56.09  ? 267 GLU A CA  1 
ATOM   1835 C C   . GLU A 1 243 ? 43.267 97.991  50.644 1.00 55.50  ? 267 GLU A C   1 
ATOM   1836 O O   . GLU A 1 243 ? 43.088 97.126  51.499 1.00 52.42  ? 267 GLU A O   1 
ATOM   1837 C CB  . GLU A 1 243 ? 41.344 98.453  49.176 1.00 77.99  ? 267 GLU A CB  1 
ATOM   1838 C CG  . GLU A 1 243 ? 40.815 98.713  47.775 1.00 87.67  ? 267 GLU A CG  1 
ATOM   1839 C CD  . GLU A 1 243 ? 39.455 99.397  47.781 1.00 92.75  ? 267 GLU A CD  1 
ATOM   1840 O OE1 . GLU A 1 243 ? 38.475 98.793  48.284 1.00 94.11  ? 267 GLU A OE1 1 
ATOM   1841 O OE2 . GLU A 1 243 ? 39.370 100.542 47.283 1.00 94.33  ? 267 GLU A OE2 1 
ATOM   1842 N N   . CYS A 1 244 ? 43.923 99.122  50.867 1.00 56.88  ? 268 CYS A N   1 
ATOM   1843 C CA  . CYS A 1 244 ? 44.416 99.486  52.176 1.00 56.37  ? 268 CYS A CA  1 
ATOM   1844 C C   . CYS A 1 244 ? 44.361 100.999 52.289 1.00 55.57  ? 268 CYS A C   1 
ATOM   1845 O O   . CYS A 1 244 ? 45.099 101.700 51.595 1.00 55.18  ? 268 CYS A O   1 
ATOM   1846 C CB  . CYS A 1 244 ? 45.861 99.008  52.398 1.00 66.85  ? 268 CYS A CB  1 
ATOM   1847 S SG  . CYS A 1 244 ? 46.035 97.220  52.699 1.00 73.03  ? 268 CYS A SG  1 
ATOM   1848 N N   . ILE A 1 245 ? 43.481 101.501 53.149 1.00 59.43  ? 269 ILE A N   1 
ATOM   1849 C CA  . ILE A 1 245 ? 43.387 102.944 53.358 1.00 63.39  ? 269 ILE A CA  1 
ATOM   1850 C C   . ILE A 1 245 ? 43.835 103.257 54.787 1.00 66.43  ? 269 ILE A C   1 
ATOM   1851 O O   . ILE A 1 245 ? 43.269 102.738 55.760 1.00 63.07  ? 269 ILE A O   1 
ATOM   1852 C CB  . ILE A 1 245 ? 41.949 103.485 53.156 1.00 76.98  ? 269 ILE A CB  1 
ATOM   1853 C CG1 . ILE A 1 245 ? 41.321 102.929 51.860 1.00 78.65  ? 269 ILE A CG1 1 
ATOM   1854 C CG2 . ILE A 1 245 ? 41.977 105.017 53.205 1.00 76.94  ? 269 ILE A CG2 1 
ATOM   1855 C CD1 . ILE A 1 245 ? 42.020 103.294 50.538 1.00 85.60  ? 269 ILE A CD1 1 
ATOM   1856 N N   . ALA A 1 246 ? 44.828 104.139 54.892 1.00 76.13  ? 270 ALA A N   1 
ATOM   1857 C CA  . ALA A 1 246 ? 45.442 104.484 56.163 1.00 83.25  ? 270 ALA A CA  1 
ATOM   1858 C C   . ALA A 1 246 ? 45.196 105.903 56.650 1.00 85.08  ? 270 ALA A C   1 
ATOM   1859 O O   . ALA A 1 246 ? 45.151 106.848 55.856 1.00 87.18  ? 270 ALA A O   1 
ATOM   1860 C CB  . ALA A 1 246 ? 46.943 104.231 56.059 1.00 93.16  ? 270 ALA A CB  1 
ATOM   1861 N N   . SER A 1 247 ? 45.044 106.039 57.966 1.00 87.53  ? 271 SER A N   1 
ATOM   1862 C CA  . SER A 1 247 ? 44.840 107.338 58.605 1.00 84.53  ? 271 SER A CA  1 
ATOM   1863 C C   . SER A 1 247 ? 46.057 107.741 59.437 1.00 84.61  ? 271 SER A C   1 
ATOM   1864 O O   . SER A 1 247 ? 46.252 107.262 60.557 1.00 91.54  ? 271 SER A O   1 
ATOM   1865 C CB  . SER A 1 247 ? 43.606 107.313 59.510 1.00 84.18  ? 271 SER A CB  1 
ATOM   1866 O OG  . SER A 1 247 ? 43.709 106.297 60.493 1.00 80.98  ? 271 SER A OG  1 
ATOM   1867 N N   . GLY A 1 248 ? 46.876 108.621 58.875 1.00 88.23  ? 272 GLY A N   1 
ATOM   1868 C CA  . GLY A 1 248 ? 48.053 109.103 59.573 1.00 97.33  ? 272 GLY A CA  1 
ATOM   1869 C C   . GLY A 1 248 ? 48.283 110.579 59.310 1.00 110.86 ? 272 GLY A C   1 
ATOM   1870 O O   . GLY A 1 248 ? 47.935 111.082 58.237 1.00 101.89 ? 272 GLY A O   1 
ATOM   1871 N N   . VAL A 1 249 ? 48.866 111.280 60.287 1.00 151.36 ? 273 VAL A N   1 
ATOM   1872 C CA  . VAL A 1 249 ? 49.130 112.718 60.135 1.00 167.19 ? 273 VAL A CA  1 
ATOM   1873 C C   . VAL A 1 249 ? 50.155 112.876 59.005 1.00 165.93 ? 273 VAL A C   1 
ATOM   1874 O O   . VAL A 1 249 ? 49.804 113.423 57.950 1.00 189.52 ? 273 VAL A O   1 
ATOM   1875 C CB  . VAL A 1 249 ? 49.540 113.363 61.471 1.00 153.09 ? 273 VAL A CB  1 
ATOM   1876 C CG1 . VAL A 1 249 ? 49.815 114.850 61.262 1.00 147.44 ? 273 VAL A CG1 1 
ATOM   1877 C CG2 . VAL A 1 249 ? 48.404 113.170 62.495 1.00 147.70 ? 273 VAL A CG2 1 
ATOM   1878 N N   . PRO A 1 250 ? 51.429 112.472 59.201 1.00 126.61 ? 274 PRO A N   1 
ATOM   1879 C CA  . PRO A 1 250 ? 52.280 112.644 58.007 1.00 117.60 ? 274 PRO A CA  1 
ATOM   1880 C C   . PRO A 1 250 ? 51.656 111.605 57.043 1.00 118.23 ? 274 PRO A C   1 
ATOM   1881 O O   . PRO A 1 250 ? 51.716 110.392 57.303 1.00 120.98 ? 274 PRO A O   1 
ATOM   1882 C CB  . PRO A 1 250 ? 53.661 112.207 58.472 1.00 73.72  ? 274 PRO A CB  1 
ATOM   1883 C CG  . PRO A 1 250 ? 53.606 112.281 59.971 1.00 66.50  ? 274 PRO A CG  1 
ATOM   1884 C CD  . PRO A 1 250 ? 52.190 111.940 60.345 1.00 83.38  ? 274 PRO A CD  1 
ATOM   1885 N N   . THR A 1 251 ? 51.056 112.097 55.951 1.00 103.75 ? 275 THR A N   1 
ATOM   1886 C CA  . THR A 1 251 ? 50.289 111.267 55.005 1.00 100.47 ? 275 THR A CA  1 
ATOM   1887 C C   . THR A 1 251 ? 50.992 109.961 54.679 1.00 92.54  ? 275 THR A C   1 
ATOM   1888 O O   . THR A 1 251 ? 52.036 109.949 54.021 1.00 95.60  ? 275 THR A O   1 
ATOM   1889 C CB  . THR A 1 251 ? 49.908 112.078 53.750 1.00 88.73  ? 275 THR A CB  1 
ATOM   1890 O OG1 . THR A 1 251 ? 49.024 113.148 54.134 1.00 89.97  ? 275 THR A OG1 1 
ATOM   1891 C CG2 . THR A 1 251 ? 49.205 111.187 52.725 1.00 89.79  ? 275 THR A CG2 1 
ATOM   1892 N N   . PRO A 1 252 ? 50.411 108.834 55.145 1.00 75.53  ? 276 PRO A N   1 
ATOM   1893 C CA  . PRO A 1 252 ? 50.933 107.476 54.970 1.00 70.06  ? 276 PRO A CA  1 
ATOM   1894 C C   . PRO A 1 252 ? 51.131 107.008 53.563 1.00 69.25  ? 276 PRO A C   1 
ATOM   1895 O O   . PRO A 1 252 ? 50.418 107.438 52.671 1.00 62.85  ? 276 PRO A O   1 
ATOM   1896 C CB  . PRO A 1 252 ? 49.902 106.593 55.671 1.00 69.81  ? 276 PRO A CB  1 
ATOM   1897 C CG  . PRO A 1 252 ? 49.170 107.499 56.578 1.00 72.21  ? 276 PRO A CG  1 
ATOM   1898 C CD  . PRO A 1 252 ? 49.111 108.806 55.841 1.00 74.75  ? 276 PRO A CD  1 
ATOM   1899 N N   . ASP A 1 253 ? 52.106 106.120 53.381 1.00 81.48  ? 277 ASP A N   1 
ATOM   1900 C CA  . ASP A 1 253 ? 52.355 105.497 52.092 1.00 88.71  ? 277 ASP A CA  1 
ATOM   1901 C C   . ASP A 1 253 ? 51.989 104.013 52.216 1.00 87.48  ? 277 ASP A C   1 
ATOM   1902 O O   . ASP A 1 253 ? 52.193 103.404 53.268 1.00 90.83  ? 277 ASP A O   1 
ATOM   1903 C CB  . ASP A 1 253 ? 53.823 105.620 51.696 1.00 99.59  ? 277 ASP A CB  1 
ATOM   1904 C CG  . ASP A 1 253 ? 54.279 107.063 51.572 1.00 106.13 ? 277 ASP A CG  1 
ATOM   1905 O OD1 . ASP A 1 253 ? 53.564 107.876 50.939 1.00 108.81 ? 277 ASP A OD1 1 
ATOM   1906 O OD2 . ASP A 1 253 ? 55.368 107.379 52.098 1.00 108.74 ? 277 ASP A OD2 1 
ATOM   1907 N N   . ILE A 1 254 ? 51.453 103.441 51.139 1.00 75.24  ? 278 ILE A N   1 
ATOM   1908 C CA  . ILE A 1 254 ? 51.074 102.035 51.119 1.00 69.85  ? 278 ILE A CA  1 
ATOM   1909 C C   . ILE A 1 254 ? 52.058 101.243 50.259 1.00 65.97  ? 278 ILE A C   1 
ATOM   1910 O O   . ILE A 1 254 ? 52.536 101.745 49.244 1.00 64.13  ? 278 ILE A O   1 
ATOM   1911 C CB  . ILE A 1 254 ? 49.607 101.867 50.584 1.00 71.02  ? 278 ILE A CB  1 
ATOM   1912 C CG1 . ILE A 1 254 ? 48.599 102.260 51.672 1.00 71.85  ? 278 ILE A CG1 1 
ATOM   1913 C CG2 . ILE A 1 254 ? 49.328 100.438 50.163 1.00 70.36  ? 278 ILE A CG2 1 
ATOM   1914 C CD1 . ILE A 1 254 ? 48.507 103.756 51.949 1.00 74.90  ? 278 ILE A CD1 1 
ATOM   1915 N N   . ALA A 1 255 ? 52.400 100.029 50.699 1.00 68.80  ? 279 ALA A N   1 
ATOM   1916 C CA  . ALA A 1 255 ? 53.296 99.138  49.944 1.00 69.05  ? 279 ALA A CA  1 
ATOM   1917 C C   . ALA A 1 255 ? 52.735 97.711  49.982 1.00 69.58  ? 279 ALA A C   1 
ATOM   1918 O O   . ALA A 1 255 ? 52.129 97.309  50.974 1.00 72.61  ? 279 ALA A O   1 
ATOM   1919 C CB  . ALA A 1 255 ? 54.704 99.195  50.484 1.00 59.01  ? 279 ALA A CB  1 
ATOM   1920 N N   . TRP A 1 256 ? 52.972 96.940  48.921 1.00 64.87  ? 280 TRP A N   1 
ATOM   1921 C CA  . TRP A 1 256 ? 52.346 95.625  48.778 1.00 61.43  ? 280 TRP A CA  1 
ATOM   1922 C C   . TRP A 1 256 ? 53.269 94.431  48.639 1.00 59.78  ? 280 TRP A C   1 
ATOM   1923 O O   . TRP A 1 256 ? 54.326 94.530  48.023 1.00 57.89  ? 280 TRP A O   1 
ATOM   1924 C CB  . TRP A 1 256 ? 51.388 95.675  47.568 1.00 64.08  ? 280 TRP A CB  1 
ATOM   1925 C CG  . TRP A 1 256 ? 50.203 96.562  47.778 1.00 65.75  ? 280 TRP A CG  1 
ATOM   1926 C CD1 . TRP A 1 256 ? 50.101 97.882  47.472 1.00 67.14  ? 280 TRP A CD1 1 
ATOM   1927 C CD2 . TRP A 1 256 ? 48.954 96.189  48.372 1.00 67.42  ? 280 TRP A CD2 1 
ATOM   1928 N NE1 . TRP A 1 256 ? 48.866 98.359  47.834 1.00 67.55  ? 280 TRP A NE1 1 
ATOM   1929 C CE2 . TRP A 1 256 ? 48.142 97.339  48.389 1.00 67.73  ? 280 TRP A CE2 1 
ATOM   1930 C CE3 . TRP A 1 256 ? 48.443 94.992  48.894 1.00 67.46  ? 280 TRP A CE3 1 
ATOM   1931 C CZ2 . TRP A 1 256 ? 46.846 97.332  48.906 1.00 67.78  ? 280 TRP A CZ2 1 
ATOM   1932 C CZ3 . TRP A 1 256 ? 47.158 94.984  49.407 1.00 68.36  ? 280 TRP A CZ3 1 
ATOM   1933 C CH2 . TRP A 1 256 ? 46.372 96.149  49.409 1.00 68.08  ? 280 TRP A CH2 1 
ATOM   1934 N N   . TYR A 1 257 ? 52.847 93.303  49.211 1.00 53.29  ? 281 TYR A N   1 
ATOM   1935 C CA  . TYR A 1 257 ? 53.620 92.071  49.179 1.00 53.96  ? 281 TYR A CA  1 
ATOM   1936 C C   . TYR A 1 257 ? 52.724 90.841  49.183 1.00 55.76  ? 281 TYR A C   1 
ATOM   1937 O O   . TYR A 1 257 ? 51.566 90.909  49.591 1.00 55.16  ? 281 TYR A O   1 
ATOM   1938 C CB  . TYR A 1 257 ? 54.512 91.944  50.437 1.00 57.72  ? 281 TYR A CB  1 
ATOM   1939 C CG  . TYR A 1 257 ? 55.390 93.134  50.774 1.00 59.82  ? 281 TYR A CG  1 
ATOM   1940 C CD1 . TYR A 1 257 ? 54.900 94.190  51.544 1.00 59.51  ? 281 TYR A CD1 1 
ATOM   1941 C CD2 . TYR A 1 257 ? 56.716 93.197  50.331 1.00 60.11  ? 281 TYR A CD2 1 
ATOM   1942 C CE1 . TYR A 1 257 ? 55.703 95.281  51.868 1.00 60.15  ? 281 TYR A CE1 1 
ATOM   1943 C CE2 . TYR A 1 257 ? 57.527 94.288  50.650 1.00 60.78  ? 281 TYR A CE2 1 
ATOM   1944 C CZ  . TYR A 1 257 ? 57.010 95.324  51.418 1.00 60.85  ? 281 TYR A CZ  1 
ATOM   1945 O OH  . TYR A 1 257 ? 57.791 96.412  51.733 1.00 61.87  ? 281 TYR A OH  1 
ATOM   1946 N N   . LYS A 1 258 ? 53.269 89.726  48.698 1.00 69.45  ? 282 LYS A N   1 
ATOM   1947 C CA  . LYS A 1 258 ? 52.607 88.428  48.813 1.00 73.06  ? 282 LYS A CA  1 
ATOM   1948 C C   . LYS A 1 258 ? 53.567 87.559  49.673 1.00 77.44  ? 282 LYS A C   1 
ATOM   1949 O O   . LYS A 1 258 ? 54.782 87.569  49.456 1.00 83.45  ? 282 LYS A O   1 
ATOM   1950 C CB  . LYS A 1 258 ? 52.370 87.776  47.452 1.00 58.60  ? 282 LYS A CB  1 
ATOM   1951 C CG  . LYS A 1 258 ? 51.552 86.489  47.518 1.00 53.68  ? 282 LYS A CG  1 
ATOM   1952 C CD  . LYS A 1 258 ? 51.288 85.913  46.135 1.00 49.98  ? 282 LYS A CD  1 
ATOM   1953 C CE  . LYS A 1 258 ? 50.556 84.588  46.230 1.00 49.34  ? 282 LYS A CE  1 
ATOM   1954 N NZ  . LYS A 1 258 ? 50.344 83.948  44.901 1.00 51.05  ? 282 LYS A NZ  1 
ATOM   1955 N N   . LYS A 1 259 ? 53.025 86.833  50.653 1.00 70.81  ? 283 LYS A N   1 
ATOM   1956 C CA  . LYS A 1 259 ? 53.845 85.998  51.534 1.00 71.47  ? 283 LYS A CA  1 
ATOM   1957 C C   . LYS A 1 259 ? 54.552 84.872  50.789 1.00 76.06  ? 283 LYS A C   1 
ATOM   1958 O O   . LYS A 1 259 ? 53.922 84.110  50.050 1.00 70.59  ? 283 LYS A O   1 
ATOM   1959 C CB  . LYS A 1 259 ? 53.008 85.410  52.692 1.00 76.39  ? 283 LYS A CB  1 
ATOM   1960 C CG  . LYS A 1 259 ? 52.779 86.381  53.855 1.00 81.51  ? 283 LYS A CG  1 
ATOM   1961 C CD  . LYS A 1 259 ? 52.094 85.699  55.038 1.00 83.58  ? 283 LYS A CD  1 
ATOM   1962 C CE  . LYS A 1 259 ? 51.875 86.668  56.200 1.00 84.11  ? 283 LYS A CE  1 
ATOM   1963 N NZ  . LYS A 1 259 ? 51.228 86.001  57.368 1.00 85.07  ? 283 LYS A NZ  1 
ATOM   1964 N N   . GLY A 1 260 ? 55.872 84.800  50.981 1.00 109.23 ? 284 GLY A N   1 
ATOM   1965 C CA  . GLY A 1 260 ? 56.701 83.771  50.363 1.00 120.61 ? 284 GLY A CA  1 
ATOM   1966 C C   . GLY A 1 260 ? 56.554 83.698  48.856 1.00 123.98 ? 284 GLY A C   1 
ATOM   1967 O O   . GLY A 1 260 ? 56.396 82.615  48.287 1.00 128.34 ? 284 GLY A O   1 
ATOM   1968 N N   . GLY A 1 261 ? 56.609 84.862  48.215 1.00 97.68  ? 285 GLY A N   1 
ATOM   1969 C CA  . GLY A 1 261 ? 56.454 84.945  46.775 1.00 93.33  ? 285 GLY A CA  1 
ATOM   1970 C C   . GLY A 1 261 ? 56.509 86.373  46.264 1.00 89.83  ? 285 GLY A C   1 
ATOM   1971 O O   . GLY A 1 261 ? 56.527 87.332  47.048 1.00 91.19  ? 285 GLY A O   1 
ATOM   1972 N N   . ASP A 1 262 ? 56.565 86.506  44.942 1.00 97.15  ? 286 ASP A N   1 
ATOM   1973 C CA  . ASP A 1 262 ? 56.573 87.811  44.298 1.00 98.27  ? 286 ASP A CA  1 
ATOM   1974 C C   . ASP A 1 262 ? 55.217 88.090  43.648 1.00 95.39  ? 286 ASP A C   1 
ATOM   1975 O O   . ASP A 1 262 ? 54.560 87.181  43.130 1.00 88.85  ? 286 ASP A O   1 
ATOM   1976 C CB  . ASP A 1 262 ? 57.665 87.882  43.217 1.00 105.75 ? 286 ASP A CB  1 
ATOM   1977 C CG  . ASP A 1 262 ? 59.047 88.151  43.790 1.00 114.45 ? 286 ASP A CG  1 
ATOM   1978 O OD1 . ASP A 1 262 ? 59.210 89.136  44.549 1.00 118.19 ? 286 ASP A OD1 1 
ATOM   1979 O OD2 . ASP A 1 262 ? 59.979 87.382  43.472 1.00 118.54 ? 286 ASP A OD2 1 
ATOM   1980 N N   . LEU A 1 263 ? 54.797 89.352  43.706 1.00 87.84  ? 287 LEU A N   1 
ATOM   1981 C CA  . LEU A 1 263 ? 53.561 89.784  43.051 1.00 90.86  ? 287 LEU A CA  1 
ATOM   1982 C C   . LEU A 1 263 ? 53.873 89.777  41.548 1.00 95.68  ? 287 LEU A C   1 
ATOM   1983 O O   . LEU A 1 263 ? 54.862 90.381  41.102 1.00 103.69 ? 287 LEU A O   1 
ATOM   1984 C CB  . LEU A 1 263 ? 53.166 91.187  43.512 1.00 87.07  ? 287 LEU A CB  1 
ATOM   1985 C CG  . LEU A 1 263 ? 53.423 91.531  44.981 1.00 75.88  ? 287 LEU A CG  1 
ATOM   1986 C CD1 . LEU A 1 263 ? 54.734 92.319  45.117 1.00 70.56  ? 287 LEU A CD1 1 
ATOM   1987 C CD2 . LEU A 1 263 ? 52.262 92.336  45.535 1.00 70.55  ? 287 LEU A CD2 1 
ATOM   1988 N N   . PRO A 1 264 ? 53.029 89.097  40.748 1.00 119.16 ? 288 PRO A N   1 
ATOM   1989 C CA  . PRO A 1 264 ? 53.245 89.011  39.292 1.00 123.54 ? 288 PRO A CA  1 
ATOM   1990 C C   . PRO A 1 264 ? 53.235 90.369  38.611 1.00 132.62 ? 288 PRO A C   1 
ATOM   1991 O O   . PRO A 1 264 ? 52.181 90.988  38.494 1.00 146.19 ? 288 PRO A O   1 
ATOM   1992 C CB  . PRO A 1 264 ? 52.129 88.078  38.823 1.00 84.29  ? 288 PRO A CB  1 
ATOM   1993 C CG  . PRO A 1 264 ? 51.049 88.229  39.858 1.00 73.51  ? 288 PRO A CG  1 
ATOM   1994 C CD  . PRO A 1 264 ? 51.759 88.465  41.159 1.00 80.23  ? 288 PRO A CD  1 
ATOM   1995 N N   . SER A 1 265 ? 54.405 90.816  38.146 1.00 125.45 ? 289 SER A N   1 
ATOM   1996 C CA  . SER A 1 265 ? 54.549 92.156  37.567 1.00 123.76 ? 289 SER A CA  1 
ATOM   1997 C C   . SER A 1 265 ? 53.709 92.436  36.328 1.00 120.02 ? 289 SER A C   1 
ATOM   1998 O O   . SER A 1 265 ? 53.439 93.600  36.014 1.00 117.45 ? 289 SER A O   1 
ATOM   1999 C CB  . SER A 1 265 ? 56.029 92.465  37.279 1.00 134.95 ? 289 SER A CB  1 
ATOM   2000 O OG  . SER A 1 265 ? 56.450 91.883  36.057 1.00 141.41 ? 289 SER A OG  1 
ATOM   2001 N N   . ASP A 1 266 ? 53.298 91.380  35.626 1.00 112.15 ? 290 ASP A N   1 
ATOM   2002 C CA  . ASP A 1 266 ? 52.464 91.537  34.435 1.00 107.83 ? 290 ASP A CA  1 
ATOM   2003 C C   . ASP A 1 266 ? 50.973 91.670  34.771 1.00 102.60 ? 290 ASP A C   1 
ATOM   2004 O O   . ASP A 1 266 ? 50.318 92.623  34.331 1.00 99.98  ? 290 ASP A O   1 
ATOM   2005 C CB  . ASP A 1 266 ? 52.681 90.372  33.449 1.00 122.78 ? 290 ASP A CB  1 
ATOM   2006 C CG  . ASP A 1 266 ? 52.768 89.020  34.136 1.00 128.21 ? 290 ASP A CG  1 
ATOM   2007 O OD1 . ASP A 1 266 ? 53.709 88.813  34.939 1.00 131.59 ? 290 ASP A OD1 1 
ATOM   2008 O OD2 . ASP A 1 266 ? 51.898 88.161  33.864 1.00 131.02 ? 290 ASP A OD2 1 
ATOM   2009 N N   . LYS A 1 267 ? 50.455 90.738  35.575 1.00 90.80  ? 291 LYS A N   1 
ATOM   2010 C CA  . LYS A 1 267 ? 49.041 90.726  35.951 1.00 82.57  ? 291 LYS A CA  1 
ATOM   2011 C C   . LYS A 1 267 ? 48.646 91.743  37.020 1.00 78.78  ? 291 LYS A C   1 
ATOM   2012 O O   . LYS A 1 267 ? 47.460 92.038  37.189 1.00 79.21  ? 291 LYS A O   1 
ATOM   2013 C CB  . LYS A 1 267 ? 48.645 89.324  36.419 1.00 77.27  ? 291 LYS A CB  1 
ATOM   2014 C CG  . LYS A 1 267 ? 48.546 88.305  35.302 1.00 73.62  ? 291 LYS A CG  1 
ATOM   2015 C CD  . LYS A 1 267 ? 48.404 86.891  35.846 1.00 72.84  ? 291 LYS A CD  1 
ATOM   2016 C CE  . LYS A 1 267 ? 47.038 86.653  36.458 1.00 71.49  ? 291 LYS A CE  1 
ATOM   2017 N NZ  . LYS A 1 267 ? 46.853 85.216  36.801 1.00 72.36  ? 291 LYS A NZ  1 
ATOM   2018 N N   . ALA A 1 268 ? 49.636 92.286  37.722 1.00 70.06  ? 292 ALA A N   1 
ATOM   2019 C CA  . ALA A 1 268 ? 49.374 93.236  38.796 1.00 68.29  ? 292 ALA A CA  1 
ATOM   2020 C C   . ALA A 1 268 ? 49.517 94.690  38.389 1.00 67.90  ? 292 ALA A C   1 
ATOM   2021 O O   . ALA A 1 268 ? 50.389 95.043  37.602 1.00 66.36  ? 292 ALA A O   1 
ATOM   2022 C CB  . ALA A 1 268 ? 50.293 92.940  39.995 1.00 81.23  ? 292 ALA A CB  1 
ATOM   2023 N N   . LYS A 1 269 ? 48.638 95.528  38.928 1.00 70.91  ? 293 LYS A N   1 
ATOM   2024 C CA  . LYS A 1 269 ? 48.678 96.951  38.669 1.00 73.42  ? 293 LYS A CA  1 
ATOM   2025 C C   . LYS A 1 269 ? 48.315 97.725  39.921 1.00 68.65  ? 293 LYS A C   1 
ATOM   2026 O O   . LYS A 1 269 ? 47.281 97.471  40.537 1.00 62.35  ? 293 LYS A O   1 
ATOM   2027 C CB  . LYS A 1 269 ? 47.706 97.333  37.542 1.00 102.58 ? 293 LYS A CB  1 
ATOM   2028 C CG  . LYS A 1 269 ? 48.217 97.047  36.132 1.00 120.49 ? 293 LYS A CG  1 
ATOM   2029 C CD  . LYS A 1 269 ? 47.125 97.273  35.085 1.00 129.22 ? 293 LYS A CD  1 
ATOM   2030 C CE  . LYS A 1 269 ? 47.706 97.492  33.690 1.00 131.42 ? 293 LYS A CE  1 
ATOM   2031 N NZ  . LYS A 1 269 ? 48.477 96.315  33.181 1.00 131.90 ? 293 LYS A NZ  1 
ATOM   2032 N N   . PHE A 1 270 ? 49.191 98.645  40.313 1.00 72.36  ? 294 PHE A N   1 
ATOM   2033 C CA  . PHE A 1 270 ? 48.928 99.528  41.438 1.00 75.77  ? 294 PHE A CA  1 
ATOM   2034 C C   . PHE A 1 270 ? 47.936 100.590 40.933 1.00 73.48  ? 294 PHE A C   1 
ATOM   2035 O O   . PHE A 1 270 ? 48.171 101.249 39.919 1.00 73.20  ? 294 PHE A O   1 
ATOM   2036 C CB  . PHE A 1 270 ? 50.230 100.188 41.913 1.00 85.52  ? 294 PHE A CB  1 
ATOM   2037 C CG  . PHE A 1 270 ? 51.261 99.198  42.383 1.00 94.39  ? 294 PHE A CG  1 
ATOM   2038 C CD1 . PHE A 1 270 ? 52.144 98.601  41.479 1.00 98.35  ? 294 PHE A CD1 1 
ATOM   2039 C CD2 . PHE A 1 270 ? 51.353 98.856  43.730 1.00 97.81  ? 294 PHE A CD2 1 
ATOM   2040 C CE1 . PHE A 1 270 ? 53.109 97.676  41.912 1.00 99.19  ? 294 PHE A CE1 1 
ATOM   2041 C CE2 . PHE A 1 270 ? 52.309 97.936  44.177 1.00 98.93  ? 294 PHE A CE2 1 
ATOM   2042 C CZ  . PHE A 1 270 ? 53.191 97.346  43.263 1.00 99.60  ? 294 PHE A CZ  1 
ATOM   2043 N N   . GLU A 1 271 ? 46.846 100.754 41.672 1.00 72.36  ? 295 GLU A N   1 
ATOM   2044 C CA  . GLU A 1 271 ? 45.834 101.751 41.377 1.00 71.23  ? 295 GLU A CA  1 
ATOM   2045 C C   . GLU A 1 271 ? 45.656 102.620 42.590 1.00 70.37  ? 295 GLU A C   1 
ATOM   2046 O O   . GLU A 1 271 ? 46.333 102.456 43.564 1.00 74.02  ? 295 GLU A O   1 
ATOM   2047 C CB  . GLU A 1 271 ? 44.500 101.098 41.088 1.00 68.77  ? 295 GLU A CB  1 
ATOM   2048 C CG  . GLU A 1 271 ? 44.446 100.345 39.798 1.00 64.13  ? 295 GLU A CG  1 
ATOM   2049 C CD  . GLU A 1 271 ? 43.095 99.798  39.540 1.00 61.72  ? 295 GLU A CD  1 
ATOM   2050 O OE1 . GLU A 1 271 ? 42.139 100.231 40.194 1.00 60.45  ? 295 GLU A OE1 1 
ATOM   2051 O OE2 . GLU A 1 271 ? 42.982 98.928  38.677 1.00 61.83  ? 295 GLU A OE2 1 
ATOM   2052 N N   . ASN A 1 272 ? 44.730 103.551 42.508 1.00 66.14  ? 296 ASN A N   1 
ATOM   2053 C CA  . ASN A 1 272 ? 44.381 104.435 43.599 1.00 64.99  ? 296 ASN A CA  1 
ATOM   2054 C C   . ASN A 1 272 ? 45.429 105.084 44.466 1.00 64.73  ? 296 ASN A C   1 
ATOM   2055 O O   . ASN A 1 272 ? 45.272 105.154 45.672 1.00 62.23  ? 296 ASN A O   1 
ATOM   2056 C CB  . ASN A 1 272 ? 43.369 103.741 44.502 1.00 68.51  ? 296 ASN A CB  1 
ATOM   2057 C CG  . ASN A 1 272 ? 42.565 104.711 45.309 1.00 70.35  ? 296 ASN A CG  1 
ATOM   2058 O OD1 . ASN A 1 272 ? 42.660 105.908 45.132 1.00 72.20  ? 296 ASN A OD1 1 
ATOM   2059 N ND2 . ASN A 1 272 ? 41.759 104.196 46.201 1.00 70.66  ? 296 ASN A ND2 1 
ATOM   2060 N N   . PHE A 1 273 ? 46.481 105.607 43.869 1.00 73.48  ? 297 PHE A N   1 
ATOM   2061 C CA  . PHE A 1 273 ? 47.477 106.315 44.655 1.00 76.93  ? 297 PHE A CA  1 
ATOM   2062 C C   . PHE A 1 273 ? 48.095 105.308 45.571 1.00 76.52  ? 297 PHE A C   1 
ATOM   2063 O O   . PHE A 1 273 ? 48.336 105.529 46.737 1.00 75.90  ? 297 PHE A O   1 
ATOM   2064 C CB  . PHE A 1 273 ? 46.893 107.463 45.467 1.00 79.94  ? 297 PHE A CB  1 
ATOM   2065 C CG  . PHE A 1 273 ? 46.487 108.612 44.644 1.00 84.59  ? 297 PHE A CG  1 
ATOM   2066 C CD1 . PHE A 1 273 ? 45.233 108.667 44.096 1.00 86.79  ? 297 PHE A CD1 1 
ATOM   2067 C CD2 . PHE A 1 273 ? 47.355 109.637 44.407 1.00 86.49  ? 297 PHE A CD2 1 
ATOM   2068 C CE1 . PHE A 1 273 ? 44.862 109.723 43.339 1.00 87.36  ? 297 PHE A CE1 1 
ATOM   2069 C CE2 . PHE A 1 273 ? 46.980 110.689 43.648 1.00 87.51  ? 297 PHE A CE2 1 
ATOM   2070 C CZ  . PHE A 1 273 ? 45.733 110.733 43.114 1.00 87.66  ? 297 PHE A CZ  1 
ATOM   2071 N N   . ASN A 1 274 ? 48.343 104.171 44.952 1.00 80.71  ? 298 ASN A N   1 
ATOM   2072 C CA  . ASN A 1 274 ? 48.996 102.989 45.491 1.00 81.60  ? 298 ASN A CA  1 
ATOM   2073 C C   . ASN A 1 274 ? 48.111 102.267 46.513 1.00 81.77  ? 298 ASN A C   1 
ATOM   2074 O O   . ASN A 1 274 ? 48.416 101.144 46.932 1.00 82.86  ? 298 ASN A O   1 
ATOM   2075 C CB  . ASN A 1 274 ? 50.378 103.312 46.100 1.00 79.33  ? 298 ASN A CB  1 
ATOM   2076 C CG  . ASN A 1 274 ? 51.440 102.314 45.658 1.00 81.43  ? 298 ASN A CG  1 
ATOM   2077 O OD1 . ASN A 1 274 ? 51.951 101.524 46.463 1.00 82.83  ? 298 ASN A OD1 1 
ATOM   2078 N ND2 . ASN A 1 274 ? 51.764 102.332 44.365 1.00 80.99  ? 298 ASN A ND2 1 
ATOM   2079 N N   . LYS A 1 275 ? 46.980 102.888 46.865 1.00 74.04  ? 299 LYS A N   1 
ATOM   2080 C CA  . LYS A 1 275 ? 46.061 102.357 47.875 1.00 70.14  ? 299 LYS A CA  1 
ATOM   2081 C C   . LYS A 1 275 ? 45.365 101.054 47.519 1.00 67.97  ? 299 LYS A C   1 
ATOM   2082 O O   . LYS A 1 275 ? 44.724 100.444 48.368 1.00 69.74  ? 299 LYS A O   1 
ATOM   2083 C CB  . LYS A 1 275 ? 45.008 103.415 48.243 1.00 67.21  ? 299 LYS A CB  1 
ATOM   2084 C CG  . LYS A 1 275 ? 45.573 104.635 48.965 1.00 65.57  ? 299 LYS A CG  1 
ATOM   2085 C CD  . LYS A 1 275 ? 44.493 105.653 49.279 1.00 63.94  ? 299 LYS A CD  1 
ATOM   2086 C CE  . LYS A 1 275 ? 45.092 107.035 49.388 1.00 63.87  ? 299 LYS A CE  1 
ATOM   2087 N NZ  . LYS A 1 275 ? 44.098 108.053 49.824 1.00 64.55  ? 299 LYS A NZ  1 
ATOM   2088 N N   . ALA A 1 276 ? 45.505 100.620 46.271 1.00 57.21  ? 300 ALA A N   1 
ATOM   2089 C CA  . ALA A 1 276 ? 44.869 99.385  45.828 1.00 51.28  ? 300 ALA A CA  1 
ATOM   2090 C C   . ALA A 1 276 ? 45.734 98.595  44.841 1.00 50.13  ? 300 ALA A C   1 
ATOM   2091 O O   . ALA A 1 276 ? 46.603 99.153  44.169 1.00 46.47  ? 300 ALA A O   1 
ATOM   2092 C CB  . ALA A 1 276 ? 43.497 99.695  45.214 1.00 41.71  ? 300 ALA A CB  1 
ATOM   2093 N N   . LEU A 1 277 ? 45.475 97.293  44.756 1.00 51.44  ? 301 LEU A N   1 
ATOM   2094 C CA  . LEU A 1 277 ? 46.237 96.411  43.891 1.00 54.90  ? 301 LEU A CA  1 
ATOM   2095 C C   . LEU A 1 277 ? 45.327 95.448  43.141 1.00 54.06  ? 301 LEU A C   1 
ATOM   2096 O O   . LEU A 1 277 ? 44.632 94.628  43.741 1.00 52.03  ? 301 LEU A O   1 
ATOM   2097 C CB  . LEU A 1 277 ? 47.234 95.616  44.741 1.00 63.12  ? 301 LEU A CB  1 
ATOM   2098 C CG  . LEU A 1 277 ? 48.376 94.819  44.100 1.00 71.40  ? 301 LEU A CG  1 
ATOM   2099 C CD1 . LEU A 1 277 ? 49.220 94.231  45.211 1.00 76.20  ? 301 LEU A CD1 1 
ATOM   2100 C CD2 . LEU A 1 277 ? 47.877 93.702  43.197 1.00 76.64  ? 301 LEU A CD2 1 
ATOM   2101 N N   . ARG A 1 278 ? 45.334 95.542  41.820 1.00 54.63  ? 302 ARG A N   1 
ATOM   2102 C CA  . ARG A 1 278 ? 44.511 94.659  41.011 1.00 55.57  ? 302 ARG A CA  1 
ATOM   2103 C C   . ARG A 1 278 ? 45.364 93.589  40.366 1.00 54.87  ? 302 ARG A C   1 
ATOM   2104 O O   . ARG A 1 278 ? 46.472 93.860  39.924 1.00 54.87  ? 302 ARG A O   1 
ATOM   2105 C CB  . ARG A 1 278 ? 43.785 95.452  39.903 1.00 55.64  ? 302 ARG A CB  1 
ATOM   2106 C CG  . ARG A 1 278 ? 42.861 94.614  39.012 1.00 54.14  ? 302 ARG A CG  1 
ATOM   2107 C CD  . ARG A 1 278 ? 42.164 95.470  37.938 1.00 54.34  ? 302 ARG A CD  1 
ATOM   2108 N NE  . ARG A 1 278 ? 41.556 96.666  38.524 1.00 52.43  ? 302 ARG A NE  1 
ATOM   2109 C CZ  . ARG A 1 278 ? 40.261 96.820  38.762 1.00 51.16  ? 302 ARG A CZ  1 
ATOM   2110 N NH1 . ARG A 1 278 ? 39.396 95.853  38.451 1.00 49.76  ? 302 ARG A NH1 1 
ATOM   2111 N NH2 . ARG A 1 278 ? 39.844 97.946  39.339 1.00 48.75  ? 302 ARG A NH2 1 
ATOM   2112 N N   . ILE A 1 279 ? 44.841 92.368  40.359 1.00 55.86  ? 303 ILE A N   1 
ATOM   2113 C CA  . ILE A 1 279 ? 45.467 91.229  39.673 1.00 57.24  ? 303 ILE A CA  1 
ATOM   2114 C C   . ILE A 1 279 ? 44.369 90.776  38.697 1.00 61.76  ? 303 ILE A C   1 
ATOM   2115 O O   . ILE A 1 279 ? 43.253 90.446  39.111 1.00 61.73  ? 303 ILE A O   1 
ATOM   2116 C CB  . ILE A 1 279 ? 45.908 90.137  40.660 1.00 54.65  ? 303 ILE A CB  1 
ATOM   2117 C CG1 . ILE A 1 279 ? 47.162 90.620  41.401 1.00 54.39  ? 303 ILE A CG1 1 
ATOM   2118 C CG2 . ILE A 1 279 ? 46.215 88.843  39.920 1.00 48.37  ? 303 ILE A CG2 1 
ATOM   2119 C CD1 . ILE A 1 279 ? 47.512 89.823  42.655 1.00 65.52  ? 303 ILE A CD1 1 
ATOM   2120 N N   . THR A 1 280 ? 44.713 90.738  37.411 1.00 76.50  ? 304 THR A N   1 
ATOM   2121 C CA  . THR A 1 280 ? 43.706 90.572  36.377 1.00 82.36  ? 304 THR A CA  1 
ATOM   2122 C C   . THR A 1 280 ? 43.023 89.236  36.181 1.00 80.19  ? 304 THR A C   1 
ATOM   2123 O O   . THR A 1 280 ? 41.940 89.013  36.706 1.00 85.59  ? 304 THR A O   1 
ATOM   2124 C CB  . THR A 1 280 ? 44.237 91.097  34.992 1.00 86.25  ? 304 THR A CB  1 
ATOM   2125 O OG1 . THR A 1 280 ? 45.229 92.118  35.192 1.00 90.07  ? 304 THR A OG1 1 
ATOM   2126 C CG2 . THR A 1 280 ? 43.087 91.684  34.167 1.00 90.08  ? 304 THR A CG2 1 
ATOM   2127 N N   . ASN A 1 281 ? 43.637 88.335  35.440 1.00 69.85  ? 305 ASN A N   1 
ATOM   2128 C CA  . ASN A 1 281 ? 42.990 87.058  35.139 1.00 66.13  ? 305 ASN A CA  1 
ATOM   2129 C C   . ASN A 1 281 ? 43.428 86.025  36.166 1.00 62.25  ? 305 ASN A C   1 
ATOM   2130 O O   . ASN A 1 281 ? 44.194 85.108  35.858 1.00 60.09  ? 305 ASN A O   1 
ATOM   2131 C CB  . ASN A 1 281 ? 43.367 86.635  33.704 1.00 70.02  ? 305 ASN A CB  1 
ATOM   2132 C CG  . ASN A 1 281 ? 42.833 85.255  33.325 1.00 72.00  ? 305 ASN A CG  1 
ATOM   2133 O OD1 . ASN A 1 281 ? 43.493 84.504  32.599 1.00 73.53  ? 305 ASN A OD1 1 
ATOM   2134 N ND2 . ASN A 1 281 ? 41.637 84.918  33.804 1.00 73.50  ? 305 ASN A ND2 1 
ATOM   2135 N N   . VAL A 1 282 ? 42.904 86.166  37.385 1.00 57.94  ? 306 VAL A N   1 
ATOM   2136 C CA  . VAL A 1 282 ? 43.326 85.308  38.488 1.00 55.85  ? 306 VAL A CA  1 
ATOM   2137 C C   . VAL A 1 282 ? 43.081 83.836  38.279 1.00 55.27  ? 306 VAL A C   1 
ATOM   2138 O O   . VAL A 1 282 ? 42.089 83.447  37.669 1.00 54.79  ? 306 VAL A O   1 
ATOM   2139 C CB  . VAL A 1 282 ? 42.654 85.698  39.844 1.00 46.68  ? 306 VAL A CB  1 
ATOM   2140 C CG1 . VAL A 1 282 ? 42.850 87.173  40.136 1.00 42.53  ? 306 VAL A CG1 1 
ATOM   2141 C CG2 . VAL A 1 282 ? 41.194 85.324  39.833 1.00 41.96  ? 306 VAL A CG2 1 
ATOM   2142 N N   . SER A 1 283 ? 44.032 83.032  38.753 1.00 55.59  ? 307 SER A N   1 
ATOM   2143 C CA  . SER A 1 283 ? 43.896 81.580  38.747 1.00 56.24  ? 307 SER A CA  1 
ATOM   2144 C C   . SER A 1 283 ? 44.333 81.065  40.132 1.00 53.95  ? 307 SER A C   1 
ATOM   2145 O O   . SER A 1 283 ? 44.734 81.846  40.997 1.00 50.34  ? 307 SER A O   1 
ATOM   2146 C CB  . SER A 1 283 ? 44.754 80.938  37.666 1.00 65.12  ? 307 SER A CB  1 
ATOM   2147 O OG  . SER A 1 283 ? 46.122 80.983  38.018 1.00 70.06  ? 307 SER A OG  1 
ATOM   2148 N N   . GLU A 1 284 ? 44.246 79.750  40.315 1.00 55.98  ? 308 GLU A N   1 
ATOM   2149 C CA  . GLU A 1 284 ? 44.633 79.060  41.551 1.00 61.23  ? 308 GLU A CA  1 
ATOM   2150 C C   . GLU A 1 284 ? 45.966 79.569  42.120 1.00 63.37  ? 308 GLU A C   1 
ATOM   2151 O O   . GLU A 1 284 ? 46.078 79.818  43.314 1.00 61.63  ? 308 GLU A O   1 
ATOM   2152 C CB  . GLU A 1 284 ? 44.723 77.544  41.302 1.00 67.35  ? 308 GLU A CB  1 
ATOM   2153 C CG  . GLU A 1 284 ? 43.520 76.916  40.557 1.00 73.90  ? 308 GLU A CG  1 
ATOM   2154 C CD  . GLU A 1 284 ? 43.608 77.012  39.014 1.00 77.04  ? 308 GLU A CD  1 
ATOM   2155 O OE1 . GLU A 1 284 ? 43.314 78.098  38.456 1.00 76.54  ? 308 GLU A OE1 1 
ATOM   2156 O OE2 . GLU A 1 284 ? 43.970 75.999  38.363 1.00 76.71  ? 308 GLU A OE2 1 
ATOM   2157 N N   . GLU A 1 285 ? 46.960 79.743  41.253 1.00 69.26  ? 309 GLU A N   1 
ATOM   2158 C CA  . GLU A 1 285 ? 48.291 80.227  41.637 1.00 71.48  ? 309 GLU A CA  1 
ATOM   2159 C C   . GLU A 1 285 ? 48.272 81.559  42.373 1.00 68.72  ? 309 GLU A C   1 
ATOM   2160 O O   . GLU A 1 285 ? 49.196 81.874  43.127 1.00 67.63  ? 309 GLU A O   1 
ATOM   2161 C CB  . GLU A 1 285 ? 49.168 80.394  40.387 1.00 95.70  ? 309 GLU A CB  1 
ATOM   2162 C CG  . GLU A 1 285 ? 48.939 79.332  39.308 1.00 109.57 ? 309 GLU A CG  1 
ATOM   2163 C CD  . GLU A 1 285 ? 49.994 79.355  38.204 1.00 115.80 ? 309 GLU A CD  1 
ATOM   2164 O OE1 . GLU A 1 285 ? 50.358 80.462  37.732 1.00 117.93 ? 309 GLU A OE1 1 
ATOM   2165 O OE2 . GLU A 1 285 ? 50.446 78.256  37.804 1.00 117.12 ? 309 GLU A OE2 1 
ATOM   2166 N N   . ASP A 1 286 ? 47.215 82.337  42.159 1.00 59.67  ? 310 ASP A N   1 
ATOM   2167 C CA  . ASP A 1 286 ? 47.115 83.676  42.729 1.00 53.47  ? 310 ASP A CA  1 
ATOM   2168 C C   . ASP A 1 286 ? 46.543 83.725  44.130 1.00 48.13  ? 310 ASP A C   1 
ATOM   2169 O O   . ASP A 1 286 ? 46.490 84.787  44.746 1.00 43.33  ? 310 ASP A O   1 
ATOM   2170 C CB  . ASP A 1 286 ? 46.331 84.591  41.780 1.00 66.74  ? 310 ASP A CB  1 
ATOM   2171 C CG  . ASP A 1 286 ? 47.103 84.918  40.510 1.00 72.17  ? 310 ASP A CG  1 
ATOM   2172 O OD1 . ASP A 1 286 ? 48.227 85.458  40.624 1.00 76.48  ? 310 ASP A OD1 1 
ATOM   2173 O OD2 . ASP A 1 286 ? 46.580 84.636  39.405 1.00 74.22  ? 310 ASP A OD2 1 
ATOM   2174 N N   . SER A 1 287 ? 46.119 82.567  44.632 1.00 44.70  ? 311 SER A N   1 
ATOM   2175 C CA  . SER A 1 287 ? 45.628 82.471  46.007 1.00 46.90  ? 311 SER A CA  1 
ATOM   2176 C C   . SER A 1 287 ? 46.793 82.529  47.013 1.00 47.15  ? 311 SER A C   1 
ATOM   2177 O O   . SER A 1 287 ? 47.973 82.392  46.641 1.00 44.22  ? 311 SER A O   1 
ATOM   2178 C CB  . SER A 1 287 ? 44.814 81.188  46.216 1.00 57.84  ? 311 SER A CB  1 
ATOM   2179 O OG  . SER A 1 287 ? 45.563 80.034  45.912 1.00 65.26  ? 311 SER A OG  1 
ATOM   2180 N N   . GLY A 1 288 ? 46.451 82.748  48.284 1.00 53.69  ? 312 GLY A N   1 
ATOM   2181 C CA  . GLY A 1 288 ? 47.458 82.855  49.325 1.00 59.93  ? 312 GLY A CA  1 
ATOM   2182 C C   . GLY A 1 288 ? 47.377 84.170  50.068 1.00 62.61  ? 312 GLY A C   1 
ATOM   2183 O O   . GLY A 1 288 ? 46.456 84.952  49.852 1.00 65.19  ? 312 GLY A O   1 
ATOM   2184 N N   . GLU A 1 289 ? 48.369 84.433  50.908 1.00 60.09  ? 313 GLU A N   1 
ATOM   2185 C CA  . GLU A 1 289 ? 48.352 85.609  51.764 1.00 58.72  ? 313 GLU A CA  1 
ATOM   2186 C C   . GLU A 1 289 ? 49.059 86.815  51.181 1.00 58.27  ? 313 GLU A C   1 
ATOM   2187 O O   . GLU A 1 289 ? 50.222 86.739  50.787 1.00 58.79  ? 313 GLU A O   1 
ATOM   2188 C CB  . GLU A 1 289 ? 48.970 85.272  53.148 1.00 58.63  ? 313 GLU A CB  1 
ATOM   2189 C CG  . GLU A 1 289 ? 48.595 83.897  53.714 1.00 62.46  ? 313 GLU A CG  1 
ATOM   2190 C CD  . GLU A 1 289 ? 47.090 83.693  53.911 1.00 63.71  ? 313 GLU A CD  1 
ATOM   2191 O OE1 . GLU A 1 289 ? 46.491 84.421  54.746 1.00 63.80  ? 313 GLU A OE1 1 
ATOM   2192 O OE2 . GLU A 1 289 ? 46.512 82.798  53.238 1.00 62.52  ? 313 GLU A OE2 1 
ATOM   2193 N N   . TYR A 1 290 ? 48.329 87.922  51.098 1.00 59.86  ? 314 TYR A N   1 
ATOM   2194 C CA  . TYR A 1 290 ? 48.900 89.180  50.655 1.00 56.79  ? 314 TYR A CA  1 
ATOM   2195 C C   . TYR A 1 290 ? 48.875 90.106  51.863 1.00 56.30  ? 314 TYR A C   1 
ATOM   2196 O O   . TYR A 1 290 ? 48.034 89.939  52.755 1.00 56.90  ? 314 TYR A O   1 
ATOM   2197 C CB  . TYR A 1 290 ? 48.058 89.820  49.545 1.00 48.31  ? 314 TYR A CB  1 
ATOM   2198 C CG  . TYR A 1 290 ? 48.001 88.997  48.289 1.00 46.72  ? 314 TYR A CG  1 
ATOM   2199 C CD1 . TYR A 1 290 ? 47.161 87.891  48.197 1.00 44.02  ? 314 TYR A CD1 1 
ATOM   2200 C CD2 . TYR A 1 290 ? 48.797 89.324  47.180 1.00 45.31  ? 314 TYR A CD2 1 
ATOM   2201 C CE1 . TYR A 1 290 ? 47.109 87.129  47.035 1.00 45.53  ? 314 TYR A CE1 1 
ATOM   2202 C CE2 . TYR A 1 290 ? 48.751 88.567  46.019 1.00 42.28  ? 314 TYR A CE2 1 
ATOM   2203 C CZ  . TYR A 1 290 ? 47.906 87.473  45.956 1.00 44.12  ? 314 TYR A CZ  1 
ATOM   2204 O OH  . TYR A 1 290 ? 47.859 86.701  44.826 1.00 45.93  ? 314 TYR A OH  1 
ATOM   2205 N N   . PHE A 1 291 ? 49.808 91.054  51.912 1.00 48.12  ? 315 PHE A N   1 
ATOM   2206 C CA  . PHE A 1 291 ? 49.796 92.038  52.983 1.00 45.82  ? 315 PHE A CA  1 
ATOM   2207 C C   . PHE A 1 291 ? 50.285 93.399  52.531 1.00 47.95  ? 315 PHE A C   1 
ATOM   2208 O O   . PHE A 1 291 ? 51.011 93.504  51.537 1.00 45.75  ? 315 PHE A O   1 
ATOM   2209 C CB  . PHE A 1 291 ? 50.560 91.549  54.228 1.00 55.28  ? 315 PHE A CB  1 
ATOM   2210 C CG  . PHE A 1 291 ? 52.051 91.414  54.050 1.00 57.85  ? 315 PHE A CG  1 
ATOM   2211 C CD1 . PHE A 1 291 ? 52.901 92.467  54.373 1.00 58.65  ? 315 PHE A CD1 1 
ATOM   2212 C CD2 . PHE A 1 291 ? 52.602 90.218  53.604 1.00 59.23  ? 315 PHE A CD2 1 
ATOM   2213 C CE1 . PHE A 1 291 ? 54.280 92.341  54.240 1.00 59.57  ? 315 PHE A CE1 1 
ATOM   2214 C CE2 . PHE A 1 291 ? 53.981 90.075  53.464 1.00 61.18  ? 315 PHE A CE2 1 
ATOM   2215 C CZ  . PHE A 1 291 ? 54.825 91.137  53.789 1.00 61.21  ? 315 PHE A CZ  1 
ATOM   2216 N N   . CYS A 1 292 ? 49.861 94.431  53.254 1.00 51.53  ? 316 CYS A N   1 
ATOM   2217 C CA  . CYS A 1 292 ? 50.223 95.797  52.933 1.00 58.35  ? 316 CYS A CA  1 
ATOM   2218 C C   . CYS A 1 292 ? 50.770 96.539  54.151 1.00 61.28  ? 316 CYS A C   1 
ATOM   2219 O O   . CYS A 1 292 ? 50.456 96.197  55.298 1.00 62.97  ? 316 CYS A O   1 
ATOM   2220 C CB  . CYS A 1 292 ? 49.002 96.561  52.389 1.00 67.06  ? 316 CYS A CB  1 
ATOM   2221 S SG  . CYS A 1 292 ? 47.814 97.052  53.683 1.00 73.71  ? 316 CYS A SG  1 
ATOM   2222 N N   . LEU A 1 293 ? 51.587 97.558  53.893 1.00 65.84  ? 317 LEU A N   1 
ATOM   2223 C CA  . LEU A 1 293 ? 52.153 98.361  54.953 1.00 67.44  ? 317 LEU A CA  1 
ATOM   2224 C C   . LEU A 1 293 ? 51.824 99.839  54.837 1.00 67.45  ? 317 LEU A C   1 
ATOM   2225 O O   . LEU A 1 293 ? 52.081 100.469 53.808 1.00 66.72  ? 317 LEU A O   1 
ATOM   2226 C CB  . LEU A 1 293 ? 53.681 98.206  55.001 1.00 80.29  ? 317 LEU A CB  1 
ATOM   2227 C CG  . LEU A 1 293 ? 54.257 97.178  55.984 1.00 84.56  ? 317 LEU A CG  1 
ATOM   2228 C CD1 . LEU A 1 293 ? 54.197 95.766  55.411 1.00 85.90  ? 317 LEU A CD1 1 
ATOM   2229 C CD2 . LEU A 1 293 ? 55.690 97.572  56.303 1.00 86.74  ? 317 LEU A CD2 1 
ATOM   2230 N N   . ALA A 1 294 ? 51.232 100.373 55.904 1.00 68.96  ? 318 ALA A N   1 
ATOM   2231 C CA  . ALA A 1 294 ? 50.956 101.802 56.003 1.00 70.77  ? 318 ALA A CA  1 
ATOM   2232 C C   . ALA A 1 294 ? 52.200 102.442 56.637 1.00 74.36  ? 318 ALA A C   1 
ATOM   2233 O O   . ALA A 1 294 ? 52.241 102.711 57.841 1.00 72.30  ? 318 ALA A O   1 
ATOM   2234 C CB  . ALA A 1 294 ? 49.741 102.052 56.860 1.00 72.60  ? 318 ALA A CB  1 
ATOM   2235 N N   . SER A 1 295 ? 53.203 102.694 55.796 1.00 88.40  ? 319 SER A N   1 
ATOM   2236 C CA  . SER A 1 295 ? 54.468 103.244 56.243 1.00 96.99  ? 319 SER A CA  1 
ATOM   2237 C C   . SER A 1 295 ? 54.479 104.746 56.511 1.00 99.63  ? 319 SER A C   1 
ATOM   2238 O O   . SER A 1 295 ? 54.785 105.556 55.632 1.00 98.55  ? 319 SER A O   1 
ATOM   2239 C CB  . SER A 1 295 ? 55.594 102.856 55.256 1.00 108.53 ? 319 SER A CB  1 
ATOM   2240 O OG  . SER A 1 295 ? 55.267 103.201 53.921 1.00 118.03 ? 319 SER A OG  1 
ATOM   2241 N N   . ASN A 1 296 ? 54.126 105.098 57.745 1.00 97.50  ? 320 ASN A N   1 
ATOM   2242 C CA  . ASN A 1 296 ? 54.153 106.484 58.226 1.00 101.41 ? 320 ASN A CA  1 
ATOM   2243 C C   . ASN A 1 296 ? 55.605 106.893 58.582 1.00 104.60 ? 320 ASN A C   1 
ATOM   2244 O O   . ASN A 1 296 ? 56.577 106.339 58.053 1.00 107.55 ? 320 ASN A O   1 
ATOM   2245 C CB  . ASN A 1 296 ? 53.285 106.596 59.489 1.00 110.56 ? 320 ASN A CB  1 
ATOM   2246 C CG  . ASN A 1 296 ? 52.813 108.017 59.760 1.00 107.20 ? 320 ASN A CG  1 
ATOM   2247 O OD1 . ASN A 1 296 ? 53.257 108.970 59.121 1.00 105.31 ? 320 ASN A OD1 1 
ATOM   2248 N ND2 . ASN A 1 296 ? 51.902 108.160 60.715 1.00 105.10 ? 320 ASN A ND2 1 
ATOM   2249 N N   . LYS A 1 297 ? 55.726 107.882 59.469 1.00 109.38 ? 321 LYS A N   1 
ATOM   2250 C CA  . LYS A 1 297 ? 57.015 108.358 59.971 1.00 106.99 ? 321 LYS A CA  1 
ATOM   2251 C C   . LYS A 1 297 ? 57.156 107.864 61.418 1.00 107.14 ? 321 LYS A C   1 
ATOM   2252 O O   . LYS A 1 297 ? 58.213 107.379 61.812 1.00 110.33 ? 321 LYS A O   1 
ATOM   2253 C CB  . LYS A 1 297 ? 57.078 109.883 59.918 1.00 103.23 ? 321 LYS A CB  1 
ATOM   2254 C CG  . LYS A 1 297 ? 58.484 110.466 59.984 1.00 99.00  ? 321 LYS A CG  1 
ATOM   2255 C CD  . LYS A 1 297 ? 58.480 111.975 59.667 1.00 97.78  ? 321 LYS A CD  1 
ATOM   2256 C CE  . LYS A 1 297 ? 57.948 112.817 60.839 1.00 98.27  ? 321 LYS A CE  1 
ATOM   2257 N NZ  . LYS A 1 297 ? 57.894 114.282 60.537 1.00 98.28  ? 321 LYS A NZ  1 
ATOM   2258 N N   . MET A 1 298 ? 56.076 107.984 62.188 1.00 100.32 ? 322 MET A N   1 
ATOM   2259 C CA  . MET A 1 298 ? 56.024 107.528 63.581 1.00 99.67  ? 322 MET A CA  1 
ATOM   2260 C C   . MET A 1 298 ? 55.818 106.013 63.719 1.00 96.04  ? 322 MET A C   1 
ATOM   2261 O O   . MET A 1 298 ? 55.885 105.477 64.829 1.00 92.16  ? 322 MET A O   1 
ATOM   2262 C CB  . MET A 1 298 ? 54.888 108.243 64.333 1.00 126.79 ? 322 MET A CB  1 
ATOM   2263 C CG  . MET A 1 298 ? 55.329 109.388 65.249 1.00 139.21 ? 322 MET A CG  1 
ATOM   2264 S SD  . MET A 1 298 ? 56.370 110.640 64.453 1.00 145.69 ? 322 MET A SD  1 
ATOM   2265 C CE  . MET A 1 298 ? 55.330 111.167 63.095 1.00 147.84 ? 322 MET A CE  1 
ATOM   2266 N N   . GLY A 1 299 ? 55.567 105.333 62.600 1.00 99.08  ? 323 GLY A N   1 
ATOM   2267 C CA  . GLY A 1 299 ? 55.326 103.898 62.637 1.00 96.58  ? 323 GLY A CA  1 
ATOM   2268 C C   . GLY A 1 299 ? 55.044 103.263 61.284 1.00 93.69  ? 323 GLY A C   1 
ATOM   2269 O O   . GLY A 1 299 ? 55.132 103.920 60.244 1.00 94.83  ? 323 GLY A O   1 
ATOM   2270 N N   . SER A 1 300 ? 54.689 101.980 61.314 1.00 95.03  ? 324 SER A N   1 
ATOM   2271 C CA  . SER A 1 300 ? 54.434 101.198 60.111 1.00 90.20  ? 324 SER A CA  1 
ATOM   2272 C C   . SER A 1 300 ? 53.689 99.909  60.477 1.00 90.63  ? 324 SER A C   1 
ATOM   2273 O O   . SER A 1 300 ? 54.294 98.942  60.959 1.00 91.74  ? 324 SER A O   1 
ATOM   2274 C CB  . SER A 1 300 ? 55.774 100.873 59.427 1.00 79.82  ? 324 SER A CB  1 
ATOM   2275 O OG  . SER A 1 300 ? 55.644 99.833  58.471 1.00 76.63  ? 324 SER A OG  1 
ATOM   2276 N N   . ILE A 1 301 ? 52.370 99.905  60.258 1.00 84.06  ? 325 ILE A N   1 
ATOM   2277 C CA  . ILE A 1 301 ? 51.542 98.739  60.579 1.00 78.65  ? 325 ILE A CA  1 
ATOM   2278 C C   . ILE A 1 301 ? 51.255 97.881  59.357 1.00 78.67  ? 325 ILE A C   1 
ATOM   2279 O O   . ILE A 1 301 ? 51.604 98.255  58.231 1.00 79.69  ? 325 ILE A O   1 
ATOM   2280 C CB  . ILE A 1 301 ? 50.217 99.133  61.286 1.00 78.93  ? 325 ILE A CB  1 
ATOM   2281 C CG1 . ILE A 1 301 ? 49.399 100.077 60.410 1.00 78.07  ? 325 ILE A CG1 1 
ATOM   2282 C CG2 . ILE A 1 301 ? 50.529 99.768  62.646 1.00 78.25  ? 325 ILE A CG2 1 
ATOM   2283 C CD1 . ILE A 1 301 ? 47.947 100.254 60.847 1.00 79.47  ? 325 ILE A CD1 1 
ATOM   2284 N N   . ARG A 1 302 ? 50.629 96.729  59.577 1.00 78.53  ? 326 ARG A N   1 
ATOM   2285 C CA  . ARG A 1 302 ? 50.386 95.801  58.484 1.00 73.11  ? 326 ARG A CA  1 
ATOM   2286 C C   . ARG A 1 302 ? 49.000 95.166  58.507 1.00 69.96  ? 326 ARG A C   1 
ATOM   2287 O O   . ARG A 1 302 ? 48.426 94.923  59.576 1.00 71.72  ? 326 ARG A O   1 
ATOM   2288 C CB  . ARG A 1 302 ? 51.493 94.708  58.492 1.00 63.13  ? 326 ARG A CB  1 
ATOM   2289 C CG  . ARG A 1 302 ? 51.074 93.322  58.952 1.00 62.82  ? 326 ARG A CG  1 
ATOM   2290 C CD  . ARG A 1 302 ? 51.220 92.319  57.820 1.00 61.65  ? 326 ARG A CD  1 
ATOM   2291 N NE  . ARG A 1 302 ? 52.358 91.407  57.977 1.00 61.33  ? 326 ARG A NE  1 
ATOM   2292 C CZ  . ARG A 1 302 ? 53.639 91.736  57.840 1.00 60.50  ? 326 ARG A CZ  1 
ATOM   2293 N NH1 . ARG A 1 302 ? 53.991 92.972  57.540 1.00 62.84  ? 326 ARG A NH1 1 
ATOM   2294 N NH2 . ARG A 1 302 ? 54.574 90.817  57.993 1.00 60.06  ? 326 ARG A NH2 1 
ATOM   2295 N N   . HIS A 1 303 ? 48.453 94.942  57.314 1.00 59.40  ? 327 HIS A N   1 
ATOM   2296 C CA  . HIS A 1 303 ? 47.164 94.278  57.186 1.00 55.56  ? 327 HIS A CA  1 
ATOM   2297 C C   . HIS A 1 303 ? 47.392 93.032  56.356 1.00 52.09  ? 327 HIS A C   1 
ATOM   2298 O O   . HIS A 1 303 ? 48.149 93.065  55.387 1.00 51.19  ? 327 HIS A O   1 
ATOM   2299 C CB  . HIS A 1 303 ? 46.148 95.172  56.501 1.00 54.82  ? 327 HIS A CB  1 
ATOM   2300 C CG  . HIS A 1 303 ? 44.734 94.711  56.671 1.00 56.26  ? 327 HIS A CG  1 
ATOM   2301 N ND1 . HIS A 1 303 ? 44.121 93.837  55.798 1.00 56.04  ? 327 HIS A ND1 1 
ATOM   2302 C CD2 . HIS A 1 303 ? 43.814 94.996  57.626 1.00 56.59  ? 327 HIS A CD2 1 
ATOM   2303 C CE1 . HIS A 1 303 ? 42.885 93.606  56.204 1.00 54.90  ? 327 HIS A CE1 1 
ATOM   2304 N NE2 . HIS A 1 303 ? 42.674 94.298  57.311 1.00 55.07  ? 327 HIS A NE2 1 
ATOM   2305 N N   . THR A 1 304 ? 46.758 91.931  56.740 1.00 52.96  ? 328 THR A N   1 
ATOM   2306 C CA  . THR A 1 304 ? 46.924 90.694  56.012 1.00 52.56  ? 328 THR A CA  1 
ATOM   2307 C C   . THR A 1 304 ? 45.608 90.259  55.391 1.00 52.67  ? 328 THR A C   1 
ATOM   2308 O O   . THR A 1 304 ? 44.578 90.188  56.067 1.00 54.81  ? 328 THR A O   1 
ATOM   2309 C CB  . THR A 1 304 ? 47.507 89.589  56.927 1.00 50.13  ? 328 THR A CB  1 
ATOM   2310 O OG1 . THR A 1 304 ? 48.755 90.055  57.458 1.00 52.01  ? 328 THR A OG1 1 
ATOM   2311 C CG2 . THR A 1 304 ? 47.764 88.298  56.143 1.00 46.36  ? 328 THR A CG2 1 
ATOM   2312 N N   . ILE A 1 305 ? 45.647 89.998  54.087 1.00 48.94  ? 329 ILE A N   1 
ATOM   2313 C CA  . ILE A 1 305 ? 44.471 89.584  53.357 1.00 50.73  ? 329 ILE A CA  1 
ATOM   2314 C C   . ILE A 1 305 ? 44.654 88.156  52.885 1.00 50.71  ? 329 ILE A C   1 
ATOM   2315 O O   . ILE A 1 305 ? 45.657 87.822  52.274 1.00 49.27  ? 329 ILE A O   1 
ATOM   2316 C CB  . ILE A 1 305 ? 44.220 90.516  52.132 1.00 58.24  ? 329 ILE A CB  1 
ATOM   2317 C CG1 . ILE A 1 305 ? 44.001 91.955  52.613 1.00 60.36  ? 329 ILE A CG1 1 
ATOM   2318 C CG2 . ILE A 1 305 ? 43.016 90.012  51.320 1.00 55.83  ? 329 ILE A CG2 1 
ATOM   2319 C CD1 . ILE A 1 305 ? 44.073 93.014  51.520 1.00 74.54  ? 329 ILE A CD1 1 
ATOM   2320 N N   . SER A 1 306 ? 43.680 87.313  53.189 1.00 52.43  ? 330 SER A N   1 
ATOM   2321 C CA  . SER A 1 306 ? 43.724 85.929  52.765 1.00 53.60  ? 330 SER A CA  1 
ATOM   2322 C C   . SER A 1 306 ? 42.858 85.785  51.522 1.00 52.19  ? 330 SER A C   1 
ATOM   2323 O O   . SER A 1 306 ? 41.672 86.132  51.523 1.00 54.06  ? 330 SER A O   1 
ATOM   2324 C CB  . SER A 1 306 ? 43.221 85.030  53.890 1.00 52.12  ? 330 SER A CB  1 
ATOM   2325 O OG  . SER A 1 306 ? 43.876 85.379  55.103 1.00 56.95  ? 330 SER A OG  1 
ATOM   2326 N N   . VAL A 1 307 ? 43.453 85.280  50.452 1.00 48.67  ? 331 VAL A N   1 
ATOM   2327 C CA  . VAL A 1 307 ? 42.720 85.141  49.218 1.00 44.26  ? 331 VAL A CA  1 
ATOM   2328 C C   . VAL A 1 307 ? 42.558 83.693  48.826 1.00 44.75  ? 331 VAL A C   1 
ATOM   2329 O O   . VAL A 1 307 ? 43.538 83.005  48.562 1.00 45.59  ? 331 VAL A O   1 
ATOM   2330 C CB  . VAL A 1 307 ? 43.434 85.913  48.049 1.00 40.16  ? 331 VAL A CB  1 
ATOM   2331 C CG1 . VAL A 1 307 ? 42.766 85.599  46.724 1.00 39.74  ? 331 VAL A CG1 1 
ATOM   2332 C CG2 . VAL A 1 307 ? 43.406 87.418  48.296 1.00 36.20  ? 331 VAL A CG2 1 
ATOM   2333 N N   . ARG A 1 308 ? 41.326 83.214  48.852 1.00 48.53  ? 332 ARG A N   1 
ATOM   2334 C CA  . ARG A 1 308 ? 41.074 81.874  48.360 1.00 51.61  ? 332 ARG A CA  1 
ATOM   2335 C C   . ARG A 1 308 ? 40.372 82.021  46.991 1.00 51.84  ? 332 ARG A C   1 
ATOM   2336 O O   . ARG A 1 308 ? 39.527 82.909  46.789 1.00 53.82  ? 332 ARG A O   1 
ATOM   2337 C CB  . ARG A 1 308 ? 40.249 81.013  49.342 1.00 49.86  ? 332 ARG A CB  1 
ATOM   2338 C CG  . ARG A 1 308 ? 39.162 81.760  50.096 1.00 54.18  ? 332 ARG A CG  1 
ATOM   2339 C CD  . ARG A 1 308 ? 38.147 80.803  50.773 1.00 55.95  ? 332 ARG A CD  1 
ATOM   2340 N NE  . ARG A 1 308 ? 36.878 81.468  51.094 1.00 56.25  ? 332 ARG A NE  1 
ATOM   2341 C CZ  . ARG A 1 308 ? 36.761 82.678  51.648 1.00 56.28  ? 332 ARG A CZ  1 
ATOM   2342 N NH1 . ARG A 1 308 ? 37.836 83.395  51.962 1.00 56.32  ? 332 ARG A NH1 1 
ATOM   2343 N NH2 . ARG A 1 308 ? 35.554 83.184  51.885 1.00 56.91  ? 332 ARG A NH2 1 
ATOM   2344 N N   . VAL A 1 309 ? 40.767 81.158  46.057 1.00 46.56  ? 333 VAL A N   1 
ATOM   2345 C CA  . VAL A 1 309 ? 40.257 81.181  44.703 1.00 42.29  ? 333 VAL A CA  1 
ATOM   2346 C C   . VAL A 1 309 ? 39.346 80.002  44.424 1.00 44.63  ? 333 VAL A C   1 
ATOM   2347 O O   . VAL A 1 309 ? 39.788 78.847  44.358 1.00 44.89  ? 333 VAL A O   1 
ATOM   2348 C CB  . VAL A 1 309 ? 41.446 81.172  43.671 1.00 37.54  ? 333 VAL A CB  1 
ATOM   2349 C CG1 . VAL A 1 309 ? 40.929 80.901  42.252 1.00 32.72  ? 333 VAL A CG1 1 
ATOM   2350 C CG2 . VAL A 1 309 ? 42.194 82.480  43.729 1.00 30.04  ? 333 VAL A CG2 1 
ATOM   2351 N N   . LYS A 1 310 ? 38.060 80.295  44.299 1.00 49.95  ? 334 LYS A N   1 
ATOM   2352 C CA  . LYS A 1 310 ? 37.082 79.270  43.932 1.00 55.50  ? 334 LYS A CA  1 
ATOM   2353 C C   . LYS A 1 310 ? 36.792 79.452  42.423 1.00 55.60  ? 334 LYS A C   1 
ATOM   2354 O O   . LYS A 1 310 ? 37.191 80.458  41.828 1.00 56.73  ? 334 LYS A O   1 
ATOM   2355 C CB  . LYS A 1 310 ? 35.802 79.400  44.772 1.00 68.84  ? 334 LYS A CB  1 
ATOM   2356 C CG  . LYS A 1 310 ? 35.986 79.131  46.271 1.00 74.18  ? 334 LYS A CG  1 
ATOM   2357 C CD  . LYS A 1 310 ? 36.361 77.673  46.579 1.00 77.53  ? 334 LYS A CD  1 
ATOM   2358 C CE  . LYS A 1 310 ? 36.306 77.361  48.093 1.00 79.74  ? 334 LYS A CE  1 
ATOM   2359 N NZ  . LYS A 1 310 ? 34.934 76.973  48.593 1.00 79.53  ? 334 LYS A NZ  1 
ATOM   2360 N N   . ALA A 1 311 ? 36.109 78.495  41.808 1.00 56.97  ? 335 ALA A N   1 
ATOM   2361 C CA  . ALA A 1 311 ? 35.856 78.571  40.377 1.00 54.96  ? 335 ALA A CA  1 
ATOM   2362 C C   . ALA A 1 311 ? 34.492 78.101  39.903 1.00 54.28  ? 335 ALA A C   1 
ATOM   2363 O O   . ALA A 1 311 ? 34.005 77.058  40.332 1.00 55.85  ? 335 ALA A O   1 
ATOM   2364 C CB  . ALA A 1 311 ? 36.918 77.746  39.630 1.00 41.07  ? 335 ALA A CB  1 
ATOM   2365 N N   . ALA A 1 312 ? 33.876 78.902  39.037 1.00 49.78  ? 336 ALA A N   1 
ATOM   2366 C CA  . ALA A 1 312 ? 32.644 78.491  38.355 1.00 48.63  ? 336 ALA A CA  1 
ATOM   2367 C C   . ALA A 1 312 ? 33.105 77.413  37.352 1.00 47.12  ? 336 ALA A C   1 
ATOM   2368 O O   . ALA A 1 312 ? 34.242 77.448  36.863 1.00 51.22  ? 336 ALA A O   1 
ATOM   2369 C CB  . ALA A 1 312 ? 32.029 79.659  37.604 1.00 41.72  ? 336 ALA A CB  1 
ATOM   2370 N N   . PRO A 1 313 ? 32.221 76.462  37.020 1.00 44.61  ? 337 PRO A N   1 
ATOM   2371 C CA  . PRO A 1 313 ? 32.596 75.405  36.086 1.00 44.61  ? 337 PRO A CA  1 
ATOM   2372 C C   . PRO A 1 313 ? 33.028 75.916  34.721 1.00 46.01  ? 337 PRO A C   1 
ATOM   2373 O O   . PRO A 1 313 ? 32.469 76.886  34.209 1.00 45.49  ? 337 PRO A O   1 
ATOM   2374 C CB  . PRO A 1 313 ? 31.318 74.557  35.968 1.00 41.80  ? 337 PRO A CB  1 
ATOM   2375 C CG  . PRO A 1 313 ? 30.534 74.894  37.157 1.00 39.86  ? 337 PRO A CG  1 
ATOM   2376 C CD  . PRO A 1 313 ? 30.802 76.350  37.392 1.00 41.47  ? 337 PRO A CD  1 
ATOM   2377 N N   . TYR A 1 314 ? 34.041 75.260  34.156 1.00 56.00  ? 338 TYR A N   1 
ATOM   2378 C CA  . TYR A 1 314 ? 34.523 75.540  32.807 1.00 59.41  ? 338 TYR A CA  1 
ATOM   2379 C C   . TYR A 1 314 ? 34.807 74.190  32.175 1.00 58.26  ? 338 TYR A C   1 
ATOM   2380 O O   . TYR A 1 314 ? 35.267 73.269  32.846 1.00 60.05  ? 338 TYR A O   1 
ATOM   2381 C CB  . TYR A 1 314 ? 35.734 76.464  32.788 1.00 63.79  ? 338 TYR A CB  1 
ATOM   2382 C CG  . TYR A 1 314 ? 36.907 76.070  33.655 1.00 69.08  ? 338 TYR A CG  1 
ATOM   2383 C CD1 . TYR A 1 314 ? 38.055 75.498  33.097 1.00 73.14  ? 338 TYR A CD1 1 
ATOM   2384 C CD2 . TYR A 1 314 ? 36.895 76.297  35.031 1.00 71.17  ? 338 TYR A CD2 1 
ATOM   2385 C CE1 . TYR A 1 314 ? 39.168 75.163  33.892 1.00 73.75  ? 338 TYR A CE1 1 
ATOM   2386 C CE2 . TYR A 1 314 ? 37.995 75.965  35.833 1.00 72.42  ? 338 TYR A CE2 1 
ATOM   2387 C CZ  . TYR A 1 314 ? 39.126 75.400  35.260 1.00 73.46  ? 338 TYR A CZ  1 
ATOM   2388 O OH  . TYR A 1 314 ? 40.206 75.067  36.050 1.00 73.10  ? 338 TYR A OH  1 
ATOM   2389 N N   . TRP A 1 315 ? 34.525 74.086  30.881 1.00 53.81  ? 339 TRP A N   1 
ATOM   2390 C CA  . TRP A 1 315 ? 34.617 72.827  30.195 1.00 54.25  ? 339 TRP A CA  1 
ATOM   2391 C C   . TRP A 1 315 ? 35.977 72.187  30.089 1.00 55.14  ? 339 TRP A C   1 
ATOM   2392 O O   . TRP A 1 315 ? 36.953 72.848  29.714 1.00 56.40  ? 339 TRP A O   1 
ATOM   2393 C CB  . TRP A 1 315 ? 34.074 72.957  28.765 1.00 52.77  ? 339 TRP A CB  1 
ATOM   2394 C CG  . TRP A 1 315 ? 32.587 73.127  28.640 1.00 49.65  ? 339 TRP A CG  1 
ATOM   2395 C CD1 . TRP A 1 315 ? 31.919 74.218  28.143 1.00 48.27  ? 339 TRP A CD1 1 
ATOM   2396 C CD2 . TRP A 1 315 ? 31.586 72.172  28.996 1.00 47.95  ? 339 TRP A CD2 1 
ATOM   2397 N NE1 . TRP A 1 315 ? 30.571 73.992  28.167 1.00 47.71  ? 339 TRP A NE1 1 
ATOM   2398 C CE2 . TRP A 1 315 ? 30.335 72.746  28.687 1.00 46.95  ? 339 TRP A CE2 1 
ATOM   2399 C CE3 . TRP A 1 315 ? 31.623 70.887  29.546 1.00 46.86  ? 339 TRP A CE3 1 
ATOM   2400 C CZ2 . TRP A 1 315 ? 29.126 72.076  28.916 1.00 47.31  ? 339 TRP A CZ2 1 
ATOM   2401 C CZ3 . TRP A 1 315 ? 30.416 70.223  29.770 1.00 46.79  ? 339 TRP A CZ3 1 
ATOM   2402 C CH2 . TRP A 1 315 ? 29.186 70.820  29.456 1.00 45.12  ? 339 TRP A CH2 1 
ATOM   2403 N N   . LEU A 1 316 ? 36.032 70.922  30.502 1.00 61.13  ? 340 LEU A N   1 
ATOM   2404 C CA  . LEU A 1 316 ? 37.185 70.093  30.226 1.00 64.49  ? 340 LEU A CA  1 
ATOM   2405 C C   . LEU A 1 316 ? 36.748 69.264  28.999 1.00 66.94  ? 340 LEU A C   1 
ATOM   2406 O O   . LEU A 1 316 ? 37.365 69.335  27.932 1.00 69.83  ? 340 LEU A O   1 
ATOM   2407 C CB  . LEU A 1 316 ? 37.519 69.135  31.369 1.00 62.11  ? 340 LEU A CB  1 
ATOM   2408 C CG  . LEU A 1 316 ? 38.813 69.392  32.161 1.00 60.14  ? 340 LEU A CG  1 
ATOM   2409 C CD1 . LEU A 1 316 ? 39.190 70.878  32.178 1.00 59.45  ? 340 LEU A CD1 1 
ATOM   2410 C CD2 . LEU A 1 316 ? 38.645 68.861  33.586 1.00 57.16  ? 340 LEU A CD2 1 
ATOM   2411 N N   . ASP A 1 317 ? 35.656 68.518  29.157 1.00 71.05  ? 341 ASP A N   1 
ATOM   2412 C CA  . ASP A 1 317 ? 35.176 67.626  28.116 1.00 71.41  ? 341 ASP A CA  1 
ATOM   2413 C C   . ASP A 1 317 ? 33.708 67.840  27.801 1.00 67.27  ? 341 ASP A C   1 
ATOM   2414 O O   . ASP A 1 317 ? 32.847 67.133  28.323 1.00 62.26  ? 341 ASP A O   1 
ATOM   2415 C CB  . ASP A 1 317 ? 35.417 66.176  28.560 1.00 87.23  ? 341 ASP A CB  1 
ATOM   2416 C CG  . ASP A 1 317 ? 36.070 65.332  27.479 1.00 98.84  ? 341 ASP A CG  1 
ATOM   2417 O OD1 . ASP A 1 317 ? 36.724 64.323  27.831 1.00 104.61 ? 341 ASP A OD1 1 
ATOM   2418 O OD2 . ASP A 1 317 ? 35.930 65.677  26.283 1.00 104.25 ? 341 ASP A OD2 1 
ATOM   2419 N N   . GLU A 1 318 ? 33.435 68.822  26.943 1.00 59.00  ? 342 GLU A N   1 
ATOM   2420 C CA  . GLU A 1 318 ? 32.066 69.135  26.526 1.00 60.34  ? 342 GLU A CA  1 
ATOM   2421 C C   . GLU A 1 318 ? 31.514 68.069  25.586 1.00 61.76  ? 342 GLU A C   1 
ATOM   2422 O O   . GLU A 1 318 ? 32.192 67.647  24.648 1.00 57.72  ? 342 GLU A O   1 
ATOM   2423 C CB  . GLU A 1 318 ? 32.024 70.509  25.828 1.00 63.61  ? 342 GLU A CB  1 
ATOM   2424 C CG  . GLU A 1 318 ? 30.667 70.882  25.222 1.00 69.74  ? 342 GLU A CG  1 
ATOM   2425 C CD  . GLU A 1 318 ? 30.557 72.359  24.828 1.00 72.54  ? 342 GLU A CD  1 
ATOM   2426 O OE1 . GLU A 1 318 ? 31.572 73.086  24.883 1.00 73.42  ? 342 GLU A OE1 1 
ATOM   2427 O OE2 . GLU A 1 318 ? 29.444 72.789  24.456 1.00 74.07  ? 342 GLU A OE2 1 
ATOM   2428 N N   . PRO A 1 319 ? 30.293 67.583  25.855 1.00 70.08  ? 343 PRO A N   1 
ATOM   2429 C CA  . PRO A 1 319 ? 29.717 66.567  24.968 1.00 74.30  ? 343 PRO A CA  1 
ATOM   2430 C C   . PRO A 1 319 ? 29.347 67.172  23.610 1.00 79.95  ? 343 PRO A C   1 
ATOM   2431 O O   . PRO A 1 319 ? 28.787 68.271  23.543 1.00 81.64  ? 343 PRO A O   1 
ATOM   2432 C CB  . PRO A 1 319 ? 28.468 66.088  25.718 1.00 62.04  ? 343 PRO A CB  1 
ATOM   2433 C CG  . PRO A 1 319 ? 28.146 67.171  26.652 1.00 58.15  ? 343 PRO A CG  1 
ATOM   2434 C CD  . PRO A 1 319 ? 29.468 67.775  27.059 1.00 59.34  ? 343 PRO A CD  1 
ATOM   2435 N N   . LYS A 1 320 ? 29.684 66.450  22.541 1.00 78.52  ? 344 LYS A N   1 
ATOM   2436 C CA  . LYS A 1 320 ? 29.351 66.863  21.178 1.00 81.68  ? 344 LYS A CA  1 
ATOM   2437 C C   . LYS A 1 320 ? 28.280 65.899  20.649 1.00 80.91  ? 344 LYS A C   1 
ATOM   2438 O O   . LYS A 1 320 ? 28.060 64.824  21.225 1.00 78.88  ? 344 LYS A O   1 
ATOM   2439 C CB  . LYS A 1 320 ? 30.586 66.787  20.261 1.00 95.24  ? 344 LYS A CB  1 
ATOM   2440 C CG  . LYS A 1 320 ? 31.849 67.450  20.805 1.00 100.86 ? 344 LYS A CG  1 
ATOM   2441 C CD  . LYS A 1 320 ? 33.097 66.889  20.116 1.00 103.50 ? 344 LYS A CD  1 
ATOM   2442 C CE  . LYS A 1 320 ? 34.353 67.100  20.962 1.00 103.43 ? 344 LYS A CE  1 
ATOM   2443 N NZ  . LYS A 1 320 ? 35.394 66.062  20.680 1.00 102.50 ? 344 LYS A NZ  1 
ATOM   2444 N N   . ASN A 1 321 ? 27.625 66.301  19.557 1.00 84.93  ? 345 ASN A N   1 
ATOM   2445 C CA  . ASN A 1 321 ? 26.606 65.476  18.900 1.00 82.25  ? 345 ASN A CA  1 
ATOM   2446 C C   . ASN A 1 321 ? 27.189 64.124  18.474 1.00 78.63  ? 345 ASN A C   1 
ATOM   2447 O O   . ASN A 1 321 ? 28.386 64.000  18.205 1.00 75.53  ? 345 ASN A O   1 
ATOM   2448 C CB  . ASN A 1 321 ? 26.056 66.187  17.663 1.00 98.03  ? 345 ASN A CB  1 
ATOM   2449 C CG  . ASN A 1 321 ? 25.549 67.590  17.965 1.00 106.99 ? 345 ASN A CG  1 
ATOM   2450 O OD1 . ASN A 1 321 ? 25.833 68.531  17.223 1.00 112.01 ? 345 ASN A OD1 1 
ATOM   2451 N ND2 . ASN A 1 321 ? 24.786 67.734  19.046 1.00 111.42 ? 345 ASN A ND2 1 
ATOM   2452 N N   . LEU A 1 322 ? 26.326 63.118  18.417 1.00 77.18  ? 346 LEU A N   1 
ATOM   2453 C CA  . LEU A 1 322 ? 26.745 61.790  18.038 1.00 74.46  ? 346 LEU A CA  1 
ATOM   2454 C C   . LEU A 1 322 ? 26.045 61.244  16.795 1.00 75.65  ? 346 LEU A C   1 
ATOM   2455 O O   . LEU A 1 322 ? 24.824 61.076  16.778 1.00 80.81  ? 346 LEU A O   1 
ATOM   2456 C CB  . LEU A 1 322 ? 26.532 60.799  19.199 1.00 56.00  ? 346 LEU A CB  1 
ATOM   2457 C CG  . LEU A 1 322 ? 27.521 60.807  20.379 1.00 48.41  ? 346 LEU A CG  1 
ATOM   2458 C CD1 . LEU A 1 322 ? 27.163 59.679  21.347 1.00 43.14  ? 346 LEU A CD1 1 
ATOM   2459 C CD2 . LEU A 1 322 ? 28.959 60.649  19.900 1.00 45.70  ? 346 LEU A CD2 1 
ATOM   2460 N N   . ILE A 1 323 ? 26.827 60.996  15.745 1.00 73.93  ? 347 ILE A N   1 
ATOM   2461 C CA  . ILE A 1 323 ? 26.294 60.349  14.540 1.00 75.37  ? 347 ILE A CA  1 
ATOM   2462 C C   . ILE A 1 323 ? 26.928 58.951  14.450 1.00 71.16  ? 347 ILE A C   1 
ATOM   2463 O O   . ILE A 1 323 ? 28.114 58.797  14.155 1.00 71.40  ? 347 ILE A O   1 
ATOM   2464 C CB  . ILE A 1 323 ? 26.564 61.159  13.265 1.00 74.59  ? 347 ILE A CB  1 
ATOM   2465 C CG1 . ILE A 1 323 ? 25.920 62.551  13.390 1.00 77.38  ? 347 ILE A CG1 1 
ATOM   2466 C CG2 . ILE A 1 323 ? 26.002 60.409  12.055 1.00 76.45  ? 347 ILE A CG2 1 
ATOM   2467 C CD1 . ILE A 1 323 ? 26.692 63.536  14.259 1.00 82.87  ? 347 ILE A CD1 1 
ATOM   2468 N N   . LEU A 1 324 ? 26.117 57.937  14.712 1.00 73.94  ? 348 LEU A N   1 
ATOM   2469 C CA  . LEU A 1 324 ? 26.607 56.575  14.748 1.00 76.37  ? 348 LEU A CA  1 
ATOM   2470 C C   . LEU A 1 324 ? 25.954 55.666  13.722 1.00 80.61  ? 348 LEU A C   1 
ATOM   2471 O O   . LEU A 1 324 ? 24.839 55.923  13.270 1.00 78.27  ? 348 LEU A O   1 
ATOM   2472 C CB  . LEU A 1 324 ? 26.379 55.990  16.159 1.00 73.21  ? 348 LEU A CB  1 
ATOM   2473 C CG  . LEU A 1 324 ? 27.028 56.744  17.333 1.00 70.99  ? 348 LEU A CG  1 
ATOM   2474 C CD1 . LEU A 1 324 ? 26.418 56.295  18.649 1.00 68.77  ? 348 LEU A CD1 1 
ATOM   2475 C CD2 . LEU A 1 324 ? 28.539 56.545  17.337 1.00 69.20  ? 348 LEU A CD2 1 
ATOM   2476 N N   . ALA A 1 325 ? 26.677 54.616  13.342 1.00 86.65  ? 349 ALA A N   1 
ATOM   2477 C CA  . ALA A 1 325 ? 26.136 53.609  12.442 1.00 93.73  ? 349 ALA A CA  1 
ATOM   2478 C C   . ALA A 1 325 ? 25.437 52.566  13.322 1.00 93.95  ? 349 ALA A C   1 
ATOM   2479 O O   . ALA A 1 325 ? 25.923 52.233  14.408 1.00 97.20  ? 349 ALA A O   1 
ATOM   2480 C CB  . ALA A 1 325 ? 27.244 52.967  11.637 1.00 97.32  ? 349 ALA A CB  1 
ATOM   2481 N N   . PRO A 1 326 ? 24.282 52.047  12.865 1.00 92.85  ? 350 PRO A N   1 
ATOM   2482 C CA  . PRO A 1 326 ? 23.532 51.045  13.636 1.00 91.60  ? 350 PRO A CA  1 
ATOM   2483 C C   . PRO A 1 326 ? 24.388 49.888  14.137 1.00 91.80  ? 350 PRO A C   1 
ATOM   2484 O O   . PRO A 1 326 ? 24.969 49.155  13.337 1.00 95.61  ? 350 PRO A O   1 
ATOM   2485 C CB  . PRO A 1 326 ? 22.431 50.583  12.668 1.00 79.43  ? 350 PRO A CB  1 
ATOM   2486 C CG  . PRO A 1 326 ? 22.798 51.177  11.322 1.00 76.91  ? 350 PRO A CG  1 
ATOM   2487 C CD  . PRO A 1 326 ? 23.580 52.411  11.623 1.00 79.54  ? 350 PRO A CD  1 
ATOM   2488 N N   . GLY A 1 327 ? 24.461 49.739  15.462 1.00 87.91  ? 351 GLY A N   1 
ATOM   2489 C CA  . GLY A 1 327 ? 25.237 48.673  16.080 1.00 81.23  ? 351 GLY A CA  1 
ATOM   2490 C C   . GLY A 1 327 ? 26.501 49.174  16.756 1.00 79.33  ? 351 GLY A C   1 
ATOM   2491 O O   . GLY A 1 327 ? 27.105 48.473  17.572 1.00 77.74  ? 351 GLY A O   1 
ATOM   2492 N N   . GLU A 1 328 ? 26.896 50.399  16.429 1.00 74.60  ? 352 GLU A N   1 
ATOM   2493 C CA  . GLU A 1 328 ? 28.119 50.976  16.967 1.00 75.80  ? 352 GLU A CA  1 
ATOM   2494 C C   . GLU A 1 328 ? 27.961 51.505  18.383 1.00 80.28  ? 352 GLU A C   1 
ATOM   2495 O O   . GLU A 1 328 ? 26.943 52.121  18.714 1.00 79.73  ? 352 GLU A O   1 
ATOM   2496 C CB  . GLU A 1 328 ? 28.598 52.119  16.055 1.00 73.39  ? 352 GLU A CB  1 
ATOM   2497 C CG  . GLU A 1 328 ? 30.049 52.520  16.259 1.00 70.11  ? 352 GLU A CG  1 
ATOM   2498 C CD  . GLU A 1 328 ? 30.373 53.871  15.657 1.00 70.05  ? 352 GLU A CD  1 
ATOM   2499 O OE1 . GLU A 1 328 ? 29.630 54.344  14.764 1.00 67.94  ? 352 GLU A OE1 1 
ATOM   2500 O OE2 . GLU A 1 328 ? 31.386 54.462  16.082 1.00 70.59  ? 352 GLU A OE2 1 
ATOM   2501 N N   . ASP A 1 329 ? 28.967 51.248  19.217 1.00 77.05  ? 353 ASP A N   1 
ATOM   2502 C CA  . ASP A 1 329 ? 28.984 51.765  20.587 1.00 79.28  ? 353 ASP A CA  1 
ATOM   2503 C C   . ASP A 1 329 ? 29.412 53.246  20.579 1.00 73.81  ? 353 ASP A C   1 
ATOM   2504 O O   . ASP A 1 329 ? 30.416 53.618  19.959 1.00 67.36  ? 353 ASP A O   1 
ATOM   2505 C CB  . ASP A 1 329 ? 29.962 50.968  21.461 1.00 99.06  ? 353 ASP A CB  1 
ATOM   2506 C CG  . ASP A 1 329 ? 29.677 49.473  21.450 1.00 118.23 ? 353 ASP A CG  1 
ATOM   2507 O OD1 . ASP A 1 329 ? 30.000 48.803  20.437 1.00 128.24 ? 353 ASP A OD1 1 
ATOM   2508 O OD2 . ASP A 1 329 ? 29.131 48.967  22.458 1.00 127.79 ? 353 ASP A OD2 1 
ATOM   2509 N N   . GLY A 1 330 ? 28.628 54.084  21.256 1.00 73.29  ? 354 GLY A N   1 
ATOM   2510 C CA  . GLY A 1 330 ? 28.937 55.504  21.357 1.00 71.12  ? 354 GLY A CA  1 
ATOM   2511 C C   . GLY A 1 330 ? 29.076 55.937  22.810 1.00 70.76  ? 354 GLY A C   1 
ATOM   2512 O O   . GLY A 1 330 ? 28.741 55.178  23.724 1.00 70.29  ? 354 GLY A O   1 
ATOM   2513 N N   . ARG A 1 331 ? 29.576 57.150  23.033 1.00 75.99  ? 355 ARG A N   1 
ATOM   2514 C CA  . ARG A 1 331 ? 29.728 57.654  24.392 1.00 75.77  ? 355 ARG A CA  1 
ATOM   2515 C C   . ARG A 1 331 ? 29.658 59.171  24.501 1.00 72.46  ? 355 ARG A C   1 
ATOM   2516 O O   . ARG A 1 331 ? 30.058 59.903  23.586 1.00 72.84  ? 355 ARG A O   1 
ATOM   2517 C CB  . ARG A 1 331 ? 31.052 57.146  25.022 1.00 79.42  ? 355 ARG A CB  1 
ATOM   2518 C CG  . ARG A 1 331 ? 32.233 58.132  25.078 1.00 81.59  ? 355 ARG A CG  1 
ATOM   2519 C CD  . ARG A 1 331 ? 33.030 58.183  23.784 1.00 80.82  ? 355 ARG A CD  1 
ATOM   2520 N NE  . ARG A 1 331 ? 32.811 59.412  23.029 1.00 82.00  ? 355 ARG A NE  1 
ATOM   2521 C CZ  . ARG A 1 331 ? 33.516 60.530  23.179 1.00 81.79  ? 355 ARG A CZ  1 
ATOM   2522 N NH1 . ARG A 1 331 ? 34.497 60.580  24.064 1.00 82.30  ? 355 ARG A NH1 1 
ATOM   2523 N NH2 . ARG A 1 331 ? 33.240 61.600  22.441 1.00 81.63  ? 355 ARG A NH2 1 
ATOM   2524 N N   . LEU A 1 332 ? 29.103 59.624  25.623 1.00 64.39  ? 356 LEU A N   1 
ATOM   2525 C CA  . LEU A 1 332 ? 29.041 61.043  25.933 1.00 60.36  ? 356 LEU A CA  1 
ATOM   2526 C C   . LEU A 1 332 ? 29.741 61.286  27.266 1.00 59.25  ? 356 LEU A C   1 
ATOM   2527 O O   . LEU A 1 332 ? 29.422 60.665  28.277 1.00 57.20  ? 356 LEU A O   1 
ATOM   2528 C CB  . LEU A 1 332 ? 27.599 61.543  26.003 1.00 57.71  ? 356 LEU A CB  1 
ATOM   2529 C CG  . LEU A 1 332 ? 26.825 61.586  24.674 1.00 56.57  ? 356 LEU A CG  1 
ATOM   2530 C CD1 . LEU A 1 332 ? 25.346 61.830  24.945 1.00 55.35  ? 356 LEU A CD1 1 
ATOM   2531 C CD2 . LEU A 1 332 ? 27.394 62.662  23.752 1.00 55.64  ? 356 LEU A CD2 1 
ATOM   2532 N N   . VAL A 1 333 ? 30.735 62.163  27.235 1.00 62.26  ? 357 VAL A N   1 
ATOM   2533 C CA  . VAL A 1 333 ? 31.470 62.529  28.425 1.00 65.55  ? 357 VAL A CA  1 
ATOM   2534 C C   . VAL A 1 333 ? 31.215 64.006  28.664 1.00 64.13  ? 357 VAL A C   1 
ATOM   2535 O O   . VAL A 1 333 ? 31.408 64.840  27.778 1.00 63.16  ? 357 VAL A O   1 
ATOM   2536 C CB  . VAL A 1 333 ? 33.001 62.284  28.274 1.00 73.83  ? 357 VAL A CB  1 
ATOM   2537 C CG1 . VAL A 1 333 ? 33.757 62.827  29.492 1.00 77.52  ? 357 VAL A CG1 1 
ATOM   2538 C CG2 . VAL A 1 333 ? 33.273 60.793  28.097 1.00 78.09  ? 357 VAL A CG2 1 
ATOM   2539 N N   . CYS A 1 334 ? 30.751 64.310  29.870 1.00 69.57  ? 358 CYS A N   1 
ATOM   2540 C CA  . CYS A 1 334 ? 30.466 65.673  30.270 1.00 70.19  ? 358 CYS A CA  1 
ATOM   2541 C C   . CYS A 1 334 ? 31.228 65.952  31.548 1.00 68.22  ? 358 CYS A C   1 
ATOM   2542 O O   . CYS A 1 334 ? 30.783 65.611  32.640 1.00 69.16  ? 358 CYS A O   1 
ATOM   2543 C CB  . CYS A 1 334 ? 28.978 65.835  30.494 1.00 72.69  ? 358 CYS A CB  1 
ATOM   2544 S SG  . CYS A 1 334 ? 28.517 67.471  31.121 1.00 76.68  ? 358 CYS A SG  1 
ATOM   2545 N N   . ARG A 1 335 ? 32.383 66.581  31.397 1.00 55.91  ? 359 ARG A N   1 
ATOM   2546 C CA  . ARG A 1 335 ? 33.235 66.856  32.522 1.00 51.78  ? 359 ARG A CA  1 
ATOM   2547 C C   . ARG A 1 335 ? 33.722 68.281  32.521 1.00 48.99  ? 359 ARG A C   1 
ATOM   2548 O O   . ARG A 1 335 ? 34.279 68.759  31.539 1.00 46.05  ? 359 ARG A O   1 
ATOM   2549 C CB  . ARG A 1 335 ? 34.438 65.890  32.515 1.00 62.64  ? 359 ARG A CB  1 
ATOM   2550 C CG  . ARG A 1 335 ? 34.122 64.509  33.095 1.00 71.64  ? 359 ARG A CG  1 
ATOM   2551 C CD  . ARG A 1 335 ? 35.340 63.572  33.138 1.00 76.13  ? 359 ARG A CD  1 
ATOM   2552 N NE  . ARG A 1 335 ? 36.510 64.134  33.826 1.00 78.32  ? 359 ARG A NE  1 
ATOM   2553 C CZ  . ARG A 1 335 ? 36.606 64.335  35.142 1.00 79.17  ? 359 ARG A CZ  1 
ATOM   2554 N NH1 . ARG A 1 335 ? 35.597 64.022  35.953 1.00 79.18  ? 359 ARG A NH1 1 
ATOM   2555 N NH2 . ARG A 1 335 ? 37.722 64.852  35.654 1.00 79.72  ? 359 ARG A NH2 1 
ATOM   2556 N N   . ALA A 1 336 ? 33.476 68.971  33.625 1.00 51.53  ? 360 ALA A N   1 
ATOM   2557 C CA  . ALA A 1 336 ? 33.949 70.328  33.785 1.00 52.72  ? 360 ALA A CA  1 
ATOM   2558 C C   . ALA A 1 336 ? 34.776 70.409  35.054 1.00 54.33  ? 360 ALA A C   1 
ATOM   2559 O O   . ALA A 1 336 ? 34.512 69.696  36.016 1.00 55.50  ? 360 ALA A O   1 
ATOM   2560 C CB  . ALA A 1 336 ? 32.775 71.296  33.896 1.00 48.72  ? 360 ALA A CB  1 
ATOM   2561 N N   . ASN A 1 337 ? 35.790 71.258  35.042 1.00 54.83  ? 361 ASN A N   1 
ATOM   2562 C CA  . ASN A 1 337 ? 36.572 71.488  36.241 1.00 60.13  ? 361 ASN A CA  1 
ATOM   2563 C C   . ASN A 1 337 ? 36.026 72.737  36.933 1.00 61.26  ? 361 ASN A C   1 
ATOM   2564 O O   . ASN A 1 337 ? 35.724 73.736  36.292 1.00 60.05  ? 361 ASN A O   1 
ATOM   2565 C CB  . ASN A 1 337 ? 38.059 71.693  35.926 1.00 76.19  ? 361 ASN A CB  1 
ATOM   2566 C CG  . ASN A 1 337 ? 38.928 71.687  37.184 1.00 84.76  ? 361 ASN A CG  1 
ATOM   2567 O OD1 . ASN A 1 337 ? 38.568 71.082  38.205 1.00 87.40  ? 361 ASN A OD1 1 
ATOM   2568 N ND2 . ASN A 1 337 ? 40.088 72.343  37.108 1.00 89.00  ? 361 ASN A ND2 1 
ATOM   2569 N N   . GLY A 1 338 ? 35.891 72.651  38.251 1.00 69.93  ? 362 GLY A N   1 
ATOM   2570 C CA  . GLY A 1 338 ? 35.427 73.767  39.051 1.00 70.05  ? 362 GLY A CA  1 
ATOM   2571 C C   . GLY A 1 338 ? 35.844 73.592  40.498 1.00 68.71  ? 362 GLY A C   1 
ATOM   2572 O O   . GLY A 1 338 ? 36.398 72.567  40.876 1.00 71.08  ? 362 GLY A O   1 
ATOM   2573 N N   . ASN A 1 339 ? 35.577 74.606  41.307 1.00 58.60  ? 363 ASN A N   1 
ATOM   2574 C CA  . ASN A 1 339 ? 35.890 74.566  42.709 1.00 54.40  ? 363 ASN A CA  1 
ATOM   2575 C C   . ASN A 1 339 ? 34.835 75.347  43.490 1.00 52.44  ? 363 ASN A C   1 
ATOM   2576 O O   . ASN A 1 339 ? 34.790 76.575  43.429 1.00 51.25  ? 363 ASN A O   1 
ATOM   2577 C CB  . ASN A 1 339 ? 37.285 75.170  42.966 1.00 55.18  ? 363 ASN A CB  1 
ATOM   2578 C CG  . ASN A 1 339 ? 37.775 74.935  44.391 1.00 54.91  ? 363 ASN A CG  1 
ATOM   2579 O OD1 . ASN A 1 339 ? 37.111 74.257  45.185 1.00 53.86  ? 363 ASN A OD1 1 
ATOM   2580 N ND2 . ASN A 1 339 ? 38.932 75.503  44.721 1.00 54.23  ? 363 ASN A ND2 1 
ATOM   2581 N N   . PRO A 1 340 ? 33.930 74.627  44.192 1.00 49.56  ? 364 PRO A N   1 
ATOM   2582 C CA  . PRO A 1 340 ? 33.858 73.170  44.410 1.00 50.09  ? 364 PRO A CA  1 
ATOM   2583 C C   . PRO A 1 340 ? 33.687 72.382  43.121 1.00 52.50  ? 364 PRO A C   1 
ATOM   2584 O O   . PRO A 1 340 ? 33.241 72.935  42.129 1.00 54.29  ? 364 PRO A O   1 
ATOM   2585 C CB  . PRO A 1 340 ? 32.607 73.006  45.283 1.00 41.61  ? 364 PRO A CB  1 
ATOM   2586 C CG  . PRO A 1 340 ? 32.446 74.307  45.954 1.00 40.90  ? 364 PRO A CG  1 
ATOM   2587 C CD  . PRO A 1 340 ? 32.850 75.316  44.916 1.00 43.93  ? 364 PRO A CD  1 
ATOM   2588 N N   . LYS A 1 341 ? 34.005 71.087  43.162 1.00 47.40  ? 365 LYS A N   1 
ATOM   2589 C CA  . LYS A 1 341 ? 33.904 70.223  41.987 1.00 51.38  ? 365 LYS A CA  1 
ATOM   2590 C C   . LYS A 1 341 ? 32.455 70.118  41.533 1.00 46.75  ? 365 LYS A C   1 
ATOM   2591 O O   . LYS A 1 341 ? 31.580 69.832  42.329 1.00 44.52  ? 365 LYS A O   1 
ATOM   2592 C CB  . LYS A 1 341 ? 34.482 68.828  42.271 1.00 71.17  ? 365 LYS A CB  1 
ATOM   2593 C CG  . LYS A 1 341 ? 35.991 68.802  42.537 1.00 89.09  ? 365 LYS A CG  1 
ATOM   2594 C CD  . LYS A 1 341 ? 36.843 68.890  41.265 1.00 97.73  ? 365 LYS A CD  1 
ATOM   2595 C CE  . LYS A 1 341 ? 36.915 67.546  40.517 1.00 100.38 ? 365 LYS A CE  1 
ATOM   2596 N NZ  . LYS A 1 341 ? 37.722 67.643  39.261 1.00 100.42 ? 365 LYS A NZ  1 
ATOM   2597 N N   . PRO A 1 342 ? 32.200 70.337  40.228 1.00 49.91  ? 366 PRO A N   1 
ATOM   2598 C CA  . PRO A 1 342 ? 30.874 70.297  39.596 1.00 50.48  ? 366 PRO A CA  1 
ATOM   2599 C C   . PRO A 1 342 ? 30.085 69.015  39.738 1.00 49.55  ? 366 PRO A C   1 
ATOM   2600 O O   . PRO A 1 342 ? 30.653 67.961  39.926 1.00 52.74  ? 366 PRO A O   1 
ATOM   2601 C CB  . PRO A 1 342 ? 31.170 70.586  38.125 1.00 56.60  ? 366 PRO A CB  1 
ATOM   2602 C CG  . PRO A 1 342 ? 32.448 71.336  38.149 1.00 56.66  ? 366 PRO A CG  1 
ATOM   2603 C CD  . PRO A 1 342 ? 33.242 70.715  39.252 1.00 55.70  ? 366 PRO A CD  1 
ATOM   2604 N N   . THR A 1 343 ? 28.769 69.133  39.620 1.00 50.36  ? 367 THR A N   1 
ATOM   2605 C CA  . THR A 1 343 ? 27.845 68.006  39.660 1.00 50.69  ? 367 THR A CA  1 
ATOM   2606 C C   . THR A 1 343 ? 27.359 67.769  38.239 1.00 47.44  ? 367 THR A C   1 
ATOM   2607 O O   . THR A 1 343 ? 27.277 68.708  37.451 1.00 46.15  ? 367 THR A O   1 
ATOM   2608 C CB  . THR A 1 343 ? 26.555 68.337  40.448 1.00 57.85  ? 367 THR A CB  1 
ATOM   2609 O OG1 . THR A 1 343 ? 26.874 69.082  41.627 1.00 65.35  ? 367 THR A OG1 1 
ATOM   2610 C CG2 . THR A 1 343 ? 25.832 67.068  40.827 1.00 60.19  ? 367 THR A CG2 1 
ATOM   2611 N N   . VAL A 1 344 ? 26.995 66.533  37.928 1.00 44.10  ? 368 VAL A N   1 
ATOM   2612 C CA  . VAL A 1 344 ? 26.457 66.233  36.618 1.00 46.29  ? 368 VAL A CA  1 
ATOM   2613 C C   . VAL A 1 344 ? 25.030 65.701  36.710 1.00 46.57  ? 368 VAL A C   1 
ATOM   2614 O O   . VAL A 1 344 ? 24.759 64.768  37.466 1.00 42.74  ? 368 VAL A O   1 
ATOM   2615 C CB  . VAL A 1 344 ? 27.343 65.190  35.852 1.00 55.96  ? 368 VAL A CB  1 
ATOM   2616 C CG1 . VAL A 1 344 ? 26.706 64.821  34.500 1.00 59.39  ? 368 VAL A CG1 1 
ATOM   2617 C CG2 . VAL A 1 344 ? 28.751 65.753  35.641 1.00 58.17  ? 368 VAL A CG2 1 
ATOM   2618 N N   . GLN A 1 345 ? 24.126 66.338  35.960 1.00 51.94  ? 369 GLN A N   1 
ATOM   2619 C CA  . GLN A 1 345 ? 22.739 65.883  35.839 1.00 57.07  ? 369 GLN A CA  1 
ATOM   2620 C C   . GLN A 1 345 ? 22.425 65.675  34.344 1.00 56.90  ? 369 GLN A C   1 
ATOM   2621 O O   . GLN A 1 345 ? 22.701 66.549  33.503 1.00 58.30  ? 369 GLN A O   1 
ATOM   2622 C CB  . GLN A 1 345 ? 21.759 66.890  36.428 1.00 61.96  ? 369 GLN A CB  1 
ATOM   2623 C CG  . GLN A 1 345 ? 22.105 67.368  37.831 1.00 68.19  ? 369 GLN A CG  1 
ATOM   2624 C CD  . GLN A 1 345 ? 21.006 68.237  38.430 1.00 69.83  ? 369 GLN A CD  1 
ATOM   2625 O OE1 . GLN A 1 345 ? 19.896 67.756  38.711 1.00 69.01  ? 369 GLN A OE1 1 
ATOM   2626 N NE2 . GLN A 1 345 ? 21.305 69.523  38.622 1.00 67.26  ? 369 GLN A NE2 1 
ATOM   2627 N N   . TRP A 1 346 ? 21.843 64.522  34.024 1.00 55.52  ? 370 TRP A N   1 
ATOM   2628 C CA  . TRP A 1 346 ? 21.519 64.182  32.643 1.00 56.68  ? 370 TRP A CA  1 
ATOM   2629 C C   . TRP A 1 346 ? 20.030 64.290  32.332 1.00 59.78  ? 370 TRP A C   1 
ATOM   2630 O O   . TRP A 1 346 ? 19.186 63.941  33.154 1.00 56.28  ? 370 TRP A O   1 
ATOM   2631 C CB  . TRP A 1 346 ? 21.997 62.759  32.320 1.00 60.02  ? 370 TRP A CB  1 
ATOM   2632 C CG  . TRP A 1 346 ? 23.492 62.570  32.313 1.00 62.62  ? 370 TRP A CG  1 
ATOM   2633 C CD1 . TRP A 1 346 ? 24.248 61.995  33.291 1.00 64.76  ? 370 TRP A CD1 1 
ATOM   2634 C CD2 . TRP A 1 346 ? 24.404 62.950  31.274 1.00 64.38  ? 370 TRP A CD2 1 
ATOM   2635 N NE1 . TRP A 1 346 ? 25.574 61.990  32.929 1.00 65.73  ? 370 TRP A NE1 1 
ATOM   2636 C CE2 . TRP A 1 346 ? 25.697 62.571  31.695 1.00 65.39  ? 370 TRP A CE2 1 
ATOM   2637 C CE3 . TRP A 1 346 ? 24.255 63.576  30.031 1.00 63.68  ? 370 TRP A CE3 1 
ATOM   2638 C CZ2 . TRP A 1 346 ? 26.836 62.796  30.914 1.00 65.68  ? 370 TRP A CZ2 1 
ATOM   2639 C CZ3 . TRP A 1 346 ? 25.385 63.798  29.258 1.00 63.95  ? 370 TRP A CZ3 1 
ATOM   2640 C CH2 . TRP A 1 346 ? 26.658 63.411  29.701 1.00 64.88  ? 370 TRP A CH2 1 
ATOM   2641 N N   . MET A 1 347 ? 19.718 64.773  31.135 1.00 70.56  ? 371 MET A N   1 
ATOM   2642 C CA  . MET A 1 347 ? 18.339 64.906  30.707 1.00 74.88  ? 371 MET A CA  1 
ATOM   2643 C C   . MET A 1 347 ? 18.147 64.414  29.279 1.00 76.18  ? 371 MET A C   1 
ATOM   2644 O O   . MET A 1 347 ? 19.008 64.601  28.430 1.00 79.45  ? 371 MET A O   1 
ATOM   2645 C CB  . MET A 1 347 ? 17.890 66.366  30.779 1.00 74.59  ? 371 MET A CB  1 
ATOM   2646 C CG  . MET A 1 347 ? 17.502 66.843  32.157 1.00 75.56  ? 371 MET A CG  1 
ATOM   2647 S SD  . MET A 1 347 ? 16.797 68.482  32.046 1.00 78.24  ? 371 MET A SD  1 
ATOM   2648 C CE  . MET A 1 347 ? 16.170 68.730  33.720 1.00 78.38  ? 371 MET A CE  1 
ATOM   2649 N N   . VAL A 1 348 ? 17.012 63.770  29.036 1.00 63.88  ? 372 VAL A N   1 
ATOM   2650 C CA  . VAL A 1 348 ? 16.649 63.319  27.701 1.00 60.82  ? 372 VAL A CA  1 
ATOM   2651 C C   . VAL A 1 348 ? 15.448 64.160  27.267 1.00 59.47  ? 372 VAL A C   1 
ATOM   2652 O O   . VAL A 1 348 ? 14.323 63.940  27.727 1.00 57.25  ? 372 VAL A O   1 
ATOM   2653 C CB  . VAL A 1 348 ? 16.244 61.822  27.670 1.00 63.99  ? 372 VAL A CB  1 
ATOM   2654 C CG1 . VAL A 1 348 ? 16.226 61.319  26.232 1.00 63.48  ? 372 VAL A CG1 1 
ATOM   2655 C CG2 . VAL A 1 348 ? 17.208 60.997  28.508 1.00 64.71  ? 372 VAL A CG2 1 
ATOM   2656 N N   . ASN A 1 349 ? 15.713 65.127  26.391 1.00 68.46  ? 373 ASN A N   1 
ATOM   2657 C CA  . ASN A 1 349 ? 14.696 66.035  25.863 1.00 72.57  ? 373 ASN A CA  1 
ATOM   2658 C C   . ASN A 1 349 ? 13.962 66.796  26.968 1.00 75.43  ? 373 ASN A C   1 
ATOM   2659 O O   . ASN A 1 349 ? 12.730 66.879  26.967 1.00 78.98  ? 373 ASN A O   1 
ATOM   2660 C CB  . ASN A 1 349 ? 13.687 65.270  24.989 1.00 74.15  ? 373 ASN A CB  1 
ATOM   2661 C CG  . ASN A 1 349 ? 14.356 64.476  23.873 1.00 73.58  ? 373 ASN A CG  1 
ATOM   2662 O OD1 . ASN A 1 349 ? 15.037 65.038  23.012 1.00 71.86  ? 373 ASN A OD1 1 
ATOM   2663 N ND2 . ASN A 1 349 ? 14.160 63.160  23.884 1.00 71.01  ? 373 ASN A ND2 1 
ATOM   2664 N N   . GLY A 1 350 ? 14.730 67.344  27.913 1.00 73.18  ? 374 GLY A N   1 
ATOM   2665 C CA  . GLY A 1 350 ? 14.158 68.117  29.008 1.00 73.20  ? 374 GLY A CA  1 
ATOM   2666 C C   . GLY A 1 350 ? 13.735 67.304  30.216 1.00 74.73  ? 374 GLY A C   1 
ATOM   2667 O O   . GLY A 1 350 ? 13.852 67.755  31.357 1.00 71.50  ? 374 GLY A O   1 
ATOM   2668 N N   . GLU A 1 351 ? 13.219 66.107  29.959 1.00 77.48  ? 375 GLU A N   1 
ATOM   2669 C CA  . GLU A 1 351 ? 12.790 65.200  31.018 1.00 80.56  ? 375 GLU A CA  1 
ATOM   2670 C C   . GLU A 1 351 ? 14.039 64.686  31.735 1.00 84.42  ? 375 GLU A C   1 
ATOM   2671 O O   . GLU A 1 351 ? 15.005 64.271  31.093 1.00 76.95  ? 375 GLU A O   1 
ATOM   2672 C CB  . GLU A 1 351 ? 12.006 64.029  30.406 1.00 106.27 ? 375 GLU A CB  1 
ATOM   2673 C CG  . GLU A 1 351 ? 11.026 63.337  31.353 1.00 121.30 ? 375 GLU A CG  1 
ATOM   2674 C CD  . GLU A 1 351 ? 10.078 62.379  30.626 1.00 128.61 ? 375 GLU A CD  1 
ATOM   2675 O OE1 . GLU A 1 351 ? 10.555 61.371  30.051 1.00 131.20 ? 375 GLU A OE1 1 
ATOM   2676 O OE2 . GLU A 1 351 ? 8.852  62.637  30.628 1.00 131.26 ? 375 GLU A OE2 1 
ATOM   2677 N N   . PRO A 1 352 ? 14.050 64.748  33.078 1.00 93.95  ? 376 PRO A N   1 
ATOM   2678 C CA  . PRO A 1 352 ? 15.206 64.269  33.852 1.00 94.34  ? 376 PRO A CA  1 
ATOM   2679 C C   . PRO A 1 352 ? 15.395 62.776  33.609 1.00 91.44  ? 376 PRO A C   1 
ATOM   2680 O O   . PRO A 1 352 ? 14.417 62.028  33.571 1.00 92.45  ? 376 PRO A O   1 
ATOM   2681 C CB  . PRO A 1 352 ? 14.815 64.550  35.299 1.00 120.05 ? 376 PRO A CB  1 
ATOM   2682 C CG  . PRO A 1 352 ? 13.795 65.634  35.214 1.00 123.17 ? 376 PRO A CG  1 
ATOM   2683 C CD  . PRO A 1 352 ? 13.021 65.333  33.959 1.00 118.52 ? 376 PRO A CD  1 
ATOM   2684 N N   . LEU A 1 353 ? 16.652 62.354  33.467 1.00 85.36  ? 377 LEU A N   1 
ATOM   2685 C CA  . LEU A 1 353 ? 16.990 60.958  33.164 1.00 80.92  ? 377 LEU A CA  1 
ATOM   2686 C C   . LEU A 1 353 ? 16.205 59.945  33.990 1.00 81.71  ? 377 LEU A C   1 
ATOM   2687 O O   . LEU A 1 353 ? 15.628 59.002  33.439 1.00 76.74  ? 377 LEU A O   1 
ATOM   2688 C CB  . LEU A 1 353 ? 18.495 60.726  33.345 1.00 81.20  ? 377 LEU A CB  1 
ATOM   2689 C CG  . LEU A 1 353 ? 19.101 59.447  32.745 1.00 80.35  ? 377 LEU A CG  1 
ATOM   2690 C CD1 . LEU A 1 353 ? 19.368 59.635  31.265 1.00 79.01  ? 377 LEU A CD1 1 
ATOM   2691 C CD2 . LEU A 1 353 ? 20.393 59.095  33.476 1.00 80.68  ? 377 LEU A CD2 1 
ATOM   2692 N N   . GLN A 1 354 ? 16.184 60.162  35.306 1.00 85.91  ? 378 GLN A N   1 
ATOM   2693 C CA  . GLN A 1 354 ? 15.488 59.303  36.269 1.00 94.65  ? 378 GLN A CA  1 
ATOM   2694 C C   . GLN A 1 354 ? 14.076 58.886  35.825 1.00 92.96  ? 378 GLN A C   1 
ATOM   2695 O O   . GLN A 1 354 ? 13.699 57.723  35.956 1.00 87.92  ? 378 GLN A O   1 
ATOM   2696 C CB  . GLN A 1 354 ? 15.433 60.021  37.633 1.00 124.09 ? 378 GLN A CB  1 
ATOM   2697 C CG  . GLN A 1 354 ? 14.899 59.194  38.803 1.00 142.13 ? 378 GLN A CG  1 
ATOM   2698 C CD  . GLN A 1 354 ? 14.988 59.937  40.137 1.00 149.56 ? 378 GLN A CD  1 
ATOM   2699 O OE1 . GLN A 1 354 ? 16.052 60.434  40.517 1.00 151.60 ? 378 GLN A OE1 1 
ATOM   2700 N NE2 . GLN A 1 354 ? 13.870 60.009  40.854 1.00 151.21 ? 378 GLN A NE2 1 
ATOM   2701 N N   . SER A 1 355 ? 13.315 59.832  35.281 1.00 90.62  ? 379 SER A N   1 
ATOM   2702 C CA  . SER A 1 355 ? 11.939 59.575  34.847 1.00 91.32  ? 379 SER A CA  1 
ATOM   2703 C C   . SER A 1 355 ? 11.790 59.553  33.327 1.00 94.20  ? 379 SER A C   1 
ATOM   2704 O O   . SER A 1 355 ? 10.803 60.059  32.782 1.00 93.16  ? 379 SER A O   1 
ATOM   2705 C CB  . SER A 1 355 ? 11.013 60.650  35.432 1.00 110.43 ? 379 SER A CB  1 
ATOM   2706 O OG  . SER A 1 355 ? 11.279 61.921  34.860 1.00 110.97 ? 379 SER A OG  1 
ATOM   2707 N N   . ALA A 1 356 ? 12.763 58.952  32.650 1.00 102.39 ? 380 ALA A N   1 
ATOM   2708 C CA  . ALA A 1 356 ? 12.759 58.898  31.190 1.00 106.09 ? 380 ALA A CA  1 
ATOM   2709 C C   . ALA A 1 356 ? 12.370 57.524  30.652 1.00 109.01 ? 380 ALA A C   1 
ATOM   2710 O O   . ALA A 1 356 ? 12.483 56.526  31.368 1.00 111.84 ? 380 ALA A O   1 
ATOM   2711 C CB  . ALA A 1 356 ? 14.149 59.292  30.656 1.00 100.15 ? 380 ALA A CB  1 
ATOM   2712 N N   . PRO A 1 357 ? 11.883 57.457  29.387 1.00 131.66 ? 381 PRO A N   1 
ATOM   2713 C CA  . PRO A 1 357 ? 11.484 56.180  28.755 1.00 131.22 ? 381 PRO A CA  1 
ATOM   2714 C C   . PRO A 1 357 ? 12.699 55.245  28.827 1.00 125.09 ? 381 PRO A C   1 
ATOM   2715 O O   . PRO A 1 357 ? 13.703 55.483  28.143 1.00 142.93 ? 381 PRO A O   1 
ATOM   2716 C CB  . PRO A 1 357 ? 11.160 56.585  27.326 1.00 131.47 ? 381 PRO A CB  1 
ATOM   2717 C CG  . PRO A 1 357 ? 10.761 58.020  27.421 1.00 129.31 ? 381 PRO A CG  1 
ATOM   2718 C CD  . PRO A 1 357 ? 11.647 58.604  28.484 1.00 127.38 ? 381 PRO A CD  1 
ATOM   2719 N N   . PRO A 1 358 ? 12.590 54.140  29.599 1.00 105.53 ? 382 PRO A N   1 
ATOM   2720 C CA  . PRO A 1 358 ? 13.703 53.194  29.775 1.00 102.36 ? 382 PRO A CA  1 
ATOM   2721 C C   . PRO A 1 358 ? 14.408 52.725  28.529 1.00 106.96 ? 382 PRO A C   1 
ATOM   2722 O O   . PRO A 1 358 ? 13.763 52.513  27.510 1.00 107.40 ? 382 PRO A O   1 
ATOM   2723 C CB  . PRO A 1 358 ? 13.082 52.038  30.561 1.00 78.04  ? 382 PRO A CB  1 
ATOM   2724 C CG  . PRO A 1 358 ? 11.822 52.596  31.135 1.00 71.71  ? 382 PRO A CG  1 
ATOM   2725 C CD  . PRO A 1 358 ? 11.328 53.560  30.100 1.00 81.60  ? 382 PRO A CD  1 
ATOM   2726 N N   . ASN A 1 359 ? 15.732 52.571  28.612 1.00 116.98 ? 383 ASN A N   1 
ATOM   2727 C CA  . ASN A 1 359 ? 16.534 52.105  27.476 1.00 124.69 ? 383 ASN A CA  1 
ATOM   2728 C C   . ASN A 1 359 ? 17.663 51.186  27.947 1.00 126.18 ? 383 ASN A C   1 
ATOM   2729 O O   . ASN A 1 359 ? 18.544 51.597  28.714 1.00 128.96 ? 383 ASN A O   1 
ATOM   2730 C CB  . ASN A 1 359 ? 17.081 53.293  26.684 1.00 122.98 ? 383 ASN A CB  1 
ATOM   2731 C CG  . ASN A 1 359 ? 18.066 52.874  25.611 1.00 120.41 ? 383 ASN A CG  1 
ATOM   2732 O OD1 . ASN A 1 359 ? 19.147 52.375  25.916 1.00 119.15 ? 383 ASN A OD1 1 
ATOM   2733 N ND2 . ASN A 1 359 ? 17.701 53.079  24.347 1.00 119.22 ? 383 ASN A ND2 1 
ATOM   2734 N N   . PRO A 1 360 ? 17.655 49.927  27.465 1.00 136.34 ? 384 PRO A N   1 
ATOM   2735 C CA  . PRO A 1 360 ? 18.653 48.912  27.827 1.00 138.29 ? 384 PRO A CA  1 
ATOM   2736 C C   . PRO A 1 360 ? 20.045 49.141  27.259 1.00 142.25 ? 384 PRO A C   1 
ATOM   2737 O O   . PRO A 1 360 ? 21.040 48.699  27.837 1.00 157.49 ? 384 PRO A O   1 
ATOM   2738 C CB  . PRO A 1 360 ? 18.049 47.602  27.298 1.00 112.49 ? 384 PRO A CB  1 
ATOM   2739 C CG  . PRO A 1 360 ? 16.690 47.964  26.736 1.00 104.71 ? 384 PRO A CG  1 
ATOM   2740 C CD  . PRO A 1 360 ? 16.746 49.419  26.420 1.00 110.19 ? 384 PRO A CD  1 
ATOM   2741 N N   . ASN A 1 361 ? 20.100 49.831  26.123 1.00 123.87 ? 385 ASN A N   1 
ATOM   2742 C CA  . ASN A 1 361 ? 21.351 50.108  25.416 1.00 111.22 ? 385 ASN A CA  1 
ATOM   2743 C C   . ASN A 1 361 ? 22.183 51.222  26.059 1.00 102.09 ? 385 ASN A C   1 
ATOM   2744 O O   . ASN A 1 361 ? 23.228 51.611  25.527 1.00 90.60  ? 385 ASN A O   1 
ATOM   2745 C CB  . ASN A 1 361 ? 21.033 50.514  23.963 1.00 133.31 ? 385 ASN A CB  1 
ATOM   2746 C CG  . ASN A 1 361 ? 20.259 49.443  23.195 1.00 147.73 ? 385 ASN A CG  1 
ATOM   2747 O OD1 . ASN A 1 361 ? 19.810 48.443  23.768 1.00 156.02 ? 385 ASN A OD1 1 
ATOM   2748 N ND2 . ASN A 1 361 ? 20.093 49.658  21.887 1.00 155.14 ? 385 ASN A ND2 1 
ATOM   2749 N N   . ARG A 1 362 ? 21.731 51.716  27.209 1.00 100.66 ? 386 ARG A N   1 
ATOM   2750 C CA  . ARG A 1 362 ? 22.368 52.850  27.867 1.00 100.09 ? 386 ARG A CA  1 
ATOM   2751 C C   . ARG A 1 362 ? 22.886 52.535  29.256 1.00 99.35  ? 386 ARG A C   1 
ATOM   2752 O O   . ARG A 1 362 ? 22.143 52.058  30.111 1.00 101.26 ? 386 ARG A O   1 
ATOM   2753 C CB  . ARG A 1 362 ? 21.347 54.005  27.929 1.00 98.14  ? 386 ARG A CB  1 
ATOM   2754 C CG  . ARG A 1 362 ? 21.796 55.269  28.666 1.00 97.31  ? 386 ARG A CG  1 
ATOM   2755 C CD  . ARG A 1 362 ? 20.730 56.366  28.545 1.00 96.30  ? 386 ARG A CD  1 
ATOM   2756 N NE  . ARG A 1 362 ? 19.404 55.911  28.975 1.00 95.76  ? 386 ARG A NE  1 
ATOM   2757 C CZ  . ARG A 1 362 ? 18.247 56.415  28.543 1.00 95.18  ? 386 ARG A CZ  1 
ATOM   2758 N NH1 . ARG A 1 362 ? 18.221 57.400  27.657 1.00 94.57  ? 386 ARG A NH1 1 
ATOM   2759 N NH2 . ARG A 1 362 ? 17.105 55.924  28.999 1.00 95.54  ? 386 ARG A NH2 1 
ATOM   2760 N N   . GLU A 1 363 ? 24.178 52.776  29.463 1.00 98.51  ? 387 GLU A N   1 
ATOM   2761 C CA  . GLU A 1 363 ? 24.805 52.576  30.772 1.00 101.10 ? 387 GLU A CA  1 
ATOM   2762 C C   . GLU A 1 363 ? 25.366 53.912  31.265 1.00 92.14  ? 387 GLU A C   1 
ATOM   2763 O O   . GLU A 1 363 ? 26.156 54.564  30.579 1.00 81.03  ? 387 GLU A O   1 
ATOM   2764 C CB  . GLU A 1 363 ? 25.916 51.517  30.715 1.00 134.76 ? 387 GLU A CB  1 
ATOM   2765 C CG  . GLU A 1 363 ? 25.418 50.068  30.582 1.00 161.94 ? 387 GLU A CG  1 
ATOM   2766 C CD  . GLU A 1 363 ? 24.763 49.526  31.852 1.00 173.10 ? 387 GLU A CD  1 
ATOM   2767 O OE1 . GLU A 1 363 ? 23.678 48.911  31.736 1.00 175.90 ? 387 GLU A OE1 1 
ATOM   2768 O OE2 . GLU A 1 363 ? 25.332 49.705  32.954 1.00 175.53 ? 387 GLU A OE2 1 
ATOM   2769 N N   . VAL A 1 364 ? 24.938 54.310  32.460 1.00 83.31  ? 388 VAL A N   1 
ATOM   2770 C CA  . VAL A 1 364 ? 25.342 55.580  33.047 1.00 83.94  ? 388 VAL A CA  1 
ATOM   2771 C C   . VAL A 1 364 ? 26.429 55.392  34.102 1.00 85.84  ? 388 VAL A C   1 
ATOM   2772 O O   . VAL A 1 364 ? 26.339 54.509  34.956 1.00 87.32  ? 388 VAL A O   1 
ATOM   2773 C CB  . VAL A 1 364 ? 24.103 56.328  33.664 1.00 70.90  ? 388 VAL A CB  1 
ATOM   2774 C CG1 . VAL A 1 364 ? 23.005 56.480  32.612 1.00 63.51  ? 388 VAL A CG1 1 
ATOM   2775 C CG2 . VAL A 1 364 ? 23.552 55.572  34.868 1.00 65.23  ? 388 VAL A CG2 1 
ATOM   2776 N N   . ALA A 1 365 ? 27.477 56.206  34.018 1.00 89.54  ? 389 ALA A N   1 
ATOM   2777 C CA  . ALA A 1 365 ? 28.581 56.127  34.977 1.00 87.49  ? 389 ALA A CA  1 
ATOM   2778 C C   . ALA A 1 365 ? 28.963 57.520  35.454 1.00 85.46  ? 389 ALA A C   1 
ATOM   2779 O O   . ALA A 1 365 ? 30.051 58.011  35.170 1.00 87.07  ? 389 ALA A O   1 
ATOM   2780 C CB  . ALA A 1 365 ? 29.785 55.433  34.347 1.00 59.29  ? 389 ALA A CB  1 
ATOM   2781 N N   . GLY A 1 366 ? 28.051 58.139  36.193 1.00 78.72  ? 390 GLY A N   1 
ATOM   2782 C CA  . GLY A 1 366 ? 28.270 59.484  36.678 1.00 74.71  ? 390 GLY A CA  1 
ATOM   2783 C C   . GLY A 1 366 ? 28.299 60.461  35.520 1.00 73.96  ? 390 GLY A C   1 
ATOM   2784 O O   . GLY A 1 366 ? 27.285 60.678  34.854 1.00 73.47  ? 390 GLY A O   1 
ATOM   2785 N N   . ASP A 1 367 ? 29.476 61.023  35.266 1.00 70.96  ? 391 ASP A N   1 
ATOM   2786 C CA  . ASP A 1 367 ? 29.667 62.010  34.207 1.00 71.05  ? 391 ASP A CA  1 
ATOM   2787 C C   . ASP A 1 367 ? 29.817 61.415  32.811 1.00 70.57  ? 391 ASP A C   1 
ATOM   2788 O O   . ASP A 1 367 ? 30.034 62.143  31.841 1.00 67.67  ? 391 ASP A O   1 
ATOM   2789 C CB  . ASP A 1 367 ? 30.903 62.875  34.521 1.00 80.90  ? 391 ASP A CB  1 
ATOM   2790 C CG  . ASP A 1 367 ? 32.151 62.048  34.814 1.00 87.47  ? 391 ASP A CG  1 
ATOM   2791 O OD1 . ASP A 1 367 ? 32.183 60.853  34.455 1.00 91.32  ? 391 ASP A OD1 1 
ATOM   2792 O OD2 . ASP A 1 367 ? 33.109 62.603  35.396 1.00 90.61  ? 391 ASP A OD2 1 
ATOM   2793 N N   . THR A 1 368 ? 29.672 60.101  32.710 1.00 66.71  ? 392 THR A N   1 
ATOM   2794 C CA  . THR A 1 368 ? 29.872 59.412  31.450 1.00 64.87  ? 392 THR A CA  1 
ATOM   2795 C C   . THR A 1 368 ? 28.724 58.485  31.082 1.00 65.24  ? 392 THR A C   1 
ATOM   2796 O O   . THR A 1 368 ? 28.282 57.670  31.898 1.00 61.84  ? 392 THR A O   1 
ATOM   2797 C CB  . THR A 1 368 ? 31.192 58.578  31.509 1.00 71.38  ? 392 THR A CB  1 
ATOM   2798 O OG1 . THR A 1 368 ? 32.271 59.416  31.955 1.00 73.88  ? 392 THR A OG1 1 
ATOM   2799 C CG2 . THR A 1 368 ? 31.538 58.000  30.143 1.00 74.02  ? 392 THR A CG2 1 
ATOM   2800 N N   . ILE A 1 369 ? 28.227 58.641  29.855 1.00 77.02  ? 393 ILE A N   1 
ATOM   2801 C CA  . ILE A 1 369 ? 27.177 57.777  29.327 1.00 79.62  ? 393 ILE A CA  1 
ATOM   2802 C C   . ILE A 1 369 ? 27.772 56.997  28.153 1.00 80.11  ? 393 ILE A C   1 
ATOM   2803 O O   . ILE A 1 369 ? 28.609 57.513  27.403 1.00 81.87  ? 393 ILE A O   1 
ATOM   2804 C CB  . ILE A 1 369 ? 25.945 58.569  28.793 1.00 80.83  ? 393 ILE A CB  1 
ATOM   2805 C CG1 . ILE A 1 369 ? 25.467 59.592  29.828 1.00 82.14  ? 393 ILE A CG1 1 
ATOM   2806 C CG2 . ILE A 1 369 ? 24.818 57.612  28.414 1.00 79.75  ? 393 ILE A CG2 1 
ATOM   2807 C CD1 . ILE A 1 369 ? 25.013 59.044  31.198 1.00 89.27  ? 393 ILE A CD1 1 
ATOM   2808 N N   . ILE A 1 370 ? 27.339 55.747  28.010 1.00 82.84  ? 394 ILE A N   1 
ATOM   2809 C CA  . ILE A 1 370 ? 27.786 54.902  26.912 1.00 84.05  ? 394 ILE A CA  1 
ATOM   2810 C C   . ILE A 1 370 ? 26.577 54.202  26.287 1.00 81.69  ? 394 ILE A C   1 
ATOM   2811 O O   . ILE A 1 370 ? 25.754 53.604  26.982 1.00 82.55  ? 394 ILE A O   1 
ATOM   2812 C CB  . ILE A 1 370 ? 28.900 53.890  27.390 1.00 96.42  ? 394 ILE A CB  1 
ATOM   2813 C CG1 . ILE A 1 370 ? 29.499 53.151  26.190 1.00 98.80  ? 394 ILE A CG1 1 
ATOM   2814 C CG2 . ILE A 1 370 ? 28.366 52.947  28.467 1.00 99.23  ? 394 ILE A CG2 1 
ATOM   2815 C CD1 . ILE A 1 370 ? 30.799 52.404  26.486 1.00 98.07  ? 394 ILE A CD1 1 
ATOM   2816 N N   . PHE A 1 371 ? 26.460 54.332  24.968 1.00 80.40  ? 395 PHE A N   1 
ATOM   2817 C CA  . PHE A 1 371 ? 25.361 53.729  24.224 1.00 82.46  ? 395 PHE A CA  1 
ATOM   2818 C C   . PHE A 1 371 ? 25.836 52.518  23.413 1.00 81.73  ? 395 PHE A C   1 
ATOM   2819 O O   . PHE A 1 371 ? 26.469 52.669  22.363 1.00 82.38  ? 395 PHE A O   1 
ATOM   2820 C CB  . PHE A 1 371 ? 24.713 54.764  23.288 1.00 84.44  ? 395 PHE A CB  1 
ATOM   2821 C CG  . PHE A 1 371 ? 24.209 55.990  23.996 1.00 87.79  ? 395 PHE A CG  1 
ATOM   2822 C CD1 . PHE A 1 371 ? 25.010 57.121  24.113 1.00 88.81  ? 395 PHE A CD1 1 
ATOM   2823 C CD2 . PHE A 1 371 ? 22.933 56.015  24.547 1.00 88.65  ? 395 PHE A CD2 1 
ATOM   2824 C CE1 . PHE A 1 371 ? 24.548 58.259  24.773 1.00 88.79  ? 395 PHE A CE1 1 
ATOM   2825 C CE2 . PHE A 1 371 ? 22.464 57.148  25.209 1.00 88.24  ? 395 PHE A CE2 1 
ATOM   2826 C CZ  . PHE A 1 371 ? 23.273 58.272  25.318 1.00 88.35  ? 395 PHE A CZ  1 
ATOM   2827 N N   . ARG A 1 372 ? 25.531 51.321  23.917 1.00 85.85  ? 396 ARG A N   1 
ATOM   2828 C CA  . ARG A 1 372 ? 25.897 50.069  23.259 1.00 88.05  ? 396 ARG A CA  1 
ATOM   2829 C C   . ARG A 1 372 ? 24.813 49.637  22.279 1.00 85.93  ? 396 ARG A C   1 
ATOM   2830 O O   . ARG A 1 372 ? 23.626 49.760  22.577 1.00 80.69  ? 396 ARG A O   1 
ATOM   2831 C CB  . ARG A 1 372 ? 26.104 48.955  24.288 1.00 115.32 ? 396 ARG A CB  1 
ATOM   2832 C CG  . ARG A 1 372 ? 27.303 49.141  25.199 1.00 127.55 ? 396 ARG A CG  1 
ATOM   2833 C CD  . ARG A 1 372 ? 27.370 48.019  26.222 1.00 133.72 ? 396 ARG A CD  1 
ATOM   2834 N NE  . ARG A 1 372 ? 26.248 48.066  27.162 1.00 135.87 ? 396 ARG A NE  1 
ATOM   2835 C CZ  . ARG A 1 372 ? 25.778 47.015  27.832 1.00 136.38 ? 396 ARG A CZ  1 
ATOM   2836 N NH1 . ARG A 1 372 ? 26.326 45.813  27.672 1.00 135.94 ? 396 ARG A NH1 1 
ATOM   2837 N NH2 . ARG A 1 372 ? 24.753 47.167  28.662 1.00 136.60 ? 396 ARG A NH2 1 
ATOM   2838 N N   . ASP A 1 373 ? 25.233 49.115  21.123 1.00 88.95  ? 397 ASP A N   1 
ATOM   2839 C CA  . ASP A 1 373 ? 24.324 48.655  20.065 1.00 91.66  ? 397 ASP A CA  1 
ATOM   2840 C C   . ASP A 1 373 ? 23.265 49.720  19.750 1.00 89.70  ? 397 ASP A C   1 
ATOM   2841 O O   . ASP A 1 373 ? 22.059 49.495  19.885 1.00 82.57  ? 397 ASP A O   1 
ATOM   2842 C CB  . ASP A 1 373 ? 23.656 47.326  20.463 1.00 109.16 ? 397 ASP A CB  1 
ATOM   2843 C CG  . ASP A 1 373 ? 23.153 46.531  19.257 1.00 119.79 ? 397 ASP A CG  1 
ATOM   2844 O OD1 . ASP A 1 373 ? 22.712 47.149  18.257 1.00 124.98 ? 397 ASP A OD1 1 
ATOM   2845 O OD2 . ASP A 1 373 ? 23.185 45.280  19.322 1.00 124.98 ? 397 ASP A OD2 1 
ATOM   2846 N N   . THR A 1 374 ? 23.749 50.890  19.332 1.00 84.25  ? 398 THR A N   1 
ATOM   2847 C CA  . THR A 1 374 ? 22.892 52.029  18.992 1.00 84.04  ? 398 THR A CA  1 
ATOM   2848 C C   . THR A 1 374 ? 21.997 51.635  17.828 1.00 86.64  ? 398 THR A C   1 
ATOM   2849 O O   . THR A 1 374 ? 22.473 51.309  16.741 1.00 88.31  ? 398 THR A O   1 
ATOM   2850 C CB  . THR A 1 374 ? 23.750 53.266  18.641 1.00 87.14  ? 398 THR A CB  1 
ATOM   2851 O OG1 . THR A 1 374 ? 24.684 53.505  19.702 1.00 87.00  ? 398 THR A OG1 1 
ATOM   2852 C CG2 . THR A 1 374 ? 22.874 54.497  18.473 1.00 85.93  ? 398 THR A CG2 1 
ATOM   2853 N N   . GLN A 1 375 ? 20.693 51.687  18.054 1.00 92.11  ? 399 GLN A N   1 
ATOM   2854 C CA  . GLN A 1 375 ? 19.758 51.247  17.042 1.00 95.85  ? 399 GLN A CA  1 
ATOM   2855 C C   . GLN A 1 375 ? 18.815 52.318  16.562 1.00 97.12  ? 399 GLN A C   1 
ATOM   2856 O O   . GLN A 1 375 ? 18.806 53.430  17.060 1.00 88.89  ? 399 GLN A O   1 
ATOM   2857 C CB  . GLN A 1 375 ? 18.955 50.064  17.578 1.00 126.97 ? 399 GLN A CB  1 
ATOM   2858 C CG  . GLN A 1 375 ? 18.732 48.943  16.572 1.00 140.11 ? 399 GLN A CG  1 
ATOM   2859 C CD  . GLN A 1 375 ? 20.001 48.492  15.880 1.00 145.98 ? 399 GLN A CD  1 
ATOM   2860 O OE1 . GLN A 1 375 ? 20.063 48.476  14.660 1.00 147.85 ? 399 GLN A OE1 1 
ATOM   2861 N NE2 . GLN A 1 375 ? 21.011 48.114  16.653 1.00 146.96 ? 399 GLN A NE2 1 
ATOM   2862 N N   . ILE A 1 376 ? 18.020 51.952  15.573 1.00 102.01 ? 400 ILE A N   1 
ATOM   2863 C CA  . ILE A 1 376 ? 17.042 52.834  14.974 1.00 116.62 ? 400 ILE A CA  1 
ATOM   2864 C C   . ILE A 1 376 ? 16.347 53.746  15.933 1.00 117.40 ? 400 ILE A C   1 
ATOM   2865 O O   . ILE A 1 376 ? 16.137 54.908  15.653 1.00 118.16 ? 400 ILE A O   1 
ATOM   2866 C CB  . ILE A 1 376 ? 15.877 52.040  14.431 1.00 133.41 ? 400 ILE A CB  1 
ATOM   2867 C CG1 . ILE A 1 376 ? 16.389 50.752  13.760 1.00 141.29 ? 400 ILE A CG1 1 
ATOM   2868 C CG2 . ILE A 1 376 ? 15.050 52.910  13.499 1.00 140.65 ? 400 ILE A CG2 1 
ATOM   2869 C CD1 . ILE A 1 376 ? 15.563 50.330  12.544 1.00 144.62 ? 400 ILE A CD1 1 
ATOM   2870 N N   . SER A 1 377 ? 15.945 53.186  17.058 1.00 137.66 ? 401 SER A N   1 
ATOM   2871 C CA  . SER A 1 377 ? 15.245 53.959  18.061 1.00 135.37 ? 401 SER A CA  1 
ATOM   2872 C C   . SER A 1 377 ? 16.319 54.832  18.611 1.00 127.24 ? 401 SER A C   1 
ATOM   2873 O O   . SER A 1 377 ? 17.290 55.124  17.949 1.00 135.80 ? 401 SER A O   1 
ATOM   2874 C CB  . SER A 1 377 ? 14.821 53.032  19.178 1.00 123.91 ? 401 SER A CB  1 
ATOM   2875 O OG  . SER A 1 377 ? 14.581 51.758  18.637 1.00 122.38 ? 401 SER A OG  1 
ATOM   2876 N N   . SER A 1 378 ? 16.123 55.250  19.846 1.00 90.44  ? 402 SER A N   1 
ATOM   2877 C CA  . SER A 1 378 ? 17.195 55.889  20.568 1.00 82.26  ? 402 SER A CA  1 
ATOM   2878 C C   . SER A 1 378 ? 17.704 57.200  20.052 1.00 78.40  ? 402 SER A C   1 
ATOM   2879 O O   . SER A 1 378 ? 18.720 57.675  20.520 1.00 61.44  ? 402 SER A O   1 
ATOM   2880 C CB  . SER A 1 378 ? 18.367 54.915  20.660 1.00 96.80  ? 402 SER A CB  1 
ATOM   2881 O OG  . SER A 1 378 ? 19.378 55.454  21.482 1.00 103.94 ? 402 SER A OG  1 
ATOM   2882 N N   . ARG A 1 379 ? 17.020 57.797  19.090 1.00 107.71 ? 403 ARG A N   1 
ATOM   2883 C CA  . ARG A 1 379 ? 17.441 59.113  18.632 1.00 119.89 ? 403 ARG A CA  1 
ATOM   2884 C C   . ARG A 1 379 ? 16.799 60.170  19.506 1.00 120.72 ? 403 ARG A C   1 
ATOM   2885 O O   . ARG A 1 379 ? 15.595 60.351  19.484 1.00 133.89 ? 403 ARG A O   1 
ATOM   2886 C CB  . ARG A 1 379 ? 17.038 59.344  17.188 1.00 124.52 ? 403 ARG A CB  1 
ATOM   2887 C CG  . ARG A 1 379 ? 16.983 58.079  16.402 1.00 119.58 ? 403 ARG A CG  1 
ATOM   2888 C CD  . ARG A 1 379 ? 16.210 58.273  15.144 1.00 117.09 ? 403 ARG A CD  1 
ATOM   2889 N NE  . ARG A 1 379 ? 17.069 58.763  14.084 1.00 117.29 ? 403 ARG A NE  1 
ATOM   2890 C CZ  . ARG A 1 379 ? 17.151 58.200  12.889 1.00 118.24 ? 403 ARG A CZ  1 
ATOM   2891 N NH1 . ARG A 1 379 ? 16.424 57.132  12.606 1.00 117.94 ? 403 ARG A NH1 1 
ATOM   2892 N NH2 . ARG A 1 379 ? 17.967 58.703  11.982 1.00 118.29 ? 403 ARG A NH2 1 
ATOM   2893 N N   . ALA A 1 380 ? 17.624 60.866  20.275 1.00 95.66  ? 404 ALA A N   1 
ATOM   2894 C CA  . ALA A 1 380 ? 17.159 61.908  21.184 1.00 80.53  ? 404 ALA A CA  1 
ATOM   2895 C C   . ALA A 1 380 ? 18.190 63.031  21.310 1.00 71.85  ? 404 ALA A C   1 
ATOM   2896 O O   . ALA A 1 380 ? 19.223 62.999  20.639 1.00 62.63  ? 404 ALA A O   1 
ATOM   2897 C CB  . ALA A 1 380 ? 16.855 61.300  22.549 1.00 100.60 ? 404 ALA A CB  1 
ATOM   2898 N N   . VAL A 1 381 ? 17.910 64.020  22.161 1.00 68.40  ? 405 VAL A N   1 
ATOM   2899 C CA  . VAL A 1 381 ? 18.805 65.170  22.333 1.00 67.75  ? 405 VAL A CA  1 
ATOM   2900 C C   . VAL A 1 381 ? 19.159 65.370  23.805 1.00 69.93  ? 405 VAL A C   1 
ATOM   2901 O O   . VAL A 1 381 ? 18.559 66.193  24.497 1.00 74.00  ? 405 VAL A O   1 
ATOM   2902 C CB  . VAL A 1 381 ? 18.156 66.470  21.777 1.00 58.22  ? 405 VAL A CB  1 
ATOM   2903 C CG1 . VAL A 1 381 ? 19.231 67.515  21.524 1.00 55.39  ? 405 VAL A CG1 1 
ATOM   2904 C CG2 . VAL A 1 381 ? 17.389 66.187  20.492 1.00 54.80  ? 405 VAL A CG2 1 
ATOM   2905 N N   . TYR A 1 382 ? 20.155 64.617  24.263 1.00 66.90  ? 406 TYR A N   1 
ATOM   2906 C CA  . TYR A 1 382 ? 20.584 64.633  25.658 1.00 64.31  ? 406 TYR A CA  1 
ATOM   2907 C C   . TYR A 1 382 ? 21.122 65.970  26.152 1.00 62.96  ? 406 TYR A C   1 
ATOM   2908 O O   . TYR A 1 382 ? 21.645 66.773  25.367 1.00 64.10  ? 406 TYR A O   1 
ATOM   2909 C CB  . TYR A 1 382 ? 21.611 63.521  25.893 1.00 59.71  ? 406 TYR A CB  1 
ATOM   2910 C CG  . TYR A 1 382 ? 21.027 62.137  25.767 1.00 55.96  ? 406 TYR A CG  1 
ATOM   2911 C CD1 . TYR A 1 382 ? 20.737 61.592  24.518 1.00 55.07  ? 406 TYR A CD1 1 
ATOM   2912 C CD2 . TYR A 1 382 ? 20.747 61.377  26.900 1.00 55.05  ? 406 TYR A CD2 1 
ATOM   2913 C CE1 . TYR A 1 382 ? 20.183 60.325  24.397 1.00 54.96  ? 406 TYR A CE1 1 
ATOM   2914 C CE2 . TYR A 1 382 ? 20.194 60.112  26.796 1.00 54.34  ? 406 TYR A CE2 1 
ATOM   2915 C CZ  . TYR A 1 382 ? 19.914 59.590  25.540 1.00 56.09  ? 406 TYR A CZ  1 
ATOM   2916 O OH  . TYR A 1 382 ? 19.366 58.329  25.425 1.00 57.60  ? 406 TYR A OH  1 
ATOM   2917 N N   . GLN A 1 383 ? 20.973 66.203  27.457 1.00 57.86  ? 407 GLN A N   1 
ATOM   2918 C CA  . GLN A 1 383 ? 21.426 67.438  28.098 1.00 55.00  ? 407 GLN A CA  1 
ATOM   2919 C C   . GLN A 1 383 ? 22.431 67.181  29.201 1.00 54.20  ? 407 GLN A C   1 
ATOM   2920 O O   . GLN A 1 383 ? 22.429 66.125  29.820 1.00 51.95  ? 407 GLN A O   1 
ATOM   2921 C CB  . GLN A 1 383 ? 20.247 68.184  28.744 1.00 57.32  ? 407 GLN A CB  1 
ATOM   2922 C CG  . GLN A 1 383 ? 19.485 69.111  27.834 1.00 59.47  ? 407 GLN A CG  1 
ATOM   2923 C CD  . GLN A 1 383 ? 18.530 68.383  26.920 1.00 61.31  ? 407 GLN A CD  1 
ATOM   2924 O OE1 . GLN A 1 383 ? 18.264 68.840  25.804 1.00 61.76  ? 407 GLN A OE1 1 
ATOM   2925 N NE2 . GLN A 1 383 ? 17.997 67.249  27.385 1.00 59.89  ? 407 GLN A NE2 1 
ATOM   2926 N N   . CYS A 1 384 ? 23.297 68.155  29.431 1.00 57.99  ? 408 CYS A N   1 
ATOM   2927 C CA  . CYS A 1 384 ? 24.206 68.066  30.539 1.00 60.36  ? 408 CYS A CA  1 
ATOM   2928 C C   . CYS A 1 384 ? 24.253 69.365  31.332 1.00 58.14  ? 408 CYS A C   1 
ATOM   2929 O O   . CYS A 1 384 ? 24.554 70.432  30.786 1.00 54.55  ? 408 CYS A O   1 
ATOM   2930 C CB  . CYS A 1 384 ? 25.630 67.714  30.106 1.00 71.25  ? 408 CYS A CB  1 
ATOM   2931 S SG  . CYS A 1 384 ? 26.564 67.189  31.560 1.00 83.69  ? 408 CYS A SG  1 
ATOM   2932 N N   . ASN A 1 385 ? 23.920 69.268  32.617 1.00 58.03  ? 409 ASN A N   1 
ATOM   2933 C CA  . ASN A 1 385 ? 24.078 70.396  33.512 1.00 57.95  ? 409 ASN A CA  1 
ATOM   2934 C C   . ASN A 1 385 ? 25.223 70.068  34.488 1.00 57.29  ? 409 ASN A C   1 
ATOM   2935 O O   . ASN A 1 385 ? 25.110 69.153  35.300 1.00 60.56  ? 409 ASN A O   1 
ATOM   2936 C CB  . ASN A 1 385 ? 22.780 70.688  34.295 1.00 52.58  ? 409 ASN A CB  1 
ATOM   2937 C CG  . ASN A 1 385 ? 22.863 71.972  35.135 1.00 54.22  ? 409 ASN A CG  1 
ATOM   2938 O OD1 . ASN A 1 385 ? 23.863 72.700  35.073 1.00 53.31  ? 409 ASN A OD1 1 
ATOM   2939 N ND2 . ASN A 1 385 ? 21.817 72.253  35.923 1.00 55.81  ? 409 ASN A ND2 1 
ATOM   2940 N N   . THR A 1 386 ? 26.351 70.759  34.348 1.00 56.19  ? 410 THR A N   1 
ATOM   2941 C CA  . THR A 1 386 ? 27.434 70.623  35.331 1.00 55.19  ? 410 THR A CA  1 
ATOM   2942 C C   . THR A 1 386 ? 27.459 71.935  36.092 1.00 52.66  ? 410 THR A C   1 
ATOM   2943 O O   . THR A 1 386 ? 27.674 73.007  35.522 1.00 51.85  ? 410 THR A O   1 
ATOM   2944 C CB  . THR A 1 386 ? 28.824 70.337  34.753 1.00 48.51  ? 410 THR A CB  1 
ATOM   2945 O OG1 . THR A 1 386 ? 29.005 71.033  33.513 1.00 51.64  ? 410 THR A OG1 1 
ATOM   2946 C CG2 . THR A 1 386 ? 28.989 68.865  34.556 1.00 51.68  ? 410 THR A CG2 1 
ATOM   2947 N N   . SER A 1 387 ? 27.290 71.823  37.401 1.00 52.89  ? 411 SER A N   1 
ATOM   2948 C CA  . SER A 1 387 ? 27.116 72.993  38.234 1.00 54.20  ? 411 SER A CA  1 
ATOM   2949 C C   . SER A 1 387 ? 27.758 72.905  39.587 1.00 56.07  ? 411 SER A C   1 
ATOM   2950 O O   . SER A 1 387 ? 28.072 71.824  40.090 1.00 58.96  ? 411 SER A O   1 
ATOM   2951 C CB  . SER A 1 387 ? 25.599 73.177  38.462 1.00 45.57  ? 411 SER A CB  1 
ATOM   2952 O OG  . SER A 1 387 ? 25.001 71.964  38.942 1.00 41.67  ? 411 SER A OG  1 
ATOM   2953 N N   . ASN A 1 388 ? 27.974 74.080  40.149 1.00 53.84  ? 412 ASN A N   1 
ATOM   2954 C CA  . ASN A 1 388 ? 28.403 74.200  41.516 1.00 54.24  ? 412 ASN A CA  1 
ATOM   2955 C C   . ASN A 1 388 ? 27.857 75.523  42.043 1.00 56.24  ? 412 ASN A C   1 
ATOM   2956 O O   . ASN A 1 388 ? 27.222 76.291  41.310 1.00 53.92  ? 412 ASN A O   1 
ATOM   2957 C CB  . ASN A 1 388 ? 29.914 74.118  41.676 1.00 55.80  ? 412 ASN A CB  1 
ATOM   2958 C CG  . ASN A 1 388 ? 30.654 75.240  40.982 1.00 54.78  ? 412 ASN A CG  1 
ATOM   2959 O OD1 . ASN A 1 388 ? 31.870 75.175  40.833 1.00 57.30  ? 412 ASN A OD1 1 
ATOM   2960 N ND2 . ASN A 1 388 ? 29.943 76.268  40.560 1.00 55.94  ? 412 ASN A ND2 1 
ATOM   2961 N N   . GLU A 1 389 ? 28.109 75.770  43.321 1.00 64.27  ? 413 GLU A N   1 
ATOM   2962 C CA  . GLU A 1 389 ? 27.679 76.969  44.014 1.00 69.03  ? 413 GLU A CA  1 
ATOM   2963 C C   . GLU A 1 389 ? 27.751 78.229  43.163 1.00 66.23  ? 413 GLU A C   1 
ATOM   2964 O O   . GLU A 1 389 ? 26.877 79.080  43.240 1.00 66.41  ? 413 GLU A O   1 
ATOM   2965 C CB  . GLU A 1 389 ? 28.594 77.156  45.231 1.00 81.74  ? 413 GLU A CB  1 
ATOM   2966 C CG  . GLU A 1 389 ? 28.008 77.936  46.384 1.00 95.25  ? 413 GLU A CG  1 
ATOM   2967 C CD  . GLU A 1 389 ? 28.957 77.994  47.575 1.00 100.51 ? 413 GLU A CD  1 
ATOM   2968 O OE1 . GLU A 1 389 ? 28.639 78.715  48.554 1.00 102.33 ? 413 GLU A OE1 1 
ATOM   2969 O OE2 . GLU A 1 389 ? 30.014 77.315  47.522 1.00 101.83 ? 413 GLU A OE2 1 
ATOM   2970 N N   . HIS A 1 390 ? 28.778 78.307  42.321 1.00 57.19  ? 414 HIS A N   1 
ATOM   2971 C CA  . HIS A 1 390 ? 29.103 79.524  41.574 1.00 50.84  ? 414 HIS A CA  1 
ATOM   2972 C C   . HIS A 1 390 ? 28.664 79.647  40.126 1.00 47.92  ? 414 HIS A C   1 
ATOM   2973 O O   . HIS A 1 390 ? 28.888 80.683  39.502 1.00 46.04  ? 414 HIS A O   1 
ATOM   2974 C CB  . HIS A 1 390 ? 30.627 79.733  41.653 1.00 50.77  ? 414 HIS A CB  1 
ATOM   2975 C CG  . HIS A 1 390 ? 31.159 79.824  43.051 1.00 53.55  ? 414 HIS A CG  1 
ATOM   2976 N ND1 . HIS A 1 390 ? 31.960 78.849  43.611 1.00 54.03  ? 414 HIS A ND1 1 
ATOM   2977 C CD2 . HIS A 1 390 ? 31.005 80.778  44.000 1.00 53.81  ? 414 HIS A CD2 1 
ATOM   2978 C CE1 . HIS A 1 390 ? 32.277 79.200  44.845 1.00 53.32  ? 414 HIS A CE1 1 
ATOM   2979 N NE2 . HIS A 1 390 ? 31.710 80.365  45.104 1.00 54.54  ? 414 HIS A NE2 1 
ATOM   2980 N N   . GLY A 1 391 ? 28.053 78.599  39.588 1.00 43.41  ? 415 GLY A N   1 
ATOM   2981 C CA  . GLY A 1 391 ? 27.621 78.628  38.199 1.00 41.14  ? 415 GLY A CA  1 
ATOM   2982 C C   . GLY A 1 391 ? 27.366 77.250  37.608 1.00 43.95  ? 415 GLY A C   1 
ATOM   2983 O O   . GLY A 1 391 ? 27.546 76.232  38.278 1.00 44.18  ? 415 GLY A O   1 
ATOM   2984 N N   . TYR A 1 392 ? 26.928 77.212  36.357 1.00 47.79  ? 416 TYR A N   1 
ATOM   2985 C CA  . TYR A 1 392 ? 26.673 75.943  35.690 1.00 49.32  ? 416 TYR A CA  1 
ATOM   2986 C C   . TYR A 1 392 ? 27.017 76.022  34.202 1.00 50.32  ? 416 TYR A C   1 
ATOM   2987 O O   . TYR A 1 392 ? 27.334 77.100  33.696 1.00 51.16  ? 416 TYR A O   1 
ATOM   2988 C CB  . TYR A 1 392 ? 25.190 75.548  35.847 1.00 54.36  ? 416 TYR A CB  1 
ATOM   2989 C CG  . TYR A 1 392 ? 24.208 76.421  35.082 1.00 59.25  ? 416 TYR A CG  1 
ATOM   2990 C CD1 . TYR A 1 392 ? 23.774 76.061  33.798 1.00 60.25  ? 416 TYR A CD1 1 
ATOM   2991 C CD2 . TYR A 1 392 ? 23.719 77.606  35.634 1.00 58.53  ? 416 TYR A CD2 1 
ATOM   2992 C CE1 . TYR A 1 392 ? 22.885 76.853  33.094 1.00 61.34  ? 416 TYR A CE1 1 
ATOM   2993 C CE2 . TYR A 1 392 ? 22.829 78.407  34.933 1.00 60.01  ? 416 TYR A CE2 1 
ATOM   2994 C CZ  . TYR A 1 392 ? 22.415 78.023  33.664 1.00 61.41  ? 416 TYR A CZ  1 
ATOM   2995 O OH  . TYR A 1 392 ? 21.523 78.799  32.964 1.00 61.06  ? 416 TYR A OH  1 
ATOM   2996 N N   . LEU A 1 393 ? 26.998 74.869  33.530 1.00 49.65  ? 417 LEU A N   1 
ATOM   2997 C CA  . LEU A 1 393 ? 27.176 74.796  32.082 1.00 48.62  ? 417 LEU A CA  1 
ATOM   2998 C C   . LEU A 1 393 ? 26.145 73.822  31.531 1.00 49.26  ? 417 LEU A C   1 
ATOM   2999 O O   . LEU A 1 393 ? 25.970 72.721  32.078 1.00 51.70  ? 417 LEU A O   1 
ATOM   3000 C CB  . LEU A 1 393 ? 28.561 74.318  31.674 1.00 43.42  ? 417 LEU A CB  1 
ATOM   3001 C CG  . LEU A 1 393 ? 29.743 75.271  31.851 1.00 44.54  ? 417 LEU A CG  1 
ATOM   3002 C CD1 . LEU A 1 393 ? 31.031 74.488  31.682 1.00 41.78  ? 417 LEU A CD1 1 
ATOM   3003 C CD2 . LEU A 1 393 ? 29.666 76.456  30.879 1.00 43.54  ? 417 LEU A CD2 1 
ATOM   3004 N N   . LEU A 1 394 ? 25.477 74.224  30.447 1.00 46.65  ? 418 LEU A N   1 
ATOM   3005 C CA  . LEU A 1 394 ? 24.444 73.397  29.826 1.00 48.38  ? 418 LEU A CA  1 
ATOM   3006 C C   . LEU A 1 394 ? 24.818 73.027  28.405 1.00 49.03  ? 418 LEU A C   1 
ATOM   3007 O O   . LEU A 1 394 ? 24.922 73.885  27.523 1.00 48.00  ? 418 LEU A O   1 
ATOM   3008 C CB  . LEU A 1 394 ? 23.099 74.142  29.844 1.00 52.56  ? 418 LEU A CB  1 
ATOM   3009 C CG  . LEU A 1 394 ? 21.725 73.468  29.607 1.00 53.04  ? 418 LEU A CG  1 
ATOM   3010 C CD1 . LEU A 1 394 ? 21.383 73.414  28.137 1.00 54.90  ? 418 LEU A CD1 1 
ATOM   3011 C CD2 . LEU A 1 394 ? 21.658 72.092  30.238 1.00 54.16  ? 418 LEU A CD2 1 
ATOM   3012 N N   . ALA A 1 395 ? 25.026 71.738  28.186 1.00 52.60  ? 419 ALA A N   1 
ATOM   3013 C CA  . ALA A 1 395 ? 25.377 71.269  26.859 1.00 57.21  ? 419 ALA A CA  1 
ATOM   3014 C C   . ALA A 1 395 ? 24.289 70.412  26.242 1.00 58.32  ? 419 ALA A C   1 
ATOM   3015 O O   . ALA A 1 395 ? 23.693 69.567  26.914 1.00 57.73  ? 419 ALA A O   1 
ATOM   3016 C CB  . ALA A 1 395 ? 26.689 70.469  26.905 1.00 57.04  ? 419 ALA A CB  1 
ATOM   3017 N N   . ASN A 1 396 ? 24.019 70.670  24.963 1.00 67.23  ? 420 ASN A N   1 
ATOM   3018 C CA  . ASN A 1 396 ? 23.079 69.857  24.199 1.00 67.12  ? 420 ASN A CA  1 
ATOM   3019 C C   . ASN A 1 396 ? 23.891 68.985  23.256 1.00 66.50  ? 420 ASN A C   1 
ATOM   3020 O O   . ASN A 1 396 ? 24.846 69.456  22.632 1.00 67.88  ? 420 ASN A O   1 
ATOM   3021 C CB  . ASN A 1 396 ? 22.135 70.722  23.376 1.00 62.09  ? 420 ASN A CB  1 
ATOM   3022 C CG  . ASN A 1 396 ? 21.036 71.324  24.207 1.00 61.65  ? 420 ASN A CG  1 
ATOM   3023 O OD1 . ASN A 1 396 ? 20.022 70.677  24.481 1.00 59.97  ? 420 ASN A OD1 1 
ATOM   3024 N ND2 . ASN A 1 396 ? 21.230 72.575  24.625 1.00 60.39  ? 420 ASN A ND2 1 
ATOM   3025 N N   . ALA A 1 397 ? 23.518 67.712  23.176 1.00 60.55  ? 421 ALA A N   1 
ATOM   3026 C CA  . ALA A 1 397 ? 24.168 66.777  22.264 1.00 59.57  ? 421 ALA A CA  1 
ATOM   3027 C C   . ALA A 1 397 ? 23.193 65.674  21.855 1.00 61.81  ? 421 ALA A C   1 
ATOM   3028 O O   . ALA A 1 397 ? 22.665 64.963  22.719 1.00 63.22  ? 421 ALA A O   1 
ATOM   3029 C CB  . ALA A 1 397 ? 25.402 66.179  22.904 1.00 46.83  ? 421 ALA A CB  1 
ATOM   3030 N N   . PHE A 1 398 ? 22.950 65.535  20.546 1.00 64.48  ? 422 PHE A N   1 
ATOM   3031 C CA  . PHE A 1 398 ? 22.028 64.504  20.048 1.00 69.63  ? 422 PHE A CA  1 
ATOM   3032 C C   . PHE A 1 398 ? 22.713 63.189  19.709 1.00 70.48  ? 422 PHE A C   1 
ATOM   3033 O O   . PHE A 1 398 ? 23.931 63.136  19.615 1.00 67.66  ? 422 PHE A O   1 
ATOM   3034 C CB  . PHE A 1 398 ? 21.184 65.016  18.859 1.00 80.92  ? 422 PHE A CB  1 
ATOM   3035 C CG  . PHE A 1 398 ? 21.983 65.444  17.654 1.00 89.16  ? 422 PHE A CG  1 
ATOM   3036 C CD1 . PHE A 1 398 ? 22.533 64.502  16.785 1.00 92.24  ? 422 PHE A CD1 1 
ATOM   3037 C CD2 . PHE A 1 398 ? 22.156 66.801  17.370 1.00 92.73  ? 422 PHE A CD2 1 
ATOM   3038 C CE1 . PHE A 1 398 ? 23.259 64.906  15.652 1.00 93.22  ? 422 PHE A CE1 1 
ATOM   3039 C CE2 . PHE A 1 398 ? 22.878 67.215  16.244 1.00 93.99  ? 422 PHE A CE2 1 
ATOM   3040 C CZ  . PHE A 1 398 ? 23.427 66.262  15.379 1.00 93.95  ? 422 PHE A CZ  1 
ATOM   3041 N N   . VAL A 1 399 ? 21.917 62.131  19.552 1.00 78.16  ? 423 VAL A N   1 
ATOM   3042 C CA  . VAL A 1 399 ? 22.428 60.780  19.284 1.00 80.04  ? 423 VAL A CA  1 
ATOM   3043 C C   . VAL A 1 399 ? 21.692 60.159  18.095 1.00 84.84  ? 423 VAL A C   1 
ATOM   3044 O O   . VAL A 1 399 ? 20.867 59.254  18.242 1.00 89.65  ? 423 VAL A O   1 
ATOM   3045 C CB  . VAL A 1 399 ? 22.278 59.858  20.559 1.00 68.19  ? 423 VAL A CB  1 
ATOM   3046 C CG1 . VAL A 1 399 ? 22.896 58.489  20.311 1.00 60.51  ? 423 VAL A CG1 1 
ATOM   3047 C CG2 . VAL A 1 399 ? 22.949 60.506  21.757 1.00 60.66  ? 423 VAL A CG2 1 
ATOM   3048 N N   . SER A 1 400 ? 22.010 60.661  16.909 1.00 85.72  ? 424 SER A N   1 
ATOM   3049 C CA  . SER A 1 400 ? 21.384 60.188  15.680 1.00 86.27  ? 424 SER A CA  1 
ATOM   3050 C C   . SER A 1 400 ? 22.037 58.936  15.096 1.00 86.47  ? 424 SER A C   1 
ATOM   3051 O O   . SER A 1 400 ? 23.263 58.807  15.100 1.00 85.75  ? 424 SER A O   1 
ATOM   3052 C CB  . SER A 1 400 ? 21.407 61.303  14.625 1.00 84.18  ? 424 SER A CB  1 
ATOM   3053 O OG  . SER A 1 400 ? 22.726 61.792  14.446 1.00 86.94  ? 424 SER A OG  1 
ATOM   3054 N N   . VAL A 1 401 ? 21.198 58.009  14.624 1.00 86.71  ? 425 VAL A N   1 
ATOM   3055 C CA  . VAL A 1 401 ? 21.658 56.792  13.949 1.00 87.53  ? 425 VAL A CA  1 
ATOM   3056 C C   . VAL A 1 401 ? 21.653 57.027  12.429 1.00 86.33  ? 425 VAL A C   1 
ATOM   3057 O O   . VAL A 1 401 ? 20.794 57.742  11.900 1.00 83.76  ? 425 VAL A O   1 
ATOM   3058 C CB  . VAL A 1 401 ? 20.773 55.562  14.331 1.00 101.48 ? 425 VAL A CB  1 
ATOM   3059 C CG1 . VAL A 1 401 ? 20.070 54.958  13.113 1.00 106.63 ? 425 VAL A CG1 1 
ATOM   3060 C CG2 . VAL A 1 401 ? 21.636 54.520  15.040 1.00 106.62 ? 425 VAL A CG2 1 
ATOM   3061 N N   . LEU A 1 402 ? 22.627 56.436  11.740 1.00 96.82  ? 426 LEU A N   1 
ATOM   3062 C CA  . LEU A 1 402 ? 22.769 56.593  10.289 1.00 99.45  ? 426 LEU A CA  1 
ATOM   3063 C C   . LEU A 1 402 ? 22.078 55.449  9.538  1.00 101.66 ? 426 LEU A C   1 
ATOM   3064 O O   . LEU A 1 402 ? 21.154 54.859  10.132 1.00 104.66 ? 426 LEU A O   1 
ATOM   3065 C CB  . LEU A 1 402 ? 24.258 56.666  9.913  1.00 87.48  ? 426 LEU A CB  1 
ATOM   3066 C CG  . LEU A 1 402 ? 24.676 57.790  8.945  1.00 86.14  ? 426 LEU A CG  1 
ATOM   3067 C CD1 . LEU A 1 402 ? 26.172 58.049  9.076  1.00 83.94  ? 426 LEU A CD1 1 
ATOM   3068 C CD2 . LEU A 1 402 ? 24.284 57.478  7.487  1.00 85.78  ? 426 LEU A CD2 1 
HETATM 3069 C C1  . NAG B 2 .   ? 21.718 73.403  36.508 1.00 62.03  ? 1   NAG A C1  1 
HETATM 3070 C C2  . NAG B 2 .   ? 20.593 74.400  36.193 1.00 64.13  ? 1   NAG A C2  1 
HETATM 3071 C C3  . NAG B 2 .   ? 20.681 75.574  37.169 1.00 67.57  ? 1   NAG A C3  1 
HETATM 3072 C C4  . NAG B 2 .   ? 20.577 75.039  38.592 1.00 68.91  ? 1   NAG A C4  1 
HETATM 3073 C C5  . NAG B 2 .   ? 21.710 74.035  38.827 1.00 67.89  ? 1   NAG A C5  1 
HETATM 3074 C C6  . NAG B 2 .   ? 21.631 73.401  40.197 1.00 68.89  ? 1   NAG A C6  1 
HETATM 3075 C C7  . NAG B 2 .   ? 19.869 74.393  33.903 1.00 63.01  ? 1   NAG A C7  1 
HETATM 3076 C C8  . NAG B 2 .   ? 19.703 75.220  32.641 1.00 60.87  ? 1   NAG A C8  1 
HETATM 3077 N N2  . NAG B 2 .   ? 20.697 74.871  34.826 1.00 63.93  ? 1   NAG A N2  1 
HETATM 3078 O O3  . NAG B 2 .   ? 19.632 76.504  36.927 1.00 68.13  ? 1   NAG A O3  1 
HETATM 3079 O O4  . NAG B 2 .   ? 20.648 76.106  39.525 1.00 69.30  ? 1   NAG A O4  1 
HETATM 3080 O O5  . NAG B 2 .   ? 21.613 72.955  37.866 1.00 65.21  ? 1   NAG A O5  1 
HETATM 3081 O O6  . NAG B 2 .   ? 20.708 72.318  40.195 1.00 67.67  ? 1   NAG A O6  1 
HETATM 3082 O O7  . NAG B 2 .   ? 19.242 73.334  34.036 1.00 62.95  ? 1   NAG A O7  1 
HETATM 3083 O O   . HOH C 3 .   ? 34.126 80.209  50.293 1.00 39.32  ? 2   HOH A O   1 
HETATM 3084 O O   . HOH C 3 .   ? 49.364 106.774 68.604 1.00 60.66  ? 3   HOH A O   1 
HETATM 3085 O O   . HOH C 3 .   ? 27.976 101.455 29.000 1.00 71.21  ? 4   HOH A O   1 
HETATM 3086 O O   . HOH C 3 .   ? 37.052 90.614  55.552 1.00 43.87  ? 5   HOH A O   1 
HETATM 3087 O O   . HOH C 3 .   ? 36.108 63.589  19.740 1.00 60.23  ? 6   HOH A O   1 
HETATM 3088 O O   . HOH C 3 .   ? 35.805 99.248  49.154 1.00 54.53  ? 7   HOH A O   1 
HETATM 3089 O O   . HOH C 3 .   ? -8.178 78.781  28.816 1.00 83.72  ? 8   HOH A O   1 
HETATM 3090 O O   . HOH C 3 .   ? 32.610 64.533  24.646 1.00 59.23  ? 9   HOH A O   1 
HETATM 3091 O O   . HOH C 3 .   ? 53.196 104.391 48.667 1.00 57.64  ? 10  HOH A O   1 
HETATM 3092 O O   . HOH C 3 .   ? 29.492 92.924  54.975 1.00 85.64  ? 11  HOH A O   1 
HETATM 3093 O O   . HOH C 3 .   ? 21.214 70.472  19.911 1.00 62.92  ? 12  HOH A O   1 
HETATM 3094 O O   . HOH C 3 .   ? 41.079 82.829  32.302 1.00 54.97  ? 13  HOH A O   1 
HETATM 3095 O O   . HOH C 3 .   ? 39.556 118.244 48.748 1.00 64.25  ? 14  HOH A O   1 
HETATM 3096 O O   . HOH C 3 .   ? 30.018 76.349  26.933 1.00 78.74  ? 15  HOH A O   1 
HETATM 3097 O O   . HOH C 3 .   ? 38.396 91.816  44.809 1.00 54.07  ? 16  HOH A O   1 
HETATM 3098 O O   . HOH C 3 .   ? 35.372 79.644  36.150 1.00 59.81  ? 17  HOH A O   1 
HETATM 3099 O O   . HOH C 3 .   ? 29.742 103.186 32.788 1.00 94.86  ? 18  HOH A O   1 
HETATM 3100 O O   . HOH C 3 .   ? 5.763  72.270  20.992 1.00 68.27  ? 19  HOH A O   1 
HETATM 3101 O O   . HOH C 3 .   ? 25.381 72.187  23.424 1.00 71.26  ? 20  HOH A O   1 
HETATM 3102 O O   . HOH C 3 .   ? 41.676 78.690  46.885 1.00 72.96  ? 21  HOH A O   1 
HETATM 3103 O O   . HOH C 3 .   ? 23.632 106.513 52.859 1.00 98.35  ? 22  HOH A O   1 
HETATM 3104 O O   . HOH C 3 .   ? 21.326 81.018  34.210 1.00 68.31  ? 23  HOH A O   1 
HETATM 3105 O O   . HOH C 3 .   ? 3.106  73.778  34.044 1.00 62.33  ? 24  HOH A O   1 
HETATM 3106 O O   . HOH C 3 .   ? 0.344  88.026  38.723 1.00 73.53  ? 429 HOH A O   1 
HETATM 3107 O O   . HOH C 3 .   ? 27.307 70.521  22.250 1.00 77.79  ? 430 HOH A O   1 
HETATM 3108 O O   . HOH C 3 .   ? 20.142 88.333  33.685 1.00 110.43 ? 431 HOH A O   1 
HETATM 3109 O O   . HOH C 3 .   ? 57.410 84.644  43.547 1.00 121.97 ? 432 HOH A O   1 
HETATM 3110 O O   . HOH C 3 .   ? 34.262 97.707  46.329 1.00 109.53 ? 433 HOH A O   1 
HETATM 3111 O O   . HOH C 3 .   ? 34.629 94.428  47.148 1.00 136.62 ? 434 HOH A O   1 
HETATM 3112 O O   . HOH C 3 .   ? 8.412  87.267  33.964 1.00 93.17  ? 435 HOH A O   1 
HETATM 3113 O O   . HOH C 3 .   ? 36.378 69.058  37.963 1.00 125.69 ? 436 HOH A O   1 
HETATM 3114 O O   . HOH C 3 .   ? 61.873 91.949  45.285 1.00 73.83  ? 437 HOH A O   1 
HETATM 3115 O O   . HOH C 3 .   ? 38.636 79.874  26.603 1.00 110.08 ? 438 HOH A O   1 
HETATM 3116 O O   . HOH C 3 .   ? 37.446 68.173  45.403 1.00 86.71  ? 439 HOH A O   1 
HETATM 3117 O O   . HOH C 3 .   ? 47.604 107.610 48.267 1.00 169.72 ? 440 HOH A O   1 
HETATM 3118 O O   . HOH C 3 .   ? 17.000 97.692  41.828 1.00 99.62  ? 441 HOH A O   1 
HETATM 3119 O O   . HOH C 3 .   ? 55.713 99.467  47.960 1.00 121.30 ? 442 HOH A O   1 
HETATM 3120 O O   . HOH C 3 .   ? 25.714 74.229  8.129  1.00 85.47  ? 443 HOH A O   1 
HETATM 3121 O O   . HOH C 3 .   ? 15.535 70.111  37.275 1.00 101.67 ? 444 HOH A O   1 
HETATM 3122 O O   . HOH C 3 .   ? 40.747 73.076  30.711 1.00 88.83  ? 445 HOH A O   1 
HETATM 3123 O O   . HOH C 3 .   ? 6.857  66.806  10.568 1.00 90.31  ? 446 HOH A O   1 
HETATM 3124 O O   . HOH C 3 .   ? 19.124 59.918  6.339  1.00 95.34  ? 447 HOH A O   1 
HETATM 3125 O O   . HOH C 3 .   ? 3.673  97.520  16.079 1.00 87.50  ? 448 HOH A O   1 
HETATM 3126 O O   . HOH C 3 .   ? 14.430 103.964 37.590 1.00 103.67 ? 449 HOH A O   1 
HETATM 3127 O O   . HOH C 3 .   ? 47.744 78.445  35.743 1.00 82.58  ? 450 HOH A O   1 
HETATM 3128 O O   . HOH C 3 .   ? 12.083 84.635  7.004  1.00 85.68  ? 451 HOH A O   1 
HETATM 3129 O O   . HOH C 3 .   ? 38.053 126.433 64.544 1.00 112.08 ? 452 HOH A O   1 
HETATM 3130 O O   . HOH C 3 .   ? 19.258 100.587 23.340 1.00 117.47 ? 453 HOH A O   1 
HETATM 3131 O O   . HOH C 3 .   ? 32.040 80.820  34.411 1.00 112.90 ? 454 HOH A O   1 
HETATM 3132 O O   . HOH C 3 .   ? 23.003 81.266  42.392 1.00 100.95 ? 455 HOH A O   1 
HETATM 3133 O O   . HOH C 3 .   ? 35.542 94.358  43.892 1.00 128.80 ? 456 HOH A O   1 
HETATM 3134 O O   . HOH C 3 .   ? 44.668 92.204  28.200 1.00 95.24  ? 457 HOH A O   1 
HETATM 3135 O O   . HOH C 3 .   ? 37.459 103.223 59.839 1.00 90.65  ? 458 HOH A O   1 
HETATM 3136 O O   . HOH C 3 .   ? 26.830 67.716  7.609  1.00 87.22  ? 459 HOH A O   1 
HETATM 3137 O O   . HOH C 3 .   ? 35.184 63.993  17.690 1.00 109.43 ? 460 HOH A O   1 
HETATM 3138 O O   . HOH C 3 .   ? 31.249 87.967  50.317 1.00 72.51  ? 461 HOH A O   1 
HETATM 3139 O O   . HOH C 3 .   ? 8.096  69.899  11.143 1.00 87.51  ? 462 HOH A O   1 
HETATM 3140 O O   . HOH C 3 .   ? 10.780 63.841  37.074 1.00 92.88  ? 463 HOH A O   1 
HETATM 3141 O O   . HOH C 3 .   ? 4.518  72.710  32.275 1.00 93.79  ? 464 HOH A O   1 
HETATM 3142 O O   . HOH C 3 .   ? 20.564 120.198 58.723 1.00 85.28  ? 465 HOH A O   1 
HETATM 3143 O O   . HOH C 3 .   ? 56.616 78.645  36.248 1.00 83.55  ? 466 HOH A O   1 
HETATM 3144 O O   . HOH C 3 .   ? 4.542  62.972  13.028 1.00 100.04 ? 467 HOH A O   1 
HETATM 3145 O O   . HOH C 3 .   ? 3.944  72.162  15.992 1.00 80.53  ? 468 HOH A O   1 
HETATM 3146 O O   . HOH C 3 .   ? 48.832 126.124 64.389 1.00 81.81  ? 469 HOH A O   1 
HETATM 3147 O O   . HOH C 3 .   ? 49.653 123.368 52.624 1.00 91.92  ? 470 HOH A O   1 
HETATM 3148 O O   . HOH C 3 .   ? 25.473 98.660  44.496 1.00 80.68  ? 471 HOH A O   1 
HETATM 3149 O O   . HOH C 3 .   ? 38.205 101.142 42.468 1.00 123.84 ? 472 HOH A O   1 
HETATM 3150 O O   . HOH C 3 .   ? 28.023 73.049  45.708 1.00 109.45 ? 473 HOH A O   1 
HETATM 3151 O O   . HOH C 3 .   ? 11.312 71.928  34.895 1.00 80.46  ? 474 HOH A O   1 
HETATM 3152 O O   . HOH C 3 .   ? 50.234 121.066 56.304 1.00 83.15  ? 475 HOH A O   1 
HETATM 3153 O O   . HOH C 3 .   ? 37.135 92.112  52.858 1.00 71.18  ? 476 HOH A O   1 
HETATM 3154 O O   . HOH C 3 .   ? 16.085 76.028  9.741  1.00 108.31 ? 477 HOH A O   1 
HETATM 3155 O O   . HOH C 3 .   ? 6.857  100.952 35.767 1.00 105.98 ? 478 HOH A O   1 
HETATM 3156 O O   . HOH C 3 .   ? 41.766 101.636 35.849 1.00 83.67  ? 479 HOH A O   1 
HETATM 3157 O O   . HOH C 3 .   ? 16.211 70.342  40.052 1.00 97.00  ? 480 HOH A O   1 
HETATM 3158 O O   . HOH C 3 .   ? 23.319 100.992 50.402 1.00 84.62  ? 481 HOH A O   1 
HETATM 3159 O O   . HOH C 3 .   ? 15.122 49.579  16.467 1.00 89.14  ? 482 HOH A O   1 
HETATM 3160 O O   . HOH C 3 .   ? 37.023 94.738  49.594 1.00 112.36 ? 483 HOH A O   1 
HETATM 3161 O O   . HOH C 3 .   ? -0.112 67.347  9.201  1.00 93.24  ? 484 HOH A O   1 
HETATM 3162 O O   . HOH C 3 .   ? 8.522  62.439  16.657 1.00 80.74  ? 485 HOH A O   1 
HETATM 3163 O O   . HOH C 3 .   ? 19.247 77.108  7.848  1.00 92.90  ? 486 HOH A O   1 
HETATM 3164 O O   . HOH C 3 .   ? 2.548  85.366  34.029 1.00 81.27  ? 487 HOH A O   1 
HETATM 3165 O O   . HOH C 3 .   ? 57.037 121.014 70.967 1.00 111.26 ? 488 HOH A O   1 
HETATM 3166 O O   . HOH C 3 .   ? 48.230 118.263 69.362 1.00 82.22  ? 489 HOH A O   1 
HETATM 3167 O O   . HOH C 3 .   ? 26.077 100.423 22.647 1.00 78.84  ? 490 HOH A O   1 
HETATM 3168 O O   . HOH C 3 .   ? 30.441 68.594  44.369 1.00 118.98 ? 491 HOH A O   1 
HETATM 3169 O O   . HOH C 3 .   ? 11.676 108.110 41.405 1.00 95.38  ? 492 HOH A O   1 
HETATM 3170 O O   . HOH C 3 .   ? 16.947 43.469  29.369 1.00 85.34  ? 493 HOH A O   1 
HETATM 3171 O O   . HOH C 3 .   ? 3.323  72.323  26.356 1.00 89.89  ? 494 HOH A O   1 
HETATM 3172 O O   . HOH C 3 .   ? 36.856 109.859 43.083 1.00 135.83 ? 495 HOH A O   1 
HETATM 3173 O O   . HOH C 3 .   ? 22.368 89.402  25.572 1.00 50.53  ? 496 HOH A O   1 
HETATM 3174 O O   . HOH C 3 .   ? -2.412 77.706  31.090 1.00 66.34  ? 497 HOH A O   1 
HETATM 3175 O O   . HOH C 3 .   ? 30.603 94.989  42.338 1.00 59.67  ? 498 HOH A O   1 
HETATM 3176 O O   . HOH C 3 .   ? 23.970 77.511  21.590 1.00 90.18  ? 499 HOH A O   1 
HETATM 3177 O O   . HOH C 3 .   ? 18.499 61.527  12.362 1.00 72.85  ? 500 HOH A O   1 
HETATM 3178 O O   . HOH C 3 .   ? 44.152 77.574  44.145 1.00 72.26  ? 501 HOH A O   1 
HETATM 3179 O O   . HOH C 3 .   ? 24.189 90.769  36.882 1.00 72.84  ? 502 HOH A O   1 
HETATM 3180 O O   . HOH C 3 .   ? 34.658 75.263  25.178 1.00 88.37  ? 503 HOH A O   1 
HETATM 3181 O O   . HOH C 3 .   ? 17.921 87.529  39.886 1.00 64.19  ? 504 HOH A O   1 
HETATM 3182 O O   . HOH C 3 .   ? 40.743 109.761 36.191 1.00 85.80  ? 505 HOH A O   1 
HETATM 3183 O O   . HOH C 3 .   ? 5.615  78.555  24.835 1.00 70.49  ? 506 HOH A O   1 
HETATM 3184 O O   . HOH C 3 .   ? 40.865 121.620 71.030 1.00 87.27  ? 507 HOH A O   1 
HETATM 3185 O O   . HOH C 3 .   ? 53.299 83.062  47.206 1.00 74.27  ? 508 HOH A O   1 
HETATM 3186 O O   . HOH C 3 .   ? 35.003 88.070  49.695 1.00 62.17  ? 509 HOH A O   1 
HETATM 3187 O O   . HOH C 3 .   ? 49.323 84.892  56.465 1.00 72.80  ? 510 HOH A O   1 
HETATM 3188 O O   . HOH C 3 .   ? 33.975 76.605  29.926 1.00 64.55  ? 511 HOH A O   1 
HETATM 3189 O O   . HOH C 3 .   ? 1.627  63.395  28.972 1.00 86.14  ? 512 HOH A O   1 
HETATM 3190 O O   . HOH C 3 .   ? 23.398 84.168  21.568 1.00 67.05  ? 513 HOH A O   1 
HETATM 3191 O O   . HOH C 3 .   ? 41.039 101.991 41.635 1.00 65.31  ? 514 HOH A O   1 
HETATM 3192 O O   . HOH C 3 .   ? 40.198 107.107 43.005 1.00 78.88  ? 515 HOH A O   1 
HETATM 3193 O O   . HOH C 3 .   ? 36.018 90.243  42.285 1.00 66.50  ? 516 HOH A O   1 
HETATM 3194 O O   . HOH C 3 .   ? 58.068 89.139  48.878 1.00 88.26  ? 517 HOH A O   1 
HETATM 3195 O O   . HOH C 3 .   ? 0.815  96.167  41.461 1.00 110.08 ? 518 HOH A O   1 
HETATM 3196 O O   . HOH C 3 .   ? 20.591 56.929  6.827  1.00 83.24  ? 519 HOH A O   1 
HETATM 3197 O O   . HOH C 3 .   ? 29.720 81.164  26.559 1.00 106.19 ? 520 HOH A O   1 
HETATM 3198 O O   . HOH C 3 .   ? 53.998 81.448  51.979 1.00 67.51  ? 521 HOH A O   1 
HETATM 3199 O O   . HOH C 3 .   ? 19.691 116.869 61.213 1.00 107.48 ? 522 HOH A O   1 
HETATM 3200 O O   . HOH C 3 .   ? 36.492 103.458 43.126 1.00 61.44  ? 523 HOH A O   1 
HETATM 3201 O O   . HOH C 3 .   ? 38.150 95.584  48.094 1.00 67.89  ? 524 HOH A O   1 
HETATM 3202 O O   . HOH C 3 .   ? 3.242  66.785  18.481 1.00 84.15  ? 525 HOH A O   1 
HETATM 3203 O O   . HOH C 3 .   ? 35.912 89.319  46.523 1.00 97.27  ? 526 HOH A O   1 
HETATM 3204 O O   . HOH C 3 .   ? 28.199 68.800  19.367 1.00 74.33  ? 527 HOH A O   1 
HETATM 3205 O O   . HOH C 3 .   ? 11.913 65.112  22.578 1.00 69.43  ? 528 HOH A O   1 
HETATM 3206 O O   . HOH C 3 .   ? 53.314 99.052  46.808 1.00 88.08  ? 529 HOH A O   1 
HETATM 3207 O O   . HOH C 3 .   ? 44.999 76.456  35.767 1.00 98.30  ? 530 HOH A O   1 
HETATM 3208 O O   . HOH C 3 .   ? 28.175 71.291  43.979 1.00 56.68  ? 531 HOH A O   1 
HETATM 3209 O O   . HOH C 3 .   ? 21.836 91.482  26.571 1.00 76.68  ? 532 HOH A O   1 
HETATM 3210 O O   . HOH C 3 .   ? 37.148 90.137  44.374 1.00 78.59  ? 533 HOH A O   1 
HETATM 3211 O O   . HOH C 3 .   ? 23.499 87.958  24.126 1.00 63.16  ? 534 HOH A O   1 
HETATM 3212 O O   . HOH C 3 .   ? 34.882 81.660  37.629 1.00 75.44  ? 535 HOH A O   1 
HETATM 3213 O O   . HOH C 3 .   ? 29.617 96.969  50.523 1.00 91.39  ? 536 HOH A O   1 
HETATM 3214 O O   . HOH C 3 .   ? 9.613  59.562  9.361  1.00 94.16  ? 537 HOH A O   1 
HETATM 3215 O O   . HOH C 3 .   ? 45.995 86.490  32.310 1.00 79.14  ? 538 HOH A O   1 
HETATM 3216 O O   . HOH C 3 .   ? 21.805 72.472  21.144 1.00 82.15  ? 539 HOH A O   1 
HETATM 3217 O O   . HOH C 3 .   ? 36.452 93.828  55.060 1.00 65.92  ? 540 HOH A O   1 
HETATM 3218 O O   . HOH C 3 .   ? 31.466 57.904  17.236 1.00 52.35  ? 541 HOH A O   1 
HETATM 3219 O O   . HOH C 3 .   ? 3.284  79.020  23.812 1.00 73.47  ? 542 HOH A O   1 
HETATM 3220 O O   . HOH C 3 .   ? 23.852 76.812  26.524 1.00 64.05  ? 543 HOH A O   1 
HETATM 3221 O O   . HOH C 3 .   ? 49.349 103.651 69.067 1.00 73.28  ? 544 HOH A O   1 
HETATM 3222 O O   . HOH C 3 .   ? 58.963 96.827  48.464 1.00 80.03  ? 545 HOH A O   1 
HETATM 3223 O O   . HOH C 3 .   ? 34.042 70.449  14.223 1.00 79.85  ? 546 HOH A O   1 
HETATM 3224 O O   . HOH C 3 .   ? 28.194 92.783  52.402 1.00 89.09  ? 547 HOH A O   1 
HETATM 3225 O O   . HOH C 3 .   ? 18.039 63.988  36.294 1.00 90.58  ? 548 HOH A O   1 
HETATM 3226 O O   . HOH C 3 .   ? 28.621 107.060 29.524 1.00 75.38  ? 549 HOH A O   1 
HETATM 3227 O O   . HOH C 3 .   ? 2.252  88.845  33.076 1.00 95.13  ? 550 HOH A O   1 
HETATM 3228 O O   . HOH C 3 .   ? 5.524  66.466  32.028 1.00 98.04  ? 551 HOH A O   1 
HETATM 3229 O O   . HOH C 3 .   ? 23.540 79.994  21.726 1.00 81.23  ? 552 HOH A O   1 
HETATM 3230 O O   . HOH C 3 .   ? 35.724 112.217 38.645 1.00 83.95  ? 553 HOH A O   1 
HETATM 3231 O O   . HOH C 3 .   ? 18.876 54.758  31.334 1.00 89.40  ? 554 HOH A O   1 
HETATM 3232 O O   . HOH C 3 .   ? 27.311 101.173 26.372 1.00 99.55  ? 555 HOH A O   1 
HETATM 3233 O O   . HOH C 3 .   ? 51.386 87.051  36.228 1.00 88.01  ? 556 HOH A O   1 
HETATM 3234 O O   . HOH C 3 .   ? 43.846 78.702  35.181 1.00 53.84  ? 557 HOH A O   1 
HETATM 3235 O O   . HOH C 3 .   ? 56.880 85.215  53.916 1.00 91.21  ? 558 HOH A O   1 
HETATM 3236 O O   . HOH C 3 .   ? 34.488 102.555 39.428 1.00 87.64  ? 559 HOH A O   1 
HETATM 3237 O O   . HOH C 3 .   ? 53.725 85.771  36.989 1.00 83.08  ? 560 HOH A O   1 
HETATM 3238 O O   . HOH C 3 .   ? 38.453 103.868 44.518 1.00 71.04  ? 561 HOH A O   1 
HETATM 3239 O O   . HOH C 3 .   ? 7.492  66.783  17.602 1.00 102.16 ? 562 HOH A O   1 
HETATM 3240 O O   . HOH C 3 .   ? 28.894 107.116 25.946 1.00 88.25  ? 563 HOH A O   1 
HETATM 3241 O O   . HOH C 3 .   ? 52.083 114.093 54.172 1.00 78.80  ? 564 HOH A O   1 
HETATM 3242 O O   . HOH C 3 .   ? 35.710 72.987  47.742 1.00 70.46  ? 565 HOH A O   1 
HETATM 3243 O O   . HOH C 3 .   ? 8.781  107.413 54.256 1.00 94.81  ? 566 HOH A O   1 
HETATM 3244 O O   . HOH C 3 .   ? 26.382 82.935  28.786 1.00 54.85  ? 567 HOH A O   1 
HETATM 3245 O O   . HOH C 3 .   ? 35.489 96.736  38.616 1.00 50.99  ? 568 HOH A O   1 
HETATM 3246 O O   . HOH C 3 .   ? 42.763 80.388  51.661 1.00 52.30  ? 569 HOH A O   1 
HETATM 3247 O O   . HOH C 3 .   ? 31.281 60.681  16.959 1.00 71.91  ? 570 HOH A O   1 
HETATM 3248 O O   . HOH C 3 .   ? 36.201 93.600  41.411 1.00 72.83  ? 571 HOH A O   1 
HETATM 3249 O O   . HOH C 3 .   ? 1.064  79.973  34.665 1.00 74.57  ? 572 HOH A O   1 
HETATM 3250 O O   . HOH C 3 .   ? 20.565 52.081  7.256  1.00 67.04  ? 573 HOH A O   1 
HETATM 3251 O O   . HOH C 3 .   ? 13.649 50.572  32.716 1.00 85.64  ? 574 HOH A O   1 
HETATM 3252 O O   . HOH C 3 .   ? 28.441 71.202  10.771 1.00 77.00  ? 575 HOH A O   1 
HETATM 3253 O O   . HOH C 3 .   ? 50.004 94.000  30.875 1.00 82.21  ? 576 HOH A O   1 
HETATM 3254 O O   . HOH C 3 .   ? 50.657 81.808  49.577 1.00 71.76  ? 577 HOH A O   1 
HETATM 3255 O O   . HOH C 3 .   ? 51.674 100.332 37.934 1.00 77.38  ? 578 HOH A O   1 
HETATM 3256 O O   . HOH C 3 .   ? 37.538 78.734  30.184 1.00 58.25  ? 579 HOH A O   1 
HETATM 3257 O O   . HOH C 3 .   ? 13.227 59.728  14.736 1.00 81.99  ? 580 HOH A O   1 
HETATM 3258 O O   . HOH C 3 .   ? 26.764 78.541  27.571 1.00 82.37  ? 581 HOH A O   1 
HETATM 3259 O O   . HOH C 3 .   ? 33.060 69.522  18.456 1.00 89.58  ? 582 HOH A O   1 
HETATM 3260 O O   . HOH C 3 .   ? 33.173 82.665  35.937 1.00 66.08  ? 583 HOH A O   1 
HETATM 3261 O O   . HOH C 3 .   ? 13.629 95.520  18.186 1.00 78.62  ? 584 HOH A O   1 
HETATM 3262 O O   . HOH C 3 .   ? 11.530 100.757 42.867 1.00 70.85  ? 585 HOH A O   1 
HETATM 3263 O O   . HOH C 3 .   ? 25.050 81.003  38.384 1.00 88.83  ? 586 HOH A O   1 
HETATM 3264 O O   . HOH C 3 .   ? 22.349 56.906  37.575 1.00 75.39  ? 587 HOH A O   1 
HETATM 3265 O O   . HOH C 3 .   ? 13.210 68.804  35.295 1.00 77.56  ? 588 HOH A O   1 
HETATM 3266 O O   . HOH C 3 .   ? 34.575 128.108 50.012 1.00 75.71  ? 589 HOH A O   1 
HETATM 3267 O O   . HOH C 3 .   ? 58.065 99.250  47.756 1.00 81.23  ? 590 HOH A O   1 
HETATM 3268 O O   . HOH C 3 .   ? 27.496 121.950 64.732 1.00 64.00  ? 591 HOH A O   1 
HETATM 3269 O O   . HOH C 3 .   ? -3.609 97.665  30.907 1.00 86.67  ? 592 HOH A O   1 
HETATM 3270 O O   . HOH C 3 .   ? 22.439 88.006  37.721 1.00 88.47  ? 593 HOH A O   1 
HETATM 3271 O O   . HOH C 3 .   ? 35.931 111.012 41.140 1.00 85.51  ? 594 HOH A O   1 
HETATM 3272 O O   . HOH C 3 .   ? 14.602 67.697  3.139  1.00 81.20  ? 595 HOH A O   1 
HETATM 3273 O O   . HOH C 3 .   ? 28.122 81.391  33.789 1.00 80.01  ? 596 HOH A O   1 
HETATM 3274 O O   . HOH C 3 .   ? 23.672 81.261  12.599 1.00 89.89  ? 597 HOH A O   1 
HETATM 3275 O O   . HOH C 3 .   ? 33.679 93.669  45.374 1.00 94.84  ? 598 HOH A O   1 
HETATM 3276 O O   . HOH C 3 .   ? 25.579 108.778 55.793 1.00 77.81  ? 599 HOH A O   1 
HETATM 3277 O O   . HOH C 3 .   ? 14.749 89.099  37.777 1.00 75.88  ? 600 HOH A O   1 
HETATM 3278 O O   . HOH C 3 .   ? 6.644  101.148 25.238 1.00 79.72  ? 601 HOH A O   1 
HETATM 3279 O O   . HOH C 3 .   ? 10.223 77.100  8.917  1.00 71.15  ? 602 HOH A O   1 
HETATM 3280 O O   . HOH C 3 .   ? 13.198 58.357  18.777 1.00 78.02  ? 603 HOH A O   1 
HETATM 3281 O O   . HOH C 3 .   ? 30.429 84.599  37.839 1.00 68.70  ? 604 HOH A O   1 
HETATM 3282 O O   . HOH C 3 .   ? 33.196 65.685  13.988 1.00 75.13  ? 605 HOH A O   1 
HETATM 3283 O O   . HOH C 3 .   ? 12.568 85.747  9.581  1.00 92.44  ? 606 HOH A O   1 
HETATM 3284 O O   . HOH C 3 .   ? 15.646 93.203  17.369 1.00 67.70  ? 607 HOH A O   1 
HETATM 3285 O O   . HOH C 3 .   ? 54.153 94.848  39.854 1.00 90.64  ? 608 HOH A O   1 
HETATM 3286 O O   . HOH C 3 .   ? 3.982  103.072 28.958 1.00 86.12  ? 609 HOH A O   1 
HETATM 3287 O O   . HOH C 3 .   ? 53.128 120.360 66.770 1.00 94.10  ? 610 HOH A O   1 
HETATM 3288 O O   . HOH C 3 .   ? 21.009 100.011 21.867 1.00 95.61  ? 611 HOH A O   1 
HETATM 3289 O O   . HOH C 3 .   ? 6.938  87.368  9.059  1.00 85.02  ? 612 HOH A O   1 
HETATM 3290 O O   . HOH C 3 .   ? 12.151 53.580  25.772 1.00 76.83  ? 613 HOH A O   1 
HETATM 3291 O O   . HOH C 3 .   ? 26.121 76.202  9.539  1.00 84.37  ? 614 HOH A O   1 
HETATM 3292 O O   . HOH C 3 .   ? 4.270  59.236  22.759 1.00 110.28 ? 615 HOH A O   1 
HETATM 3293 O O   . HOH C 3 .   ? 50.341 84.847  34.343 1.00 72.10  ? 616 HOH A O   1 
HETATM 3294 O O   . HOH C 3 .   ? 6.946  64.343  21.386 1.00 69.36  ? 617 HOH A O   1 
HETATM 3295 O O   . HOH C 3 .   ? 52.166 84.574  42.632 1.00 69.52  ? 618 HOH A O   1 
HETATM 3296 O O   . HOH C 3 .   ? 1.320  63.559  24.296 1.00 102.82 ? 619 HOH A O   1 
HETATM 3297 O O   . HOH C 3 .   ? 30.158 102.324 53.786 1.00 81.28  ? 620 HOH A O   1 
HETATM 3298 O O   . HOH C 3 .   ? 32.183 87.285  41.434 1.00 80.99  ? 621 HOH A O   1 
HETATM 3299 O O   . HOH C 3 .   ? 42.707 90.403  31.604 1.00 67.35  ? 622 HOH A O   1 
HETATM 3300 O O   . HOH C 3 .   ? 50.531 118.402 69.942 1.00 72.90  ? 623 HOH A O   1 
HETATM 3301 O O   . HOH C 3 .   ? 27.799 94.837  29.772 1.00 81.71  ? 624 HOH A O   1 
HETATM 3302 O O   . HOH C 3 .   ? -0.838 89.881  30.266 1.00 86.05  ? 625 HOH A O   1 
HETATM 3303 O O   . HOH C 3 .   ? 22.422 48.124  30.020 1.00 93.20  ? 626 HOH A O   1 
HETATM 3304 O O   . HOH C 3 .   ? 47.976 80.126  52.051 1.00 82.60  ? 627 HOH A O   1 
HETATM 3305 O O   . HOH C 3 .   ? 58.151 95.694  38.214 1.00 109.33 ? 628 HOH A O   1 
HETATM 3306 O O   . HOH C 3 .   ? 39.177 75.359  49.336 1.00 80.33  ? 629 HOH A O   1 
HETATM 3307 O O   . HOH C 3 .   ? 32.465 60.181  19.173 1.00 74.88  ? 630 HOH A O   1 
HETATM 3308 O O   . HOH C 3 .   ? 35.873 91.800  39.550 1.00 74.41  ? 631 HOH A O   1 
HETATM 3309 O O   . HOH C 3 .   ? 26.165 84.759  30.335 1.00 64.63  ? 632 HOH A O   1 
HETATM 3310 O O   . HOH C 3 .   ? 44.005 104.067 38.465 1.00 77.98  ? 633 HOH A O   1 
HETATM 3311 O O   . HOH C 3 .   ? 23.782 87.333  41.263 1.00 81.61  ? 634 HOH A O   1 
HETATM 3312 O O   . HOH C 3 .   ? 43.285 108.358 36.644 1.00 82.88  ? 635 HOH A O   1 
HETATM 3313 O O   . HOH C 3 .   ? 45.018 81.692  51.293 1.00 77.52  ? 636 HOH A O   1 
HETATM 3314 O O   . HOH C 3 .   ? 55.730 82.024  39.510 1.00 74.74  ? 637 HOH A O   1 
HETATM 3315 O O   . HOH C 3 .   ? 26.727 73.108  13.859 1.00 99.15  ? 638 HOH A O   1 
HETATM 3316 O O   . HOH C 3 .   ? 34.732 110.040 36.818 1.00 106.05 ? 639 HOH A O   1 
HETATM 3317 O O   . HOH C 3 .   ? 4.927  68.257  13.725 1.00 93.77  ? 640 HOH A O   1 
HETATM 3318 O O   . HOH C 3 .   ? 19.609 89.095  43.105 1.00 71.64  ? 641 HOH A O   1 
HETATM 3319 O O   . HOH C 3 .   ? 6.480  90.729  10.203 1.00 77.04  ? 642 HOH A O   1 
HETATM 3320 O O   . HOH C 3 .   ? 36.438 126.994 62.549 1.00 69.78  ? 643 HOH A O   1 
HETATM 3321 O O   . HOH C 3 .   ? 39.154 81.738  28.593 1.00 107.96 ? 644 HOH A O   1 
HETATM 3322 O O   . HOH C 3 .   ? 22.285 53.445  6.503  1.00 81.95  ? 645 HOH A O   1 
HETATM 3323 O O   . HOH C 3 .   ? 28.393 68.613  14.076 1.00 85.70  ? 646 HOH A O   1 
HETATM 3324 O O   . HOH C 3 .   ? 9.899  97.040  20.891 1.00 90.85  ? 647 HOH A O   1 
HETATM 3325 O O   . HOH C 3 .   ? 35.590 84.273  34.382 1.00 99.52  ? 648 HOH A O   1 
HETATM 3326 O O   . HOH C 3 .   ? 16.857 61.728  5.159  1.00 89.51  ? 649 HOH A O   1 
HETATM 3327 O O   . HOH C 3 .   ? 26.574 93.644  45.335 1.00 88.86  ? 650 HOH A O   1 
HETATM 3328 O O   . HOH C 3 .   ? 60.678 98.106  46.432 1.00 78.34  ? 651 HOH A O   1 
HETATM 3329 O O   . HOH C 3 .   ? 34.804 72.355  25.090 1.00 89.98  ? 652 HOH A O   1 
HETATM 3330 O O   . HOH C 3 .   ? 22.498 78.800  10.874 1.00 118.21 ? 653 HOH A O   1 
HETATM 3331 O O   . HOH C 3 .   ? 17.746 95.823  43.848 1.00 74.72  ? 654 HOH A O   1 
HETATM 3332 O O   . HOH C 3 .   ? 19.298 95.055  45.623 1.00 77.29  ? 655 HOH A O   1 
HETATM 3333 O O   . HOH C 3 .   ? 30.006 96.214  38.782 1.00 88.93  ? 656 HOH A O   1 
HETATM 3334 O O   . HOH C 3 .   ? 28.896 93.194  32.179 1.00 76.83  ? 657 HOH A O   1 
HETATM 3335 O O   . HOH C 3 .   ? 38.898 102.523 33.964 1.00 92.33  ? 658 HOH A O   1 
HETATM 3336 O O   . HOH C 3 .   ? 34.216 95.172  49.093 1.00 103.45 ? 659 HOH A O   1 
HETATM 3337 O O   . HOH C 3 .   ? 22.909 64.219  4.638  1.00 87.76  ? 660 HOH A O   1 
HETATM 3338 O O   . HOH C 3 .   ? 52.042 101.156 35.253 1.00 79.59  ? 661 HOH A O   1 
HETATM 3339 O O   . HOH C 3 .   ? 29.732 83.291  43.425 1.00 85.05  ? 662 HOH A O   1 
HETATM 3340 O O   . HOH C 3 .   ? 6.267  67.229  37.146 1.00 102.00 ? 663 HOH A O   1 
HETATM 3341 O O   . HOH C 3 .   ? 33.750 131.045 49.381 1.00 69.80  ? 664 HOH A O   1 
HETATM 3342 O O   . HOH C 3 .   ? 17.447 57.854  6.465  1.00 80.79  ? 665 HOH A O   1 
HETATM 3343 O O   . HOH C 3 .   ? 28.811 76.246  11.226 1.00 100.13 ? 666 HOH A O   1 
HETATM 3344 O O   . HOH C 3 .   ? 12.544 66.732  3.780  1.00 98.76  ? 667 HOH A O   1 
HETATM 3345 O O   . HOH C 3 .   ? 40.937 75.573  30.181 1.00 84.31  ? 668 HOH A O   1 
HETATM 3346 O O   . HOH C 3 .   ? 15.779 61.158  9.662  1.00 98.57  ? 669 HOH A O   1 
HETATM 3347 O O   . HOH C 3 .   ? 43.398 123.756 72.421 1.00 65.86  ? 670 HOH A O   1 
HETATM 3348 O O   . HOH C 3 .   ? 60.470 87.762  46.875 1.00 86.84  ? 671 HOH A O   1 
HETATM 3349 O O   . HOH C 3 .   ? 3.898  78.344  19.083 1.00 62.56  ? 672 HOH A O   1 
HETATM 3350 O O   . HOH C 3 .   ? 28.057 81.685  31.474 1.00 81.78  ? 673 HOH A O   1 
HETATM 3351 O O   . HOH C 3 .   ? 20.399 104.458 52.814 1.00 76.33  ? 674 HOH A O   1 
HETATM 3352 O O   . HOH C 3 .   ? 31.434 89.779  44.584 1.00 98.40  ? 675 HOH A O   1 
HETATM 3353 O O   . HOH C 3 .   ? 49.815 79.934  50.377 1.00 89.79  ? 676 HOH A O   1 
HETATM 3354 O O   . HOH C 3 .   ? 32.112 96.510  46.250 1.00 76.75  ? 677 HOH A O   1 
HETATM 3355 O O   . HOH C 3 .   ? 24.076 82.173  20.212 1.00 83.44  ? 678 HOH A O   1 
HETATM 3356 O O   . HOH C 3 .   ? 9.654  91.772  10.845 1.00 100.22 ? 679 HOH A O   1 
HETATM 3357 O O   . HOH C 3 .   ? 21.949 121.564 61.345 1.00 80.19  ? 680 HOH A O   1 
HETATM 3358 O O   . HOH C 3 .   ? 46.375 127.759 71.671 1.00 70.32  ? 681 HOH A O   1 
HETATM 3359 O O   . HOH C 3 .   ? -1.067 74.468  38.286 1.00 76.75  ? 682 HOH A O   1 
HETATM 3360 O O   . HOH C 3 .   ? 33.419 99.978  34.941 1.00 78.18  ? 683 HOH A O   1 
HETATM 3361 O O   . HOH C 3 .   ? 34.306 81.737  33.579 1.00 74.48  ? 684 HOH A O   1 
HETATM 3362 O O   . HOH C 3 .   ? 0.828  84.868  31.513 1.00 84.31  ? 685 HOH A O   1 
HETATM 3363 O O   . HOH C 3 .   ? 15.034 44.494  26.709 1.00 88.32  ? 686 HOH A O   1 
HETATM 3364 O O   . HOH C 3 .   ? 12.550 94.032  13.600 1.00 75.41  ? 687 HOH A O   1 
HETATM 3365 O O   . HOH C 3 .   ? 31.006 78.987  27.903 1.00 80.43  ? 688 HOH A O   1 
HETATM 3366 O O   . HOH C 3 .   ? 0.332  83.456  36.111 1.00 88.92  ? 689 HOH A O   1 
HETATM 3367 O O   . HOH C 3 .   ? 44.457 92.382  30.740 1.00 79.22  ? 690 HOH A O   1 
HETATM 3368 O O   . HOH C 3 .   ? 14.239 57.247  9.553  1.00 84.52  ? 691 HOH A O   1 
HETATM 3369 O O   . HOH C 3 .   ? 3.506  63.927  20.863 1.00 82.46  ? 692 HOH A O   1 
HETATM 3370 O O   . HOH C 3 .   ? -0.302 76.324  43.041 1.00 79.08  ? 693 HOH A O   1 
HETATM 3371 O O   . HOH C 3 .   ? 53.390 112.500 47.382 1.00 77.28  ? 694 HOH A O   1 
HETATM 3372 O O   . HOH C 3 .   ? 63.398 99.699  47.351 1.00 71.76  ? 695 HOH A O   1 
HETATM 3373 O O   . HOH C 3 .   ? 39.978 73.289  42.340 1.00 108.92 ? 696 HOH A O   1 
HETATM 3374 O O   . HOH C 3 .   ? 40.262 73.158  47.435 1.00 80.47  ? 697 HOH A O   1 
HETATM 3375 O O   . HOH C 3 .   ? 12.467 78.985  39.512 1.00 66.92  ? 698 HOH A O   1 
HETATM 3376 O O   . HOH C 3 .   ? 5.832  70.058  12.153 1.00 84.66  ? 699 HOH A O   1 
HETATM 3377 O O   . HOH C 3 .   ? 19.209 64.940  38.647 1.00 81.46  ? 700 HOH A O   1 
HETATM 3378 O O   . HOH C 3 .   ? 22.882 123.526 58.006 1.00 94.14  ? 701 HOH A O   1 
HETATM 3379 O O   . HOH C 3 .   ? 60.887 85.857  45.231 1.00 84.48  ? 702 HOH A O   1 
HETATM 3380 O O   . HOH C 3 .   ? 58.209 97.405  43.463 1.00 89.56  ? 703 HOH A O   1 
HETATM 3381 O O   . HOH C 3 .   ? 25.679 123.233 55.569 1.00 81.48  ? 704 HOH A O   1 
HETATM 3382 O O   . HOH C 3 .   ? 47.025 91.565  33.378 1.00 78.90  ? 705 HOH A O   1 
HETATM 3383 O O   . HOH C 3 .   ? 27.762 94.869  38.921 1.00 88.19  ? 706 HOH A O   1 
HETATM 3384 O O   . HOH C 3 .   ? 29.665 122.726 66.656 1.00 97.29  ? 707 HOH A O   1 
HETATM 3385 O O   . HOH C 3 .   ? 9.964  69.800  38.644 1.00 76.61  ? 708 HOH A O   1 
HETATM 3386 O O   . HOH C 3 .   ? 11.588 55.631  10.613 1.00 91.99  ? 709 HOH A O   1 
HETATM 3387 O O   . HOH C 3 .   ? 25.753 94.437  28.061 1.00 99.88  ? 710 HOH A O   1 
HETATM 3388 O O   . HOH C 3 .   ? 44.804 104.935 34.600 1.00 75.23  ? 711 HOH A O   1 
HETATM 3389 O O   . HOH C 3 .   ? 53.461 80.849  35.958 1.00 74.29  ? 712 HOH A O   1 
HETATM 3390 O O   . HOH C 3 .   ? 5.615  96.814  17.313 1.00 87.49  ? 713 HOH A O   1 
HETATM 3391 O O   . HOH C 3 .   ? 22.260 87.866  44.433 1.00 92.69  ? 714 HOH A O   1 
HETATM 3392 O O   . HOH C 3 .   ? -1.618 68.551  7.693  1.00 109.14 ? 715 HOH A O   1 
HETATM 3393 O O   . HOH C 3 .   ? 55.680 95.138  31.238 1.00 91.70  ? 716 HOH A O   1 
HETATM 3394 O O   . HOH C 3 .   ? 33.164 131.842 52.878 1.00 83.47  ? 717 HOH A O   1 
HETATM 3395 O O   . HOH C 3 .   ? 21.103 46.391  24.752 1.00 72.44  ? 718 HOH A O   1 
HETATM 3396 O O   . HOH C 3 .   ? 24.615 46.042  32.885 1.00 86.84  ? 719 HOH A O   1 
HETATM 3397 O O   . HOH C 3 .   ? 62.356 95.463  44.043 1.00 73.10  ? 720 HOH A O   1 
HETATM 3398 O O   . HOH C 3 .   ? 48.607 79.907  45.421 1.00 69.60  ? 721 HOH A O   1 
HETATM 3399 O O   . HOH C 3 .   ? 42.861 113.755 37.242 1.00 89.18  ? 722 HOH A O   1 
HETATM 3400 O O   . HOH C 3 .   ? -0.350 65.591  11.681 1.00 111.46 ? 723 HOH A O   1 
HETATM 3401 O O   . HOH C 3 .   ? 2.552  89.358  36.298 1.00 88.48  ? 724 HOH A O   1 
HETATM 3402 O O   . HOH C 3 .   ? 24.088 76.821  6.576  1.00 80.38  ? 725 HOH A O   1 
HETATM 3403 O O   . HOH C 3 .   ? 33.834 86.953  52.554 1.00 86.84  ? 726 HOH A O   1 
HETATM 3404 O O   . HOH C 3 .   ? 37.894 114.379 70.886 1.00 97.81  ? 727 HOH A O   1 
HETATM 3405 O O   . HOH C 3 .   ? 60.856 112.828 57.715 1.00 88.25  ? 728 HOH A O   1 
HETATM 3406 O O   . HOH C 3 .   ? 27.658 124.934 52.788 1.00 91.17  ? 729 HOH A O   1 
HETATM 3407 O O   . HOH C 3 .   ? 21.881 45.234  31.413 1.00 88.91  ? 730 HOH A O   1 
HETATM 3408 O O   . HOH C 3 .   ? 38.070 92.261  33.536 1.00 88.48  ? 731 HOH A O   1 
HETATM 3409 O O   . HOH C 3 .   ? 4.943  64.466  26.997 1.00 85.88  ? 732 HOH A O   1 
HETATM 3410 O O   . HOH C 3 .   ? 32.479 92.234  31.717 1.00 91.91  ? 733 HOH A O   1 
HETATM 3411 O O   . HOH C 3 .   ? 36.208 130.014 51.275 1.00 76.81  ? 734 HOH A O   1 
HETATM 3412 O O   . HOH C 3 .   ? 41.536 95.459  50.527 1.00 85.44  ? 735 HOH A O   1 
HETATM 3413 O O   . HOH C 3 .   ? 28.610 102.616 31.083 1.00 83.23  ? 736 HOH A O   1 
HETATM 3414 O O   . HOH C 3 .   ? 18.217 77.253  40.663 1.00 74.22  ? 737 HOH A O   1 
HETATM 3415 O O   . HOH C 3 .   ? 10.945 79.017  33.359 1.00 93.47  ? 738 HOH A O   1 
HETATM 3416 O O   . HOH C 3 .   ? 29.690 74.755  45.346 1.00 73.03  ? 739 HOH A O   1 
HETATM 3417 O O   . HOH C 3 .   ? 30.300 70.978  44.838 1.00 77.59  ? 740 HOH A O   1 
HETATM 3418 O O   . HOH C 3 .   ? 38.276 73.261  48.808 1.00 89.04  ? 741 HOH A O   1 
HETATM 3419 O O   . HOH C 3 .   ? 16.483 72.033  38.519 1.00 76.16  ? 742 HOH A O   1 
HETATM 3420 O O   . HOH C 3 .   ? 56.970 93.117  46.760 1.00 94.86  ? 743 HOH A O   1 
HETATM 3421 O O   . HOH C 3 .   ? 31.601 68.031  35.176 1.00 84.45  ? 744 HOH A O   1 
HETATM 3422 O O   . HOH C 3 .   ? 49.719 85.634  42.702 1.00 80.05  ? 745 HOH A O   1 
HETATM 3423 O O   . HOH C 3 .   ? 10.693 90.078  18.167 1.00 90.77  ? 746 HOH A O   1 
HETATM 3424 O O   . HOH C 3 .   ? 23.427 74.031  23.256 1.00 75.19  ? 747 HOH A O   1 
HETATM 3425 O O   . HOH C 3 .   ? 30.352 103.540 49.530 1.00 82.09  ? 748 HOH A O   1 
HETATM 3426 O O   . HOH C 3 .   ? 45.862 78.269  37.692 1.00 83.15  ? 749 HOH A O   1 
HETATM 3427 O O   . HOH C 3 .   ? 29.999 63.837  22.761 1.00 99.36  ? 750 HOH A O   1 
HETATM 3428 O O   . HOH C 3 .   ? 26.220 79.805  34.645 1.00 69.70  ? 751 HOH A O   1 
HETATM 3429 O O   . HOH C 3 .   ? 32.868 108.423 35.627 1.00 84.80  ? 752 HOH A O   1 
HETATM 3430 O O   . HOH C 3 .   ? 51.106 84.174  49.705 1.00 101.60 ? 753 HOH A O   1 
HETATM 3431 O O   . HOH C 3 .   ? 36.622 100.542 40.304 1.00 88.64  ? 754 HOH A O   1 
HETATM 3432 O O   . HOH C 3 .   ? 11.141 58.315  10.709 1.00 109.99 ? 755 HOH A O   1 
HETATM 3433 O O   . HOH C 3 .   ? -7.756 76.852  27.379 1.00 97.00  ? 756 HOH A O   1 
HETATM 3434 O O   . HOH C 3 .   ? 23.574 70.499  37.882 1.00 78.68  ? 757 HOH A O   1 
HETATM 3435 O O   . HOH C 3 .   ? 32.862 77.520  46.959 1.00 71.41  ? 758 HOH A O   1 
HETATM 3436 O O   . HOH C 3 .   ? 21.457 91.987  28.935 1.00 91.75  ? 759 HOH A O   1 
HETATM 3437 O O   . HOH C 3 .   ? 41.693 119.632 50.086 1.00 113.67 ? 760 HOH A O   1 
HETATM 3438 O O   . HOH C 3 .   ? 39.007 93.504  58.370 1.00 83.52  ? 761 HOH A O   1 
HETATM 3439 O O   . HOH C 3 .   ? 36.597 94.161  45.580 1.00 72.61  ? 762 HOH A O   1 
HETATM 3440 O O   . HOH C 3 .   ? 34.285 106.890 46.335 1.00 116.10 ? 763 HOH A O   1 
HETATM 3441 O O   . HOH C 3 .   ? 29.921 59.283  16.186 1.00 75.93  ? 764 HOH A O   1 
HETATM 3442 O O   . HOH C 3 .   ? 49.798 108.498 67.485 1.00 97.65  ? 765 HOH A O   1 
HETATM 3443 O O   . HOH C 3 .   ? 41.640 114.389 40.749 1.00 78.84  ? 766 HOH A O   1 
HETATM 3444 O O   . HOH C 3 .   ? 27.428 108.375 27.638 1.00 91.81  ? 767 HOH A O   1 
HETATM 3445 O O   . HOH C 3 .   ? 55.889 98.935  43.519 1.00 89.52  ? 768 HOH A O   1 
HETATM 3446 O O   . HOH C 3 .   ? 14.897 62.947  20.984 1.00 122.76 ? 769 HOH A O   1 
HETATM 3447 O O   . HOH C 3 .   ? 28.439 104.168 55.566 1.00 104.03 ? 770 HOH A O   1 
HETATM 3448 O O   . HOH C 3 .   ? -2.798 99.483  29.742 1.00 90.63  ? 771 HOH A O   1 
HETATM 3449 O O   . HOH C 3 .   ? 35.602 109.784 60.609 1.00 105.84 ? 772 HOH A O   1 
HETATM 3450 O O   . HOH C 3 .   ? 26.727 50.206  20.293 1.00 97.99  ? 773 HOH A O   1 
HETATM 3451 O O   . HOH C 3 .   ? 31.723 64.728  38.845 1.00 82.57  ? 774 HOH A O   1 
HETATM 3452 O O   . HOH C 3 .   ? 43.978 87.742  56.031 1.00 76.16  ? 775 HOH A O   1 
HETATM 3453 O O   . HOH C 3 .   ? 27.433 73.291  26.053 1.00 87.09  ? 776 HOH A O   1 
HETATM 3454 O O   . HOH C 3 .   ? 35.283 69.889  45.670 1.00 68.21  ? 777 HOH A O   1 
HETATM 3455 O O   . HOH C 3 .   ? 37.065 90.187  47.942 1.00 107.25 ? 778 HOH A O   1 
HETATM 3456 O O   . HOH C 3 .   ? 56.695 87.362  52.546 1.00 82.97  ? 779 HOH A O   1 
HETATM 3457 O O   . HOH C 3 .   ? 34.658 97.519  48.787 1.00 129.37 ? 780 HOH A O   1 
HETATM 3458 O O   . HOH C 3 .   ? 59.599 89.701  35.770 1.00 75.80  ? 781 HOH A O   1 
HETATM 3459 O O   . HOH C 3 .   ? 33.655 95.630  40.091 1.00 78.34  ? 782 HOH A O   1 
HETATM 3460 O O   . HOH C 3 .   ? 32.620 94.342  52.355 1.00 104.24 ? 783 HOH A O   1 
HETATM 3461 O O   . HOH C 3 .   ? 37.006 78.954  34.692 1.00 92.04  ? 784 HOH A O   1 
HETATM 3462 O O   . HOH C 3 .   ? 46.569 88.627  33.049 1.00 79.47  ? 785 HOH A O   1 
HETATM 3463 O O   . HOH C 3 .   ? 37.598 121.735 45.419 1.00 97.19  ? 786 HOH A O   1 
HETATM 3464 O O   . HOH C 3 .   ? 13.304 105.973 23.955 1.00 110.11 ? 787 HOH A O   1 
HETATM 3465 O O   . HOH C 3 .   ? 21.566 61.643  9.740  1.00 100.35 ? 788 HOH A O   1 
HETATM 3466 O O   . HOH C 3 .   ? 28.143 68.793  10.908 1.00 100.82 ? 789 HOH A O   1 
HETATM 3467 O O   . HOH C 3 .   ? 38.070 65.233  40.518 1.00 98.14  ? 790 HOH A O   1 
HETATM 3468 O O   . HOH C 3 .   ? 29.383 109.256 31.555 1.00 93.25  ? 791 HOH A O   1 
HETATM 3469 O O   . HOH C 3 .   ? 51.560 89.187  56.930 1.00 87.15  ? 792 HOH A O   1 
HETATM 3470 O O   . HOH C 3 .   ? 35.294 86.918  41.772 1.00 73.27  ? 793 HOH A O   1 
HETATM 3471 O O   . HOH C 3 .   ? 54.905 84.209  44.293 1.00 91.60  ? 794 HOH A O   1 
HETATM 3472 O O   . HOH C 3 .   ? 29.533 125.577 56.310 1.00 86.47  ? 795 HOH A O   1 
HETATM 3473 O O   . HOH C 3 .   ? 39.904 92.540  52.089 1.00 68.07  ? 796 HOH A O   1 
HETATM 3474 O O   . HOH C 3 .   ? 39.443 120.485 66.330 1.00 121.92 ? 797 HOH A O   1 
HETATM 3475 O O   . HOH C 3 .   ? 42.277 101.196 47.571 1.00 85.19  ? 798 HOH A O   1 
HETATM 3476 O O   . HOH C 3 .   ? 11.708 95.170  15.842 1.00 107.60 ? 799 HOH A O   1 
HETATM 3477 O O   . HOH C 3 .   ? 54.980 96.908  46.811 1.00 102.39 ? 800 HOH A O   1 
HETATM 3478 O O   . HOH C 3 .   ? 43.372 100.021 63.123 1.00 88.32  ? 801 HOH A O   1 
HETATM 3479 O O   . HOH C 3 .   ? 21.673 106.245 51.920 1.00 105.78 ? 802 HOH A O   1 
HETATM 3480 O O   . HOH C 3 .   ? 36.825 94.948  38.949 1.00 83.46  ? 803 HOH A O   1 
HETATM 3481 O O   . HOH C 3 .   ? 63.916 101.531 44.734 1.00 93.76  ? 804 HOH A O   1 
HETATM 3482 O O   . HOH C 3 .   ? 18.109 112.564 50.884 1.00 98.88  ? 805 HOH A O   1 
HETATM 3483 O O   . HOH C 3 .   ? 41.543 71.515  49.623 1.00 81.32  ? 806 HOH A O   1 
HETATM 3484 O O   . HOH C 3 .   ? 50.103 91.067  29.467 1.00 91.88  ? 807 HOH A O   1 
HETATM 3485 O O   . HOH C 3 .   ? 34.651 92.470  49.212 1.00 94.98  ? 808 HOH A O   1 
HETATM 3486 O O   . HOH C 3 .   ? 2.172  67.343  12.292 1.00 80.87  ? 809 HOH A O   1 
HETATM 3487 O O   . HOH C 3 .   ? 15.373 99.062  42.496 1.00 85.14  ? 810 HOH A O   1 
HETATM 3488 O O   . HOH C 3 .   ? 30.903 90.027  37.624 1.00 90.02  ? 811 HOH A O   1 
HETATM 3489 O O   . HOH C 3 .   ? 25.714 72.745  34.141 1.00 126.19 ? 812 HOH A O   1 
HETATM 3490 O O   . HOH C 3 .   ? 32.969 103.216 40.998 1.00 79.09  ? 813 HOH A O   1 
HETATM 3491 O O   . HOH C 3 .   ? 14.655 104.578 53.920 1.00 87.26  ? 814 HOH A O   1 
HETATM 3492 O O   . HOH C 3 .   ? 0.281  66.143  28.204 1.00 91.53  ? 815 HOH A O   1 
HETATM 3493 O O   . HOH C 3 .   ? 21.353 90.354  40.145 1.00 102.67 ? 816 HOH A O   1 
HETATM 3494 O O   . HOH C 3 .   ? 12.195 65.198  12.168 1.00 131.59 ? 817 HOH A O   1 
HETATM 3495 O O   . HOH C 3 .   ? 37.240 98.297  37.260 1.00 69.70  ? 818 HOH A O   1 
HETATM 3496 O O   . HOH C 3 .   ? 8.327  82.675  6.626  1.00 89.85  ? 819 HOH A O   1 
HETATM 3497 O O   . HOH C 3 .   ? 35.936 85.207  53.721 1.00 82.41  ? 820 HOH A O   1 
HETATM 3498 O O   . HOH C 3 .   ? 41.438 104.422 40.252 1.00 100.28 ? 821 HOH A O   1 
HETATM 3499 O O   . HOH C 3 .   ? 3.439  86.288  38.926 1.00 97.51  ? 822 HOH A O   1 
HETATM 3500 O O   . HOH C 3 .   ? 31.899 58.556  21.124 1.00 103.79 ? 823 HOH A O   1 
HETATM 3501 O O   . HOH C 3 .   ? 12.853 96.485  21.747 1.00 102.61 ? 824 HOH A O   1 
HETATM 3502 O O   . HOH C 3 .   ? 35.920 127.952 47.680 1.00 89.45  ? 825 HOH A O   1 
HETATM 3503 O O   . HOH C 3 .   ? 51.895 124.368 62.970 1.00 87.45  ? 826 HOH A O   1 
HETATM 3504 O O   . HOH C 3 .   ? 29.128 119.965 67.962 1.00 82.64  ? 827 HOH A O   1 
HETATM 3505 O O   . HOH C 3 .   ? 19.801 50.420  31.627 1.00 100.74 ? 828 HOH A O   1 
HETATM 3506 O O   . HOH C 3 .   ? 7.968  95.472  17.674 1.00 83.59  ? 829 HOH A O   1 
HETATM 3507 O O   . HOH C 3 .   ? 12.368 67.580  38.039 1.00 77.31  ? 830 HOH A O   1 
HETATM 3508 O O   . HOH C 3 .   ? 39.163 74.052  39.555 1.00 85.23  ? 831 HOH A O   1 
HETATM 3509 O O   . HOH C 3 .   ? 16.866 78.734  8.234  1.00 97.55  ? 832 HOH A O   1 
HETATM 3510 O O   . HOH C 3 .   ? 15.631 60.127  11.705 1.00 150.52 ? 833 HOH A O   1 
HETATM 3511 O O   . HOH C 3 .   ? 26.008 85.402  33.912 1.00 89.17  ? 834 HOH A O   1 
HETATM 3512 O O   . HOH C 3 .   ? 13.871 99.589  44.825 1.00 93.04  ? 835 HOH A O   1 
HETATM 3513 O O   . HOH C 3 .   ? 59.050 83.132  44.094 1.00 81.56  ? 836 HOH A O   1 
HETATM 3514 O O   . HOH C 3 .   ? 61.371 107.757 61.085 1.00 92.05  ? 837 HOH A O   1 
HETATM 3515 O O   . HOH C 3 .   ? 40.933 77.504  42.350 1.00 85.74  ? 838 HOH A O   1 
HETATM 3516 O O   . HOH C 3 .   ? 17.800 61.793  37.283 1.00 101.25 ? 839 HOH A O   1 
HETATM 3517 O O   . HOH C 3 .   ? 4.219  106.591 27.468 1.00 110.23 ? 840 HOH A O   1 
HETATM 3518 O O   . HOH C 3 .   ? 36.275 131.897 46.930 1.00 87.23  ? 841 HOH A O   1 
HETATM 3519 O O   . HOH C 3 .   ? 17.127 98.657  23.338 1.00 95.15  ? 842 HOH A O   1 
HETATM 3520 O O   . HOH C 3 .   ? 50.831 120.235 73.250 1.00 115.10 ? 843 HOH A O   1 
HETATM 3521 O O   . HOH C 3 .   ? 33.140 66.062  16.428 1.00 73.05  ? 844 HOH A O   1 
HETATM 3522 O O   . HOH C 3 .   ? 7.446  93.072  12.142 1.00 87.29  ? 845 HOH A O   1 
HETATM 3523 O O   . HOH C 3 .   ? 29.589 116.088 62.175 1.00 83.68  ? 846 HOH A O   1 
HETATM 3524 O O   . HOH C 3 .   ? 35.286 66.962  36.229 1.00 87.40  ? 847 HOH A O   1 
HETATM 3525 O O   . HOH C 3 .   ? 35.881 103.862 57.363 1.00 76.26  ? 848 HOH A O   1 
HETATM 3526 O O   . HOH C 3 .   ? 10.307 63.681  24.474 1.00 83.88  ? 849 HOH A O   1 
HETATM 3527 O O   . HOH C 3 .   ? 32.071 96.121  43.850 1.00 100.52 ? 850 HOH A O   1 
HETATM 3528 O O   . HOH C 3 .   ? 19.340 102.841 22.900 1.00 100.06 ? 851 HOH A O   1 
HETATM 3529 O O   . HOH C 3 .   ? 22.714 89.817  27.628 1.00 110.33 ? 852 HOH A O   1 
HETATM 3530 O O   . HOH C 3 .   ? 24.832 99.312  47.687 1.00 81.73  ? 853 HOH A O   1 
HETATM 3531 O O   . HOH C 3 .   ? 44.637 126.444 50.819 1.00 94.32  ? 854 HOH A O   1 
HETATM 3532 O O   . HOH C 3 .   ? 33.046 72.258  17.796 1.00 96.25  ? 855 HOH A O   1 
HETATM 3533 O O   . HOH C 3 .   ? 19.088 55.777  9.102  1.00 111.85 ? 856 HOH A O   1 
HETATM 3534 O O   . HOH C 3 .   ? 24.378 123.988 65.100 1.00 81.60  ? 857 HOH A O   1 
HETATM 3535 O O   . HOH C 3 .   ? 50.723 109.879 50.823 1.00 108.90 ? 858 HOH A O   1 
HETATM 3536 O O   . HOH C 3 .   ? 5.032  104.044 23.037 1.00 91.17  ? 859 HOH A O   1 
HETATM 3537 O O   . HOH C 3 .   ? 31.424 81.669  39.616 1.00 175.97 ? 860 HOH A O   1 
HETATM 3538 O O   . HOH C 3 .   ? 26.301 91.484  48.143 1.00 82.30  ? 861 HOH A O   1 
HETATM 3539 O O   . HOH C 3 .   ? 56.175 80.908  34.017 1.00 77.25  ? 862 HOH A O   1 
HETATM 3540 O O   . HOH C 3 .   ? 17.635 94.437  15.546 1.00 78.47  ? 863 HOH A O   1 
HETATM 3541 O O   . HOH C 3 .   ? 17.377 66.285  35.514 1.00 91.76  ? 864 HOH A O   1 
HETATM 3542 O O   . HOH C 3 .   ? 32.862 130.573 55.570 1.00 70.89  ? 865 HOH A O   1 
HETATM 3543 O O   . HOH C 3 .   ? 1.078  92.478  33.156 1.00 97.10  ? 866 HOH A O   1 
HETATM 3544 O O   . HOH C 3 .   ? 33.032 86.822  48.059 1.00 81.80  ? 867 HOH A O   1 
HETATM 3545 O O   . HOH C 3 .   ? 5.373  69.807  25.275 1.00 99.87  ? 868 HOH A O   1 
HETATM 3546 O O   . HOH C 3 .   ? 34.302 113.363 62.895 1.00 79.74  ? 869 HOH A O   1 
HETATM 3547 O O   . HOH C 3 .   ? -4.678 77.040  29.721 1.00 82.61  ? 870 HOH A O   1 
HETATM 3548 O O   . HOH C 3 .   ? 22.729 85.083  42.048 1.00 117.96 ? 871 HOH A O   1 
HETATM 3549 O O   . HOH C 3 .   ? 20.786 76.839  41.842 1.00 81.44  ? 872 HOH A O   1 
HETATM 3550 O O   . HOH C 3 .   ? 53.876 119.932 72.648 1.00 84.46  ? 873 HOH A O   1 
HETATM 3551 O O   . HOH C 3 .   ? 45.881 118.646 67.021 1.00 121.61 ? 874 HOH A O   1 
HETATM 3552 O O   . HOH C 3 .   ? 32.886 79.256  48.595 1.00 89.49  ? 875 HOH A O   1 
HETATM 3553 O O   . HOH C 3 .   ? 26.251 72.215  43.280 1.00 66.84  ? 876 HOH A O   1 
HETATM 3554 O O   . HOH C 3 .   ? 34.593 61.215  19.326 1.00 88.09  ? 877 HOH A O   1 
HETATM 3555 O O   . HOH C 3 .   ? 34.081 71.377  47.547 1.00 113.24 ? 878 HOH A O   1 
HETATM 3556 O O   . HOH C 3 .   ? 16.935 73.712  40.200 1.00 89.86  ? 879 HOH A O   1 
HETATM 3557 O O   . HOH C 3 .   ? 15.699 57.451  26.987 1.00 82.21  ? 880 HOH A O   1 
HETATM 3558 O O   . HOH C 3 .   ? 58.990 79.309  32.052 1.00 81.08  ? 881 HOH A O   1 
HETATM 3559 O O   . HOH C 3 .   ? 46.173 75.424  33.822 1.00 94.13  ? 882 HOH A O   1 
HETATM 3560 O O   . HOH C 3 .   ? 38.874 119.772 50.383 1.00 111.25 ? 883 HOH A O   1 
HETATM 3561 O O   . HOH C 3 .   ? 33.617 65.423  37.239 1.00 82.97  ? 884 HOH A O   1 
HETATM 3562 O O   . HOH C 3 .   ? 34.175 100.065 39.781 1.00 87.58  ? 885 HOH A O   1 
HETATM 3563 O O   . HOH C 3 .   ? 28.009 75.232  13.551 1.00 94.33  ? 886 HOH A O   1 
HETATM 3564 O O   . HOH C 3 .   ? 28.285 93.529  40.644 1.00 89.72  ? 887 HOH A O   1 
HETATM 3565 O O   . HOH C 3 .   ? 3.148  108.913 29.659 1.00 87.13  ? 888 HOH A O   1 
HETATM 3566 O O   . HOH C 3 .   ? 47.667 75.269  41.304 1.00 87.65  ? 889 HOH A O   1 
HETATM 3567 O O   . HOH C 3 .   ? 36.275 74.971  48.188 1.00 113.69 ? 890 HOH A O   1 
HETATM 3568 O O   . HOH C 3 .   ? 14.236 73.370  38.985 1.00 97.46  ? 891 HOH A O   1 
HETATM 3569 O O   . HOH C 3 .   ? -3.106 89.593  29.499 1.00 86.54  ? 892 HOH A O   1 
HETATM 3570 O O   . HOH C 3 .   ? 13.897 47.021  28.879 1.00 67.81  ? 893 HOH A O   1 
HETATM 3571 O O   . HOH C 3 .   ? 6.833  105.042 20.403 1.00 84.57  ? 894 HOH A O   1 
HETATM 3572 O O   . HOH C 3 .   ? 29.604 90.651  56.101 1.00 80.87  ? 895 HOH A O   1 
HETATM 3573 O O   . HOH C 3 .   ? 1.702  104.566 21.857 1.00 81.00  ? 896 HOH A O   1 
HETATM 3574 O O   . HOH C 3 .   ? 30.639 101.351 58.973 1.00 94.58  ? 897 HOH A O   1 
HETATM 3575 O O   . HOH C 3 .   ? 48.861 114.263 50.399 1.00 90.18  ? 898 HOH A O   1 
HETATM 3576 O O   . HOH C 3 .   ? 40.434 76.975  39.637 1.00 71.25  ? 899 HOH A O   1 
HETATM 3577 O O   . HOH C 3 .   ? 33.242 108.080 60.603 1.00 97.35  ? 900 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ILE 1   25  ?   ?   ?   A . n 
A 1 2   GLU 2   26  ?   ?   ?   A . n 
A 1 3   ILE 3   27  ?   ?   ?   A . n 
A 1 4   PRO 4   28  ?   ?   ?   A . n 
A 1 5   MET 5   29  ?   ?   ?   A . n 
A 1 6   ASP 6   30  ?   ?   ?   A . n 
A 1 7   PRO 7   31  ?   ?   ?   A . n 
A 1 8   SER 8   32  ?   ?   ?   A . n 
A 1 9   ILE 9   33  ?   ?   ?   A . n 
A 1 10  GLN 10  34  ?   ?   ?   A . n 
A 1 11  ASN 11  35  ?   ?   ?   A . n 
A 1 12  GLU 12  36  ?   ?   ?   A . n 
A 1 13  LEU 13  37  37  LEU LEU A . n 
A 1 14  THR 14  38  38  THR THR A . n 
A 1 15  GLN 15  39  39  GLN GLN A . n 
A 1 16  PRO 16  40  40  PRO PRO A . n 
A 1 17  PRO 17  41  41  PRO PRO A . n 
A 1 18  THR 18  42  42  THR THR A . n 
A 1 19  ILE 19  43  43  ILE ILE A . n 
A 1 20  THR 20  44  44  THR THR A . n 
A 1 21  LYS 21  45  45  LYS LYS A . n 
A 1 22  GLN 22  46  46  GLN GLN A . n 
A 1 23  SER 23  47  47  SER SER A . n 
A 1 24  ALA 24  48  48  ALA ALA A . n 
A 1 25  LYS 25  49  49  LYS LYS A . n 
A 1 26  ASP 26  50  50  ASP ASP A . n 
A 1 27  HIS 27  51  51  HIS HIS A . n 
A 1 28  ILE 28  52  52  ILE ILE A . n 
A 1 29  VAL 29  53  53  VAL VAL A . n 
A 1 30  ASP 30  54  54  ASP ASP A . n 
A 1 31  PRO 31  55  55  PRO PRO A . n 
A 1 32  ARG 32  56  56  ARG ARG A . n 
A 1 33  ASP 33  57  57  ASP ASP A . n 
A 1 34  ASN 34  58  58  ASN ASN A . n 
A 1 35  ILE 35  59  59  ILE ILE A . n 
A 1 36  LEU 36  60  60  LEU LEU A . n 
A 1 37  ILE 37  61  61  ILE ILE A . n 
A 1 38  GLU 38  62  62  GLU GLU A . n 
A 1 39  CYS 39  63  63  CYS CYS A . n 
A 1 40  GLU 40  64  64  GLU GLU A . n 
A 1 41  ALA 41  65  65  ALA ALA A . n 
A 1 42  LYS 42  66  66  LYS LYS A . n 
A 1 43  GLY 43  67  67  GLY GLY A . n 
A 1 44  ASN 44  68  68  ASN ASN A . n 
A 1 45  PRO 45  69  69  PRO PRO A . n 
A 1 46  ALA 46  70  70  ALA ALA A . n 
A 1 47  PRO 47  71  71  PRO PRO A . n 
A 1 48  SER 48  72  72  SER SER A . n 
A 1 49  PHE 49  73  73  PHE PHE A . n 
A 1 50  HIS 50  74  74  HIS HIS A . n 
A 1 51  TRP 51  75  75  TRP TRP A . n 
A 1 52  THR 52  76  76  THR THR A . n 
A 1 53  ARG 53  77  77  ARG ARG A . n 
A 1 54  ASN 54  78  78  ASN ASN A . n 
A 1 55  SER 55  79  79  SER SER A . n 
A 1 56  ARG 56  80  80  ARG ARG A . n 
A 1 57  PHE 57  81  81  PHE PHE A . n 
A 1 58  PHE 58  82  82  PHE PHE A . n 
A 1 59  ASN 59  83  83  ASN ASN A . n 
A 1 60  ILE 60  84  84  ILE ILE A . n 
A 1 61  ALA 61  85  85  ALA ALA A . n 
A 1 62  LYS 62  86  86  LYS LYS A . n 
A 1 63  ASP 63  87  87  ASP ASP A . n 
A 1 64  PRO 64  88  88  PRO PRO A . n 
A 1 65  ARG 65  89  89  ARG ARG A . n 
A 1 66  VAL 66  90  90  VAL VAL A . n 
A 1 67  SER 67  91  91  SER SER A . n 
A 1 68  MET 68  92  92  MET MET A . n 
A 1 69  ARG 69  93  93  ARG ARG A . n 
A 1 70  ARG 70  94  94  ARG ARG A . n 
A 1 71  ARG 71  95  95  ARG ARG A . n 
A 1 72  SER 72  96  96  SER SER A . n 
A 1 73  GLY 73  97  97  GLY GLY A . n 
A 1 74  THR 74  98  98  THR THR A . n 
A 1 75  LEU 75  99  99  LEU LEU A . n 
A 1 76  VAL 76  100 100 VAL VAL A . n 
A 1 77  ILE 77  101 101 ILE ILE A . n 
A 1 78  ASP 78  102 102 ASP ASP A . n 
A 1 79  PHE 79  103 103 PHE PHE A . n 
A 1 80  ARG 80  104 104 ARG ARG A . n 
A 1 81  SER 81  105 105 SER SER A . n 
A 1 82  GLY 82  106 106 GLY GLY A . n 
A 1 83  GLY 83  107 107 GLY GLY A . n 
A 1 84  ARG 84  108 108 ARG ARG A . n 
A 1 85  PRO 85  109 109 PRO PRO A . n 
A 1 86  GLU 86  110 110 GLU GLU A . n 
A 1 87  GLU 87  111 111 GLU GLU A . n 
A 1 88  TYR 88  112 112 TYR TYR A . n 
A 1 89  GLU 89  113 113 GLU GLU A . n 
A 1 90  GLY 90  114 114 GLY GLY A . n 
A 1 91  GLU 91  115 115 GLU GLU A . n 
A 1 92  TYR 92  116 116 TYR TYR A . n 
A 1 93  GLN 93  117 117 GLN GLN A . n 
A 1 94  CYS 94  118 118 CYS CYS A . n 
A 1 95  PHE 95  119 119 PHE PHE A . n 
A 1 96  ALA 96  120 120 ALA ALA A . n 
A 1 97  ARG 97  121 121 ARG ARG A . n 
A 1 98  ASN 98  122 122 ASN ASN A . n 
A 1 99  LYS 99  123 123 LYS LYS A . n 
A 1 100 PHE 100 124 124 PHE PHE A . n 
A 1 101 GLY 101 125 125 GLY GLY A . n 
A 1 102 THR 102 126 126 THR THR A . n 
A 1 103 ALA 103 127 127 ALA ALA A . n 
A 1 104 LEU 104 128 128 LEU LEU A . n 
A 1 105 SER 105 129 129 SER SER A . n 
A 1 106 ASN 106 130 130 ASN ASN A . n 
A 1 107 ARG 107 131 131 ARG ARG A . n 
A 1 108 ILE 108 132 132 ILE ILE A . n 
A 1 109 ARG 109 133 133 ARG ARG A . n 
A 1 110 LEU 110 134 134 LEU LEU A . n 
A 1 111 GLN 111 135 135 GLN GLN A . n 
A 1 112 VAL 112 136 136 VAL VAL A . n 
A 1 113 SER 113 137 137 SER SER A . n 
A 1 114 LYS 114 138 138 LYS LYS A . n 
A 1 115 SER 115 139 139 SER SER A . n 
A 1 116 PRO 116 140 140 PRO PRO A . n 
A 1 117 LEU 117 141 141 LEU LEU A . n 
A 1 118 TRP 118 142 142 TRP TRP A . n 
A 1 119 PRO 119 143 143 PRO PRO A . n 
A 1 120 LYS 120 144 144 LYS LYS A . n 
A 1 121 GLU 121 145 145 GLU GLU A . n 
A 1 122 ASN 122 146 146 ASN ASN A . n 
A 1 123 LEU 123 147 147 LEU LEU A . n 
A 1 124 ASP 124 148 148 ASP ASP A . n 
A 1 125 PRO 125 149 149 PRO PRO A . n 
A 1 126 VAL 126 150 150 VAL VAL A . n 
A 1 127 VAL 127 151 151 VAL VAL A . n 
A 1 128 VAL 128 152 152 VAL VAL A . n 
A 1 129 GLN 129 153 153 GLN GLN A . n 
A 1 130 GLU 130 154 154 GLU GLU A . n 
A 1 131 GLY 131 155 155 GLY GLY A . n 
A 1 132 ALA 132 156 156 ALA ALA A . n 
A 1 133 PRO 133 157 157 PRO PRO A . n 
A 1 134 LEU 134 158 158 LEU LEU A . n 
A 1 135 THR 135 159 159 THR THR A . n 
A 1 136 LEU 136 160 160 LEU LEU A . n 
A 1 137 GLN 137 161 161 GLN GLN A . n 
A 1 138 CYS 138 162 162 CYS CYS A . n 
A 1 139 ASN 139 163 163 ASN ASN A . n 
A 1 140 PRO 140 164 164 PRO PRO A . n 
A 1 141 PRO 141 165 165 PRO PRO A . n 
A 1 142 PRO 142 166 166 PRO PRO A . n 
A 1 143 GLY 143 167 167 GLY GLY A . n 
A 1 144 LEU 144 168 168 LEU LEU A . n 
A 1 145 PRO 145 169 169 PRO PRO A . n 
A 1 146 SER 146 170 170 SER SER A . n 
A 1 147 PRO 147 171 171 PRO PRO A . n 
A 1 148 VAL 148 172 172 VAL VAL A . n 
A 1 149 ILE 149 173 173 ILE ILE A . n 
A 1 150 PHE 150 174 174 PHE PHE A . n 
A 1 151 TRP 151 175 175 TRP TRP A . n 
A 1 152 MET 152 176 176 MET MET A . n 
A 1 153 SER 153 177 177 SER SER A . n 
A 1 154 SER 154 178 178 SER SER A . n 
A 1 155 SER 155 179 179 SER SER A . n 
A 1 156 MET 156 180 180 MET MET A . n 
A 1 157 GLU 157 181 181 GLU GLU A . n 
A 1 158 PRO 158 182 182 PRO PRO A . n 
A 1 159 ILE 159 183 183 ILE ILE A . n 
A 1 160 THR 160 184 184 THR THR A . n 
A 1 161 GLN 161 185 185 GLN GLN A . n 
A 1 162 ASP 162 186 186 ASP ASP A . n 
A 1 163 LYS 163 187 187 LYS LYS A . n 
A 1 164 ARG 164 188 188 ARG ARG A . n 
A 1 165 VAL 165 189 189 VAL VAL A . n 
A 1 166 SER 166 190 190 SER SER A . n 
A 1 167 GLN 167 191 191 GLN GLN A . n 
A 1 168 GLY 168 192 192 GLY GLY A . n 
A 1 169 HIS 169 193 193 HIS HIS A . n 
A 1 170 ASN 170 194 194 ASN ASN A . n 
A 1 171 GLY 171 195 195 GLY GLY A . n 
A 1 172 ASP 172 196 196 ASP ASP A . n 
A 1 173 LEU 173 197 197 LEU LEU A . n 
A 1 174 TYR 174 198 198 TYR TYR A . n 
A 1 175 PHE 175 199 199 PHE PHE A . n 
A 1 176 SER 176 200 200 SER SER A . n 
A 1 177 ASN 177 201 201 ASN ASN A . n 
A 1 178 VAL 178 202 202 VAL VAL A . n 
A 1 179 MET 179 203 203 MET MET A . n 
A 1 180 LEU 180 204 204 LEU LEU A . n 
A 1 181 GLN 181 205 205 GLN GLN A . n 
A 1 182 ASP 182 206 206 ASP ASP A . n 
A 1 183 MET 183 207 207 MET MET A . n 
A 1 184 GLN 184 208 208 GLN GLN A . n 
A 1 185 THR 185 209 209 THR THR A . n 
A 1 186 ASP 186 210 210 ASP ASP A . n 
A 1 187 TYR 187 211 211 TYR TYR A . n 
A 1 188 SER 188 212 212 SER SER A . n 
A 1 189 CYS 189 213 213 CYS CYS A . n 
A 1 190 ASN 190 214 214 ASN ASN A . n 
A 1 191 ALA 191 215 215 ALA ALA A . n 
A 1 192 ARG 192 216 216 ARG ARG A . n 
A 1 193 PHE 193 217 217 PHE PHE A . n 
A 1 194 HIS 194 218 218 HIS HIS A . n 
A 1 195 PHE 195 219 219 PHE PHE A . n 
A 1 196 THR 196 220 220 THR THR A . n 
A 1 197 HIS 197 221 221 HIS HIS A . n 
A 1 198 THR 198 222 222 THR THR A . n 
A 1 199 ILE 199 223 223 ILE ILE A . n 
A 1 200 GLN 200 224 224 GLN GLN A . n 
A 1 201 GLN 201 225 225 GLN GLN A . n 
A 1 202 LYS 202 226 226 LYS LYS A . n 
A 1 203 ASN 203 227 227 ASN ASN A . n 
A 1 204 PRO 204 228 228 PRO PRO A . n 
A 1 205 PHE 205 229 229 PHE PHE A . n 
A 1 206 THR 206 230 230 THR THR A . n 
A 1 207 LEU 207 231 231 LEU LEU A . n 
A 1 208 LYS 208 232 232 LYS LYS A . n 
A 1 209 VAL 209 233 233 VAL VAL A . n 
A 1 210 LEU 210 234 234 LEU LEU A . n 
A 1 211 THR 211 235 235 THR THR A . n 
A 1 212 THR 212 236 236 THR THR A . n 
A 1 213 ARG 213 237 237 ARG ARG A . n 
A 1 214 GLY 214 238 238 GLY GLY A . n 
A 1 215 VAL 215 239 239 VAL VAL A . n 
A 1 216 ALA 216 240 240 ALA ALA A . n 
A 1 217 GLU 217 241 241 GLU GLU A . n 
A 1 218 ARG 218 242 242 ARG ARG A . n 
A 1 219 THR 219 243 243 THR THR A . n 
A 1 220 PRO 220 244 244 PRO PRO A . n 
A 1 221 SER 221 245 245 SER SER A . n 
A 1 222 PHE 222 246 246 PHE PHE A . n 
A 1 223 MET 223 247 247 MET MET A . n 
A 1 224 TYR 224 248 248 TYR TYR A . n 
A 1 225 PRO 225 249 249 PRO PRO A . n 
A 1 226 GLN 226 250 250 GLN GLN A . n 
A 1 227 GLY 227 251 251 GLY GLY A . n 
A 1 228 THR 228 252 252 THR THR A . n 
A 1 229 ALA 229 253 253 ALA ALA A . n 
A 1 230 SER 230 254 254 SER SER A . n 
A 1 231 SER 231 255 255 SER SER A . n 
A 1 232 GLN 232 256 256 GLN GLN A . n 
A 1 233 MET 233 257 257 MET MET A . n 
A 1 234 VAL 234 258 258 VAL VAL A . n 
A 1 235 LEU 235 259 259 LEU LEU A . n 
A 1 236 ARG 236 260 260 ARG ARG A . n 
A 1 237 GLY 237 261 261 GLY GLY A . n 
A 1 238 MET 238 262 262 MET MET A . n 
A 1 239 ASP 239 263 263 ASP ASP A . n 
A 1 240 LEU 240 264 264 LEU LEU A . n 
A 1 241 LEU 241 265 265 LEU LEU A . n 
A 1 242 LEU 242 266 266 LEU LEU A . n 
A 1 243 GLU 243 267 267 GLU GLU A . n 
A 1 244 CYS 244 268 268 CYS CYS A . n 
A 1 245 ILE 245 269 269 ILE ILE A . n 
A 1 246 ALA 246 270 270 ALA ALA A . n 
A 1 247 SER 247 271 271 SER SER A . n 
A 1 248 GLY 248 272 272 GLY GLY A . n 
A 1 249 VAL 249 273 273 VAL VAL A . n 
A 1 250 PRO 250 274 274 PRO PRO A . n 
A 1 251 THR 251 275 275 THR THR A . n 
A 1 252 PRO 252 276 276 PRO PRO A . n 
A 1 253 ASP 253 277 277 ASP ASP A . n 
A 1 254 ILE 254 278 278 ILE ILE A . n 
A 1 255 ALA 255 279 279 ALA ALA A . n 
A 1 256 TRP 256 280 280 TRP TRP A . n 
A 1 257 TYR 257 281 281 TYR TYR A . n 
A 1 258 LYS 258 282 282 LYS LYS A . n 
A 1 259 LYS 259 283 283 LYS LYS A . n 
A 1 260 GLY 260 284 284 GLY GLY A . n 
A 1 261 GLY 261 285 285 GLY GLY A . n 
A 1 262 ASP 262 286 286 ASP ASP A . n 
A 1 263 LEU 263 287 287 LEU LEU A . n 
A 1 264 PRO 264 288 288 PRO PRO A . n 
A 1 265 SER 265 289 289 SER SER A . n 
A 1 266 ASP 266 290 290 ASP ASP A . n 
A 1 267 LYS 267 291 291 LYS LYS A . n 
A 1 268 ALA 268 292 292 ALA ALA A . n 
A 1 269 LYS 269 293 293 LYS LYS A . n 
A 1 270 PHE 270 294 294 PHE PHE A . n 
A 1 271 GLU 271 295 295 GLU GLU A . n 
A 1 272 ASN 272 296 296 ASN ASN A . n 
A 1 273 PHE 273 297 297 PHE PHE A . n 
A 1 274 ASN 274 298 298 ASN ASN A . n 
A 1 275 LYS 275 299 299 LYS LYS A . n 
A 1 276 ALA 276 300 300 ALA ALA A . n 
A 1 277 LEU 277 301 301 LEU LEU A . n 
A 1 278 ARG 278 302 302 ARG ARG A . n 
A 1 279 ILE 279 303 303 ILE ILE A . n 
A 1 280 THR 280 304 304 THR THR A . n 
A 1 281 ASN 281 305 305 ASN ASN A . n 
A 1 282 VAL 282 306 306 VAL VAL A . n 
A 1 283 SER 283 307 307 SER SER A . n 
A 1 284 GLU 284 308 308 GLU GLU A . n 
A 1 285 GLU 285 309 309 GLU GLU A . n 
A 1 286 ASP 286 310 310 ASP ASP A . n 
A 1 287 SER 287 311 311 SER SER A . n 
A 1 288 GLY 288 312 312 GLY GLY A . n 
A 1 289 GLU 289 313 313 GLU GLU A . n 
A 1 290 TYR 290 314 314 TYR TYR A . n 
A 1 291 PHE 291 315 315 PHE PHE A . n 
A 1 292 CYS 292 316 316 CYS CYS A . n 
A 1 293 LEU 293 317 317 LEU LEU A . n 
A 1 294 ALA 294 318 318 ALA ALA A . n 
A 1 295 SER 295 319 319 SER SER A . n 
A 1 296 ASN 296 320 320 ASN ASN A . n 
A 1 297 LYS 297 321 321 LYS LYS A . n 
A 1 298 MET 298 322 322 MET MET A . n 
A 1 299 GLY 299 323 323 GLY GLY A . n 
A 1 300 SER 300 324 324 SER SER A . n 
A 1 301 ILE 301 325 325 ILE ILE A . n 
A 1 302 ARG 302 326 326 ARG ARG A . n 
A 1 303 HIS 303 327 327 HIS HIS A . n 
A 1 304 THR 304 328 328 THR THR A . n 
A 1 305 ILE 305 329 329 ILE ILE A . n 
A 1 306 SER 306 330 330 SER SER A . n 
A 1 307 VAL 307 331 331 VAL VAL A . n 
A 1 308 ARG 308 332 332 ARG ARG A . n 
A 1 309 VAL 309 333 333 VAL VAL A . n 
A 1 310 LYS 310 334 334 LYS LYS A . n 
A 1 311 ALA 311 335 335 ALA ALA A . n 
A 1 312 ALA 312 336 336 ALA ALA A . n 
A 1 313 PRO 313 337 337 PRO PRO A . n 
A 1 314 TYR 314 338 338 TYR TYR A . n 
A 1 315 TRP 315 339 339 TRP TRP A . n 
A 1 316 LEU 316 340 340 LEU LEU A . n 
A 1 317 ASP 317 341 341 ASP ASP A . n 
A 1 318 GLU 318 342 342 GLU GLU A . n 
A 1 319 PRO 319 343 343 PRO PRO A . n 
A 1 320 LYS 320 344 344 LYS LYS A . n 
A 1 321 ASN 321 345 345 ASN ASN A . n 
A 1 322 LEU 322 346 346 LEU LEU A . n 
A 1 323 ILE 323 347 347 ILE ILE A . n 
A 1 324 LEU 324 348 348 LEU LEU A . n 
A 1 325 ALA 325 349 349 ALA ALA A . n 
A 1 326 PRO 326 350 350 PRO PRO A . n 
A 1 327 GLY 327 351 351 GLY GLY A . n 
A 1 328 GLU 328 352 352 GLU GLU A . n 
A 1 329 ASP 329 353 353 ASP ASP A . n 
A 1 330 GLY 330 354 354 GLY GLY A . n 
A 1 331 ARG 331 355 355 ARG ARG A . n 
A 1 332 LEU 332 356 356 LEU LEU A . n 
A 1 333 VAL 333 357 357 VAL VAL A . n 
A 1 334 CYS 334 358 358 CYS CYS A . n 
A 1 335 ARG 335 359 359 ARG ARG A . n 
A 1 336 ALA 336 360 360 ALA ALA A . n 
A 1 337 ASN 337 361 361 ASN ASN A . n 
A 1 338 GLY 338 362 362 GLY GLY A . n 
A 1 339 ASN 339 363 363 ASN ASN A . n 
A 1 340 PRO 340 364 364 PRO PRO A . n 
A 1 341 LYS 341 365 365 LYS LYS A . n 
A 1 342 PRO 342 366 366 PRO PRO A . n 
A 1 343 THR 343 367 367 THR THR A . n 
A 1 344 VAL 344 368 368 VAL VAL A . n 
A 1 345 GLN 345 369 369 GLN GLN A . n 
A 1 346 TRP 346 370 370 TRP TRP A . n 
A 1 347 MET 347 371 371 MET MET A . n 
A 1 348 VAL 348 372 372 VAL VAL A . n 
A 1 349 ASN 349 373 373 ASN ASN A . n 
A 1 350 GLY 350 374 374 GLY GLY A . n 
A 1 351 GLU 351 375 375 GLU GLU A . n 
A 1 352 PRO 352 376 376 PRO PRO A . n 
A 1 353 LEU 353 377 377 LEU LEU A . n 
A 1 354 GLN 354 378 378 GLN GLN A . n 
A 1 355 SER 355 379 379 SER SER A . n 
A 1 356 ALA 356 380 380 ALA ALA A . n 
A 1 357 PRO 357 381 381 PRO PRO A . n 
A 1 358 PRO 358 382 382 PRO PRO A . n 
A 1 359 ASN 359 383 383 ASN ASN A . n 
A 1 360 PRO 360 384 384 PRO PRO A . n 
A 1 361 ASN 361 385 385 ASN ASN A . n 
A 1 362 ARG 362 386 386 ARG ARG A . n 
A 1 363 GLU 363 387 387 GLU GLU A . n 
A 1 364 VAL 364 388 388 VAL VAL A . n 
A 1 365 ALA 365 389 389 ALA ALA A . n 
A 1 366 GLY 366 390 390 GLY GLY A . n 
A 1 367 ASP 367 391 391 ASP ASP A . n 
A 1 368 THR 368 392 392 THR THR A . n 
A 1 369 ILE 369 393 393 ILE ILE A . n 
A 1 370 ILE 370 394 394 ILE ILE A . n 
A 1 371 PHE 371 395 395 PHE PHE A . n 
A 1 372 ARG 372 396 396 ARG ARG A . n 
A 1 373 ASP 373 397 397 ASP ASP A . n 
A 1 374 THR 374 398 398 THR THR A . n 
A 1 375 GLN 375 399 399 GLN GLN A . n 
A 1 376 ILE 376 400 400 ILE ILE A . n 
A 1 377 SER 377 401 401 SER SER A . n 
A 1 378 SER 378 402 402 SER SER A . n 
A 1 379 ARG 379 403 403 ARG ARG A . n 
A 1 380 ALA 380 404 404 ALA ALA A . n 
A 1 381 VAL 381 405 405 VAL VAL A . n 
A 1 382 TYR 382 406 406 TYR TYR A . n 
A 1 383 GLN 383 407 407 GLN GLN A . n 
A 1 384 CYS 384 408 408 CYS CYS A . n 
A 1 385 ASN 385 409 409 ASN ASN A . n 
A 1 386 THR 386 410 410 THR THR A . n 
A 1 387 SER 387 411 411 SER SER A . n 
A 1 388 ASN 388 412 412 ASN ASN A . n 
A 1 389 GLU 389 413 413 GLU GLU A . n 
A 1 390 HIS 390 414 414 HIS HIS A . n 
A 1 391 GLY 391 415 415 GLY GLY A . n 
A 1 392 TYR 392 416 416 TYR TYR A . n 
A 1 393 LEU 393 417 417 LEU LEU A . n 
A 1 394 LEU 394 418 418 LEU LEU A . n 
A 1 395 ALA 395 419 419 ALA ALA A . n 
A 1 396 ASN 396 420 420 ASN ASN A . n 
A 1 397 ALA 397 421 421 ALA ALA A . n 
A 1 398 PHE 398 422 422 PHE PHE A . n 
A 1 399 VAL 399 423 423 VAL VAL A . n 
A 1 400 SER 400 424 424 SER SER A . n 
A 1 401 VAL 401 425 425 VAL VAL A . n 
A 1 402 LEU 402 426 426 LEU LEU A . n 
A 1 403 ASP 403 427 ?   ?   ?   A . n 
A 1 404 VAL 404 428 ?   ?   ?   A . n 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    ASN 
_pdbx_struct_mod_residue.label_seq_id     385 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     ASN 
_pdbx_struct_mod_residue.auth_seq_id      409 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   ASN 
_pdbx_struct_mod_residue.details          '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_defined_assembly   ?    dimeric   2 
2 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 1,2 A,B,C 
2 1   A,B,C 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000 0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_565 x,x-y+1,-z+5/6 0.5000000000 0.8660254038 0.0000000000 -85.7125000000 0.8660254038 
-0.5000000000 0.0000000000 148.4584048437 0.0000000000 0.0000000000 -1.0000000000 73.1600000000 
# 
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 2010-11-03 
2 'Structure model' 1 1 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .   ? 1 
SOLVE    phasing           .   ? 2 
CNS      refinement        1.1 ? 3 
HKL-2000 'data reduction'  .   ? 4 
HKL-2000 'data scaling'    .   ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 456 ? ? O  A HOH 762 ? ? 2.00 
2  1 O   A HOH 526 ? ? O  A HOH 778 ? ? 2.02 
3  1 N   A ASP 397 ? ? O  A HOH 773 ? ? 2.03 
4  1 O   A HOH 483 ? ? O  A HOH 524 ? ? 2.06 
5  1 OD1 A ASN 409 ? ? O  A HOH 812 ? ? 2.07 
6  1 ND2 A ASN 409 ? ? O5 A NAG 1   ? ? 2.08 
7  1 O   A ARG 133 ? ? O  A HOH 431 ? ? 2.08 
8  1 O   A LEU 417 ? ? O  A HOH 812 ? ? 2.08 
9  1 N   A THR 410 ? ? O  A HOH 812 ? ? 2.10 
10 1 O   A HOH 570 ? ? O  A HOH 764 ? ? 2.10 
11 1 O   A HOH 3   ? ? O  A HOH 765 ? ? 2.10 
12 1 O   A HOH 7   ? ? O  A HOH 780 ? ? 2.11 
13 1 O   A HOH 565 ? ? O  A HOH 890 ? ? 2.11 
14 1 O   A HOH 434 ? ? O  A HOH 659 ? ? 2.12 
15 1 O   A HOH 18  ? ? O  A HOH 736 ? ? 2.12 
16 1 O   A HOH 496 ? ? O  A HOH 852 ? ? 2.13 
17 1 O   A HOH 16  ? ? O  A HOH 533 ? ? 2.14 
18 1 O   A LYS 123 ? ? O  A HOH 485 ? ? 2.14 
19 1 O   A HOH 434 ? ? O  A HOH 598 ? ? 2.15 
20 1 O   A HOH 532 ? ? O  A HOH 852 ? ? 2.16 
21 1 NE2 A GLN 185 ? ? O  A HOH 495 ? ? 2.19 
22 1 O   A HOH 22  ? ? O  A HOH 802 ? ? 2.19 
# 
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 N A ALA 85 ? ? CA A ALA 85 ? ? C  A ALA 85 ? ? 130.03 111.00 19.03  2.70 N 
2 1 N A LYS 86 ? ? CA A LYS 86 ? ? CB A LYS 86 ? ? 98.14  110.60 -12.46 1.80 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 38  ? ? -69.63  75.48   
2  1 PRO A 40  ? ? -58.60  172.02  
3  1 PRO A 55  ? ? -58.50  3.50    
4  1 ARG A 56  ? ? -67.50  -109.23 
5  1 CYS A 63  ? ? -167.62 116.45  
6  1 SER A 79  ? ? 69.79   -0.23   
7  1 ALA A 85  ? ? -39.14  -27.62  
8  1 ARG A 95  ? ? 53.04   16.66   
9  1 ARG A 104 ? ? -61.56  0.76    
10 1 SER A 137 ? ? -68.25  94.72   
11 1 ASN A 163 ? ? 52.87   74.79   
12 1 PRO A 166 ? ? -45.25  -95.68  
13 1 ASP A 206 ? ? -66.61  3.58    
14 1 ARG A 237 ? ? 47.97   70.65   
15 1 ALA A 240 ? ? -12.15  105.40  
16 1 TYR A 248 ? ? -74.41  -71.07  
17 1 ASN A 298 ? ? 70.75   -7.39   
18 1 THR A 304 ? ? -72.32  -83.95  
19 1 ASN A 320 ? ? -78.75  -155.68 
20 1 SER A 324 ? ? -164.55 100.88  
21 1 SER A 379 ? ? -108.33 40.43   
22 1 SER A 401 ? ? -71.47  -154.49 
23 1 GLU A 413 ? ? -37.68  -36.63  
# 
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 ILE 25  ? A ILE 1   
2  1 Y 1 A GLU 26  ? A GLU 2   
3  1 Y 1 A ILE 27  ? A ILE 3   
4  1 Y 1 A PRO 28  ? A PRO 4   
5  1 Y 1 A MET 29  ? A MET 5   
6  1 Y 1 A ASP 30  ? A ASP 6   
7  1 Y 1 A PRO 31  ? A PRO 7   
8  1 Y 1 A SER 32  ? A SER 8   
9  1 Y 1 A ILE 33  ? A ILE 9   
10 1 Y 1 A GLN 34  ? A GLN 10  
11 1 Y 1 A ASN 35  ? A ASN 11  
12 1 Y 1 A GLU 36  ? A GLU 12  
13 1 Y 1 A ASP 427 ? A ASP 403 
14 1 Y 1 A VAL 428 ? A VAL 404 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 water                  HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAG 1   1   1   NAG NAG A . 
C 3 HOH 1   2   2   HOH WAT A . 
C 3 HOH 2   3   3   HOH WAT A . 
C 3 HOH 3   4   4   HOH WAT A . 
C 3 HOH 4   5   5   HOH WAT A . 
C 3 HOH 5   6   6   HOH WAT A . 
C 3 HOH 6   7   7   HOH WAT A . 
C 3 HOH 7   8   8   HOH WAT A . 
C 3 HOH 8   9   9   HOH WAT A . 
C 3 HOH 9   10  10  HOH WAT A . 
C 3 HOH 10  11  11  HOH WAT A . 
C 3 HOH 11  12  12  HOH WAT A . 
C 3 HOH 12  13  13  HOH WAT A . 
C 3 HOH 13  14  14  HOH WAT A . 
C 3 HOH 14  15  15  HOH WAT A . 
C 3 HOH 15  16  16  HOH WAT A . 
C 3 HOH 16  17  17  HOH WAT A . 
C 3 HOH 17  18  18  HOH WAT A . 
C 3 HOH 18  19  19  HOH WAT A . 
C 3 HOH 19  20  20  HOH WAT A . 
C 3 HOH 20  21  21  HOH WAT A . 
C 3 HOH 21  22  22  HOH WAT A . 
C 3 HOH 22  23  23  HOH WAT A . 
C 3 HOH 23  24  24  HOH WAT A . 
C 3 HOH 24  429 429 HOH WAT A . 
C 3 HOH 25  430 430 HOH WAT A . 
C 3 HOH 26  431 431 HOH WAT A . 
C 3 HOH 27  432 432 HOH WAT A . 
C 3 HOH 28  433 433 HOH WAT A . 
C 3 HOH 29  434 434 HOH WAT A . 
C 3 HOH 30  435 435 HOH WAT A . 
C 3 HOH 31  436 436 HOH WAT A . 
C 3 HOH 32  437 437 HOH WAT A . 
C 3 HOH 33  438 438 HOH WAT A . 
C 3 HOH 34  439 439 HOH WAT A . 
C 3 HOH 35  440 440 HOH WAT A . 
C 3 HOH 36  441 441 HOH WAT A . 
C 3 HOH 37  442 442 HOH WAT A . 
C 3 HOH 38  443 443 HOH WAT A . 
C 3 HOH 39  444 444 HOH WAT A . 
C 3 HOH 40  445 445 HOH WAT A . 
C 3 HOH 41  446 446 HOH WAT A . 
C 3 HOH 42  447 447 HOH WAT A . 
C 3 HOH 43  448 448 HOH WAT A . 
C 3 HOH 44  449 449 HOH WAT A . 
C 3 HOH 45  450 450 HOH WAT A . 
C 3 HOH 46  451 451 HOH WAT A . 
C 3 HOH 47  452 452 HOH WAT A . 
C 3 HOH 48  453 453 HOH WAT A . 
C 3 HOH 49  454 454 HOH WAT A . 
C 3 HOH 50  455 455 HOH WAT A . 
C 3 HOH 51  456 456 HOH WAT A . 
C 3 HOH 52  457 457 HOH WAT A . 
C 3 HOH 53  458 458 HOH WAT A . 
C 3 HOH 54  459 459 HOH WAT A . 
C 3 HOH 55  460 460 HOH WAT A . 
C 3 HOH 56  461 461 HOH WAT A . 
C 3 HOH 57  462 462 HOH WAT A . 
C 3 HOH 58  463 463 HOH WAT A . 
C 3 HOH 59  464 464 HOH WAT A . 
C 3 HOH 60  465 465 HOH WAT A . 
C 3 HOH 61  466 466 HOH WAT A . 
C 3 HOH 62  467 467 HOH WAT A . 
C 3 HOH 63  468 468 HOH WAT A . 
C 3 HOH 64  469 469 HOH WAT A . 
C 3 HOH 65  470 470 HOH WAT A . 
C 3 HOH 66  471 471 HOH WAT A . 
C 3 HOH 67  472 472 HOH WAT A . 
C 3 HOH 68  473 473 HOH WAT A . 
C 3 HOH 69  474 474 HOH WAT A . 
C 3 HOH 70  475 475 HOH WAT A . 
C 3 HOH 71  476 476 HOH WAT A . 
C 3 HOH 72  477 477 HOH WAT A . 
C 3 HOH 73  478 478 HOH WAT A . 
C 3 HOH 74  479 479 HOH WAT A . 
C 3 HOH 75  480 480 HOH WAT A . 
C 3 HOH 76  481 481 HOH WAT A . 
C 3 HOH 77  482 482 HOH WAT A . 
C 3 HOH 78  483 483 HOH WAT A . 
C 3 HOH 79  484 484 HOH WAT A . 
C 3 HOH 80  485 485 HOH WAT A . 
C 3 HOH 81  486 486 HOH WAT A . 
C 3 HOH 82  487 487 HOH WAT A . 
C 3 HOH 83  488 488 HOH WAT A . 
C 3 HOH 84  489 489 HOH WAT A . 
C 3 HOH 85  490 490 HOH WAT A . 
C 3 HOH 86  491 491 HOH WAT A . 
C 3 HOH 87  492 492 HOH WAT A . 
C 3 HOH 88  493 493 HOH WAT A . 
C 3 HOH 89  494 494 HOH WAT A . 
C 3 HOH 90  495 495 HOH WAT A . 
C 3 HOH 91  496 1   HOH WAT A . 
C 3 HOH 92  497 25  HOH WAT A . 
C 3 HOH 93  498 26  HOH WAT A . 
C 3 HOH 94  499 27  HOH WAT A . 
C 3 HOH 95  500 28  HOH WAT A . 
C 3 HOH 96  501 29  HOH WAT A . 
C 3 HOH 97  502 30  HOH WAT A . 
C 3 HOH 98  503 31  HOH WAT A . 
C 3 HOH 99  504 32  HOH WAT A . 
C 3 HOH 100 505 33  HOH WAT A . 
C 3 HOH 101 506 34  HOH WAT A . 
C 3 HOH 102 507 35  HOH WAT A . 
C 3 HOH 103 508 36  HOH WAT A . 
C 3 HOH 104 509 37  HOH WAT A . 
C 3 HOH 105 510 38  HOH WAT A . 
C 3 HOH 106 511 39  HOH WAT A . 
C 3 HOH 107 512 40  HOH WAT A . 
C 3 HOH 108 513 41  HOH WAT A . 
C 3 HOH 109 514 42  HOH WAT A . 
C 3 HOH 110 515 43  HOH WAT A . 
C 3 HOH 111 516 44  HOH WAT A . 
C 3 HOH 112 517 45  HOH WAT A . 
C 3 HOH 113 518 46  HOH WAT A . 
C 3 HOH 114 519 47  HOH WAT A . 
C 3 HOH 115 520 48  HOH WAT A . 
C 3 HOH 116 521 49  HOH WAT A . 
C 3 HOH 117 522 50  HOH WAT A . 
C 3 HOH 118 523 51  HOH WAT A . 
C 3 HOH 119 524 52  HOH WAT A . 
C 3 HOH 120 525 53  HOH WAT A . 
C 3 HOH 121 526 54  HOH WAT A . 
C 3 HOH 122 527 55  HOH WAT A . 
C 3 HOH 123 528 56  HOH WAT A . 
C 3 HOH 124 529 57  HOH WAT A . 
C 3 HOH 125 530 58  HOH WAT A . 
C 3 HOH 126 531 59  HOH WAT A . 
C 3 HOH 127 532 60  HOH WAT A . 
C 3 HOH 128 533 61  HOH WAT A . 
C 3 HOH 129 534 62  HOH WAT A . 
C 3 HOH 130 535 63  HOH WAT A . 
C 3 HOH 131 536 64  HOH WAT A . 
C 3 HOH 132 537 65  HOH WAT A . 
C 3 HOH 133 538 66  HOH WAT A . 
C 3 HOH 134 539 67  HOH WAT A . 
C 3 HOH 135 540 68  HOH WAT A . 
C 3 HOH 136 541 69  HOH WAT A . 
C 3 HOH 137 542 70  HOH WAT A . 
C 3 HOH 138 543 71  HOH WAT A . 
C 3 HOH 139 544 72  HOH WAT A . 
C 3 HOH 140 545 73  HOH WAT A . 
C 3 HOH 141 546 74  HOH WAT A . 
C 3 HOH 142 547 75  HOH WAT A . 
C 3 HOH 143 548 76  HOH WAT A . 
C 3 HOH 144 549 77  HOH WAT A . 
C 3 HOH 145 550 78  HOH WAT A . 
C 3 HOH 146 551 79  HOH WAT A . 
C 3 HOH 147 552 80  HOH WAT A . 
C 3 HOH 148 553 81  HOH WAT A . 
C 3 HOH 149 554 82  HOH WAT A . 
C 3 HOH 150 555 83  HOH WAT A . 
C 3 HOH 151 556 84  HOH WAT A . 
C 3 HOH 152 557 85  HOH WAT A . 
C 3 HOH 153 558 86  HOH WAT A . 
C 3 HOH 154 559 87  HOH WAT A . 
C 3 HOH 155 560 88  HOH WAT A . 
C 3 HOH 156 561 89  HOH WAT A . 
C 3 HOH 157 562 90  HOH WAT A . 
C 3 HOH 158 563 91  HOH WAT A . 
C 3 HOH 159 564 92  HOH WAT A . 
C 3 HOH 160 565 93  HOH WAT A . 
C 3 HOH 161 566 94  HOH WAT A . 
C 3 HOH 162 567 95  HOH WAT A . 
C 3 HOH 163 568 96  HOH WAT A . 
C 3 HOH 164 569 97  HOH WAT A . 
C 3 HOH 165 570 98  HOH WAT A . 
C 3 HOH 166 571 99  HOH WAT A . 
C 3 HOH 167 572 100 HOH WAT A . 
C 3 HOH 168 573 101 HOH WAT A . 
C 3 HOH 169 574 102 HOH WAT A . 
C 3 HOH 170 575 103 HOH WAT A . 
C 3 HOH 171 576 104 HOH WAT A . 
C 3 HOH 172 577 105 HOH WAT A . 
C 3 HOH 173 578 106 HOH WAT A . 
C 3 HOH 174 579 107 HOH WAT A . 
C 3 HOH 175 580 108 HOH WAT A . 
C 3 HOH 176 581 109 HOH WAT A . 
C 3 HOH 177 582 110 HOH WAT A . 
C 3 HOH 178 583 111 HOH WAT A . 
C 3 HOH 179 584 112 HOH WAT A . 
C 3 HOH 180 585 113 HOH WAT A . 
C 3 HOH 181 586 114 HOH WAT A . 
C 3 HOH 182 587 115 HOH WAT A . 
C 3 HOH 183 588 116 HOH WAT A . 
C 3 HOH 184 589 117 HOH WAT A . 
C 3 HOH 185 590 118 HOH WAT A . 
C 3 HOH 186 591 119 HOH WAT A . 
C 3 HOH 187 592 120 HOH WAT A . 
C 3 HOH 188 593 121 HOH WAT A . 
C 3 HOH 189 594 122 HOH WAT A . 
C 3 HOH 190 595 123 HOH WAT A . 
C 3 HOH 191 596 124 HOH WAT A . 
C 3 HOH 192 597 125 HOH WAT A . 
C 3 HOH 193 598 126 HOH WAT A . 
C 3 HOH 194 599 127 HOH WAT A . 
C 3 HOH 195 600 128 HOH WAT A . 
C 3 HOH 196 601 129 HOH WAT A . 
C 3 HOH 197 602 130 HOH WAT A . 
C 3 HOH 198 603 131 HOH WAT A . 
C 3 HOH 199 604 132 HOH WAT A . 
C 3 HOH 200 605 133 HOH WAT A . 
C 3 HOH 201 606 134 HOH WAT A . 
C 3 HOH 202 607 135 HOH WAT A . 
C 3 HOH 203 608 136 HOH WAT A . 
C 3 HOH 204 609 137 HOH WAT A . 
C 3 HOH 205 610 138 HOH WAT A . 
C 3 HOH 206 611 139 HOH WAT A . 
C 3 HOH 207 612 140 HOH WAT A . 
C 3 HOH 208 613 141 HOH WAT A . 
C 3 HOH 209 614 142 HOH WAT A . 
C 3 HOH 210 615 143 HOH WAT A . 
C 3 HOH 211 616 144 HOH WAT A . 
C 3 HOH 212 617 145 HOH WAT A . 
C 3 HOH 213 618 146 HOH WAT A . 
C 3 HOH 214 619 147 HOH WAT A . 
C 3 HOH 215 620 148 HOH WAT A . 
C 3 HOH 216 621 149 HOH WAT A . 
C 3 HOH 217 622 150 HOH WAT A . 
C 3 HOH 218 623 151 HOH WAT A . 
C 3 HOH 219 624 152 HOH WAT A . 
C 3 HOH 220 625 153 HOH WAT A . 
C 3 HOH 221 626 154 HOH WAT A . 
C 3 HOH 222 627 155 HOH WAT A . 
C 3 HOH 223 628 156 HOH WAT A . 
C 3 HOH 224 629 157 HOH WAT A . 
C 3 HOH 225 630 158 HOH WAT A . 
C 3 HOH 226 631 159 HOH WAT A . 
C 3 HOH 227 632 160 HOH WAT A . 
C 3 HOH 228 633 161 HOH WAT A . 
C 3 HOH 229 634 162 HOH WAT A . 
C 3 HOH 230 635 163 HOH WAT A . 
C 3 HOH 231 636 164 HOH WAT A . 
C 3 HOH 232 637 165 HOH WAT A . 
C 3 HOH 233 638 166 HOH WAT A . 
C 3 HOH 234 639 167 HOH WAT A . 
C 3 HOH 235 640 168 HOH WAT A . 
C 3 HOH 236 641 169 HOH WAT A . 
C 3 HOH 237 642 170 HOH WAT A . 
C 3 HOH 238 643 171 HOH WAT A . 
C 3 HOH 239 644 172 HOH WAT A . 
C 3 HOH 240 645 173 HOH WAT A . 
C 3 HOH 241 646 174 HOH WAT A . 
C 3 HOH 242 647 175 HOH WAT A . 
C 3 HOH 243 648 176 HOH WAT A . 
C 3 HOH 244 649 177 HOH WAT A . 
C 3 HOH 245 650 178 HOH WAT A . 
C 3 HOH 246 651 179 HOH WAT A . 
C 3 HOH 247 652 180 HOH WAT A . 
C 3 HOH 248 653 181 HOH WAT A . 
C 3 HOH 249 654 182 HOH WAT A . 
C 3 HOH 250 655 183 HOH WAT A . 
C 3 HOH 251 656 184 HOH WAT A . 
C 3 HOH 252 657 185 HOH WAT A . 
C 3 HOH 253 658 186 HOH WAT A . 
C 3 HOH 254 659 187 HOH WAT A . 
C 3 HOH 255 660 188 HOH WAT A . 
C 3 HOH 256 661 189 HOH WAT A . 
C 3 HOH 257 662 190 HOH WAT A . 
C 3 HOH 258 663 191 HOH WAT A . 
C 3 HOH 259 664 192 HOH WAT A . 
C 3 HOH 260 665 193 HOH WAT A . 
C 3 HOH 261 666 194 HOH WAT A . 
C 3 HOH 262 667 195 HOH WAT A . 
C 3 HOH 263 668 196 HOH WAT A . 
C 3 HOH 264 669 197 HOH WAT A . 
C 3 HOH 265 670 198 HOH WAT A . 
C 3 HOH 266 671 199 HOH WAT A . 
C 3 HOH 267 672 200 HOH WAT A . 
C 3 HOH 268 673 201 HOH WAT A . 
C 3 HOH 269 674 202 HOH WAT A . 
C 3 HOH 270 675 203 HOH WAT A . 
C 3 HOH 271 676 204 HOH WAT A . 
C 3 HOH 272 677 205 HOH WAT A . 
C 3 HOH 273 678 206 HOH WAT A . 
C 3 HOH 274 679 207 HOH WAT A . 
C 3 HOH 275 680 208 HOH WAT A . 
C 3 HOH 276 681 209 HOH WAT A . 
C 3 HOH 277 682 210 HOH WAT A . 
C 3 HOH 278 683 211 HOH WAT A . 
C 3 HOH 279 684 212 HOH WAT A . 
C 3 HOH 280 685 213 HOH WAT A . 
C 3 HOH 281 686 214 HOH WAT A . 
C 3 HOH 282 687 215 HOH WAT A . 
C 3 HOH 283 688 216 HOH WAT A . 
C 3 HOH 284 689 217 HOH WAT A . 
C 3 HOH 285 690 218 HOH WAT A . 
C 3 HOH 286 691 219 HOH WAT A . 
C 3 HOH 287 692 220 HOH WAT A . 
C 3 HOH 288 693 221 HOH WAT A . 
C 3 HOH 289 694 222 HOH WAT A . 
C 3 HOH 290 695 223 HOH WAT A . 
C 3 HOH 291 696 224 HOH WAT A . 
C 3 HOH 292 697 225 HOH WAT A . 
C 3 HOH 293 698 226 HOH WAT A . 
C 3 HOH 294 699 227 HOH WAT A . 
C 3 HOH 295 700 228 HOH WAT A . 
C 3 HOH 296 701 229 HOH WAT A . 
C 3 HOH 297 702 230 HOH WAT A . 
C 3 HOH 298 703 231 HOH WAT A . 
C 3 HOH 299 704 232 HOH WAT A . 
C 3 HOH 300 705 233 HOH WAT A . 
C 3 HOH 301 706 234 HOH WAT A . 
C 3 HOH 302 707 235 HOH WAT A . 
C 3 HOH 303 708 236 HOH WAT A . 
C 3 HOH 304 709 237 HOH WAT A . 
C 3 HOH 305 710 238 HOH WAT A . 
C 3 HOH 306 711 239 HOH WAT A . 
C 3 HOH 307 712 240 HOH WAT A . 
C 3 HOH 308 713 241 HOH WAT A . 
C 3 HOH 309 714 242 HOH WAT A . 
C 3 HOH 310 715 243 HOH WAT A . 
C 3 HOH 311 716 244 HOH WAT A . 
C 3 HOH 312 717 245 HOH WAT A . 
C 3 HOH 313 718 246 HOH WAT A . 
C 3 HOH 314 719 247 HOH WAT A . 
C 3 HOH 315 720 248 HOH WAT A . 
C 3 HOH 316 721 249 HOH WAT A . 
C 3 HOH 317 722 250 HOH WAT A . 
C 3 HOH 318 723 251 HOH WAT A . 
C 3 HOH 319 724 252 HOH WAT A . 
C 3 HOH 320 725 253 HOH WAT A . 
C 3 HOH 321 726 254 HOH WAT A . 
C 3 HOH 322 727 255 HOH WAT A . 
C 3 HOH 323 728 256 HOH WAT A . 
C 3 HOH 324 729 257 HOH WAT A . 
C 3 HOH 325 730 258 HOH WAT A . 
C 3 HOH 326 731 259 HOH WAT A . 
C 3 HOH 327 732 260 HOH WAT A . 
C 3 HOH 328 733 261 HOH WAT A . 
C 3 HOH 329 734 262 HOH WAT A . 
C 3 HOH 330 735 263 HOH WAT A . 
C 3 HOH 331 736 264 HOH WAT A . 
C 3 HOH 332 737 265 HOH WAT A . 
C 3 HOH 333 738 266 HOH WAT A . 
C 3 HOH 334 739 267 HOH WAT A . 
C 3 HOH 335 740 268 HOH WAT A . 
C 3 HOH 336 741 269 HOH WAT A . 
C 3 HOH 337 742 270 HOH WAT A . 
C 3 HOH 338 743 271 HOH WAT A . 
C 3 HOH 339 744 272 HOH WAT A . 
C 3 HOH 340 745 273 HOH WAT A . 
C 3 HOH 341 746 274 HOH WAT A . 
C 3 HOH 342 747 275 HOH WAT A . 
C 3 HOH 343 748 276 HOH WAT A . 
C 3 HOH 344 749 277 HOH WAT A . 
C 3 HOH 345 750 278 HOH WAT A . 
C 3 HOH 346 751 279 HOH WAT A . 
C 3 HOH 347 752 280 HOH WAT A . 
C 3 HOH 348 753 281 HOH WAT A . 
C 3 HOH 349 754 282 HOH WAT A . 
C 3 HOH 350 755 283 HOH WAT A . 
C 3 HOH 351 756 284 HOH WAT A . 
C 3 HOH 352 757 285 HOH WAT A . 
C 3 HOH 353 758 286 HOH WAT A . 
C 3 HOH 354 759 287 HOH WAT A . 
C 3 HOH 355 760 288 HOH WAT A . 
C 3 HOH 356 761 289 HOH WAT A . 
C 3 HOH 357 762 290 HOH WAT A . 
C 3 HOH 358 763 291 HOH WAT A . 
C 3 HOH 359 764 292 HOH WAT A . 
C 3 HOH 360 765 293 HOH WAT A . 
C 3 HOH 361 766 294 HOH WAT A . 
C 3 HOH 362 767 295 HOH WAT A . 
C 3 HOH 363 768 296 HOH WAT A . 
C 3 HOH 364 769 297 HOH WAT A . 
C 3 HOH 365 770 298 HOH WAT A . 
C 3 HOH 366 771 299 HOH WAT A . 
C 3 HOH 367 772 300 HOH WAT A . 
C 3 HOH 368 773 301 HOH WAT A . 
C 3 HOH 369 774 302 HOH WAT A . 
C 3 HOH 370 775 303 HOH WAT A . 
C 3 HOH 371 776 304 HOH WAT A . 
C 3 HOH 372 777 305 HOH WAT A . 
C 3 HOH 373 778 306 HOH WAT A . 
C 3 HOH 374 779 307 HOH WAT A . 
C 3 HOH 375 780 308 HOH WAT A . 
C 3 HOH 376 781 309 HOH WAT A . 
C 3 HOH 377 782 310 HOH WAT A . 
C 3 HOH 378 783 311 HOH WAT A . 
C 3 HOH 379 784 312 HOH WAT A . 
C 3 HOH 380 785 313 HOH WAT A . 
C 3 HOH 381 786 314 HOH WAT A . 
C 3 HOH 382 787 315 HOH WAT A . 
C 3 HOH 383 788 316 HOH WAT A . 
C 3 HOH 384 789 317 HOH WAT A . 
C 3 HOH 385 790 318 HOH WAT A . 
C 3 HOH 386 791 319 HOH WAT A . 
C 3 HOH 387 792 320 HOH WAT A . 
C 3 HOH 388 793 321 HOH WAT A . 
C 3 HOH 389 794 322 HOH WAT A . 
C 3 HOH 390 795 323 HOH WAT A . 
C 3 HOH 391 796 324 HOH WAT A . 
C 3 HOH 392 797 325 HOH WAT A . 
C 3 HOH 393 798 326 HOH WAT A . 
C 3 HOH 394 799 327 HOH WAT A . 
C 3 HOH 395 800 328 HOH WAT A . 
C 3 HOH 396 801 329 HOH WAT A . 
C 3 HOH 397 802 330 HOH WAT A . 
C 3 HOH 398 803 331 HOH WAT A . 
C 3 HOH 399 804 332 HOH WAT A . 
C 3 HOH 400 805 333 HOH WAT A . 
C 3 HOH 401 806 334 HOH WAT A . 
C 3 HOH 402 807 335 HOH WAT A . 
C 3 HOH 403 808 336 HOH WAT A . 
C 3 HOH 404 809 337 HOH WAT A . 
C 3 HOH 405 810 338 HOH WAT A . 
C 3 HOH 406 811 339 HOH WAT A . 
C 3 HOH 407 812 340 HOH WAT A . 
C 3 HOH 408 813 341 HOH WAT A . 
C 3 HOH 409 814 342 HOH WAT A . 
C 3 HOH 410 815 343 HOH WAT A . 
C 3 HOH 411 816 344 HOH WAT A . 
C 3 HOH 412 817 345 HOH WAT A . 
C 3 HOH 413 818 346 HOH WAT A . 
C 3 HOH 414 819 347 HOH WAT A . 
C 3 HOH 415 820 348 HOH WAT A . 
C 3 HOH 416 821 349 HOH WAT A . 
C 3 HOH 417 822 350 HOH WAT A . 
C 3 HOH 418 823 351 HOH WAT A . 
C 3 HOH 419 824 352 HOH WAT A . 
C 3 HOH 420 825 353 HOH WAT A . 
C 3 HOH 421 826 354 HOH WAT A . 
C 3 HOH 422 827 355 HOH WAT A . 
C 3 HOH 423 828 356 HOH WAT A . 
C 3 HOH 424 829 357 HOH WAT A . 
C 3 HOH 425 830 358 HOH WAT A . 
C 3 HOH 426 831 359 HOH WAT A . 
C 3 HOH 427 832 360 HOH WAT A . 
C 3 HOH 428 833 361 HOH WAT A . 
C 3 HOH 429 834 362 HOH WAT A . 
C 3 HOH 430 835 363 HOH WAT A . 
C 3 HOH 431 836 364 HOH WAT A . 
C 3 HOH 432 837 365 HOH WAT A . 
C 3 HOH 433 838 366 HOH WAT A . 
C 3 HOH 434 839 367 HOH WAT A . 
C 3 HOH 435 840 368 HOH WAT A . 
C 3 HOH 436 841 369 HOH WAT A . 
C 3 HOH 437 842 370 HOH WAT A . 
C 3 HOH 438 843 371 HOH WAT A . 
C 3 HOH 439 844 372 HOH WAT A . 
C 3 HOH 440 845 373 HOH WAT A . 
C 3 HOH 441 846 374 HOH WAT A . 
C 3 HOH 442 847 375 HOH WAT A . 
C 3 HOH 443 848 376 HOH WAT A . 
C 3 HOH 444 849 377 HOH WAT A . 
C 3 HOH 445 850 378 HOH WAT A . 
C 3 HOH 446 851 379 HOH WAT A . 
C 3 HOH 447 852 380 HOH WAT A . 
C 3 HOH 448 853 381 HOH WAT A . 
C 3 HOH 449 854 382 HOH WAT A . 
C 3 HOH 450 855 383 HOH WAT A . 
C 3 HOH 451 856 384 HOH WAT A . 
C 3 HOH 452 857 385 HOH WAT A . 
C 3 HOH 453 858 386 HOH WAT A . 
C 3 HOH 454 859 387 HOH WAT A . 
C 3 HOH 455 860 388 HOH WAT A . 
C 3 HOH 456 861 389 HOH WAT A . 
C 3 HOH 457 862 390 HOH WAT A . 
C 3 HOH 458 863 391 HOH WAT A . 
C 3 HOH 459 864 392 HOH WAT A . 
C 3 HOH 460 865 393 HOH WAT A . 
C 3 HOH 461 866 394 HOH WAT A . 
C 3 HOH 462 867 395 HOH WAT A . 
C 3 HOH 463 868 396 HOH WAT A . 
C 3 HOH 464 869 397 HOH WAT A . 
C 3 HOH 465 870 398 HOH WAT A . 
C 3 HOH 466 871 399 HOH WAT A . 
C 3 HOH 467 872 400 HOH WAT A . 
C 3 HOH 468 873 401 HOH WAT A . 
C 3 HOH 469 874 402 HOH WAT A . 
C 3 HOH 470 875 403 HOH WAT A . 
C 3 HOH 471 876 404 HOH WAT A . 
C 3 HOH 472 877 405 HOH WAT A . 
C 3 HOH 473 878 406 HOH WAT A . 
C 3 HOH 474 879 407 HOH WAT A . 
C 3 HOH 475 880 408 HOH WAT A . 
C 3 HOH 476 881 409 HOH WAT A . 
C 3 HOH 477 882 410 HOH WAT A . 
C 3 HOH 478 883 411 HOH WAT A . 
C 3 HOH 479 884 412 HOH WAT A . 
C 3 HOH 480 885 413 HOH WAT A . 
C 3 HOH 481 886 414 HOH WAT A . 
C 3 HOH 482 887 415 HOH WAT A . 
C 3 HOH 483 888 416 HOH WAT A . 
C 3 HOH 484 889 417 HOH WAT A . 
C 3 HOH 485 890 418 HOH WAT A . 
C 3 HOH 486 891 419 HOH WAT A . 
C 3 HOH 487 892 420 HOH WAT A . 
C 3 HOH 488 893 421 HOH WAT A . 
C 3 HOH 489 894 422 HOH WAT A . 
C 3 HOH 490 895 423 HOH WAT A . 
C 3 HOH 491 896 424 HOH WAT A . 
C 3 HOH 492 897 425 HOH WAT A . 
C 3 HOH 493 898 426 HOH WAT A . 
C 3 HOH 494 899 427 HOH WAT A . 
C 3 HOH 495 900 428 HOH WAT A . 
# 
