data_9DFL
# 
_entry.id   9DFL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DFL         pdb_00009dfl 10.2210/pdb9dfl/pdb 
WWPDB D_1000288005 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-16 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DFL 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wang.yifan@uga.edu 
_pdbx_contact_author.name_first         Yifan 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-2469 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, B.'   1 0000-0003-3150-7501 
'Wang, Y.' 2 0000-0003-0378-2469 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108123 
_citation.page_last                 108123 
_citation.title                     
'Elucidating ligand interactions and small-molecule activation in the pyrrolnitrin biosynthetic enzyme PrnB.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2024.108123 
_citation.pdbx_database_id_PubMed   39725034 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, B.'       1 ? 
primary 'Usai, R.'     2 ? 
primary 'Campbell, J.' 3 ? 
primary 'Wang, Y.'     4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man PrnB                                     41592.242 2   ? ? ? ? 
2 non-polymer nat 'PROTOPORPHYRIN IX CONTAINING FE'        616.487   2   ? ? ? ? 
3 non-polymer syn 'INDOLYLPROPIONIC ACID'                  189.211   2   ? ? ? ? 
4 non-polymer syn GLYCEROL                                 92.094    3   ? ? ? ? 
5 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 122.143   1   ? ? ? ? 
6 water       nat water                                    18.015    290 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGENLYFQGMISNEISKLDPLNLDAFFNQLPSLNQNLEVSLLIDKLREITKSYLPTTFSINDALAATRD
LGMIMSSVRKLGIQPVSAVSDLEVFLETLSEITNMVPRETSYHYGPWNPIGERERRFTHFPDERGLIEGVRIAIPGIELA
IREINQLSNLSLNDPAFESLAKSAALHVYQAVDGIGETIKKTDPYVFSHELRPFFDPIRIGGKSYIGAGGGQIPLFVVDV
KLWLGNHSPNSEYVSFIKDSVFYLPPELRPICVDSLLEPSVINQKFAEFGSVEITDQVIKGMESLLSVIQVLLKFRKPHF
QLAQRTLSKENRGNYTTGSAGYTNSFNHMVLEFTIEVEKQIRAVLAPYRS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGENLYFQGMISNEISKLDPLNLDAFFNQLPSLNQNLEVSLLIDKLREITKSYLPTTFSINDALAATRD
LGMIMSSVRKLGIQPVSAVSDLEVFLETLSEITNMVPRETSYHYGPWNPIGERERRFTHFPDERGLIEGVRIAIPGIELA
IREINQLSNLSLNDPAFESLAKSAALHVYQAVDGIGETIKKTDPYVFSHELRPFFDPIRIGGKSYIGAGGGQIPLFVVDV
KLWLGNHSPNSEYVSFIKDSVFYLPPELRPICVDSLLEPSVINQKFAEFGSVEITDQVIKGMESLLSVIQVLLKFRKPHF
QLAQRTLSKENRGNYTTGSAGYTNSFNHMVLEFTIEVEKQIRAVLAPYRS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'        HEM 
3 'INDOLYLPROPIONIC ACID'                  IOP 
4 GLYCEROL                                 GOL 
5 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL TRS 
6 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  GLU n 
1 15  ASN n 
1 16  LEU n 
1 17  TYR n 
1 18  PHE n 
1 19  GLN n 
1 20  GLY n 
1 21  MET n 
1 22  ILE n 
1 23  SER n 
1 24  ASN n 
1 25  GLU n 
1 26  ILE n 
1 27  SER n 
1 28  LYS n 
1 29  LEU n 
1 30  ASP n 
1 31  PRO n 
1 32  LEU n 
1 33  ASN n 
1 34  LEU n 
1 35  ASP n 
1 36  ALA n 
1 37  PHE n 
1 38  PHE n 
1 39  ASN n 
1 40  GLN n 
1 41  LEU n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  ASN n 
1 46  GLN n 
1 47  ASN n 
1 48  LEU n 
1 49  GLU n 
1 50  VAL n 
1 51  SER n 
1 52  LEU n 
1 53  LEU n 
1 54  ILE n 
1 55  ASP n 
1 56  LYS n 
1 57  LEU n 
1 58  ARG n 
1 59  GLU n 
1 60  ILE n 
1 61  THR n 
1 62  LYS n 
1 63  SER n 
1 64  TYR n 
1 65  LEU n 
1 66  PRO n 
1 67  THR n 
1 68  THR n 
1 69  PHE n 
1 70  SER n 
1 71  ILE n 
1 72  ASN n 
1 73  ASP n 
1 74  ALA n 
1 75  LEU n 
1 76  ALA n 
1 77  ALA n 
1 78  THR n 
1 79  ARG n 
1 80  ASP n 
1 81  LEU n 
1 82  GLY n 
1 83  MET n 
1 84  ILE n 
1 85  MET n 
1 86  SER n 
1 87  SER n 
1 88  VAL n 
1 89  ARG n 
1 90  LYS n 
1 91  LEU n 
1 92  GLY n 
1 93  ILE n 
1 94  GLN n 
1 95  PRO n 
1 96  VAL n 
1 97  SER n 
1 98  ALA n 
1 99  VAL n 
1 100 SER n 
1 101 ASP n 
1 102 LEU n 
1 103 GLU n 
1 104 VAL n 
1 105 PHE n 
1 106 LEU n 
1 107 GLU n 
1 108 THR n 
1 109 LEU n 
1 110 SER n 
1 111 GLU n 
1 112 ILE n 
1 113 THR n 
1 114 ASN n 
1 115 MET n 
1 116 VAL n 
1 117 PRO n 
1 118 ARG n 
1 119 GLU n 
1 120 THR n 
1 121 SER n 
1 122 TYR n 
1 123 HIS n 
1 124 TYR n 
1 125 GLY n 
1 126 PRO n 
1 127 TRP n 
1 128 ASN n 
1 129 PRO n 
1 130 ILE n 
1 131 GLY n 
1 132 GLU n 
1 133 ARG n 
1 134 GLU n 
1 135 ARG n 
1 136 ARG n 
1 137 PHE n 
1 138 THR n 
1 139 HIS n 
1 140 PHE n 
1 141 PRO n 
1 142 ASP n 
1 143 GLU n 
1 144 ARG n 
1 145 GLY n 
1 146 LEU n 
1 147 ILE n 
1 148 GLU n 
1 149 GLY n 
1 150 VAL n 
1 151 ARG n 
1 152 ILE n 
1 153 ALA n 
1 154 ILE n 
1 155 PRO n 
1 156 GLY n 
1 157 ILE n 
1 158 GLU n 
1 159 LEU n 
1 160 ALA n 
1 161 ILE n 
1 162 ARG n 
1 163 GLU n 
1 164 ILE n 
1 165 ASN n 
1 166 GLN n 
1 167 LEU n 
1 168 SER n 
1 169 ASN n 
1 170 LEU n 
1 171 SER n 
1 172 LEU n 
1 173 ASN n 
1 174 ASP n 
1 175 PRO n 
1 176 ALA n 
1 177 PHE n 
1 178 GLU n 
1 179 SER n 
1 180 LEU n 
1 181 ALA n 
1 182 LYS n 
1 183 SER n 
1 184 ALA n 
1 185 ALA n 
1 186 LEU n 
1 187 HIS n 
1 188 VAL n 
1 189 TYR n 
1 190 GLN n 
1 191 ALA n 
1 192 VAL n 
1 193 ASP n 
1 194 GLY n 
1 195 ILE n 
1 196 GLY n 
1 197 GLU n 
1 198 THR n 
1 199 ILE n 
1 200 LYS n 
1 201 LYS n 
1 202 THR n 
1 203 ASP n 
1 204 PRO n 
1 205 TYR n 
1 206 VAL n 
1 207 PHE n 
1 208 SER n 
1 209 HIS n 
1 210 GLU n 
1 211 LEU n 
1 212 ARG n 
1 213 PRO n 
1 214 PHE n 
1 215 PHE n 
1 216 ASP n 
1 217 PRO n 
1 218 ILE n 
1 219 ARG n 
1 220 ILE n 
1 221 GLY n 
1 222 GLY n 
1 223 LYS n 
1 224 SER n 
1 225 TYR n 
1 226 ILE n 
1 227 GLY n 
1 228 ALA n 
1 229 GLY n 
1 230 GLY n 
1 231 GLY n 
1 232 GLN n 
1 233 ILE n 
1 234 PRO n 
1 235 LEU n 
1 236 PHE n 
1 237 VAL n 
1 238 VAL n 
1 239 ASP n 
1 240 VAL n 
1 241 LYS n 
1 242 LEU n 
1 243 TRP n 
1 244 LEU n 
1 245 GLY n 
1 246 ASN n 
1 247 HIS n 
1 248 SER n 
1 249 PRO n 
1 250 ASN n 
1 251 SER n 
1 252 GLU n 
1 253 TYR n 
1 254 VAL n 
1 255 SER n 
1 256 PHE n 
1 257 ILE n 
1 258 LYS n 
1 259 ASP n 
1 260 SER n 
1 261 VAL n 
1 262 PHE n 
1 263 TYR n 
1 264 LEU n 
1 265 PRO n 
1 266 PRO n 
1 267 GLU n 
1 268 LEU n 
1 269 ARG n 
1 270 PRO n 
1 271 ILE n 
1 272 CYS n 
1 273 VAL n 
1 274 ASP n 
1 275 SER n 
1 276 LEU n 
1 277 LEU n 
1 278 GLU n 
1 279 PRO n 
1 280 SER n 
1 281 VAL n 
1 282 ILE n 
1 283 ASN n 
1 284 GLN n 
1 285 LYS n 
1 286 PHE n 
1 287 ALA n 
1 288 GLU n 
1 289 PHE n 
1 290 GLY n 
1 291 SER n 
1 292 VAL n 
1 293 GLU n 
1 294 ILE n 
1 295 THR n 
1 296 ASP n 
1 297 GLN n 
1 298 VAL n 
1 299 ILE n 
1 300 LYS n 
1 301 GLY n 
1 302 MET n 
1 303 GLU n 
1 304 SER n 
1 305 LEU n 
1 306 LEU n 
1 307 SER n 
1 308 VAL n 
1 309 ILE n 
1 310 GLN n 
1 311 VAL n 
1 312 LEU n 
1 313 LEU n 
1 314 LYS n 
1 315 PHE n 
1 316 ARG n 
1 317 LYS n 
1 318 PRO n 
1 319 HIS n 
1 320 PHE n 
1 321 GLN n 
1 322 LEU n 
1 323 ALA n 
1 324 GLN n 
1 325 ARG n 
1 326 THR n 
1 327 LEU n 
1 328 SER n 
1 329 LYS n 
1 330 GLU n 
1 331 ASN n 
1 332 ARG n 
1 333 GLY n 
1 334 ASN n 
1 335 TYR n 
1 336 THR n 
1 337 THR n 
1 338 GLY n 
1 339 SER n 
1 340 ALA n 
1 341 GLY n 
1 342 TYR n 
1 343 THR n 
1 344 ASN n 
1 345 SER n 
1 346 PHE n 
1 347 ASN n 
1 348 HIS n 
1 349 MET n 
1 350 VAL n 
1 351 LEU n 
1 352 GLU n 
1 353 PHE n 
1 354 THR n 
1 355 ILE n 
1 356 GLU n 
1 357 VAL n 
1 358 GLU n 
1 359 LYS n 
1 360 GLN n 
1 361 ILE n 
1 362 ARG n 
1 363 ALA n 
1 364 VAL n 
1 365 LEU n 
1 366 ALA n 
1 367 PRO n 
1 368 TYR n 
1 369 ARG n 
1 370 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   370 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Flavobacteriales bacterium' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2021391 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                  ?                               'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                                 ?                               'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                               ?                               'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                          ?                               'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                                 ?                               'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                                ?                               'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                          ?                               'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                                  ?                               'C2 H5 N O2'       75.067  
GOL non-polymer         . GLYCEROL                                 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'        HEME                            'C34 H32 Fe N4 O4' 616.487 
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 
IOP non-polymer         . 'INDOLYLPROPIONIC ACID'                  ?                               'C11 H11 N O2'     189.211 
LEU 'L-peptide linking' y LEUCINE                                  ?                               'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                   ?                               'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                               ?                               'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                            ?                               'C9 H11 N O2'      165.189 
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 
TRS non-polymer         . 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 'TRIS BUFFER'                   'C4 H12 N O3 1'    122.143 
TYR 'L-peptide linking' y TYROSINE                                 ?                               'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                                   ?                               'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  GLU 14  -6  ?   ?   ?   A . n 
A 1 15  ASN 15  -5  ?   ?   ?   A . n 
A 1 16  LEU 16  -4  ?   ?   ?   A . n 
A 1 17  TYR 17  -3  ?   ?   ?   A . n 
A 1 18  PHE 18  -2  ?   ?   ?   A . n 
A 1 19  GLN 19  -1  ?   ?   ?   A . n 
A 1 20  GLY 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   ?   ?   ?   A . n 
A 1 22  ILE 22  2   2   ILE ILE A . n 
A 1 23  SER 23  3   3   SER SER A . n 
A 1 24  ASN 24  4   4   ASN ASN A . n 
A 1 25  GLU 25  5   5   GLU GLU A . n 
A 1 26  ILE 26  6   6   ILE ILE A . n 
A 1 27  SER 27  7   7   SER SER A . n 
A 1 28  LYS 28  8   8   LYS LYS A . n 
A 1 29  LEU 29  9   9   LEU LEU A . n 
A 1 30  ASP 30  10  10  ASP ASP A . n 
A 1 31  PRO 31  11  11  PRO PRO A . n 
A 1 32  LEU 32  12  12  LEU LEU A . n 
A 1 33  ASN 33  13  13  ASN ASN A . n 
A 1 34  LEU 34  14  14  LEU LEU A . n 
A 1 35  ASP 35  15  15  ASP ASP A . n 
A 1 36  ALA 36  16  16  ALA ALA A . n 
A 1 37  PHE 37  17  17  PHE PHE A . n 
A 1 38  PHE 38  18  18  PHE PHE A . n 
A 1 39  ASN 39  19  19  ASN ASN A . n 
A 1 40  GLN 40  20  20  GLN GLN A . n 
A 1 41  LEU 41  21  21  LEU LEU A . n 
A 1 42  PRO 42  22  22  PRO PRO A . n 
A 1 43  SER 43  23  23  SER SER A . n 
A 1 44  LEU 44  24  24  LEU LEU A . n 
A 1 45  ASN 45  25  25  ASN ASN A . n 
A 1 46  GLN 46  26  26  GLN GLN A . n 
A 1 47  ASN 47  27  27  ASN ASN A . n 
A 1 48  LEU 48  28  28  LEU LEU A . n 
A 1 49  GLU 49  29  29  GLU GLU A . n 
A 1 50  VAL 50  30  30  VAL VAL A . n 
A 1 51  SER 51  31  31  SER SER A . n 
A 1 52  LEU 52  32  32  LEU LEU A . n 
A 1 53  LEU 53  33  33  LEU LEU A . n 
A 1 54  ILE 54  34  34  ILE ILE A . n 
A 1 55  ASP 55  35  35  ASP ASP A . n 
A 1 56  LYS 56  36  36  LYS LYS A . n 
A 1 57  LEU 57  37  37  LEU LEU A . n 
A 1 58  ARG 58  38  38  ARG ARG A . n 
A 1 59  GLU 59  39  39  GLU GLU A . n 
A 1 60  ILE 60  40  40  ILE ILE A . n 
A 1 61  THR 61  41  41  THR THR A . n 
A 1 62  LYS 62  42  42  LYS LYS A . n 
A 1 63  SER 63  43  43  SER SER A . n 
A 1 64  TYR 64  44  44  TYR TYR A . n 
A 1 65  LEU 65  45  45  LEU LEU A . n 
A 1 66  PRO 66  46  46  PRO PRO A . n 
A 1 67  THR 67  47  47  THR THR A . n 
A 1 68  THR 68  48  48  THR THR A . n 
A 1 69  PHE 69  49  49  PHE PHE A . n 
A 1 70  SER 70  50  50  SER SER A . n 
A 1 71  ILE 71  51  51  ILE ILE A . n 
A 1 72  ASN 72  52  52  ASN ASN A . n 
A 1 73  ASP 73  53  53  ASP ASP A . n 
A 1 74  ALA 74  54  54  ALA ALA A . n 
A 1 75  LEU 75  55  55  LEU LEU A . n 
A 1 76  ALA 76  56  56  ALA ALA A . n 
A 1 77  ALA 77  57  57  ALA ALA A . n 
A 1 78  THR 78  58  58  THR THR A . n 
A 1 79  ARG 79  59  59  ARG ARG A . n 
A 1 80  ASP 80  60  60  ASP ASP A . n 
A 1 81  LEU 81  61  61  LEU LEU A . n 
A 1 82  GLY 82  62  62  GLY GLY A . n 
A 1 83  MET 83  63  63  MET MET A . n 
A 1 84  ILE 84  64  64  ILE ILE A . n 
A 1 85  MET 85  65  65  MET MET A . n 
A 1 86  SER 86  66  66  SER SER A . n 
A 1 87  SER 87  67  67  SER SER A . n 
A 1 88  VAL 88  68  68  VAL VAL A . n 
A 1 89  ARG 89  69  69  ARG ARG A . n 
A 1 90  LYS 90  70  70  LYS LYS A . n 
A 1 91  LEU 91  71  71  LEU LEU A . n 
A 1 92  GLY 92  72  72  GLY GLY A . n 
A 1 93  ILE 93  73  73  ILE ILE A . n 
A 1 94  GLN 94  74  74  GLN GLN A . n 
A 1 95  PRO 95  75  75  PRO PRO A . n 
A 1 96  VAL 96  76  76  VAL VAL A . n 
A 1 97  SER 97  77  77  SER SER A . n 
A 1 98  ALA 98  78  78  ALA ALA A . n 
A 1 99  VAL 99  79  79  VAL VAL A . n 
A 1 100 SER 100 80  80  SER SER A . n 
A 1 101 ASP 101 81  81  ASP ASP A . n 
A 1 102 LEU 102 82  82  LEU LEU A . n 
A 1 103 GLU 103 83  83  GLU GLU A . n 
A 1 104 VAL 104 84  84  VAL VAL A . n 
A 1 105 PHE 105 85  85  PHE PHE A . n 
A 1 106 LEU 106 86  86  LEU LEU A . n 
A 1 107 GLU 107 87  87  GLU GLU A . n 
A 1 108 THR 108 88  88  THR THR A . n 
A 1 109 LEU 109 89  89  LEU LEU A . n 
A 1 110 SER 110 90  90  SER SER A . n 
A 1 111 GLU 111 91  91  GLU GLU A . n 
A 1 112 ILE 112 92  92  ILE ILE A . n 
A 1 113 THR 113 93  93  THR THR A . n 
A 1 114 ASN 114 94  94  ASN ASN A . n 
A 1 115 MET 115 95  95  MET MET A . n 
A 1 116 VAL 116 96  96  VAL VAL A . n 
A 1 117 PRO 117 97  97  PRO PRO A . n 
A 1 118 ARG 118 98  98  ARG ARG A . n 
A 1 119 GLU 119 99  99  GLU GLU A . n 
A 1 120 THR 120 100 100 THR THR A . n 
A 1 121 SER 121 101 101 SER SER A . n 
A 1 122 TYR 122 102 102 TYR TYR A . n 
A 1 123 HIS 123 103 103 HIS HIS A . n 
A 1 124 TYR 124 104 104 TYR TYR A . n 
A 1 125 GLY 125 105 105 GLY GLY A . n 
A 1 126 PRO 126 106 106 PRO PRO A . n 
A 1 127 TRP 127 107 107 TRP TRP A . n 
A 1 128 ASN 128 108 108 ASN ASN A . n 
A 1 129 PRO 129 109 109 PRO PRO A . n 
A 1 130 ILE 130 110 110 ILE ILE A . n 
A 1 131 GLY 131 111 111 GLY GLY A . n 
A 1 132 GLU 132 112 112 GLU GLU A . n 
A 1 133 ARG 133 113 113 ARG ARG A . n 
A 1 134 GLU 134 114 114 GLU GLU A . n 
A 1 135 ARG 135 115 115 ARG ARG A . n 
A 1 136 ARG 136 116 116 ARG ARG A . n 
A 1 137 PHE 137 117 117 PHE PHE A . n 
A 1 138 THR 138 118 118 THR THR A . n 
A 1 139 HIS 139 119 119 HIS HIS A . n 
A 1 140 PHE 140 120 120 PHE PHE A . n 
A 1 141 PRO 141 121 121 PRO PRO A . n 
A 1 142 ASP 142 122 122 ASP ASP A . n 
A 1 143 GLU 143 123 123 GLU GLU A . n 
A 1 144 ARG 144 124 124 ARG ARG A . n 
A 1 145 GLY 145 125 125 GLY GLY A . n 
A 1 146 LEU 146 126 126 LEU LEU A . n 
A 1 147 ILE 147 127 127 ILE ILE A . n 
A 1 148 GLU 148 128 128 GLU GLU A . n 
A 1 149 GLY 149 129 129 GLY GLY A . n 
A 1 150 VAL 150 130 130 VAL VAL A . n 
A 1 151 ARG 151 131 131 ARG ARG A . n 
A 1 152 ILE 152 132 132 ILE ILE A . n 
A 1 153 ALA 153 133 133 ALA ALA A . n 
A 1 154 ILE 154 134 134 ILE ILE A . n 
A 1 155 PRO 155 135 135 PRO PRO A . n 
A 1 156 GLY 156 136 136 GLY GLY A . n 
A 1 157 ILE 157 137 137 ILE ILE A . n 
A 1 158 GLU 158 138 138 GLU GLU A . n 
A 1 159 LEU 159 139 139 LEU LEU A . n 
A 1 160 ALA 160 140 140 ALA ALA A . n 
A 1 161 ILE 161 141 141 ILE ILE A . n 
A 1 162 ARG 162 142 142 ARG ARG A . n 
A 1 163 GLU 163 143 143 GLU GLU A . n 
A 1 164 ILE 164 144 144 ILE ILE A . n 
A 1 165 ASN 165 145 145 ASN ASN A . n 
A 1 166 GLN 166 146 146 GLN GLN A . n 
A 1 167 LEU 167 147 147 LEU LEU A . n 
A 1 168 SER 168 148 148 SER SER A . n 
A 1 169 ASN 169 149 149 ASN ASN A . n 
A 1 170 LEU 170 150 150 LEU LEU A . n 
A 1 171 SER 171 151 151 SER SER A . n 
A 1 172 LEU 172 152 152 LEU LEU A . n 
A 1 173 ASN 173 153 153 ASN ASN A . n 
A 1 174 ASP 174 154 154 ASP ASP A . n 
A 1 175 PRO 175 155 155 PRO PRO A . n 
A 1 176 ALA 176 156 156 ALA ALA A . n 
A 1 177 PHE 177 157 157 PHE PHE A . n 
A 1 178 GLU 178 158 158 GLU GLU A . n 
A 1 179 SER 179 159 159 SER SER A . n 
A 1 180 LEU 180 160 160 LEU LEU A . n 
A 1 181 ALA 181 161 161 ALA ALA A . n 
A 1 182 LYS 182 162 162 LYS LYS A . n 
A 1 183 SER 183 163 163 SER SER A . n 
A 1 184 ALA 184 164 164 ALA ALA A . n 
A 1 185 ALA 185 165 165 ALA ALA A . n 
A 1 186 LEU 186 166 166 LEU LEU A . n 
A 1 187 HIS 187 167 167 HIS HIS A . n 
A 1 188 VAL 188 168 168 VAL VAL A . n 
A 1 189 TYR 189 169 169 TYR TYR A . n 
A 1 190 GLN 190 170 170 GLN GLN A . n 
A 1 191 ALA 191 171 171 ALA ALA A . n 
A 1 192 VAL 192 172 172 VAL VAL A . n 
A 1 193 ASP 193 173 173 ASP ASP A . n 
A 1 194 GLY 194 174 174 GLY GLY A . n 
A 1 195 ILE 195 175 175 ILE ILE A . n 
A 1 196 GLY 196 176 176 GLY GLY A . n 
A 1 197 GLU 197 177 177 GLU GLU A . n 
A 1 198 THR 198 178 178 THR THR A . n 
A 1 199 ILE 199 179 179 ILE ILE A . n 
A 1 200 LYS 200 180 180 LYS LYS A . n 
A 1 201 LYS 201 181 181 LYS LYS A . n 
A 1 202 THR 202 182 182 THR THR A . n 
A 1 203 ASP 203 183 183 ASP ASP A . n 
A 1 204 PRO 204 184 184 PRO PRO A . n 
A 1 205 TYR 205 185 185 TYR TYR A . n 
A 1 206 VAL 206 186 186 VAL VAL A . n 
A 1 207 PHE 207 187 187 PHE PHE A . n 
A 1 208 SER 208 188 188 SER SER A . n 
A 1 209 HIS 209 189 189 HIS HIS A . n 
A 1 210 GLU 210 190 190 GLU GLU A . n 
A 1 211 LEU 211 191 191 LEU LEU A . n 
A 1 212 ARG 212 192 192 ARG ARG A . n 
A 1 213 PRO 213 193 193 PRO PRO A . n 
A 1 214 PHE 214 194 194 PHE PHE A . n 
A 1 215 PHE 215 195 195 PHE PHE A . n 
A 1 216 ASP 216 196 196 ASP ASP A . n 
A 1 217 PRO 217 197 197 PRO PRO A . n 
A 1 218 ILE 218 198 198 ILE ILE A . n 
A 1 219 ARG 219 199 199 ARG ARG A . n 
A 1 220 ILE 220 200 200 ILE ILE A . n 
A 1 221 GLY 221 201 201 GLY GLY A . n 
A 1 222 GLY 222 202 202 GLY GLY A . n 
A 1 223 LYS 223 203 203 LYS LYS A . n 
A 1 224 SER 224 204 204 SER SER A . n 
A 1 225 TYR 225 205 205 TYR TYR A . n 
A 1 226 ILE 226 206 206 ILE ILE A . n 
A 1 227 GLY 227 207 207 GLY GLY A . n 
A 1 228 ALA 228 208 208 ALA ALA A . n 
A 1 229 GLY 229 209 209 GLY GLY A . n 
A 1 230 GLY 230 210 210 GLY GLY A . n 
A 1 231 GLY 231 211 211 GLY GLY A . n 
A 1 232 GLN 232 212 212 GLN GLN A . n 
A 1 233 ILE 233 213 213 ILE ILE A . n 
A 1 234 PRO 234 214 214 PRO PRO A . n 
A 1 235 LEU 235 215 215 LEU LEU A . n 
A 1 236 PHE 236 216 216 PHE PHE A . n 
A 1 237 VAL 237 217 217 VAL VAL A . n 
A 1 238 VAL 238 218 218 VAL VAL A . n 
A 1 239 ASP 239 219 219 ASP ASP A . n 
A 1 240 VAL 240 220 220 VAL VAL A . n 
A 1 241 LYS 241 221 221 LYS LYS A . n 
A 1 242 LEU 242 222 222 LEU LEU A . n 
A 1 243 TRP 243 223 223 TRP TRP A . n 
A 1 244 LEU 244 224 224 LEU LEU A . n 
A 1 245 GLY 245 225 225 GLY GLY A . n 
A 1 246 ASN 246 226 226 ASN ASN A . n 
A 1 247 HIS 247 227 227 HIS HIS A . n 
A 1 248 SER 248 228 228 SER SER A . n 
A 1 249 PRO 249 229 229 PRO PRO A . n 
A 1 250 ASN 250 230 230 ASN ASN A . n 
A 1 251 SER 251 231 231 SER SER A . n 
A 1 252 GLU 252 232 232 GLU GLU A . n 
A 1 253 TYR 253 233 233 TYR TYR A . n 
A 1 254 VAL 254 234 234 VAL VAL A . n 
A 1 255 SER 255 235 235 SER SER A . n 
A 1 256 PHE 256 236 236 PHE PHE A . n 
A 1 257 ILE 257 237 237 ILE ILE A . n 
A 1 258 LYS 258 238 238 LYS LYS A . n 
A 1 259 ASP 259 239 239 ASP ASP A . n 
A 1 260 SER 260 240 240 SER SER A . n 
A 1 261 VAL 261 241 241 VAL VAL A . n 
A 1 262 PHE 262 242 242 PHE PHE A . n 
A 1 263 TYR 263 243 243 TYR TYR A . n 
A 1 264 LEU 264 244 244 LEU LEU A . n 
A 1 265 PRO 265 245 245 PRO PRO A . n 
A 1 266 PRO 266 246 246 PRO PRO A . n 
A 1 267 GLU 267 247 247 GLU GLU A . n 
A 1 268 LEU 268 248 248 LEU LEU A . n 
A 1 269 ARG 269 249 249 ARG ARG A . n 
A 1 270 PRO 270 250 250 PRO PRO A . n 
A 1 271 ILE 271 251 251 ILE ILE A . n 
A 1 272 CYS 272 252 252 CYS CYS A . n 
A 1 273 VAL 273 253 253 VAL VAL A . n 
A 1 274 ASP 274 254 254 ASP ASP A . n 
A 1 275 SER 275 255 255 SER SER A . n 
A 1 276 LEU 276 256 256 LEU LEU A . n 
A 1 277 LEU 277 257 257 LEU LEU A . n 
A 1 278 GLU 278 258 258 GLU GLU A . n 
A 1 279 PRO 279 259 259 PRO PRO A . n 
A 1 280 SER 280 260 260 SER SER A . n 
A 1 281 VAL 281 261 261 VAL VAL A . n 
A 1 282 ILE 282 262 262 ILE ILE A . n 
A 1 283 ASN 283 263 263 ASN ASN A . n 
A 1 284 GLN 284 264 264 GLN GLN A . n 
A 1 285 LYS 285 265 265 LYS LYS A . n 
A 1 286 PHE 286 266 266 PHE PHE A . n 
A 1 287 ALA 287 267 267 ALA ALA A . n 
A 1 288 GLU 288 268 268 GLU GLU A . n 
A 1 289 PHE 289 269 269 PHE PHE A . n 
A 1 290 GLY 290 270 270 GLY GLY A . n 
A 1 291 SER 291 271 271 SER SER A . n 
A 1 292 VAL 292 272 272 VAL VAL A . n 
A 1 293 GLU 293 273 273 GLU GLU A . n 
A 1 294 ILE 294 274 274 ILE ILE A . n 
A 1 295 THR 295 275 275 THR THR A . n 
A 1 296 ASP 296 276 276 ASP ASP A . n 
A 1 297 GLN 297 277 277 GLN GLN A . n 
A 1 298 VAL 298 278 278 VAL VAL A . n 
A 1 299 ILE 299 279 279 ILE ILE A . n 
A 1 300 LYS 300 280 280 LYS LYS A . n 
A 1 301 GLY 301 281 281 GLY GLY A . n 
A 1 302 MET 302 282 282 MET MET A . n 
A 1 303 GLU 303 283 283 GLU GLU A . n 
A 1 304 SER 304 284 284 SER SER A . n 
A 1 305 LEU 305 285 285 LEU LEU A . n 
A 1 306 LEU 306 286 286 LEU LEU A . n 
A 1 307 SER 307 287 287 SER SER A . n 
A 1 308 VAL 308 288 288 VAL VAL A . n 
A 1 309 ILE 309 289 289 ILE ILE A . n 
A 1 310 GLN 310 290 290 GLN GLN A . n 
A 1 311 VAL 311 291 291 VAL VAL A . n 
A 1 312 LEU 312 292 292 LEU LEU A . n 
A 1 313 LEU 313 293 293 LEU LEU A . n 
A 1 314 LYS 314 294 294 LYS LYS A . n 
A 1 315 PHE 315 295 295 PHE PHE A . n 
A 1 316 ARG 316 296 296 ARG ARG A . n 
A 1 317 LYS 317 297 297 LYS LYS A . n 
A 1 318 PRO 318 298 298 PRO PRO A . n 
A 1 319 HIS 319 299 299 HIS HIS A . n 
A 1 320 PHE 320 300 300 PHE PHE A . n 
A 1 321 GLN 321 301 301 GLN GLN A . n 
A 1 322 LEU 322 302 302 LEU LEU A . n 
A 1 323 ALA 323 303 303 ALA ALA A . n 
A 1 324 GLN 324 304 304 GLN GLN A . n 
A 1 325 ARG 325 305 305 ARG ARG A . n 
A 1 326 THR 326 306 306 THR THR A . n 
A 1 327 LEU 327 307 307 LEU LEU A . n 
A 1 328 SER 328 308 308 SER SER A . n 
A 1 329 LYS 329 309 309 LYS LYS A . n 
A 1 330 GLU 330 310 310 GLU GLU A . n 
A 1 331 ASN 331 311 311 ASN ASN A . n 
A 1 332 ARG 332 312 312 ARG ARG A . n 
A 1 333 GLY 333 313 313 GLY GLY A . n 
A 1 334 ASN 334 314 314 ASN ASN A . n 
A 1 335 TYR 335 315 315 TYR TYR A . n 
A 1 336 THR 336 316 316 THR THR A . n 
A 1 337 THR 337 317 317 THR THR A . n 
A 1 338 GLY 338 318 318 GLY GLY A . n 
A 1 339 SER 339 319 319 SER SER A . n 
A 1 340 ALA 340 320 320 ALA ALA A . n 
A 1 341 GLY 341 321 321 GLY GLY A . n 
A 1 342 TYR 342 322 322 TYR TYR A . n 
A 1 343 THR 343 323 323 THR THR A . n 
A 1 344 ASN 344 324 324 ASN ASN A . n 
A 1 345 SER 345 325 325 SER SER A . n 
A 1 346 PHE 346 326 326 PHE PHE A . n 
A 1 347 ASN 347 327 327 ASN ASN A . n 
A 1 348 HIS 348 328 328 HIS HIS A . n 
A 1 349 MET 349 329 329 MET MET A . n 
A 1 350 VAL 350 330 330 VAL VAL A . n 
A 1 351 LEU 351 331 331 LEU LEU A . n 
A 1 352 GLU 352 332 332 GLU GLU A . n 
A 1 353 PHE 353 333 333 PHE PHE A . n 
A 1 354 THR 354 334 334 THR THR A . n 
A 1 355 ILE 355 335 335 ILE ILE A . n 
A 1 356 GLU 356 336 336 GLU GLU A . n 
A 1 357 VAL 357 337 337 VAL VAL A . n 
A 1 358 GLU 358 338 338 GLU GLU A . n 
A 1 359 LYS 359 339 339 LYS LYS A . n 
A 1 360 GLN 360 340 340 GLN GLN A . n 
A 1 361 ILE 361 341 341 ILE ILE A . n 
A 1 362 ARG 362 342 342 ARG ARG A . n 
A 1 363 ALA 363 343 343 ALA ALA A . n 
A 1 364 VAL 364 344 344 VAL VAL A . n 
A 1 365 LEU 365 345 345 LEU LEU A . n 
A 1 366 ALA 366 346 346 ALA ALA A . n 
A 1 367 PRO 367 347 347 PRO PRO A . n 
A 1 368 TYR 368 348 ?   ?   ?   A . n 
A 1 369 ARG 369 349 ?   ?   ?   A . n 
A 1 370 SER 370 350 ?   ?   ?   A . n 
B 1 1   MET 1   -19 ?   ?   ?   B . n 
B 1 2   GLY 2   -18 ?   ?   ?   B . n 
B 1 3   SER 3   -17 ?   ?   ?   B . n 
B 1 4   SER 4   -16 ?   ?   ?   B . n 
B 1 5   HIS 5   -15 ?   ?   ?   B . n 
B 1 6   HIS 6   -14 ?   ?   ?   B . n 
B 1 7   HIS 7   -13 ?   ?   ?   B . n 
B 1 8   HIS 8   -12 ?   ?   ?   B . n 
B 1 9   HIS 9   -11 ?   ?   ?   B . n 
B 1 10  HIS 10  -10 ?   ?   ?   B . n 
B 1 11  SER 11  -9  ?   ?   ?   B . n 
B 1 12  SER 12  -8  ?   ?   ?   B . n 
B 1 13  GLY 13  -7  ?   ?   ?   B . n 
B 1 14  GLU 14  -6  ?   ?   ?   B . n 
B 1 15  ASN 15  -5  ?   ?   ?   B . n 
B 1 16  LEU 16  -4  ?   ?   ?   B . n 
B 1 17  TYR 17  -3  ?   ?   ?   B . n 
B 1 18  PHE 18  -2  ?   ?   ?   B . n 
B 1 19  GLN 19  -1  -1  GLN GLN B . n 
B 1 20  GLY 20  0   0   GLY GLY B . n 
B 1 21  MET 21  1   1   MET MET B . n 
B 1 22  ILE 22  2   2   ILE ILE B . n 
B 1 23  SER 23  3   3   SER SER B . n 
B 1 24  ASN 24  4   4   ASN ASN B . n 
B 1 25  GLU 25  5   5   GLU GLU B . n 
B 1 26  ILE 26  6   6   ILE ILE B . n 
B 1 27  SER 27  7   7   SER SER B . n 
B 1 28  LYS 28  8   8   LYS LYS B . n 
B 1 29  LEU 29  9   9   LEU LEU B . n 
B 1 30  ASP 30  10  10  ASP ASP B . n 
B 1 31  PRO 31  11  11  PRO PRO B . n 
B 1 32  LEU 32  12  12  LEU LEU B . n 
B 1 33  ASN 33  13  13  ASN ASN B . n 
B 1 34  LEU 34  14  14  LEU LEU B . n 
B 1 35  ASP 35  15  15  ASP ASP B . n 
B 1 36  ALA 36  16  16  ALA ALA B . n 
B 1 37  PHE 37  17  17  PHE PHE B . n 
B 1 38  PHE 38  18  18  PHE PHE B . n 
B 1 39  ASN 39  19  19  ASN ASN B . n 
B 1 40  GLN 40  20  20  GLN GLN B . n 
B 1 41  LEU 41  21  21  LEU LEU B . n 
B 1 42  PRO 42  22  22  PRO PRO B . n 
B 1 43  SER 43  23  23  SER SER B . n 
B 1 44  LEU 44  24  24  LEU LEU B . n 
B 1 45  ASN 45  25  25  ASN ASN B . n 
B 1 46  GLN 46  26  26  GLN GLN B . n 
B 1 47  ASN 47  27  27  ASN ASN B . n 
B 1 48  LEU 48  28  28  LEU LEU B . n 
B 1 49  GLU 49  29  29  GLU GLU B . n 
B 1 50  VAL 50  30  30  VAL VAL B . n 
B 1 51  SER 51  31  31  SER SER B . n 
B 1 52  LEU 52  32  32  LEU LEU B . n 
B 1 53  LEU 53  33  33  LEU LEU B . n 
B 1 54  ILE 54  34  34  ILE ILE B . n 
B 1 55  ASP 55  35  35  ASP ASP B . n 
B 1 56  LYS 56  36  36  LYS LYS B . n 
B 1 57  LEU 57  37  37  LEU LEU B . n 
B 1 58  ARG 58  38  38  ARG ARG B . n 
B 1 59  GLU 59  39  39  GLU GLU B . n 
B 1 60  ILE 60  40  40  ILE ILE B . n 
B 1 61  THR 61  41  41  THR THR B . n 
B 1 62  LYS 62  42  42  LYS LYS B . n 
B 1 63  SER 63  43  43  SER SER B . n 
B 1 64  TYR 64  44  44  TYR TYR B . n 
B 1 65  LEU 65  45  45  LEU LEU B . n 
B 1 66  PRO 66  46  46  PRO PRO B . n 
B 1 67  THR 67  47  47  THR THR B . n 
B 1 68  THR 68  48  48  THR THR B . n 
B 1 69  PHE 69  49  49  PHE PHE B . n 
B 1 70  SER 70  50  50  SER SER B . n 
B 1 71  ILE 71  51  51  ILE ILE B . n 
B 1 72  ASN 72  52  52  ASN ASN B . n 
B 1 73  ASP 73  53  53  ASP ASP B . n 
B 1 74  ALA 74  54  54  ALA ALA B . n 
B 1 75  LEU 75  55  55  LEU LEU B . n 
B 1 76  ALA 76  56  56  ALA ALA B . n 
B 1 77  ALA 77  57  57  ALA ALA B . n 
B 1 78  THR 78  58  58  THR THR B . n 
B 1 79  ARG 79  59  59  ARG ARG B . n 
B 1 80  ASP 80  60  60  ASP ASP B . n 
B 1 81  LEU 81  61  61  LEU LEU B . n 
B 1 82  GLY 82  62  62  GLY GLY B . n 
B 1 83  MET 83  63  63  MET MET B . n 
B 1 84  ILE 84  64  64  ILE ILE B . n 
B 1 85  MET 85  65  65  MET MET B . n 
B 1 86  SER 86  66  66  SER SER B . n 
B 1 87  SER 87  67  67  SER SER B . n 
B 1 88  VAL 88  68  68  VAL VAL B . n 
B 1 89  ARG 89  69  69  ARG ARG B . n 
B 1 90  LYS 90  70  70  LYS LYS B . n 
B 1 91  LEU 91  71  71  LEU LEU B . n 
B 1 92  GLY 92  72  72  GLY GLY B . n 
B 1 93  ILE 93  73  73  ILE ILE B . n 
B 1 94  GLN 94  74  74  GLN GLN B . n 
B 1 95  PRO 95  75  75  PRO PRO B . n 
B 1 96  VAL 96  76  76  VAL VAL B . n 
B 1 97  SER 97  77  77  SER SER B . n 
B 1 98  ALA 98  78  78  ALA ALA B . n 
B 1 99  VAL 99  79  79  VAL VAL B . n 
B 1 100 SER 100 80  80  SER SER B . n 
B 1 101 ASP 101 81  81  ASP ASP B . n 
B 1 102 LEU 102 82  82  LEU LEU B . n 
B 1 103 GLU 103 83  83  GLU GLU B . n 
B 1 104 VAL 104 84  84  VAL VAL B . n 
B 1 105 PHE 105 85  85  PHE PHE B . n 
B 1 106 LEU 106 86  86  LEU LEU B . n 
B 1 107 GLU 107 87  87  GLU GLU B . n 
B 1 108 THR 108 88  88  THR THR B . n 
B 1 109 LEU 109 89  89  LEU LEU B . n 
B 1 110 SER 110 90  90  SER SER B . n 
B 1 111 GLU 111 91  91  GLU GLU B . n 
B 1 112 ILE 112 92  92  ILE ILE B . n 
B 1 113 THR 113 93  93  THR THR B . n 
B 1 114 ASN 114 94  94  ASN ASN B . n 
B 1 115 MET 115 95  95  MET MET B . n 
B 1 116 VAL 116 96  96  VAL VAL B . n 
B 1 117 PRO 117 97  97  PRO PRO B . n 
B 1 118 ARG 118 98  98  ARG ARG B . n 
B 1 119 GLU 119 99  99  GLU GLU B . n 
B 1 120 THR 120 100 100 THR THR B . n 
B 1 121 SER 121 101 101 SER SER B . n 
B 1 122 TYR 122 102 102 TYR TYR B . n 
B 1 123 HIS 123 103 103 HIS HIS B . n 
B 1 124 TYR 124 104 104 TYR TYR B . n 
B 1 125 GLY 125 105 105 GLY GLY B . n 
B 1 126 PRO 126 106 106 PRO PRO B . n 
B 1 127 TRP 127 107 107 TRP TRP B . n 
B 1 128 ASN 128 108 108 ASN ASN B . n 
B 1 129 PRO 129 109 109 PRO PRO B . n 
B 1 130 ILE 130 110 110 ILE ILE B . n 
B 1 131 GLY 131 111 111 GLY GLY B . n 
B 1 132 GLU 132 112 112 GLU GLU B . n 
B 1 133 ARG 133 113 113 ARG ARG B . n 
B 1 134 GLU 134 114 114 GLU GLU B . n 
B 1 135 ARG 135 115 115 ARG ARG B . n 
B 1 136 ARG 136 116 116 ARG ARG B . n 
B 1 137 PHE 137 117 117 PHE PHE B . n 
B 1 138 THR 138 118 118 THR THR B . n 
B 1 139 HIS 139 119 119 HIS HIS B . n 
B 1 140 PHE 140 120 120 PHE PHE B . n 
B 1 141 PRO 141 121 121 PRO PRO B . n 
B 1 142 ASP 142 122 122 ASP ASP B . n 
B 1 143 GLU 143 123 123 GLU GLU B . n 
B 1 144 ARG 144 124 124 ARG ARG B . n 
B 1 145 GLY 145 125 125 GLY GLY B . n 
B 1 146 LEU 146 126 126 LEU LEU B . n 
B 1 147 ILE 147 127 127 ILE ILE B . n 
B 1 148 GLU 148 128 128 GLU GLU B . n 
B 1 149 GLY 149 129 129 GLY GLY B . n 
B 1 150 VAL 150 130 130 VAL VAL B . n 
B 1 151 ARG 151 131 131 ARG ARG B . n 
B 1 152 ILE 152 132 132 ILE ILE B . n 
B 1 153 ALA 153 133 133 ALA ALA B . n 
B 1 154 ILE 154 134 134 ILE ILE B . n 
B 1 155 PRO 155 135 135 PRO PRO B . n 
B 1 156 GLY 156 136 136 GLY GLY B . n 
B 1 157 ILE 157 137 137 ILE ILE B . n 
B 1 158 GLU 158 138 138 GLU GLU B . n 
B 1 159 LEU 159 139 139 LEU LEU B . n 
B 1 160 ALA 160 140 140 ALA ALA B . n 
B 1 161 ILE 161 141 141 ILE ILE B . n 
B 1 162 ARG 162 142 142 ARG ARG B . n 
B 1 163 GLU 163 143 143 GLU GLU B . n 
B 1 164 ILE 164 144 144 ILE ILE B . n 
B 1 165 ASN 165 145 145 ASN ASN B . n 
B 1 166 GLN 166 146 146 GLN GLN B . n 
B 1 167 LEU 167 147 147 LEU LEU B . n 
B 1 168 SER 168 148 148 SER SER B . n 
B 1 169 ASN 169 149 149 ASN ASN B . n 
B 1 170 LEU 170 150 150 LEU LEU B . n 
B 1 171 SER 171 151 151 SER SER B . n 
B 1 172 LEU 172 152 152 LEU LEU B . n 
B 1 173 ASN 173 153 153 ASN ASN B . n 
B 1 174 ASP 174 154 154 ASP ASP B . n 
B 1 175 PRO 175 155 155 PRO PRO B . n 
B 1 176 ALA 176 156 156 ALA ALA B . n 
B 1 177 PHE 177 157 157 PHE PHE B . n 
B 1 178 GLU 178 158 158 GLU GLU B . n 
B 1 179 SER 179 159 159 SER SER B . n 
B 1 180 LEU 180 160 160 LEU LEU B . n 
B 1 181 ALA 181 161 161 ALA ALA B . n 
B 1 182 LYS 182 162 162 LYS LYS B . n 
B 1 183 SER 183 163 163 SER SER B . n 
B 1 184 ALA 184 164 164 ALA ALA B . n 
B 1 185 ALA 185 165 165 ALA ALA B . n 
B 1 186 LEU 186 166 166 LEU LEU B . n 
B 1 187 HIS 187 167 167 HIS HIS B . n 
B 1 188 VAL 188 168 168 VAL VAL B . n 
B 1 189 TYR 189 169 169 TYR TYR B . n 
B 1 190 GLN 190 170 170 GLN GLN B . n 
B 1 191 ALA 191 171 171 ALA ALA B . n 
B 1 192 VAL 192 172 172 VAL VAL B . n 
B 1 193 ASP 193 173 173 ASP ASP B . n 
B 1 194 GLY 194 174 174 GLY GLY B . n 
B 1 195 ILE 195 175 175 ILE ILE B . n 
B 1 196 GLY 196 176 176 GLY GLY B . n 
B 1 197 GLU 197 177 177 GLU GLU B . n 
B 1 198 THR 198 178 178 THR THR B . n 
B 1 199 ILE 199 179 179 ILE ILE B . n 
B 1 200 LYS 200 180 180 LYS LYS B . n 
B 1 201 LYS 201 181 181 LYS LYS B . n 
B 1 202 THR 202 182 182 THR THR B . n 
B 1 203 ASP 203 183 183 ASP ASP B . n 
B 1 204 PRO 204 184 184 PRO PRO B . n 
B 1 205 TYR 205 185 185 TYR TYR B . n 
B 1 206 VAL 206 186 186 VAL VAL B . n 
B 1 207 PHE 207 187 187 PHE PHE B . n 
B 1 208 SER 208 188 188 SER SER B . n 
B 1 209 HIS 209 189 189 HIS HIS B . n 
B 1 210 GLU 210 190 190 GLU GLU B . n 
B 1 211 LEU 211 191 191 LEU LEU B . n 
B 1 212 ARG 212 192 192 ARG ARG B . n 
B 1 213 PRO 213 193 193 PRO PRO B . n 
B 1 214 PHE 214 194 194 PHE PHE B . n 
B 1 215 PHE 215 195 195 PHE PHE B . n 
B 1 216 ASP 216 196 196 ASP ASP B . n 
B 1 217 PRO 217 197 197 PRO PRO B . n 
B 1 218 ILE 218 198 198 ILE ILE B . n 
B 1 219 ARG 219 199 199 ARG ARG B . n 
B 1 220 ILE 220 200 200 ILE ILE B . n 
B 1 221 GLY 221 201 201 GLY GLY B . n 
B 1 222 GLY 222 202 202 GLY GLY B . n 
B 1 223 LYS 223 203 203 LYS LYS B . n 
B 1 224 SER 224 204 204 SER SER B . n 
B 1 225 TYR 225 205 205 TYR TYR B . n 
B 1 226 ILE 226 206 206 ILE ILE B . n 
B 1 227 GLY 227 207 207 GLY GLY B . n 
B 1 228 ALA 228 208 208 ALA ALA B . n 
B 1 229 GLY 229 209 209 GLY GLY B . n 
B 1 230 GLY 230 210 210 GLY GLY B . n 
B 1 231 GLY 231 211 211 GLY GLY B . n 
B 1 232 GLN 232 212 212 GLN GLN B . n 
B 1 233 ILE 233 213 213 ILE ILE B . n 
B 1 234 PRO 234 214 214 PRO PRO B . n 
B 1 235 LEU 235 215 215 LEU LEU B . n 
B 1 236 PHE 236 216 216 PHE PHE B . n 
B 1 237 VAL 237 217 217 VAL VAL B . n 
B 1 238 VAL 238 218 218 VAL VAL B . n 
B 1 239 ASP 239 219 219 ASP ASP B . n 
B 1 240 VAL 240 220 220 VAL VAL B . n 
B 1 241 LYS 241 221 221 LYS LYS B . n 
B 1 242 LEU 242 222 222 LEU LEU B . n 
B 1 243 TRP 243 223 223 TRP TRP B . n 
B 1 244 LEU 244 224 224 LEU LEU B . n 
B 1 245 GLY 245 225 225 GLY GLY B . n 
B 1 246 ASN 246 226 226 ASN ASN B . n 
B 1 247 HIS 247 227 227 HIS HIS B . n 
B 1 248 SER 248 228 228 SER SER B . n 
B 1 249 PRO 249 229 229 PRO PRO B . n 
B 1 250 ASN 250 230 230 ASN ASN B . n 
B 1 251 SER 251 231 231 SER SER B . n 
B 1 252 GLU 252 232 232 GLU GLU B . n 
B 1 253 TYR 253 233 233 TYR TYR B . n 
B 1 254 VAL 254 234 234 VAL VAL B . n 
B 1 255 SER 255 235 235 SER SER B . n 
B 1 256 PHE 256 236 236 PHE PHE B . n 
B 1 257 ILE 257 237 237 ILE ILE B . n 
B 1 258 LYS 258 238 238 LYS LYS B . n 
B 1 259 ASP 259 239 239 ASP ASP B . n 
B 1 260 SER 260 240 240 SER SER B . n 
B 1 261 VAL 261 241 241 VAL VAL B . n 
B 1 262 PHE 262 242 242 PHE PHE B . n 
B 1 263 TYR 263 243 243 TYR TYR B . n 
B 1 264 LEU 264 244 244 LEU LEU B . n 
B 1 265 PRO 265 245 245 PRO PRO B . n 
B 1 266 PRO 266 246 246 PRO PRO B . n 
B 1 267 GLU 267 247 247 GLU GLU B . n 
B 1 268 LEU 268 248 248 LEU LEU B . n 
B 1 269 ARG 269 249 249 ARG ARG B . n 
B 1 270 PRO 270 250 250 PRO PRO B . n 
B 1 271 ILE 271 251 251 ILE ILE B . n 
B 1 272 CYS 272 252 252 CYS CYS B . n 
B 1 273 VAL 273 253 253 VAL VAL B . n 
B 1 274 ASP 274 254 254 ASP ASP B . n 
B 1 275 SER 275 255 255 SER SER B . n 
B 1 276 LEU 276 256 256 LEU LEU B . n 
B 1 277 LEU 277 257 257 LEU LEU B . n 
B 1 278 GLU 278 258 258 GLU GLU B . n 
B 1 279 PRO 279 259 259 PRO PRO B . n 
B 1 280 SER 280 260 260 SER SER B . n 
B 1 281 VAL 281 261 261 VAL VAL B . n 
B 1 282 ILE 282 262 262 ILE ILE B . n 
B 1 283 ASN 283 263 263 ASN ASN B . n 
B 1 284 GLN 284 264 264 GLN GLN B . n 
B 1 285 LYS 285 265 265 LYS LYS B . n 
B 1 286 PHE 286 266 266 PHE PHE B . n 
B 1 287 ALA 287 267 267 ALA ALA B . n 
B 1 288 GLU 288 268 268 GLU GLU B . n 
B 1 289 PHE 289 269 269 PHE PHE B . n 
B 1 290 GLY 290 270 270 GLY GLY B . n 
B 1 291 SER 291 271 271 SER SER B . n 
B 1 292 VAL 292 272 272 VAL VAL B . n 
B 1 293 GLU 293 273 273 GLU GLU B . n 
B 1 294 ILE 294 274 274 ILE ILE B . n 
B 1 295 THR 295 275 275 THR THR B . n 
B 1 296 ASP 296 276 276 ASP ASP B . n 
B 1 297 GLN 297 277 277 GLN GLN B . n 
B 1 298 VAL 298 278 278 VAL VAL B . n 
B 1 299 ILE 299 279 279 ILE ILE B . n 
B 1 300 LYS 300 280 280 LYS LYS B . n 
B 1 301 GLY 301 281 281 GLY GLY B . n 
B 1 302 MET 302 282 282 MET MET B . n 
B 1 303 GLU 303 283 283 GLU GLU B . n 
B 1 304 SER 304 284 284 SER SER B . n 
B 1 305 LEU 305 285 285 LEU LEU B . n 
B 1 306 LEU 306 286 286 LEU LEU B . n 
B 1 307 SER 307 287 287 SER SER B . n 
B 1 308 VAL 308 288 288 VAL VAL B . n 
B 1 309 ILE 309 289 289 ILE ILE B . n 
B 1 310 GLN 310 290 290 GLN GLN B . n 
B 1 311 VAL 311 291 291 VAL VAL B . n 
B 1 312 LEU 312 292 292 LEU LEU B . n 
B 1 313 LEU 313 293 293 LEU LEU B . n 
B 1 314 LYS 314 294 294 LYS LYS B . n 
B 1 315 PHE 315 295 295 PHE PHE B . n 
B 1 316 ARG 316 296 296 ARG ARG B . n 
B 1 317 LYS 317 297 297 LYS LYS B . n 
B 1 318 PRO 318 298 298 PRO PRO B . n 
B 1 319 HIS 319 299 299 HIS HIS B . n 
B 1 320 PHE 320 300 300 PHE PHE B . n 
B 1 321 GLN 321 301 301 GLN GLN B . n 
B 1 322 LEU 322 302 302 LEU LEU B . n 
B 1 323 ALA 323 303 303 ALA ALA B . n 
B 1 324 GLN 324 304 304 GLN GLN B . n 
B 1 325 ARG 325 305 305 ARG ARG B . n 
B 1 326 THR 326 306 306 THR THR B . n 
B 1 327 LEU 327 307 307 LEU LEU B . n 
B 1 328 SER 328 308 308 SER SER B . n 
B 1 329 LYS 329 309 309 LYS LYS B . n 
B 1 330 GLU 330 310 310 GLU GLU B . n 
B 1 331 ASN 331 311 311 ASN ASN B . n 
B 1 332 ARG 332 312 312 ARG ARG B . n 
B 1 333 GLY 333 313 313 GLY GLY B . n 
B 1 334 ASN 334 314 314 ASN ASN B . n 
B 1 335 TYR 335 315 315 TYR TYR B . n 
B 1 336 THR 336 316 316 THR THR B . n 
B 1 337 THR 337 317 317 THR THR B . n 
B 1 338 GLY 338 318 318 GLY GLY B . n 
B 1 339 SER 339 319 319 SER SER B . n 
B 1 340 ALA 340 320 320 ALA ALA B . n 
B 1 341 GLY 341 321 321 GLY GLY B . n 
B 1 342 TYR 342 322 322 TYR TYR B . n 
B 1 343 THR 343 323 323 THR THR B . n 
B 1 344 ASN 344 324 324 ASN ASN B . n 
B 1 345 SER 345 325 325 SER SER B . n 
B 1 346 PHE 346 326 326 PHE PHE B . n 
B 1 347 ASN 347 327 327 ASN ASN B . n 
B 1 348 HIS 348 328 328 HIS HIS B . n 
B 1 349 MET 349 329 329 MET MET B . n 
B 1 350 VAL 350 330 330 VAL VAL B . n 
B 1 351 LEU 351 331 331 LEU LEU B . n 
B 1 352 GLU 352 332 332 GLU GLU B . n 
B 1 353 PHE 353 333 333 PHE PHE B . n 
B 1 354 THR 354 334 334 THR THR B . n 
B 1 355 ILE 355 335 335 ILE ILE B . n 
B 1 356 GLU 356 336 336 GLU GLU B . n 
B 1 357 VAL 357 337 337 VAL VAL B . n 
B 1 358 GLU 358 338 338 GLU GLU B . n 
B 1 359 LYS 359 339 339 LYS LYS B . n 
B 1 360 GLN 360 340 340 GLN GLN B . n 
B 1 361 ILE 361 341 341 ILE ILE B . n 
B 1 362 ARG 362 342 342 ARG ARG B . n 
B 1 363 ALA 363 343 343 ALA ALA B . n 
B 1 364 VAL 364 344 344 VAL VAL B . n 
B 1 365 LEU 365 345 345 LEU LEU B . n 
B 1 366 ALA 366 346 346 ALA ALA B . n 
B 1 367 PRO 367 347 347 PRO PRO B . n 
B 1 368 TYR 368 348 348 TYR TYR B . n 
B 1 369 ARG 369 349 ?   ?   ?   B . n 
B 1 370 SER 370 350 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 HEM ? ? HEM ? ? 'SUBJECT OF INVESTIGATION' ? 
2 IOP ? ? IOP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEM 1   401 381 HEM HEM A . 
D 3 IOP 1   402 401 IOP IOP A . 
E 4 GOL 1   403 501 GOL GOL A . 
F 4 GOL 1   404 601 GOL GOL A . 
G 4 GOL 1   405 701 GOL GOL A . 
H 2 HEM 1   401 381 HEM HEM B . 
I 3 IOP 1   402 401 IOP IOP B . 
J 5 TRS 1   403 502 TRS TRS B . 
K 6 HOH 1   501 14  HOH HOH A . 
K 6 HOH 2   502 188 HOH HOH A . 
K 6 HOH 3   503 224 HOH HOH A . 
K 6 HOH 4   504 257 HOH HOH A . 
K 6 HOH 5   505 64  HOH HOH A . 
K 6 HOH 6   506 106 HOH HOH A . 
K 6 HOH 7   507 174 HOH HOH A . 
K 6 HOH 8   508 194 HOH HOH A . 
K 6 HOH 9   509 238 HOH HOH A . 
K 6 HOH 10  510 198 HOH HOH A . 
K 6 HOH 11  511 118 HOH HOH A . 
K 6 HOH 12  512 47  HOH HOH A . 
K 6 HOH 13  513 219 HOH HOH A . 
K 6 HOH 14  514 299 HOH HOH A . 
K 6 HOH 15  515 155 HOH HOH A . 
K 6 HOH 16  516 316 HOH HOH A . 
K 6 HOH 17  517 52  HOH HOH A . 
K 6 HOH 18  518 172 HOH HOH A . 
K 6 HOH 19  519 50  HOH HOH A . 
K 6 HOH 20  520 163 HOH HOH A . 
K 6 HOH 21  521 63  HOH HOH A . 
K 6 HOH 22  522 109 HOH HOH A . 
K 6 HOH 23  523 20  HOH HOH A . 
K 6 HOH 24  524 298 HOH HOH A . 
K 6 HOH 25  525 126 HOH HOH A . 
K 6 HOH 26  526 77  HOH HOH A . 
K 6 HOH 27  527 306 HOH HOH A . 
K 6 HOH 28  528 196 HOH HOH A . 
K 6 HOH 29  529 90  HOH HOH A . 
K 6 HOH 30  530 10  HOH HOH A . 
K 6 HOH 31  531 154 HOH HOH A . 
K 6 HOH 32  532 158 HOH HOH A . 
K 6 HOH 33  533 2   HOH HOH A . 
K 6 HOH 34  534 149 HOH HOH A . 
K 6 HOH 35  535 73  HOH HOH A . 
K 6 HOH 36  536 36  HOH HOH A . 
K 6 HOH 37  537 110 HOH HOH A . 
K 6 HOH 38  538 34  HOH HOH A . 
K 6 HOH 39  539 134 HOH HOH A . 
K 6 HOH 40  540 182 HOH HOH A . 
K 6 HOH 41  541 213 HOH HOH A . 
K 6 HOH 42  542 242 HOH HOH A . 
K 6 HOH 43  543 78  HOH HOH A . 
K 6 HOH 44  544 67  HOH HOH A . 
K 6 HOH 45  545 142 HOH HOH A . 
K 6 HOH 46  546 53  HOH HOH A . 
K 6 HOH 47  547 124 HOH HOH A . 
K 6 HOH 48  548 43  HOH HOH A . 
K 6 HOH 49  549 121 HOH HOH A . 
K 6 HOH 50  550 84  HOH HOH A . 
K 6 HOH 51  551 70  HOH HOH A . 
K 6 HOH 52  552 83  HOH HOH A . 
K 6 HOH 53  553 88  HOH HOH A . 
K 6 HOH 54  554 216 HOH HOH A . 
K 6 HOH 55  555 11  HOH HOH A . 
K 6 HOH 56  556 85  HOH HOH A . 
K 6 HOH 57  557 297 HOH HOH A . 
K 6 HOH 58  558 72  HOH HOH A . 
K 6 HOH 59  559 135 HOH HOH A . 
K 6 HOH 60  560 132 HOH HOH A . 
K 6 HOH 61  561 162 HOH HOH A . 
K 6 HOH 62  562 15  HOH HOH A . 
K 6 HOH 63  563 48  HOH HOH A . 
K 6 HOH 64  564 152 HOH HOH A . 
K 6 HOH 65  565 60  HOH HOH A . 
K 6 HOH 66  566 104 HOH HOH A . 
K 6 HOH 67  567 140 HOH HOH A . 
K 6 HOH 68  568 113 HOH HOH A . 
K 6 HOH 69  569 82  HOH HOH A . 
K 6 HOH 70  570 30  HOH HOH A . 
K 6 HOH 71  571 136 HOH HOH A . 
K 6 HOH 72  572 246 HOH HOH A . 
K 6 HOH 73  573 18  HOH HOH A . 
K 6 HOH 74  574 117 HOH HOH A . 
K 6 HOH 75  575 249 HOH HOH A . 
K 6 HOH 76  576 201 HOH HOH A . 
K 6 HOH 77  577 37  HOH HOH A . 
K 6 HOH 78  578 156 HOH HOH A . 
K 6 HOH 79  579 159 HOH HOH A . 
K 6 HOH 80  580 115 HOH HOH A . 
K 6 HOH 81  581 26  HOH HOH A . 
K 6 HOH 82  582 190 HOH HOH A . 
K 6 HOH 83  583 56  HOH HOH A . 
K 6 HOH 84  584 91  HOH HOH A . 
K 6 HOH 85  585 6   HOH HOH A . 
K 6 HOH 86  586 231 HOH HOH A . 
K 6 HOH 87  587 107 HOH HOH A . 
K 6 HOH 88  588 192 HOH HOH A . 
K 6 HOH 89  589 166 HOH HOH A . 
K 6 HOH 90  590 120 HOH HOH A . 
K 6 HOH 91  591 302 HOH HOH A . 
K 6 HOH 92  592 150 HOH HOH A . 
K 6 HOH 93  593 222 HOH HOH A . 
K 6 HOH 94  594 28  HOH HOH A . 
K 6 HOH 95  595 27  HOH HOH A . 
K 6 HOH 96  596 199 HOH HOH A . 
K 6 HOH 97  597 151 HOH HOH A . 
K 6 HOH 98  598 102 HOH HOH A . 
K 6 HOH 99  599 248 HOH HOH A . 
K 6 HOH 100 600 74  HOH HOH A . 
K 6 HOH 101 601 49  HOH HOH A . 
K 6 HOH 102 602 313 HOH HOH A . 
K 6 HOH 103 603 144 HOH HOH A . 
K 6 HOH 104 604 256 HOH HOH A . 
K 6 HOH 105 605 130 HOH HOH A . 
K 6 HOH 106 606 285 HOH HOH A . 
K 6 HOH 107 607 307 HOH HOH A . 
K 6 HOH 108 608 258 HOH HOH A . 
K 6 HOH 109 609 252 HOH HOH A . 
K 6 HOH 110 610 179 HOH HOH A . 
K 6 HOH 111 611 243 HOH HOH A . 
K 6 HOH 112 612 254 HOH HOH A . 
K 6 HOH 113 613 250 HOH HOH A . 
K 6 HOH 114 614 25  HOH HOH A . 
K 6 HOH 115 615 178 HOH HOH A . 
K 6 HOH 116 616 308 HOH HOH A . 
K 6 HOH 117 617 260 HOH HOH A . 
K 6 HOH 118 618 261 HOH HOH A . 
K 6 HOH 119 619 223 HOH HOH A . 
K 6 HOH 120 620 300 HOH HOH A . 
K 6 HOH 121 621 205 HOH HOH A . 
K 6 HOH 122 622 197 HOH HOH A . 
K 6 HOH 123 623 24  HOH HOH A . 
K 6 HOH 124 624 176 HOH HOH A . 
K 6 HOH 125 625 75  HOH HOH A . 
K 6 HOH 126 626 181 HOH HOH A . 
K 6 HOH 127 627 237 HOH HOH A . 
K 6 HOH 128 628 133 HOH HOH A . 
K 6 HOH 129 629 311 HOH HOH A . 
K 6 HOH 130 630 207 HOH HOH A . 
K 6 HOH 131 631 287 HOH HOH A . 
K 6 HOH 132 632 294 HOH HOH A . 
K 6 HOH 133 633 46  HOH HOH A . 
K 6 HOH 134 634 310 HOH HOH A . 
K 6 HOH 135 635 239 HOH HOH A . 
K 6 HOH 136 636 233 HOH HOH A . 
K 6 HOH 137 637 288 HOH HOH A . 
K 6 HOH 138 638 125 HOH HOH A . 
K 6 HOH 139 639 187 HOH HOH A . 
K 6 HOH 140 640 309 HOH HOH A . 
K 6 HOH 141 641 292 HOH HOH A . 
K 6 HOH 142 642 225 HOH HOH A . 
K 6 HOH 143 643 234 HOH HOH A . 
K 6 HOH 144 644 226 HOH HOH A . 
K 6 HOH 145 645 314 HOH HOH A . 
L 6 HOH 1   501 95  HOH HOH B . 
L 6 HOH 2   502 171 HOH HOH B . 
L 6 HOH 3   503 87  HOH HOH B . 
L 6 HOH 4   504 19  HOH HOH B . 
L 6 HOH 5   505 138 HOH HOH B . 
L 6 HOH 6   506 94  HOH HOH B . 
L 6 HOH 7   507 131 HOH HOH B . 
L 6 HOH 8   508 228 HOH HOH B . 
L 6 HOH 9   509 167 HOH HOH B . 
L 6 HOH 10  510 145 HOH HOH B . 
L 6 HOH 11  511 259 HOH HOH B . 
L 6 HOH 12  512 9   HOH HOH B . 
L 6 HOH 13  513 12  HOH HOH B . 
L 6 HOH 14  514 57  HOH HOH B . 
L 6 HOH 15  515 96  HOH HOH B . 
L 6 HOH 16  516 59  HOH HOH B . 
L 6 HOH 17  517 221 HOH HOH B . 
L 6 HOH 18  518 8   HOH HOH B . 
L 6 HOH 19  519 305 HOH HOH B . 
L 6 HOH 20  520 23  HOH HOH B . 
L 6 HOH 21  521 38  HOH HOH B . 
L 6 HOH 22  522 93  HOH HOH B . 
L 6 HOH 23  523 230 HOH HOH B . 
L 6 HOH 24  524 129 HOH HOH B . 
L 6 HOH 25  525 4   HOH HOH B . 
L 6 HOH 26  526 55  HOH HOH B . 
L 6 HOH 27  527 148 HOH HOH B . 
L 6 HOH 28  528 203 HOH HOH B . 
L 6 HOH 29  529 170 HOH HOH B . 
L 6 HOH 30  530 112 HOH HOH B . 
L 6 HOH 31  531 153 HOH HOH B . 
L 6 HOH 32  532 168 HOH HOH B . 
L 6 HOH 33  533 3   HOH HOH B . 
L 6 HOH 34  534 165 HOH HOH B . 
L 6 HOH 35  535 103 HOH HOH B . 
L 6 HOH 36  536 164 HOH HOH B . 
L 6 HOH 37  537 247 HOH HOH B . 
L 6 HOH 38  538 122 HOH HOH B . 
L 6 HOH 39  539 17  HOH HOH B . 
L 6 HOH 40  540 240 HOH HOH B . 
L 6 HOH 41  541 16  HOH HOH B . 
L 6 HOH 42  542 105 HOH HOH B . 
L 6 HOH 43  543 100 HOH HOH B . 
L 6 HOH 44  544 215 HOH HOH B . 
L 6 HOH 45  545 218 HOH HOH B . 
L 6 HOH 46  546 286 HOH HOH B . 
L 6 HOH 47  547 71  HOH HOH B . 
L 6 HOH 48  548 33  HOH HOH B . 
L 6 HOH 49  549 116 HOH HOH B . 
L 6 HOH 50  550 22  HOH HOH B . 
L 6 HOH 51  551 98  HOH HOH B . 
L 6 HOH 52  552 89  HOH HOH B . 
L 6 HOH 53  553 147 HOH HOH B . 
L 6 HOH 54  554 40  HOH HOH B . 
L 6 HOH 55  555 92  HOH HOH B . 
L 6 HOH 56  556 123 HOH HOH B . 
L 6 HOH 57  557 21  HOH HOH B . 
L 6 HOH 58  558 65  HOH HOH B . 
L 6 HOH 59  559 127 HOH HOH B . 
L 6 HOH 60  560 183 HOH HOH B . 
L 6 HOH 61  561 13  HOH HOH B . 
L 6 HOH 62  562 161 HOH HOH B . 
L 6 HOH 63  563 212 HOH HOH B . 
L 6 HOH 64  564 141 HOH HOH B . 
L 6 HOH 65  565 68  HOH HOH B . 
L 6 HOH 66  566 62  HOH HOH B . 
L 6 HOH 67  567 169 HOH HOH B . 
L 6 HOH 68  568 236 HOH HOH B . 
L 6 HOH 69  569 173 HOH HOH B . 
L 6 HOH 70  570 35  HOH HOH B . 
L 6 HOH 71  571 128 HOH HOH B . 
L 6 HOH 72  572 5   HOH HOH B . 
L 6 HOH 73  573 189 HOH HOH B . 
L 6 HOH 74  574 101 HOH HOH B . 
L 6 HOH 75  575 281 HOH HOH B . 
L 6 HOH 76  576 108 HOH HOH B . 
L 6 HOH 77  577 157 HOH HOH B . 
L 6 HOH 78  578 217 HOH HOH B . 
L 6 HOH 79  579 32  HOH HOH B . 
L 6 HOH 80  580 66  HOH HOH B . 
L 6 HOH 81  581 272 HOH HOH B . 
L 6 HOH 82  582 99  HOH HOH B . 
L 6 HOH 83  583 160 HOH HOH B . 
L 6 HOH 84  584 54  HOH HOH B . 
L 6 HOH 85  585 61  HOH HOH B . 
L 6 HOH 86  586 220 HOH HOH B . 
L 6 HOH 87  587 111 HOH HOH B . 
L 6 HOH 88  588 244 HOH HOH B . 
L 6 HOH 89  589 143 HOH HOH B . 
L 6 HOH 90  590 282 HOH HOH B . 
L 6 HOH 91  591 245 HOH HOH B . 
L 6 HOH 92  592 255 HOH HOH B . 
L 6 HOH 93  593 119 HOH HOH B . 
L 6 HOH 94  594 263 HOH HOH B . 
L 6 HOH 95  595 81  HOH HOH B . 
L 6 HOH 96  596 146 HOH HOH B . 
L 6 HOH 97  597 317 HOH HOH B . 
L 6 HOH 98  598 202 HOH HOH B . 
L 6 HOH 99  599 241 HOH HOH B . 
L 6 HOH 100 600 293 HOH HOH B . 
L 6 HOH 101 601 280 HOH HOH B . 
L 6 HOH 102 602 1   HOH HOH B . 
L 6 HOH 103 603 42  HOH HOH B . 
L 6 HOH 104 604 200 HOH HOH B . 
L 6 HOH 105 605 265 HOH HOH B . 
L 6 HOH 106 606 303 HOH HOH B . 
L 6 HOH 107 607 279 HOH HOH B . 
L 6 HOH 108 608 79  HOH HOH B . 
L 6 HOH 109 609 296 HOH HOH B . 
L 6 HOH 110 610 295 HOH HOH B . 
L 6 HOH 111 611 304 HOH HOH B . 
L 6 HOH 112 612 271 HOH HOH B . 
L 6 HOH 113 613 266 HOH HOH B . 
L 6 HOH 114 614 195 HOH HOH B . 
L 6 HOH 115 615 41  HOH HOH B . 
L 6 HOH 116 616 180 HOH HOH B . 
L 6 HOH 117 617 264 HOH HOH B . 
L 6 HOH 118 618 277 HOH HOH B . 
L 6 HOH 119 619 251 HOH HOH B . 
L 6 HOH 120 620 177 HOH HOH B . 
L 6 HOH 121 621 58  HOH HOH B . 
L 6 HOH 122 622 214 HOH HOH B . 
L 6 HOH 123 623 232 HOH HOH B . 
L 6 HOH 124 624 270 HOH HOH B . 
L 6 HOH 125 625 312 HOH HOH B . 
L 6 HOH 126 626 29  HOH HOH B . 
L 6 HOH 127 627 276 HOH HOH B . 
L 6 HOH 128 628 45  HOH HOH B . 
L 6 HOH 129 629 268 HOH HOH B . 
L 6 HOH 130 630 278 HOH HOH B . 
L 6 HOH 131 631 204 HOH HOH B . 
L 6 HOH 132 632 273 HOH HOH B . 
L 6 HOH 133 633 291 HOH HOH B . 
L 6 HOH 134 634 289 HOH HOH B . 
L 6 HOH 135 635 290 HOH HOH B . 
L 6 HOH 136 636 211 HOH HOH B . 
L 6 HOH 137 637 235 HOH HOH B . 
L 6 HOH 138 638 186 HOH HOH B . 
L 6 HOH 139 639 253 HOH HOH B . 
L 6 HOH 140 640 315 HOH HOH B . 
L 6 HOH 141 641 284 HOH HOH B . 
L 6 HOH 142 642 267 HOH HOH B . 
L 6 HOH 143 643 227 HOH HOH B . 
L 6 HOH 144 644 262 HOH HOH B . 
L 6 HOH 145 645 283 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.19.2_4158 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DENZO     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.51 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DFL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     142.246 
_cell.length_a_esd                 ? 
_cell.length_b                     122.605 
_cell.length_b_esd                 ? 
_cell.length_c                     66.821 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DFL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DFL 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.77 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Bis-Tris (pH 5.5) and 3.0 M sodium chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            285 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-08-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97857 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97857 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DFL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.50 
_reflns.d_resolution_low                               50.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     38534 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          2.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.648 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.260 
_reflns.pdbx_Rpim_I_all                                0.101 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       249662 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.971 
_reflns.pdbx_CC_star                                   0.993 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.239 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.50 2.54  ? ? ? ? ? ? 1902 ? ? ? ? ? ? ? ? ? ? ? 5.2 0.424 ? ? 1.086 0.465 ? 1  1 0.598 0.865 ? 98.2 ? 0.976 ? ? ? ? ? ? ? ? ? 
2.54 2.59  ? ? ? ? ? ? 1934 ? ? ? ? ? ? ? ? ? ? ? 5.6 0.434 ? ? 1.026 0.422 ? 2  1 0.745 0.924 ? 98.5 ? 0.932 ? ? ? ? ? ? ? ? ? 
2.59 2.64  ? ? ? ? ? ? 1873 ? ? ? ? ? ? ? ? ? ? ? 6.2 0.447 ? ? 0.996 0.392 ? 3  1 0.777 0.935 ? 98.6 ? 0.914 ? ? ? ? ? ? ? ? ? 
2.64 2.69  ? ? ? ? ? ? 1925 ? ? ? ? ? ? ? ? ? ? ? 6.8 0.451 ? ? 0.951 0.360 ? 4  1 0.821 0.949 ? 99.2 ? 0.879 ? ? ? ? ? ? ? ? ? 
2.69 2.75  ? ? ? ? ? ? 1927 ? ? ? ? ? ? ? ? ? ? ? 6.9 0.470 ? ? 0.845 0.317 ? 5  1 0.832 0.953 ? 99.1 ? 0.783 ? ? ? ? ? ? ? ? ? 
2.75 2.82  ? ? ? ? ? ? 1930 ? ? ? ? ? ? ? ? ? ? ? 7.0 0.474 ? ? 0.750 0.281 ? 6  1 0.893 0.971 ? 99.0 ? 0.695 ? ? ? ? ? ? ? ? ? 
2.82 2.89  ? ? ? ? ? ? 1921 ? ? ? ? ? ? ? ? ? ? ? 7.0 0.493 ? ? 0.635 0.237 ? 7  1 0.923 0.980 ? 99.0 ? 0.588 ? ? ? ? ? ? ? ? ? 
2.89 2.96  ? ? ? ? ? ? 1896 ? ? ? ? ? ? ? ? ? ? ? 7.0 0.504 ? ? 0.541 0.202 ? 8  1 0.935 0.983 ? 99.0 ? 0.501 ? ? ? ? ? ? ? ? ? 
2.96 3.05  ? ? ? ? ? ? 1922 ? ? ? ? ? ? ? ? ? ? ? 7.0 0.563 ? ? 0.503 0.189 ? 9  1 0.927 0.981 ? 99.0 ? 0.466 ? ? ? ? ? ? ? ? ? 
3.05 3.15  ? ? ? ? ? ? 1935 ? ? ? ? ? ? ? ? ? ? ? 7.0 0.562 ? ? 0.414 0.155 ? 10 1 0.959 0.989 ? 99.3 ? 0.383 ? ? ? ? ? ? ? ? ? 
3.15 3.26  ? ? ? ? ? ? 1935 ? ? ? ? ? ? ? ? ? ? ? 6.9 0.599 ? ? 0.359 0.135 ? 11 1 0.962 0.990 ? 99.5 ? 0.332 ? ? ? ? ? ? ? ? ? 
3.26 3.39  ? ? ? ? ? ? 1901 ? ? ? ? ? ? ? ? ? ? ? 6.8 0.666 ? ? 0.273 0.103 ? 12 1 0.973 0.993 ? 99.1 ? 0.252 ? ? ? ? ? ? ? ? ? 
3.39 3.55  ? ? ? ? ? ? 1954 ? ? ? ? ? ? ? ? ? ? ? 6.7 0.752 ? ? 0.231 0.088 ? 13 1 0.968 0.992 ? 99.6 ? 0.213 ? ? ? ? ? ? ? ? ? 
3.55 3.73  ? ? ? ? ? ? 1950 ? ? ? ? ? ? ? ? ? ? ? 6.6 0.799 ? ? 0.193 0.075 ? 14 1 0.983 0.996 ? 99.2 ? 0.178 ? ? ? ? ? ? ? ? ? 
3.73 3.97  ? ? ? ? ? ? 1901 ? ? ? ? ? ? ? ? ? ? ? 6.2 0.879 ? ? 0.164 0.065 ? 15 1 0.987 0.997 ? 99.1 ? 0.150 ? ? ? ? ? ? ? ? ? 
3.97 4.27  ? ? ? ? ? ? 1938 ? ? ? ? ? ? ? ? ? ? ? 5.7 0.982 ? ? 0.133 0.055 ? 16 1 0.986 0.996 ? 99.4 ? 0.121 ? ? ? ? ? ? ? ? ? 
4.27 4.70  ? ? ? ? ? ? 1937 ? ? ? ? ? ? ? ? ? ? ? 5.1 0.905 ? ? 0.114 0.050 ? 17 1 0.988 0.997 ? 99.0 ? 0.101 ? ? ? ? ? ? ? ? ? 
4.70 5.38  ? ? ? ? ? ? 1900 ? ? ? ? ? ? ? ? ? ? ? 6.0 0.795 ? ? 0.109 0.044 ? 18 1 0.990 0.997 ? 98.0 ? 0.099 ? ? ? ? ? ? ? ? ? 
5.38 6.78  ? ? ? ? ? ? 1962 ? ? ? ? ? ? ? ? ? ? ? 7.2 0.781 ? ? 0.116 0.043 ? 19 1 0.993 0.998 ? 99.8 ? 0.108 ? ? ? ? ? ? ? ? ? 
6.78 50.00 ? ? ? ? ? ? 1991 ? ? ? ? ? ? ? ? ? ? ? 6.6 1.044 ? ? 0.078 0.030 ? 20 1 0.996 0.999 ? 99.4 ? 0.072 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DFL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.51 
_refine.ls_d_res_low                             46.75 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     38443 
_refine.ls_number_reflns_R_free                  1996 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.27 
_refine.ls_percent_reflns_R_free                 5.19 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2037 
_refine.ls_R_factor_R_free                       0.2578 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2008 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               NONE 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.42 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.37 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5503 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         140 
_refine_hist.number_atoms_solvent             290 
_refine_hist.number_atoms_total               5933 
_refine_hist.d_res_high                       2.51 
_refine_hist.d_res_low                        46.75 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 5799 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.010  ? 7897 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.011 ? 787  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 872  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 1012 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.51 2.57  . . 136 2417 91.00 . . . . 0.2663 . . . . . . . . . . . 0.3417 
'X-RAY DIFFRACTION' 2.57 2.64  . . 136 2584 99.00 . . . . 0.2484 . . . . . . . . . . . 0.3131 
'X-RAY DIFFRACTION' 2.64 2.72  . . 139 2595 99.00 . . . . 0.2335 . . . . . . . . . . . 0.2693 
'X-RAY DIFFRACTION' 2.72 2.81  . . 158 2604 99.00 . . . . 0.2273 . . . . . . . . . . . 0.2979 
'X-RAY DIFFRACTION' 2.81 2.91  . . 134 2635 99.00 . . . . 0.2274 . . . . . . . . . . . 0.3165 
'X-RAY DIFFRACTION' 2.91 3.02  . . 143 2624 99.00 . . . . 0.2145 . . . . . . . . . . . 0.3305 
'X-RAY DIFFRACTION' 3.02 3.16  . . 133 2600 99.00 . . . . 0.2084 . . . . . . . . . . . 0.2654 
'X-RAY DIFFRACTION' 3.16 3.33  . . 151 2637 99.00 . . . . 0.2151 . . . . . . . . . . . 0.2497 
'X-RAY DIFFRACTION' 3.33 3.54  . . 144 2604 99.00 . . . . 0.1999 . . . . . . . . . . . 0.3169 
'X-RAY DIFFRACTION' 3.54 3.81  . . 146 2635 99.00 . . . . 0.1864 . . . . . . . . . . . 0.2630 
'X-RAY DIFFRACTION' 3.81 4.19  . . 140 2643 99.00 . . . . 0.1649 . . . . . . . . . . . 0.2241 
'X-RAY DIFFRACTION' 4.19 4.80  . . 144 2617 99.00 . . . . 0.1502 . . . . . . . . . . . 0.1872 
'X-RAY DIFFRACTION' 4.80 6.04  . . 150 2613 98.00 . . . . 0.1970 . . . . . . . . . . . 0.2375 
'X-RAY DIFFRACTION' 6.04 46.75 . . 142 2639 97.00 . . . . 0.2211 . . . . . . . . . . . 0.2219 
# 
_struct.entry_id                     9DFL 
_struct.title                        'Crystal structure of PrnB in complex with 3-indolepropionic acid' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9DFL 
_struct_keywords.text            
'Pyrrolnitrin biosynthesis, Histidine-ligated heme enzyme, binary complex, 3-indolepropionic acid bound, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 5 ? 
K N N 6 ? 
L N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9DFL 
_struct_ref.pdbx_db_accession          9DFL 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9DFL A 1 ? 370 ? 9DFL -19 ? 350 ? -19 350 
2 1 9DFL B 1 ? 370 ? 9DFL -19 ? 350 ? -19 350 
# 
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 ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,K 
2 1 B,H,I,J,L     
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 23  ? LYS A 28  ? SER A 3   LYS A 8   1 ? 6  
HELX_P HELX_P2  AA2 LEU A 34  ? ASN A 47  ? LEU A 14  ASN A 27  1 ? 14 
HELX_P HELX_P3  AA3 GLU A 49  ? TYR A 64  ? GLU A 29  TYR A 44  1 ? 16 
HELX_P HELX_P4  AA4 LEU A 65  ? PHE A 69  ? LEU A 45  PHE A 49  5 ? 5  
HELX_P HELX_P5  AA5 SER A 70  ? LEU A 91  ? SER A 50  LEU A 71  1 ? 22 
HELX_P HELX_P6  AA6 GLN A 94  ? VAL A 99  ? GLN A 74  VAL A 79  1 ? 6  
HELX_P HELX_P7  AA7 ASP A 101 ? ASN A 114 ? ASP A 81  ASN A 94  1 ? 14 
HELX_P HELX_P8  AA8 THR A 120 ? GLY A 125 ? THR A 100 GLY A 105 1 ? 6  
HELX_P HELX_P9  AA9 ILE A 130 ? GLU A 134 ? ILE A 110 GLU A 114 5 ? 5  
HELX_P HELX_P10 AB1 PHE A 140 ? ASP A 142 ? PHE A 120 ASP A 122 5 ? 3  
HELX_P HELX_P11 AB2 GLU A 143 ? LEU A 167 ? GLU A 123 LEU A 147 1 ? 25 
HELX_P HELX_P12 AB3 SER A 168 ? LEU A 170 ? SER A 148 LEU A 150 5 ? 3  
HELX_P HELX_P13 AB4 ASP A 174 ? THR A 202 ? ASP A 154 THR A 182 1 ? 29 
HELX_P HELX_P14 AB5 ASP A 203 ? LEU A 211 ? ASP A 183 LEU A 191 1 ? 9  
HELX_P HELX_P15 AB6 ARG A 212 ? PHE A 215 ? ARG A 192 PHE A 195 5 ? 4  
HELX_P HELX_P16 AB7 GLY A 229 ? ILE A 233 ? GLY A 209 ILE A 213 5 ? 5  
HELX_P HELX_P17 AB8 PRO A 234 ? TRP A 243 ? PRO A 214 TRP A 223 1 ? 10 
HELX_P HELX_P18 AB9 SER A 251 ? VAL A 261 ? SER A 231 VAL A 241 1 ? 11 
HELX_P HELX_P19 AC1 PHE A 262 ? LEU A 264 ? PHE A 242 LEU A 244 5 ? 3  
HELX_P HELX_P20 AC2 PRO A 265 ? GLU A 267 ? PRO A 245 GLU A 247 5 ? 3  
HELX_P HELX_P21 AC3 LEU A 268 ? LEU A 277 ? LEU A 248 LEU A 257 1 ? 10 
HELX_P HELX_P22 AC4 SER A 280 ? GLY A 290 ? SER A 260 GLY A 270 1 ? 11 
HELX_P HELX_P23 AC5 THR A 295 ? LEU A 327 ? THR A 275 LEU A 307 1 ? 33 
HELX_P HELX_P24 AC6 THR A 343 ? LEU A 365 ? THR A 323 LEU A 345 1 ? 23 
HELX_P HELX_P25 AC7 MET B 21  ? LYS B 28  ? MET B 1   LYS B 8   1 ? 8  
HELX_P HELX_P26 AC8 LEU B 34  ? ASN B 47  ? LEU B 14  ASN B 27  1 ? 14 
HELX_P HELX_P27 AC9 GLU B 49  ? TYR B 64  ? GLU B 29  TYR B 44  1 ? 16 
HELX_P HELX_P28 AD1 LEU B 65  ? PHE B 69  ? LEU B 45  PHE B 49  5 ? 5  
HELX_P HELX_P29 AD2 SER B 70  ? LEU B 91  ? SER B 50  LEU B 71  1 ? 22 
HELX_P HELX_P30 AD3 GLN B 94  ? VAL B 99  ? GLN B 74  VAL B 79  1 ? 6  
HELX_P HELX_P31 AD4 ASP B 101 ? ASN B 114 ? ASP B 81  ASN B 94  1 ? 14 
HELX_P HELX_P32 AD5 THR B 120 ? GLY B 125 ? THR B 100 GLY B 105 1 ? 6  
HELX_P HELX_P33 AD6 ILE B 130 ? GLU B 134 ? ILE B 110 GLU B 114 5 ? 5  
HELX_P HELX_P34 AD7 PHE B 140 ? ASP B 142 ? PHE B 120 ASP B 122 5 ? 3  
HELX_P HELX_P35 AD8 GLU B 143 ? GLN B 166 ? GLU B 123 GLN B 146 1 ? 24 
HELX_P HELX_P36 AD9 LEU B 167 ? LEU B 170 ? LEU B 147 LEU B 150 5 ? 4  
HELX_P HELX_P37 AE1 ASP B 174 ? THR B 202 ? ASP B 154 THR B 182 1 ? 29 
HELX_P HELX_P38 AE2 ASP B 203 ? LEU B 211 ? ASP B 183 LEU B 191 1 ? 9  
HELX_P HELX_P39 AE3 ARG B 212 ? PHE B 215 ? ARG B 192 PHE B 195 5 ? 4  
HELX_P HELX_P40 AE4 GLY B 229 ? ILE B 233 ? GLY B 209 ILE B 213 5 ? 5  
HELX_P HELX_P41 AE5 PRO B 234 ? TRP B 243 ? PRO B 214 TRP B 223 1 ? 10 
HELX_P HELX_P42 AE6 SER B 251 ? VAL B 261 ? SER B 231 VAL B 241 1 ? 11 
HELX_P HELX_P43 AE7 PRO B 265 ? GLU B 267 ? PRO B 245 GLU B 247 5 ? 3  
HELX_P HELX_P44 AE8 LEU B 268 ? LEU B 277 ? LEU B 248 LEU B 257 1 ? 10 
HELX_P HELX_P45 AE9 SER B 280 ? GLY B 290 ? SER B 260 GLY B 270 1 ? 11 
HELX_P HELX_P46 AF1 THR B 295 ? LEU B 327 ? THR B 275 LEU B 307 1 ? 33 
HELX_P HELX_P47 AF2 THR B 343 ? ALA B 366 ? THR B 323 ALA B 346 1 ? 24 
# 
_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 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 319 NE2 ? ? ? 1_555 C HEM . FE ? ? A HIS 299 A HEM 401 1_555 ? ? ? ? ? ? ? 2.190 ? ? 
metalc2 metalc ? ? B HIS 319 NE2 ? ? ? 1_555 H HEM . FE ? ? B HIS 299 B HEM 401 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 319 ? A HIS 299 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NA ? C HEM . ? A HEM 401 ? 1_555 95.7  ? 
2  NE2 ? A HIS 319 ? A HIS 299 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NB ? C HEM . ? A HEM 401 ? 1_555 103.5 ? 
3  NA  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NB ? C HEM . ? A HEM 401 ? 1_555 94.6  ? 
4  NE2 ? A HIS 319 ? A HIS 299 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC ? C HEM . ? A HEM 401 ? 1_555 90.9  ? 
5  NA  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC ? C HEM . ? A HEM 401 ? 1_555 172.3 ? 
6  NB  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC ? C HEM . ? A HEM 401 ? 1_555 87.6  ? 
7  NE2 ? A HIS 319 ? A HIS 299 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 89.6  ? 
8  NA  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 84.4  ? 
9  NB  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 167.0 ? 
10 NC  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 91.8  ? 
11 NE2 ? B HIS 319 ? B HIS 299 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NA ? H HEM . ? B HEM 401 ? 1_555 98.2  ? 
12 NE2 ? B HIS 319 ? B HIS 299 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NB ? H HEM . ? B HEM 401 ? 1_555 106.6 ? 
13 NA  ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NB ? H HEM . ? B HEM 401 ? 1_555 92.1  ? 
14 NE2 ? B HIS 319 ? B HIS 299 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NC ? H HEM . ? B HEM 401 ? 1_555 90.6  ? 
15 NA  ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NC ? H HEM . ? B HEM 401 ? 1_555 170.9 ? 
16 NB  ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 NC ? H HEM . ? B HEM 401 ? 1_555 87.6  ? 
17 NE2 ? B HIS 319 ? B HIS 299 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 ND ? H HEM . ? B HEM 401 ? 1_555 87.2  ? 
18 NA  ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 ND ? H HEM . ? B HEM 401 ? 1_555 86.5  ? 
19 NB  ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 ND ? H HEM . ? B HEM 401 ? 1_555 166.2 ? 
20 NC  ? H HEM .   ? B HEM 401 ? 1_555 FE ? H HEM . ? B HEM 401 ? 1_555 ND ? H HEM . ? B HEM 401 ? 1_555 91.7  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 218 ? ILE A 220 ? ILE A 198 ILE A 200 
AA1 2 LYS A 223 ? TYR A 225 ? LYS A 203 TYR A 205 
AA2 1 ILE B 218 ? ILE B 220 ? ILE B 198 ILE B 200 
AA2 2 LYS B 223 ? TYR B 225 ? LYS B 203 TYR B 205 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 220 ? N ILE A 200 O LYS A 223 ? O LYS A 203 
AA2 1 2 N ILE B 220 ? N ILE B 200 O LYS B 223 ? O LYS B 203 
# 
_pdbx_entry_details.entry_id                   9DFL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            B 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             247 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_2            B 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             247 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.645 
_pdbx_validate_rmsd_bond.bond_target_value         1.517 
_pdbx_validate_rmsd_bond.bond_deviation            0.128 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               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 ASN A 149 ? ? -104.52 46.17 
2 1 PRO A 214 ? ? -72.30  24.86 
3 1 SER A 271 ? ? -162.70 6.01  
4 1 ILE A 274 ? ? -66.41  96.81 
5 1 PRO B 97  ? ? -86.71  49.24 
6 1 PRO B 214 ? ? -79.35  35.32 
7 1 SER B 271 ? ? -142.75 -8.04 
8 1 PRO B 347 ? ? -70.50  22.10 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 644 ? 6.41 . 
2 1 O ? B HOH 645 ? 7.57 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A GLU -6  ? A GLU 14  
15 1 Y 1 A ASN -5  ? A ASN 15  
16 1 Y 1 A LEU -4  ? A LEU 16  
17 1 Y 1 A TYR -3  ? A TYR 17  
18 1 Y 1 A PHE -2  ? A PHE 18  
19 1 Y 1 A GLN -1  ? A GLN 19  
20 1 Y 1 A GLY 0   ? A GLY 20  
21 1 Y 1 A MET 1   ? A MET 21  
22 1 Y 1 A TYR 348 ? A TYR 368 
23 1 Y 1 A ARG 349 ? A ARG 369 
24 1 Y 1 A SER 350 ? A SER 370 
25 1 Y 1 B MET -19 ? B MET 1   
26 1 Y 1 B GLY -18 ? B GLY 2   
27 1 Y 1 B SER -17 ? B SER 3   
28 1 Y 1 B SER -16 ? B SER 4   
29 1 Y 1 B HIS -15 ? B HIS 5   
30 1 Y 1 B HIS -14 ? B HIS 6   
31 1 Y 1 B HIS -13 ? B HIS 7   
32 1 Y 1 B HIS -12 ? B HIS 8   
33 1 Y 1 B HIS -11 ? B HIS 9   
34 1 Y 1 B HIS -10 ? B HIS 10  
35 1 Y 1 B SER -9  ? B SER 11  
36 1 Y 1 B SER -8  ? B SER 12  
37 1 Y 1 B GLY -7  ? B GLY 13  
38 1 Y 1 B GLU -6  ? B GLU 14  
39 1 Y 1 B ASN -5  ? B ASN 15  
40 1 Y 1 B LEU -4  ? B LEU 16  
41 1 Y 1 B TYR -3  ? B TYR 17  
42 1 Y 1 B PHE -2  ? B PHE 18  
43 1 Y 1 B ARG 349 ? B ARG 369 
44 1 Y 1 B SER 350 ? B SER 370 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
GOL C1     C  N N 137 
GOL O1     O  N N 138 
GOL C2     C  N N 139 
GOL O2     O  N N 140 
GOL C3     C  N N 141 
GOL O3     O  N N 142 
GOL H11    H  N N 143 
GOL H12    H  N N 144 
GOL HO1    H  N N 145 
GOL H2     H  N N 146 
GOL HO2    H  N N 147 
GOL H31    H  N N 148 
GOL H32    H  N N 149 
GOL HO3    H  N N 150 
HEM CHA    C  N N 151 
HEM CHB    C  N N 152 
HEM CHC    C  N N 153 
HEM CHD    C  N N 154 
HEM C1A    C  Y N 155 
HEM C2A    C  Y N 156 
HEM C3A    C  Y N 157 
HEM C4A    C  Y N 158 
HEM CMA    C  N N 159 
HEM CAA    C  N N 160 
HEM CBA    C  N N 161 
HEM CGA    C  N N 162 
HEM O1A    O  N N 163 
HEM O2A    O  N N 164 
HEM C1B    C  N N 165 
HEM C2B    C  N N 166 
HEM C3B    C  N N 167 
HEM C4B    C  N N 168 
HEM CMB    C  N N 169 
HEM CAB    C  N N 170 
HEM CBB    C  N N 171 
HEM C1C    C  Y N 172 
HEM C2C    C  Y N 173 
HEM C3C    C  Y N 174 
HEM C4C    C  Y N 175 
HEM CMC    C  N N 176 
HEM CAC    C  N N 177 
HEM CBC    C  N N 178 
HEM C1D    C  N N 179 
HEM C2D    C  N N 180 
HEM C3D    C  N N 181 
HEM C4D    C  N N 182 
HEM CMD    C  N N 183 
HEM CAD    C  N N 184 
HEM CBD    C  N N 185 
HEM CGD    C  N N 186 
HEM O1D    O  N N 187 
HEM O2D    O  N N 188 
HEM NA     N  Y N 189 
HEM NB     N  N N 190 
HEM NC     N  Y N 191 
HEM ND     N  N N 192 
HEM FE     FE N N 193 
HEM HHB    H  N N 194 
HEM HHC    H  N N 195 
HEM HHD    H  N N 196 
HEM HMA    H  N N 197 
HEM HMAA   H  N N 198 
HEM HMAB   H  N N 199 
HEM HAA    H  N N 200 
HEM HAAA   H  N N 201 
HEM HBA    H  N N 202 
HEM HBAA   H  N N 203 
HEM HMB    H  N N 204 
HEM HMBA   H  N N 205 
HEM HMBB   H  N N 206 
HEM HAB    H  N N 207 
HEM HBB    H  N N 208 
HEM HBBA   H  N N 209 
HEM HMC    H  N N 210 
HEM HMCA   H  N N 211 
HEM HMCB   H  N N 212 
HEM HAC    H  N N 213 
HEM HBC    H  N N 214 
HEM HBCA   H  N N 215 
HEM HMD    H  N N 216 
HEM HMDA   H  N N 217 
HEM HMDB   H  N N 218 
HEM HAD    H  N N 219 
HEM HADA   H  N N 220 
HEM HBD    H  N N 221 
HEM HBDA   H  N N 222 
HEM H2A    H  N N 223 
HEM H2D    H  N N 224 
HEM HHA    H  N N 225 
HIS N      N  N N 226 
HIS CA     C  N S 227 
HIS C      C  N N 228 
HIS O      O  N N 229 
HIS CB     C  N N 230 
HIS CG     C  Y N 231 
HIS ND1    N  Y N 232 
HIS CD2    C  Y N 233 
HIS CE1    C  Y N 234 
HIS NE2    N  Y N 235 
HIS OXT    O  N N 236 
HIS H      H  N N 237 
HIS H2     H  N N 238 
HIS HA     H  N N 239 
HIS HB2    H  N N 240 
HIS HB3    H  N N 241 
HIS HD1    H  N N 242 
HIS HD2    H  N N 243 
HIS HE1    H  N N 244 
HIS HE2    H  N N 245 
HIS HXT    H  N N 246 
HOH O      O  N N 247 
HOH H1     H  N N 248 
HOH H2     H  N N 249 
ILE N      N  N N 250 
ILE CA     C  N S 251 
ILE C      C  N N 252 
ILE O      O  N N 253 
ILE CB     C  N S 254 
ILE CG1    C  N N 255 
ILE CG2    C  N N 256 
ILE CD1    C  N N 257 
ILE OXT    O  N N 258 
ILE H      H  N N 259 
ILE H2     H  N N 260 
ILE HA     H  N N 261 
ILE HB     H  N N 262 
ILE HG12   H  N N 263 
ILE HG13   H  N N 264 
ILE HG21   H  N N 265 
ILE HG22   H  N N 266 
ILE HG23   H  N N 267 
ILE HD11   H  N N 268 
ILE HD12   H  N N 269 
ILE HD13   H  N N 270 
ILE HXT    H  N N 271 
IOP "C1'"  C  N N 272 
IOP O1     O  N N 273 
IOP O2     O  N N 274 
IOP "C2'"  C  N N 275 
IOP "C3'"  C  N N 276 
IOP N1     N  Y N 277 
IOP C2     C  Y N 278 
IOP C3     C  Y N 279 
IOP C3A    C  Y N 280 
IOP C4     C  Y N 281 
IOP C5     C  Y N 282 
IOP C6     C  Y N 283 
IOP C7     C  Y N 284 
IOP C7A    C  Y N 285 
IOP HO2    H  N N 286 
IOP "H2'1" H  N N 287 
IOP "H2'2" H  N N 288 
IOP "H3'1" H  N N 289 
IOP "H3'2" H  N N 290 
IOP HN1    H  N N 291 
IOP H2     H  N N 292 
IOP H4     H  N N 293 
IOP H5     H  N N 294 
IOP H6     H  N N 295 
IOP H7     H  N N 296 
LEU N      N  N N 297 
LEU CA     C  N S 298 
LEU C      C  N N 299 
LEU O      O  N N 300 
LEU CB     C  N N 301 
LEU CG     C  N N 302 
LEU CD1    C  N N 303 
LEU CD2    C  N N 304 
LEU OXT    O  N N 305 
LEU H      H  N N 306 
LEU H2     H  N N 307 
LEU HA     H  N N 308 
LEU HB2    H  N N 309 
LEU HB3    H  N N 310 
LEU HG     H  N N 311 
LEU HD11   H  N N 312 
LEU HD12   H  N N 313 
LEU HD13   H  N N 314 
LEU HD21   H  N N 315 
LEU HD22   H  N N 316 
LEU HD23   H  N N 317 
LEU HXT    H  N N 318 
LYS N      N  N N 319 
LYS CA     C  N S 320 
LYS C      C  N N 321 
LYS O      O  N N 322 
LYS CB     C  N N 323 
LYS CG     C  N N 324 
LYS CD     C  N N 325 
LYS CE     C  N N 326 
LYS NZ     N  N N 327 
LYS OXT    O  N N 328 
LYS H      H  N N 329 
LYS H2     H  N N 330 
LYS HA     H  N N 331 
LYS HB2    H  N N 332 
LYS HB3    H  N N 333 
LYS HG2    H  N N 334 
LYS HG3    H  N N 335 
LYS HD2    H  N N 336 
LYS HD3    H  N N 337 
LYS HE2    H  N N 338 
LYS HE3    H  N N 339 
LYS HZ1    H  N N 340 
LYS HZ2    H  N N 341 
LYS HZ3    H  N N 342 
LYS HXT    H  N N 343 
MET N      N  N N 344 
MET CA     C  N S 345 
MET C      C  N N 346 
MET O      O  N N 347 
MET CB     C  N N 348 
MET CG     C  N N 349 
MET SD     S  N N 350 
MET CE     C  N N 351 
MET OXT    O  N N 352 
MET H      H  N N 353 
MET H2     H  N N 354 
MET HA     H  N N 355 
MET HB2    H  N N 356 
MET HB3    H  N N 357 
MET HG2    H  N N 358 
MET HG3    H  N N 359 
MET HE1    H  N N 360 
MET HE2    H  N N 361 
MET HE3    H  N N 362 
MET HXT    H  N N 363 
PHE N      N  N N 364 
PHE CA     C  N S 365 
PHE C      C  N N 366 
PHE O      O  N N 367 
PHE CB     C  N N 368 
PHE CG     C  Y N 369 
PHE CD1    C  Y N 370 
PHE CD2    C  Y N 371 
PHE CE1    C  Y N 372 
PHE CE2    C  Y N 373 
PHE CZ     C  Y N 374 
PHE OXT    O  N N 375 
PHE H      H  N N 376 
PHE H2     H  N N 377 
PHE HA     H  N N 378 
PHE HB2    H  N N 379 
PHE HB3    H  N N 380 
PHE HD1    H  N N 381 
PHE HD2    H  N N 382 
PHE HE1    H  N N 383 
PHE HE2    H  N N 384 
PHE HZ     H  N N 385 
PHE HXT    H  N N 386 
PRO N      N  N N 387 
PRO CA     C  N S 388 
PRO C      C  N N 389 
PRO O      O  N N 390 
PRO CB     C  N N 391 
PRO CG     C  N N 392 
PRO CD     C  N N 393 
PRO OXT    O  N N 394 
PRO H      H  N N 395 
PRO HA     H  N N 396 
PRO HB2    H  N N 397 
PRO HB3    H  N N 398 
PRO HG2    H  N N 399 
PRO HG3    H  N N 400 
PRO HD2    H  N N 401 
PRO HD3    H  N N 402 
PRO HXT    H  N N 403 
SER N      N  N N 404 
SER CA     C  N S 405 
SER C      C  N N 406 
SER O      O  N N 407 
SER CB     C  N N 408 
SER OG     O  N N 409 
SER OXT    O  N N 410 
SER H      H  N N 411 
SER H2     H  N N 412 
SER HA     H  N N 413 
SER HB2    H  N N 414 
SER HB3    H  N N 415 
SER HG     H  N N 416 
SER HXT    H  N N 417 
THR N      N  N N 418 
THR CA     C  N S 419 
THR C      C  N N 420 
THR O      O  N N 421 
THR CB     C  N R 422 
THR OG1    O  N N 423 
THR CG2    C  N N 424 
THR OXT    O  N N 425 
THR H      H  N N 426 
THR H2     H  N N 427 
THR HA     H  N N 428 
THR HB     H  N N 429 
THR HG1    H  N N 430 
THR HG21   H  N N 431 
THR HG22   H  N N 432 
THR HG23   H  N N 433 
THR HXT    H  N N 434 
TRP N      N  N N 435 
TRP CA     C  N S 436 
TRP C      C  N N 437 
TRP O      O  N N 438 
TRP CB     C  N N 439 
TRP CG     C  Y N 440 
TRP CD1    C  Y N 441 
TRP CD2    C  Y N 442 
TRP NE1    N  Y N 443 
TRP CE2    C  Y N 444 
TRP CE3    C  Y N 445 
TRP CZ2    C  Y N 446 
TRP CZ3    C  Y N 447 
TRP CH2    C  Y N 448 
TRP OXT    O  N N 449 
TRP H      H  N N 450 
TRP H2     H  N N 451 
TRP HA     H  N N 452 
TRP HB2    H  N N 453 
TRP HB3    H  N N 454 
TRP HD1    H  N N 455 
TRP HE1    H  N N 456 
TRP HE3    H  N N 457 
TRP HZ2    H  N N 458 
TRP HZ3    H  N N 459 
TRP HH2    H  N N 460 
TRP HXT    H  N N 461 
TRS C      C  N N 462 
TRS C1     C  N N 463 
TRS C2     C  N N 464 
TRS C3     C  N N 465 
TRS N      N  N N 466 
TRS O1     O  N N 467 
TRS O2     O  N N 468 
TRS O3     O  N N 469 
TRS H11    H  N N 470 
TRS H12    H  N N 471 
TRS H21    H  N N 472 
TRS H22    H  N N 473 
TRS H31    H  N N 474 
TRS H32    H  N N 475 
TRS HN1    H  N N 476 
TRS HN2    H  N N 477 
TRS HN3    H  N N 478 
TRS HO1    H  N N 479 
TRS HO2    H  N N 480 
TRS HO3    H  N N 481 
TYR N      N  N N 482 
TYR CA     C  N S 483 
TYR C      C  N N 484 
TYR O      O  N N 485 
TYR CB     C  N N 486 
TYR CG     C  Y N 487 
TYR CD1    C  Y N 488 
TYR CD2    C  Y N 489 
TYR CE1    C  Y N 490 
TYR CE2    C  Y N 491 
TYR CZ     C  Y N 492 
TYR OH     O  N N 493 
TYR OXT    O  N N 494 
TYR H      H  N N 495 
TYR H2     H  N N 496 
TYR HA     H  N N 497 
TYR HB2    H  N N 498 
TYR HB3    H  N N 499 
TYR HD1    H  N N 500 
TYR HD2    H  N N 501 
TYR HE1    H  N N 502 
TYR HE2    H  N N 503 
TYR HH     H  N N 504 
TYR HXT    H  N N 505 
VAL N      N  N N 506 
VAL CA     C  N S 507 
VAL C      C  N N 508 
VAL O      O  N N 509 
VAL CB     C  N N 510 
VAL CG1    C  N N 511 
VAL CG2    C  N N 512 
VAL OXT    O  N N 513 
VAL H      H  N N 514 
VAL H2     H  N N 515 
VAL HA     H  N N 516 
VAL HB     H  N N 517 
VAL HG11   H  N N 518 
VAL HG12   H  N N 519 
VAL HG13   H  N N 520 
VAL HG21   H  N N 521 
VAL HG22   H  N N 522 
VAL HG23   H  N N 523 
VAL HXT    H  N N 524 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
GOL C1    O1     sing N N 129 
GOL C1    C2     sing N N 130 
GOL C1    H11    sing N N 131 
GOL C1    H12    sing N N 132 
GOL O1    HO1    sing N N 133 
GOL C2    O2     sing N N 134 
GOL C2    C3     sing N N 135 
GOL C2    H2     sing N N 136 
GOL O2    HO2    sing N N 137 
GOL C3    O3     sing N N 138 
GOL C3    H31    sing N N 139 
GOL C3    H32    sing N N 140 
GOL O3    HO3    sing N N 141 
HEM CHA   C1A    sing N N 142 
HEM CHA   C4D    doub N N 143 
HEM CHA   HHA    sing N N 144 
HEM CHB   C4A    sing N N 145 
HEM CHB   C1B    doub N N 146 
HEM CHB   HHB    sing N N 147 
HEM CHC   C4B    sing N N 148 
HEM CHC   C1C    doub N N 149 
HEM CHC   HHC    sing N N 150 
HEM CHD   C4C    doub N N 151 
HEM CHD   C1D    sing N N 152 
HEM CHD   HHD    sing N N 153 
HEM C1A   C2A    doub Y N 154 
HEM C1A   NA     sing Y N 155 
HEM C2A   C3A    sing Y N 156 
HEM C2A   CAA    sing N N 157 
HEM C3A   C4A    doub Y N 158 
HEM C3A   CMA    sing N N 159 
HEM C4A   NA     sing Y N 160 
HEM CMA   HMA    sing N N 161 
HEM CMA   HMAA   sing N N 162 
HEM CMA   HMAB   sing N N 163 
HEM CAA   CBA    sing N N 164 
HEM CAA   HAA    sing N N 165 
HEM CAA   HAAA   sing N N 166 
HEM CBA   CGA    sing N N 167 
HEM CBA   HBA    sing N N 168 
HEM CBA   HBAA   sing N N 169 
HEM CGA   O1A    doub N N 170 
HEM CGA   O2A    sing N N 171 
HEM C1B   C2B    sing N N 172 
HEM C1B   NB     sing N N 173 
HEM C2B   C3B    doub N N 174 
HEM C2B   CMB    sing N N 175 
HEM C3B   C4B    sing N N 176 
HEM C3B   CAB    sing N N 177 
HEM C4B   NB     doub N N 178 
HEM CMB   HMB    sing N N 179 
HEM CMB   HMBA   sing N N 180 
HEM CMB   HMBB   sing N N 181 
HEM CAB   CBB    doub N N 182 
HEM CAB   HAB    sing N N 183 
HEM CBB   HBB    sing N N 184 
HEM CBB   HBBA   sing N N 185 
HEM C1C   C2C    sing Y N 186 
HEM C1C   NC     sing Y N 187 
HEM C2C   C3C    doub Y N 188 
HEM C2C   CMC    sing N N 189 
HEM C3C   C4C    sing Y N 190 
HEM C3C   CAC    sing N N 191 
HEM C4C   NC     sing Y N 192 
HEM CMC   HMC    sing N N 193 
HEM CMC   HMCA   sing N N 194 
HEM CMC   HMCB   sing N N 195 
HEM CAC   CBC    doub N N 196 
HEM CAC   HAC    sing N N 197 
HEM CBC   HBC    sing N N 198 
HEM CBC   HBCA   sing N N 199 
HEM C1D   C2D    sing N N 200 
HEM C1D   ND     doub N N 201 
HEM C2D   C3D    doub N N 202 
HEM C2D   CMD    sing N N 203 
HEM C3D   C4D    sing N N 204 
HEM C3D   CAD    sing N N 205 
HEM C4D   ND     sing N N 206 
HEM CMD   HMD    sing N N 207 
HEM CMD   HMDA   sing N N 208 
HEM CMD   HMDB   sing N N 209 
HEM CAD   CBD    sing N N 210 
HEM CAD   HAD    sing N N 211 
HEM CAD   HADA   sing N N 212 
HEM CBD   CGD    sing N N 213 
HEM CBD   HBD    sing N N 214 
HEM CBD   HBDA   sing N N 215 
HEM CGD   O1D    doub N N 216 
HEM CGD   O2D    sing N N 217 
HEM O2A   H2A    sing N N 218 
HEM O2D   H2D    sing N N 219 
HEM FE    NA     sing N N 220 
HEM FE    NB     sing N N 221 
HEM FE    NC     sing N N 222 
HEM FE    ND     sing N N 223 
HIS N     CA     sing N N 224 
HIS N     H      sing N N 225 
HIS N     H2     sing N N 226 
HIS CA    C      sing N N 227 
HIS CA    CB     sing N N 228 
HIS CA    HA     sing N N 229 
HIS C     O      doub N N 230 
HIS C     OXT    sing N N 231 
HIS CB    CG     sing N N 232 
HIS CB    HB2    sing N N 233 
HIS CB    HB3    sing N N 234 
HIS CG    ND1    sing Y N 235 
HIS CG    CD2    doub Y N 236 
HIS ND1   CE1    doub Y N 237 
HIS ND1   HD1    sing N N 238 
HIS CD2   NE2    sing Y N 239 
HIS CD2   HD2    sing N N 240 
HIS CE1   NE2    sing Y N 241 
HIS CE1   HE1    sing N N 242 
HIS NE2   HE2    sing N N 243 
HIS OXT   HXT    sing N N 244 
HOH O     H1     sing N N 245 
HOH O     H2     sing N N 246 
ILE N     CA     sing N N 247 
ILE N     H      sing N N 248 
ILE N     H2     sing N N 249 
ILE CA    C      sing N N 250 
ILE CA    CB     sing N N 251 
ILE CA    HA     sing N N 252 
ILE C     O      doub N N 253 
ILE C     OXT    sing N N 254 
ILE CB    CG1    sing N N 255 
ILE CB    CG2    sing N N 256 
ILE CB    HB     sing N N 257 
ILE CG1   CD1    sing N N 258 
ILE CG1   HG12   sing N N 259 
ILE CG1   HG13   sing N N 260 
ILE CG2   HG21   sing N N 261 
ILE CG2   HG22   sing N N 262 
ILE CG2   HG23   sing N N 263 
ILE CD1   HD11   sing N N 264 
ILE CD1   HD12   sing N N 265 
ILE CD1   HD13   sing N N 266 
ILE OXT   HXT    sing N N 267 
IOP "C1'" O1     doub N N 268 
IOP "C1'" O2     sing N N 269 
IOP "C1'" "C2'"  sing N N 270 
IOP O2    HO2    sing N N 271 
IOP "C2'" "C3'"  sing N N 272 
IOP "C2'" "H2'1" sing N N 273 
IOP "C2'" "H2'2" sing N N 274 
IOP "C3'" C3     sing N N 275 
IOP "C3'" "H3'1" sing N N 276 
IOP "C3'" "H3'2" sing N N 277 
IOP N1    C2     sing Y N 278 
IOP N1    C7A    sing Y N 279 
IOP N1    HN1    sing N N 280 
IOP C2    C3     doub Y N 281 
IOP C2    H2     sing N N 282 
IOP C3    C3A    sing Y N 283 
IOP C3A   C4     doub Y N 284 
IOP C3A   C7A    sing Y N 285 
IOP C4    C5     sing Y N 286 
IOP C4    H4     sing N N 287 
IOP C5    C6     doub Y N 288 
IOP C5    H5     sing N N 289 
IOP C6    C7     sing Y N 290 
IOP C6    H6     sing N N 291 
IOP C7    C7A    doub Y N 292 
IOP C7    H7     sing N N 293 
LEU N     CA     sing N N 294 
LEU N     H      sing N N 295 
LEU N     H2     sing N N 296 
LEU CA    C      sing N N 297 
LEU CA    CB     sing N N 298 
LEU CA    HA     sing N N 299 
LEU C     O      doub N N 300 
LEU C     OXT    sing N N 301 
LEU CB    CG     sing N N 302 
LEU CB    HB2    sing N N 303 
LEU CB    HB3    sing N N 304 
LEU CG    CD1    sing N N 305 
LEU CG    CD2    sing N N 306 
LEU CG    HG     sing N N 307 
LEU CD1   HD11   sing N N 308 
LEU CD1   HD12   sing N N 309 
LEU CD1   HD13   sing N N 310 
LEU CD2   HD21   sing N N 311 
LEU CD2   HD22   sing N N 312 
LEU CD2   HD23   sing N N 313 
LEU OXT   HXT    sing N N 314 
LYS N     CA     sing N N 315 
LYS N     H      sing N N 316 
LYS N     H2     sing N N 317 
LYS CA    C      sing N N 318 
LYS CA    CB     sing N N 319 
LYS CA    HA     sing N N 320 
LYS C     O      doub N N 321 
LYS C     OXT    sing N N 322 
LYS CB    CG     sing N N 323 
LYS CB    HB2    sing N N 324 
LYS CB    HB3    sing N N 325 
LYS CG    CD     sing N N 326 
LYS CG    HG2    sing N N 327 
LYS CG    HG3    sing N N 328 
LYS CD    CE     sing N N 329 
LYS CD    HD2    sing N N 330 
LYS CD    HD3    sing N N 331 
LYS CE    NZ     sing N N 332 
LYS CE    HE2    sing N N 333 
LYS CE    HE3    sing N N 334 
LYS NZ    HZ1    sing N N 335 
LYS NZ    HZ2    sing N N 336 
LYS NZ    HZ3    sing N N 337 
LYS OXT   HXT    sing N N 338 
MET N     CA     sing N N 339 
MET N     H      sing N N 340 
MET N     H2     sing N N 341 
MET CA    C      sing N N 342 
MET CA    CB     sing N N 343 
MET CA    HA     sing N N 344 
MET C     O      doub N N 345 
MET C     OXT    sing N N 346 
MET CB    CG     sing N N 347 
MET CB    HB2    sing N N 348 
MET CB    HB3    sing N N 349 
MET CG    SD     sing N N 350 
MET CG    HG2    sing N N 351 
MET CG    HG3    sing N N 352 
MET SD    CE     sing N N 353 
MET CE    HE1    sing N N 354 
MET CE    HE2    sing N N 355 
MET CE    HE3    sing N N 356 
MET OXT   HXT    sing N N 357 
PHE N     CA     sing N N 358 
PHE N     H      sing N N 359 
PHE N     H2     sing N N 360 
PHE CA    C      sing N N 361 
PHE CA    CB     sing N N 362 
PHE CA    HA     sing N N 363 
PHE C     O      doub N N 364 
PHE C     OXT    sing N N 365 
PHE CB    CG     sing N N 366 
PHE CB    HB2    sing N N 367 
PHE CB    HB3    sing N N 368 
PHE CG    CD1    doub Y N 369 
PHE CG    CD2    sing Y N 370 
PHE CD1   CE1    sing Y N 371 
PHE CD1   HD1    sing N N 372 
PHE CD2   CE2    doub Y N 373 
PHE CD2   HD2    sing N N 374 
PHE CE1   CZ     doub Y N 375 
PHE CE1   HE1    sing N N 376 
PHE CE2   CZ     sing Y N 377 
PHE CE2   HE2    sing N N 378 
PHE CZ    HZ     sing N N 379 
PHE OXT   HXT    sing N N 380 
PRO N     CA     sing N N 381 
PRO N     CD     sing N N 382 
PRO N     H      sing N N 383 
PRO CA    C      sing N N 384 
PRO CA    CB     sing N N 385 
PRO CA    HA     sing N N 386 
PRO C     O      doub N N 387 
PRO C     OXT    sing N N 388 
PRO CB    CG     sing N N 389 
PRO CB    HB2    sing N N 390 
PRO CB    HB3    sing N N 391 
PRO CG    CD     sing N N 392 
PRO CG    HG2    sing N N 393 
PRO CG    HG3    sing N N 394 
PRO CD    HD2    sing N N 395 
PRO CD    HD3    sing N N 396 
PRO OXT   HXT    sing N N 397 
SER N     CA     sing N N 398 
SER N     H      sing N N 399 
SER N     H2     sing N N 400 
SER CA    C      sing N N 401 
SER CA    CB     sing N N 402 
SER CA    HA     sing N N 403 
SER C     O      doub N N 404 
SER C     OXT    sing N N 405 
SER CB    OG     sing N N 406 
SER CB    HB2    sing N N 407 
SER CB    HB3    sing N N 408 
SER OG    HG     sing N N 409 
SER OXT   HXT    sing N N 410 
THR N     CA     sing N N 411 
THR N     H      sing N N 412 
THR N     H2     sing N N 413 
THR CA    C      sing N N 414 
THR CA    CB     sing N N 415 
THR CA    HA     sing N N 416 
THR C     O      doub N N 417 
THR C     OXT    sing N N 418 
THR CB    OG1    sing N N 419 
THR CB    CG2    sing N N 420 
THR CB    HB     sing N N 421 
THR OG1   HG1    sing N N 422 
THR CG2   HG21   sing N N 423 
THR CG2   HG22   sing N N 424 
THR CG2   HG23   sing N N 425 
THR OXT   HXT    sing N N 426 
TRP N     CA     sing N N 427 
TRP N     H      sing N N 428 
TRP N     H2     sing N N 429 
TRP CA    C      sing N N 430 
TRP CA    CB     sing N N 431 
TRP CA    HA     sing N N 432 
TRP C     O      doub N N 433 
TRP C     OXT    sing N N 434 
TRP CB    CG     sing N N 435 
TRP CB    HB2    sing N N 436 
TRP CB    HB3    sing N N 437 
TRP CG    CD1    doub Y N 438 
TRP CG    CD2    sing Y N 439 
TRP CD1   NE1    sing Y N 440 
TRP CD1   HD1    sing N N 441 
TRP CD2   CE2    doub Y N 442 
TRP CD2   CE3    sing Y N 443 
TRP NE1   CE2    sing Y N 444 
TRP NE1   HE1    sing N N 445 
TRP CE2   CZ2    sing Y N 446 
TRP CE3   CZ3    doub Y N 447 
TRP CE3   HE3    sing N N 448 
TRP CZ2   CH2    doub Y N 449 
TRP CZ2   HZ2    sing N N 450 
TRP CZ3   CH2    sing Y N 451 
TRP CZ3   HZ3    sing N N 452 
TRP CH2   HH2    sing N N 453 
TRP OXT   HXT    sing N N 454 
TRS C     C1     sing N N 455 
TRS C     C2     sing N N 456 
TRS C     C3     sing N N 457 
TRS C     N      sing N N 458 
TRS C1    O1     sing N N 459 
TRS C1    H11    sing N N 460 
TRS C1    H12    sing N N 461 
TRS C2    O2     sing N N 462 
TRS C2    H21    sing N N 463 
TRS C2    H22    sing N N 464 
TRS C3    O3     sing N N 465 
TRS C3    H31    sing N N 466 
TRS C3    H32    sing N N 467 
TRS N     HN1    sing N N 468 
TRS N     HN2    sing N N 469 
TRS N     HN3    sing N N 470 
TRS O1    HO1    sing N N 471 
TRS O2    HO2    sing N N 472 
TRS O3    HO3    sing N N 473 
TYR N     CA     sing N N 474 
TYR N     H      sing N N 475 
TYR N     H2     sing N N 476 
TYR CA    C      sing N N 477 
TYR CA    CB     sing N N 478 
TYR CA    HA     sing N N 479 
TYR C     O      doub N N 480 
TYR C     OXT    sing N N 481 
TYR CB    CG     sing N N 482 
TYR CB    HB2    sing N N 483 
TYR CB    HB3    sing N N 484 
TYR CG    CD1    doub Y N 485 
TYR CG    CD2    sing Y N 486 
TYR CD1   CE1    sing Y N 487 
TYR CD1   HD1    sing N N 488 
TYR CD2   CE2    doub Y N 489 
TYR CD2   HD2    sing N N 490 
TYR CE1   CZ     doub Y N 491 
TYR CE1   HE1    sing N N 492 
TYR CE2   CZ     sing Y N 493 
TYR CE2   HE2    sing N N 494 
TYR CZ    OH     sing N N 495 
TYR OH    HH     sing N N 496 
TYR OXT   HXT    sing N N 497 
VAL N     CA     sing N N 498 
VAL N     H      sing N N 499 
VAL N     H2     sing N N 500 
VAL CA    C      sing N N 501 
VAL CA    CB     sing N N 502 
VAL CA    HA     sing N N 503 
VAL C     O      doub N N 504 
VAL C     OXT    sing N N 505 
VAL CB    CG1    sing N N 506 
VAL CB    CG2    sing N N 507 
VAL CB    HB     sing N N 508 
VAL CG1   HG11   sing N N 509 
VAL CG1   HG12   sing N N 510 
VAL CG1   HG13   sing N N 511 
VAL CG2   HG21   sing N N 512 
VAL CG2   HG22   sing N N 513 
VAL CG2   HG23   sing N N 514 
VAL OXT   HXT    sing N N 515 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R35GM147510 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2V7I 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DFL 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.007030 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000555 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008156 
_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]   0.015012 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . ILE A 1 22  ? 50.756 -3.990  33.584  1.00 40.09 ?  2   ILE A N     1 
ATOM   2    C  CA    . ILE A 1 22  ? 51.062 -2.558  33.493  1.00 55.14 ?  2   ILE A CA    1 
ATOM   3    C  C     . ILE A 1 22  ? 51.822 -2.299  32.181  1.00 50.13 ?  2   ILE A C     1 
ATOM   4    O  O     . ILE A 1 22  ? 52.861 -2.897  31.891  1.00 44.03 ?  2   ILE A O     1 
ATOM   5    C  CB    . ILE A 1 22  ? 51.819 -2.033  34.782  1.00 56.11 ?  2   ILE A CB    1 
ATOM   6    C  CG1   . ILE A 1 22  ? 52.116 -0.514  34.715  1.00 60.01 ?  2   ILE A CG1   1 
ATOM   7    C  CG2   . ILE A 1 22  ? 53.038 -2.900  35.135  1.00 49.59 ?  2   ILE A CG2   1 
ATOM   8    C  CD1   . ILE A 1 22  ? 53.327 -0.074  33.857  1.00 47.50 ?  2   ILE A CD1   1 
ATOM   9    N  N     . SER A 1 23  ? 51.283 -1.360  31.405  1.00 47.79 ?  3   SER A N     1 
ATOM   10   C  CA    . SER A 1 23  ? 51.541 -1.302  29.971  1.00 37.13 ?  3   SER A CA    1 
ATOM   11   C  C     . SER A 1 23  ? 52.867 -0.624  29.636  1.00 44.17 ?  3   SER A C     1 
ATOM   12   O  O     . SER A 1 23  ? 53.549 -1.029  28.686  1.00 43.28 ?  3   SER A O     1 
ATOM   13   C  CB    . SER A 1 23  ? 50.371 -0.595  29.286  1.00 36.64 ?  3   SER A CB    1 
ATOM   14   O  OG    . SER A 1 23  ? 50.624 0.791   29.126  1.00 46.91 ?  3   SER A OG    1 
ATOM   15   N  N     . ASN A 1 24  ? 53.252 0.404   30.398  1.00 54.01 ?  4   ASN A N     1 
ATOM   16   C  CA    . ASN A 1 24  ? 54.476 1.132   30.091  1.00 38.28 ?  4   ASN A CA    1 
ATOM   17   C  C     . ASN A 1 24  ? 55.720 0.279   30.294  1.00 37.87 ?  4   ASN A C     1 
ATOM   18   O  O     . ASN A 1 24  ? 56.728 0.502   29.622  1.00 42.24 ?  4   ASN A O     1 
ATOM   19   C  CB    . ASN A 1 24  ? 54.554 2.402   30.931  1.00 34.53 ?  4   ASN A CB    1 
ATOM   20   C  CG    . ASN A 1 24  ? 54.426 3.657   30.088  1.00 57.88 ?  4   ASN A CG    1 
ATOM   21   O  OD1   . ASN A 1 24  ? 55.088 3.792   29.052  1.00 56.46 ?  4   ASN A OD1   1 
ATOM   22   N  ND2   . ASN A 1 24  ? 53.578 4.586   30.525  1.00 59.19 ?  4   ASN A ND2   1 
ATOM   23   N  N     . GLU A 1 25  ? 55.674 -0.703  31.197  1.00 43.50 ?  5   GLU A N     1 
ATOM   24   C  CA    . GLU A 1 25  ? 56.829 -1.570  31.403  1.00 45.73 ?  5   GLU A CA    1 
ATOM   25   C  C     . GLU A 1 25  ? 56.918 -2.697  30.383  1.00 36.22 ?  5   GLU A C     1 
ATOM   26   O  O     . GLU A 1 25  ? 57.968 -3.340  30.289  1.00 39.92 ?  5   GLU A O     1 
ATOM   27   C  CB    . GLU A 1 25  ? 56.815 -2.167  32.815  1.00 51.70 ?  5   GLU A CB    1 
ATOM   28   C  CG    . GLU A 1 25  ? 57.228 -1.184  33.912  1.00 59.06 ?  5   GLU A CG    1 
ATOM   29   C  CD    . GLU A 1 25  ? 57.212 -1.809  35.302  1.00 76.01 ?  5   GLU A CD    1 
ATOM   30   O  OE1   . GLU A 1 25  ? 56.224 -2.503  35.641  1.00 69.08 ?  5   GLU A OE1   1 
ATOM   31   O  OE2   . GLU A 1 25  ? 58.186 -1.598  36.058  1.00 82.74 ?  5   GLU A OE2   1 
ATOM   32   N  N     . ILE A 1 26  ? 55.851 -2.966  29.638  1.00 32.98 ?  6   ILE A N     1 
ATOM   33   C  CA    . ILE A 1 26  ? 55.940 -3.912  28.529  1.00 31.27 ?  6   ILE A CA    1 
ATOM   34   C  C     . ILE A 1 26  ? 56.345 -3.208  27.239  1.00 30.44 ?  6   ILE A C     1 
ATOM   35   O  O     . ILE A 1 26  ? 57.220 -3.684  26.511  1.00 28.54 ?  6   ILE A O     1 
ATOM   36   C  CB    . ILE A 1 26  ? 54.606 -4.663  28.373  1.00 29.69 ?  6   ILE A CB    1 
ATOM   37   C  CG1   . ILE A 1 26  ? 54.300 -5.461  29.637  1.00 25.52 ?  6   ILE A CG1   1 
ATOM   38   C  CG2   . ILE A 1 26  ? 54.642 -5.593  27.175  1.00 23.12 ?  6   ILE A CG2   1 
ATOM   39   C  CD1   . ILE A 1 26  ? 52.856 -5.502  29.926  1.00 26.58 ?  6   ILE A CD1   1 
ATOM   40   N  N     . SER A 1 27  ? 55.744 -2.048  26.969  1.00 30.79 ?  7   SER A N     1 
ATOM   41   C  CA    . SER A 1 27  ? 56.019 -1.331  25.729  1.00 26.12 ?  7   SER A CA    1 
ATOM   42   C  C     . SER A 1 27  ? 57.501 -1.028  25.556  1.00 26.55 ?  7   SER A C     1 
ATOM   43   O  O     . SER A 1 27  ? 57.996 -1.028  24.428  1.00 32.49 ?  7   SER A O     1 
ATOM   44   C  CB    . SER A 1 27  ? 55.198 -0.042  25.685  1.00 24.00 ?  7   SER A CB    1 
ATOM   45   O  OG    . SER A 1 27  ? 55.583 0.816   26.733  1.00 35.99 ?  7   SER A OG    1 
ATOM   46   N  N     . LYS A 1 28  ? 58.235 -0.797  26.647  1.00 34.42 ?  8   LYS A N     1 
ATOM   47   C  CA    . LYS A 1 28  ? 59.643 -0.415  26.552  1.00 30.78 ?  8   LYS A CA    1 
ATOM   48   C  C     . LYS A 1 28  ? 60.585 -1.600  26.378  1.00 29.69 ?  8   LYS A C     1 
ATOM   49   O  O     . LYS A 1 28  ? 61.798 -1.400  26.301  1.00 27.54 ?  8   LYS A O     1 
ATOM   50   C  CB    . LYS A 1 28  ? 60.058 0.371   27.793  1.00 34.58 ?  8   LYS A CB    1 
ATOM   51   C  CG    . LYS A 1 28  ? 59.997 -0.436  29.076  1.00 38.90 ?  8   LYS A CG    1 
ATOM   52   C  CD    . LYS A 1 28  ? 59.929 0.479   30.303  1.00 52.14 ?  8   LYS A CD    1 
ATOM   53   C  CE    . LYS A 1 28  ? 61.171 1.351   30.471  1.00 66.82 ?  8   LYS A CE    1 
ATOM   54   N  NZ    . LYS A 1 28  ? 62.122 0.767   31.476  1.00 72.81 ?  8   LYS A NZ    1 
ATOM   55   N  N     . LEU A 1 29  ? 60.072 -2.819  26.321  1.00 30.34 ?  9   LEU A N     1 
ATOM   56   C  CA    . LEU A 1 29  ? 60.928 -3.986  26.255  1.00 25.53 ?  9   LEU A CA    1 
ATOM   57   C  C     . LEU A 1 29  ? 61.145 -4.419  24.809  1.00 29.28 ?  9   LEU A C     1 
ATOM   58   O  O     . LEU A 1 29  ? 60.283 -4.250  23.941  1.00 23.03 ?  9   LEU A O     1 
ATOM   59   C  CB    . LEU A 1 29  ? 60.328 -5.128  27.069  1.00 25.03 ?  9   LEU A CB    1 
ATOM   60   C  CG    . LEU A 1 29  ? 60.349 -4.920  28.591  1.00 29.14 ?  9   LEU A CG    1 
ATOM   61   C  CD1   . LEU A 1 29  ? 59.593 -6.038  29.292  1.00 25.09 ?  9   LEU A CD1   1 
ATOM   62   C  CD2   . LEU A 1 29  ? 61.789 -4.818  29.115  1.00 22.05 ?  9   LEU A CD2   1 
ATOM   63   N  N     . ASP A 1 30  ? 62.335 -4.946  24.552  1.00 30.44 ?  10  ASP A N     1 
ATOM   64   C  CA    . ASP A 1 30  ? 62.660 -5.606  23.290  1.00 26.00 ?  10  ASP A CA    1 
ATOM   65   C  C     . ASP A 1 30  ? 63.388 -6.889  23.635  1.00 23.21 ?  10  ASP A C     1 
ATOM   66   O  O     . ASP A 1 30  ? 64.602 -7.007  23.454  1.00 30.73 ?  10  ASP A O     1 
ATOM   67   C  CB    . ASP A 1 30  ? 63.505 -4.707  22.387  1.00 28.94 ?  10  ASP A CB    1 
ATOM   68   C  CG    . ASP A 1 30  ? 63.642 -5.272  20.968  1.00 34.79 ?  10  ASP A CG    1 
ATOM   69   O  OD1   . ASP A 1 30  ? 62.739 -6.028  20.538  1.00 29.61 ?  10  ASP A OD1   1 
ATOM   70   O  OD2   . ASP A 1 30  ? 64.651 -4.969  20.288  1.00 35.87 ?  10  ASP A OD2   1 
ATOM   71   N  N     . PRO A 1 31  ? 62.668 -7.882  24.147  1.00 18.06 ?  11  PRO A N     1 
ATOM   72   C  CA    . PRO A 1 31  ? 63.343 -9.066  24.692  1.00 22.51 ?  11  PRO A CA    1 
ATOM   73   C  C     . PRO A 1 31  ? 63.973 -9.946  23.634  1.00 31.63 ?  11  PRO A C     1 
ATOM   74   O  O     . PRO A 1 31  ? 64.893 -10.710 23.955  1.00 33.31 ?  11  PRO A O     1 
ATOM   75   C  CB    . PRO A 1 31  ? 62.214 -9.802  25.435  1.00 25.67 ?  11  PRO A CB    1 
ATOM   76   C  CG    . PRO A 1 31  ? 60.959 -9.389  24.699  1.00 26.82 ?  11  PRO A CG    1 
ATOM   77   C  CD    . PRO A 1 31  ? 61.200 -7.962  24.259  1.00 22.24 ?  11  PRO A CD    1 
ATOM   78   N  N     . LEU A 1 32  ? 63.502 -9.881  22.389  1.00 28.19 ?  12  LEU A N     1 
ATOM   79   C  CA    . LEU A 1 32  ? 64.077 -10.662 21.306  1.00 29.06 ?  12  LEU A CA    1 
ATOM   80   C  C     . LEU A 1 32  ? 64.923 -9.806  20.368  1.00 30.79 ?  12  LEU A C     1 
ATOM   81   O  O     . LEU A 1 32  ? 65.304 -10.279 19.293  1.00 27.29 ?  12  LEU A O     1 
ATOM   82   C  CB    . LEU A 1 32  ? 62.970 -11.398 20.541  1.00 24.16 ?  12  LEU A CB    1 
ATOM   83   C  CG    . LEU A 1 32  ? 62.034 -12.251 21.424  1.00 23.85 ?  12  LEU A CG    1 
ATOM   84   C  CD1   . LEU A 1 32  ? 60.800 -12.684 20.675  1.00 23.79 ?  12  LEU A CD1   1 
ATOM   85   C  CD2   . LEU A 1 32  ? 62.716 -13.461 22.039  1.00 20.08 ?  12  LEU A CD2   1 
ATOM   86   N  N     . ASN A 1 33  ? 65.245 -8.564  20.760  1.00 28.13 ?  13  ASN A N     1 
ATOM   87   C  CA    . ASN A 1 33  ? 66.155 -7.709  19.995  1.00 29.38 ?  13  ASN A CA    1 
ATOM   88   C  C     . ASN A 1 33  ? 65.652 -7.532  18.553  1.00 31.83 ?  13  ASN A C     1 
ATOM   89   O  O     . ASN A 1 33  ? 66.381 -7.705  17.572  1.00 29.87 ?  13  ASN A O     1 
ATOM   90   C  CB    . ASN A 1 33  ? 67.585 -8.269  20.046  1.00 21.81 ?  13  ASN A CB    1 
ATOM   91   C  CG    . ASN A 1 33  ? 68.621 -7.308  19.453  1.00 32.59 ?  13  ASN A CG    1 
ATOM   92   O  OD1   . ASN A 1 33  ? 68.435 -6.094  19.467  1.00 41.01 ?  13  ASN A OD1   1 
ATOM   93   N  ND2   . ASN A 1 33  ? 69.707 -7.857  18.915  1.00 37.32 ?  13  ASN A ND2   1 
ATOM   94   N  N     . LEU A 1 34  ? 64.370 -7.191  18.434  1.00 30.67 ?  14  LEU A N     1 
ATOM   95   C  CA    . LEU A 1 34  ? 63.675 -7.113  17.157  1.00 27.66 ?  14  LEU A CA    1 
ATOM   96   C  C     . LEU A 1 34  ? 63.415 -5.675  16.704  1.00 28.90 ?  14  LEU A C     1 
ATOM   97   O  O     . LEU A 1 34  ? 62.683 -5.462  15.729  1.00 28.86 ?  14  LEU A O     1 
ATOM   98   C  CB    . LEU A 1 34  ? 62.357 -7.887  17.252  1.00 22.09 ?  14  LEU A CB    1 
ATOM   99   C  CG    . LEU A 1 34  ? 62.499 -9.401  17.222  1.00 25.19 ?  14  LEU A CG    1 
ATOM   100  C  CD1   . LEU A 1 34  ? 61.228 -10.091 17.726  1.00 18.54 ?  14  LEU A CD1   1 
ATOM   101  C  CD2   . LEU A 1 34  ? 62.892 -9.874  15.806  1.00 22.93 ?  14  LEU A CD2   1 
ATOM   102  N  N     . ASP A 1 35  ? 64.001 -4.685  17.381  1.00 25.92 ?  15  ASP A N     1 
ATOM   103  C  CA    . ASP A 1 35  ? 63.680 -3.289  17.095  1.00 30.10 ?  15  ASP A CA    1 
ATOM   104  C  C     . ASP A 1 35  ? 64.095 -2.901  15.676  1.00 29.30 ?  15  ASP A C     1 
ATOM   105  O  O     . ASP A 1 35  ? 63.310 -2.296  14.932  1.00 30.85 ?  15  ASP A O     1 
ATOM   106  C  CB    . ASP A 1 35  ? 64.345 -2.376  18.130  1.00 23.55 ?  15  ASP A CB    1 
ATOM   107  C  CG    . ASP A 1 35  ? 63.481 -2.152  19.373  1.00 31.83 ?  15  ASP A CG    1 
ATOM   108  O  OD1   . ASP A 1 35  ? 62.404 -2.779  19.518  1.00 30.53 ?  15  ASP A OD1   1 
ATOM   109  O  OD2   . ASP A 1 35  ? 63.888 -1.324  20.214  1.00 36.17 ?  15  ASP A OD2   1 
ATOM   110  N  N     . ALA A 1 36  ? 65.332 -3.240  15.287  1.00 25.42 ?  16  ALA A N     1 
ATOM   111  C  CA    . ALA A 1 36  ? 65.794 -2.977  13.922  1.00 24.87 ?  16  ALA A CA    1 
ATOM   112  C  C     . ALA A 1 36  ? 64.951 -3.724  12.894  1.00 27.44 ?  16  ALA A C     1 
ATOM   113  O  O     . ALA A 1 36  ? 64.592 -3.168  11.848  1.00 33.07 ?  16  ALA A O     1 
ATOM   114  C  CB    . ALA A 1 36  ? 67.264 -3.371  13.771  1.00 14.65 ?  16  ALA A CB    1 
ATOM   115  N  N     . PHE A 1 37  ? 64.636 -4.989  13.177  1.00 23.34 ?  17  PHE A N     1 
ATOM   116  C  CA    . PHE A 1 37  ? 63.763 -5.769  12.313  1.00 25.47 ?  17  PHE A CA    1 
ATOM   117  C  C     . PHE A 1 37  ? 62.415 -5.084  12.096  1.00 28.15 ?  17  PHE A C     1 
ATOM   118  O  O     . PHE A 1 37  ? 61.911 -5.041  10.964  1.00 28.95 ?  17  PHE A O     1 
ATOM   119  C  CB    . PHE A 1 37  ? 63.569 -7.160  12.911  1.00 22.12 ?  17  PHE A CB    1 
ATOM   120  C  CG    . PHE A 1 37  ? 62.795 -8.084  12.036  1.00 23.85 ?  17  PHE A CG    1 
ATOM   121  C  CD1   . PHE A 1 37  ? 63.432 -8.807  11.039  1.00 23.05 ?  17  PHE A CD1   1 
ATOM   122  C  CD2   . PHE A 1 37  ? 61.426 -8.235  12.202  1.00 24.26 ?  17  PHE A CD2   1 
ATOM   123  C  CE1   . PHE A 1 37  ? 62.724 -9.674  10.233  1.00 21.22 ?  17  PHE A CE1   1 
ATOM   124  C  CE2   . PHE A 1 37  ? 60.708 -9.104  11.389  1.00 19.88 ?  17  PHE A CE2   1 
ATOM   125  C  CZ    . PHE A 1 37  ? 61.361 -9.827  10.413  1.00 20.24 ?  17  PHE A CZ    1 
ATOM   126  N  N     . PHE A 1 38  ? 61.809 -4.539  13.161  1.00 21.42 ?  18  PHE A N     1 
ATOM   127  C  CA    . PHE A 1 38  ? 60.482 -3.946  12.999  1.00 26.22 ?  18  PHE A CA    1 
ATOM   128  C  C     . PHE A 1 38  ? 60.515 -2.627  12.218  1.00 32.84 ?  18  PHE A C     1 
ATOM   129  O  O     . PHE A 1 38  ? 59.467 -2.170  11.739  1.00 22.49 ?  18  PHE A O     1 
ATOM   130  C  CB    . PHE A 1 38  ? 59.817 -3.771  14.368  1.00 28.72 ?  18  PHE A CB    1 
ATOM   131  C  CG    . PHE A 1 38  ? 59.144 -5.032  14.867  1.00 27.41 ?  18  PHE A CG    1 
ATOM   132  C  CD1   . PHE A 1 38  ? 58.021 -5.535  14.231  1.00 25.24 ?  18  PHE A CD1   1 
ATOM   133  C  CD2   . PHE A 1 38  ? 59.678 -5.748  15.928  1.00 24.48 ?  18  PHE A CD2   1 
ATOM   134  C  CE1   . PHE A 1 38  ? 57.416 -6.710  14.668  1.00 21.31 ?  18  PHE A CE1   1 
ATOM   135  C  CE2   . PHE A 1 38  ? 59.084 -6.930  16.359  1.00 26.65 ?  18  PHE A CE2   1 
ATOM   136  C  CZ    . PHE A 1 38  ? 57.952 -7.406  15.728  1.00 23.53 ?  18  PHE A CZ    1 
ATOM   137  N  N     . ASN A 1 39  ? 61.689 -2.010  12.067  1.00 27.88 ?  19  ASN A N     1 
ATOM   138  C  CA    . ASN A 1 39  ? 61.794 -0.909  11.125  1.00 31.51 ?  19  ASN A CA    1 
ATOM   139  C  C     . ASN A 1 39  ? 61.830 -1.414  9.696   1.00 31.11 ?  19  ASN A C     1 
ATOM   140  O  O     . ASN A 1 39  ? 61.377 -0.713  8.791   1.00 31.21 ?  19  ASN A O     1 
ATOM   141  C  CB    . ASN A 1 39  ? 63.029 -0.067  11.416  1.00 29.19 ?  19  ASN A CB    1 
ATOM   142  C  CG    . ASN A 1 39  ? 62.951 0.591   12.755  1.00 36.15 ?  19  ASN A CG    1 
ATOM   143  O  OD1   . ASN A 1 39  ? 61.900 1.110   13.140  1.00 42.24 ?  19  ASN A OD1   1 
ATOM   144  N  ND2   . ASN A 1 39  ? 64.053 0.559   13.495  1.00 35.62 ?  19  ASN A ND2   1 
ATOM   145  N  N     . GLN A 1 40  ? 62.331 -2.628  9.473   1.00 29.48 ?  20  GLN A N     1 
ATOM   146  C  CA    . GLN A 1 40  ? 62.286 -3.202  8.136   1.00 28.10 ?  20  GLN A CA    1 
ATOM   147  C  C     . GLN A 1 40  ? 60.983 -3.920  7.832   1.00 25.11 ?  20  GLN A C     1 
ATOM   148  O  O     . GLN A 1 40  ? 60.708 -4.186  6.665   1.00 34.99 ?  20  GLN A O     1 
ATOM   149  C  CB    . GLN A 1 40  ? 63.442 -4.183  7.924   1.00 27.12 ?  20  GLN A CB    1 
ATOM   150  C  CG    . GLN A 1 40  ? 64.772 -3.738  8.509   1.00 30.45 ?  20  GLN A CG    1 
ATOM   151  C  CD    . GLN A 1 40  ? 65.174 -2.346  8.060   1.00 46.14 ?  20  GLN A CD    1 
ATOM   152  O  OE1   . GLN A 1 40  ? 65.615 -1.526  8.874   1.00 60.66 ?  20  GLN A OE1   1 
ATOM   153  N  NE2   . GLN A 1 40  ? 65.025 -2.066  6.769   1.00 31.80 ?  20  GLN A NE2   1 
ATOM   154  N  N     . LEU A 1 41  ? 60.178 -4.241  8.837   1.00 26.94 ?  21  LEU A N     1 
ATOM   155  C  CA    . LEU A 1 41  ? 59.038 -5.123  8.595   1.00 27.49 ?  21  LEU A CA    1 
ATOM   156  C  C     . LEU A 1 41  ? 58.072 -4.595  7.544   1.00 26.64 ?  21  LEU A C     1 
ATOM   157  O  O     . LEU A 1 41  ? 57.681 -5.376  6.656   1.00 28.12 ?  21  LEU A O     1 
ATOM   158  C  CB    . LEU A 1 41  ? 58.310 -5.421  9.912   1.00 27.97 ?  21  LEU A CB    1 
ATOM   159  C  CG    . LEU A 1 41  ? 57.145 -6.381  9.660   1.00 21.48 ?  21  LEU A CG    1 
ATOM   160  C  CD1   . LEU A 1 41  ? 57.679 -7.721  9.199   1.00 17.88 ?  21  LEU A CD1   1 
ATOM   161  C  CD2   . LEU A 1 41  ? 56.260 -6.516  10.881  1.00 20.70 ?  21  LEU A CD2   1 
ATOM   162  N  N     . PRO A 1 42  ? 57.617 -3.337  7.581   1.00 26.56 ?  22  PRO A N     1 
ATOM   163  C  CA    . PRO A 1 42  ? 56.633 -2.905  6.568   1.00 28.12 ?  22  PRO A CA    1 
ATOM   164  C  C     . PRO A 1 42  ? 57.133 -3.038  5.135   1.00 27.74 ?  22  PRO A C     1 
ATOM   165  O  O     . PRO A 1 42  ? 56.327 -3.317  4.240   1.00 29.16 ?  22  PRO A O     1 
ATOM   166  C  CB    . PRO A 1 42  ? 56.351 -1.442  6.940   1.00 29.63 ?  22  PRO A CB    1 
ATOM   167  C  CG    . PRO A 1 42  ? 56.744 -1.333  8.384   1.00 29.19 ?  22  PRO A CG    1 
ATOM   168  C  CD    . PRO A 1 42  ? 57.907 -2.262  8.552   1.00 25.46 ?  22  PRO A CD    1 
ATOM   169  N  N     . SER A 1 43  ? 58.436 -2.869  4.893   1.00 27.74 ?  23  SER A N     1 
ATOM   170  C  CA    . SER A 1 43  ? 58.990 -3.096  3.559   1.00 33.40 ?  23  SER A CA    1 
ATOM   171  C  C     . SER A 1 43  ? 59.119 -4.587  3.253   1.00 33.28 ?  23  SER A C     1 
ATOM   172  O  O     . SER A 1 43  ? 58.791 -5.036  2.146   1.00 26.33 ?  23  SER A O     1 
ATOM   173  C  CB    . SER A 1 43  ? 60.357 -2.418  3.426   1.00 36.11 ?  23  SER A CB    1 
ATOM   174  O  OG    . SER A 1 43  ? 61.139 -3.046  2.408   1.00 42.93 ?  23  SER A OG    1 
ATOM   175  N  N     . LEU A 1 44  ? 59.641 -5.356  4.211   1.00 28.19 ?  24  LEU A N     1 
ATOM   176  C  CA    . LEU A 1 44  ? 59.611 -6.807  4.099   1.00 25.26 ?  24  LEU A CA    1 
ATOM   177  C  C     . LEU A 1 44  ? 58.220 -7.293  3.725   1.00 25.20 ?  24  LEU A C     1 
ATOM   178  O  O     . LEU A 1 44  ? 58.050 -8.092  2.795   1.00 25.01 ?  24  LEU A O     1 
ATOM   179  C  CB    . LEU A 1 44  ? 60.070 -7.433  5.410   1.00 25.55 ?  24  LEU A CB    1 
ATOM   180  C  CG    . LEU A 1 44  ? 61.501 -7.979  5.470   1.00 34.45 ?  24  LEU A CG    1 
ATOM   181  C  CD1   . LEU A 1 44  ? 62.494 -6.841  5.513   1.00 36.94 ?  24  LEU A CD1   1 
ATOM   182  C  CD2   . LEU A 1 44  ? 61.683 -8.867  6.713   1.00 32.08 ?  24  LEU A CD2   1 
ATOM   183  N  N     . ASN A 1 45  ? 57.205 -6.802  4.424   1.00 27.76 ?  25  ASN A N     1 
ATOM   184  C  CA    . ASN A 1 45  ? 55.851 -7.231  4.094   1.00 32.50 ?  25  ASN A CA    1 
ATOM   185  C  C     . ASN A 1 45  ? 55.441 -6.729  2.714   1.00 35.25 ?  25  ASN A C     1 
ATOM   186  O  O     . ASN A 1 45  ? 54.771 -7.450  1.964   1.00 37.32 ?  25  ASN A O     1 
ATOM   187  C  CB    . ASN A 1 45  ? 54.864 -6.758  5.166   1.00 24.14 ?  25  ASN A CB    1 
ATOM   188  C  CG    . ASN A 1 45  ? 54.707 -7.759  6.285   1.00 24.82 ?  25  ASN A CG    1 
ATOM   189  O  OD1   . ASN A 1 45  ? 55.009 -8.943  6.127   1.00 28.33 ?  25  ASN A OD1   1 
ATOM   190  N  ND2   . ASN A 1 45  ? 54.227 -7.293  7.430   1.00 26.01 ?  25  ASN A ND2   1 
ATOM   191  N  N     . GLN A 1 46  ? 55.861 -5.510  2.351   1.00 27.03 ?  26  GLN A N     1 
ATOM   192  C  CA    A GLN A 1 46  ? 55.431 -4.934  1.082   0.52 28.58 ?  26  GLN A CA    1 
ATOM   193  C  CA    B GLN A 1 46  ? 55.450 -4.920  1.079   0.48 28.96 ?  26  GLN A CA    1 
ATOM   194  C  C     . GLN A 1 46  ? 56.049 -5.663  -0.109  1.00 32.43 ?  26  GLN A C     1 
ATOM   195  O  O     . GLN A 1 46  ? 55.405 -5.815  -1.149  1.00 31.19 ?  26  GLN A O     1 
ATOM   196  C  CB    A GLN A 1 46  ? 55.768 -3.446  1.059   0.52 31.13 ?  26  GLN A CB    1 
ATOM   197  C  CB    B GLN A 1 46  ? 55.859 -3.451  1.024   0.48 31.11 ?  26  GLN A CB    1 
ATOM   198  C  CG    A GLN A 1 46  ? 55.432 -2.730  -0.218  0.52 30.16 ?  26  GLN A CG    1 
ATOM   199  C  CG    B GLN A 1 46  ? 55.229 -2.702  -0.119  0.48 30.30 ?  26  GLN A CG    1 
ATOM   200  C  CD    A GLN A 1 46  ? 56.549 -1.804  -0.639  0.52 32.33 ?  26  GLN A CD    1 
ATOM   201  C  CD    B GLN A 1 46  ? 53.770 -2.412  0.140   0.48 33.75 ?  26  GLN A CD    1 
ATOM   202  O  OE1   A GLN A 1 46  ? 56.746 -0.742  -0.043  0.52 32.55 ?  26  GLN A OE1   1 
ATOM   203  O  OE1   B GLN A 1 46  ? 52.901 -3.253  -0.081  0.48 32.55 ?  26  GLN A OE1   1 
ATOM   204  N  NE2   A GLN A 1 46  ? 57.290 -2.197  -1.673  0.52 37.19 ?  26  GLN A NE2   1 
ATOM   205  N  NE2   B GLN A 1 46  ? 53.493 -1.208  0.631   0.48 38.50 ?  26  GLN A NE2   1 
ATOM   206  N  N     . ASN A 1 47  ? 57.287 -6.115  0.014   1.00 30.99 ?  27  ASN A N     1 
ATOM   207  C  CA    . ASN A 1 47  ? 57.932 -6.855  -1.051  1.00 19.66 ?  27  ASN A CA    1 
ATOM   208  C  C     . ASN A 1 47  ? 57.750 -8.356  -0.916  1.00 24.49 ?  27  ASN A C     1 
ATOM   209  O  O     . ASN A 1 47  ? 58.495 -9.111  -1.540  1.00 30.80 ?  27  ASN A O     1 
ATOM   210  C  CB    . ASN A 1 47  ? 59.413 -6.499  -1.103  1.00 20.15 ?  27  ASN A CB    1 
ATOM   211  C  CG    . ASN A 1 47  ? 59.650 -5.122  -1.686  1.00 30.19 ?  27  ASN A CG    1 
ATOM   212  O  OD1   . ASN A 1 47  ? 59.136 -4.788  -2.763  1.00 38.10 ?  27  ASN A OD1   1 
ATOM   213  N  ND2   . ASN A 1 47  ? 60.436 -4.319  -0.995  1.00 28.90 ?  27  ASN A ND2   1 
ATOM   214  N  N     . LEU A 1 48  ? 56.788 -8.803  -0.104  1.00 27.02 ?  28  LEU A N     1 
ATOM   215  C  CA    . LEU A 1 48  ? 56.473 -10.229 0.089   1.00 29.05 ?  28  LEU A CA    1 
ATOM   216  C  C     . LEU A 1 48  ? 57.699 -11.099 0.368   1.00 28.34 ?  28  LEU A C     1 
ATOM   217  O  O     . LEU A 1 48  ? 57.797 -12.220 -0.127  1.00 30.55 ?  28  LEU A O     1 
ATOM   218  C  CB    . LEU A 1 48  ? 55.725 -10.808 -1.115  1.00 27.64 ?  28  LEU A CB    1 
ATOM   219  C  CG    . LEU A 1 48  ? 54.510 -10.161 -1.764  1.00 28.46 ?  28  LEU A CG    1 
ATOM   220  C  CD1   . LEU A 1 48  ? 53.897 -11.205 -2.690  1.00 39.16 ?  28  LEU A CD1   1 
ATOM   221  C  CD2   . LEU A 1 48  ? 53.515 -9.739  -0.732  1.00 31.80 ?  28  LEU A CD2   1 
ATOM   222  N  N     . GLU A 1 49  ? 58.633 -10.617 1.188   1.00 28.76 ?  29  GLU A N     1 
ATOM   223  C  CA    . GLU A 1 49  ? 59.875 -11.366 1.387   1.00 21.48 ?  29  GLU A CA    1 
ATOM   224  C  C     . GLU A 1 49  ? 59.676 -12.400 2.489   1.00 23.16 ?  29  GLU A C     1 
ATOM   225  O  O     . GLU A 1 49  ? 60.161 -12.280 3.609   1.00 26.52 ?  29  GLU A O     1 
ATOM   226  C  CB    . GLU A 1 49  ? 61.037 -10.431 1.672   1.00 25.25 ?  29  GLU A CB    1 
ATOM   227  C  CG    . GLU A 1 49  ? 61.831 -10.087 0.405   1.00 27.55 ?  29  GLU A CG    1 
ATOM   228  C  CD    . GLU A 1 49  ? 62.260 -8.642  0.377   1.00 35.16 ?  29  GLU A CD    1 
ATOM   229  O  OE1   . GLU A 1 49  ? 61.933 -7.920  1.340   1.00 41.71 ?  29  GLU A OE1   1 
ATOM   230  O  OE2   . GLU A 1 49  ? 62.904 -8.212  -0.597  1.00 35.32 ?  29  GLU A OE2   1 
ATOM   231  N  N     . VAL A 1 50  ? 58.977 -13.472 2.128   1.00 26.06 ?  30  VAL A N     1 
ATOM   232  C  CA    . VAL A 1 50  ? 58.633 -14.509 3.081   1.00 24.19 ?  30  VAL A CA    1 
ATOM   233  C  C     . VAL A 1 50  ? 59.862 -15.194 3.678   1.00 24.77 ?  30  VAL A C     1 
ATOM   234  O  O     . VAL A 1 50  ? 59.784 -15.721 4.791   1.00 28.41 ?  30  VAL A O     1 
ATOM   235  C  CB    . VAL A 1 50  ? 57.686 -15.524 2.399   1.00 29.43 ?  30  VAL A CB    1 
ATOM   236  C  CG1   . VAL A 1 50  ? 58.343 -16.191 1.183   1.00 19.75 ?  30  VAL A CG1   1 
ATOM   237  C  CG2   . VAL A 1 50  ? 57.181 -16.560 3.412   1.00 32.79 ?  30  VAL A CG2   1 
ATOM   238  N  N     . SER A 1 51  ? 61.013 -15.161 2.995   1.00 24.01 ?  31  SER A N     1 
ATOM   239  C  CA    . SER A 1 51  ? 62.195 -15.881 3.486   1.00 27.19 ?  31  SER A CA    1 
ATOM   240  C  C     . SER A 1 51  ? 62.813 -15.202 4.706   1.00 24.65 ?  31  SER A C     1 
ATOM   241  O  O     . SER A 1 51  ? 63.301 -15.872 5.617   1.00 27.74 ?  31  SER A O     1 
ATOM   242  C  CB    . SER A 1 51  ? 63.249 -16.007 2.383   1.00 27.57 ?  31  SER A CB    1 
ATOM   243  O  OG    . SER A 1 51  ? 62.875 -16.976 1.436   1.00 28.97 ?  31  SER A OG    1 
ATOM   244  N  N     . LEU A 1 52  ? 62.843 -13.879 4.723   1.00 23.69 ?  32  LEU A N     1 
ATOM   245  C  CA    . LEU A 1 52  ? 63.379 -13.188 5.881   1.00 20.91 ?  32  LEU A CA    1 
ATOM   246  C  C     . LEU A 1 52  ? 62.468 -13.368 7.093   1.00 25.42 ?  32  LEU A C     1 
ATOM   247  O  O     . LEU A 1 52  ? 62.949 -13.505 8.227   1.00 21.10 ?  32  LEU A O     1 
ATOM   248  C  CB    . LEU A 1 52  ? 63.590 -11.718 5.528   1.00 25.68 ?  32  LEU A CB    1 
ATOM   249  C  CG    . LEU A 1 52  ? 64.450 -11.616 4.255   1.00 29.99 ?  32  LEU A CG    1 
ATOM   250  C  CD1   . LEU A 1 52  ? 64.676 -10.167 3.809   1.00 20.52 ?  32  LEU A CD1   1 
ATOM   251  C  CD2   . LEU A 1 52  ? 65.791 -12.350 4.459   1.00 23.01 ?  32  LEU A CD2   1 
ATOM   252  N  N     . LEU A 1 53  ? 61.152 -13.394 6.864   1.00 23.23 ?  33  LEU A N     1 
ATOM   253  C  CA    . LEU A 1 53  ? 60.200 -13.740 7.915   1.00 22.05 ?  33  LEU A CA    1 
ATOM   254  C  C     . LEU A 1 53  ? 60.529 -15.097 8.538   1.00 27.34 ?  33  LEU A C     1 
ATOM   255  O  O     . LEU A 1 53  ? 60.729 -15.208 9.755   1.00 25.47 ?  33  LEU A O     1 
ATOM   256  C  CB    . LEU A 1 53  ? 58.778 -13.757 7.347   1.00 20.90 ?  33  LEU A CB    1 
ATOM   257  C  CG    . LEU A 1 53  ? 58.179 -12.516 6.681   1.00 17.79 ?  33  LEU A CG    1 
ATOM   258  C  CD1   . LEU A 1 53  ? 56.713 -12.767 6.401   1.00 18.43 ?  33  LEU A CD1   1 
ATOM   259  C  CD2   . LEU A 1 53  ? 58.356 -11.287 7.543   1.00 20.02 ?  33  LEU A CD2   1 
ATOM   260  N  N     . ILE A 1 54  ? 60.581 -16.147 7.708   1.00 24.77 ?  34  ILE A N     1 
ATOM   261  C  CA    . ILE A 1 54  ? 60.832 -17.495 8.208   1.00 21.56 ?  34  ILE A CA    1 
ATOM   262  C  C     . ILE A 1 54  ? 62.216 -17.594 8.831   1.00 27.33 ?  34  ILE A C     1 
ATOM   263  O  O     . ILE A 1 54  ? 62.396 -18.235 9.874   1.00 28.75 ?  34  ILE A O     1 
ATOM   264  C  CB    . ILE A 1 54  ? 60.657 -18.522 7.074   1.00 32.31 ?  34  ILE A CB    1 
ATOM   265  C  CG1   . ILE A 1 54  ? 59.318 -18.309 6.358   1.00 30.07 ?  34  ILE A CG1   1 
ATOM   266  C  CG2   . ILE A 1 54  ? 60.890 -19.965 7.577   1.00 25.55 ?  34  ILE A CG2   1 
ATOM   267  C  CD1   . ILE A 1 54  ? 58.180 -19.118 6.887   1.00 34.56 ?  34  ILE A CD1   1 
ATOM   268  N  N     . ASP A 1 55  ? 63.221 -16.985 8.195   1.00 27.47 ?  35  ASP A N     1 
ATOM   269  C  CA    . ASP A 1 55  ? 64.565 -17.011 8.767   1.00 31.59 ?  35  ASP A CA    1 
ATOM   270  C  C     . ASP A 1 55  ? 64.598 -16.375 10.161  1.00 32.03 ?  35  ASP A C     1 
ATOM   271  O  O     . ASP A 1 55  ? 65.356 -16.820 11.027  1.00 29.88 ?  35  ASP A O     1 
ATOM   272  C  CB    . ASP A 1 55  ? 65.544 -16.299 7.834   1.00 31.19 ?  35  ASP A CB    1 
ATOM   273  C  CG    . ASP A 1 55  ? 66.039 -17.194 6.683   1.00 51.92 ?  35  ASP A CG    1 
ATOM   274  O  OD1   . ASP A 1 55  ? 65.491 -18.314 6.477   1.00 56.35 ?  35  ASP A OD1   1 
ATOM   275  O  OD2   . ASP A 1 55  ? 66.989 -16.770 5.978   1.00 51.83 ?  35  ASP A OD2   1 
ATOM   276  N  N     . LYS A 1 56  ? 63.778 -15.345 10.392  1.00 24.05 ?  36  LYS A N     1 
ATOM   277  C  CA    . LYS A 1 56  ? 63.741 -14.679 11.689  1.00 26.29 ?  36  LYS A CA    1 
ATOM   278  C  C     . LYS A 1 56  ? 63.061 -15.552 12.752  1.00 32.66 ?  36  LYS A C     1 
ATOM   279  O  O     . LYS A 1 56  ? 63.491 -15.580 13.909  1.00 23.77 ?  36  LYS A O     1 
ATOM   280  C  CB    . LYS A 1 56  ? 63.033 -13.335 11.539  1.00 18.32 ?  36  LYS A CB    1 
ATOM   281  C  CG    . LYS A 1 56  ? 63.121 -12.407 12.741  1.00 28.01 ?  36  LYS A CG    1 
ATOM   282  C  CD    . LYS A 1 56  ? 64.515 -12.339 13.314  1.00 28.29 ?  36  LYS A CD    1 
ATOM   283  C  CE    . LYS A 1 56  ? 65.344 -11.274 12.641  1.00 25.62 ?  36  LYS A CE    1 
ATOM   284  N  NZ    . LYS A 1 56  ? 66.605 -11.101 13.419  1.00 35.49 ?  36  LYS A NZ    1 
ATOM   285  N  N     . LEU A 1 57  ? 62.015 -16.288 12.369  1.00 29.16 ?  37  LEU A N     1 
ATOM   286  C  CA    . LEU A 1 57  ? 61.360 -17.211 13.288  1.00 27.08 ?  37  LEU A CA    1 
ATOM   287  C  C     . LEU A 1 57  ? 62.310 -18.321 13.734  1.00 29.40 ?  37  LEU A C     1 
ATOM   288  O  O     . LEU A 1 57  ? 62.364 -18.670 14.918  1.00 30.02 ?  37  LEU A O     1 
ATOM   289  C  CB    . LEU A 1 57  ? 60.114 -17.803 12.613  1.00 27.23 ?  37  LEU A CB    1 
ATOM   290  C  CG    . LEU A 1 57  ? 58.938 -16.834 12.451  1.00 24.81 ?  37  LEU A CG    1 
ATOM   291  C  CD1   . LEU A 1 57  ? 57.720 -17.489 11.800  1.00 16.44 ?  37  LEU A CD1   1 
ATOM   292  C  CD2   . LEU A 1 57  ? 58.579 -16.245 13.804  1.00 21.56 ?  37  LEU A CD2   1 
ATOM   293  N  N     . ARG A 1 58  ? 63.043 -18.911 12.788  1.00 32.22 ?  38  ARG A N     1 
ATOM   294  C  CA    . ARG A 1 58  ? 64.011 -19.951 13.134  1.00 34.02 ?  38  ARG A CA    1 
ATOM   295  C  C     . ARG A 1 58  ? 65.105 -19.399 14.039  1.00 30.16 ?  38  ARG A C     1 
ATOM   296  O  O     . ARG A 1 58  ? 65.448 -20.006 15.059  1.00 32.19 ?  38  ARG A O     1 
ATOM   297  C  CB    . ARG A 1 58  ? 64.628 -20.545 11.864  1.00 31.06 ?  38  ARG A CB    1 
ATOM   298  C  CG    . ARG A 1 58  ? 63.632 -21.182 10.904  1.00 35.30 ?  38  ARG A CG    1 
ATOM   299  C  CD    . ARG A 1 58  ? 64.342 -21.708 9.684   1.00 22.82 ?  38  ARG A CD    1 
ATOM   300  N  NE    . ARG A 1 58  ? 63.491 -22.588 8.895   1.00 33.02 ?  38  ARG A NE    1 
ATOM   301  C  CZ    . ARG A 1 58  ? 63.437 -22.580 7.565   1.00 37.44 ?  38  ARG A CZ    1 
ATOM   302  N  NH1   . ARG A 1 58  ? 64.141 -21.719 6.845   1.00 34.72 ?  38  ARG A NH1   1 
ATOM   303  N  NH2   . ARG A 1 58  ? 62.651 -23.451 6.945   1.00 26.97 ?  38  ARG A NH2   1 
ATOM   304  N  N     . GLU A 1 59  ? 65.675 -18.251 13.659  1.00 22.57 ?  39  GLU A N     1 
ATOM   305  C  CA    . GLU A 1 59  ? 66.680 -17.576 14.473  1.00 30.68 ?  39  GLU A CA    1 
ATOM   306  C  C     . GLU A 1 59  ? 66.218 -17.382 15.922  1.00 30.35 ?  39  GLU A C     1 
ATOM   307  O  O     . GLU A 1 59  ? 66.999 -17.577 16.855  1.00 26.79 ?  39  GLU A O     1 
ATOM   308  C  CB    . GLU A 1 59  ? 67.029 -16.227 13.832  1.00 26.74 ?  39  GLU A CB    1 
ATOM   309  C  CG    . GLU A 1 59  ? 67.940 -16.371 12.621  1.00 38.62 ?  39  GLU A CG    1 
ATOM   310  C  CD    . GLU A 1 59  ? 67.971 -15.154 11.689  1.00 39.48 ?  39  GLU A CD    1 
ATOM   311  O  OE1   . GLU A 1 59  ? 67.557 -14.046 12.092  1.00 36.31 ?  39  GLU A OE1   1 
ATOM   312  O  OE2   . GLU A 1 59  ? 68.430 -15.317 10.538  1.00 44.97 ?  39  GLU A OE2   1 
ATOM   313  N  N     . ILE A 1 60  ? 64.954 -16.998 16.124  1.00 25.76 ?  40  ILE A N     1 
ATOM   314  C  CA    . ILE A 1 60  ? 64.455 -16.727 17.467  1.00 31.34 ?  40  ILE A CA    1 
ATOM   315  C  C     . ILE A 1 60  ? 64.422 -18.005 18.299  1.00 30.59 ?  40  ILE A C     1 
ATOM   316  O  O     . ILE A 1 60  ? 64.905 -18.031 19.439  1.00 32.25 ?  40  ILE A O     1 
ATOM   317  C  CB    . ILE A 1 60  ? 63.065 -16.061 17.414  1.00 28.62 ?  40  ILE A CB    1 
ATOM   318  C  CG1   . ILE A 1 60  ? 63.169 -14.647 16.848  1.00 17.93 ?  40  ILE A CG1   1 
ATOM   319  C  CG2   . ILE A 1 60  ? 62.432 -16.060 18.827  1.00 22.93 ?  40  ILE A CG2   1 
ATOM   320  C  CD1   . ILE A 1 60  ? 61.867 -14.066 16.452  1.00 17.92 ?  40  ILE A CD1   1 
ATOM   321  N  N     . THR A 1 61  ? 63.845 -19.079 17.753  1.00 24.46 ?  41  THR A N     1 
ATOM   322  C  CA    . THR A 1 61  ? 63.726 -20.310 18.525  1.00 26.24 ?  41  THR A CA    1 
ATOM   323  C  C     . THR A 1 61  ? 65.071 -20.952 18.828  1.00 29.96 ?  41  THR A C     1 
ATOM   324  O  O     . THR A 1 61  ? 65.102 -21.938 19.570  1.00 31.27 ?  41  THR A O     1 
ATOM   325  C  CB    . THR A 1 61  ? 62.840 -21.328 17.806  1.00 28.85 ?  41  THR A CB    1 
ATOM   326  O  OG1   . THR A 1 61  ? 63.512 -21.829 16.633  1.00 37.09 ?  41  THR A OG1   1 
ATOM   327  C  CG2   . THR A 1 61  ? 61.517 -20.686 17.414  1.00 29.00 ?  41  THR A CG2   1 
ATOM   328  N  N     . LYS A 1 62  ? 66.169 -20.431 18.263  1.00 32.14 ?  42  LYS A N     1 
ATOM   329  C  CA    . LYS A 1 62  ? 67.521 -20.902 18.546  1.00 33.91 ?  42  LYS A CA    1 
ATOM   330  C  C     . LYS A 1 62  ? 68.372 -19.909 19.323  1.00 27.83 ?  42  LYS A C     1 
ATOM   331  O  O     . LYS A 1 62  ? 69.404 -20.306 19.870  1.00 31.19 ?  42  LYS A O     1 
ATOM   332  C  CB    . LYS A 1 62  ? 68.273 -21.226 17.245  1.00 31.04 ?  42  LYS A CB    1 
ATOM   333  C  CG    . LYS A 1 62  ? 67.578 -22.143 16.289  1.00 30.85 ?  42  LYS A CG    1 
ATOM   334  C  CD    . LYS A 1 62  ? 68.474 -22.324 15.092  1.00 35.09 ?  42  LYS A CD    1 
ATOM   335  C  CE    . LYS A 1 62  ? 67.774 -22.997 13.927  1.00 40.13 ?  42  LYS A CE    1 
ATOM   336  N  NZ    . LYS A 1 62  ? 68.516 -22.650 12.678  1.00 39.49 ?  42  LYS A NZ    1 
ATOM   337  N  N     . SER A 1 63  ? 67.994 -18.634 19.353  1.00 25.48 ?  43  SER A N     1 
ATOM   338  C  CA    . SER A 1 63  ? 68.801 -17.613 19.993  1.00 31.68 ?  43  SER A CA    1 
ATOM   339  C  C     . SER A 1 63  ? 68.340 -17.274 21.403  1.00 31.34 ?  43  SER A C     1 
ATOM   340  O  O     . SER A 1 63  ? 69.005 -16.478 22.073  1.00 31.70 ?  43  SER A O     1 
ATOM   341  C  CB    . SER A 1 63  ? 68.802 -16.333 19.155  1.00 31.87 ?  43  SER A CB    1 
ATOM   342  O  OG    . SER A 1 63  ? 69.713 -16.427 18.075  1.00 38.36 ?  43  SER A OG    1 
ATOM   343  N  N     . TYR A 1 64  ? 67.226 -17.839 21.860  1.00 28.21 ?  44  TYR A N     1 
ATOM   344  C  CA    . TYR A 1 64  ? 66.585 -17.392 23.091  1.00 34.84 ?  44  TYR A CA    1 
ATOM   345  C  C     . TYR A 1 64  ? 65.973 -18.598 23.772  1.00 36.20 ?  44  TYR A C     1 
ATOM   346  O  O     . TYR A 1 64  ? 65.352 -19.438 23.114  1.00 39.17 ?  44  TYR A O     1 
ATOM   347  C  CB    . TYR A 1 64  ? 65.513 -16.320 22.819  1.00 29.11 ?  44  TYR A CB    1 
ATOM   348  C  CG    . TYR A 1 64  ? 66.129 -15.022 22.365  1.00 29.13 ?  44  TYR A CG    1 
ATOM   349  C  CD1   . TYR A 1 64  ? 66.705 -14.146 23.285  1.00 21.39 ?  44  TYR A CD1   1 
ATOM   350  C  CD2   . TYR A 1 64  ? 66.183 -14.687 21.003  1.00 27.24 ?  44  TYR A CD2   1 
ATOM   351  C  CE1   . TYR A 1 64  ? 67.299 -12.953 22.874  1.00 19.57 ?  44  TYR A CE1   1 
ATOM   352  C  CE2   . TYR A 1 64  ? 66.787 -13.501 20.576  1.00 28.24 ?  44  TYR A CE2   1 
ATOM   353  C  CZ    . TYR A 1 64  ? 67.340 -12.635 21.517  1.00 31.33 ?  44  TYR A CZ    1 
ATOM   354  O  OH    . TYR A 1 64  ? 67.939 -11.467 21.088  1.00 27.86 ?  44  TYR A OH    1 
ATOM   355  N  N     . LEU A 1 65  ? 66.202 -18.707 25.073  1.00 35.45 ?  45  LEU A N     1 
ATOM   356  C  CA    . LEU A 1 65  ? 65.529 -19.723 25.860  1.00 39.16 ?  45  LEU A CA    1 
ATOM   357  C  C     . LEU A 1 65  ? 64.381 -19.033 26.560  1.00 38.23 ?  45  LEU A C     1 
ATOM   358  O  O     . LEU A 1 65  ? 64.594 -18.367 27.590  1.00 34.35 ?  45  LEU A O     1 
ATOM   359  C  CB    . LEU A 1 65  ? 66.473 -20.374 26.873  1.00 40.64 ?  45  LEU A CB    1 
ATOM   360  C  CG    . LEU A 1 65  ? 67.801 -20.886 26.324  1.00 35.76 ?  45  LEU A CG    1 
ATOM   361  C  CD1   . LEU A 1 65  ? 68.958 -20.408 27.190  1.00 30.32 ?  45  LEU A CD1   1 
ATOM   362  C  CD2   . LEU A 1 65  ? 67.756 -22.407 26.193  1.00 30.85 ?  45  LEU A CD2   1 
ATOM   363  N  N     . PRO A 1 66  ? 63.160 -19.126 26.036  1.00 33.00 ?  46  PRO A N     1 
ATOM   364  C  CA    . PRO A 1 66  ? 62.054 -18.373 26.638  1.00 34.22 ?  46  PRO A CA    1 
ATOM   365  C  C     . PRO A 1 66  ? 61.783 -18.772 28.073  1.00 32.72 ?  46  PRO A C     1 
ATOM   366  O  O     . PRO A 1 66  ? 61.246 -17.951 28.829  1.00 35.08 ?  46  PRO A O     1 
ATOM   367  C  CB    . PRO A 1 66  ? 60.864 -18.690 25.721  1.00 27.48 ?  46  PRO A CB    1 
ATOM   368  C  CG    . PRO A 1 66  ? 61.225 -19.957 25.037  1.00 28.08 ?  46  PRO A CG    1 
ATOM   369  C  CD    . PRO A 1 66  ? 62.726 -19.987 24.925  1.00 31.72 ?  46  PRO A CD    1 
ATOM   370  N  N     . THR A 1 67  ? 62.169 -19.986 28.484  1.00 29.66 ?  47  THR A N     1 
ATOM   371  C  CA    . THR A 1 67  ? 61.941 -20.399 29.863  1.00 25.19 ?  47  THR A CA    1 
ATOM   372  C  C     . THR A 1 67  ? 62.587 -19.433 30.848  1.00 27.78 ?  47  THR A C     1 
ATOM   373  O  O     . THR A 1 67  ? 62.050 -19.209 31.934  1.00 32.34 ?  47  THR A O     1 
ATOM   374  C  CB    . THR A 1 67  ? 62.445 -21.827 30.078  1.00 34.71 ?  47  THR A CB    1 
ATOM   375  O  OG1   . THR A 1 67  ? 61.918 -22.333 31.312  1.00 33.63 ?  47  THR A OG1   1 
ATOM   376  C  CG2   . THR A 1 67  ? 63.961 -21.867 30.122  1.00 28.51 ?  47  THR A CG2   1 
ATOM   377  N  N     . THR A 1 68  ? 63.684 -18.791 30.463  1.00 29.21 ?  48  THR A N     1 
ATOM   378  C  CA    . THR A 1 68  ? 64.354 -17.860 31.357  1.00 31.07 ?  48  THR A CA    1 
ATOM   379  C  C     . THR A 1 68  ? 63.713 -16.476 31.379  1.00 38.24 ?  48  THR A C     1 
ATOM   380  O  O     . THR A 1 68  ? 64.296 -15.568 31.985  1.00 34.56 ?  48  THR A O     1 
ATOM   381  C  CB    . THR A 1 68  ? 65.834 -17.718 30.981  1.00 31.93 ?  48  THR A CB    1 
ATOM   382  O  OG1   . THR A 1 68  ? 65.952 -16.964 29.767  1.00 31.72 ?  48  THR A OG1   1 
ATOM   383  C  CG2   . THR A 1 68  ? 66.486 -19.087 30.805  1.00 28.04 ?  48  THR A CG2   1 
ATOM   384  N  N     . PHE A 1 69  ? 62.552 -16.283 30.753  1.00 32.44 ?  49  PHE A N     1 
ATOM   385  C  CA    . PHE A 1 69  ? 61.958 -14.954 30.671  1.00 34.38 ?  49  PHE A CA    1 
ATOM   386  C  C     . PHE A 1 69  ? 61.106 -14.651 31.901  1.00 29.74 ?  49  PHE A C     1 
ATOM   387  O  O     . PHE A 1 69  ? 60.482 -15.542 32.481  1.00 31.90 ?  49  PHE A O     1 
ATOM   388  C  CB    . PHE A 1 69  ? 61.072 -14.803 29.431  1.00 28.28 ?  49  PHE A CB    1 
ATOM   389  C  CG    . PHE A 1 69  ? 61.808 -14.766 28.130  1.00 30.66 ?  49  PHE A CG    1 
ATOM   390  C  CD1   . PHE A 1 69  ? 63.117 -15.193 28.026  1.00 36.42 ?  49  PHE A CD1   1 
ATOM   391  C  CD2   . PHE A 1 69  ? 61.165 -14.313 26.992  1.00 27.33 ?  49  PHE A CD2   1 
ATOM   392  C  CE1   . PHE A 1 69  ? 63.775 -15.165 26.808  1.00 33.58 ?  49  PHE A CE1   1 
ATOM   393  C  CE2   . PHE A 1 69  ? 61.815 -14.269 25.790  1.00 30.27 ?  49  PHE A CE2   1 
ATOM   394  C  CZ    . PHE A 1 69  ? 63.121 -14.698 25.692  1.00 32.26 ?  49  PHE A CZ    1 
ATOM   395  N  N     . SER A 1 70  ? 61.058 -13.370 32.264  1.00 22.65 ?  50  SER A N     1 
ATOM   396  C  CA    . SER A 1 70  ? 60.075 -12.823 33.188  1.00 24.73 ?  50  SER A CA    1 
ATOM   397  C  C     . SER A 1 70  ? 58.701 -12.690 32.519  1.00 28.91 ?  50  SER A C     1 
ATOM   398  O  O     . SER A 1 70  ? 58.559 -12.798 31.299  1.00 31.55 ?  50  SER A O     1 
ATOM   399  C  CB    . SER A 1 70  ? 60.526 -11.452 33.676  1.00 23.74 ?  50  SER A CB    1 
ATOM   400  O  OG    . SER A 1 70  ? 60.225 -10.466 32.696  1.00 28.31 ?  50  SER A OG    1 
ATOM   401  N  N     . ILE A 1 71  ? 57.679 -12.401 33.332  1.00 30.51 ?  51  ILE A N     1 
ATOM   402  C  CA    . ILE A 1 71  ? 56.327 -12.222 32.796  1.00 30.98 ?  51  ILE A CA    1 
ATOM   403  C  C     . ILE A 1 71  ? 56.300 -11.080 31.780  1.00 30.49 ?  51  ILE A C     1 
ATOM   404  O  O     . ILE A 1 71  ? 55.781 -11.228 30.668  1.00 31.02 ?  51  ILE A O     1 
ATOM   405  C  CB    . ILE A 1 71  ? 55.311 -11.982 33.928  1.00 26.17 ?  51  ILE A CB    1 
ATOM   406  C  CG1   . ILE A 1 71  ? 54.878 -13.293 34.573  1.00 30.65 ?  51  ILE A CG1   1 
ATOM   407  C  CG2   . ILE A 1 71  ? 54.075 -11.295 33.402  1.00 28.76 ?  51  ILE A CG2   1 
ATOM   408  C  CD1   . ILE A 1 71  ? 54.756 -13.205 36.124  1.00 25.17 ?  51  ILE A CD1   1 
ATOM   409  N  N     . ASN A 1 72  ? 56.846 -9.920  32.146  1.00 34.31 ?  52  ASN A N     1 
ATOM   410  C  CA    . ASN A 1 72  ? 56.820 -8.793  31.217  1.00 29.14 ?  52  ASN A CA    1 
ATOM   411  C  C     . ASN A 1 72  ? 57.606 -9.103  29.958  1.00 24.84 ?  52  ASN A C     1 
ATOM   412  O  O     . ASN A 1 72  ? 57.233 -8.656  28.872  1.00 22.43 ?  52  ASN A O     1 
ATOM   413  C  CB    . ASN A 1 72  ? 57.370 -7.537  31.883  1.00 22.79 ?  52  ASN A CB    1 
ATOM   414  C  CG    . ASN A 1 72  ? 56.442 -7.007  32.957  1.00 35.60 ?  52  ASN A CG    1 
ATOM   415  O  OD1   . ASN A 1 72  ? 55.308 -7.487  33.104  1.00 30.73 ?  52  ASN A OD1   1 
ATOM   416  N  ND2   . ASN A 1 72  ? 56.913 -6.014  33.716  1.00 30.82 ?  52  ASN A ND2   1 
ATOM   417  N  N     . ASP A 1 73  ? 58.691 -9.866  30.086  1.00 26.85 ?  53  ASP A N     1 
ATOM   418  C  CA    . ASP A 1 73  ? 59.466 -10.240 28.912  1.00 26.80 ?  53  ASP A CA    1 
ATOM   419  C  C     . ASP A 1 73  ? 58.650 -11.112 27.978  1.00 23.32 ?  53  ASP A C     1 
ATOM   420  O  O     . ASP A 1 73  ? 58.655 -10.896 26.767  1.00 27.69 ?  53  ASP A O     1 
ATOM   421  C  CB    . ASP A 1 73  ? 60.735 -10.969 29.321  1.00 25.30 ?  53  ASP A CB    1 
ATOM   422  C  CG    . ASP A 1 73  ? 61.859 -10.027 29.652  1.00 34.42 ?  53  ASP A CG    1 
ATOM   423  O  OD1   . ASP A 1 73  ? 61.790 -8.832  29.247  1.00 35.38 ?  53  ASP A OD1   1 
ATOM   424  O  OD2   . ASP A 1 73  ? 62.816 -10.501 30.316  1.00 34.93 ?  53  ASP A OD2   1 
ATOM   425  N  N     . ALA A 1 74  ? 57.943 -12.095 28.523  1.00 22.66 ?  54  ALA A N     1 
ATOM   426  C  CA    . ALA A 1 74  ? 57.191 -13.000 27.674  1.00 25.76 ?  54  ALA A CA    1 
ATOM   427  C  C     . ALA A 1 74  ? 55.995 -12.301 27.033  1.00 27.95 ?  54  ALA A C     1 
ATOM   428  O  O     . ALA A 1 74  ? 55.577 -12.681 25.930  1.00 28.80 ?  54  ALA A O     1 
ATOM   429  C  CB    . ALA A 1 74  ? 56.760 -14.222 28.479  1.00 19.21 ?  54  ALA A CB    1 
ATOM   430  N  N     . LEU A 1 75  ? 55.445 -11.277 27.684  1.00 18.53 ?  55  LEU A N     1 
ATOM   431  C  CA    . LEU A 1 75  ? 54.321 -10.562 27.091  1.00 23.50 ?  55  LEU A CA    1 
ATOM   432  C  C     . LEU A 1 75  ? 54.770 -9.735  25.898  1.00 26.30 ?  55  LEU A C     1 
ATOM   433  O  O     . LEU A 1 75  ? 54.054 -9.635  24.890  1.00 22.52 ?  55  LEU A O     1 
ATOM   434  C  CB    . LEU A 1 75  ? 53.664 -9.649  28.120  1.00 24.67 ?  55  LEU A CB    1 
ATOM   435  C  CG    . LEU A 1 75  ? 52.907 -10.274 29.267  1.00 22.52 ?  55  LEU A CG    1 
ATOM   436  C  CD1   . LEU A 1 75  ? 52.697 -9.186  30.324  1.00 23.87 ?  55  LEU A CD1   1 
ATOM   437  C  CD2   . LEU A 1 75  ? 51.600 -10.867 28.774  1.00 20.03 ?  55  LEU A CD2   1 
ATOM   438  N  N     . ALA A 1 76  ? 55.939 -9.106  26.017  1.00 22.68 ?  56  ALA A N     1 
ATOM   439  C  CA    . ALA A 1 76  ? 56.487 -8.342  24.913  1.00 20.09 ?  56  ALA A CA    1 
ATOM   440  C  C     . ALA A 1 76  ? 56.988 -9.266  23.806  1.00 25.46 ?  56  ALA A C     1 
ATOM   441  O  O     . ALA A 1 76  ? 56.864 -8.932  22.617  1.00 25.92 ?  56  ALA A O     1 
ATOM   442  C  CB    . ALA A 1 76  ? 57.592 -7.430  25.438  1.00 23.94 ?  56  ALA A CB    1 
ATOM   443  N  N     . ALA A 1 77  ? 57.527 -10.436 24.177  1.00 19.56 ?  57  ALA A N     1 
ATOM   444  C  CA    . ALA A 1 77  ? 57.886 -11.444 23.188  1.00 20.45 ?  57  ALA A CA    1 
ATOM   445  C  C     . ALA A 1 77  ? 56.657 -11.934 22.430  1.00 24.58 ?  57  ALA A C     1 
ATOM   446  O  O     . ALA A 1 77  ? 56.689 -12.036 21.199  1.00 19.69 ?  57  ALA A O     1 
ATOM   447  C  CB    . ALA A 1 77  ? 58.617 -12.604 23.858  1.00 17.76 ?  57  ALA A CB    1 
ATOM   448  N  N     . THR A 1 78  ? 55.552 -12.206 23.141  1.00 21.64 ?  58  THR A N     1 
ATOM   449  C  CA    . THR A 1 78  ? 54.318 -12.610 22.468  1.00 20.91 ?  58  THR A CA    1 
ATOM   450  C  C     . THR A 1 78  ? 53.821 -11.539 21.508  1.00 24.28 ?  58  THR A C     1 
ATOM   451  O  O     . THR A 1 78  ? 53.206 -11.857 20.488  1.00 24.04 ?  58  THR A O     1 
ATOM   452  C  CB    . THR A 1 78  ? 53.218 -12.919 23.486  1.00 21.13 ?  58  THR A CB    1 
ATOM   453  O  OG1   . THR A 1 78  ? 53.713 -13.828 24.467  1.00 30.64 ?  58  THR A OG1   1 
ATOM   454  C  CG2   . THR A 1 78  ? 51.985 -13.528 22.820  1.00 17.70 ?  58  THR A CG2   1 
ATOM   455  N  N     . ARG A 1 79  ? 54.032 -10.265 21.837  1.00 24.67 ?  59  ARG A N     1 
ATOM   456  C  CA    . ARG A 1 79  ? 53.656 -9.190  20.930  1.00 17.32 ?  59  ARG A CA    1 
ATOM   457  C  C     . ARG A 1 79  ? 54.487 -9.253  19.651  1.00 21.88 ?  59  ARG A C     1 
ATOM   458  O  O     . ARG A 1 79  ? 53.949 -9.252  18.535  1.00 18.98 ?  59  ARG A O     1 
ATOM   459  C  CB    . ARG A 1 79  ? 53.842 -7.841  21.636  1.00 20.05 ?  59  ARG A CB    1 
ATOM   460  C  CG    . ARG A 1 79  ? 53.729 -6.598  20.725  1.00 26.01 ?  59  ARG A CG    1 
ATOM   461  C  CD    . ARG A 1 79  ? 54.454 -5.405  21.305  1.00 19.43 ?  59  ARG A CD    1 
ATOM   462  N  NE    . ARG A 1 79  ? 55.879 -5.674  21.441  1.00 21.06 ?  59  ARG A NE    1 
ATOM   463  C  CZ    . ARG A 1 79  ? 56.637 -5.231  22.437  1.00 24.82 ?  59  ARG A CZ    1 
ATOM   464  N  NH1   . ARG A 1 79  ? 56.141 -4.452  23.387  1.00 22.79 ?  59  ARG A NH1   1 
ATOM   465  N  NH2   . ARG A 1 79  ? 57.921 -5.596  22.491  1.00 20.46 ?  59  ARG A NH2   1 
ATOM   466  N  N     . ASP A 1 80  ? 55.806 -9.349  19.804  1.00 22.54 ?  60  ASP A N     1 
ATOM   467  C  CA    . ASP A 1 80  ? 56.711 -9.263  18.667  1.00 22.17 ?  60  ASP A CA    1 
ATOM   468  C  C     . ASP A 1 80  ? 56.666 -10.531 17.806  1.00 29.85 ?  60  ASP A C     1 
ATOM   469  O  O     . ASP A 1 80  ? 56.427 -10.467 16.591  1.00 27.77 ?  60  ASP A O     1 
ATOM   470  C  CB    . ASP A 1 80  ? 58.109 -8.972  19.193  1.00 17.43 ?  60  ASP A CB    1 
ATOM   471  C  CG    . ASP A 1 80  ? 58.236 -7.549  19.730  1.00 22.57 ?  60  ASP A CG    1 
ATOM   472  O  OD1   . ASP A 1 80  ? 57.326 -6.712  19.503  1.00 21.62 ?  60  ASP A OD1   1 
ATOM   473  O  OD2   . ASP A 1 80  ? 59.262 -7.256  20.361  1.00 24.55 ?  60  ASP A OD2   1 
ATOM   474  N  N     . LEU A 1 81  ? 56.877 -11.693 18.423  1.00 22.17 ?  61  LEU A N     1 
ATOM   475  C  CA    . LEU A 1 81  ? 56.735 -12.955 17.715  1.00 19.39 ?  61  LEU A CA    1 
ATOM   476  C  C     . LEU A 1 81  ? 55.357 -13.079 17.069  1.00 23.97 ?  61  LEU A C     1 
ATOM   477  O  O     . LEU A 1 81  ? 55.230 -13.584 15.948  1.00 21.96 ?  61  LEU A O     1 
ATOM   478  C  CB    . LEU A 1 81  ? 56.974 -14.099 18.696  1.00 23.37 ?  61  LEU A CB    1 
ATOM   479  C  CG    . LEU A 1 81  ? 57.328 -15.473 18.165  1.00 29.59 ?  61  LEU A CG    1 
ATOM   480  C  CD1   . LEU A 1 81  ? 58.502 -15.343 17.216  1.00 21.54 ?  61  LEU A CD1   1 
ATOM   481  C  CD2   . LEU A 1 81  ? 57.646 -16.415 19.332  1.00 24.63 ?  61  LEU A CD2   1 
ATOM   482  N  N     . GLY A 1 82  ? 54.309 -12.620 17.761  1.00 23.69 ?  62  GLY A N     1 
ATOM   483  C  CA    . GLY A 1 82  ? 52.964 -12.726 17.206  1.00 22.57 ?  62  GLY A CA    1 
ATOM   484  C  C     . GLY A 1 82  ? 52.809 -11.971 15.895  1.00 30.45 ?  62  GLY A C     1 
ATOM   485  O  O     . GLY A 1 82  ? 52.183 -12.460 14.950  1.00 27.51 ?  62  GLY A O     1 
ATOM   486  N  N     . MET A 1 83  ? 53.392 -10.779 15.810  1.00 23.45 ?  63  MET A N     1 
ATOM   487  C  CA    . MET A 1 83  ? 53.252 -10.004 14.590  1.00 24.34 ?  63  MET A CA    1 
ATOM   488  C  C     . MET A 1 83  ? 54.078 -10.589 13.442  1.00 25.68 ?  63  MET A C     1 
ATOM   489  O  O     . MET A 1 83  ? 53.609 -10.621 12.303  1.00 25.65 ?  63  MET A O     1 
ATOM   490  C  CB    . MET A 1 83  ? 53.603 -8.554  14.881  1.00 26.35 ?  63  MET A CB    1 
ATOM   491  C  CG    . MET A 1 83  ? 52.477 -7.888  15.678  1.00 27.13 ?  63  MET A CG    1 
ATOM   492  S  SD    . MET A 1 83  ? 52.809 -6.174  15.996  1.00 35.33 ?  63  MET A SD    1 
ATOM   493  C  CE    . MET A 1 83  ? 52.884 -5.509  14.308  1.00 27.16 ?  63  MET A CE    1 
ATOM   494  N  N     . ILE A 1 84  ? 55.293 -11.074 13.708  1.00 22.11 ?  64  ILE A N     1 
ATOM   495  C  CA    . ILE A 1 84  ? 56.014 -11.784 12.655  1.00 19.21 ?  64  ILE A CA    1 
ATOM   496  C  C     . ILE A 1 84  ? 55.205 -12.990 12.187  1.00 21.15 ?  64  ILE A C     1 
ATOM   497  O  O     . ILE A 1 84  ? 55.033 -13.207 10.986  1.00 24.20 ?  64  ILE A O     1 
ATOM   498  C  CB    . ILE A 1 84  ? 57.423 -12.187 13.128  1.00 19.73 ?  64  ILE A CB    1 
ATOM   499  C  CG1   . ILE A 1 84  ? 58.208 -10.962 13.593  1.00 17.74 ?  64  ILE A CG1   1 
ATOM   500  C  CG2   . ILE A 1 84  ? 58.169 -12.883 12.013  1.00 19.28 ?  64  ILE A CG2   1 
ATOM   501  C  CD1   . ILE A 1 84  ? 59.525 -11.314 14.281  1.00 21.59 ?  64  ILE A CD1   1 
ATOM   502  N  N     . MET A 1 85  ? 54.658 -13.762 13.133  1.00 21.18 ?  65  MET A N     1 
ATOM   503  C  CA    . MET A 1 85  ? 53.789 -14.886 12.801  1.00 20.84 ?  65  MET A CA    1 
ATOM   504  C  C     . MET A 1 85  ? 52.590 -14.453 11.983  1.00 17.83 ?  65  MET A C     1 
ATOM   505  O  O     . MET A 1 85  ? 52.209 -15.138 11.034  1.00 20.37 ?  65  MET A O     1 
ATOM   506  C  CB    . MET A 1 85  ? 53.319 -15.597 14.078  1.00 16.20 ?  65  MET A CB    1 
ATOM   507  C  CG    . MET A 1 85  ? 54.342 -16.525 14.696  1.00 19.09 ?  65  MET A CG    1 
ATOM   508  S  SD    . MET A 1 85  ? 53.671 -17.537 16.042  1.00 31.23 ?  65  MET A SD    1 
ATOM   509  C  CE    . MET A 1 85  ? 52.719 -16.284 16.935  1.00 14.73 ?  65  MET A CE    1 
ATOM   510  N  N     . SER A 1 86  ? 51.957 -13.345 12.356  1.00 20.26 ?  66  SER A N     1 
ATOM   511  C  CA    . SER A 1 86  ? 50.790 -12.874 11.613  1.00 21.03 ?  66  SER A CA    1 
ATOM   512  C  C     . SER A 1 86  ? 51.149 -12.462 10.186  1.00 22.72 ?  66  SER A C     1 
ATOM   513  O  O     . SER A 1 86  ? 50.297 -12.530 9.287   1.00 15.93 ?  66  SER A O     1 
ATOM   514  C  CB    . SER A 1 86  ? 50.151 -11.705 12.356  1.00 18.86 ?  66  SER A CB    1 
ATOM   515  O  OG    . SER A 1 86  ? 49.454 -12.193 13.477  1.00 24.25 ?  66  SER A OG    1 
ATOM   516  N  N     . SER A 1 87  ? 52.402 -12.004 9.986   1.00 20.68 ?  67  SER A N     1 
ATOM   517  C  CA    . SER A 1 87  ? 52.922 -11.604 8.686   1.00 19.80 ?  67  SER A CA    1 
ATOM   518  C  C     . SER A 1 87  ? 53.147 -12.807 7.772   1.00 25.33 ?  67  SER A C     1 
ATOM   519  O  O     . SER A 1 87  ? 52.998 -12.699 6.551   1.00 20.08 ?  67  SER A O     1 
ATOM   520  C  CB    . SER A 1 87  ? 54.236 -10.847 8.862   1.00 17.52 ?  67  SER A CB    1 
ATOM   521  O  OG    . SER A 1 87  ? 54.060 -9.672  9.621   1.00 17.78 ?  67  SER A OG    1 
ATOM   522  N  N     . VAL A 1 88  ? 53.527 -13.949 8.343   1.00 23.57 ?  68  VAL A N     1 
ATOM   523  C  CA    . VAL A 1 88  ? 53.677 -15.155 7.548   1.00 18.83 ?  68  VAL A CA    1 
ATOM   524  C  C     . VAL A 1 88  ? 52.315 -15.706 7.182   1.00 19.27 ?  68  VAL A C     1 
ATOM   525  O  O     . VAL A 1 88  ? 52.072 -16.090 6.033   1.00 28.63 ?  68  VAL A O     1 
ATOM   526  C  CB    . VAL A 1 88  ? 54.535 -16.170 8.314   1.00 22.66 ?  68  VAL A CB    1 
ATOM   527  C  CG1   . VAL A 1 88  ? 54.494 -17.520 7.645   1.00 24.35 ?  68  VAL A CG1   1 
ATOM   528  C  CG2   . VAL A 1 88  ? 55.966 -15.638 8.434   1.00 17.83 ?  68  VAL A CG2   1 
ATOM   529  N  N     . ARG A 1 89  ? 51.387 -15.698 8.132   1.00 21.76 ?  69  ARG A N     1 
ATOM   530  C  CA    . ARG A 1 89  ? 50.033 -16.167 7.854   1.00 23.51 ?  69  ARG A CA    1 
ATOM   531  C  C     . ARG A 1 89  ? 49.316 -15.280 6.835   1.00 19.40 ?  69  ARG A C     1 
ATOM   532  O  O     . ARG A 1 89  ? 48.388 -15.739 6.156   1.00 17.09 ?  69  ARG A O     1 
ATOM   533  C  CB    . ARG A 1 89  ? 49.247 -16.237 9.158   1.00 14.21 ?  69  ARG A CB    1 
ATOM   534  C  CG    . ARG A 1 89  ? 47.791 -16.513 8.971   1.00 18.11 ?  69  ARG A CG    1 
ATOM   535  C  CD    . ARG A 1 89  ? 47.574 -17.914 8.446   1.00 22.65 ?  69  ARG A CD    1 
ATOM   536  N  NE    . ARG A 1 89  ? 46.154 -18.245 8.346   1.00 23.32 ?  69  ARG A NE    1 
ATOM   537  C  CZ    . ARG A 1 89  ? 45.369 -17.894 7.335   1.00 26.24 ?  69  ARG A CZ    1 
ATOM   538  N  NH1   . ARG A 1 89  ? 45.833 -17.218 6.298   1.00 20.51 ?  69  ARG A NH1   1 
ATOM   539  N  NH2   . ARG A 1 89  ? 44.081 -18.207 7.377   1.00 27.02 ?  69  ARG A NH2   1 
ATOM   540  N  N     . LYS A 1 90  ? 49.703 -14.008 6.733   1.00 18.90 ?  70  LYS A N     1 
ATOM   541  C  CA    . LYS A 1 90  ? 49.092 -13.123 5.743   1.00 27.44 ?  70  LYS A CA    1 
ATOM   542  C  C     . LYS A 1 90  ? 49.300 -13.670 4.331   1.00 25.94 ?  70  LYS A C     1 
ATOM   543  O  O     . LYS A 1 90  ? 48.352 -13.780 3.546   1.00 25.28 ?  70  LYS A O     1 
ATOM   544  C  CB    . LYS A 1 90  ? 49.665 -11.706 5.882   1.00 27.05 ?  70  LYS A CB    1 
ATOM   545  C  CG    . LYS A 1 90  ? 49.176 -10.711 4.850   1.00 20.43 ?  70  LYS A CG    1 
ATOM   546  C  CD    . LYS A 1 90  ? 50.295 -10.314 3.944   1.00 26.32 ?  70  LYS A CD    1 
ATOM   547  C  CE    . LYS A 1 90  ? 49.789 -9.522  2.731   1.00 29.35 ?  70  LYS A CE    1 
ATOM   548  N  NZ    . LYS A 1 90  ? 50.949 -8.902  1.997   1.00 39.53 ?  70  LYS A NZ    1 
ATOM   549  N  N     . LEU A 1 91  ? 50.529 -14.080 4.018   1.00 24.09 ?  71  LEU A N     1 
ATOM   550  C  CA    . LEU A 1 91  ? 50.817 -14.728 2.747   1.00 25.90 ?  71  LEU A CA    1 
ATOM   551  C  C     . LEU A 1 91  ? 50.112 -16.062 2.566   1.00 22.12 ?  71  LEU A C     1 
ATOM   552  O  O     . LEU A 1 91  ? 50.150 -16.615 1.466   1.00 30.75 ?  71  LEU A O     1 
ATOM   553  C  CB    . LEU A 1 91  ? 52.325 -14.927 2.598   1.00 34.41 ?  71  LEU A CB    1 
ATOM   554  C  CG    . LEU A 1 91  ? 53.144 -13.666 2.887   1.00 33.88 ?  71  LEU A CG    1 
ATOM   555  C  CD1   . LEU A 1 91  ? 54.614 -14.000 2.898   1.00 33.55 ?  71  LEU A CD1   1 
ATOM   556  C  CD2   . LEU A 1 91  ? 52.845 -12.596 1.858   1.00 34.95 ?  71  LEU A CD2   1 
ATOM   557  N  N     . GLY A 1 92  ? 49.486 -16.606 3.592   1.00 28.72 ?  72  GLY A N     1 
ATOM   558  C  CA    . GLY A 1 92  ? 48.774 -17.858 3.453   1.00 23.75 ?  72  GLY A CA    1 
ATOM   559  C  C     . GLY A 1 92  ? 49.476 -19.072 4.006   1.00 22.35 ?  72  GLY A C     1 
ATOM   560  O  O     . GLY A 1 92  ? 48.909 -20.160 3.932   1.00 31.89 ?  72  GLY A O     1 
ATOM   561  N  N     . ILE A 1 93  ? 50.687 -18.925 4.551   1.00 23.79 ?  73  ILE A N     1 
ATOM   562  C  CA    . ILE A 1 93  ? 51.422 -20.037 5.153   1.00 20.50 ?  73  ILE A CA    1 
ATOM   563  C  C     . ILE A 1 93  ? 51.125 -20.111 6.644   1.00 31.42 ?  73  ILE A C     1 
ATOM   564  O  O     . ILE A 1 93  ? 51.302 -19.122 7.377   1.00 25.93 ?  73  ILE A O     1 
ATOM   565  C  CB    . ILE A 1 93  ? 52.935 -19.883 4.941   1.00 26.11 ?  73  ILE A CB    1 
ATOM   566  C  CG1   . ILE A 1 93  ? 53.310 -20.132 3.479   1.00 29.77 ?  73  ILE A CG1   1 
ATOM   567  C  CG2   . ILE A 1 93  ? 53.707 -20.827 5.896   1.00 21.13 ?  73  ILE A CG2   1 
ATOM   568  C  CD1   . ILE A 1 93  ? 54.471 -19.288 3.020   1.00 27.72 ?  73  ILE A CD1   1 
ATOM   569  N  N     . GLN A 1 94  ? 50.730 -21.292 7.108   1.00 31.97 ?  74  GLN A N     1 
ATOM   570  C  CA    . GLN A 1 94  ? 50.648 -21.529 8.549   1.00 22.11 ?  74  GLN A CA    1 
ATOM   571  C  C     . GLN A 1 94  ? 52.034 -21.473 9.189   1.00 21.65 ?  74  GLN A C     1 
ATOM   572  O  O     . GLN A 1 94  ? 52.842 -22.379 8.956   1.00 22.58 ?  74  GLN A O     1 
ATOM   573  C  CB    . GLN A 1 94  ? 49.985 -22.865 8.796   1.00 18.27 ?  74  GLN A CB    1 
ATOM   574  C  CG    . GLN A 1 94  ? 48.488 -22.774 8.768   1.00 23.03 ?  74  GLN A CG    1 
ATOM   575  C  CD    . GLN A 1 94  ? 47.929 -21.904 9.909   1.00 32.10 ?  74  GLN A CD    1 
ATOM   576  O  OE1   . GLN A 1 94  ? 48.580 -21.709 10.947  1.00 28.53 ?  74  GLN A OE1   1 
ATOM   577  N  NE2   . GLN A 1 94  ? 46.709 -21.391 9.717   1.00 25.72 ?  74  GLN A NE2   1 
ATOM   578  N  N     . PRO A 1 95  ? 52.348 -20.457 10.009  1.00 25.33 ?  75  PRO A N     1 
ATOM   579  C  CA    . PRO A 1 95  ? 53.757 -20.262 10.432  1.00 22.70 ?  75  PRO A CA    1 
ATOM   580  C  C     . PRO A 1 95  ? 54.315 -21.356 11.334  1.00 22.77 ?  75  PRO A C     1 
ATOM   581  O  O     . PRO A 1 95  ? 55.516 -21.643 11.243  1.00 25.27 ?  75  PRO A O     1 
ATOM   582  C  CB    . PRO A 1 95  ? 53.738 -18.895 11.146  1.00 17.70 ?  75  PRO A CB    1 
ATOM   583  C  CG    . PRO A 1 95  ? 52.316 -18.668 11.530  1.00 18.35 ?  75  PRO A CG    1 
ATOM   584  C  CD    . PRO A 1 95  ? 51.443 -19.417 10.542  1.00 21.94 ?  75  PRO A CD    1 
ATOM   585  N  N     . VAL A 1 96  ? 53.507 -21.955 12.217  1.00 20.54 ?  76  VAL A N     1 
ATOM   586  C  CA    . VAL A 1 96  ? 54.024 -23.035 13.061  1.00 30.15 ?  76  VAL A CA    1 
ATOM   587  C  C     . VAL A 1 96  ? 54.206 -24.313 12.255  1.00 29.37 ?  76  VAL A C     1 
ATOM   588  O  O     . VAL A 1 96  ? 55.140 -25.087 12.512  1.00 28.31 ?  76  VAL A O     1 
ATOM   589  C  CB    . VAL A 1 96  ? 53.130 -23.280 14.299  1.00 33.53 ?  76  VAL A CB    1 
ATOM   590  C  CG1   . VAL A 1 96  ? 53.834 -24.187 15.266  1.00 36.11 ?  76  VAL A CG1   1 
ATOM   591  C  CG2   . VAL A 1 96  ? 52.817 -21.974 15.017  1.00 23.41 ?  76  VAL A CG2   1 
ATOM   592  N  N     . SER A 1 97  ? 53.344 -24.547 11.261  1.00 28.51 ?  77  SER A N     1 
ATOM   593  C  CA    . SER A 1 97  ? 53.540 -25.680 10.360  1.00 23.07 ?  77  SER A CA    1 
ATOM   594  C  C     . SER A 1 97  ? 54.857 -25.587 9.596   1.00 26.78 ?  77  SER A C     1 
ATOM   595  O  O     . SER A 1 97  ? 55.414 -26.619 9.207   1.00 38.47 ?  77  SER A O     1 
ATOM   596  C  CB    . SER A 1 97  ? 52.372 -25.791 9.381   1.00 28.52 ?  77  SER A CB    1 
ATOM   597  O  OG    . SER A 1 97  ? 51.142 -26.062 10.045  1.00 39.77 ?  77  SER A OG    1 
ATOM   598  N  N     . ALA A 1 98  ? 55.375 -24.381 9.361   1.00 24.17 ?  78  ALA A N     1 
ATOM   599  C  CA    . ALA A 1 98  ? 56.625 -24.239 8.627   1.00 25.63 ?  78  ALA A CA    1 
ATOM   600  C  C     . ALA A 1 98  ? 57.839 -24.155 9.535   1.00 31.31 ?  78  ALA A C     1 
ATOM   601  O  O     . ALA A 1 98  ? 58.897 -24.695 9.200   1.00 42.42 ?  78  ALA A O     1 
ATOM   602  C  CB    . ALA A 1 98  ? 56.591 -23.005 7.724   1.00 26.23 ?  78  ALA A CB    1 
ATOM   603  N  N     . VAL A 1 99  ? 57.735 -23.466 10.662  1.00 27.52 ?  79  VAL A N     1 
ATOM   604  C  CA    . VAL A 1 99  ? 58.822 -23.483 11.628  1.00 25.82 ?  79  VAL A CA    1 
ATOM   605  C  C     . VAL A 1 99  ? 58.357 -24.319 12.813  1.00 28.44 ?  79  VAL A C     1 
ATOM   606  O  O     . VAL A 1 99  ? 57.847 -23.790 13.809  1.00 31.56 ?  79  VAL A O     1 
ATOM   607  C  CB    . VAL A 1 99  ? 59.218 -22.058 12.032  1.00 27.42 ?  79  VAL A CB    1 
ATOM   608  C  CG1   . VAL A 1 99  ? 60.352 -22.099 13.050  1.00 33.30 ?  79  VAL A CG1   1 
ATOM   609  C  CG2   . VAL A 1 99  ? 59.597 -21.262 10.797  1.00 21.72 ?  79  VAL A CG2   1 
ATOM   610  N  N     . SER A 1 100 ? 58.505 -25.640 12.690  1.00 27.16 ?  80  SER A N     1 
ATOM   611  C  CA    . SER A 1 100 ? 57.927 -26.561 13.664  1.00 35.90 ?  80  SER A CA    1 
ATOM   612  C  C     . SER A 1 100 ? 58.396 -26.272 15.095  1.00 37.77 ?  80  SER A C     1 
ATOM   613  O  O     . SER A 1 100 ? 57.626 -26.458 16.045  1.00 31.46 ?  80  SER A O     1 
ATOM   614  C  CB    . SER A 1 100 ? 58.258 -28.000 13.269  1.00 33.02 ?  80  SER A CB    1 
ATOM   615  O  OG    . SER A 1 100 ? 59.560 -28.360 13.705  1.00 43.54 ?  80  SER A OG    1 
ATOM   616  N  N     . ASP A 1 101 ? 59.638 -25.804 15.267  1.00 33.61 ?  81  ASP A N     1 
ATOM   617  C  CA    . ASP A 1 101 ? 60.172 -25.490 16.589  1.00 33.44 ?  81  ASP A CA    1 
ATOM   618  C  C     . ASP A 1 101 ? 59.480 -24.312 17.267  1.00 30.11 ?  81  ASP A C     1 
ATOM   619  O  O     . ASP A 1 101 ? 59.771 -24.051 18.435  1.00 32.60 ?  81  ASP A O     1 
ATOM   620  C  CB    . ASP A 1 101 ? 61.666 -25.189 16.498  1.00 32.65 ?  81  ASP A CB    1 
ATOM   621  C  CG    . ASP A 1 101 ? 62.495 -26.436 16.330  1.00 43.82 ?  81  ASP A CG    1 
ATOM   622  O  OD1   . ASP A 1 101 ? 61.952 -27.534 16.583  1.00 45.78 ?  81  ASP A OD1   1 
ATOM   623  O  OD2   . ASP A 1 101 ? 63.681 -26.322 15.938  1.00 43.21 ?  81  ASP A OD2   1 
ATOM   624  N  N     . LEU A 1 102 ? 58.603 -23.586 16.572  1.00 25.87 ?  82  LEU A N     1 
ATOM   625  C  CA    . LEU A 1 102 ? 57.857 -22.515 17.222  1.00 28.84 ?  82  LEU A CA    1 
ATOM   626  C  C     . LEU A 1 102 ? 56.922 -23.044 18.303  1.00 30.70 ?  82  LEU A C     1 
ATOM   627  O  O     . LEU A 1 102 ? 56.599 -22.325 19.256  1.00 32.01 ?  82  LEU A O     1 
ATOM   628  C  CB    . LEU A 1 102 ? 57.044 -21.743 16.192  1.00 24.34 ?  82  LEU A CB    1 
ATOM   629  C  CG    . LEU A 1 102 ? 57.690 -20.485 15.659  1.00 21.42 ?  82  LEU A CG    1 
ATOM   630  C  CD1   . LEU A 1 102 ? 56.779 -19.876 14.623  1.00 21.75 ?  82  LEU A CD1   1 
ATOM   631  C  CD2   . LEU A 1 102 ? 57.937 -19.519 16.777  1.00 22.31 ?  82  LEU A CD2   1 
ATOM   632  N  N     . GLU A 1 103 ? 56.479 -24.290 18.174  1.00 29.73 ?  83  GLU A N     1 
ATOM   633  C  CA    . GLU A 1 103 ? 55.367 -24.759 18.984  1.00 31.45 ?  83  GLU A CA    1 
ATOM   634  C  C     . GLU A 1 103 ? 55.753 -24.901 20.448  1.00 32.77 ?  83  GLU A C     1 
ATOM   635  O  O     . GLU A 1 103 ? 54.931 -24.627 21.325  1.00 34.29 ?  83  GLU A O     1 
ATOM   636  C  CB    . GLU A 1 103 ? 54.848 -26.081 18.435  1.00 33.42 ?  83  GLU A CB    1 
ATOM   637  C  CG    . GLU A 1 103 ? 53.365 -26.274 18.641  1.00 47.61 ?  83  GLU A CG    1 
ATOM   638  C  CD    . GLU A 1 103 ? 52.886 -27.619 18.135  1.00 59.35 ?  83  GLU A CD    1 
ATOM   639  O  OE1   . GLU A 1 103 ? 53.075 -28.614 18.867  1.00 59.48 ?  83  GLU A OE1   1 
ATOM   640  O  OE2   . GLU A 1 103 ? 52.325 -27.675 17.011  1.00 59.20 ?  83  GLU A OE2   1 
ATOM   641  N  N     . VAL A 1 104 ? 56.980 -25.345 20.737  1.00 27.43 ?  84  VAL A N     1 
ATOM   642  C  CA    . VAL A 1 104 ? 57.377 -25.427 22.139  1.00 34.02 ?  84  VAL A CA    1 
ATOM   643  C  C     . VAL A 1 104 ? 57.783 -24.056 22.651  1.00 29.34 ?  84  VAL A C     1 
ATOM   644  O  O     . VAL A 1 104 ? 57.575 -23.751 23.836  1.00 26.82 ?  84  VAL A O     1 
ATOM   645  C  CB    . VAL A 1 104 ? 58.493 -26.471 22.374  1.00 33.27 ?  84  VAL A CB    1 
ATOM   646  C  CG1   . VAL A 1 104 ? 58.124 -27.791 21.741  1.00 35.29 ?  84  VAL A CG1   1 
ATOM   647  C  CG2   . VAL A 1 104 ? 59.852 -25.981 21.897  1.00 33.38 ?  84  VAL A CG2   1 
ATOM   648  N  N     . PHE A 1 105 ? 58.354 -23.221 21.774  1.00 26.36 ?  85  PHE A N     1 
ATOM   649  C  CA    . PHE A 1 105 ? 58.668 -21.840 22.124  1.00 24.24 ?  85  PHE A CA    1 
ATOM   650  C  C     . PHE A 1 105 ? 57.410 -21.098 22.555  1.00 25.44 ?  85  PHE A C     1 
ATOM   651  O  O     . PHE A 1 105 ? 57.406 -20.386 23.565  1.00 24.72 ?  85  PHE A O     1 
ATOM   652  C  CB    . PHE A 1 105 ? 59.322 -21.152 20.923  1.00 25.41 ?  85  PHE A CB    1 
ATOM   653  C  CG    . PHE A 1 105 ? 60.145 -19.939 21.270  1.00 26.32 ?  85  PHE A CG    1 
ATOM   654  C  CD1   . PHE A 1 105 ? 59.540 -18.718 21.540  1.00 24.96 ?  85  PHE A CD1   1 
ATOM   655  C  CD2   . PHE A 1 105 ? 61.531 -20.008 21.295  1.00 23.97 ?  85  PHE A CD2   1 
ATOM   656  C  CE1   . PHE A 1 105 ? 60.310 -17.604 21.851  1.00 21.66 ?  85  PHE A CE1   1 
ATOM   657  C  CE2   . PHE A 1 105 ? 62.299 -18.897 21.610  1.00 20.62 ?  85  PHE A CE2   1 
ATOM   658  C  CZ    . PHE A 1 105 ? 61.689 -17.698 21.878  1.00 22.66 ?  85  PHE A CZ    1 
ATOM   659  N  N     . LEU A 1 106 ? 56.320 -21.264 21.801  1.00 29.89 ?  86  LEU A N     1 
ATOM   660  C  CA    . LEU A 1 106 ? 55.071 -20.601 22.164  1.00 28.53 ?  86  LEU A CA    1 
ATOM   661  C  C     . LEU A 1 106 ? 54.447 -21.252 23.390  1.00 28.47 ?  86  LEU A C     1 
ATOM   662  O  O     . LEU A 1 106 ? 53.872 -20.559 24.236  1.00 26.50 ?  86  LEU A O     1 
ATOM   663  C  CB    . LEU A 1 106 ? 54.097 -20.618 20.985  1.00 18.82 ?  86  LEU A CB    1 
ATOM   664  C  CG    . LEU A 1 106 ? 54.556 -19.819 19.768  1.00 18.68 ?  86  LEU A CG    1 
ATOM   665  C  CD1   . LEU A 1 106 ? 53.676 -20.148 18.554  1.00 16.50 ?  86  LEU A CD1   1 
ATOM   666  C  CD2   . LEU A 1 106 ? 54.559 -18.334 20.074  1.00 13.49 ?  86  LEU A CD2   1 
ATOM   667  N  N     . GLU A 1 107 ? 54.550 -22.582 23.491  1.00 24.98 ?  87  GLU A N     1 
ATOM   668  C  CA    . GLU A 1 107 ? 54.157 -23.301 24.696  1.00 26.13 ?  87  GLU A CA    1 
ATOM   669  C  C     . GLU A 1 107 ? 54.778 -22.665 25.933  1.00 28.56 ?  87  GLU A C     1 
ATOM   670  O  O     . GLU A 1 107 ? 54.076 -22.324 26.893  1.00 28.33 ?  87  GLU A O     1 
ATOM   671  C  CB    . GLU A 1 107 ? 54.582 -24.766 24.575  1.00 32.96 ?  87  GLU A CB    1 
ATOM   672  C  CG    . GLU A 1 107 ? 53.741 -25.771 25.368  1.00 54.34 ?  87  GLU A CG    1 
ATOM   673  C  CD    . GLU A 1 107 ? 54.398 -27.169 25.475  1.00 77.18 ?  87  GLU A CD    1 
ATOM   674  O  OE1   . GLU A 1 107 ? 55.652 -27.250 25.472  1.00 72.10 ?  87  GLU A OE1   1 
ATOM   675  O  OE2   . GLU A 1 107 ? 53.661 -28.186 25.562  1.00 75.88 ?  87  GLU A OE2   1 
ATOM   676  N  N     . THR A 1 108 ? 56.100 -22.475 25.910  1.00 26.19 ?  88  THR A N     1 
ATOM   677  C  CA    . THR A 1 108 ? 56.807 -21.927 27.061  1.00 19.47 ?  88  THR A CA    1 
ATOM   678  C  C     . THR A 1 108 ? 56.407 -20.478 27.334  1.00 23.25 ?  88  THR A C     1 
ATOM   679  O  O     . THR A 1 108 ? 56.271 -20.081 28.493  1.00 31.18 ?  88  THR A O     1 
ATOM   680  C  CB    . THR A 1 108 ? 58.314 -22.057 26.841  1.00 21.74 ?  88  THR A CB    1 
ATOM   681  O  OG1   . THR A 1 108 ? 58.688 -23.426 26.975  1.00 21.98 ?  88  THR A OG1   1 
ATOM   682  C  CG2   . THR A 1 108 ? 59.092 -21.244 27.850  1.00 22.76 ?  88  THR A CG2   1 
ATOM   683  N  N     . LEU A 1 109 ? 56.192 -19.680 26.288  1.00 25.52 ?  89  LEU A N     1 
ATOM   684  C  CA    . LEU A 1 109 ? 55.687 -18.319 26.476  1.00 28.85 ?  89  LEU A CA    1 
ATOM   685  C  C     . LEU A 1 109 ? 54.306 -18.318 27.126  1.00 25.06 ?  89  LEU A C     1 
ATOM   686  O  O     . LEU A 1 109 ? 54.020 -17.507 28.019  1.00 20.70 ?  89  LEU A O     1 
ATOM   687  C  CB    . LEU A 1 109 ? 55.616 -17.599 25.126  1.00 23.11 ?  89  LEU A CB    1 
ATOM   688  C  CG    . LEU A 1 109 ? 56.893 -17.051 24.506  1.00 25.67 ?  89  LEU A CG    1 
ATOM   689  C  CD1   . LEU A 1 109 ? 56.524 -16.304 23.237  1.00 28.30 ?  89  LEU A CD1   1 
ATOM   690  C  CD2   . LEU A 1 109 ? 57.659 -16.150 25.472  1.00 26.57 ?  89  LEU A CD2   1 
ATOM   691  N  N     . SER A 1 110 ? 53.434 -19.209 26.662  1.00 22.89 ?  90  SER A N     1 
ATOM   692  C  CA    . SER A 1 110 ? 52.073 -19.285 27.168  1.00 27.27 ?  90  SER A CA    1 
ATOM   693  C  C     . SER A 1 110 ? 52.023 -19.695 28.638  1.00 29.16 ?  90  SER A C     1 
ATOM   694  O  O     . SER A 1 110 ? 51.075 -19.327 29.348  1.00 27.40 ?  90  SER A O     1 
ATOM   695  C  CB    . SER A 1 110 ? 51.271 -20.271 26.324  1.00 26.12 ?  90  SER A CB    1 
ATOM   696  O  OG    . SER A 1 110 ? 49.901 -19.935 26.332  1.00 31.94 ?  90  SER A OG    1 
ATOM   697  N  N     . GLU A 1 111 ? 53.009 -20.473 29.100  1.00 23.60 ?  91  GLU A N     1 
ATOM   698  C  CA    . GLU A 1 111 ? 53.043 -20.885 30.501  1.00 28.20 ?  91  GLU A CA    1 
ATOM   699  C  C     . GLU A 1 111 ? 53.392 -19.716 31.412  1.00 20.93 ?  91  GLU A C     1 
ATOM   700  O  O     . GLU A 1 111 ? 52.862 -19.601 32.516  1.00 25.37 ?  91  GLU A O     1 
ATOM   701  C  CB    . GLU A 1 111 ? 54.074 -21.989 30.702  1.00 28.50 ?  91  GLU A CB    1 
ATOM   702  C  CG    . GLU A 1 111 ? 53.743 -23.307 30.101  1.00 28.65 ?  91  GLU A CG    1 
ATOM   703  C  CD    . GLU A 1 111 ? 54.934 -24.252 30.160  1.00 45.23 ?  91  GLU A CD    1 
ATOM   704  O  OE1   . GLU A 1 111 ? 55.968 -23.888 30.787  1.00 35.68 ?  91  GLU A OE1   1 
ATOM   705  O  OE2   . GLU A 1 111 ? 54.844 -25.342 29.551  1.00 59.96 ?  91  GLU A OE2   1 
ATOM   706  N  N     . ILE A 1 112 ? 54.311 -18.863 30.971  1.00 18.89 ?  92  ILE A N     1 
ATOM   707  C  CA    . ILE A 1 112 ? 54.746 -17.732 31.774  1.00 19.92 ?  92  ILE A CA    1 
ATOM   708  C  C     . ILE A 1 112 ? 53.684 -16.646 31.796  1.00 27.81 ?  92  ILE A C     1 
ATOM   709  O  O     . ILE A 1 112 ? 53.468 -15.994 32.824  1.00 35.67 ?  92  ILE A O     1 
ATOM   710  C  CB    . ILE A 1 112 ? 56.083 -17.204 31.230  1.00 19.82 ?  92  ILE A CB    1 
ATOM   711  C  CG1   . ILE A 1 112 ? 57.173 -18.259 31.443  1.00 19.56 ?  92  ILE A CG1   1 
ATOM   712  C  CG2   . ILE A 1 112 ? 56.417 -15.842 31.820  1.00 19.53 ?  92  ILE A CG2   1 
ATOM   713  C  CD1   . ILE A 1 112 ? 58.467 -17.967 30.760  1.00 25.63 ?  92  ILE A CD1   1 
ATOM   714  N  N     . THR A 1 113 ? 53.018 -16.419 30.660  1.00 27.46 ?  93  THR A N     1 
ATOM   715  C  CA    . THR A 1 113 ? 52.033 -15.357 30.534  1.00 19.40 ?  93  THR A CA    1 
ATOM   716  C  C     . THR A 1 113 ? 50.643 -15.790 30.981  1.00 24.54 ?  93  THR A C     1 
ATOM   717  O  O     . THR A 1 113 ? 49.791 -14.932 31.222  1.00 29.45 ?  93  THR A O     1 
ATOM   718  C  CB    . THR A 1 113 ? 51.939 -14.885 29.073  1.00 26.29 ?  93  THR A CB    1 
ATOM   719  O  OG1   . THR A 1 113 ? 51.618 -15.997 28.231  1.00 22.84 ?  93  THR A OG1   1 
ATOM   720  C  CG2   . THR A 1 113 ? 53.254 -14.265 28.571  1.00 24.91 ?  93  THR A CG2   1 
ATOM   721  N  N     . ASN A 1 114 ? 50.375 -17.092 31.050  1.00 23.61 ?  94  ASN A N     1 
ATOM   722  C  CA    . ASN A 1 114 ? 49.007 -17.606 31.182  1.00 26.47 ?  94  ASN A CA    1 
ATOM   723  C  C     . ASN A 1 114 ? 48.021 -16.903 30.226  1.00 27.21 ?  94  ASN A C     1 
ATOM   724  O  O     . ASN A 1 114 ? 46.856 -16.675 30.554  1.00 29.44 ?  94  ASN A O     1 
ATOM   725  C  CB    . ASN A 1 114 ? 48.545 -17.533 32.646  1.00 27.84 ?  94  ASN A CB    1 
ATOM   726  C  CG    . ASN A 1 114 ? 47.379 -18.503 32.954  1.00 43.35 ?  94  ASN A CG    1 
ATOM   727  O  OD1   . ASN A 1 114 ? 47.219 -19.526 32.275  1.00 38.02 ?  94  ASN A OD1   1 
ATOM   728  N  ND2   . ASN A 1 114 ? 46.594 -18.203 34.006  1.00 35.22 ?  94  ASN A ND2   1 
ATOM   729  N  N     . MET A 1 115 ? 48.491 -16.564 29.020  1.00 25.65 ?  95  MET A N     1 
ATOM   730  C  CA    . MET A 1 115 ? 47.651 -16.094 27.920  1.00 20.20 ?  95  MET A CA    1 
ATOM   731  C  C     . MET A 1 115 ? 47.911 -16.926 26.656  1.00 25.15 ?  95  MET A C     1 
ATOM   732  O  O     . MET A 1 115 ? 48.828 -17.750 26.595  1.00 24.10 ?  95  MET A O     1 
ATOM   733  C  CB    . MET A 1 115 ? 47.847 -14.588 27.632  1.00 15.58 ?  95  MET A CB    1 
ATOM   734  C  CG    . MET A 1 115 ? 48.007 -13.670 28.855  1.00 20.64 ?  95  MET A CG    1 
ATOM   735  S  SD    . MET A 1 115 ? 48.092 -11.883 28.499  1.00 22.32 ?  95  MET A SD    1 
ATOM   736  C  CE    . MET A 1 115 ? 46.712 -11.595 27.384  1.00 20.60 ?  95  MET A CE    1 
ATOM   737  N  N     . VAL A 1 116 ? 47.076 -16.714 25.643  1.00 20.02 ?  96  VAL A N     1 
ATOM   738  C  CA    . VAL A 1 116 ? 47.145 -17.436 24.375  1.00 18.35 ?  96  VAL A CA    1 
ATOM   739  C  C     . VAL A 1 116 ? 48.506 -17.194 23.733  1.00 18.79 ?  96  VAL A C     1 
ATOM   740  O  O     . VAL A 1 116 ? 49.101 -16.131 23.939  1.00 17.96 ?  96  VAL A O     1 
ATOM   741  C  CB    . VAL A 1 116 ? 46.014 -16.988 23.439  1.00 24.11 ?  96  VAL A CB    1 
ATOM   742  C  CG1   . VAL A 1 116 ? 44.643 -17.569 23.876  1.00 15.73 ?  96  VAL A CG1   1 
ATOM   743  C  CG2   . VAL A 1 116 ? 45.992 -15.454 23.347  1.00 17.85 ?  96  VAL A CG2   1 
ATOM   744  N  N     . PRO A 1 117 ? 49.046 -18.157 22.945  1.00 25.27 ?  97  PRO A N     1 
ATOM   745  C  CA    . PRO A 1 117 ? 50.349 -18.004 22.282  1.00 24.93 ?  97  PRO A CA    1 
ATOM   746  C  C     . PRO A 1 117 ? 50.296 -17.166 21.000  1.00 24.84 ?  97  PRO A C     1 
ATOM   747  O  O     . PRO A 1 117 ? 50.782 -17.577 19.946  1.00 22.00 ?  97  PRO A O     1 
ATOM   748  C  CB    . PRO A 1 117 ? 50.737 -19.452 21.974  1.00 20.84 ?  97  PRO A CB    1 
ATOM   749  C  CG    . PRO A 1 117 ? 49.426 -20.087 21.660  1.00 21.32 ?  97  PRO A CG    1 
ATOM   750  C  CD    . PRO A 1 117 ? 48.435 -19.461 22.636  1.00 25.10 ?  97  PRO A CD    1 
ATOM   751  N  N     . ARG A 1 118 ? 49.734 -15.970 21.110  1.00 25.87 ?  98  ARG A N     1 
ATOM   752  C  CA    . ARG A 1 118 ? 49.289 -15.160 19.990  1.00 21.98 ?  98  ARG A CA    1 
ATOM   753  C  C     . ARG A 1 118 ? 49.103 -13.730 20.494  1.00 24.79 ?  98  ARG A C     1 
ATOM   754  O  O     . ARG A 1 118 ? 48.802 -13.508 21.669  1.00 25.21 ?  98  ARG A O     1 
ATOM   755  C  CB    . ARG A 1 118 ? 47.975 -15.713 19.421  1.00 24.78 ?  98  ARG A CB    1 
ATOM   756  C  CG    . ARG A 1 118 ? 47.482 -14.979 18.180  1.00 24.38 ?  98  ARG A CG    1 
ATOM   757  C  CD    . ARG A 1 118 ? 48.256 -15.468 17.017  1.00 26.35 ?  98  ARG A CD    1 
ATOM   758  N  NE    . ARG A 1 118 ? 48.221 -14.555 15.885  1.00 30.81 ?  98  ARG A NE    1 
ATOM   759  C  CZ    . ARG A 1 118 ? 47.253 -14.515 14.982  1.00 24.40 ?  98  ARG A CZ    1 
ATOM   760  N  NH1   . ARG A 1 118 ? 46.178 -15.281 15.084  1.00 16.55 ?  98  ARG A NH1   1 
ATOM   761  N  NH2   . ARG A 1 118 ? 47.373 -13.690 13.946  1.00 29.28 ?  98  ARG A NH2   1 
ATOM   762  N  N     . GLU A 1 119 ? 49.278 -12.763 19.609  1.00 23.65 ?  99  GLU A N     1 
ATOM   763  C  CA    . GLU A 1 119 ? 49.107 -11.384 20.028  1.00 26.15 ?  99  GLU A CA    1 
ATOM   764  C  C     . GLU A 1 119 ? 47.633 -10.991 19.975  1.00 27.41 ?  99  GLU A C     1 
ATOM   765  O  O     . GLU A 1 119 ? 46.858 -11.493 19.157  1.00 24.44 ?  99  GLU A O     1 
ATOM   766  C  CB    . GLU A 1 119 ? 49.953 -10.449 19.157  1.00 27.90 ?  99  GLU A CB    1 
ATOM   767  C  CG    . GLU A 1 119 ? 49.316 -10.040 17.846  1.00 27.93 ?  99  GLU A CG    1 
ATOM   768  C  CD    . GLU A 1 119 ? 49.507 -11.066 16.747  1.00 33.33 ?  99  GLU A CD    1 
ATOM   769  O  OE1   . GLU A 1 119 ? 49.586 -12.286 17.056  1.00 30.72 ?  99  GLU A OE1   1 
ATOM   770  O  OE2   . GLU A 1 119 ? 49.579 -10.640 15.566  1.00 33.57 ?  99  GLU A OE2   1 
ATOM   771  N  N     . THR A 1 120 ? 47.242 -10.113 20.886  1.00 22.13 ?  100 THR A N     1 
ATOM   772  C  CA    . THR A 1 120 ? 45.897 -9.573  20.913  1.00 20.95 ?  100 THR A CA    1 
ATOM   773  C  C     . THR A 1 120 ? 45.993 -8.070  20.750  1.00 19.77 ?  100 THR A C     1 
ATOM   774  O  O     . THR A 1 120 ? 47.074 -7.519  20.565  1.00 20.98 ?  100 THR A O     1 
ATOM   775  C  CB    . THR A 1 120 ? 45.150 -9.930  22.209  1.00 22.02 ?  100 THR A CB    1 
ATOM   776  O  OG1   . THR A 1 120 ? 45.783 -9.308  23.340  1.00 27.10 ?  100 THR A OG1   1 
ATOM   777  C  CG2   . THR A 1 120 ? 45.059 -11.440 22.410  1.00 22.24 ?  100 THR A CG2   1 
ATOM   778  N  N     . SER A 1 121 ? 44.842 -7.406  20.824  1.00 20.51 ?  101 SER A N     1 
ATOM   779  C  CA    . SER A 1 121 ? 44.839 -5.954  20.777  1.00 19.90 ?  101 SER A CA    1 
ATOM   780  C  C     . SER A 1 121 ? 45.543 -5.331  21.976  1.00 21.13 ?  101 SER A C     1 
ATOM   781  O  O     . SER A 1 121 ? 45.919 -4.156  21.906  1.00 21.94 ?  101 SER A O     1 
ATOM   782  C  CB    . SER A 1 121 ? 43.403 -5.448  20.667  1.00 21.88 ?  101 SER A CB    1 
ATOM   783  O  OG    . SER A 1 121 ? 42.917 -5.675  19.353  1.00 26.30 ?  101 SER A OG    1 
ATOM   784  N  N     . TYR A 1 122 ? 45.750 -6.086  23.064  1.00 20.72 ?  102 TYR A N     1 
ATOM   785  C  CA    . TYR A 1 122 ? 46.558 -5.578  24.176  1.00 21.09 ?  102 TYR A CA    1 
ATOM   786  C  C     . TYR A 1 122 ? 48.004 -5.369  23.750  1.00 24.54 ?  102 TYR A C     1 
ATOM   787  O  O     . TYR A 1 122 ? 48.618 -4.345  24.088  1.00 26.98 ?  102 TYR A O     1 
ATOM   788  C  CB    . TYR A 1 122 ? 46.502 -6.534  25.373  1.00 20.94 ?  102 TYR A CB    1 
ATOM   789  C  CG    . TYR A 1 122 ? 45.399 -6.208  26.347  1.00 22.19 ?  102 TYR A CG    1 
ATOM   790  C  CD1   . TYR A 1 122 ? 44.108 -6.687  26.135  1.00 18.70 ?  102 TYR A CD1   1 
ATOM   791  C  CD2   . TYR A 1 122 ? 45.637 -5.401  27.467  1.00 18.17 ?  102 TYR A CD2   1 
ATOM   792  C  CE1   . TYR A 1 122 ? 43.082 -6.377  26.997  1.00 19.03 ?  102 TYR A CE1   1 
ATOM   793  C  CE2   . TYR A 1 122 ? 44.620 -5.096  28.336  1.00 21.41 ?  102 TYR A CE2   1 
ATOM   794  C  CZ    . TYR A 1 122 ? 43.335 -5.588  28.097  1.00 23.38 ?  102 TYR A CZ    1 
ATOM   795  O  OH    . TYR A 1 122 ? 42.294 -5.309  28.960  1.00 27.07 ?  102 TYR A OH    1 
ATOM   796  N  N     . HIS A 1 123 ? 48.577 -6.357  23.045  1.00 18.01 ?  103 HIS A N     1 
ATOM   797  C  CA    . HIS A 1 123 ? 49.945 -6.245  22.548  1.00 20.91 ?  103 HIS A CA    1 
ATOM   798  C  C     . HIS A 1 123 ? 50.026 -5.264  21.386  1.00 21.23 ?  103 HIS A C     1 
ATOM   799  O  O     . HIS A 1 123 ? 51.072 -4.640  21.157  1.00 19.29 ?  103 HIS A O     1 
ATOM   800  C  CB    . HIS A 1 123 ? 50.468 -7.615  22.089  1.00 19.35 ?  103 HIS A CB    1 
ATOM   801  C  CG    . HIS A 1 123 ? 50.227 -8.740  23.054  1.00 18.19 ?  103 HIS A CG    1 
ATOM   802  N  ND1   . HIS A 1 123 ? 49.003 -9.356  23.195  1.00 17.81 ?  103 HIS A ND1   1 
ATOM   803  C  CD2   . HIS A 1 123 ? 51.071 -9.395  23.884  1.00 20.08 ?  103 HIS A CD2   1 
ATOM   804  C  CE1   . HIS A 1 123 ? 49.097 -10.328 24.081  1.00 18.92 ?  103 HIS A CE1   1 
ATOM   805  N  NE2   . HIS A 1 123 ? 50.342 -10.370 24.519  1.00 22.36 ?  103 HIS A NE2   1 
ATOM   806  N  N     . TYR A 1 124 ? 48.935 -5.136  20.636  1.00 25.57 ?  104 TYR A N     1 
ATOM   807  C  CA    . TYR A 1 124 ? 48.908 -4.320  19.432  1.00 20.09 ?  104 TYR A CA    1 
ATOM   808  C  C     . TYR A 1 124 ? 48.743 -2.849  19.761  1.00 24.41 ?  104 TYR A C     1 
ATOM   809  O  O     . TYR A 1 124 ? 49.190 -1.995  18.987  1.00 22.87 ?  104 TYR A O     1 
ATOM   810  C  CB    . TYR A 1 124 ? 47.776 -4.794  18.521  1.00 22.08 ?  104 TYR A CB    1 
ATOM   811  C  CG    . TYR A 1 124 ? 47.828 -4.265  17.093  1.00 28.45 ?  104 TYR A CG    1 
ATOM   812  C  CD1   . TYR A 1 124 ? 49.043 -4.114  16.420  1.00 21.92 ?  104 TYR A CD1   1 
ATOM   813  C  CD2   . TYR A 1 124 ? 46.654 -3.935  16.423  1.00 17.71 ?  104 TYR A CD2   1 
ATOM   814  C  CE1   . TYR A 1 124 ? 49.076 -3.634  15.126  1.00 24.44 ?  104 TYR A CE1   1 
ATOM   815  C  CE2   . TYR A 1 124 ? 46.676 -3.464  15.162  1.00 22.97 ?  104 TYR A CE2   1 
ATOM   816  C  CZ    . TYR A 1 124 ? 47.883 -3.311  14.496  1.00 27.72 ?  104 TYR A CZ    1 
ATOM   817  O  OH    . TYR A 1 124 ? 47.868 -2.824  13.199  1.00 24.04 ?  104 TYR A OH    1 
ATOM   818  N  N     . GLY A 1 125 ? 48.131 -2.541  20.912  1.00 25.55 ?  105 GLY A N     1 
ATOM   819  C  CA    . GLY A 1 125 ? 47.828 -1.184  21.292  1.00 21.22 ?  105 GLY A CA    1 
ATOM   820  C  C     . GLY A 1 125 ? 48.623 -0.728  22.494  1.00 25.58 ?  105 GLY A C     1 
ATOM   821  O  O     . GLY A 1 125 ? 49.733 -0.203  22.359  1.00 31.02 ?  105 GLY A O     1 
ATOM   822  N  N     . PRO A 1 126 ? 48.073 -0.933  23.699  1.00 22.66 ?  106 PRO A N     1 
ATOM   823  C  CA    . PRO A 1 126 ? 48.724 -0.408  24.920  1.00 19.60 ?  106 PRO A CA    1 
ATOM   824  C  C     . PRO A 1 126 ? 50.118 -0.951  25.188  1.00 23.43 ?  106 PRO A C     1 
ATOM   825  O  O     . PRO A 1 126 ? 50.955 -0.217  25.718  1.00 28.49 ?  106 PRO A O     1 
ATOM   826  C  CB    . PRO A 1 126 ? 47.751 -0.808  26.037  1.00 23.68 ?  106 PRO A CB    1 
ATOM   827  C  CG    . PRO A 1 126 ? 46.901 -1.915  25.445  1.00 27.53 ?  106 PRO A CG    1 
ATOM   828  C  CD    . PRO A 1 126 ? 46.793 -1.598  23.987  1.00 24.47 ?  106 PRO A CD    1 
ATOM   829  N  N     . TRP A 1 127 ? 50.402 -2.210  24.862  1.00 24.39 ?  107 TRP A N     1 
ATOM   830  C  CA    . TRP A 1 127 ? 51.751 -2.742  25.027  1.00 22.48 ?  107 TRP A CA    1 
ATOM   831  C  C     . TRP A 1 127 ? 52.654 -2.448  23.831  1.00 25.98 ?  107 TRP A C     1 
ATOM   832  O  O     . TRP A 1 127 ? 53.848 -2.762  23.877  1.00 26.72 ?  107 TRP A O     1 
ATOM   833  C  CB    . TRP A 1 127 ? 51.680 -4.249  25.297  1.00 18.49 ?  107 TRP A CB    1 
ATOM   834  C  CG    . TRP A 1 127 ? 50.814 -4.564  26.515  1.00 33.06 ?  107 TRP A CG    1 
ATOM   835  C  CD1   . TRP A 1 127 ? 50.336 -3.662  27.438  1.00 25.48 ?  107 TRP A CD1   1 
ATOM   836  C  CD2   . TRP A 1 127 ? 50.330 -5.857  26.938  1.00 25.67 ?  107 TRP A CD2   1 
ATOM   837  N  NE1   . TRP A 1 127 ? 49.585 -4.314  28.385  1.00 27.92 ?  107 TRP A NE1   1 
ATOM   838  C  CE2   . TRP A 1 127 ? 49.567 -5.656  28.107  1.00 23.34 ?  107 TRP A CE2   1 
ATOM   839  C  CE3   . TRP A 1 127 ? 50.467 -7.157  26.439  1.00 27.44 ?  107 TRP A CE3   1 
ATOM   840  C  CZ2   . TRP A 1 127 ? 48.951 -6.707  28.793  1.00 19.99 ?  107 TRP A CZ2   1 
ATOM   841  C  CZ3   . TRP A 1 127 ? 49.846 -8.203  27.118  1.00 23.80 ?  107 TRP A CZ3   1 
ATOM   842  C  CH2   . TRP A 1 127 ? 49.098 -7.967  28.283  1.00 24.18 ?  107 TRP A CH2   1 
ATOM   843  N  N     . ASN A 1 128 ? 52.107 -1.871  22.767  1.00 21.11 ?  108 ASN A N     1 
ATOM   844  C  CA    . ASN A 1 128 ? 52.889 -1.446  21.617  1.00 22.97 ?  108 ASN A CA    1 
ATOM   845  C  C     . ASN A 1 128 ? 53.503 -0.083  21.918  1.00 24.41 ?  108 ASN A C     1 
ATOM   846  O  O     . ASN A 1 128 ? 52.764 0.852   22.230  1.00 24.37 ?  108 ASN A O     1 
ATOM   847  C  CB    . ASN A 1 128 ? 51.971 -1.369  20.402  1.00 23.62 ?  108 ASN A CB    1 
ATOM   848  C  CG    . ASN A 1 128 ? 52.701 -1.408  19.086  1.00 21.77 ?  108 ASN A CG    1 
ATOM   849  O  OD1   . ASN A 1 128 ? 53.930 -1.386  19.016  1.00 23.21 ?  108 ASN A OD1   1 
ATOM   850  N  ND2   . ASN A 1 128 ? 51.930 -1.465  18.016  1.00 22.07 ?  108 ASN A ND2   1 
ATOM   851  N  N     . PRO A 1 129 ? 54.829 0.074   21.852  1.00 26.37 ?  109 PRO A N     1 
ATOM   852  C  CA    . PRO A 1 129 ? 55.431 1.384   22.164  1.00 22.83 ?  109 PRO A CA    1 
ATOM   853  C  C     . PRO A 1 129 ? 54.948 2.491   21.231  1.00 26.33 ?  109 PRO A C     1 
ATOM   854  O  O     . PRO A 1 129 ? 54.638 2.270   20.059  1.00 26.76 ?  109 PRO A O     1 
ATOM   855  C  CB    . PRO A 1 129 ? 56.938 1.139   21.994  1.00 23.27 ?  109 PRO A CB    1 
ATOM   856  C  CG    . PRO A 1 129 ? 57.038 -0.106  21.143  1.00 22.75 ?  109 PRO A CG    1 
ATOM   857  C  CD    . PRO A 1 129 ? 55.836 -0.931  21.466  1.00 20.43 ?  109 PRO A CD    1 
ATOM   858  N  N     . ILE A 1 130 ? 54.867 3.687   21.778  1.00 32.37 ?  110 ILE A N     1 
ATOM   859  C  CA    . ILE A 1 130 ? 54.580 4.893   21.013  1.00 33.18 ?  110 ILE A CA    1 
ATOM   860  C  C     . ILE A 1 130 ? 55.851 5.345   20.293  1.00 33.90 ?  110 ILE A C     1 
ATOM   861  O  O     . ILE A 1 130 ? 56.972 5.131   20.773  1.00 35.69 ?  110 ILE A O     1 
ATOM   862  C  CB    . ILE A 1 130 ? 54.026 5.970   21.974  1.00 36.07 ?  110 ILE A CB    1 
ATOM   863  C  CG1   . ILE A 1 130 ? 52.529 5.755   22.224  1.00 38.36 ?  110 ILE A CG1   1 
ATOM   864  C  CG2   . ILE A 1 130 ? 54.263 7.369   21.470  1.00 36.14 ?  110 ILE A CG2   1 
ATOM   865  C  CD1   . ILE A 1 130 ? 52.091 6.127   23.643  1.00 49.29 ?  110 ILE A CD1   1 
ATOM   866  N  N     . GLY A 1 131 ? 55.695 5.937   19.111  1.00 28.87 ?  111 GLY A N     1 
ATOM   867  C  CA    . GLY A 1 131 ? 56.828 6.574   18.460  1.00 28.33 ?  111 GLY A CA    1 
ATOM   868  C  C     . GLY A 1 131 ? 57.658 5.718   17.515  1.00 35.21 ?  111 GLY A C     1 
ATOM   869  O  O     . GLY A 1 131 ? 57.122 4.895   16.763  1.00 28.85 ?  111 GLY A O     1 
ATOM   870  N  N     . GLU A 1 132 ? 58.983 5.907   17.553  1.00 29.94 ?  112 GLU A N     1 
ATOM   871  C  CA    . GLU A 1 132 ? 59.865 5.263   16.582  1.00 29.81 ?  112 GLU A CA    1 
ATOM   872  C  C     . GLU A 1 132 ? 59.895 3.742   16.729  1.00 31.35 ?  112 GLU A C     1 
ATOM   873  O  O     . GLU A 1 132 ? 60.111 3.034   15.739  1.00 32.05 ?  112 GLU A O     1 
ATOM   874  C  CB    . GLU A 1 132 ? 61.285 5.837   16.680  1.00 32.49 ?  112 GLU A CB    1 
ATOM   875  C  CG    . GLU A 1 132 ? 61.848 6.069   18.102  1.00 49.55 ?  112 GLU A CG    1 
ATOM   876  C  CD    . GLU A 1 132 ? 61.364 7.381   18.771  1.00 59.16 ?  112 GLU A CD    1 
ATOM   877  O  OE1   . GLU A 1 132 ? 60.152 7.532   19.059  1.00 48.06 ?  112 GLU A OE1   1 
ATOM   878  O  OE2   . GLU A 1 132 ? 62.211 8.275   19.003  1.00 62.79 ?  112 GLU A OE2   1 
ATOM   879  N  N     . ARG A 1 133 ? 59.681 3.215   17.930  1.00 30.33 ?  113 ARG A N     1 
ATOM   880  C  CA    . ARG A 1 133 ? 59.721 1.772   18.122  1.00 29.71 ?  113 ARG A CA    1 
ATOM   881  C  C     . ARG A 1 133 ? 58.387 1.090   17.831  1.00 28.77 ?  113 ARG A C     1 
ATOM   882  O  O     . ARG A 1 133 ? 58.313 -0.141  17.914  1.00 24.45 ?  113 ARG A O     1 
ATOM   883  C  CB    . ARG A 1 133 ? 60.179 1.435   19.546  1.00 25.01 ?  113 ARG A CB    1 
ATOM   884  C  CG    . ARG A 1 133 ? 61.645 1.734   19.817  1.00 21.78 ?  113 ARG A CG    1 
ATOM   885  C  CD    . ARG A 1 133 ? 62.059 1.350   21.222  1.00 23.95 ?  113 ARG A CD    1 
ATOM   886  N  NE    . ARG A 1 133 ? 62.001 -0.091  21.444  1.00 37.78 ?  113 ARG A NE    1 
ATOM   887  C  CZ    . ARG A 1 133 ? 61.091 -0.698  22.193  1.00 26.17 ?  113 ARG A CZ    1 
ATOM   888  N  NH1   . ARG A 1 133 ? 60.142 -0.016  22.812  1.00 24.37 ?  113 ARG A NH1   1 
ATOM   889  N  NH2   . ARG A 1 133 ? 61.125 -2.019  22.307  1.00 23.07 ?  113 ARG A NH2   1 
ATOM   890  N  N     . GLU A 1 134 ? 57.355 1.848   17.461  1.00 22.24 ?  114 GLU A N     1 
ATOM   891  C  CA    . GLU A 1 134 ? 56.029 1.271   17.294  1.00 25.55 ?  114 GLU A CA    1 
ATOM   892  C  C     . GLU A 1 134 ? 56.065 0.123   16.294  1.00 27.00 ?  114 GLU A C     1 
ATOM   893  O  O     . GLU A 1 134 ? 56.643 0.245   15.211  1.00 26.37 ?  114 GLU A O     1 
ATOM   894  C  CB    . GLU A 1 134 ? 55.035 2.345   16.845  1.00 21.54 ?  114 GLU A CB    1 
ATOM   895  C  CG    . GLU A 1 134 ? 53.592 1.916   16.935  1.00 22.38 ?  114 GLU A CG    1 
ATOM   896  C  CD    . GLU A 1 134 ? 52.608 3.055   16.687  1.00 30.73 ?  114 GLU A CD    1 
ATOM   897  O  OE1   . GLU A 1 134 ? 52.268 3.778   17.641  1.00 30.80 ?  114 GLU A OE1   1 
ATOM   898  O  OE2   . GLU A 1 134 ? 52.155 3.227   15.536  1.00 38.65 ?  114 GLU A OE2   1 
ATOM   899  N  N     . ARG A 1 135 ? 55.463 -1.005  16.671  1.00 27.88 ?  115 ARG A N     1 
ATOM   900  C  CA    . ARG A 1 135 ? 55.404 -2.172  15.796  1.00 23.18 ?  115 ARG A CA    1 
ATOM   901  C  C     . ARG A 1 135 ? 54.196 -2.056  14.872  1.00 24.16 ?  115 ARG A C     1 
ATOM   902  O  O     . ARG A 1 135 ? 53.055 -1.961  15.335  1.00 27.40 ?  115 ARG A O     1 
ATOM   903  C  CB    . ARG A 1 135 ? 55.322 -3.458  16.616  1.00 23.17 ?  115 ARG A CB    1 
ATOM   904  C  CG    . ARG A 1 135 ? 56.666 -3.950  17.093  1.00 24.74 ?  115 ARG A CG    1 
ATOM   905  C  CD    . ARG A 1 135 ? 57.016 -3.401  18.453  1.00 19.31 ?  115 ARG A CD    1 
ATOM   906  N  NE    . ARG A 1 135 ? 58.139 -4.139  18.993  1.00 22.08 ?  115 ARG A NE    1 
ATOM   907  C  CZ    . ARG A 1 135 ? 59.386 -3.706  18.969  1.00 21.78 ?  115 ARG A CZ    1 
ATOM   908  N  NH1   . ARG A 1 135 ? 59.689 -2.514  18.492  1.00 19.74 ?  115 ARG A NH1   1 
ATOM   909  N  NH2   . ARG A 1 135 ? 60.353 -4.491  19.434  1.00 22.29 ?  115 ARG A NH2   1 
ATOM   910  N  N     . ARG A 1 136 ? 54.446 -2.076  13.567  1.00 24.71 ?  116 ARG A N     1 
ATOM   911  C  CA    . ARG A 1 136 ? 53.403 -1.932  12.571  1.00 21.03 ?  116 ARG A CA    1 
ATOM   912  C  C     . ARG A 1 136 ? 53.630 -2.968  11.492  1.00 23.75 ?  116 ARG A C     1 
ATOM   913  O  O     . ARG A 1 136 ? 54.769 -3.339  11.211  1.00 23.65 ?  116 ARG A O     1 
ATOM   914  C  CB    . ARG A 1 136 ? 53.397 -0.527  11.972  1.00 27.93 ?  116 ARG A CB    1 
ATOM   915  C  CG    . ARG A 1 136 ? 52.944 0.528   12.957  1.00 27.01 ?  116 ARG A CG    1 
ATOM   916  C  CD    . ARG A 1 136 ? 52.466 1.776   12.283  1.00 29.45 ?  116 ARG A CD    1 
ATOM   917  N  NE    . ARG A 1 136 ? 53.064 2.927   12.945  1.00 44.75 ?  116 ARG A NE    1 
ATOM   918  C  CZ    . ARG A 1 136 ? 53.684 3.916   12.318  1.00 51.95 ?  116 ARG A CZ    1 
ATOM   919  N  NH1   . ARG A 1 136 ? 53.780 3.945   10.996  1.00 52.73 ?  116 ARG A NH1   1 
ATOM   920  N  NH2   . ARG A 1 136 ? 54.228 4.897   13.034  1.00 53.48 ?  116 ARG A NH2   1 
ATOM   921  N  N     . PHE A 1 137 ? 52.523 -3.450  10.915  1.00 23.53 ?  117 PHE A N     1 
ATOM   922  C  CA    . PHE A 1 137 ? 52.570 -4.425  9.830   1.00 22.53 ?  117 PHE A CA    1 
ATOM   923  C  C     . PHE A 1 137 ? 52.969 -3.773  8.501   1.00 32.75 ?  117 PHE A C     1 
ATOM   924  O  O     . PHE A 1 137 ? 53.652 -4.397  7.674   1.00 28.88 ?  117 PHE A O     1 
ATOM   925  C  CB    . PHE A 1 137 ? 51.200 -5.112  9.673   1.00 23.34 ?  117 PHE A CB    1 
ATOM   926  C  CG    . PHE A 1 137 ? 50.827 -6.053  10.793  1.00 21.53 ?  117 PHE A CG    1 
ATOM   927  C  CD1   . PHE A 1 137 ? 51.498 -7.260  10.973  1.00 23.07 ?  117 PHE A CD1   1 
ATOM   928  C  CD2   . PHE A 1 137 ? 49.773 -5.755  11.637  1.00 25.17 ?  117 PHE A CD2   1 
ATOM   929  C  CE1   . PHE A 1 137 ? 51.148 -8.129  11.995  1.00 22.07 ?  117 PHE A CE1   1 
ATOM   930  C  CE2   . PHE A 1 137 ? 49.414 -6.620  12.660  1.00 25.69 ?  117 PHE A CE2   1 
ATOM   931  C  CZ    . PHE A 1 137 ? 50.108 -7.809  12.839  1.00 23.27 ?  117 PHE A CZ    1 
ATOM   932  N  N     . THR A 1 138 ? 52.534 -2.529  8.269   1.00 29.36 ?  118 THR A N     1 
ATOM   933  C  CA    . THR A 1 138 ? 52.614 -1.895  6.958   1.00 27.56 ?  118 THR A CA    1 
ATOM   934  C  C     . THR A 1 138 ? 53.065 -0.453  7.105   1.00 30.67 ?  118 THR A C     1 
ATOM   935  O  O     . THR A 1 138 ? 53.097 0.104   8.210   1.00 28.87 ?  118 THR A O     1 
ATOM   936  C  CB    . THR A 1 138 ? 51.262 -1.900  6.225   1.00 29.46 ?  118 THR A CB    1 
ATOM   937  O  OG1   . THR A 1 138 ? 50.360 -0.987  6.874   1.00 29.99 ?  118 THR A OG1   1 
ATOM   938  C  CG2   . THR A 1 138 ? 50.645 -3.298  6.185   1.00 29.04 ?  118 THR A CG2   1 
ATOM   939  N  N     . HIS A 1 139 ? 53.371 0.165   5.957   1.00 31.65 ?  119 HIS A N     1 
ATOM   940  C  CA    A HIS A 1 139 ? 53.725 1.577   5.865   0.54 27.35 ?  119 HIS A CA    1 
ATOM   941  C  CA    B HIS A 1 139 ? 53.721 1.580   5.928   0.46 27.26 ?  119 HIS A CA    1 
ATOM   942  C  C     . HIS A 1 139 ? 52.515 2.489   5.711   1.00 26.51 ?  119 HIS A C     1 
ATOM   943  O  O     . HIS A 1 139 ? 52.670 3.710   5.768   1.00 29.34 ?  119 HIS A O     1 
ATOM   944  C  CB    A HIS A 1 139 ? 54.677 1.802   4.688   0.54 26.97 ?  119 HIS A CB    1 
ATOM   945  C  CB    B HIS A 1 139 ? 54.779 1.849   4.854   0.46 26.91 ?  119 HIS A CB    1 
ATOM   946  C  CG    A HIS A 1 139 ? 54.092 1.431   3.358   0.54 27.75 ?  119 HIS A CG    1 
ATOM   947  C  CG    B HIS A 1 139 ? 56.189 1.720   5.347   0.46 28.23 ?  119 HIS A CG    1 
ATOM   948  N  ND1   A HIS A 1 139 ? 53.881 0.125   2.976   0.54 30.63 ?  119 HIS A ND1   1 
ATOM   949  N  ND1   B HIS A 1 139 ? 56.615 2.272   6.536   0.46 25.33 ?  119 HIS A ND1   1 
ATOM   950  C  CD2   A HIS A 1 139 ? 53.678 2.197   2.322   0.54 25.49 ?  119 HIS A CD2   1 
ATOM   951  C  CD2   B HIS A 1 139 ? 57.270 1.104   4.809   0.46 27.13 ?  119 HIS A CD2   1 
ATOM   952  C  CE1   A HIS A 1 139 ? 53.361 0.103   1.762   0.54 29.22 ?  119 HIS A CE1   1 
ATOM   953  C  CE1   B HIS A 1 139 ? 57.897 2.001   6.709   0.46 25.09 ?  119 HIS A CE1   1 
ATOM   954  N  NE2   A HIS A 1 139 ? 53.228 1.346   1.343   0.54 22.49 ?  119 HIS A NE2   1 
ATOM   955  N  NE2   B HIS A 1 139 ? 58.317 1.292   5.678   0.46 22.24 ?  119 HIS A NE2   1 
ATOM   956  N  N     . PHE A 1 140 ? 51.320 1.930   5.506   1.00 27.43 ?  120 PHE A N     1 
ATOM   957  C  CA    . PHE A 1 140 ? 50.110 2.742   5.344   1.00 25.30 ?  120 PHE A CA    1 
ATOM   958  C  C     . PHE A 1 140 ? 49.776 3.494   6.633   1.00 35.40 ?  120 PHE A C     1 
ATOM   959  O  O     . PHE A 1 140 ? 49.733 2.886   7.718   1.00 34.70 ?  120 PHE A O     1 
ATOM   960  C  CB    . PHE A 1 140 ? 48.923 1.868   4.940   1.00 24.37 ?  120 PHE A CB    1 
ATOM   961  C  CG    . PHE A 1 140 ? 49.119 1.140   3.649   1.00 33.56 ?  120 PHE A CG    1 
ATOM   962  C  CD1   . PHE A 1 140 ? 48.772 1.741   2.437   1.00 35.34 ?  120 PHE A CD1   1 
ATOM   963  C  CD2   . PHE A 1 140 ? 49.663 -0.143  3.633   1.00 28.34 ?  120 PHE A CD2   1 
ATOM   964  C  CE1   . PHE A 1 140 ? 48.955 1.077   1.237   1.00 28.08 ?  120 PHE A CE1   1 
ATOM   965  C  CE2   . PHE A 1 140 ? 49.852 -0.813  2.440   1.00 28.19 ?  120 PHE A CE2   1 
ATOM   966  C  CZ    . PHE A 1 140 ? 49.495 -0.205  1.237   1.00 30.27 ?  120 PHE A CZ    1 
ATOM   967  N  N     . PRO A 1 141 ? 49.507 4.802   6.561   1.00 35.37 ?  121 PRO A N     1 
ATOM   968  C  CA    . PRO A 1 141 ? 49.123 5.536   7.772   1.00 27.66 ?  121 PRO A CA    1 
ATOM   969  C  C     . PRO A 1 141 ? 47.793 5.103   8.314   1.00 25.78 ?  121 PRO A C     1 
ATOM   970  O  O     . PRO A 1 141 ? 47.508 5.383   9.481   1.00 28.04 ?  121 PRO A O     1 
ATOM   971  C  CB    . PRO A 1 141 ? 49.067 6.997   7.306   1.00 28.37 ?  121 PRO A CB    1 
ATOM   972  C  CG    . PRO A 1 141 ? 49.581 6.992   5.886   1.00 32.55 ?  121 PRO A CG    1 
ATOM   973  C  CD    . PRO A 1 141 ? 49.375 5.632   5.354   1.00 28.76 ?  121 PRO A CD    1 
ATOM   974  N  N     . ASP A 1 142 ? 46.962 4.443   7.506   1.00 22.51 ?  122 ASP A N     1 
ATOM   975  C  CA    . ASP A 1 142 ? 45.678 3.965   8.008   1.00 31.96 ?  122 ASP A CA    1 
ATOM   976  C  C     . ASP A 1 142 ? 45.844 2.975   9.150   1.00 31.20 ?  122 ASP A C     1 
ATOM   977  O  O     . ASP A 1 142 ? 44.947 2.850   9.990   1.00 26.44 ?  122 ASP A O     1 
ATOM   978  C  CB    . ASP A 1 142 ? 44.884 3.324   6.878   1.00 23.94 ?  122 ASP A CB    1 
ATOM   979  C  CG    . ASP A 1 142 ? 44.862 4.178   5.649   1.00 29.20 ?  122 ASP A CG    1 
ATOM   980  O  OD1   . ASP A 1 142 ? 45.966 4.510   5.153   1.00 33.02 ?  122 ASP A OD1   1 
ATOM   981  O  OD2   . ASP A 1 142 ? 43.748 4.521   5.186   1.00 29.47 ?  122 ASP A OD2   1 
ATOM   982  N  N     . GLU A 1 143 ? 46.971 2.253   9.182   1.00 29.11 ?  123 GLU A N     1 
ATOM   983  C  CA    . GLU A 1 143 ? 47.214 1.307   10.262  1.00 31.57 ?  123 GLU A CA    1 
ATOM   984  C  C     . GLU A 1 143 ? 47.191 2.007   11.608  1.00 28.97 ?  123 GLU A C     1 
ATOM   985  O  O     . GLU A 1 143 ? 46.699 1.451   12.595  1.00 30.77 ?  123 GLU A O     1 
ATOM   986  C  CB    . GLU A 1 143 ? 48.558 0.605   10.066  1.00 31.85 ?  123 GLU A CB    1 
ATOM   987  C  CG    . GLU A 1 143 ? 48.871 -0.379  11.176  1.00 24.29 ?  123 GLU A CG    1 
ATOM   988  C  CD    . GLU A 1 143 ? 49.833 -1.447  10.737  1.00 29.71 ?  123 GLU A CD    1 
ATOM   989  O  OE1   . GLU A 1 143 ? 50.354 -1.341  9.613   1.00 29.72 ?  123 GLU A OE1   1 
ATOM   990  O  OE2   . GLU A 1 143 ? 50.060 -2.407  11.508  1.00 35.68 ?  123 GLU A OE2   1 
ATOM   991  N  N     . ARG A 1 144 ? 47.715 3.233   11.656  1.00 26.08 ?  124 ARG A N     1 
ATOM   992  C  CA    . ARG A 1 144 ? 47.751 3.993   12.893  1.00 26.79 ?  124 ARG A CA    1 
ATOM   993  C  C     . ARG A 1 144 ? 46.354 4.158   13.479  1.00 29.37 ?  124 ARG A C     1 
ATOM   994  O  O     . ARG A 1 144 ? 46.200 4.248   14.703  1.00 29.86 ?  124 ARG A O     1 
ATOM   995  C  CB    . ARG A 1 144 ? 48.407 5.345   12.635  1.00 29.02 ?  124 ARG A CB    1 
ATOM   996  C  CG    . ARG A 1 144 ? 49.800 5.501   13.245  1.00 37.94 ?  124 ARG A CG    1 
ATOM   997  C  CD    . ARG A 1 144 ? 50.234 6.961   13.206  1.00 56.24 ?  124 ARG A CD    1 
ATOM   998  N  NE    . ARG A 1 144 ? 49.668 7.715   14.326  1.00 68.81 ?  124 ARG A NE    1 
ATOM   999  C  CZ    . ARG A 1 144 ? 49.847 9.013   14.540  1.00 62.89 ?  124 ARG A CZ    1 
ATOM   1000 N  NH1   . ARG A 1 144 ? 50.558 9.761   13.711  1.00 66.22 ?  124 ARG A NH1   1 
ATOM   1001 N  NH2   . ARG A 1 144 ? 49.290 9.576   15.611  1.00 62.53 ?  124 ARG A NH2   1 
ATOM   1002 N  N     . GLY A 1 145 ? 45.324 4.147   12.629  1.00 23.23 ?  125 GLY A N     1 
ATOM   1003 C  CA    . GLY A 1 145 ? 43.965 4.318   13.110  1.00 24.02 ?  125 GLY A CA    1 
ATOM   1004 C  C     . GLY A 1 145 ? 43.453 3.165   13.954  1.00 30.72 ?  125 GLY A C     1 
ATOM   1005 O  O     . GLY A 1 145 ? 42.572 3.359   14.801  1.00 29.88 ?  125 GLY A O     1 
ATOM   1006 N  N     . LEU A 1 146 ? 43.978 1.956   13.738  1.00 28.63 ?  126 LEU A N     1 
ATOM   1007 C  CA    . LEU A 1 146 ? 43.604 0.833   14.598  1.00 31.18 ?  126 LEU A CA    1 
ATOM   1008 C  C     . LEU A 1 146 ? 44.442 0.799   15.875  1.00 26.59 ?  126 LEU A C     1 
ATOM   1009 O  O     . LEU A 1 146 ? 43.923 0.495   16.958  1.00 23.72 ?  126 LEU A O     1 
ATOM   1010 C  CB    . LEU A 1 146 ? 43.752 -0.492  13.844  1.00 27.03 ?  126 LEU A CB    1 
ATOM   1011 C  CG    . LEU A 1 146 ? 43.259 -0.636  12.403  1.00 26.26 ?  126 LEU A CG    1 
ATOM   1012 C  CD1   . LEU A 1 146 ? 44.001 -1.782  11.754  1.00 25.59 ?  126 LEU A CD1   1 
ATOM   1013 C  CD2   . LEU A 1 146 ? 41.751 -0.877  12.311  1.00 25.30 ?  126 LEU A CD2   1 
ATOM   1014 N  N     . ILE A 1 147 ? 45.740 1.078   15.760  1.00 24.95 ?  127 ILE A N     1 
ATOM   1015 C  CA    . ILE A 1 147 ? 46.622 1.007   16.918  1.00 24.89 ?  127 ILE A CA    1 
ATOM   1016 C  C     . ILE A 1 147 ? 46.261 2.095   17.927  1.00 32.52 ?  127 ILE A C     1 
ATOM   1017 O  O     . ILE A 1 147 ? 46.127 1.833   19.129  1.00 30.36 ?  127 ILE A O     1 
ATOM   1018 C  CB    . ILE A 1 147 ? 48.092 1.101   16.474  1.00 26.21 ?  127 ILE A CB    1 
ATOM   1019 C  CG1   . ILE A 1 147 ? 48.487 -0.183  15.745  1.00 23.61 ?  127 ILE A CG1   1 
ATOM   1020 C  CG2   . ILE A 1 147 ? 49.008 1.364   17.674  1.00 19.76 ?  127 ILE A CG2   1 
ATOM   1021 C  CD1   . ILE A 1 147 ? 49.773 -0.101  14.968  1.00 22.28 ?  127 ILE A CD1   1 
ATOM   1022 N  N     . GLU A 1 148 ? 46.081 3.331   17.455  1.00 29.49 ?  128 GLU A N     1 
ATOM   1023 C  CA    . GLU A 1 148 ? 45.662 4.377   18.371  1.00 25.01 ?  128 GLU A CA    1 
ATOM   1024 C  C     . GLU A 1 148 ? 44.277 4.089   18.907  1.00 27.41 ?  128 GLU A C     1 
ATOM   1025 O  O     . GLU A 1 148 ? 43.962 4.461   20.041  1.00 37.41 ?  128 GLU A O     1 
ATOM   1026 C  CB    . GLU A 1 148 ? 45.679 5.747   17.688  1.00 38.59 ?  128 GLU A CB    1 
ATOM   1027 C  CG    . GLU A 1 148 ? 47.033 6.222   17.149  1.00 36.93 ?  128 GLU A CG    1 
ATOM   1028 C  CD    . GLU A 1 148 ? 48.085 6.409   18.231  1.00 50.27 ?  128 GLU A CD    1 
ATOM   1029 O  OE1   . GLU A 1 148 ? 47.736 6.375   19.435  1.00 53.64 ?  128 GLU A OE1   1 
ATOM   1030 O  OE2   . GLU A 1 148 ? 49.270 6.614   17.876  1.00 59.34 ?  128 GLU A OE2   1 
ATOM   1031 N  N     . GLY A 1 149 ? 43.441 3.418   18.117  1.00 26.35 ?  129 GLY A N     1 
ATOM   1032 C  CA    . GLY A 1 149 ? 42.074 3.165   18.549  1.00 21.06 ?  129 GLY A CA    1 
ATOM   1033 C  C     . GLY A 1 149 ? 42.008 2.260   19.766  1.00 27.70 ?  129 GLY A C     1 
ATOM   1034 O  O     . GLY A 1 149 ? 41.266 2.531   20.714  1.00 32.79 ?  129 GLY A O     1 
ATOM   1035 N  N     . VAL A 1 150 ? 42.783 1.179   19.768  1.00 23.10 ?  130 VAL A N     1 
ATOM   1036 C  CA    . VAL A 1 150 ? 42.726 0.284   20.917  1.00 26.85 ?  130 VAL A CA    1 
ATOM   1037 C  C     . VAL A 1 150 ? 43.674 0.752   22.015  1.00 24.73 ?  130 VAL A C     1 
ATOM   1038 O  O     . VAL A 1 150 ? 43.422 0.494   23.195  1.00 29.06 ?  130 VAL A O     1 
ATOM   1039 C  CB    . VAL A 1 150 ? 42.994 -1.195  20.533  1.00 24.22 ?  130 VAL A CB    1 
ATOM   1040 C  CG1   . VAL A 1 150 ? 41.846 -1.735  19.691  1.00 21.18 ?  130 VAL A CG1   1 
ATOM   1041 C  CG2   . VAL A 1 150 ? 44.351 -1.390  19.837  1.00 14.70 ?  130 VAL A CG2   1 
ATOM   1042 N  N     . ARG A 1 151 ? 44.749 1.454   21.655  1.00 24.87 ?  131 ARG A N     1 
ATOM   1043 C  CA    . ARG A 1 151 ? 45.650 1.978   22.671  1.00 24.81 ?  131 ARG A CA    1 
ATOM   1044 C  C     . ARG A 1 151 ? 44.962 3.022   23.549  1.00 28.79 ?  131 ARG A C     1 
ATOM   1045 O  O     . ARG A 1 151 ? 45.275 3.126   24.740  1.00 29.74 ?  131 ARG A O     1 
ATOM   1046 C  CB    . ARG A 1 151 ? 46.889 2.539   22.001  1.00 21.01 ?  131 ARG A CB    1 
ATOM   1047 C  CG    . ARG A 1 151 ? 47.866 3.225   22.898  1.00 21.80 ?  131 ARG A CG    1 
ATOM   1048 C  CD    . ARG A 1 151 ? 48.885 3.961   22.035  1.00 30.64 ?  131 ARG A CD    1 
ATOM   1049 N  NE    . ARG A 1 151 ? 49.918 3.070   21.511  1.00 30.64 ?  131 ARG A NE    1 
ATOM   1050 C  CZ    . ARG A 1 151 ? 50.633 3.297   20.418  1.00 25.88 ?  131 ARG A CZ    1 
ATOM   1051 N  NH1   . ARG A 1 151 ? 50.385 4.331   19.636  1.00 33.67 ?  131 ARG A NH1   1 
ATOM   1052 N  NH2   . ARG A 1 151 ? 51.629 2.468   20.108  1.00 22.67 ?  131 ARG A NH2   1 
ATOM   1053 N  N     . ILE A 1 152 ? 44.004 3.777   22.999  1.00 30.04 ?  132 ILE A N     1 
ATOM   1054 C  CA    . ILE A 1 152 ? 43.205 4.693   23.818  1.00 27.18 ?  132 ILE A CA    1 
ATOM   1055 C  C     . ILE A 1 152 ? 42.072 3.952   24.524  1.00 21.76 ?  132 ILE A C     1 
ATOM   1056 O  O     . ILE A 1 152 ? 41.828 4.152   25.720  1.00 28.63 ?  132 ILE A O     1 
ATOM   1057 C  CB    . ILE A 1 152 ? 42.658 5.855   22.962  1.00 32.96 ?  132 ILE A CB    1 
ATOM   1058 C  CG1   . ILE A 1 152 ? 43.778 6.746   22.440  1.00 26.58 ?  132 ILE A CG1   1 
ATOM   1059 C  CG2   . ILE A 1 152 ? 41.663 6.716   23.742  1.00 27.85 ?  132 ILE A CG2   1 
ATOM   1060 C  CD1   . ILE A 1 152 ? 43.427 7.355   21.099  1.00 27.01 ?  132 ILE A CD1   1 
ATOM   1061 N  N     . ALA A 1 153 ? 41.348 3.106   23.797  1.00 19.69 ?  133 ALA A N     1 
ATOM   1062 C  CA    . ALA A 1 153 ? 40.143 2.494   24.348  1.00 25.23 ?  133 ALA A CA    1 
ATOM   1063 C  C     . ALA A 1 153 ? 40.435 1.661   25.600  1.00 29.07 ?  133 ALA A C     1 
ATOM   1064 O  O     . ALA A 1 153 ? 39.679 1.715   26.574  1.00 26.03 ?  133 ALA A O     1 
ATOM   1065 C  CB    . ALA A 1 153 ? 39.460 1.632   23.285  1.00 21.29 ?  133 ALA A CB    1 
ATOM   1066 N  N     . ILE A 1 154 ? 41.523 0.894   25.601  1.00 29.96 ?  134 ILE A N     1 
ATOM   1067 C  CA    . ILE A 1 154 ? 41.675 -0.183  26.582  1.00 25.96 ?  134 ILE A CA    1 
ATOM   1068 C  C     . ILE A 1 154 ? 41.896 0.364   27.989  1.00 24.56 ?  134 ILE A C     1 
ATOM   1069 O  O     . ILE A 1 154 ? 41.173 -0.055  28.906  1.00 26.76 ?  134 ILE A O     1 
ATOM   1070 C  CB    . ILE A 1 154 ? 42.779 -1.177  26.171  1.00 26.83 ?  134 ILE A CB    1 
ATOM   1071 C  CG1   . ILE A 1 154 ? 42.308 -2.024  24.978  1.00 27.04 ?  134 ILE A CG1   1 
ATOM   1072 C  CG2   . ILE A 1 154 ? 43.195 -2.043  27.363  1.00 20.72 ?  134 ILE A CG2   1 
ATOM   1073 C  CD1   . ILE A 1 154 ? 43.411 -2.772  24.249  1.00 22.37 ?  134 ILE A CD1   1 
ATOM   1074 N  N     . PRO A 1 155 ? 42.855 1.265   28.234  1.00 27.29 ?  135 PRO A N     1 
ATOM   1075 C  CA    . PRO A 1 155 ? 42.993 1.805   29.609  1.00 22.53 ?  135 PRO A CA    1 
ATOM   1076 C  C     . PRO A 1 155 ? 41.712 2.367   30.213  1.00 24.17 ?  135 PRO A C     1 
ATOM   1077 O  O     . PRO A 1 155 ? 41.455 2.152   31.403  1.00 29.00 ?  135 PRO A O     1 
ATOM   1078 C  CB    . PRO A 1 155 ? 44.064 2.895   29.453  1.00 20.09 ?  135 PRO A CB    1 
ATOM   1079 C  CG    . PRO A 1 155 ? 44.553 2.803   28.010  1.00 28.79 ?  135 PRO A CG    1 
ATOM   1080 C  CD    . PRO A 1 155 ? 44.064 1.534   27.438  1.00 20.05 ?  135 PRO A CD    1 
ATOM   1081 N  N     . GLY A 1 156 ? 40.893 3.063   29.427  1.00 22.53 ?  136 GLY A N     1 
ATOM   1082 C  CA    . GLY A 1 156 ? 39.687 3.666   29.974  1.00 20.93 ?  136 GLY A CA    1 
ATOM   1083 C  C     . GLY A 1 156 ? 38.583 2.666   30.278  1.00 25.79 ?  136 GLY A C     1 
ATOM   1084 O  O     . GLY A 1 156 ? 37.839 2.824   31.253  1.00 25.82 ?  136 GLY A O     1 
ATOM   1085 N  N     . ILE A 1 157 ? 38.434 1.641   29.436  1.00 22.76 ?  137 ILE A N     1 
ATOM   1086 C  CA    . ILE A 1 157 ? 37.478 0.579   29.741  1.00 20.94 ?  137 ILE A CA    1 
ATOM   1087 C  C     . ILE A 1 157 ? 37.878 -0.135  31.024  1.00 25.76 ?  137 ILE A C     1 
ATOM   1088 O  O     . ILE A 1 157 ? 37.030 -0.494  31.850  1.00 21.94 ?  137 ILE A O     1 
ATOM   1089 C  CB    . ILE A 1 157 ? 37.381 -0.408  28.565  1.00 18.74 ?  137 ILE A CB    1 
ATOM   1090 C  CG1   . ILE A 1 157 ? 36.909 0.307   27.310  1.00 22.36 ?  137 ILE A CG1   1 
ATOM   1091 C  CG2   . ILE A 1 157 ? 36.454 -1.560  28.879  1.00 19.51 ?  137 ILE A CG2   1 
ATOM   1092 C  CD1   . ILE A 1 157 ? 37.188 -0.495  26.073  1.00 24.83 ?  137 ILE A CD1   1 
ATOM   1093 N  N     . GLU A 1 158 ? 39.178 -0.370  31.197  1.00 26.87 ?  138 GLU A N     1 
ATOM   1094 C  CA    . GLU A 1 158 ? 39.654 -1.092  32.364  1.00 25.31 ?  138 GLU A CA    1 
ATOM   1095 C  C     . GLU A 1 158 ? 39.338 -0.326  33.641  1.00 26.56 ?  138 GLU A C     1 
ATOM   1096 O  O     . GLU A 1 158 ? 38.843 -0.903  34.617  1.00 28.20 ?  138 GLU A O     1 
ATOM   1097 C  CB    . GLU A 1 158 ? 41.151 -1.363  32.217  1.00 25.23 ?  138 GLU A CB    1 
ATOM   1098 C  CG    . GLU A 1 158 ? 41.423 -2.680  31.476  1.00 27.84 ?  138 GLU A CG    1 
ATOM   1099 C  CD    . GLU A 1 158 ? 42.886 -3.088  31.494  1.00 36.10 ?  138 GLU A CD    1 
ATOM   1100 O  OE1   . GLU A 1 158 ? 43.732 -2.171  31.621  1.00 38.83 ?  138 GLU A OE1   1 
ATOM   1101 O  OE2   . GLU A 1 158 ? 43.186 -4.305  31.347  1.00 27.08 ?  138 GLU A OE2   1 
ATOM   1102 N  N     . LEU A 1 159 ? 39.574 0.985   33.636  1.00 29.85 ?  139 LEU A N     1 
ATOM   1103 C  CA    . LEU A 1 159 ? 39.166 1.810   34.761  1.00 25.60 ?  139 LEU A CA    1 
ATOM   1104 C  C     . LEU A 1 159 ? 37.658 1.773   34.949  1.00 25.73 ?  139 LEU A C     1 
ATOM   1105 O  O     . LEU A 1 159 ? 37.172 1.653   36.075  1.00 29.98 ?  139 LEU A O     1 
ATOM   1106 C  CB    . LEU A 1 159 ? 39.640 3.238   34.555  1.00 25.02 ?  139 LEU A CB    1 
ATOM   1107 C  CG    . LEU A 1 159 ? 41.105 3.441   34.882  1.00 26.38 ?  139 LEU A CG    1 
ATOM   1108 C  CD1   . LEU A 1 159 ? 41.664 4.500   33.943  1.00 30.33 ?  139 LEU A CD1   1 
ATOM   1109 C  CD2   . LEU A 1 159 ? 41.263 3.844   36.319  1.00 30.64 ?  139 LEU A CD2   1 
ATOM   1110 N  N     . ALA A 1 160 ? 36.895 1.866   33.864  1.00 22.47 ?  140 ALA A N     1 
ATOM   1111 C  CA    . ALA A 1 160 ? 35.453 1.772   34.024  1.00 23.46 ?  140 ALA A CA    1 
ATOM   1112 C  C     . ALA A 1 160 ? 35.051 0.429   34.598  1.00 25.85 ?  140 ALA A C     1 
ATOM   1113 O  O     . ALA A 1 160 ? 34.092 0.354   35.367  1.00 25.19 ?  140 ALA A O     1 
ATOM   1114 C  CB    . ALA A 1 160 ? 34.743 2.003   32.701  1.00 21.18 ?  140 ALA A CB    1 
ATOM   1115 N  N     . ILE A 1 161 ? 35.777 -0.633  34.241  1.00 31.16 ?  141 ILE A N     1 
ATOM   1116 C  CA    . ILE A 1 161 ? 35.445 -1.975  34.711  1.00 25.73 ?  141 ILE A CA    1 
ATOM   1117 C  C     . ILE A 1 161 ? 35.545 -2.034  36.226  1.00 29.65 ?  141 ILE A C     1 
ATOM   1118 O  O     . ILE A 1 161 ? 34.640 -2.532  36.907  1.00 29.78 ?  141 ILE A O     1 
ATOM   1119 C  CB    . ILE A 1 161 ? 36.359 -3.022  34.046  1.00 24.08 ?  141 ILE A CB    1 
ATOM   1120 C  CG1   . ILE A 1 161 ? 35.768 -3.457  32.708  1.00 25.52 ?  141 ILE A CG1   1 
ATOM   1121 C  CG2   . ILE A 1 161 ? 36.577 -4.237  34.970  1.00 20.71 ?  141 ILE A CG2   1 
ATOM   1122 C  CD1   . ILE A 1 161 ? 36.738 -4.193  31.819  1.00 25.51 ?  141 ILE A CD1   1 
ATOM   1123 N  N     . ARG A 1 162 ? 36.640 -1.500  36.775  1.00 25.48 ?  142 ARG A N     1 
ATOM   1124 C  CA    . ARG A 1 162 ? 36.830 -1.528  38.219  1.00 28.86 ?  142 ARG A CA    1 
ATOM   1125 C  C     . ARG A 1 162 ? 35.757 -0.712  38.925  1.00 29.17 ?  142 ARG A C     1 
ATOM   1126 O  O     . ARG A 1 162 ? 35.176 -1.167  39.912  1.00 35.96 ?  142 ARG A O     1 
ATOM   1127 C  CB    . ARG A 1 162 ? 38.237 -1.030  38.575  1.00 38.48 ?  142 ARG A CB    1 
ATOM   1128 C  CG    . ARG A 1 162 ? 39.384 -1.922  38.027  1.00 48.90 ?  142 ARG A CG    1 
ATOM   1129 C  CD    . ARG A 1 162 ? 38.877 -3.352  37.712  1.00 47.61 ?  142 ARG A CD    1 
ATOM   1130 N  NE    . ARG A 1 162 ? 39.878 -4.281  37.196  1.00 52.33 ?  142 ARG A NE    1 
ATOM   1131 C  CZ    . ARG A 1 162 ? 40.282 -5.373  37.837  1.00 57.40 ?  142 ARG A CZ    1 
ATOM   1132 N  NH1   . ARG A 1 162 ? 39.830 -5.675  39.046  1.00 58.19 ?  142 ARG A NH1   1 
ATOM   1133 N  NH2   . ARG A 1 162 ? 41.154 -6.189  37.247  1.00 44.37 ?  142 ARG A NH2   1 
ATOM   1134 N  N     . GLU A 1 163 ? 35.449 0.477   38.402  1.00 30.93 ?  143 GLU A N     1 
ATOM   1135 C  CA    . GLU A 1 163 ? 34.446 1.341   39.010  1.00 27.27 ?  143 GLU A CA    1 
ATOM   1136 C  C     . GLU A 1 163 ? 33.042 0.758   38.889  1.00 28.09 ?  143 GLU A C     1 
ATOM   1137 O  O     . GLU A 1 163 ? 32.231 0.887   39.815  1.00 32.46 ?  143 GLU A O     1 
ATOM   1138 C  CB    . GLU A 1 163 ? 34.518 2.725   38.377  1.00 23.29 ?  143 GLU A CB    1 
ATOM   1139 C  CG    . GLU A 1 163 ? 35.804 3.436   38.738  1.00 30.43 ?  143 GLU A CG    1 
ATOM   1140 C  CD    . GLU A 1 163 ? 36.058 4.723   37.947  1.00 41.33 ?  143 GLU A CD    1 
ATOM   1141 O  OE1   . GLU A 1 163 ? 36.083 4.694   36.684  1.00 31.83 ?  143 GLU A OE1   1 
ATOM   1142 O  OE2   . GLU A 1 163 ? 36.244 5.768   38.622  1.00 44.97 ?  143 GLU A OE2   1 
ATOM   1143 N  N     . ILE A 1 164 ? 32.724 0.121   37.763  1.00 25.85 ?  144 ILE A N     1 
ATOM   1144 C  CA    . ILE A 1 164 ? 31.382 -0.427  37.610  1.00 29.68 ?  144 ILE A CA    1 
ATOM   1145 C  C     . ILE A 1 164 ? 31.176 -1.612  38.541  1.00 41.14 ?  144 ILE A C     1 
ATOM   1146 O  O     . ILE A 1 164 ? 30.058 -1.857  39.021  1.00 39.00 ?  144 ILE A O     1 
ATOM   1147 C  CB    . ILE A 1 164 ? 31.120 -0.805  36.147  1.00 27.71 ?  144 ILE A CB    1 
ATOM   1148 C  CG1   . ILE A 1 164 ? 30.972 0.463   35.311  1.00 25.70 ?  144 ILE A CG1   1 
ATOM   1149 C  CG2   . ILE A 1 164 ? 29.879 -1.672  36.036  1.00 26.54 ?  144 ILE A CG2   1 
ATOM   1150 C  CD1   . ILE A 1 164 ? 30.689 0.215   33.840  1.00 28.66 ?  144 ILE A CD1   1 
ATOM   1151 N  N     . ASN A 1 165 ? 32.241 -2.354  38.832  1.00 40.70 ?  145 ASN A N     1 
ATOM   1152 C  CA    . ASN A 1 165 ? 32.112 -3.466  39.759  1.00 42.10 ?  145 ASN A CA    1 
ATOM   1153 C  C     . ASN A 1 165 ? 31.703 -2.999  41.158  1.00 36.65 ?  145 ASN A C     1 
ATOM   1154 O  O     . ASN A 1 165 ? 31.009 -3.733  41.871  1.00 37.11 ?  145 ASN A O     1 
ATOM   1155 C  CB    . ASN A 1 165 ? 33.422 -4.252  39.792  1.00 47.14 ?  145 ASN A CB    1 
ATOM   1156 C  CG    . ASN A 1 165 ? 33.245 -5.646  40.345  1.00 54.22 ?  145 ASN A CG    1 
ATOM   1157 O  OD1   . ASN A 1 165 ? 32.209 -6.289  40.150  1.00 54.57 ?  145 ASN A OD1   1 
ATOM   1158 N  ND2   . ASN A 1 165 ? 34.251 -6.115  41.068  1.00 55.33 ?  145 ASN A ND2   1 
ATOM   1159 N  N     . GLN A 1 166 ? 32.093 -1.778  41.554  1.00 30.49 ?  146 GLN A N     1 
ATOM   1160 C  CA    . GLN A 1 166 ? 31.770 -1.251  42.882  1.00 37.63 ?  146 GLN A CA    1 
ATOM   1161 C  C     . GLN A 1 166 ? 30.320 -0.806  43.029  1.00 35.95 ?  146 GLN A C     1 
ATOM   1162 O  O     . GLN A 1 166 ? 29.860 -0.630  44.160  1.00 38.30 ?  146 GLN A O     1 
ATOM   1163 C  CB    . GLN A 1 166 ? 32.668 -0.059  43.243  1.00 34.16 ?  146 GLN A CB    1 
ATOM   1164 C  CG    . GLN A 1 166 ? 34.148 -0.376  43.439  1.00 34.75 ?  146 GLN A CG    1 
ATOM   1165 C  CD    . GLN A 1 166 ? 34.991 0.874   43.651  1.00 44.50 ?  146 GLN A CD    1 
ATOM   1166 O  OE1   . GLN A 1 166 ? 35.823 1.227   42.805  1.00 46.17 ?  146 GLN A OE1   1 
ATOM   1167 N  NE2   . GLN A 1 166 ? 34.794 1.540   44.785  1.00 42.14 ?  146 GLN A NE2   1 
ATOM   1168 N  N     . LEU A 1 167 ? 29.598 -0.603  41.927  1.00 34.12 ?  147 LEU A N     1 
ATOM   1169 C  CA    . LEU A 1 167 ? 28.210 -0.162  42.026  1.00 36.99 ?  147 LEU A CA    1 
ATOM   1170 C  C     . LEU A 1 167 ? 27.325 -1.215  42.680  1.00 43.19 ?  147 LEU A C     1 
ATOM   1171 O  O     . LEU A 1 167 ? 26.299 -0.873  43.282  1.00 38.76 ?  147 LEU A O     1 
ATOM   1172 C  CB    . LEU A 1 167 ? 27.670 0.181   40.633  1.00 37.62 ?  147 LEU A CB    1 
ATOM   1173 C  CG    . LEU A 1 167 ? 28.410 1.305   39.904  1.00 28.44 ?  147 LEU A CG    1 
ATOM   1174 C  CD1   . LEU A 1 167 ? 27.956 1.401   38.448  1.00 30.01 ?  147 LEU A CD1   1 
ATOM   1175 C  CD2   . LEU A 1 167 ? 28.223 2.624   40.650  1.00 29.44 ?  147 LEU A CD2   1 
ATOM   1176 N  N     . SER A 1 168 ? 27.693 -2.494  42.557  1.00 47.09 ?  148 SER A N     1 
ATOM   1177 C  CA    . SER A 1 168 ? 26.873 -3.565  43.114  1.00 46.67 ?  148 SER A CA    1 
ATOM   1178 C  C     . SER A 1 168 ? 26.705 -3.407  44.619  1.00 39.64 ?  148 SER A C     1 
ATOM   1179 O  O     . SER A 1 168 ? 25.626 -3.665  45.162  1.00 44.89 ?  148 SER A O     1 
ATOM   1180 C  CB    . SER A 1 168 ? 27.499 -4.921  42.787  1.00 55.39 ?  148 SER A CB    1 
ATOM   1181 O  OG    . SER A 1 168 ? 26.957 -5.469  41.594  1.00 63.22 ?  148 SER A OG    1 
ATOM   1182 N  N     . ASN A 1 169 ? 27.753 -2.974  45.304  1.00 39.64 ?  149 ASN A N     1 
ATOM   1183 C  CA    . ASN A 1 169 ? 27.754 -2.867  46.765  1.00 44.97 ?  149 ASN A CA    1 
ATOM   1184 C  C     . ASN A 1 169 ? 27.619 -1.424  47.227  1.00 44.75 ?  149 ASN A C     1 
ATOM   1185 O  O     . ASN A 1 169 ? 28.348 -0.961  48.097  1.00 50.53 ?  149 ASN A O     1 
ATOM   1186 C  CB    . ASN A 1 169 ? 29.012 -3.511  47.329  1.00 40.43 ?  149 ASN A CB    1 
ATOM   1187 C  CG    . ASN A 1 169 ? 28.844 -5.003  47.541  1.00 48.77 ?  149 ASN A CG    1 
ATOM   1188 O  OD1   . ASN A 1 169 ? 28.176 -5.684  46.759  1.00 53.18 ?  149 ASN A OD1   1 
ATOM   1189 N  ND2   . ASN A 1 169 ? 29.422 -5.514  48.617  1.00 55.64 ?  149 ASN A ND2   1 
ATOM   1190 N  N     . LEU A 1 170 ? 26.679 -0.699  46.624  1.00 45.37 ?  150 LEU A N     1 
ATOM   1191 C  CA    . LEU A 1 170 ? 26.387 0.684   46.968  1.00 40.28 ?  150 LEU A CA    1 
ATOM   1192 C  C     . LEU A 1 170 ? 24.934 0.962   46.622  1.00 41.74 ?  150 LEU A C     1 
ATOM   1193 O  O     . LEU A 1 170 ? 24.423 0.437   45.631  1.00 39.95 ?  150 LEU A O     1 
ATOM   1194 C  CB    . LEU A 1 170 ? 27.295 1.657   46.219  1.00 42.38 ?  150 LEU A CB    1 
ATOM   1195 C  CG    . LEU A 1 170 ? 28.692 1.851   46.797  1.00 48.40 ?  150 LEU A CG    1 
ATOM   1196 C  CD1   . LEU A 1 170 ? 29.409 2.970   46.054  1.00 38.45 ?  150 LEU A CD1   1 
ATOM   1197 C  CD2   . LEU A 1 170 ? 28.605 2.133   48.293  1.00 36.78 ?  150 LEU A CD2   1 
ATOM   1198 N  N     . SER A 1 171 ? 24.272 1.784   47.433  1.00 44.95 ?  151 SER A N     1 
ATOM   1199 C  CA    . SER A 1 171 ? 22.866 2.095   47.213  1.00 41.86 ?  151 SER A CA    1 
ATOM   1200 C  C     . SER A 1 171 ? 22.695 3.264   46.247  1.00 41.00 ?  151 SER A C     1 
ATOM   1201 O  O     . SER A 1 171 ? 23.486 4.211   46.251  1.00 33.79 ?  151 SER A O     1 
ATOM   1202 C  CB    . SER A 1 171 ? 22.176 2.423   48.532  1.00 43.09 ?  151 SER A CB    1 
ATOM   1203 O  OG    . SER A 1 171 ? 20.832 2.788   48.285  1.00 50.20 ?  151 SER A OG    1 
ATOM   1204 N  N     . LEU A 1 172 ? 21.646 3.181   45.420  1.00 40.94 ?  152 LEU A N     1 
ATOM   1205 C  CA    . LEU A 1 172 ? 21.279 4.282   44.532  1.00 39.83 ?  152 LEU A CA    1 
ATOM   1206 C  C     . LEU A 1 172 ? 21.184 5.598   45.288  1.00 44.92 ?  152 LEU A C     1 
ATOM   1207 O  O     . LEU A 1 172 ? 21.530 6.660   44.753  1.00 45.56 ?  152 LEU A O     1 
ATOM   1208 C  CB    . LEU A 1 172 ? 19.934 3.992   43.863  1.00 41.31 ?  152 LEU A CB    1 
ATOM   1209 C  CG    . LEU A 1 172 ? 19.798 2.816   42.907  1.00 38.83 ?  152 LEU A CG    1 
ATOM   1210 C  CD1   . LEU A 1 172 ? 18.328 2.541   42.665  1.00 37.76 ?  152 LEU A CD1   1 
ATOM   1211 C  CD2   . LEU A 1 172 ? 20.506 3.151   41.609  1.00 37.74 ?  152 LEU A CD2   1 
ATOM   1212 N  N     . ASN A 1 173 ? 20.685 5.548   46.527  1.00 39.62 ?  153 ASN A N     1 
ATOM   1213 C  CA    . ASN A 1 173 ? 20.524 6.738   47.350  1.00 41.30 ?  153 ASN A CA    1 
ATOM   1214 C  C     . ASN A 1 173 ? 21.856 7.297   47.841  1.00 43.75 ?  153 ASN A C     1 
ATOM   1215 O  O     . ASN A 1 173 ? 21.900 8.437   48.306  1.00 52.28 ?  153 ASN A O     1 
ATOM   1216 C  CB    . ASN A 1 173 ? 19.603 6.403   48.524  1.00 47.69 ?  153 ASN A CB    1 
ATOM   1217 C  CG    . ASN A 1 173 ? 19.233 7.611   49.352  1.00 50.75 ?  153 ASN A CG    1 
ATOM   1218 O  OD1   . ASN A 1 173 ? 18.435 8.449   48.932  1.00 57.56 ?  153 ASN A OD1   1 
ATOM   1219 N  ND2   . ASN A 1 173 ? 19.800 7.698   50.549  1.00 48.26 ?  153 ASN A ND2   1 
ATOM   1220 N  N     . ASP A 1 174 ? 22.933 6.531   47.760  1.00 41.01 ?  154 ASP A N     1 
ATOM   1221 C  CA    . ASP A 1 174 ? 24.242 7.033   48.159  1.00 36.16 ?  154 ASP A CA    1 
ATOM   1222 C  C     . ASP A 1 174 ? 24.835 7.843   47.012  1.00 41.64 ?  154 ASP A C     1 
ATOM   1223 O  O     . ASP A 1 174 ? 24.911 7.341   45.884  1.00 41.57 ?  154 ASP A O     1 
ATOM   1224 C  CB    . ASP A 1 174 ? 25.158 5.856   48.545  1.00 37.64 ?  154 ASP A CB    1 
ATOM   1225 C  CG    . ASP A 1 174 ? 26.581 6.282   48.957  1.00 41.97 ?  154 ASP A CG    1 
ATOM   1226 O  OD1   . ASP A 1 174 ? 26.922 7.484   48.928  1.00 45.79 ?  154 ASP A OD1   1 
ATOM   1227 O  OD2   . ASP A 1 174 ? 27.384 5.385   49.301  1.00 40.13 ?  154 ASP A OD2   1 
ATOM   1228 N  N     . PRO A 1 175 ? 25.235 9.098   47.247  1.00 48.96 ?  155 PRO A N     1 
ATOM   1229 C  CA    . PRO A 1 175 ? 25.937 9.855   46.192  1.00 47.20 ?  155 PRO A CA    1 
ATOM   1230 C  C     . PRO A 1 175 ? 27.147 9.134   45.635  1.00 38.21 ?  155 PRO A C     1 
ATOM   1231 O  O     . PRO A 1 175 ? 27.493 9.340   44.463  1.00 43.83 ?  155 PRO A O     1 
ATOM   1232 C  CB    . PRO A 1 175 ? 26.349 11.157  46.900  1.00 43.44 ?  155 PRO A CB    1 
ATOM   1233 C  CG    . PRO A 1 175 ? 26.180 10.895  48.349  1.00 43.17 ?  155 PRO A CG    1 
ATOM   1234 C  CD    . PRO A 1 175 ? 25.068 9.899   48.466  1.00 45.03 ?  155 PRO A CD    1 
ATOM   1235 N  N     . ALA A 1 176 ? 27.808 8.302   46.447  1.00 37.94 ?  156 ALA A N     1 
ATOM   1236 C  CA    . ALA A 1 176 ? 28.960 7.544   45.968  1.00 44.25 ?  156 ALA A CA    1 
ATOM   1237 C  C     . ALA A 1 176 ? 28.618 6.710   44.740  1.00 36.45 ?  156 ALA A C     1 
ATOM   1238 O  O     . ALA A 1 176 ? 29.456 6.567   43.845  1.00 33.21 ?  156 ALA A O     1 
ATOM   1239 C  CB    . ALA A 1 176 ? 29.507 6.649   47.080  1.00 42.57 ?  156 ALA A CB    1 
ATOM   1240 N  N     . PHE A 1 177 ? 27.399 6.165   44.680  1.00 31.49 ?  157 PHE A N     1 
ATOM   1241 C  CA    . PHE A 1 177 ? 26.961 5.429   43.500  1.00 32.09 ?  157 PHE A CA    1 
ATOM   1242 C  C     . PHE A 1 177 ? 27.021 6.306   42.255  1.00 34.25 ?  157 PHE A C     1 
ATOM   1243 O  O     . PHE A 1 177 ? 27.637 5.936   41.251  1.00 32.04 ?  157 PHE A O     1 
ATOM   1244 C  CB    . PHE A 1 177 ? 25.543 4.902   43.710  1.00 32.98 ?  157 PHE A CB    1 
ATOM   1245 C  CG    . PHE A 1 177 ? 24.985 4.149   42.525  1.00 39.28 ?  157 PHE A CG    1 
ATOM   1246 C  CD1   . PHE A 1 177 ? 24.548 4.818   41.386  1.00 32.18 ?  157 PHE A CD1   1 
ATOM   1247 C  CD2   . PHE A 1 177 ? 24.882 2.764   42.560  1.00 34.94 ?  157 PHE A CD2   1 
ATOM   1248 C  CE1   . PHE A 1 177 ? 24.041 4.124   40.317  1.00 30.96 ?  157 PHE A CE1   1 
ATOM   1249 C  CE2   . PHE A 1 177 ? 24.366 2.065   41.485  1.00 37.48 ?  157 PHE A CE2   1 
ATOM   1250 C  CZ    . PHE A 1 177 ? 23.945 2.746   40.362  1.00 34.31 ?  157 PHE A CZ    1 
ATOM   1251 N  N     . GLU A 1 178 ? 26.360 7.465   42.299  1.00 35.35 ?  158 GLU A N     1 
ATOM   1252 C  CA    . GLU A 1 178 ? 26.304 8.334   41.131  1.00 34.93 ?  158 GLU A CA    1 
ATOM   1253 C  C     . GLU A 1 178 ? 27.692 8.822   40.733  1.00 32.65 ?  158 GLU A C     1 
ATOM   1254 O  O     . GLU A 1 178 ? 28.020 8.879   39.541  1.00 38.45 ?  158 GLU A O     1 
ATOM   1255 C  CB    . GLU A 1 178 ? 25.361 9.504   41.404  1.00 37.49 ?  158 GLU A CB    1 
ATOM   1256 C  CG    . GLU A 1 178 ? 25.242 10.513  40.274  1.00 37.73 ?  158 GLU A CG    1 
ATOM   1257 C  CD    . GLU A 1 178 ? 24.963 11.931  40.771  1.00 51.61 ?  158 GLU A CD    1 
ATOM   1258 O  OE1   . GLU A 1 178 ? 25.018 12.162  42.006  1.00 53.57 ?  158 GLU A OE1   1 
ATOM   1259 O  OE2   . GLU A 1 178 ? 24.697 12.817  39.927  1.00 45.38 ?  158 GLU A OE2   1 
ATOM   1260 N  N     . SER A 1 179 ? 28.543 9.132   41.706  1.00 30.11 ?  159 SER A N     1 
ATOM   1261 C  CA    . SER A 1 179 ? 29.890 9.563   41.346  1.00 33.17 ?  159 SER A CA    1 
ATOM   1262 C  C     . SER A 1 179 ? 30.724 8.442   40.728  1.00 35.55 ?  159 SER A C     1 
ATOM   1263 O  O     . SER A 1 179 ? 31.571 8.720   39.874  1.00 36.71 ?  159 SER A O     1 
ATOM   1264 C  CB    . SER A 1 179 ? 30.596 10.149  42.557  1.00 28.02 ?  159 SER A CB    1 
ATOM   1265 O  OG    . SER A 1 179 ? 29.793 11.186  43.093  1.00 50.65 ?  159 SER A OG    1 
ATOM   1266 N  N     . LEU A 1 180 ? 30.508 7.182   41.123  1.00 32.08 ?  160 LEU A N     1 
ATOM   1267 C  CA    . LEU A 1 180 ? 31.245 6.089   40.490  1.00 32.48 ?  160 LEU A CA    1 
ATOM   1268 C  C     . LEU A 1 180 ? 30.796 5.898   39.051  1.00 33.57 ?  160 LEU A C     1 
ATOM   1269 O  O     . LEU A 1 180 ? 31.627 5.757   38.142  1.00 29.98 ?  160 LEU A O     1 
ATOM   1270 C  CB    . LEU A 1 180 ? 31.073 4.788   41.280  1.00 30.40 ?  160 LEU A CB    1 
ATOM   1271 C  CG    . LEU A 1 180 ? 32.199 4.632   42.297  1.00 37.63 ?  160 LEU A CG    1 
ATOM   1272 C  CD1   . LEU A 1 180 ? 31.891 3.579   43.368  1.00 38.45 ?  160 LEU A CD1   1 
ATOM   1273 C  CD2   . LEU A 1 180 ? 33.520 4.371   41.576  1.00 27.74 ?  160 LEU A CD2   1 
ATOM   1274 N  N     . ALA A 1 181 ? 29.474 5.904   38.837  1.00 30.58 ?  161 ALA A N     1 
ATOM   1275 C  CA    . ALA A 1 181 ? 28.915 5.721   37.512  1.00 32.08 ?  161 ALA A CA    1 
ATOM   1276 C  C     . ALA A 1 181 ? 29.320 6.861   36.584  1.00 37.68 ?  161 ALA A C     1 
ATOM   1277 O  O     . ALA A 1 181 ? 29.579 6.628   35.393  1.00 33.67 ?  161 ALA A O     1 
ATOM   1278 C  CB    . ALA A 1 181 ? 27.395 5.585   37.614  1.00 25.93 ?  161 ALA A CB    1 
ATOM   1279 N  N     . LYS A 1 182 ? 29.417 8.086   37.115  1.00 32.33 ?  162 LYS A N     1 
ATOM   1280 C  CA    . LYS A 1 182 ? 29.882 9.211   36.306  1.00 31.48 ?  162 LYS A CA    1 
ATOM   1281 C  C     . LYS A 1 182 ? 31.338 9.026   35.914  1.00 28.84 ?  162 LYS A C     1 
ATOM   1282 O  O     . LYS A 1 182 ? 31.704 9.198   34.746  1.00 32.56 ?  162 LYS A O     1 
ATOM   1283 C  CB    . LYS A 1 182 ? 29.700 10.532  37.064  1.00 27.94 ?  162 LYS A CB    1 
ATOM   1284 C  CG    . LYS A 1 182 ? 28.289 11.092  37.003  1.00 33.17 ?  162 LYS A CG    1 
ATOM   1285 C  CD    . LYS A 1 182 ? 28.279 12.577  37.291  1.00 29.08 ?  162 LYS A CD    1 
ATOM   1286 C  CE    . LYS A 1 182 ? 26.891 13.159  37.100  1.00 36.06 ?  162 LYS A CE    1 
ATOM   1287 N  NZ    . LYS A 1 182 ? 26.725 14.386  37.921  1.00 44.20 ?  162 LYS A NZ    1 
ATOM   1288 N  N     . SER A 1 183 ? 32.186 8.686   36.884  1.00 25.90 ?  163 SER A N     1 
ATOM   1289 C  CA    . SER A 1 183 ? 33.578 8.394   36.586  1.00 29.53 ?  163 SER A CA    1 
ATOM   1290 C  C     . SER A 1 183 ? 33.696 7.282   35.539  1.00 33.94 ?  163 SER A C     1 
ATOM   1291 O  O     . SER A 1 183 ? 34.569 7.327   34.665  1.00 27.11 ?  163 SER A O     1 
ATOM   1292 C  CB    . SER A 1 183 ? 34.301 8.021   37.883  1.00 31.59 ?  163 SER A CB    1 
ATOM   1293 O  OG    . SER A 1 183 ? 35.698 8.274   37.809  1.00 31.37 ?  163 SER A OG    1 
ATOM   1294 N  N     . ALA A 1 184 ? 32.808 6.285   35.598  1.00 32.67 ?  164 ALA A N     1 
ATOM   1295 C  CA    . ALA A 1 184 ? 32.866 5.193   34.635  1.00 27.28 ?  164 ALA A CA    1 
ATOM   1296 C  C     . ALA A 1 184 ? 32.420 5.651   33.252  1.00 34.35 ?  164 ALA A C     1 
ATOM   1297 O  O     . ALA A 1 184 ? 33.039 5.284   32.245  1.00 31.75 ?  164 ALA A O     1 
ATOM   1298 C  CB    . ALA A 1 184 ? 32.008 4.019   35.107  1.00 23.70 ?  164 ALA A CB    1 
ATOM   1299 N  N     . ALA A 1 185 ? 31.334 6.429   33.176  1.00 32.35 ?  165 ALA A N     1 
ATOM   1300 C  CA    . ALA A 1 185 ? 30.914 6.958   31.883  1.00 30.67 ?  165 ALA A CA    1 
ATOM   1301 C  C     . ALA A 1 185 ? 32.005 7.845   31.295  1.00 32.02 ?  165 ALA A C     1 
ATOM   1302 O  O     . ALA A 1 185 ? 32.278 7.798   30.088  1.00 30.80 ?  165 ALA A O     1 
ATOM   1303 C  CB    . ALA A 1 185 ? 29.588 7.717   32.018  1.00 26.03 ?  165 ALA A CB    1 
ATOM   1304 N  N     . LEU A 1 186 ? 32.675 8.621   32.148  1.00 30.86 ?  166 LEU A N     1 
ATOM   1305 C  CA    . LEU A 1 186 ? 33.821 9.407   31.705  1.00 33.73 ?  166 LEU A CA    1 
ATOM   1306 C  C     . LEU A 1 186 ? 34.914 8.518   31.109  1.00 31.35 ?  166 LEU A C     1 
ATOM   1307 O  O     . LEU A 1 186 ? 35.455 8.812   30.038  1.00 28.47 ?  166 LEU A O     1 
ATOM   1308 C  CB    . LEU A 1 186 ? 34.360 10.221  32.880  1.00 27.77 ?  166 LEU A CB    1 
ATOM   1309 C  CG    . LEU A 1 186 ? 35.393 11.300  32.576  1.00 31.59 ?  166 LEU A CG    1 
ATOM   1310 C  CD1   . LEU A 1 186 ? 34.886 12.247  31.471  1.00 25.26 ?  166 LEU A CD1   1 
ATOM   1311 C  CD2   . LEU A 1 186 ? 35.726 12.055  33.845  1.00 21.55 ?  166 LEU A CD2   1 
ATOM   1312 N  N     . HIS A 1 187 ? 35.262 7.428   31.800  1.00 32.69 ?  167 HIS A N     1 
ATOM   1313 C  CA    . HIS A 1 187 ? 36.358 6.572   31.351  1.00 30.78 ?  167 HIS A CA    1 
ATOM   1314 C  C     . HIS A 1 187 ? 36.012 5.797   30.087  1.00 30.02 ?  167 HIS A C     1 
ATOM   1315 O  O     . HIS A 1 187 ? 36.908 5.479   29.301  1.00 25.36 ?  167 HIS A O     1 
ATOM   1316 C  CB    . HIS A 1 187 ? 36.739 5.599   32.456  1.00 25.29 ?  167 HIS A CB    1 
ATOM   1317 C  CG    . HIS A 1 187 ? 37.489 6.236   33.572  1.00 32.13 ?  167 HIS A CG    1 
ATOM   1318 N  ND1   . HIS A 1 187 ? 37.156 6.047   34.899  1.00 35.31 ?  167 HIS A ND1   1 
ATOM   1319 C  CD2   . HIS A 1 187 ? 38.564 7.056   33.563  1.00 31.18 ?  167 HIS A CD2   1 
ATOM   1320 C  CE1   . HIS A 1 187 ? 37.995 6.731   35.658  1.00 40.18 ?  167 HIS A CE1   1 
ATOM   1321 N  NE2   . HIS A 1 187 ? 38.859 7.352   34.872  1.00 38.68 ?  167 HIS A NE2   1 
ATOM   1322 N  N     . VAL A 1 188 ? 34.735 5.450   29.901  1.00 26.92 ?  168 VAL A N     1 
ATOM   1323 C  CA    . VAL A 1 188 ? 34.293 4.778   28.686  1.00 28.71 ?  168 VAL A CA    1 
ATOM   1324 C  C     . VAL A 1 188 ? 34.458 5.691   27.475  1.00 34.24 ?  168 VAL A C     1 
ATOM   1325 O  O     . VAL A 1 188 ? 34.712 5.215   26.360  1.00 32.54 ?  168 VAL A O     1 
ATOM   1326 C  CB    . VAL A 1 188 ? 32.835 4.303   28.860  1.00 30.63 ?  168 VAL A CB    1 
ATOM   1327 C  CG1   . VAL A 1 188 ? 32.275 3.772   27.576  1.00 30.69 ?  168 VAL A CG1   1 
ATOM   1328 C  CG2   . VAL A 1 188 ? 32.763 3.220   29.898  1.00 32.00 ?  168 VAL A CG2   1 
ATOM   1329 N  N     . TYR A 1 189 ? 34.349 7.013   27.672  1.00 36.10 ?  169 TYR A N     1 
ATOM   1330 C  CA    . TYR A 1 189 ? 34.495 7.962   26.568  1.00 32.32 ?  169 TYR A CA    1 
ATOM   1331 C  C     . TYR A 1 189 ? 35.807 7.779   25.837  1.00 34.21 ?  169 TYR A C     1 
ATOM   1332 O  O     . TYR A 1 189 ? 35.904 8.100   24.647  1.00 33.53 ?  169 TYR A O     1 
ATOM   1333 C  CB    . TYR A 1 189 ? 34.402 9.401   27.076  1.00 34.53 ?  169 TYR A CB    1 
ATOM   1334 C  CG    . TYR A 1 189 ? 33.081 10.039  26.759  1.00 38.57 ?  169 TYR A CG    1 
ATOM   1335 C  CD1   . TYR A 1 189 ? 32.703 10.299  25.428  1.00 24.37 ?  169 TYR A CD1   1 
ATOM   1336 C  CD2   . TYR A 1 189 ? 32.190 10.355  27.786  1.00 28.98 ?  169 TYR A CD2   1 
ATOM   1337 C  CE1   . TYR A 1 189 ? 31.478 10.872  25.143  1.00 28.14 ?  169 TYR A CE1   1 
ATOM   1338 C  CE2   . TYR A 1 189 ? 30.967 10.919  27.512  1.00 30.92 ?  169 TYR A CE2   1 
ATOM   1339 C  CZ    . TYR A 1 189 ? 30.608 11.178  26.198  1.00 35.24 ?  169 TYR A CZ    1 
ATOM   1340 O  OH    . TYR A 1 189 ? 29.375 11.742  25.966  1.00 36.63 ?  169 TYR A OH    1 
ATOM   1341 N  N     . GLN A 1 190 ? 36.828 7.282   26.538  1.00 33.06 ?  170 GLN A N     1 
ATOM   1342 C  CA    . GLN A 1 190 ? 38.085 6.913   25.893  1.00 37.60 ?  170 GLN A CA    1 
ATOM   1343 C  C     . GLN A 1 190 ? 37.867 5.979   24.700  1.00 34.94 ?  170 GLN A C     1 
ATOM   1344 O  O     . GLN A 1 190 ? 38.509 6.131   23.656  1.00 27.33 ?  170 GLN A O     1 
ATOM   1345 C  CB    . GLN A 1 190 ? 38.999 6.267   26.924  1.00 38.31 ?  170 GLN A CB    1 
ATOM   1346 C  CG    . GLN A 1 190 ? 39.481 7.243   27.962  1.00 33.27 ?  170 GLN A CG    1 
ATOM   1347 C  CD    . GLN A 1 190 ? 40.842 7.747   27.599  1.00 47.22 ?  170 GLN A CD    1 
ATOM   1348 O  OE1   . GLN A 1 190 ? 40.983 8.839   27.038  1.00 49.52 ?  170 GLN A OE1   1 
ATOM   1349 N  NE2   . GLN A 1 190 ? 41.862 6.934   27.868  1.00 46.85 ?  170 GLN A NE2   1 
ATOM   1350 N  N     . ALA A 1 191 ? 36.959 5.007   24.834  1.00 31.54 ?  171 ALA A N     1 
ATOM   1351 C  CA    . ALA A 1 191 ? 36.630 4.167   23.688  1.00 34.88 ?  171 ALA A CA    1 
ATOM   1352 C  C     . ALA A 1 191 ? 35.966 4.966   22.572  1.00 38.55 ?  171 ALA A C     1 
ATOM   1353 O  O     . ALA A 1 191 ? 36.145 4.635   21.397  1.00 29.50 ?  171 ALA A O     1 
ATOM   1354 C  CB    . ALA A 1 191 ? 35.727 3.009   24.106  1.00 27.15 ?  171 ALA A CB    1 
ATOM   1355 N  N     . VAL A 1 192 ? 35.182 5.999   22.913  1.00 35.82 ?  172 VAL A N     1 
ATOM   1356 C  CA    . VAL A 1 192 ? 34.664 6.901   21.887  1.00 28.48 ?  172 VAL A CA    1 
ATOM   1357 C  C     . VAL A 1 192 ? 35.813 7.633   21.211  1.00 27.19 ?  172 VAL A C     1 
ATOM   1358 O  O     . VAL A 1 192 ? 35.888 7.714   19.979  1.00 28.38 ?  172 VAL A O     1 
ATOM   1359 C  CB    . VAL A 1 192 ? 33.651 7.886   22.495  1.00 31.61 ?  172 VAL A CB    1 
ATOM   1360 C  CG1   . VAL A 1 192 ? 32.985 8.705   21.407  1.00 22.08 ?  172 VAL A CG1   1 
ATOM   1361 C  CG2   . VAL A 1 192 ? 32.617 7.127   23.311  1.00 31.88 ?  172 VAL A CG2   1 
ATOM   1362 N  N     . ASP A 1 193 ? 36.735 8.165   22.008  1.00 22.04 ?  173 ASP A N     1 
ATOM   1363 C  CA    . ASP A 1 193 ? 37.881 8.841   21.425  1.00 28.96 ?  173 ASP A CA    1 
ATOM   1364 C  C     . ASP A 1 193 ? 38.681 7.896   20.536  1.00 32.19 ?  173 ASP A C     1 
ATOM   1365 O  O     . ASP A 1 193 ? 39.157 8.292   19.467  1.00 33.68 ?  173 ASP A O     1 
ATOM   1366 C  CB    . ASP A 1 193 ? 38.749 9.430   22.530  1.00 25.27 ?  173 ASP A CB    1 
ATOM   1367 C  CG    . ASP A 1 193 ? 37.979 10.407  23.412  1.00 43.66 ?  173 ASP A CG    1 
ATOM   1368 O  OD1   . ASP A 1 193 ? 37.000 11.017  22.908  1.00 44.28 ?  173 ASP A OD1   1 
ATOM   1369 O  OD2   . ASP A 1 193 ? 38.335 10.552  24.615  1.00 41.74 ?  173 ASP A OD2   1 
ATOM   1370 N  N     . GLY A 1 194 ? 38.822 6.638   20.951  1.00 28.30 ?  174 GLY A N     1 
ATOM   1371 C  CA    . GLY A 1 194 ? 39.567 5.686   20.144  1.00 28.30 ?  174 GLY A CA    1 
ATOM   1372 C  C     . GLY A 1 194 ? 38.898 5.394   18.814  1.00 27.42 ?  174 GLY A C     1 
ATOM   1373 O  O     . GLY A 1 194 ? 39.557 5.374   17.777  1.00 27.24 ?  174 GLY A O     1 
ATOM   1374 N  N     . ILE A 1 195 ? 37.577 5.184   18.822  1.00 21.63 ?  175 ILE A N     1 
ATOM   1375 C  CA    . ILE A 1 195 ? 36.894 4.853   17.583  1.00 21.62 ?  175 ILE A CA    1 
ATOM   1376 C  C     . ILE A 1 195 ? 36.776 6.084   16.698  1.00 32.91 ?  175 ILE A C     1 
ATOM   1377 O  O     . ILE A 1 195 ? 36.778 5.974   15.466  1.00 33.59 ?  175 ILE A O     1 
ATOM   1378 C  CB    . ILE A 1 195 ? 35.520 4.206   17.845  1.00 21.09 ?  175 ILE A CB    1 
ATOM   1379 C  CG1   . ILE A 1 195 ? 35.127 3.359   16.645  1.00 24.48 ?  175 ILE A CG1   1 
ATOM   1380 C  CG2   . ILE A 1 195 ? 34.440 5.230   18.045  1.00 20.69 ?  175 ILE A CG2   1 
ATOM   1381 C  CD1   . ILE A 1 195 ? 36.232 2.443   16.155  1.00 21.37 ?  175 ILE A CD1   1 
ATOM   1382 N  N     . GLY A 1 196 ? 36.692 7.273   17.290  1.00 29.39 ?  176 GLY A N     1 
ATOM   1383 C  CA    . GLY A 1 196 ? 36.756 8.472   16.481  1.00 29.10 ?  176 GLY A CA    1 
ATOM   1384 C  C     . GLY A 1 196 ? 38.108 8.658   15.822  1.00 34.94 ?  176 GLY A C     1 
ATOM   1385 O  O     . GLY A 1 196 ? 38.185 9.176   14.703  1.00 33.50 ?  176 GLY A O     1 
ATOM   1386 N  N     . GLU A 1 197 ? 39.187 8.251   16.508  1.00 31.96 ?  177 GLU A N     1 
ATOM   1387 C  CA    . GLU A 1 197 ? 40.518 8.289   15.913  1.00 27.11 ?  177 GLU A CA    1 
ATOM   1388 C  C     . GLU A 1 197 ? 40.624 7.333   14.731  1.00 31.32 ?  177 GLU A C     1 
ATOM   1389 O  O     . GLU A 1 197 ? 41.347 7.613   13.766  1.00 30.03 ?  177 GLU A O     1 
ATOM   1390 C  CB    . GLU A 1 197 ? 41.569 7.931   16.957  1.00 26.16 ?  177 GLU A CB    1 
ATOM   1391 C  CG    . GLU A 1 197 ? 41.882 9.010   17.968  1.00 36.36 ?  177 GLU A CG    1 
ATOM   1392 C  CD    . GLU A 1 197 ? 42.148 10.356  17.332  1.00 48.50 ?  177 GLU A CD    1 
ATOM   1393 O  OE1   . GLU A 1 197 ? 43.100 10.454  16.519  1.00 46.85 ?  177 GLU A OE1   1 
ATOM   1394 O  OE2   . GLU A 1 197 ? 41.414 11.316  17.665  1.00 45.43 ?  177 GLU A OE2   1 
ATOM   1395 N  N     . THR A 1 198 ? 39.933 6.194   14.796  1.00 25.39 ?  178 THR A N     1 
ATOM   1396 C  CA    . THR A 1 198 ? 39.985 5.250   13.689  1.00 27.69 ?  178 THR A CA    1 
ATOM   1397 C  C     . THR A 1 198 ? 39.220 5.784   12.494  1.00 30.55 ?  178 THR A C     1 
ATOM   1398 O  O     . THR A 1 198 ? 39.705 5.712   11.354  1.00 29.18 ?  178 THR A O     1 
ATOM   1399 C  CB    . THR A 1 198 ? 39.433 3.889   14.115  1.00 25.20 ?  178 THR A CB    1 
ATOM   1400 O  OG1   . THR A 1 198 ? 40.108 3.472   15.304  1.00 21.43 ?  178 THR A OG1   1 
ATOM   1401 C  CG2   . THR A 1 198 ? 39.681 2.842   13.021  1.00 26.13 ?  178 THR A CG2   1 
ATOM   1402 N  N     . ILE A 1 199 ? 38.041 6.361   12.747  1.00 32.04 ?  179 ILE A N     1 
ATOM   1403 C  CA    . ILE A 1 199 ? 37.192 6.858   11.668  1.00 31.45 ?  179 ILE A CA    1 
ATOM   1404 C  C     . ILE A 1 199 ? 37.902 7.950   10.875  1.00 27.46 ?  179 ILE A C     1 
ATOM   1405 O  O     . ILE A 1 199 ? 37.781 8.019   9.646   1.00 33.06 ?  179 ILE A O     1 
ATOM   1406 C  CB    . ILE A 1 199 ? 35.850 7.340   12.238  1.00 31.67 ?  179 ILE A CB    1 
ATOM   1407 C  CG1   . ILE A 1 199 ? 35.086 6.151   12.808  1.00 25.25 ?  179 ILE A CG1   1 
ATOM   1408 C  CG2   . ILE A 1 199 ? 35.027 8.043   11.163  1.00 24.77 ?  179 ILE A CG2   1 
ATOM   1409 C  CD1   . ILE A 1 199 ? 33.782 6.528   13.432  1.00 24.46 ?  179 ILE A CD1   1 
ATOM   1410 N  N     . LYS A 1 200 ? 38.693 8.783   11.543  1.00 23.12 ?  180 LYS A N     1 
ATOM   1411 C  CA    . LYS A 1 200 ? 39.400 9.810   10.799  1.00 27.31 ?  180 LYS A CA    1 
ATOM   1412 C  C     . LYS A 1 200 ? 40.683 9.308   10.135  1.00 36.51 ?  180 LYS A C     1 
ATOM   1413 O  O     . LYS A 1 200 ? 41.148 9.943   9.179   1.00 35.16 ?  180 LYS A O     1 
ATOM   1414 C  CB    . LYS A 1 200 ? 39.724 11.002  11.698  1.00 26.04 ?  180 LYS A CB    1 
ATOM   1415 C  CG    . LYS A 1 200 ? 41.139 11.046  12.207  1.00 33.13 ?  180 LYS A CG    1 
ATOM   1416 C  CD    . LYS A 1 200 ? 41.258 12.103  13.308  1.00 51.96 ?  180 LYS A CD    1 
ATOM   1417 C  CE    . LYS A 1 200 ? 40.082 12.033  14.273  1.00 48.67 ?  180 LYS A CE    1 
ATOM   1418 N  NZ    . LYS A 1 200 ? 40.200 13.025  15.390  1.00 56.52 ?  180 LYS A NZ    1 
ATOM   1419 N  N     . LYS A 1 201 ? 41.268 8.192   10.591  1.00 28.21 ?  181 LYS A N     1 
ATOM   1420 C  CA    . LYS A 1 201 ? 42.577 7.799   10.097  1.00 22.97 ?  181 LYS A CA    1 
ATOM   1421 C  C     . LYS A 1 201 ? 42.560 6.595   9.165   1.00 31.72 ?  181 LYS A C     1 
ATOM   1422 O  O     . LYS A 1 201 ? 43.488 6.439   8.368   1.00 24.74 ?  181 LYS A O     1 
ATOM   1423 C  CB    . LYS A 1 201 ? 43.524 7.491   11.264  1.00 26.82 ?  181 LYS A CB    1 
ATOM   1424 C  CG    . LYS A 1 201 ? 44.105 8.700   11.944  1.00 35.98 ?  181 LYS A CG    1 
ATOM   1425 C  CD    . LYS A 1 201 ? 45.159 8.301   12.964  1.00 37.06 ?  181 LYS A CD    1 
ATOM   1426 C  CE    . LYS A 1 201 ? 46.148 9.428   13.200  1.00 41.20 ?  181 LYS A CE    1 
ATOM   1427 N  NZ    . LYS A 1 201 ? 45.847 10.098  14.488  1.00 60.46 ?  181 LYS A NZ    1 
ATOM   1428 N  N     . THR A 1 202 ? 41.547 5.745   9.239   1.00 34.57 ?  182 THR A N     1 
ATOM   1429 C  CA    . THR A 1 202 ? 41.582 4.462   8.555   1.00 28.89 ?  182 THR A CA    1 
ATOM   1430 C  C     . THR A 1 202 ? 40.531 4.443   7.462   1.00 29.92 ?  182 THR A C     1 
ATOM   1431 O  O     . THR A 1 202 ? 39.326 4.555   7.734   1.00 26.71 ?  182 THR A O     1 
ATOM   1432 C  CB    . THR A 1 202 ? 41.382 3.311   9.539   1.00 30.34 ?  182 THR A CB    1 
ATOM   1433 O  OG1   . THR A 1 202 ? 42.431 3.357   10.507  1.00 24.49 ?  182 THR A OG1   1 
ATOM   1434 C  CG2   . THR A 1 202 ? 41.439 1.967   8.821   1.00 26.05 ?  182 THR A CG2   1 
ATOM   1435 N  N     . ASP A 1 203 ? 41.002 4.315   6.233   1.00 32.10 ?  183 ASP A N     1 
ATOM   1436 C  CA    . ASP A 1 203 ? 40.134 4.231   5.085   1.00 23.63 ?  183 ASP A CA    1 
ATOM   1437 C  C     . ASP A 1 203 ? 39.544 2.832   5.009   1.00 24.32 ?  183 ASP A C     1 
ATOM   1438 O  O     . ASP A 1 203 ? 40.287 1.849   5.106   1.00 29.95 ?  183 ASP A O     1 
ATOM   1439 C  CB    . ASP A 1 203 ? 40.913 4.562   3.818   1.00 29.21 ?  183 ASP A CB    1 
ATOM   1440 C  CG    . ASP A 1 203 ? 40.105 4.338   2.578   1.00 25.99 ?  183 ASP A CG    1 
ATOM   1441 O  OD1   . ASP A 1 203 ? 39.146 5.097   2.368   1.00 27.16 ?  183 ASP A OD1   1 
ATOM   1442 O  OD2   . ASP A 1 203 ? 40.406 3.382   1.834   1.00 29.74 ?  183 ASP A OD2   1 
ATOM   1443 N  N     . PRO A 1 204 ? 38.222 2.697   4.886   1.00 26.97 ?  184 PRO A N     1 
ATOM   1444 C  CA    . PRO A 1 204 ? 37.635 1.350   4.866   1.00 27.78 ?  184 PRO A CA    1 
ATOM   1445 C  C     . PRO A 1 204 ? 38.195 0.471   3.751   1.00 32.00 ?  184 PRO A C     1 
ATOM   1446 O  O     . PRO A 1 204 ? 38.383 -0.736  3.949   1.00 29.58 ?  184 PRO A O     1 
ATOM   1447 C  CB    . PRO A 1 204 ? 36.136 1.636   4.692   1.00 23.34 ?  184 PRO A CB    1 
ATOM   1448 C  CG    . PRO A 1 204 ? 35.942 2.995   5.294   1.00 19.67 ?  184 PRO A CG    1 
ATOM   1449 C  CD    . PRO A 1 204 ? 37.192 3.752   4.952   1.00 26.67 ?  184 PRO A CD    1 
ATOM   1450 N  N     . TYR A 1 205 ? 38.501 1.054   2.593   1.00 29.42 ?  185 TYR A N     1 
ATOM   1451 C  CA    . TYR A 1 205 ? 39.058 0.275   1.494   1.00 32.89 ?  185 TYR A CA    1 
ATOM   1452 C  C     . TYR A 1 205 ? 40.499 -0.139  1.778   1.00 30.82 ?  185 TYR A C     1 
ATOM   1453 O  O     . TYR A 1 205 ? 40.873 -1.293  1.528   1.00 24.25 ?  185 TYR A O     1 
ATOM   1454 C  CB    . TYR A 1 205 ? 38.965 1.079   0.188   1.00 30.63 ?  185 TYR A CB    1 
ATOM   1455 C  CG    . TYR A 1 205 ? 39.418 0.307   -1.027  1.00 31.48 ?  185 TYR A CG    1 
ATOM   1456 C  CD1   . TYR A 1 205 ? 40.763 0.263   -1.384  1.00 31.47 ?  185 TYR A CD1   1 
ATOM   1457 C  CD2   . TYR A 1 205 ? 38.508 -0.398  -1.806  1.00 30.39 ?  185 TYR A CD2   1 
ATOM   1458 C  CE1   . TYR A 1 205 ? 41.186 -0.461  -2.482  1.00 34.71 ?  185 TYR A CE1   1 
ATOM   1459 C  CE2   . TYR A 1 205 ? 38.925 -1.112  -2.913  1.00 31.02 ?  185 TYR A CE2   1 
ATOM   1460 C  CZ    . TYR A 1 205 ? 40.267 -1.143  -3.244  1.00 31.94 ?  185 TYR A CZ    1 
ATOM   1461 O  OH    . TYR A 1 205 ? 40.702 -1.854  -4.345  1.00 38.25 ?  185 TYR A OH    1 
ATOM   1462 N  N     . VAL A 1 206 ? 41.328 0.792   2.272   1.00 31.56 ?  186 VAL A N     1 
ATOM   1463 C  CA    . VAL A 1 206 ? 42.719 0.461   2.570   1.00 29.27 ?  186 VAL A CA    1 
ATOM   1464 C  C     . VAL A 1 206 ? 42.780 -0.591  3.663   1.00 31.85 ?  186 VAL A C     1 
ATOM   1465 O  O     . VAL A 1 206 ? 43.595 -1.518  3.602   1.00 33.65 ?  186 VAL A O     1 
ATOM   1466 C  CB    . VAL A 1 206 ? 43.521 1.718   2.961   1.00 30.38 ?  186 VAL A CB    1 
ATOM   1467 C  CG1   . VAL A 1 206 ? 44.988 1.363   3.213   1.00 25.82 ?  186 VAL A CG1   1 
ATOM   1468 C  CG2   . VAL A 1 206 ? 43.415 2.780   1.894   1.00 16.26 ?  186 VAL A CG2   1 
ATOM   1469 N  N     . PHE A 1 207 ? 41.906 -0.483  4.670   1.00 32.67 ?  187 PHE A N     1 
ATOM   1470 C  CA    . PHE A 1 207 ? 41.851 -1.509  5.711   1.00 29.12 ?  187 PHE A CA    1 
ATOM   1471 C  C     . PHE A 1 207 ? 41.612 -2.896  5.115   1.00 25.24 ?  187 PHE A C     1 
ATOM   1472 O  O     . PHE A 1 207 ? 42.376 -3.832  5.376   1.00 22.04 ?  187 PHE A O     1 
ATOM   1473 C  CB    . PHE A 1 207 ? 40.764 -1.185  6.742   1.00 23.63 ?  187 PHE A CB    1 
ATOM   1474 C  CG    . PHE A 1 207 ? 40.443 -2.339  7.650   1.00 21.89 ?  187 PHE A CG    1 
ATOM   1475 C  CD1   . PHE A 1 207 ? 41.245 -2.619  8.754   1.00 22.82 ?  187 PHE A CD1   1 
ATOM   1476 C  CD2   . PHE A 1 207 ? 39.365 -3.175  7.384   1.00 28.32 ?  187 PHE A CD2   1 
ATOM   1477 C  CE1   . PHE A 1 207 ? 40.956 -3.694  9.600   1.00 25.57 ?  187 PHE A CE1   1 
ATOM   1478 C  CE2   . PHE A 1 207 ? 39.069 -4.260  8.216   1.00 25.99 ?  187 PHE A CE2   1 
ATOM   1479 C  CZ    . PHE A 1 207 ? 39.864 -4.509  9.337   1.00 24.24 ?  187 PHE A CZ    1 
ATOM   1480 N  N     . SER A 1 208 ? 40.538 -3.047  4.320   1.00 22.53 ?  188 SER A N     1 
ATOM   1481 C  CA    . SER A 1 208 ? 40.164 -4.369  3.820   1.00 24.73 ?  188 SER A CA    1 
ATOM   1482 C  C     . SER A 1 208 ? 41.228 -4.942  2.910   1.00 25.98 ?  188 SER A C     1 
ATOM   1483 O  O     . SER A 1 208 ? 41.448 -6.154  2.902   1.00 31.11 ?  188 SER A O     1 
ATOM   1484 C  CB    . SER A 1 208 ? 38.840 -4.333  3.062   1.00 25.11 ?  188 SER A CB    1 
ATOM   1485 O  OG    . SER A 1 208 ? 37.773 -3.791  3.828   1.00 25.13 ?  188 SER A OG    1 
ATOM   1486 N  N     . HIS A 1 209 ? 41.905 -4.102  2.152   1.00 23.65 ?  189 HIS A N     1 
ATOM   1487 C  CA    . HIS A 1 209 ? 42.818 -4.618  1.147   1.00 34.41 ?  189 HIS A CA    1 
ATOM   1488 C  C     . HIS A 1 209 ? 44.239 -4.750  1.659   1.00 29.68 ?  189 HIS A C     1 
ATOM   1489 O  O     . HIS A 1 209 ? 44.993 -5.588  1.145   1.00 28.47 ?  189 HIS A O     1 
ATOM   1490 C  CB    . HIS A 1 209 ? 42.775 -3.720  -0.106  1.00 34.24 ?  189 HIS A CB    1 
ATOM   1491 C  CG    . HIS A 1 209 ? 41.510 -3.865  -0.893  1.00 30.07 ?  189 HIS A CG    1 
ATOM   1492 N  ND1   . HIS A 1 209 ? 41.406 -4.697  -1.985  1.00 35.57 ?  189 HIS A ND1   1 
ATOM   1493 C  CD2   . HIS A 1 209 ? 40.278 -3.333  -0.710  1.00 35.52 ?  189 HIS A CD2   1 
ATOM   1494 C  CE1   . HIS A 1 209 ? 40.171 -4.650  -2.457  1.00 36.29 ?  189 HIS A CE1   1 
ATOM   1495 N  NE2   . HIS A 1 209 ? 39.463 -3.838  -1.694  1.00 30.85 ?  189 HIS A NE2   1 
ATOM   1496 N  N     . GLU A 1 210 ? 44.604 -3.955  2.668   1.00 30.92 ?  190 GLU A N     1 
ATOM   1497 C  CA    . GLU A 1 210 ? 45.974 -3.828  3.144   1.00 28.41 ?  190 GLU A CA    1 
ATOM   1498 C  C     . GLU A 1 210 ? 46.197 -4.251  4.586   1.00 29.60 ?  190 GLU A C     1 
ATOM   1499 O  O     . GLU A 1 210 ? 47.311 -4.673  4.911   1.00 29.45 ?  190 GLU A O     1 
ATOM   1500 C  CB    . GLU A 1 210 ? 46.453 -2.380  3.007   1.00 29.22 ?  190 GLU A CB    1 
ATOM   1501 C  CG    . GLU A 1 210 ? 46.317 -1.852  1.602   1.00 38.83 ?  190 GLU A CG    1 
ATOM   1502 C  CD    . GLU A 1 210 ? 47.078 -2.700  0.610   1.00 41.93 ?  190 GLU A CD    1 
ATOM   1503 O  OE1   . GLU A 1 210 ? 48.284 -2.940  0.838   1.00 39.04 ?  190 GLU A OE1   1 
ATOM   1504 O  OE2   . GLU A 1 210 ? 46.465 -3.142  -0.385  1.00 47.31 ?  190 GLU A OE2   1 
ATOM   1505 N  N     . LEU A 1 211 ? 45.206 -4.112  5.468   1.00 27.52 ?  191 LEU A N     1 
ATOM   1506 C  CA    . LEU A 1 211 ? 45.416 -4.341  6.896   1.00 24.86 ?  191 LEU A CA    1 
ATOM   1507 C  C     . LEU A 1 211 ? 44.742 -5.604  7.408   1.00 21.54 ?  191 LEU A C     1 
ATOM   1508 O  O     . LEU A 1 211 ? 45.377 -6.407  8.094   1.00 25.07 ?  191 LEU A O     1 
ATOM   1509 C  CB    . LEU A 1 211 ? 44.924 -3.136  7.704   1.00 23.35 ?  191 LEU A CB    1 
ATOM   1510 C  CG    . LEU A 1 211 ? 45.405 -1.751  7.293   1.00 24.62 ?  191 LEU A CG    1 
ATOM   1511 C  CD1   . LEU A 1 211 ? 44.852 -0.708  8.262   1.00 27.21 ?  191 LEU A CD1   1 
ATOM   1512 C  CD2   . LEU A 1 211 ? 46.922 -1.720  7.246   1.00 27.37 ?  191 LEU A CD2   1 
ATOM   1513 N  N     . ARG A 1 212 ? 43.466 -5.784  7.081   1.00 23.40 ?  192 ARG A N     1 
ATOM   1514 C  CA    . ARG A 1 212 ? 42.704 -6.955  7.503   1.00 21.50 ?  192 ARG A CA    1 
ATOM   1515 C  C     . ARG A 1 212 ? 43.411 -8.297  7.295   1.00 25.65 ?  192 ARG A C     1 
ATOM   1516 O  O     . ARG A 1 212 ? 43.346 -9.142  8.206   1.00 25.17 ?  192 ARG A O     1 
ATOM   1517 C  CB    . ARG A 1 212 ? 41.349 -6.931  6.788   1.00 15.84 ?  192 ARG A CB    1 
ATOM   1518 C  CG    . ARG A 1 212 ? 40.559 -8.191  6.956   1.00 20.65 ?  192 ARG A CG    1 
ATOM   1519 C  CD    . ARG A 1 212 ? 40.069 -8.301  8.381   1.00 26.73 ?  192 ARG A CD    1 
ATOM   1520 N  NE    . ARG A 1 212 ? 39.084 -9.359  8.539   1.00 25.79 ?  192 ARG A NE    1 
ATOM   1521 C  CZ    . ARG A 1 212 ? 39.385 -10.624 8.768   1.00 22.30 ?  192 ARG A CZ    1 
ATOM   1522 N  NH1   . ARG A 1 212 ? 40.643 -11.027 8.880   1.00 22.91 ?  192 ARG A NH1   1 
ATOM   1523 N  NH2   . ARG A 1 212 ? 38.403 -11.506 8.884   1.00 22.64 ?  192 ARG A NH2   1 
ATOM   1524 N  N     . PRO A 1 213 ? 44.098 -8.567  6.180   1.00 29.84 ?  193 PRO A N     1 
ATOM   1525 C  CA    . PRO A 1 213 ? 44.748 -9.887  6.031   1.00 26.34 ?  193 PRO A CA    1 
ATOM   1526 C  C     . PRO A 1 213 ? 45.869 -10.159 7.032   1.00 28.64 ?  193 PRO A C     1 
ATOM   1527 O  O     . PRO A 1 213 ? 46.385 -11.283 7.056   1.00 30.32 ?  193 PRO A O     1 
ATOM   1528 C  CB    . PRO A 1 213 ? 45.283 -9.854  4.594   1.00 25.88 ?  193 PRO A CB    1 
ATOM   1529 C  CG    . PRO A 1 213 ? 44.371 -8.857  3.893   1.00 26.20 ?  193 PRO A CG    1 
ATOM   1530 C  CD    . PRO A 1 213 ? 44.115 -7.805  4.914   1.00 26.42 ?  193 PRO A CD    1 
ATOM   1531 N  N     . PHE A 1 214 ? 46.261 -9.193  7.858   1.00 26.87 ?  194 PHE A N     1 
ATOM   1532 C  CA    . PHE A 1 214 ? 47.234 -9.469  8.906   1.00 28.83 ?  194 PHE A CA    1 
ATOM   1533 C  C     . PHE A 1 214 ? 46.601 -9.970  10.204  1.00 25.09 ?  194 PHE A C     1 
ATOM   1534 O  O     . PHE A 1 214 ? 47.321 -10.229 11.171  1.00 23.39 ?  194 PHE A O     1 
ATOM   1535 C  CB    . PHE A 1 214 ? 48.064 -8.225  9.190   1.00 24.47 ?  194 PHE A CB    1 
ATOM   1536 C  CG    . PHE A 1 214 ? 49.051 -7.916  8.123   1.00 22.18 ?  194 PHE A CG    1 
ATOM   1537 C  CD1   . PHE A 1 214 ? 50.300 -8.512  8.121   1.00 24.56 ?  194 PHE A CD1   1 
ATOM   1538 C  CD2   . PHE A 1 214 ? 48.736 -7.036  7.107   1.00 27.56 ?  194 PHE A CD2   1 
ATOM   1539 C  CE1   . PHE A 1 214 ? 51.232 -8.218  7.118   1.00 21.60 ?  194 PHE A CE1   1 
ATOM   1540 C  CE2   . PHE A 1 214 ? 49.666 -6.742  6.090   1.00 24.95 ?  194 PHE A CE2   1 
ATOM   1541 C  CZ    . PHE A 1 214 ? 50.904 -7.336  6.102   1.00 21.91 ?  194 PHE A CZ    1 
ATOM   1542 N  N     . PHE A 1 215 ? 45.287 -10.149 10.243  1.00 25.22 ?  195 PHE A N     1 
ATOM   1543 C  CA    . PHE A 1 215 ? 44.626 -10.551 11.476  1.00 24.82 ?  195 PHE A CA    1 
ATOM   1544 C  C     . PHE A 1 215 ? 43.842 -11.844 11.281  1.00 24.90 ?  195 PHE A C     1 
ATOM   1545 O  O     . PHE A 1 215 ? 42.666 -11.922 11.641  1.00 26.88 ?  195 PHE A O     1 
ATOM   1546 C  CB    . PHE A 1 215 ? 43.724 -9.413  11.962  1.00 23.90 ?  195 PHE A CB    1 
ATOM   1547 C  CG    . PHE A 1 215 ? 44.415 -8.077  11.977  1.00 26.35 ?  195 PHE A CG    1 
ATOM   1548 C  CD1   . PHE A 1 215 ? 45.293 -7.749  12.994  1.00 25.01 ?  195 PHE A CD1   1 
ATOM   1549 C  CD2   . PHE A 1 215 ? 44.228 -7.169  10.946  1.00 27.35 ?  195 PHE A CD2   1 
ATOM   1550 C  CE1   . PHE A 1 215 ? 45.946 -6.537  13.004  1.00 26.39 ?  195 PHE A CE1   1 
ATOM   1551 C  CE2   . PHE A 1 215 ? 44.879 -5.955  10.956  1.00 25.87 ?  195 PHE A CE2   1 
ATOM   1552 C  CZ    . PHE A 1 215 ? 45.736 -5.638  11.982  1.00 26.90 ?  195 PHE A CZ    1 
ATOM   1553 N  N     . ASP A 1 216 ? 44.488 -12.863 10.733  1.00 23.82 ?  196 ASP A N     1 
ATOM   1554 C  CA    . ASP A 1 216 ? 43.860 -14.121 10.356  1.00 23.74 ?  196 ASP A CA    1 
ATOM   1555 C  C     . ASP A 1 216 ? 44.241 -15.236 11.329  1.00 23.77 ?  196 ASP A C     1 
ATOM   1556 O  O     . ASP A 1 216 ? 45.236 -15.133 12.059  1.00 20.93 ?  196 ASP A O     1 
ATOM   1557 C  CB    . ASP A 1 216 ? 44.279 -14.509 8.929   1.00 24.36 ?  196 ASP A CB    1 
ATOM   1558 C  CG    . ASP A 1 216 ? 43.362 -13.919 7.852   1.00 33.67 ?  196 ASP A CG    1 
ATOM   1559 O  OD1   . ASP A 1 216 ? 42.203 -13.554 8.170   1.00 32.34 ?  196 ASP A OD1   1 
ATOM   1560 O  OD2   . ASP A 1 216 ? 43.816 -13.818 6.679   1.00 34.95 ?  196 ASP A OD2   1 
ATOM   1561 N  N     . PRO A 1 217 ? 43.478 -16.323 11.355  1.00 24.69 ?  197 PRO A N     1 
ATOM   1562 C  CA    . PRO A 1 217 ? 43.710 -17.368 12.372  1.00 25.59 ?  197 PRO A CA    1 
ATOM   1563 C  C     . PRO A 1 217 ? 45.047 -18.085 12.205  1.00 19.48 ?  197 PRO A C     1 
ATOM   1564 O  O     . PRO A 1 217 ? 45.560 -18.239 11.103  1.00 29.51 ?  197 PRO A O     1 
ATOM   1565 C  CB    . PRO A 1 217 ? 42.530 -18.326 12.163  1.00 27.13 ?  197 PRO A CB    1 
ATOM   1566 C  CG    . PRO A 1 217 ? 41.457 -17.475 11.457  1.00 17.47 ?  197 PRO A CG    1 
ATOM   1567 C  CD    . PRO A 1 217 ? 42.216 -16.514 10.612  1.00 17.83 ?  197 PRO A CD    1 
ATOM   1568 N  N     . ILE A 1 218 ? 45.622 -18.528 13.317  1.00 23.65 ?  198 ILE A N     1 
ATOM   1569 C  CA    . ILE A 1 218 ? 46.905 -19.234 13.305  1.00 26.46 ?  198 ILE A CA    1 
ATOM   1570 C  C     . ILE A 1 218 ? 46.805 -20.521 14.138  1.00 30.99 ?  198 ILE A C     1 
ATOM   1571 O  O     . ILE A 1 218 ? 46.386 -20.495 15.310  1.00 23.08 ?  198 ILE A O     1 
ATOM   1572 C  CB    . ILE A 1 218 ? 48.051 -18.327 13.803  1.00 25.33 ?  198 ILE A CB    1 
ATOM   1573 C  CG1   . ILE A 1 218 ? 48.474 -17.365 12.686  1.00 19.77 ?  198 ILE A CG1   1 
ATOM   1574 C  CG2   . ILE A 1 218 ? 49.234 -19.147 14.273  1.00 20.60 ?  198 ILE A CG2   1 
ATOM   1575 C  CD1   . ILE A 1 218 ? 49.513 -16.375 13.090  1.00 16.88 ?  198 ILE A CD1   1 
ATOM   1576 N  N     . ARG A 1 219 ? 47.201 -21.640 13.519  1.00 29.70 ?  199 ARG A N     1 
ATOM   1577 C  CA    . ARG A 1 219 ? 47.142 -22.975 14.115  1.00 30.68 ?  199 ARG A CA    1 
ATOM   1578 C  C     . ARG A 1 219 ? 48.366 -23.213 15.002  1.00 34.80 ?  199 ARG A C     1 
ATOM   1579 O  O     . ARG A 1 219 ? 49.500 -23.233 14.512  1.00 33.94 ?  199 ARG A O     1 
ATOM   1580 C  CB    . ARG A 1 219 ? 47.067 -24.027 13.001  1.00 34.64 ?  199 ARG A CB    1 
ATOM   1581 C  CG    . ARG A 1 219 ? 46.379 -25.356 13.352  1.00 41.83 ?  199 ARG A CG    1 
ATOM   1582 C  CD    . ARG A 1 219 ? 44.887 -25.152 13.647  1.00 62.33 ?  199 ARG A CD    1 
ATOM   1583 N  NE    . ARG A 1 219 ? 44.060 -26.343 13.454  1.00 58.17 ?  199 ARG A NE    1 
ATOM   1584 C  CZ    . ARG A 1 219 ? 42.784 -26.324 13.074  1.00 67.79 ?  199 ARG A CZ    1 
ATOM   1585 N  NH1   . ARG A 1 219 ? 42.159 -25.190 12.789  1.00 57.18 ?  199 ARG A NH1   1 
ATOM   1586 N  NH2   . ARG A 1 219 ? 42.119 -27.472 12.970  1.00 79.38 ?  199 ARG A NH2   1 
ATOM   1587 N  N     . ILE A 1 220 ? 48.147 -23.405 16.303  1.00 36.40 ?  200 ILE A N     1 
ATOM   1588 C  CA    . ILE A 1 220 ? 49.239 -23.601 17.261  1.00 35.50 ?  200 ILE A CA    1 
ATOM   1589 C  C     . ILE A 1 220 ? 48.850 -24.743 18.189  1.00 34.66 ?  200 ILE A C     1 
ATOM   1590 O  O     . ILE A 1 220 ? 47.940 -24.591 19.010  1.00 36.77 ?  200 ILE A O     1 
ATOM   1591 C  CB    . ILE A 1 220 ? 49.542 -22.343 18.087  1.00 31.97 ?  200 ILE A CB    1 
ATOM   1592 C  CG1   . ILE A 1 220 ? 49.862 -21.154 17.188  1.00 24.86 ?  200 ILE A CG1   1 
ATOM   1593 C  CG2   . ILE A 1 220 ? 50.699 -22.598 19.001  1.00 23.93 ?  200 ILE A CG2   1 
ATOM   1594 C  CD1   . ILE A 1 220 ? 49.998 -19.897 17.949  1.00 20.76 ?  200 ILE A CD1   1 
ATOM   1595 N  N     . GLY A 1 221 ? 49.547 -25.870 18.081  1.00 39.30 ?  201 GLY A N     1 
ATOM   1596 C  CA    . GLY A 1 221 ? 49.282 -27.019 18.920  1.00 34.94 ?  201 GLY A CA    1 
ATOM   1597 C  C     . GLY A 1 221 ? 47.868 -27.552 18.792  1.00 40.56 ?  201 GLY A C     1 
ATOM   1598 O  O     . GLY A 1 221 ? 47.175 -27.724 19.801  1.00 45.71 ?  201 GLY A O     1 
ATOM   1599 N  N     . GLY A 1 222 ? 47.425 -27.819 17.565  1.00 34.06 ?  202 GLY A N     1 
ATOM   1600 C  CA    . GLY A 1 222 ? 46.113 -28.387 17.343  1.00 30.10 ?  202 GLY A CA    1 
ATOM   1601 C  C     . GLY A 1 222 ? 44.949 -27.441 17.539  1.00 40.61 ?  202 GLY A C     1 
ATOM   1602 O  O     . GLY A 1 222 ? 43.798 -27.867 17.385  1.00 40.81 ?  202 GLY A O     1 
ATOM   1603 N  N     . LYS A 1 223 ? 45.196 -26.180 17.882  1.00 40.73 ?  203 LYS A N     1 
ATOM   1604 C  CA    . LYS A 1 223 ? 44.131 -25.202 18.012  1.00 34.43 ?  203 LYS A CA    1 
ATOM   1605 C  C     . LYS A 1 223 ? 44.406 -24.015 17.098  1.00 37.03 ?  203 LYS A C     1 
ATOM   1606 O  O     . LYS A 1 223 ? 45.533 -23.773 16.654  1.00 33.68 ?  203 LYS A O     1 
ATOM   1607 C  CB    . LYS A 1 223 ? 43.963 -24.738 19.468  1.00 37.48 ?  203 LYS A CB    1 
ATOM   1608 C  CG    . LYS A 1 223 ? 42.831 -25.466 20.219  1.00 56.00 ?  203 LYS A CG    1 
ATOM   1609 C  CD    . LYS A 1 223 ? 43.169 -25.749 21.702  1.00 55.19 ?  203 LYS A CD    1 
ATOM   1610 C  CE    . LYS A 1 223 ? 42.337 -26.923 22.264  1.00 47.73 ?  203 LYS A CE    1 
ATOM   1611 N  NZ    . LYS A 1 223 ? 40.988 -26.544 22.800  1.00 41.90 ?  203 LYS A NZ    1 
ATOM   1612 N  N     . SER A 1 224 ? 43.339 -23.289 16.815  1.00 32.12 ?  204 SER A N     1 
ATOM   1613 C  CA    . SER A 1 224 ? 43.361 -22.131 15.941  1.00 35.59 ?  204 SER A CA    1 
ATOM   1614 C  C     . SER A 1 224 ? 43.123 -20.882 16.791  1.00 25.83 ?  204 SER A C     1 
ATOM   1615 O  O     . SER A 1 224 ? 42.176 -20.846 17.578  1.00 20.36 ?  204 SER A O     1 
ATOM   1616 C  CB    . SER A 1 224 ? 42.298 -22.303 14.842  1.00 25.25 ?  204 SER A CB    1 
ATOM   1617 O  OG    . SER A 1 224 ? 41.862 -21.055 14.324  1.00 33.53 ?  204 SER A OG    1 
ATOM   1618 N  N     . TYR A 1 225 ? 43.985 -19.870 16.649  1.00 23.73 ?  205 TYR A N     1 
ATOM   1619 C  CA    . TYR A 1 225 ? 43.891 -18.648 17.450  1.00 19.25 ?  205 TYR A CA    1 
ATOM   1620 C  C     . TYR A 1 225 ? 43.626 -17.460 16.536  1.00 20.65 ?  205 TYR A C     1 
ATOM   1621 O  O     . TYR A 1 225 ? 44.490 -17.075 15.744  1.00 25.43 ?  205 TYR A O     1 
ATOM   1622 C  CB    . TYR A 1 225 ? 45.158 -18.441 18.278  1.00 22.65 ?  205 TYR A CB    1 
ATOM   1623 C  CG    . TYR A 1 225 ? 45.335 -19.511 19.341  1.00 22.05 ?  205 TYR A CG    1 
ATOM   1624 C  CD1   . TYR A 1 225 ? 45.978 -20.711 19.046  1.00 25.87 ?  205 TYR A CD1   1 
ATOM   1625 C  CD2   . TYR A 1 225 ? 44.818 -19.342 20.630  1.00 29.20 ?  205 TYR A CD2   1 
ATOM   1626 C  CE1   . TYR A 1 225 ? 46.123 -21.698 20.000  1.00 24.98 ?  205 TYR A CE1   1 
ATOM   1627 C  CE2   . TYR A 1 225 ? 44.957 -20.338 21.603  1.00 21.34 ?  205 TYR A CE2   1 
ATOM   1628 C  CZ    . TYR A 1 225 ? 45.614 -21.500 21.271  1.00 23.15 ?  205 TYR A CZ    1 
ATOM   1629 O  OH    . TYR A 1 225 ? 45.772 -22.481 22.191  1.00 29.49 ?  205 TYR A OH    1 
ATOM   1630 N  N     . ILE A 1 226 ? 42.425 -16.886 16.641  1.00 17.72 ?  206 ILE A N     1 
ATOM   1631 C  CA    . ILE A 1 226 ? 42.090 -15.702 15.864  1.00 17.13 ?  206 ILE A CA    1 
ATOM   1632 C  C     . ILE A 1 226 ? 43.111 -14.582 16.094  1.00 22.46 ?  206 ILE A C     1 
ATOM   1633 O  O     . ILE A 1 226 ? 43.776 -14.508 17.139  1.00 24.01 ?  206 ILE A O     1 
ATOM   1634 C  CB    . ILE A 1 226 ? 40.672 -15.222 16.211  1.00 19.28 ?  206 ILE A CB    1 
ATOM   1635 C  CG1   . ILE A 1 226 ? 40.610 -14.805 17.687  1.00 13.71 ?  206 ILE A CG1   1 
ATOM   1636 C  CG2   . ILE A 1 226 ? 39.639 -16.282 15.837  1.00 11.11 ?  206 ILE A CG2   1 
ATOM   1637 C  CD1   . ILE A 1 226 ? 39.412 -13.969 18.051  1.00 12.37 ?  206 ILE A CD1   1 
ATOM   1638 N  N     . GLY A 1 227 ? 43.230 -13.694 15.103  1.00 22.09 ?  207 GLY A N     1 
ATOM   1639 C  CA    . GLY A 1 227 ? 44.154 -12.581 15.187  1.00 19.81 ?  207 GLY A CA    1 
ATOM   1640 C  C     . GLY A 1 227 ? 43.603 -11.448 16.028  1.00 25.76 ?  207 GLY A C     1 
ATOM   1641 O  O     . GLY A 1 227 ? 42.486 -11.499 16.545  1.00 24.01 ?  207 GLY A O     1 
ATOM   1642 N  N     . ALA A 1 228 ? 44.414 -10.395 16.159  1.00 26.34 ?  208 ALA A N     1 
ATOM   1643 C  CA    . ALA A 1 228 ? 44.018 -9.243  16.963  1.00 20.54 ?  208 ALA A CA    1 
ATOM   1644 C  C     . ALA A 1 228 ? 42.729 -8.610  16.429  1.00 26.35 ?  208 ALA A C     1 
ATOM   1645 O  O     . ALA A 1 228 ? 42.443 -8.620  15.222  1.00 20.21 ?  208 ALA A O     1 
ATOM   1646 C  CB    . ALA A 1 228 ? 45.139 -8.210  17.006  1.00 19.87 ?  208 ALA A CB    1 
ATOM   1647 N  N     . GLY A 1 229 ? 41.933 -8.069  17.354  1.00 23.06 ?  209 GLY A N     1 
ATOM   1648 C  CA    . GLY A 1 229 ? 40.610 -7.592  17.021  1.00 19.10 ?  209 GLY A CA    1 
ATOM   1649 C  C     . GLY A 1 229 ? 40.154 -6.459  17.912  1.00 25.45 ?  209 GLY A C     1 
ATOM   1650 O  O     . GLY A 1 229 ? 40.479 -6.430  19.110  1.00 18.19 ?  209 GLY A O     1 
ATOM   1651 N  N     . GLY A 1 230 ? 39.401 -5.511  17.330  1.00 21.53 ?  210 GLY A N     1 
ATOM   1652 C  CA    . GLY A 1 230 ? 38.791 -4.459  18.135  1.00 21.87 ?  210 GLY A CA    1 
ATOM   1653 C  C     . GLY A 1 230 ? 37.946 -5.012  19.268  1.00 22.06 ?  210 GLY A C     1 
ATOM   1654 O  O     . GLY A 1 230 ? 37.996 -4.512  20.394  1.00 21.33 ?  210 GLY A O     1 
ATOM   1655 N  N     . GLY A 1 231 ? 37.174 -6.066  18.988  1.00 19.38 ?  211 GLY A N     1 
ATOM   1656 C  CA    . GLY A 1 231 ? 36.384 -6.779  19.970  1.00 16.74 ?  211 GLY A CA    1 
ATOM   1657 C  C     . GLY A 1 231 ? 37.175 -7.355  21.139  1.00 25.28 ?  211 GLY A C     1 
ATOM   1658 O  O     . GLY A 1 231 ? 36.555 -7.814  22.104  1.00 19.23 ?  211 GLY A O     1 
ATOM   1659 N  N     . GLN A 1 232 ? 38.513 -7.350  21.089  1.00 24.74 ?  212 GLN A N     1 
ATOM   1660 C  CA    . GLN A 1 232 ? 39.280 -7.820  22.244  1.00 20.16 ?  212 GLN A CA    1 
ATOM   1661 C  C     . GLN A 1 232 ? 39.500 -6.741  23.302  1.00 19.56 ?  212 GLN A C     1 
ATOM   1662 O  O     . GLN A 1 232 ? 39.969 -7.071  24.399  1.00 26.18 ?  212 GLN A O     1 
ATOM   1663 C  CB    . GLN A 1 232 ? 40.628 -8.413  21.799  1.00 17.11 ?  212 GLN A CB    1 
ATOM   1664 C  CG    . GLN A 1 232 ? 40.424 -9.559  20.787  1.00 25.94 ?  212 GLN A CG    1 
ATOM   1665 C  CD    . GLN A 1 232 ? 41.704 -10.137 20.184  1.00 27.24 ?  212 GLN A CD    1 
ATOM   1666 O  OE1   . GLN A 1 232 ? 42.690 -9.435  19.951  1.00 25.79 ?  212 GLN A OE1   1 
ATOM   1667 N  NE2   . GLN A 1 232 ? 41.681 -11.437 19.928  1.00 27.51 ?  212 GLN A NE2   1 
ATOM   1668 N  N     . ILE A 1 233 ? 39.167 -5.481  23.030  1.00 17.04 ?  213 ILE A N     1 
ATOM   1669 C  CA    . ILE A 1 233 ? 39.156 -4.539  24.152  1.00 19.71 ?  213 ILE A CA    1 
ATOM   1670 C  C     . ILE A 1 233 ? 38.108 -5.013  25.146  1.00 21.73 ?  213 ILE A C     1 
ATOM   1671 O  O     . ILE A 1 233 ? 37.077 -5.582  24.732  1.00 26.06 ?  213 ILE A O     1 
ATOM   1672 C  CB    . ILE A 1 233 ? 38.879 -3.089  23.690  1.00 24.52 ?  213 ILE A CB    1 
ATOM   1673 C  CG1   . ILE A 1 233 ? 37.431 -2.888  23.235  1.00 21.12 ?  213 ILE A CG1   1 
ATOM   1674 C  CG2   . ILE A 1 233 ? 39.846 -2.658  22.608  1.00 18.32 ?  213 ILE A CG2   1 
ATOM   1675 C  CD1   . ILE A 1 233 ? 37.149 -1.508  22.722  1.00 21.38 ?  213 ILE A CD1   1 
ATOM   1676 N  N     . PRO A 1 234 ? 38.328 -4.875  26.439  1.00 22.65 ?  214 PRO A N     1 
ATOM   1677 C  CA    . PRO A 1 234 ? 37.424 -5.495  27.426  1.00 19.66 ?  214 PRO A CA    1 
ATOM   1678 C  C     . PRO A 1 234 ? 36.055 -4.837  27.560  1.00 24.75 ?  214 PRO A C     1 
ATOM   1679 O  O     . PRO A 1 234 ? 35.421 -4.929  28.615  1.00 27.58 ?  214 PRO A O     1 
ATOM   1680 C  CB    . PRO A 1 234 ? 38.210 -5.364  28.735  1.00 18.04 ?  214 PRO A CB    1 
ATOM   1681 C  CG    . PRO A 1 234 ? 39.106 -4.212  28.524  1.00 20.06 ?  214 PRO A CG    1 
ATOM   1682 C  CD    . PRO A 1 234 ? 39.497 -4.239  27.069  1.00 25.22 ?  214 PRO A CD    1 
ATOM   1683 N  N     . LEU A 1 235 ? 35.590 -4.153  26.515  1.00 23.70 ?  215 LEU A N     1 
ATOM   1684 C  CA    . LEU A 1 235 ? 34.277 -3.542  26.583  1.00 17.11 ?  215 LEU A CA    1 
ATOM   1685 C  C     . LEU A 1 235 ? 33.213 -4.574  26.913  1.00 23.85 ?  215 LEU A C     1 
ATOM   1686 O  O     . LEU A 1 235 ? 32.271 -4.282  27.656  1.00 26.51 ?  215 LEU A O     1 
ATOM   1687 C  CB    . LEU A 1 235 ? 33.955 -2.839  25.271  1.00 21.49 ?  215 LEU A CB    1 
ATOM   1688 C  CG    . LEU A 1 235 ? 32.824 -1.815  25.376  1.00 26.05 ?  215 LEU A CG    1 
ATOM   1689 C  CD1   . LEU A 1 235 ? 33.142 -0.732  26.446  1.00 20.57 ?  215 LEU A CD1   1 
ATOM   1690 C  CD2   . LEU A 1 235 ? 32.531 -1.192  24.005  1.00 26.82 ?  215 LEU A CD2   1 
ATOM   1691 N  N     . PHE A 1 236 ? 33.348 -5.798  26.390  1.00 24.42 ?  216 PHE A N     1 
ATOM   1692 C  CA    . PHE A 1 236 ? 32.322 -6.793  26.680  1.00 23.96 ?  216 PHE A CA    1 
ATOM   1693 C  C     . PHE A 1 236 ? 32.253 -7.089  28.172  1.00 26.07 ?  216 PHE A C     1 
ATOM   1694 O  O     . PHE A 1 236 ? 31.173 -7.408  28.681  1.00 29.61 ?  216 PHE A O     1 
ATOM   1695 C  CB    . PHE A 1 236 ? 32.521 -8.073  25.845  1.00 22.06 ?  216 PHE A CB    1 
ATOM   1696 C  CG    . PHE A 1 236 ? 33.720 -8.900  26.214  1.00 20.33 ?  216 PHE A CG    1 
ATOM   1697 C  CD1   . PHE A 1 236 ? 33.624 -9.897  27.176  1.00 19.35 ?  216 PHE A CD1   1 
ATOM   1698 C  CD2   . PHE A 1 236 ? 34.932 -8.718  25.552  1.00 18.84 ?  216 PHE A CD2   1 
ATOM   1699 C  CE1   . PHE A 1 236 ? 34.727 -10.682 27.494  1.00 24.44 ?  216 PHE A CE1   1 
ATOM   1700 C  CE2   . PHE A 1 236 ? 36.035 -9.483  25.857  1.00 16.70 ?  216 PHE A CE2   1 
ATOM   1701 C  CZ    . PHE A 1 236 ? 35.940 -10.478 26.831  1.00 23.25 ?  216 PHE A CZ    1 
ATOM   1702 N  N     . VAL A 1 237 ? 33.369 -6.931  28.896  1.00 25.36 ?  217 VAL A N     1 
ATOM   1703 C  CA    . VAL A 1 237 ? 33.352 -7.094  30.353  1.00 26.62 ?  217 VAL A CA    1 
ATOM   1704 C  C     . VAL A 1 237 ? 32.445 -6.040  30.995  1.00 32.15 ?  217 VAL A C     1 
ATOM   1705 O  O     . VAL A 1 237 ? 31.684 -6.337  31.926  1.00 34.10 ?  217 VAL A O     1 
ATOM   1706 C  CB    . VAL A 1 237 ? 34.791 -7.040  30.917  1.00 22.61 ?  217 VAL A CB    1 
ATOM   1707 C  CG1   . VAL A 1 237 ? 34.820 -7.287  32.428  1.00 22.76 ?  217 VAL A CG1   1 
ATOM   1708 C  CG2   . VAL A 1 237 ? 35.682 -8.030  30.217  1.00 21.32 ?  217 VAL A CG2   1 
ATOM   1709 N  N     . VAL A 1 238 ? 32.516 -4.792  30.509  1.00 28.41 ?  218 VAL A N     1 
ATOM   1710 C  CA    . VAL A 1 238 ? 31.567 -3.769  30.939  1.00 26.02 ?  218 VAL A CA    1 
ATOM   1711 C  C     . VAL A 1 238 ? 30.144 -4.252  30.722  1.00 29.16 ?  218 VAL A C     1 
ATOM   1712 O  O     . VAL A 1 238 ? 29.316 -4.228  31.639  1.00 29.54 ?  218 VAL A O     1 
ATOM   1713 C  CB    . VAL A 1 238 ? 31.823 -2.447  30.198  1.00 25.04 ?  218 VAL A CB    1 
ATOM   1714 C  CG1   . VAL A 1 238 ? 30.681 -1.483  30.442  1.00 24.06 ?  218 VAL A CG1   1 
ATOM   1715 C  CG2   . VAL A 1 238 ? 33.141 -1.841  30.644  1.00 25.42 ?  218 VAL A CG2   1 
ATOM   1716 N  N     . ASP A 1 239 ? 29.845 -4.698  29.497  1.00 26.52 ?  219 ASP A N     1 
ATOM   1717 C  CA    . ASP A 1 239 ? 28.504 -5.166  29.154  1.00 27.94 ?  219 ASP A CA    1 
ATOM   1718 C  C     . ASP A 1 239 ? 28.001 -6.194  30.157  1.00 34.49 ?  219 ASP A C     1 
ATOM   1719 O  O     . ASP A 1 239 ? 26.906 -6.058  30.716  1.00 35.53 ?  219 ASP A O     1 
ATOM   1720 C  CB    . ASP A 1 239 ? 28.505 -5.778  27.748  1.00 30.42 ?  219 ASP A CB    1 
ATOM   1721 C  CG    . ASP A 1 239 ? 28.477 -4.733  26.638  1.00 30.38 ?  219 ASP A CG    1 
ATOM   1722 O  OD1   . ASP A 1 239 ? 27.833 -3.680  26.811  1.00 33.44 ?  219 ASP A OD1   1 
ATOM   1723 O  OD2   . ASP A 1 239 ? 29.099 -4.970  25.584  1.00 26.11 ?  219 ASP A OD2   1 
ATOM   1724 N  N     . VAL A 1 240 ? 28.807 -7.233  30.397  1.00 34.14 ?  220 VAL A N     1 
ATOM   1725 C  CA    . VAL A 1 240 ? 28.372 -8.371  31.195  1.00 32.23 ?  220 VAL A CA    1 
ATOM   1726 C  C     . VAL A 1 240 ? 27.989 -7.919  32.598  1.00 32.75 ?  220 VAL A C     1 
ATOM   1727 O  O     . VAL A 1 240 ? 26.954 -8.321  33.143  1.00 32.61 ?  220 VAL A O     1 
ATOM   1728 C  CB    . VAL A 1 240 ? 29.481 -9.443  31.207  1.00 25.98 ?  220 VAL A CB    1 
ATOM   1729 C  CG1   . VAL A 1 240 ? 29.059 -10.646 32.002  1.00 32.43 ?  220 VAL A CG1   1 
ATOM   1730 C  CG2   . VAL A 1 240 ? 29.766 -9.892  29.815  1.00 29.51 ?  220 VAL A CG2   1 
ATOM   1731 N  N     . LYS A 1 241 ? 28.811 -7.060  33.194  1.00 34.17 ?  221 LYS A N     1 
ATOM   1732 C  CA    . LYS A 1 241 ? 28.558 -6.595  34.553  1.00 36.61 ?  221 LYS A CA    1 
ATOM   1733 C  C     . LYS A 1 241 ? 27.413 -5.584  34.576  1.00 33.71 ?  221 LYS A C     1 
ATOM   1734 O  O     . LYS A 1 241 ? 26.518 -5.667  35.423  1.00 32.92 ?  221 LYS A O     1 
ATOM   1735 C  CB    . LYS A 1 241 ? 29.857 -6.004  35.106  1.00 28.69 ?  221 LYS A CB    1 
ATOM   1736 C  CG    . LYS A 1 241 ? 29.818 -5.257  36.434  1.00 39.79 ?  221 LYS A CG    1 
ATOM   1737 C  CD    . LYS A 1 241 ? 28.785 -5.749  37.448  1.00 42.06 ?  221 LYS A CD    1 
ATOM   1738 C  CE    . LYS A 1 241 ? 29.228 -6.931  38.277  1.00 56.52 ?  221 LYS A CE    1 
ATOM   1739 N  NZ    . LYS A 1 241 ? 28.044 -7.669  38.838  1.00 60.82 ?  221 LYS A NZ    1 
ATOM   1740 N  N     . LEU A 1 242 ? 27.395 -4.657  33.619  1.00 33.29 ?  222 LEU A N     1 
ATOM   1741 C  CA    . LEU A 1 242 ? 26.438 -3.559  33.649  1.00 35.30 ?  222 LEU A CA    1 
ATOM   1742 C  C     . LEU A 1 242 ? 25.031 -4.004  33.236  1.00 34.85 ?  222 LEU A C     1 
ATOM   1743 O  O     . LEU A 1 242 ? 24.058 -3.690  33.924  1.00 35.85 ?  222 LEU A O     1 
ATOM   1744 C  CB    . LEU A 1 242 ? 26.941 -2.414  32.767  1.00 24.83 ?  222 LEU A CB    1 
ATOM   1745 C  CG    . LEU A 1 242 ? 26.200 -1.075  32.818  1.00 32.25 ?  222 LEU A CG    1 
ATOM   1746 C  CD1   . LEU A 1 242 ? 26.086 -0.533  34.239  1.00 29.99 ?  222 LEU A CD1   1 
ATOM   1747 C  CD2   . LEU A 1 242 ? 26.903 -0.061  31.912  1.00 26.04 ?  222 LEU A CD2   1 
ATOM   1748 N  N     . TRP A 1 243 ? 24.882 -4.738  32.126  1.00 32.58 ?  223 TRP A N     1 
ATOM   1749 C  CA    . TRP A 1 243 ? 23.512 -5.018  31.692  1.00 30.82 ?  223 TRP A CA    1 
ATOM   1750 C  C     . TRP A 1 243 ? 23.236 -6.445  31.224  1.00 33.48 ?  223 TRP A C     1 
ATOM   1751 O  O     . TRP A 1 243 ? 22.087 -6.884  31.344  1.00 28.86 ?  223 TRP A O     1 
ATOM   1752 C  CB    . TRP A 1 243 ? 23.089 -4.043  30.583  1.00 33.35 ?  223 TRP A CB    1 
ATOM   1753 C  CG    . TRP A 1 243 ? 23.960 -4.038  29.365  1.00 31.44 ?  223 TRP A CG    1 
ATOM   1754 C  CD1   . TRP A 1 243 ? 24.971 -3.171  29.094  1.00 27.69 ?  223 TRP A CD1   1 
ATOM   1755 C  CD2   . TRP A 1 243 ? 23.873 -4.925  28.240  1.00 27.28 ?  223 TRP A CD2   1 
ATOM   1756 N  NE1   . TRP A 1 243 ? 25.528 -3.464  27.868  1.00 32.45 ?  223 TRP A NE1   1 
ATOM   1757 C  CE2   . TRP A 1 243 ? 24.875 -4.538  27.325  1.00 25.31 ?  223 TRP A CE2   1 
ATOM   1758 C  CE3   . TRP A 1 243 ? 23.048 -6.005  27.918  1.00 28.40 ?  223 TRP A CE3   1 
ATOM   1759 C  CZ2   . TRP A 1 243 ? 25.088 -5.200  26.120  1.00 24.13 ?  223 TRP A CZ2   1 
ATOM   1760 C  CZ3   . TRP A 1 243 ? 23.260 -6.661  26.709  1.00 35.36 ?  223 TRP A CZ3   1 
ATOM   1761 C  CH2   . TRP A 1 243 ? 24.273 -6.252  25.828  1.00 26.28 ?  223 TRP A CH2   1 
ATOM   1762 N  N     . LEU A 1 244 ? 24.212 -7.195  30.707  1.00 33.23 ?  224 LEU A N     1 
ATOM   1763 C  CA    . LEU A 1 244 ? 23.892 -8.531  30.204  1.00 32.59 ?  224 LEU A CA    1 
ATOM   1764 C  C     . LEU A 1 244 ? 23.776 -9.552  31.336  1.00 35.61 ?  224 LEU A C     1 
ATOM   1765 O  O     . LEU A 1 244 ? 22.770 -10.264 31.432  1.00 39.28 ?  224 LEU A O     1 
ATOM   1766 C  CB    . LEU A 1 244 ? 24.928 -8.977  29.171  1.00 25.02 ?  224 LEU A CB    1 
ATOM   1767 C  CG    . LEU A 1 244 ? 24.681 -10.329 28.504  1.00 32.82 ?  224 LEU A CG    1 
ATOM   1768 C  CD1   . LEU A 1 244 ? 23.454 -10.339 27.583  1.00 30.28 ?  224 LEU A CD1   1 
ATOM   1769 C  CD2   . LEU A 1 244 ? 25.917 -10.764 27.743  1.00 39.81 ?  224 LEU A CD2   1 
ATOM   1770 N  N     . GLY A 1 245 ? 24.788 -9.643  32.195  1.00 33.70 ?  225 GLY A N     1 
ATOM   1771 C  CA    . GLY A 1 245 ? 24.706 -10.550 33.337  1.00 36.59 ?  225 GLY A CA    1 
ATOM   1772 C  C     . GLY A 1 245 ? 24.480 -11.998 32.928  1.00 38.71 ?  225 GLY A C     1 
ATOM   1773 O  O     . GLY A 1 245 ? 25.193 -12.548 32.076  1.00 39.59 ?  225 GLY A O     1 
ATOM   1774 N  N     . ASN A 1 246 ? 23.471 -12.630 33.550  1.00 39.82 ?  226 ASN A N     1 
ATOM   1775 C  CA    . ASN A 1 246 ? 23.083 -14.015 33.282  1.00 36.44 ?  226 ASN A CA    1 
ATOM   1776 C  C     . ASN A 1 246 ? 21.673 -14.109 32.709  1.00 37.97 ?  226 ASN A C     1 
ATOM   1777 O  O     . ASN A 1 246 ? 20.960 -15.079 32.970  1.00 44.22 ?  226 ASN A O     1 
ATOM   1778 C  CB    . ASN A 1 246 ? 23.189 -14.876 34.545  1.00 28.56 ?  226 ASN A CB    1 
ATOM   1779 C  CG    . ASN A 1 246 ? 22.242 -14.424 35.673  1.00 42.52 ?  226 ASN A CG    1 
ATOM   1780 O  OD1   . ASN A 1 246 ? 21.385 -13.545 35.494  1.00 36.44 ?  226 ASN A OD1   1 
ATOM   1781 N  ND2   . ASN A 1 246 ? 22.401 -15.042 36.852  1.00 36.67 ?  226 ASN A ND2   1 
ATOM   1782 N  N     . HIS A 1 247 ? 21.252 -13.106 31.937  1.00 43.65 ?  227 HIS A N     1 
ATOM   1783 C  CA    . HIS A 1 247 ? 19.857 -12.985 31.531  1.00 43.42 ?  227 HIS A CA    1 
ATOM   1784 C  C     . HIS A 1 247 ? 19.589 -13.451 30.108  1.00 49.78 ?  227 HIS A C     1 
ATOM   1785 O  O     . HIS A 1 247 ? 18.425 -13.689 29.758  1.00 54.08 ?  227 HIS A O     1 
ATOM   1786 C  CB    . HIS A 1 247 ? 19.392 -11.531 31.687  1.00 41.13 ?  227 HIS A CB    1 
ATOM   1787 C  CG    . HIS A 1 247 ? 19.559 -10.997 33.077  1.00 47.83 ?  227 HIS A CG    1 
ATOM   1788 N  ND1   . HIS A 1 247 ? 18.986 -11.597 34.178  1.00 48.65 ?  227 HIS A ND1   1 
ATOM   1789 C  CD2   . HIS A 1 247 ? 20.261 -9.937  33.551  1.00 44.40 ?  227 HIS A CD2   1 
ATOM   1790 C  CE1   . HIS A 1 247 ? 19.312 -10.920 35.267  1.00 45.06 ?  227 HIS A CE1   1 
ATOM   1791 N  NE2   . HIS A 1 247 ? 20.087 -9.910  34.912  1.00 41.71 ?  227 HIS A NE2   1 
ATOM   1792 N  N     . SER A 1 248 ? 20.623 -13.601 29.283  1.00 42.17 ?  228 SER A N     1 
ATOM   1793 C  CA    . SER A 1 248 ? 20.467 -14.025 27.895  1.00 40.11 ?  228 SER A CA    1 
ATOM   1794 C  C     . SER A 1 248 ? 21.326 -15.262 27.655  1.00 45.48 ?  228 SER A C     1 
ATOM   1795 O  O     . SER A 1 248 ? 22.283 -15.224 26.865  1.00 37.63 ?  228 SER A O     1 
ATOM   1796 C  CB    . SER A 1 248 ? 20.831 -12.889 26.945  1.00 45.97 ?  228 SER A CB    1 
ATOM   1797 O  OG    . SER A 1 248 ? 20.137 -11.709 27.316  1.00 41.25 ?  228 SER A OG    1 
ATOM   1798 N  N     . PRO A 1 249 ? 20.969 -16.391 28.288  1.00 40.51 ?  229 PRO A N     1 
ATOM   1799 C  CA    . PRO A 1 249 ? 21.886 -17.544 28.353  1.00 41.13 ?  229 PRO A CA    1 
ATOM   1800 C  C     . PRO A 1 249 ? 22.297 -18.125 27.012  1.00 39.28 ?  229 PRO A C     1 
ATOM   1801 O  O     . PRO A 1 249 ? 23.411 -18.649 26.904  1.00 49.09 ?  229 PRO A O     1 
ATOM   1802 C  CB    . PRO A 1 249 ? 21.093 -18.577 29.170  1.00 45.79 ?  229 PRO A CB    1 
ATOM   1803 C  CG    . PRO A 1 249 ? 19.671 -18.156 29.064  1.00 43.94 ?  229 PRO A CG    1 
ATOM   1804 C  CD    . PRO A 1 249 ? 19.689 -16.664 28.959  1.00 41.16 ?  229 PRO A CD    1 
ATOM   1805 N  N     . ASN A 1 250 ? 21.453 -18.085 25.988  1.00 32.39 ?  230 ASN A N     1 
ATOM   1806 C  CA    . ASN A 1 250 ? 21.841 -18.671 24.711  1.00 41.06 ?  230 ASN A CA    1 
ATOM   1807 C  C     . ASN A 1 250 ? 22.072 -17.618 23.627  1.00 44.22 ?  230 ASN A C     1 
ATOM   1808 O  O     . ASN A 1 250 ? 22.029 -17.941 22.435  1.00 37.56 ?  230 ASN A O     1 
ATOM   1809 C  CB    . ASN A 1 250 ? 20.808 -19.706 24.267  1.00 30.84 ?  230 ASN A CB    1 
ATOM   1810 C  CG    . ASN A 1 250 ? 20.721 -20.878 25.226  1.00 42.50 ?  230 ASN A CG    1 
ATOM   1811 O  OD1   . ASN A 1 250 ? 21.639 -21.703 25.312  1.00 41.11 ?  230 ASN A OD1   1 
ATOM   1812 N  ND2   . ASN A 1 250 ? 19.618 -20.955 25.965  1.00 45.67 ?  230 ASN A ND2   1 
ATOM   1813 N  N     . SER A 1 251 ? 22.342 -16.374 24.024  1.00 39.64 ?  231 SER A N     1 
ATOM   1814 C  CA    . SER A 1 251 ? 22.653 -15.311 23.084  1.00 32.09 ?  231 SER A CA    1 
ATOM   1815 C  C     . SER A 1 251 ? 23.842 -15.695 22.211  1.00 32.72 ?  231 SER A C     1 
ATOM   1816 O  O     . SER A 1 251 ? 24.654 -16.543 22.569  1.00 35.65 ?  231 SER A O     1 
ATOM   1817 C  CB    . SER A 1 251 ? 22.958 -14.014 23.836  1.00 29.53 ?  231 SER A CB    1 
ATOM   1818 O  OG    . SER A 1 251 ? 23.125 -12.947 22.914  1.00 45.99 ?  231 SER A OG    1 
ATOM   1819 N  N     . GLU A 1 252 ? 23.942 -15.053 21.041  1.00 33.80 ?  232 GLU A N     1 
ATOM   1820 C  CA    . GLU A 1 252 ? 25.187 -15.140 20.285  1.00 32.46 ?  232 GLU A CA    1 
ATOM   1821 C  C     . GLU A 1 252 ? 26.244 -14.223 20.895  1.00 34.11 ?  232 GLU A C     1 
ATOM   1822 O  O     . GLU A 1 252 ? 27.450 -14.493 20.799  1.00 28.47 ?  232 GLU A O     1 
ATOM   1823 C  CB    . GLU A 1 252 ? 24.935 -14.813 18.805  1.00 34.65 ?  232 GLU A CB    1 
ATOM   1824 C  CG    . GLU A 1 252 ? 26.086 -14.136 18.070  1.00 39.65 ?  232 GLU A CG    1 
ATOM   1825 C  CD    . GLU A 1 252 ? 25.983 -14.208 16.526  1.00 62.05 ?  232 GLU A CD    1 
ATOM   1826 O  OE1   . GLU A 1 252 ? 26.438 -15.233 15.949  1.00 58.47 ?  232 GLU A OE1   1 
ATOM   1827 O  OE2   . GLU A 1 252 ? 25.498 -13.230 15.889  1.00 59.31 ?  232 GLU A OE2   1 
ATOM   1828 N  N     . TYR A 1 253 ? 25.803 -13.164 21.574  1.00 34.53 ?  233 TYR A N     1 
ATOM   1829 C  CA    . TYR A 1 253 ? 26.733 -12.334 22.332  1.00 29.26 ?  233 TYR A CA    1 
ATOM   1830 C  C     . TYR A 1 253 ? 27.420 -13.134 23.444  1.00 31.09 ?  233 TYR A C     1 
ATOM   1831 O  O     . TYR A 1 253 ? 28.620 -12.966 23.687  1.00 31.06 ?  233 TYR A O     1 
ATOM   1832 C  CB    . TYR A 1 253 ? 25.992 -11.118 22.891  1.00 23.54 ?  233 TYR A CB    1 
ATOM   1833 C  CG    . TYR A 1 253 ? 26.910 -10.010 23.339  1.00 27.88 ?  233 TYR A CG    1 
ATOM   1834 C  CD1   . TYR A 1 253 ? 28.153 -9.831  22.727  1.00 24.39 ?  233 TYR A CD1   1 
ATOM   1835 C  CD2   . TYR A 1 253 ? 26.556 -9.161  24.394  1.00 26.62 ?  233 TYR A CD2   1 
ATOM   1836 C  CE1   . TYR A 1 253 ? 29.011 -8.838  23.134  1.00 23.56 ?  233 TYR A CE1   1 
ATOM   1837 C  CE2   . TYR A 1 253 ? 27.414 -8.164  24.812  1.00 27.64 ?  233 TYR A CE2   1 
ATOM   1838 C  CZ    . TYR A 1 253 ? 28.642 -8.011  24.175  1.00 25.74 ?  233 TYR A CZ    1 
ATOM   1839 O  OH    . TYR A 1 253 ? 29.507 -7.024  24.570  1.00 26.10 ?  233 TYR A OH    1 
ATOM   1840 N  N     . VAL A 1 254 ? 26.683 -14.021 24.118  1.00 30.08 ?  234 VAL A N     1 
ATOM   1841 C  CA    . VAL A 1 254 ? 27.270 -14.796 25.212  1.00 31.33 ?  234 VAL A CA    1 
ATOM   1842 C  C     . VAL A 1 254 ? 28.264 -15.828 24.679  1.00 32.38 ?  234 VAL A C     1 
ATOM   1843 O  O     . VAL A 1 254 ? 29.234 -16.187 25.367  1.00 30.44 ?  234 VAL A O     1 
ATOM   1844 C  CB    . VAL A 1 254 ? 26.148 -15.444 26.054  1.00 28.46 ?  234 VAL A CB    1 
ATOM   1845 C  CG1   . VAL A 1 254 ? 26.686 -16.497 26.974  1.00 22.82 ?  234 VAL A CG1   1 
ATOM   1846 C  CG2   . VAL A 1 254 ? 25.408 -14.381 26.839  1.00 31.23 ?  234 VAL A CG2   1 
ATOM   1847 N  N     . SER A 1 255 ? 28.058 -16.310 23.449  1.00 31.32 ?  235 SER A N     1 
ATOM   1848 C  CA    . SER A 1 255 ? 29.012 -17.241 22.855  1.00 28.90 ?  235 SER A CA    1 
ATOM   1849 C  C     . SER A 1 255 ? 30.320 -16.537 22.495  1.00 32.06 ?  235 SER A C     1 
ATOM   1850 O  O     . SER A 1 255 ? 31.408 -17.079 22.734  1.00 28.49 ?  235 SER A O     1 
ATOM   1851 C  CB    . SER A 1 255 ? 28.393 -17.902 21.628  1.00 33.08 ?  235 SER A CB    1 
ATOM   1852 O  OG    . SER A 1 255 ? 28.757 -19.262 21.548  1.00 45.26 ?  235 SER A OG    1 
ATOM   1853 N  N     . PHE A 1 256 ? 30.227 -15.328 21.925  1.00 26.56 ?  236 PHE A N     1 
ATOM   1854 C  CA    . PHE A 1 256 ? 31.413 -14.513 21.669  1.00 28.73 ?  236 PHE A CA    1 
ATOM   1855 C  C     . PHE A 1 256 ? 32.177 -14.213 22.963  1.00 28.21 ?  236 PHE A C     1 
ATOM   1856 O  O     . PHE A 1 256 ? 33.412 -14.296 23.013  1.00 26.60 ?  236 PHE A O     1 
ATOM   1857 C  CB    . PHE A 1 256 ? 30.987 -13.217 20.973  1.00 24.25 ?  236 PHE A CB    1 
ATOM   1858 C  CG    . PHE A 1 256 ? 32.063 -12.164 20.910  1.00 23.81 ?  236 PHE A CG    1 
ATOM   1859 C  CD1   . PHE A 1 256 ? 32.190 -11.213 21.919  1.00 20.58 ?  236 PHE A CD1   1 
ATOM   1860 C  CD2   . PHE A 1 256 ? 32.917 -12.090 19.809  1.00 20.12 ?  236 PHE A CD2   1 
ATOM   1861 C  CE1   . PHE A 1 256 ? 33.181 -10.242 21.853  1.00 20.70 ?  236 PHE A CE1   1 
ATOM   1862 C  CE2   . PHE A 1 256 ? 33.891 -11.114 19.727  1.00 17.25 ?  236 PHE A CE2   1 
ATOM   1863 C  CZ    . PHE A 1 256 ? 34.029 -10.189 20.743  1.00 22.05 ?  236 PHE A CZ    1 
ATOM   1864 N  N     . ILE A 1 257 ? 31.460 -13.828 24.015  1.00 23.59 ?  237 ILE A N     1 
ATOM   1865 C  CA    . ILE A 1 257 ? 32.114 -13.585 25.294  1.00 27.63 ?  237 ILE A CA    1 
ATOM   1866 C  C     . ILE A 1 257 ? 32.756 -14.868 25.802  1.00 24.85 ?  237 ILE A C     1 
ATOM   1867 O  O     . ILE A 1 257 ? 33.923 -14.884 26.213  1.00 21.74 ?  237 ILE A O     1 
ATOM   1868 C  CB    . ILE A 1 257 ? 31.105 -13.015 26.306  1.00 23.26 ?  237 ILE A CB    1 
ATOM   1869 C  CG1   . ILE A 1 257 ? 30.573 -11.682 25.782  1.00 20.76 ?  237 ILE A CG1   1 
ATOM   1870 C  CG2   . ILE A 1 257 ? 31.742 -12.900 27.693  1.00 18.38 ?  237 ILE A CG2   1 
ATOM   1871 C  CD1   . ILE A 1 257 ? 29.377 -11.202 26.515  1.00 25.46 ?  237 ILE A CD1   1 
ATOM   1872 N  N     . LYS A 1 258 ? 32.000 -15.964 25.769  1.00 25.95 ?  238 LYS A N     1 
ATOM   1873 C  CA    . LYS A 1 258 ? 32.542 -17.269 26.134  1.00 24.30 ?  238 LYS A CA    1 
ATOM   1874 C  C     . LYS A 1 258 ? 33.832 -17.571 25.379  1.00 22.29 ?  238 LYS A C     1 
ATOM   1875 O  O     . LYS A 1 258 ? 34.805 -18.051 25.966  1.00 21.81 ?  238 LYS A O     1 
ATOM   1876 C  CB    . LYS A 1 258 ? 31.490 -18.348 25.868  1.00 27.69 ?  238 LYS A CB    1 
ATOM   1877 C  CG    . LYS A 1 258 ? 31.941 -19.765 26.168  1.00 24.80 ?  238 LYS A CG    1 
ATOM   1878 C  CD    . LYS A 1 258 ? 31.914 -20.605 24.903  1.00 30.20 ?  238 LYS A CD    1 
ATOM   1879 C  CE    . LYS A 1 258 ? 30.489 -20.862 24.498  1.00 31.90 ?  238 LYS A CE    1 
ATOM   1880 N  NZ    . LYS A 1 258 ? 30.396 -21.800 23.367  1.00 30.66 ?  238 LYS A NZ    1 
ATOM   1881 N  N     . ASP A 1 259 ? 33.875 -17.269 24.080  1.00 26.54 ?  239 ASP A N     1 
ATOM   1882 C  CA    . ASP A 1 259 ? 35.099 -17.510 23.328  1.00 24.63 ?  239 ASP A CA    1 
ATOM   1883 C  C     . ASP A 1 259 ? 36.191 -16.496 23.644  1.00 25.24 ?  239 ASP A C     1 
ATOM   1884 O  O     . ASP A 1 259 ? 37.359 -16.757 23.349  1.00 26.03 ?  239 ASP A O     1 
ATOM   1885 C  CB    . ASP A 1 259 ? 34.803 -17.525 21.829  1.00 23.61 ?  239 ASP A CB    1 
ATOM   1886 C  CG    . ASP A 1 259 ? 33.909 -18.698 21.417  1.00 27.06 ?  239 ASP A CG    1 
ATOM   1887 O  OD1   . ASP A 1 259 ? 33.973 -19.765 22.067  1.00 30.88 ?  239 ASP A OD1   1 
ATOM   1888 O  OD2   . ASP A 1 259 ? 33.145 -18.556 20.434  1.00 32.12 ?  239 ASP A OD2   1 
ATOM   1889 N  N     . SER A 1 260 ? 35.844 -15.363 24.262  1.00 26.44 ?  240 SER A N     1 
ATOM   1890 C  CA    . SER A 1 260 ? 36.793 -14.282 24.517  1.00 27.27 ?  240 SER A CA    1 
ATOM   1891 C  C     . SER A 1 260 ? 37.460 -14.368 25.886  1.00 25.49 ?  240 SER A C     1 
ATOM   1892 O  O     . SER A 1 260 ? 38.587 -13.876 26.042  1.00 23.71 ?  240 SER A O     1 
ATOM   1893 C  CB    . SER A 1 260 ? 36.086 -12.925 24.408  1.00 28.73 ?  240 SER A CB    1 
ATOM   1894 O  OG    . SER A 1 260 ? 35.486 -12.708 23.135  1.00 21.72 ?  240 SER A OG    1 
ATOM   1895 N  N     . VAL A 1 261 ? 36.777 -14.983 26.865  1.00 22.69 ?  241 VAL A N     1 
ATOM   1896 C  CA    . VAL A 1 261 ? 37.216 -14.986 28.265  1.00 21.74 ?  241 VAL A CA    1 
ATOM   1897 C  C     . VAL A 1 261 ? 38.709 -15.288 28.378  1.00 22.69 ?  241 VAL A C     1 
ATOM   1898 O  O     . VAL A 1 261 ? 39.461 -14.569 29.048  1.00 19.86 ?  241 VAL A O     1 
ATOM   1899 C  CB    . VAL A 1 261 ? 36.372 -15.990 29.081  1.00 26.91 ?  241 VAL A CB    1 
ATOM   1900 C  CG1   . VAL A 1 261 ? 37.010 -16.304 30.424  1.00 18.91 ?  241 VAL A CG1   1 
ATOM   1901 C  CG2   . VAL A 1 261 ? 34.964 -15.476 29.278  1.00 22.59 ?  241 VAL A CG2   1 
ATOM   1902 N  N     . PHE A 1 262 ? 39.176 -16.335 27.706  1.00 22.22 ?  242 PHE A N     1 
ATOM   1903 C  CA    . PHE A 1 262 ? 40.558 -16.729 27.945  1.00 23.11 ?  242 PHE A CA    1 
ATOM   1904 C  C     . PHE A 1 262 ? 41.558 -16.032 27.028  1.00 21.55 ?  242 PHE A C     1 
ATOM   1905 O  O     . PHE A 1 262 ? 42.766 -16.264 27.158  1.00 19.06 ?  242 PHE A O     1 
ATOM   1906 C  CB    . PHE A 1 262 ? 40.661 -18.249 27.905  1.00 15.99 ?  242 PHE A CB    1 
ATOM   1907 C  CG    . PHE A 1 262 ? 40.061 -18.873 29.130  1.00 22.78 ?  242 PHE A CG    1 
ATOM   1908 C  CD1   . PHE A 1 262 ? 40.783 -18.925 30.320  1.00 22.75 ?  242 PHE A CD1   1 
ATOM   1909 C  CD2   . PHE A 1 262 ? 38.736 -19.272 29.142  1.00 20.05 ?  242 PHE A CD2   1 
ATOM   1910 C  CE1   . PHE A 1 262 ? 40.224 -19.429 31.462  1.00 17.71 ?  242 PHE A CE1   1 
ATOM   1911 C  CE2   . PHE A 1 262 ? 38.170 -19.778 30.296  1.00 22.74 ?  242 PHE A CE2   1 
ATOM   1912 C  CZ    . PHE A 1 262 ? 38.923 -19.867 31.455  1.00 19.15 ?  242 PHE A CZ    1 
ATOM   1913 N  N     . TYR A 1 263 ? 41.096 -15.119 26.178  1.00 18.47 ?  243 TYR A N     1 
ATOM   1914 C  CA    . TYR A 1 263 ? 42.005 -14.216 25.488  1.00 22.50 ?  243 TYR A CA    1 
ATOM   1915 C  C     . TYR A 1 263 ? 42.350 -12.996 26.330  1.00 20.53 ?  243 TYR A C     1 
ATOM   1916 O  O     . TYR A 1 263 ? 43.450 -12.447 26.187  1.00 20.31 ?  243 TYR A O     1 
ATOM   1917 C  CB    . TYR A 1 263 ? 41.412 -13.755 24.146  1.00 20.23 ?  243 TYR A CB    1 
ATOM   1918 C  CG    . TYR A 1 263 ? 41.534 -14.752 23.008  1.00 21.95 ?  243 TYR A CG    1 
ATOM   1919 C  CD1   . TYR A 1 263 ? 40.795 -15.937 23.002  1.00 18.79 ?  243 TYR A CD1   1 
ATOM   1920 C  CD2   . TYR A 1 263 ? 42.381 -14.510 21.939  1.00 17.96 ?  243 TYR A CD2   1 
ATOM   1921 C  CE1   . TYR A 1 263 ? 40.888 -16.817 21.976  1.00 12.47 ?  243 TYR A CE1   1 
ATOM   1922 C  CE2   . TYR A 1 263 ? 42.478 -15.393 20.909  1.00 15.61 ?  243 TYR A CE2   1 
ATOM   1923 C  CZ    . TYR A 1 263 ? 41.723 -16.543 20.920  1.00 18.54 ?  243 TYR A CZ    1 
ATOM   1924 O  OH    . TYR A 1 263 ? 41.827 -17.443 19.859  1.00 23.37 ?  243 TYR A OH    1 
ATOM   1925 N  N     . LEU A 1 264 ? 41.430 -12.564 27.193  1.00 20.38 ?  244 LEU A N     1 
ATOM   1926 C  CA    . LEU A 1 264 ? 41.691 -11.465 28.108  1.00 18.76 ?  244 LEU A CA    1 
ATOM   1927 C  C     . LEU A 1 264 ? 42.922 -11.755 28.960  1.00 19.04 ?  244 LEU A C     1 
ATOM   1928 O  O     . LEU A 1 264 ? 43.221 -12.914 29.245  1.00 19.02 ?  244 LEU A O     1 
ATOM   1929 C  CB    . LEU A 1 264 ? 40.504 -11.254 29.042  1.00 19.74 ?  244 LEU A CB    1 
ATOM   1930 C  CG    . LEU A 1 264 ? 39.247 -10.590 28.509  1.00 21.95 ?  244 LEU A CG    1 
ATOM   1931 C  CD1   . LEU A 1 264 ? 38.134 -10.845 29.507  1.00 19.09 ?  244 LEU A CD1   1 
ATOM   1932 C  CD2   . LEU A 1 264 ? 39.497 -9.082  28.260  1.00 17.48 ?  244 LEU A CD2   1 
ATOM   1933 N  N     . PRO A 1 265 ? 43.639 -10.721 29.395  1.00 28.55 ?  245 PRO A N     1 
ATOM   1934 C  CA    . PRO A 1 265 ? 44.636 -10.901 30.475  1.00 25.26 ?  245 PRO A CA    1 
ATOM   1935 C  C     . PRO A 1 265 ? 44.009 -11.594 31.671  1.00 22.20 ?  245 PRO A C     1 
ATOM   1936 O  O     . PRO A 1 265 ? 42.808 -11.419 31.938  1.00 18.73 ?  245 PRO A O     1 
ATOM   1937 C  CB    . PRO A 1 265 ? 45.056 -9.462  30.813  1.00 17.78 ?  245 PRO A CB    1 
ATOM   1938 C  CG    . PRO A 1 265 ? 44.869 -8.731  29.489  1.00 23.90 ?  245 PRO A CG    1 
ATOM   1939 C  CD    . PRO A 1 265 ? 43.649 -9.353  28.840  1.00 21.59 ?  245 PRO A CD    1 
ATOM   1940 N  N     . PRO A 1 266 ? 44.779 -12.417 32.388  1.00 18.79 ?  246 PRO A N     1 
ATOM   1941 C  CA    . PRO A 1 266 ? 44.199 -13.183 33.513  1.00 23.12 ?  246 PRO A CA    1 
ATOM   1942 C  C     . PRO A 1 266 ? 43.552 -12.311 34.566  1.00 22.11 ?  246 PRO A C     1 
ATOM   1943 O  O     . PRO A 1 266 ? 42.532 -12.710 35.147  1.00 22.37 ?  246 PRO A O     1 
ATOM   1944 C  CB    . PRO A 1 266 ? 45.402 -13.945 34.093  1.00 20.75 ?  246 PRO A CB    1 
ATOM   1945 C  CG    . PRO A 1 266 ? 46.459 -13.913 33.000  1.00 26.74 ?  246 PRO A CG    1 
ATOM   1946 C  CD    . PRO A 1 266 ? 46.220 -12.660 32.209  1.00 18.91 ?  246 PRO A CD    1 
ATOM   1947 N  N     . GLU A 1 267 ? 44.106 -11.116 34.795  1.00 28.39 ?  247 GLU A N     1 
ATOM   1948 C  CA    . GLU A 1 267 ? 43.568 -10.172 35.771  1.00 26.10 ?  247 GLU A CA    1 
ATOM   1949 C  C     . GLU A 1 267 ? 42.058 -9.933  35.584  1.00 25.24 ?  247 GLU A C     1 
ATOM   1950 O  O     . GLU A 1 267 ? 41.337 -9.716  36.565  1.00 36.10 ?  247 GLU A O     1 
ATOM   1951 C  CB    . GLU A 1 267 ? 44.365 -8.851  35.687  1.00 21.75 ?  247 GLU A CB    1 
ATOM   1952 C  CG    . GLU A 1 267 ? 45.949 -8.908  35.910  1.00 32.26 ?  247 GLU A CG    1 
ATOM   1953 C  CD    . GLU A 1 267 ? 46.779 -9.346  34.655  1.00 43.32 ?  247 GLU A CD    1 
ATOM   1954 O  OE1   . GLU A 1 267 ? 46.190 -10.102 33.854  1.00 40.64 ?  247 GLU A OE1   1 
ATOM   1955 O  OE2   . GLU A 1 267 ? 47.995 -8.950  34.457  1.00 33.79 ?  247 GLU A OE2   1 
ATOM   1956 N  N     . LEU A 1 268 ? 41.547 -10.022 34.351  1.00 25.13 ?  248 LEU A N     1 
ATOM   1957 C  CA    . LEU A 1 268 ? 40.153 -9.694  34.050  1.00 20.09 ?  248 LEU A CA    1 
ATOM   1958 C  C     . LEU A 1 268 ? 39.202 -10.894 34.021  1.00 20.81 ?  248 LEU A C     1 
ATOM   1959 O  O     . LEU A 1 268 ? 37.982 -10.699 34.029  1.00 17.37 ?  248 LEU A O     1 
ATOM   1960 C  CB    . LEU A 1 268 ? 40.069 -8.957  32.704  1.00 18.62 ?  248 LEU A CB    1 
ATOM   1961 C  CG    . LEU A 1 268 ? 40.487 -7.488  32.749  1.00 23.04 ?  248 LEU A CG    1 
ATOM   1962 C  CD1   . LEU A 1 268 ? 40.551 -6.908  31.360  1.00 24.29 ?  248 LEU A CD1   1 
ATOM   1963 C  CD2   . LEU A 1 268 ? 39.514 -6.691  33.629  1.00 23.83 ?  248 LEU A CD2   1 
ATOM   1964 N  N     . ARG A 1 269 ? 39.714 -12.115 33.997  1.00 23.40 ?  249 ARG A N     1 
ATOM   1965 C  CA    . ARG A 1 269 ? 38.888 -13.306 33.823  1.00 23.86 ?  249 ARG A CA    1 
ATOM   1966 C  C     . ARG A 1 269 ? 37.897 -13.580 34.965  1.00 24.02 ?  249 ARG A C     1 
ATOM   1967 O  O     . ARG A 1 269 ? 36.735 -13.916 34.691  1.00 23.43 ?  249 ARG A O     1 
ATOM   1968 C  CB    . ARG A 1 269 ? 39.806 -14.507 33.593  1.00 26.05 ?  249 ARG A CB    1 
ATOM   1969 C  CG    . ARG A 1 269 ? 40.778 -14.274 32.431  1.00 22.60 ?  249 ARG A CG    1 
ATOM   1970 C  CD    . ARG A 1 269 ? 41.598 -15.497 32.066  1.00 19.57 ?  249 ARG A CD    1 
ATOM   1971 N  NE    . ARG A 1 269 ? 42.597 -15.127 31.077  1.00 25.08 ?  249 ARG A NE    1 
ATOM   1972 C  CZ    . ARG A 1 269 ? 43.735 -15.768 30.850  1.00 22.83 ?  249 ARG A CZ    1 
ATOM   1973 N  NH1   . ARG A 1 269 ? 44.041 -16.880 31.490  1.00 20.52 ?  249 ARG A NH1   1 
ATOM   1974 N  NH2   . ARG A 1 269 ? 44.589 -15.275 29.956  1.00 18.77 ?  249 ARG A NH2   1 
ATOM   1975 N  N     . PRO A 1 270 ? 38.281 -13.453 36.245  1.00 22.92 ?  250 PRO A N     1 
ATOM   1976 C  CA    . PRO A 1 270 ? 37.281 -13.713 37.300  1.00 22.66 ?  250 PRO A CA    1 
ATOM   1977 C  C     . PRO A 1 270 ? 36.130 -12.714 37.327  1.00 27.19 ?  250 PRO A C     1 
ATOM   1978 O  O     . PRO A 1 270 ? 34.989 -13.122 37.585  1.00 29.35 ?  250 PRO A O     1 
ATOM   1979 C  CB    . PRO A 1 270 ? 38.115 -13.694 38.593  1.00 17.79 ?  250 PRO A CB    1 
ATOM   1980 C  CG    . PRO A 1 270 ? 39.527 -13.912 38.161  1.00 17.90 ?  250 PRO A CG    1 
ATOM   1981 C  CD    . PRO A 1 270 ? 39.635 -13.291 36.814  1.00 23.66 ?  250 PRO A CD    1 
ATOM   1982 N  N     . ILE A 1 271 ? 36.379 -11.422 37.067  1.00 26.28 ?  251 ILE A N     1 
ATOM   1983 C  CA    . ILE A 1 271 ? 35.284 -10.453 36.980  1.00 21.48 ?  251 ILE A CA    1 
ATOM   1984 C  C     . ILE A 1 271 ? 34.274 -10.899 35.943  1.00 28.06 ?  251 ILE A C     1 
ATOM   1985 O  O     . ILE A 1 271 ? 33.055 -10.902 36.179  1.00 23.20 ?  251 ILE A O     1 
ATOM   1986 C  CB    . ILE A 1 271 ? 35.815 -9.054  36.628  1.00 28.28 ?  251 ILE A CB    1 
ATOM   1987 C  CG1   . ILE A 1 271 ? 37.210 -8.835  37.212  1.00 38.74 ?  251 ILE A CG1   1 
ATOM   1988 C  CG2   . ILE A 1 271 ? 34.816 -7.994  37.072  1.00 37.82 ?  251 ILE A CG2   1 
ATOM   1989 C  CD1   . ILE A 1 271 ? 37.733 -7.417  36.990  1.00 49.92 ?  251 ILE A CD1   1 
ATOM   1990 N  N     . CYS A 1 272 ? 34.790 -11.273 34.767  1.00 28.09 ?  252 CYS A N     1 
ATOM   1991 C  CA    . CYS A 1 272 ? 33.966 -11.651 33.634  1.00 23.36 ?  252 CYS A CA    1 
ATOM   1992 C  C     . CYS A 1 272 ? 33.199 -12.935 33.909  1.00 24.24 ?  252 CYS A C     1 
ATOM   1993 O  O     . CYS A 1 272 ? 32.001 -13.029 33.606  1.00 25.55 ?  252 CYS A O     1 
ATOM   1994 C  CB    . CYS A 1 272 ? 34.861 -11.792 32.403  1.00 32.98 ?  252 CYS A CB    1 
ATOM   1995 S  SG    . CYS A 1 272 ? 33.970 -11.970 30.878  1.00 27.32 ?  252 CYS A SG    1 
ATOM   1996 N  N     . VAL A 1 273 ? 33.866 -13.930 34.496  1.00 24.49 ?  253 VAL A N     1 
ATOM   1997 C  CA    . VAL A 1 273 ? 33.169 -15.168 34.832  1.00 25.83 ?  253 VAL A CA    1 
ATOM   1998 C  C     . VAL A 1 273 ? 32.109 -14.906 35.891  1.00 27.88 ?  253 VAL A C     1 
ATOM   1999 O  O     . VAL A 1 273 ? 30.980 -15.392 35.778  1.00 31.63 ?  253 VAL A O     1 
ATOM   2000 C  CB    . VAL A 1 273 ? 34.153 -16.258 35.294  1.00 22.97 ?  253 VAL A CB    1 
ATOM   2001 C  CG1   . VAL A 1 273 ? 33.368 -17.435 35.871  1.00 19.90 ?  253 VAL A CG1   1 
ATOM   2002 C  CG2   . VAL A 1 273 ? 35.034 -16.706 34.161  1.00 20.02 ?  253 VAL A CG2   1 
ATOM   2003 N  N     . ASP A 1 274 ? 32.452 -14.146 36.938  1.00 18.44 ?  254 ASP A N     1 
ATOM   2004 C  CA    . ASP A 1 274 ? 31.461 -13.827 37.956  1.00 22.88 ?  254 ASP A CA    1 
ATOM   2005 C  C     . ASP A 1 274 ? 30.253 -13.143 37.340  1.00 31.23 ?  254 ASP A C     1 
ATOM   2006 O  O     . ASP A 1 274 ? 29.102 -13.478 37.645  1.00 34.71 ?  254 ASP A O     1 
ATOM   2007 C  CB    . ASP A 1 274 ? 32.055 -12.915 39.028  1.00 33.03 ?  254 ASP A CB    1 
ATOM   2008 C  CG    . ASP A 1 274 ? 33.119 -13.583 39.850  1.00 35.05 ?  254 ASP A CG    1 
ATOM   2009 O  OD1   . ASP A 1 274 ? 33.405 -14.780 39.621  1.00 36.12 ?  254 ASP A OD1   1 
ATOM   2010 O  OD2   . ASP A 1 274 ? 33.690 -12.880 40.712  1.00 42.84 ?  254 ASP A OD2   1 
ATOM   2011 N  N     . SER A 1 275 ? 30.498 -12.160 36.481  1.00 25.09 ?  255 SER A N     1 
ATOM   2012 C  CA    . SER A 1 275 ? 29.394 -11.343 36.002  1.00 32.46 ?  255 SER A CA    1 
ATOM   2013 C  C     . SER A 1 275 ? 28.456 -12.157 35.114  1.00 32.34 ?  255 SER A C     1 
ATOM   2014 O  O     . SER A 1 275 ? 27.233 -11.971 35.164  1.00 31.92 ?  255 SER A O     1 
ATOM   2015 C  CB    . SER A 1 275 ? 29.950 -10.108 35.284  1.00 32.39 ?  255 SER A CB    1 
ATOM   2016 O  OG    . SER A 1 275 ? 31.004 -9.511  36.032  1.00 28.25 ?  255 SER A OG    1 
ATOM   2017 N  N     . LEU A 1 276 ? 29.013 -13.077 34.307  1.00 36.20 ?  256 LEU A N     1 
ATOM   2018 C  CA    . LEU A 1 276 ? 28.207 -13.984 33.489  1.00 28.27 ?  256 LEU A CA    1 
ATOM   2019 C  C     . LEU A 1 276 ? 27.309 -14.885 34.327  1.00 29.33 ?  256 LEU A C     1 
ATOM   2020 O  O     . LEU A 1 276 ? 26.318 -15.405 33.809  1.00 35.28 ?  256 LEU A O     1 
ATOM   2021 C  CB    . LEU A 1 276 ? 29.113 -14.862 32.623  1.00 24.39 ?  256 LEU A CB    1 
ATOM   2022 C  CG    . LEU A 1 276 ? 29.685 -14.253 31.342  1.00 32.31 ?  256 LEU A CG    1 
ATOM   2023 C  CD1   . LEU A 1 276 ? 30.832 -15.116 30.820  1.00 21.64 ?  256 LEU A CD1   1 
ATOM   2024 C  CD2   . LEU A 1 276 ? 28.597 -14.069 30.292  1.00 22.81 ?  256 LEU A CD2   1 
ATOM   2025 N  N     . LEU A 1 277 ? 27.656 -15.113 35.590  1.00 22.97 ?  257 LEU A N     1 
ATOM   2026 C  CA    . LEU A 1 277 ? 26.925 -16.026 36.447  1.00 31.59 ?  257 LEU A CA    1 
ATOM   2027 C  C     . LEU A 1 277 ? 26.047 -15.302 37.453  1.00 30.41 ?  257 LEU A C     1 
ATOM   2028 O  O     . LEU A 1 277 ? 25.414 -15.950 38.280  1.00 35.28 ?  257 LEU A O     1 
ATOM   2029 C  CB    . LEU A 1 277 ? 27.895 -16.952 37.177  1.00 25.23 ?  257 LEU A CB    1 
ATOM   2030 C  CG    . LEU A 1 277 ? 28.350 -18.246 36.502  1.00 23.47 ?  257 LEU A CG    1 
ATOM   2031 C  CD1   . LEU A 1 277 ? 27.899 -18.326 35.031  1.00 24.67 ?  257 LEU A CD1   1 
ATOM   2032 C  CD2   . LEU A 1 277 ? 29.859 -18.383 36.637  1.00 17.92 ?  257 LEU A CD2   1 
ATOM   2033 N  N     . GLU A 1 278 ? 25.976 -13.983 37.380  1.00 31.38 ?  258 GLU A N     1 
ATOM   2034 C  CA    . GLU A 1 278 ? 25.293 -13.149 38.352  1.00 35.60 ?  258 GLU A CA    1 
ATOM   2035 C  C     . GLU A 1 278 ? 24.363 -12.180 37.635  1.00 40.81 ?  258 GLU A C     1 
ATOM   2036 O  O     . GLU A 1 278 ? 24.624 -11.802 36.486  1.00 40.40 ?  258 GLU A O     1 
ATOM   2037 C  CB    . GLU A 1 278 ? 26.312 -12.363 39.198  1.00 33.34 ?  258 GLU A CB    1 
ATOM   2038 C  CG    . GLU A 1 278 ? 26.973 -13.192 40.305  1.00 35.89 ?  258 GLU A CG    1 
ATOM   2039 C  CD    . GLU A 1 278 ? 28.231 -12.559 40.912  1.00 28.57 ?  258 GLU A CD    1 
ATOM   2040 O  OE1   . GLU A 1 278 ? 28.556 -11.394 40.615  1.00 37.40 ?  258 GLU A OE1   1 
ATOM   2041 O  OE2   . GLU A 1 278 ? 28.905 -13.243 41.701  1.00 29.84 ?  258 GLU A OE2   1 
ATOM   2042 N  N     . PRO A 1 279 ? 23.261 -11.778 38.274  1.00 44.76 ?  259 PRO A N     1 
ATOM   2043 C  CA    . PRO A 1 279 ? 22.428 -10.721 37.688  1.00 40.67 ?  259 PRO A CA    1 
ATOM   2044 C  C     . PRO A 1 279 ? 23.217 -9.429  37.571  1.00 36.21 ?  259 PRO A C     1 
ATOM   2045 O  O     . PRO A 1 279 ? 24.062 -9.120  38.412  1.00 38.24 ?  259 PRO A O     1 
ATOM   2046 C  CB    . PRO A 1 279 ? 21.267 -10.582 38.680  1.00 35.61 ?  259 PRO A CB    1 
ATOM   2047 C  CG    . PRO A 1 279 ? 21.692 -11.324 39.884  1.00 33.91 ?  259 PRO A CG    1 
ATOM   2048 C  CD    . PRO A 1 279 ? 22.634 -12.375 39.462  1.00 28.25 ?  259 PRO A CD    1 
ATOM   2049 N  N     . SER A 1 280 ? 22.925 -8.676  36.511  1.00 34.79 ?  260 SER A N     1 
ATOM   2050 C  CA    . SER A 1 280 ? 23.627 -7.433  36.205  1.00 34.40 ?  260 SER A CA    1 
ATOM   2051 C  C     . SER A 1 280 ? 23.292 -6.317  37.199  1.00 33.40 ?  260 SER A C     1 
ATOM   2052 O  O     . SER A 1 280 ? 22.270 -6.336  37.888  1.00 37.16 ?  260 SER A O     1 
ATOM   2053 C  CB    . SER A 1 280 ? 23.278 -6.958  34.798  1.00 35.63 ?  260 SER A CB    1 
ATOM   2054 O  OG    . SER A 1 280 ? 21.923 -6.533  34.738  1.00 40.61 ?  260 SER A OG    1 
ATOM   2055 N  N     . VAL A 1 281 ? 24.182 -5.323  37.245  1.00 29.85 ?  261 VAL A N     1 
ATOM   2056 C  CA    . VAL A 1 281 ? 23.973 -4.147  38.086  1.00 31.57 ?  261 VAL A CA    1 
ATOM   2057 C  C     . VAL A 1 281 ? 22.620 -3.507  37.789  1.00 36.95 ?  261 VAL A C     1 
ATOM   2058 O  O     . VAL A 1 281 ? 21.817 -3.255  38.694  1.00 41.00 ?  261 VAL A O     1 
ATOM   2059 C  CB    . VAL A 1 281 ? 25.118 -3.139  37.881  1.00 36.87 ?  261 VAL A CB    1 
ATOM   2060 C  CG1   . VAL A 1 281 ? 24.758 -1.790  38.487  1.00 32.55 ?  261 VAL A CG1   1 
ATOM   2061 C  CG2   . VAL A 1 281 ? 26.416 -3.659  38.449  1.00 26.75 ?  261 VAL A CG2   1 
ATOM   2062 N  N     . ILE A 1 282 ? 22.349 -3.230  36.511  1.00 35.26 ?  262 ILE A N     1 
ATOM   2063 C  CA    . ILE A 1 282 ? 21.112 -2.539  36.156  1.00 36.46 ?  262 ILE A CA    1 
ATOM   2064 C  C     . ILE A 1 282 ? 19.899 -3.366  36.558  1.00 37.82 ?  262 ILE A C     1 
ATOM   2065 O  O     . ILE A 1 282 ? 18.927 -2.828  37.101  1.00 42.19 ?  262 ILE A O     1 
ATOM   2066 C  CB    . ILE A 1 282 ? 21.095 -2.190  34.658  1.00 25.64 ?  262 ILE A CB    1 
ATOM   2067 C  CG1   . ILE A 1 282 ? 21.809 -0.867  34.439  1.00 29.54 ?  262 ILE A CG1   1 
ATOM   2068 C  CG2   . ILE A 1 282 ? 19.668 -2.078  34.140  1.00 29.19 ?  262 ILE A CG2   1 
ATOM   2069 C  CD1   . ILE A 1 282 ? 22.556 -0.790  33.095  1.00 37.25 ?  262 ILE A CD1   1 
ATOM   2070 N  N     . ASN A 1 283 ? 19.938 -4.684  36.323  1.00 36.97 ?  263 ASN A N     1 
ATOM   2071 C  CA    . ASN A 1 283 ? 18.804 -5.533  36.696  1.00 40.75 ?  263 ASN A CA    1 
ATOM   2072 C  C     . ASN A 1 283 ? 18.523 -5.477  38.199  1.00 38.33 ?  263 ASN A C     1 
ATOM   2073 O  O     . ASN A 1 283 ? 17.361 -5.408  38.612  1.00 40.08 ?  263 ASN A O     1 
ATOM   2074 C  CB    . ASN A 1 283 ? 19.038 -6.977  36.242  1.00 37.44 ?  263 ASN A CB    1 
ATOM   2075 C  CG    . ASN A 1 283 ? 18.166 -7.986  37.005  1.00 44.98 ?  263 ASN A CG    1 
ATOM   2076 O  OD1   . ASN A 1 283 ? 18.512 -8.399  38.117  1.00 43.94 ?  263 ASN A OD1   1 
ATOM   2077 N  ND2   . ASN A 1 283 ? 17.043 -8.393  36.405  1.00 35.36 ?  263 ASN A ND2   1 
ATOM   2078 N  N     . GLN A 1 284 ? 19.567 -5.506  39.032  1.00 33.83 ?  264 GLN A N     1 
ATOM   2079 C  CA    . GLN A 1 284 ? 19.359 -5.343  40.467  1.00 38.87 ?  264 GLN A CA    1 
ATOM   2080 C  C     . GLN A 1 284 ? 18.870 -3.939  40.789  1.00 46.88 ?  264 GLN A C     1 
ATOM   2081 O  O     . GLN A 1 284 ? 17.887 -3.766  41.518  1.00 51.40 ?  264 GLN A O     1 
ATOM   2082 C  CB    . GLN A 1 284 ? 20.645 -5.621  41.248  1.00 42.11 ?  264 GLN A CB    1 
ATOM   2083 C  CG    . GLN A 1 284 ? 21.281 -6.963  41.023  1.00 44.38 ?  264 GLN A CG    1 
ATOM   2084 C  CD    . GLN A 1 284 ? 22.794 -6.877  41.153  1.00 55.66 ?  264 GLN A CD    1 
ATOM   2085 O  OE1   . GLN A 1 284 ? 23.322 -5.962  41.804  1.00 57.67 ?  264 GLN A OE1   1 
ATOM   2086 N  NE2   . GLN A 1 284 ? 23.504 -7.815  40.519  1.00 46.39 ?  264 GLN A NE2   1 
ATOM   2087 N  N     . LYS A 1 285 ? 19.559 -2.917  40.267  1.00 46.00 ?  265 LYS A N     1 
ATOM   2088 C  CA    . LYS A 1 285 ? 19.162 -1.539  40.541  1.00 40.07 ?  265 LYS A CA    1 
ATOM   2089 C  C     . LYS A 1 285 ? 17.773 -1.239  39.995  1.00 39.10 ?  265 LYS A C     1 
ATOM   2090 O  O     . LYS A 1 285 ? 17.078 -0.366  40.521  1.00 45.22 ?  265 LYS A O     1 
ATOM   2091 C  CB    . LYS A 1 285 ? 20.189 -0.570  39.964  1.00 32.83 ?  265 LYS A CB    1 
ATOM   2092 C  CG    . LYS A 1 285 ? 21.496 -0.500  40.738  1.00 32.28 ?  265 LYS A CG    1 
ATOM   2093 C  CD    . LYS A 1 285 ? 21.305 -0.865  42.203  1.00 41.27 ?  265 LYS A CD    1 
ATOM   2094 C  CE    . LYS A 1 285 ? 22.606 -0.745  42.986  1.00 38.60 ?  265 LYS A CE    1 
ATOM   2095 N  NZ    . LYS A 1 285 ? 22.488 -1.288  44.380  1.00 42.64 ?  265 LYS A NZ    1 
ATOM   2096 N  N     . PHE A 1 286 ? 17.350 -1.945  38.945  1.00 38.96 ?  266 PHE A N     1 
ATOM   2097 C  CA    . PHE A 1 286 ? 15.955 -1.875  38.530  1.00 39.01 ?  266 PHE A CA    1 
ATOM   2098 C  C     . PHE A 1 286 ? 15.036 -2.359  39.636  1.00 47.73 ?  266 PHE A C     1 
ATOM   2099 O  O     . PHE A 1 286 ? 13.918 -1.848  39.784  1.00 53.12 ?  266 PHE A O     1 
ATOM   2100 C  CB    . PHE A 1 286 ? 15.720 -2.710  37.273  1.00 30.96 ?  266 PHE A CB    1 
ATOM   2101 C  CG    . PHE A 1 286 ? 15.879 -1.947  36.001  1.00 36.18 ?  266 PHE A CG    1 
ATOM   2102 C  CD1   . PHE A 1 286 ? 16.231 -0.610  36.020  1.00 34.17 ?  266 PHE A CD1   1 
ATOM   2103 C  CD2   . PHE A 1 286 ? 15.667 -2.568  34.780  1.00 32.37 ?  266 PHE A CD2   1 
ATOM   2104 C  CE1   . PHE A 1 286 ? 16.374 0.093   34.846  1.00 41.79 ?  266 PHE A CE1   1 
ATOM   2105 C  CE2   . PHE A 1 286 ? 15.814 -1.881  33.601  1.00 37.11 ?  266 PHE A CE2   1 
ATOM   2106 C  CZ    . PHE A 1 286 ? 16.163 -0.547  33.627  1.00 46.89 ?  266 PHE A CZ    1 
ATOM   2107 N  N     . ALA A 1 287 ? 15.487 -3.344  40.419  1.00 40.67 ?  267 ALA A N     1 
ATOM   2108 C  CA    . ALA A 1 287 ? 14.654 -3.895  41.480  1.00 45.30 ?  267 ALA A CA    1 
ATOM   2109 C  C     . ALA A 1 287 ? 14.657 -2.985  42.697  1.00 51.04 ?  267 ALA A C     1 
ATOM   2110 O  O     . ALA A 1 287 ? 13.599 -2.673  43.256  1.00 54.04 ?  267 ALA A O     1 
ATOM   2111 C  CB    . ALA A 1 287 ? 15.130 -5.296  41.864  1.00 33.37 ?  267 ALA A CB    1 
ATOM   2112 N  N     . GLU A 1 288 ? 15.843 -2.551  43.117  1.00 45.68 ?  268 GLU A N     1 
ATOM   2113 C  CA    . GLU A 1 288 ? 15.937 -1.716  44.301  1.00 38.95 ?  268 GLU A CA    1 
ATOM   2114 C  C     . GLU A 1 288 ? 15.144 -0.433  44.106  1.00 47.29 ?  268 GLU A C     1 
ATOM   2115 O  O     . GLU A 1 288 ? 14.470 0.037   45.030  1.00 47.80 ?  268 GLU A O     1 
ATOM   2116 C  CB    . GLU A 1 288 ? 17.408 -1.429  44.602  1.00 40.03 ?  268 GLU A CB    1 
ATOM   2117 C  CG    . GLU A 1 288 ? 17.696 -0.055  45.173  1.00 43.45 ?  268 GLU A CG    1 
ATOM   2118 C  CD    . GLU A 1 288 ? 19.122 0.070   45.681  1.00 48.17 ?  268 GLU A CD    1 
ATOM   2119 O  OE1   . GLU A 1 288 ? 19.734 -0.973  46.025  1.00 55.33 ?  268 GLU A OE1   1 
ATOM   2120 O  OE2   . GLU A 1 288 ? 19.618 1.216   45.775  1.00 49.66 ?  268 GLU A OE2   1 
ATOM   2121 N  N     . PHE A 1 289 ? 15.167 0.110   42.883  1.00 49.23 ?  269 PHE A N     1 
ATOM   2122 C  CA    . PHE A 1 289 ? 14.431 1.332   42.566  1.00 46.87 ?  269 PHE A CA    1 
ATOM   2123 C  C     . PHE A 1 289 ? 12.931 1.161   42.802  1.00 51.38 ?  269 PHE A C     1 
ATOM   2124 O  O     . PHE A 1 289 ? 12.291 2.000   43.447  1.00 53.61 ?  269 PHE A O     1 
ATOM   2125 C  CB    . PHE A 1 289 ? 14.717 1.709   41.123  1.00 42.43 ?  269 PHE A CB    1 
ATOM   2126 C  CG    . PHE A 1 289 ? 14.235 3.067   40.720  1.00 42.75 ?  269 PHE A CG    1 
ATOM   2127 C  CD1   . PHE A 1 289 ? 15.082 4.161   40.778  1.00 44.39 ?  269 PHE A CD1   1 
ATOM   2128 C  CD2   . PHE A 1 289 ? 12.961 3.238   40.203  1.00 49.66 ?  269 PHE A CD2   1 
ATOM   2129 C  CE1   . PHE A 1 289 ? 14.655 5.408   40.364  1.00 47.88 ?  269 PHE A CE1   1 
ATOM   2130 C  CE2   . PHE A 1 289 ? 12.527 4.487   39.785  1.00 49.92 ?  269 PHE A CE2   1 
ATOM   2131 C  CZ    . PHE A 1 289 ? 13.374 5.571   39.863  1.00 46.26 ?  269 PHE A CZ    1 
ATOM   2132 N  N     . GLY A 1 290 ? 12.353 0.077   42.296  1.00 45.24 ?  270 GLY A N     1 
ATOM   2133 C  CA    . GLY A 1 290 ? 10.948 -0.190  42.540  1.00 48.10 ?  270 GLY A CA    1 
ATOM   2134 C  C     . GLY A 1 290 ? 10.652 -0.857  43.873  1.00 55.16 ?  270 GLY A C     1 
ATOM   2135 O  O     . GLY A 1 290 ? 9.774  -1.722  43.949  1.00 63.69 ?  270 GLY A O     1 
ATOM   2136 N  N     . SER A 1 291 ? 11.361 -0.469  44.935  1.00 46.79 ?  271 SER A N     1 
ATOM   2137 C  CA    . SER A 1 291 ? 11.171 -1.114  46.229  1.00 45.39 ?  271 SER A CA    1 
ATOM   2138 C  C     . SER A 1 291 ? 11.732 -0.284  47.372  1.00 49.67 ?  271 SER A C     1 
ATOM   2139 O  O     . SER A 1 291 ? 11.759 -0.741  48.520  1.00 57.81 ?  271 SER A O     1 
ATOM   2140 C  CB    . SER A 1 291 ? 11.818 -2.497  46.248  1.00 41.68 ?  271 SER A CB    1 
ATOM   2141 O  OG    . SER A 1 291 ? 10.993 -3.429  45.563  1.00 60.16 ?  271 SER A OG    1 
ATOM   2142 N  N     . VAL A 1 292 ? 12.192 0.932   47.080  1.00 47.38 ?  272 VAL A N     1 
ATOM   2143 C  CA    . VAL A 1 292 ? 12.721 1.811   48.111  1.00 48.56 ?  272 VAL A CA    1 
ATOM   2144 C  C     . VAL A 1 292 ? 12.197 3.217   47.872  1.00 49.13 ?  272 VAL A C     1 
ATOM   2145 O  O     . VAL A 1 292 ? 11.681 3.547   46.800  1.00 51.90 ?  272 VAL A O     1 
ATOM   2146 C  CB    . VAL A 1 292 ? 14.270 1.831   48.182  1.00 50.18 ?  272 VAL A CB    1 
ATOM   2147 C  CG1   . VAL A 1 292 ? 14.837 0.430   48.470  1.00 49.43 ?  272 VAL A CG1   1 
ATOM   2148 C  CG2   . VAL A 1 292 ? 14.872 2.468   46.944  1.00 44.32 ?  272 VAL A CG2   1 
ATOM   2149 N  N     . GLU A 1 293 ? 12.331 4.041   48.907  1.00 55.75 ?  273 GLU A N     1 
ATOM   2150 C  CA    . GLU A 1 293 ? 11.850 5.411   48.872  1.00 61.81 ?  273 GLU A CA    1 
ATOM   2151 C  C     . GLU A 1 293 ? 12.603 6.184   47.796  1.00 55.90 ?  273 GLU A C     1 
ATOM   2152 O  O     . GLU A 1 293 ? 13.757 6.580   47.990  1.00 56.06 ?  273 GLU A O     1 
ATOM   2153 C  CB    . GLU A 1 293 ? 12.003 6.052   50.255  1.00 62.84 ?  273 GLU A CB    1 
ATOM   2154 C  CG    . GLU A 1 293 ? 11.172 7.312   50.473  1.00 66.32 ?  273 GLU A CG    1 
ATOM   2155 C  CD    . GLU A 1 293 ? 11.848 8.274   51.439  1.00 75.75 ?  273 GLU A CD    1 
ATOM   2156 O  OE1   . GLU A 1 293 ? 12.813 7.851   52.114  1.00 73.96 ?  273 GLU A OE1   1 
ATOM   2157 O  OE2   . GLU A 1 293 ? 11.425 9.449   51.518  1.00 69.54 ?  273 GLU A OE2   1 
ATOM   2158 N  N     . ILE A 1 294 ? 11.955 6.390   46.654  1.00 48.64 ?  274 ILE A N     1 
ATOM   2159 C  CA    . ILE A 1 294 ? 12.582 7.066   45.527  1.00 52.30 ?  274 ILE A CA    1 
ATOM   2160 C  C     . ILE A 1 294 ? 12.847 8.522   45.907  1.00 51.83 ?  274 ILE A C     1 
ATOM   2161 O  O     . ILE A 1 294 ? 11.946 9.365   45.851  1.00 55.21 ?  274 ILE A O     1 
ATOM   2162 C  CB    . ILE A 1 294 ? 11.702 6.922   44.268  1.00 52.87 ?  274 ILE A CB    1 
ATOM   2163 C  CG1   . ILE A 1 294 ? 11.926 5.537   43.652  1.00 52.60 ?  274 ILE A CG1   1 
ATOM   2164 C  CG2   . ILE A 1 294 ? 12.044 7.972   43.212  1.00 53.62 ?  274 ILE A CG2   1 
ATOM   2165 C  CD1   . ILE A 1 294 ? 10.687 4.888   43.089  1.00 58.68 ?  274 ILE A CD1   1 
ATOM   2166 N  N     . THR A 1 295 ? 14.080 8.815   46.343  1.00 53.34 ?  275 THR A N     1 
ATOM   2167 C  CA    . THR A 1 295 ? 14.491 10.160  46.731  1.00 49.99 ?  275 THR A CA    1 
ATOM   2168 C  C     . THR A 1 295 ? 15.010 10.929  45.512  1.00 57.23 ?  275 THR A C     1 
ATOM   2169 O  O     . THR A 1 295 ? 14.814 10.531  44.360  1.00 60.57 ?  275 THR A O     1 
ATOM   2170 C  CB    . THR A 1 295 ? 15.567 10.120  47.818  1.00 54.69 ?  275 THR A CB    1 
ATOM   2171 O  OG1   . THR A 1 295 ? 16.622 9.238   47.420  1.00 60.98 ?  275 THR A OG1   1 
ATOM   2172 C  CG2   . THR A 1 295 ? 14.995 9.658   49.156  1.00 52.17 ?  275 THR A CG2   1 
ATOM   2173 N  N     . ASP A 1 296 ? 15.686 12.052  45.756  1.00 54.56 ?  276 ASP A N     1 
ATOM   2174 C  CA    . ASP A 1 296 ? 16.284 12.794  44.653  1.00 52.89 ?  276 ASP A CA    1 
ATOM   2175 C  C     . ASP A 1 296 ? 17.627 12.205  44.269  1.00 54.03 ?  276 ASP A C     1 
ATOM   2176 O  O     . ASP A 1 296 ? 18.009 12.241  43.095  1.00 48.51 ?  276 ASP A O     1 
ATOM   2177 C  CB    . ASP A 1 296 ? 16.458 14.267  45.024  1.00 52.45 ?  276 ASP A CB    1 
ATOM   2178 C  CG    . ASP A 1 296 ? 15.289 15.132  44.574  1.00 58.84 ?  276 ASP A CG    1 
ATOM   2179 O  OD1   . ASP A 1 296 ? 14.352 14.598  43.946  1.00 53.49 ?  276 ASP A OD1   1 
ATOM   2180 O  OD2   . ASP A 1 296 ? 15.301 16.346  44.873  1.00 64.85 ?  276 ASP A OD2   1 
ATOM   2181 N  N     . GLN A 1 297 ? 18.350 11.665  45.249  1.00 49.28 ?  277 GLN A N     1 
ATOM   2182 C  CA    . GLN A 1 297 ? 19.633 11.043  44.967  1.00 50.27 ?  277 GLN A CA    1 
ATOM   2183 C  C     . GLN A 1 297 ? 19.456 9.722   44.232  1.00 54.06 ?  277 GLN A C     1 
ATOM   2184 O  O     . GLN A 1 297 ? 20.328 9.328   43.448  1.00 47.71 ?  277 GLN A O     1 
ATOM   2185 C  CB    . GLN A 1 297 ? 20.403 10.841  46.272  1.00 48.07 ?  277 GLN A CB    1 
ATOM   2186 C  CG    . GLN A 1 297 ? 21.834 10.405  46.074  1.00 52.22 ?  277 GLN A CG    1 
ATOM   2187 C  CD    . GLN A 1 297 ? 22.634 11.415  45.291  1.00 50.68 ?  277 GLN A CD    1 
ATOM   2188 O  OE1   . GLN A 1 297 ? 22.953 12.494  45.787  1.00 51.91 ?  277 GLN A OE1   1 
ATOM   2189 N  NE2   . GLN A 1 297 ? 22.942 11.078  44.044  1.00 42.98 ?  277 GLN A NE2   1 
ATOM   2190 N  N     . VAL A 1 298 ? 18.331 9.037   44.465  1.00 50.97 ?  278 VAL A N     1 
ATOM   2191 C  CA    . VAL A 1 298 ? 18.086 7.747   43.828  1.00 45.04 ?  278 VAL A CA    1 
ATOM   2192 C  C     . VAL A 1 298 ? 17.897 7.935   42.328  1.00 50.05 ?  278 VAL A C     1 
ATOM   2193 O  O     . VAL A 1 298 ? 18.338 7.107   41.521  1.00 50.61 ?  278 VAL A O     1 
ATOM   2194 C  CB    . VAL A 1 298 ? 16.873 7.054   44.490  1.00 43.06 ?  278 VAL A CB    1 
ATOM   2195 C  CG1   . VAL A 1 298 ? 16.173 6.086   43.537  1.00 39.77 ?  278 VAL A CG1   1 
ATOM   2196 C  CG2   . VAL A 1 298 ? 17.286 6.348   45.776  1.00 46.45 ?  278 VAL A CG2   1 
ATOM   2197 N  N     . ILE A 1 299 ? 17.271 9.044   41.930  1.00 45.94 ?  279 ILE A N     1 
ATOM   2198 C  CA    . ILE A 1 299 ? 17.062 9.311   40.511  1.00 47.21 ?  279 ILE A CA    1 
ATOM   2199 C  C     . ILE A 1 299 ? 18.361 9.762   39.845  1.00 48.42 ?  279 ILE A C     1 
ATOM   2200 O  O     . ILE A 1 299 ? 18.662 9.368   38.710  1.00 47.80 ?  279 ILE A O     1 
ATOM   2201 C  CB    . ILE A 1 299 ? 15.924 10.334  40.333  1.00 48.83 ?  279 ILE A CB    1 
ATOM   2202 C  CG1   . ILE A 1 299 ? 14.583 9.672   40.685  1.00 52.90 ?  279 ILE A CG1   1 
ATOM   2203 C  CG2   . ILE A 1 299 ? 15.938 10.925  38.934  1.00 40.69 ?  279 ILE A CG2   1 
ATOM   2204 C  CD1   . ILE A 1 299 ? 13.389 10.610  40.683  1.00 42.79 ?  279 ILE A CD1   1 
ATOM   2205 N  N     . LYS A 1 300 ? 19.152 10.588  40.532  1.00 44.99 ?  280 LYS A N     1 
ATOM   2206 C  CA    . LYS A 1 300 ? 20.495 10.880  40.042  1.00 41.40 ?  280 LYS A CA    1 
ATOM   2207 C  C     . LYS A 1 300 ? 21.298 9.594   39.862  1.00 41.77 ?  280 LYS A C     1 
ATOM   2208 O  O     . LYS A 1 300 ? 21.999 9.422   38.859  1.00 38.03 ?  280 LYS A O     1 
ATOM   2209 C  CB    . LYS A 1 300 ? 21.215 11.826  41.001  1.00 41.73 ?  280 LYS A CB    1 
ATOM   2210 C  CG    . LYS A 1 300 ? 20.742 13.269  40.962  1.00 41.59 ?  280 LYS A CG    1 
ATOM   2211 C  CD    . LYS A 1 300 ? 21.750 14.159  41.672  1.00 42.93 ?  280 LYS A CD    1 
ATOM   2212 C  CE    . LYS A 1 300 ? 21.283 15.598  41.801  1.00 49.52 ?  280 LYS A CE    1 
ATOM   2213 N  NZ    . LYS A 1 300 ? 22.383 16.474  42.322  1.00 45.51 ?  280 LYS A NZ    1 
ATOM   2214 N  N     . GLY A 1 301 ? 21.194 8.674   40.825  1.00 46.97 ?  281 GLY A N     1 
ATOM   2215 C  CA    . GLY A 1 301 ? 21.915 7.415   40.723  1.00 39.08 ?  281 GLY A CA    1 
ATOM   2216 C  C     . GLY A 1 301 ? 21.484 6.605   39.518  1.00 44.71 ?  281 GLY A C     1 
ATOM   2217 O  O     . GLY A 1 301 ? 22.317 6.091   38.769  1.00 43.50 ?  281 GLY A O     1 
ATOM   2218 N  N     . MET A 1 302 ? 20.170 6.493   39.305  1.00 42.19 ?  282 MET A N     1 
ATOM   2219 C  CA    . MET A 1 302 ? 19.680 5.762   38.143  1.00 35.96 ?  282 MET A CA    1 
ATOM   2220 C  C     . MET A 1 302 ? 19.946 6.531   36.861  1.00 42.27 ?  282 MET A C     1 
ATOM   2221 O  O     . MET A 1 302 ? 20.116 5.924   35.798  1.00 44.30 ?  282 MET A O     1 
ATOM   2222 C  CB    . MET A 1 302 ? 18.189 5.461   38.296  1.00 42.79 ?  282 MET A CB    1 
ATOM   2223 C  CG    . MET A 1 302 ? 17.541 4.763   37.109  1.00 41.18 ?  282 MET A CG    1 
ATOM   2224 S  SD    . MET A 1 302 ? 17.839 2.971   37.062  1.00 53.41 ?  282 MET A SD    1 
ATOM   2225 C  CE    . MET A 1 302 ? 17.257 2.394   38.656  1.00 31.35 ?  282 MET A CE    1 
ATOM   2226 N  N     . GLU A 1 303 ? 20.009 7.861   36.940  1.00 44.13 ?  283 GLU A N     1 
ATOM   2227 C  CA    . GLU A 1 303 ? 20.408 8.634   35.775  1.00 40.61 ?  283 GLU A CA    1 
ATOM   2228 C  C     . GLU A 1 303 ? 21.883 8.471   35.455  1.00 36.04 ?  283 GLU A C     1 
ATOM   2229 O  O     . GLU A 1 303 ? 22.270 8.650   34.298  1.00 35.34 ?  283 GLU A O     1 
ATOM   2230 C  CB    . GLU A 1 303 ? 20.066 10.112  35.968  1.00 44.69 ?  283 GLU A CB    1 
ATOM   2231 C  CG    . GLU A 1 303 ? 18.881 10.543  35.124  1.00 54.09 ?  283 GLU A CG    1 
ATOM   2232 C  CD    . GLU A 1 303 ? 18.061 11.639  35.767  1.00 65.60 ?  283 GLU A CD    1 
ATOM   2233 O  OE1   . GLU A 1 303 ? 18.518 12.222  36.786  1.00 53.64 ?  283 GLU A OE1   1 
ATOM   2234 O  OE2   . GLU A 1 303 ? 16.952 11.907  35.240  1.00 62.29 ?  283 GLU A OE2   1 
ATOM   2235 N  N     . SER A 1 304 ? 22.718 8.136   36.437  1.00 32.15 ?  284 SER A N     1 
ATOM   2236 C  CA    . SER A 1 304 ? 24.116 7.894   36.115  1.00 34.32 ?  284 SER A CA    1 
ATOM   2237 C  C     . SER A 1 304 ? 24.330 6.529   35.475  1.00 39.50 ?  284 SER A C     1 
ATOM   2238 O  O     . SER A 1 304 ? 25.351 6.324   34.811  1.00 39.19 ?  284 SER A O     1 
ATOM   2239 C  CB    . SER A 1 304 ? 24.988 8.041   37.361  1.00 34.28 ?  284 SER A CB    1 
ATOM   2240 O  OG    . SER A 1 304 ? 24.619 7.095   38.341  1.00 38.59 ?  284 SER A OG    1 
ATOM   2241 N  N     . LEU A 1 305 ? 23.382 5.602   35.636  1.00 31.63 ?  285 LEU A N     1 
ATOM   2242 C  CA    . LEU A 1 305 ? 23.464 4.343   34.910  1.00 33.86 ?  285 LEU A CA    1 
ATOM   2243 C  C     . LEU A 1 305 ? 23.132 4.545   33.441  1.00 38.28 ?  285 LEU A C     1 
ATOM   2244 O  O     . LEU A 1 305 ? 23.771 3.952   32.561  1.00 33.34 ?  285 LEU A O     1 
ATOM   2245 C  CB    . LEU A 1 305 ? 22.519 3.315   35.523  1.00 31.89 ?  285 LEU A CB    1 
ATOM   2246 C  CG    . LEU A 1 305 ? 23.098 2.658   36.757  1.00 31.51 ?  285 LEU A CG    1 
ATOM   2247 C  CD1   . LEU A 1 305 ? 22.076 1.702   37.358  1.00 26.71 ?  285 LEU A CD1   1 
ATOM   2248 C  CD2   . LEU A 1 305 ? 24.386 1.959   36.351  1.00 27.34 ?  285 LEU A CD2   1 
ATOM   2249 N  N     . LEU A 1 306 ? 22.121 5.369   33.165  1.00 34.90 ?  286 LEU A N     1 
ATOM   2250 C  CA    . LEU A 1 306 ? 21.739 5.640   31.789  1.00 36.00 ?  286 LEU A CA    1 
ATOM   2251 C  C     . LEU A 1 306 ? 22.788 6.499   31.091  1.00 37.04 ?  286 LEU A C     1 
ATOM   2252 O  O     . LEU A 1 306 ? 22.939 6.419   29.865  1.00 36.53 ?  286 LEU A O     1 
ATOM   2253 C  CB    . LEU A 1 306 ? 20.362 6.303   31.760  1.00 37.07 ?  286 LEU A CB    1 
ATOM   2254 C  CG    . LEU A 1 306 ? 19.939 7.048   30.499  1.00 35.68 ?  286 LEU A CG    1 
ATOM   2255 C  CD1   . LEU A 1 306 ? 19.519 6.042   29.455  1.00 39.56 ?  286 LEU A CD1   1 
ATOM   2256 C  CD2   . LEU A 1 306 ? 18.807 8.024   30.783  1.00 33.76 ?  286 LEU A CD2   1 
ATOM   2257 N  N     . SER A 1 307 ? 23.541 7.296   31.854  1.00 31.22 ?  287 SER A N     1 
ATOM   2258 C  CA    . SER A 1 307 ? 24.664 8.029   31.279  1.00 31.27 ?  287 SER A CA    1 
ATOM   2259 C  C     . SER A 1 307 ? 25.736 7.074   30.776  1.00 38.51 ?  287 SER A C     1 
ATOM   2260 O  O     . SER A 1 307 ? 26.274 7.253   29.678  1.00 36.32 ?  287 SER A O     1 
ATOM   2261 C  CB    . SER A 1 307 ? 25.254 8.990   32.307  1.00 25.44 ?  287 SER A CB    1 
ATOM   2262 O  OG    . SER A 1 307 ? 24.367 10.053  32.557  1.00 41.42 ?  287 SER A OG    1 
ATOM   2263 N  N     . VAL A 1 308 ? 26.074 6.056   31.579  1.00 33.33 ?  288 VAL A N     1 
ATOM   2264 C  CA    . VAL A 1 308 ? 27.070 5.084   31.141  1.00 35.12 ?  288 VAL A CA    1 
ATOM   2265 C  C     . VAL A 1 308 ? 26.610 4.396   29.866  1.00 30.20 ?  288 VAL A C     1 
ATOM   2266 O  O     . VAL A 1 308 ? 27.381 4.228   28.915  1.00 27.01 ?  288 VAL A O     1 
ATOM   2267 C  CB    . VAL A 1 308 ? 27.369 4.055   32.249  1.00 34.93 ?  288 VAL A CB    1 
ATOM   2268 C  CG1   . VAL A 1 308 ? 28.429 3.077   31.763  1.00 28.20 ?  288 VAL A CG1   1 
ATOM   2269 C  CG2   . VAL A 1 308 ? 27.839 4.737   33.513  1.00 29.63 ?  288 VAL A CG2   1 
ATOM   2270 N  N     . ILE A 1 309 ? 25.345 4.000   29.820  1.00 27.46 ?  289 ILE A N     1 
ATOM   2271 C  CA    . ILE A 1 309 ? 24.861 3.291   28.652  1.00 25.39 ?  289 ILE A CA    1 
ATOM   2272 C  C     . ILE A 1 309 ? 24.855 4.208   27.431  1.00 28.22 ?  289 ILE A C     1 
ATOM   2273 O  O     . ILE A 1 309 ? 25.189 3.780   26.319  1.00 32.21 ?  289 ILE A O     1 
ATOM   2274 C  CB    . ILE A 1 309 ? 23.482 2.680   28.956  1.00 29.42 ?  289 ILE A CB    1 
ATOM   2275 C  CG1   . ILE A 1 309 ? 23.667 1.439   29.822  1.00 29.82 ?  289 ILE A CG1   1 
ATOM   2276 C  CG2   . ILE A 1 309 ? 22.708 2.349   27.678  1.00 40.06 ?  289 ILE A CG2   1 
ATOM   2277 C  CD1   . ILE A 1 309 ? 23.828 0.157   29.045  1.00 33.73 ?  289 ILE A CD1   1 
ATOM   2278 N  N     . GLN A 1 310 ? 24.536 5.489   27.615  1.00 33.36 ?  290 GLN A N     1 
ATOM   2279 C  CA    . GLN A 1 310 ? 24.551 6.386   26.461  1.00 34.11 ?  290 GLN A CA    1 
ATOM   2280 C  C     . GLN A 1 310 ? 25.961 6.605   25.937  1.00 32.30 ?  290 GLN A C     1 
ATOM   2281 O  O     . GLN A 1 310 ? 26.140 6.778   24.727  1.00 36.81 ?  290 GLN A O     1 
ATOM   2282 C  CB    . GLN A 1 310 ? 23.887 7.713   26.802  1.00 31.43 ?  290 GLN A CB    1 
ATOM   2283 C  CG    . GLN A 1 310 ? 22.463 7.534   27.255  1.00 40.54 ?  290 GLN A CG    1 
ATOM   2284 C  CD    . GLN A 1 310 ? 21.788 8.832   27.627  1.00 43.31 ?  290 GLN A CD    1 
ATOM   2285 O  OE1   . GLN A 1 310 ? 20.605 9.030   27.331  1.00 37.15 ?  290 GLN A OE1   1 
ATOM   2286 N  NE2   . GLN A 1 310 ? 22.547 9.744   28.254  1.00 30.64 ?  290 GLN A NE2   1 
ATOM   2287 N  N     . VAL A 1 311 ? 26.972 6.558   26.811  1.00 30.52 ?  291 VAL A N     1 
ATOM   2288 C  CA    . VAL A 1 311 ? 28.357 6.606   26.342  1.00 26.38 ?  291 VAL A CA    1 
ATOM   2289 C  C     . VAL A 1 311 ? 28.689 5.365   25.515  1.00 31.41 ?  291 VAL A C     1 
ATOM   2290 O  O     . VAL A 1 311 ? 29.434 5.441   24.533  1.00 32.94 ?  291 VAL A O     1 
ATOM   2291 C  CB    . VAL A 1 311 ? 29.326 6.769   27.523  1.00 25.27 ?  291 VAL A CB    1 
ATOM   2292 C  CG1   . VAL A 1 311 ? 30.730 6.891   27.016  1.00 30.22 ?  291 VAL A CG1   1 
ATOM   2293 C  CG2   . VAL A 1 311 ? 28.966 7.990   28.336  1.00 32.61 ?  291 VAL A CG2   1 
ATOM   2294 N  N     . LEU A 1 312 ? 28.148 4.203   25.889  1.00 27.81 ?  292 LEU A N     1 
ATOM   2295 C  CA    . LEU A 1 312 ? 28.340 3.024   25.048  1.00 32.94 ?  292 LEU A CA    1 
ATOM   2296 C  C     . LEU A 1 312 ? 27.720 3.225   23.661  1.00 34.84 ?  292 LEU A C     1 
ATOM   2297 O  O     . LEU A 1 312 ? 28.289 2.796   22.646  1.00 27.52 ?  292 LEU A O     1 
ATOM   2298 C  CB    . LEU A 1 312 ? 27.755 1.778   25.725  1.00 28.31 ?  292 LEU A CB    1 
ATOM   2299 C  CG    . LEU A 1 312 ? 28.400 1.225   26.992  1.00 25.16 ?  292 LEU A CG    1 
ATOM   2300 C  CD1   . LEU A 1 312 ? 27.549 0.116   27.545  1.00 26.04 ?  292 LEU A CD1   1 
ATOM   2301 C  CD2   . LEU A 1 312 ? 29.805 0.740   26.726  1.00 24.14 ?  292 LEU A CD2   1 
ATOM   2302 N  N     . LEU A 1 313 ? 26.554 3.882   23.598  1.00 34.56 ?  293 LEU A N     1 
ATOM   2303 C  CA    . LEU A 1 313 ? 25.887 4.079   22.314  1.00 30.56 ?  293 LEU A CA    1 
ATOM   2304 C  C     . LEU A 1 313 ? 26.691 5.011   21.413  1.00 33.40 ?  293 LEU A C     1 
ATOM   2305 O  O     . LEU A 1 313 ? 26.833 4.754   20.208  1.00 32.97 ?  293 LEU A O     1 
ATOM   2306 C  CB    . LEU A 1 313 ? 24.483 4.623   22.541  1.00 25.03 ?  293 LEU A CB    1 
ATOM   2307 C  CG    . LEU A 1 313 ? 23.452 3.649   23.096  1.00 30.08 ?  293 LEU A CG    1 
ATOM   2308 C  CD1   . LEU A 1 313 ? 22.182 4.409   23.304  1.00 32.93 ?  293 LEU A CD1   1 
ATOM   2309 C  CD2   . LEU A 1 313 ? 23.204 2.456   22.175  1.00 25.55 ?  293 LEU A CD2   1 
ATOM   2310 N  N     . LYS A 1 314 ? 27.243 6.087   21.984  1.00 29.15 ?  294 LYS A N     1 
ATOM   2311 C  CA    . LYS A 1 314 ? 28.102 6.983   21.220  1.00 30.08 ?  294 LYS A CA    1 
ATOM   2312 C  C     . LYS A 1 314 ? 29.314 6.268   20.649  1.00 26.94 ?  294 LYS A C     1 
ATOM   2313 O  O     . LYS A 1 314 ? 29.983 6.816   19.775  1.00 30.65 ?  294 LYS A O     1 
ATOM   2314 C  CB    . LYS A 1 314 ? 28.544 8.160   22.095  1.00 32.76 ?  294 LYS A CB    1 
ATOM   2315 C  CG    . LYS A 1 314 ? 27.385 8.827   22.818  1.00 40.46 ?  294 LYS A CG    1 
ATOM   2316 C  CD    . LYS A 1 314 ? 27.676 10.252  23.252  1.00 35.48 ?  294 LYS A CD    1 
ATOM   2317 C  CE    . LYS A 1 314 ? 26.476 10.856  23.982  1.00 35.83 ?  294 LYS A CE    1 
ATOM   2318 N  NZ    . LYS A 1 314 ? 26.755 11.020  25.443  1.00 42.35 ?  294 LYS A NZ    1 
ATOM   2319 N  N     . PHE A 1 315 ? 29.632 5.077   21.142  1.00 34.68 ?  295 PHE A N     1 
ATOM   2320 C  CA    . PHE A 1 315 ? 30.676 4.269   20.531  1.00 29.45 ?  295 PHE A CA    1 
ATOM   2321 C  C     . PHE A 1 315 ? 30.099 3.330   19.480  1.00 22.96 ?  295 PHE A C     1 
ATOM   2322 O  O     . PHE A 1 315 ? 30.654 3.208   18.386  1.00 27.92 ?  295 PHE A O     1 
ATOM   2323 C  CB    . PHE A 1 315 ? 31.444 3.439   21.581  1.00 27.26 ?  295 PHE A CB    1 
ATOM   2324 C  CG    . PHE A 1 315 ? 32.260 2.338   20.970  1.00 23.18 ?  295 PHE A CG    1 
ATOM   2325 C  CD1   . PHE A 1 315 ? 31.686 1.107   20.650  1.00 23.96 ?  295 PHE A CD1   1 
ATOM   2326 C  CD2   . PHE A 1 315 ? 33.584 2.547   20.658  1.00 26.44 ?  295 PHE A CD2   1 
ATOM   2327 C  CE1   . PHE A 1 315 ? 32.412 0.111   20.029  1.00 21.11 ?  295 PHE A CE1   1 
ATOM   2328 C  CE2   . PHE A 1 315 ? 34.322 1.546   20.031  1.00 24.47 ?  295 PHE A CE2   1 
ATOM   2329 C  CZ    . PHE A 1 315 ? 33.730 0.329   19.723  1.00 21.67 ?  295 PHE A CZ    1 
ATOM   2330 N  N     . ARG A 1 316 ? 29.018 2.624   19.805  1.00 17.37 ?  296 ARG A N     1 
ATOM   2331 C  CA    . ARG A 1 316 ? 28.590 1.556   18.912  1.00 24.60 ?  296 ARG A CA    1 
ATOM   2332 C  C     . ARG A 1 316 ? 27.958 2.098   17.633  1.00 31.18 ?  296 ARG A C     1 
ATOM   2333 O  O     . ARG A 1 316 ? 28.081 1.465   16.577  1.00 22.42 ?  296 ARG A O     1 
ATOM   2334 C  CB    . ARG A 1 316 ? 27.641 0.612   19.639  1.00 22.98 ?  296 ARG A CB    1 
ATOM   2335 C  CG    . ARG A 1 316 ? 28.251 0.037   20.900  1.00 20.84 ?  296 ARG A CG    1 
ATOM   2336 C  CD    . ARG A 1 316 ? 27.587 -1.239  21.331  1.00 21.95 ?  296 ARG A CD    1 
ATOM   2337 N  NE    . ARG A 1 316 ? 28.559 -2.091  21.993  1.00 26.83 ?  296 ARG A NE    1 
ATOM   2338 C  CZ    . ARG A 1 316 ? 28.497 -2.448  23.268  1.00 32.56 ?  296 ARG A CZ    1 
ATOM   2339 N  NH1   . ARG A 1 316 ? 27.444 -2.152  24.017  1.00 31.26 ?  296 ARG A NH1   1 
ATOM   2340 N  NH2   . ARG A 1 316 ? 29.521 -3.112  23.806  1.00 30.09 ?  296 ARG A NH2   1 
ATOM   2341 N  N     . LYS A 1 317 ? 27.311 3.280   17.706  1.00 29.68 ?  297 LYS A N     1 
ATOM   2342 C  CA    . LYS A 1 317 ? 26.692 3.873   16.523  1.00 24.28 ?  297 LYS A CA    1 
ATOM   2343 C  C     . LYS A 1 317 ? 27.713 4.264   15.456  1.00 29.35 ?  297 LYS A C     1 
ATOM   2344 O  O     . LYS A 1 317 ? 27.557 3.835   14.299  1.00 29.81 ?  297 LYS A O     1 
ATOM   2345 C  CB    . LYS A 1 317 ? 25.815 5.053   16.940  1.00 23.92 ?  297 LYS A CB    1 
ATOM   2346 C  CG    . LYS A 1 317 ? 24.461 4.612   17.448  1.00 32.07 ?  297 LYS A CG    1 
ATOM   2347 C  CD    . LYS A 1 317 ? 23.781 5.698   18.255  1.00 28.26 ?  297 LYS A CD    1 
ATOM   2348 C  CE    . LYS A 1 317 ? 22.335 5.327   18.564  1.00 24.11 ?  297 LYS A CE    1 
ATOM   2349 N  NZ    . LYS A 1 317 ? 21.616 6.491   19.154  1.00 36.53 ?  297 LYS A NZ    1 
ATOM   2350 N  N     . PRO A 1 318 ? 28.754 5.053   15.750  1.00 25.49 ?  298 PRO A N     1 
ATOM   2351 C  CA    . PRO A 1 318 ? 29.754 5.295   14.703  1.00 22.67 ?  298 PRO A CA    1 
ATOM   2352 C  C     . PRO A 1 318 ? 30.529 4.051   14.348  1.00 28.41 ?  298 PRO A C     1 
ATOM   2353 O  O     . PRO A 1 318 ? 30.864 3.874   13.172  1.00 31.14 ?  298 PRO A O     1 
ATOM   2354 C  CB    . PRO A 1 318 ? 30.663 6.377   15.306  1.00 25.15 ?  298 PRO A CB    1 
ATOM   2355 C  CG    . PRO A 1 318 ? 30.465 6.303   16.751  1.00 22.34 ?  298 PRO A CG    1 
ATOM   2356 C  CD    . PRO A 1 318 ? 29.083 5.774   16.990  1.00 25.80 ?  298 PRO A CD    1 
ATOM   2357 N  N     . HIS A 1 319 ? 30.816 3.176   15.323  1.00 34.09 ?  299 HIS A N     1 
ATOM   2358 C  CA    . HIS A 1 319 ? 31.501 1.924   15.008  1.00 28.05 ?  299 HIS A CA    1 
ATOM   2359 C  C     . HIS A 1 319 ? 30.738 1.122   13.955  1.00 29.36 ?  299 HIS A C     1 
ATOM   2360 O  O     . HIS A 1 319 ? 31.342 0.564   13.030  1.00 24.63 ?  299 HIS A O     1 
ATOM   2361 C  CB    . HIS A 1 319 ? 31.697 1.088   16.271  1.00 23.09 ?  299 HIS A CB    1 
ATOM   2362 C  CG    . HIS A 1 319 ? 32.329 -0.244  16.008  1.00 19.47 ?  299 HIS A CG    1 
ATOM   2363 N  ND1   . HIS A 1 319 ? 31.592 -1.391  15.813  1.00 19.52 ?  299 HIS A ND1   1 
ATOM   2364 C  CD2   . HIS A 1 319 ? 33.628 -0.606  15.884  1.00 18.05 ?  299 HIS A CD2   1 
ATOM   2365 C  CE1   . HIS A 1 319 ? 32.409 -2.404  15.583  1.00 23.00 ?  299 HIS A CE1   1 
ATOM   2366 N  NE2   . HIS A 1 319 ? 33.650 -1.952  15.611  1.00 21.11 ?  299 HIS A NE2   1 
ATOM   2367 N  N     . PHE A 1 320 ? 29.408 1.071   14.078  1.00 25.91 ?  300 PHE A N     1 
ATOM   2368 C  CA    . PHE A 1 320 ? 28.580 0.292   13.166  1.00 25.91 ?  300 PHE A CA    1 
ATOM   2369 C  C     . PHE A 1 320 ? 28.697 0.810   11.740  1.00 42.04 ?  300 PHE A C     1 
ATOM   2370 O  O     . PHE A 1 320 ? 28.907 0.032   10.796  1.00 43.29 ?  300 PHE A O     1 
ATOM   2371 C  CB    . PHE A 1 320 ? 27.135 0.346   13.646  1.00 31.55 ?  300 PHE A CB    1 
ATOM   2372 C  CG    . PHE A 1 320 ? 26.173 -0.457  12.825  1.00 33.67 ?  300 PHE A CG    1 
ATOM   2373 C  CD1   . PHE A 1 320 ? 26.060 -1.825  13.005  1.00 32.44 ?  300 PHE A CD1   1 
ATOM   2374 C  CD2   . PHE A 1 320 ? 25.344 0.168   11.900  1.00 39.22 ?  300 PHE A CD2   1 
ATOM   2375 C  CE1   . PHE A 1 320 ? 25.150 -2.570  12.268  1.00 35.88 ?  300 PHE A CE1   1 
ATOM   2376 C  CE2   . PHE A 1 320 ? 24.433 -0.570  11.149  1.00 43.32 ?  300 PHE A CE2   1 
ATOM   2377 C  CZ    . PHE A 1 320 ? 24.336 -1.945  11.337  1.00 43.43 ?  300 PHE A CZ    1 
ATOM   2378 N  N     . GLN A 1 321 ? 28.573 2.135   11.565  1.00 39.00 ?  301 GLN A N     1 
ATOM   2379 C  CA    . GLN A 1 321 ? 28.703 2.738   10.240  1.00 31.54 ?  301 GLN A CA    1 
ATOM   2380 C  C     . GLN A 1 321 ? 30.050 2.414   9.611   1.00 27.42 ?  301 GLN A C     1 
ATOM   2381 O  O     . GLN A 1 321 ? 30.130 2.116   8.417   1.00 29.54 ?  301 GLN A O     1 
ATOM   2382 C  CB    . GLN A 1 321 ? 28.505 4.250   10.345  1.00 36.58 ?  301 GLN A CB    1 
ATOM   2383 C  CG    . GLN A 1 321 ? 27.099 4.672   10.765  1.00 29.00 ?  301 GLN A CG    1 
ATOM   2384 C  CD    . GLN A 1 321 ? 26.018 3.962   9.954   1.00 38.79 ?  301 GLN A CD    1 
ATOM   2385 O  OE1   . GLN A 1 321 ? 26.149 3.794   8.739   1.00 51.33 ?  301 GLN A OE1   1 
ATOM   2386 N  NE2   . GLN A 1 321 ? 24.943 3.552   10.620  1.00 31.65 ?  301 GLN A NE2   1 
ATOM   2387 N  N     . LEU A 1 322 ? 31.115 2.433   10.413  1.00 31.01 ?  302 LEU A N     1 
ATOM   2388 C  CA    . LEU A 1 322 ? 32.463 2.186   9.909   1.00 31.60 ?  302 LEU A CA    1 
ATOM   2389 C  C     . LEU A 1 322 ? 32.619 0.764   9.376   1.00 33.20 ?  302 LEU A C     1 
ATOM   2390 O  O     . LEU A 1 322 ? 33.042 0.557   8.232   1.00 34.69 ?  302 LEU A O     1 
ATOM   2391 C  CB    . LEU A 1 322 ? 33.473 2.452   11.013  1.00 22.09 ?  302 LEU A CB    1 
ATOM   2392 C  CG    . LEU A 1 322 ? 34.875 2.013   10.643  1.00 25.70 ?  302 LEU A CG    1 
ATOM   2393 C  CD1   . LEU A 1 322 ? 35.385 2.866   9.504   1.00 21.07 ?  302 LEU A CD1   1 
ATOM   2394 C  CD2   . LEU A 1 322 ? 35.775 2.133   11.856  1.00 24.21 ?  302 LEU A CD2   1 
ATOM   2395 N  N     . ALA A 1 323 ? 32.320 -0.233  10.208  1.00 25.42 ?  303 ALA A N     1 
ATOM   2396 C  CA    . ALA A 1 323 ? 32.322 -1.614  9.737   1.00 34.48 ?  303 ALA A CA    1 
ATOM   2397 C  C     . ALA A 1 323 ? 31.358 -1.816  8.575   1.00 32.78 ?  303 ALA A C     1 
ATOM   2398 O  O     . ALA A 1 323 ? 31.571 -2.704  7.744   1.00 29.18 ?  303 ALA A O     1 
ATOM   2399 C  CB    . ALA A 1 323 ? 31.960 -2.573  10.879  1.00 31.47 ?  303 ALA A CB    1 
ATOM   2400 N  N     . GLN A 1 324 ? 30.280 -1.030  8.513   1.00 35.52 ?  304 GLN A N     1 
ATOM   2401 C  CA    . GLN A 1 324 ? 29.355 -1.184  7.398   1.00 35.94 ?  304 GLN A CA    1 
ATOM   2402 C  C     . GLN A 1 324 ? 29.981 -0.701  6.096   1.00 37.30 ?  304 GLN A C     1 
ATOM   2403 O  O     . GLN A 1 324 ? 29.863 -1.375  5.066   1.00 36.01 ?  304 GLN A O     1 
ATOM   2404 C  CB    . GLN A 1 324 ? 28.046 -0.451  7.666   1.00 38.43 ?  304 GLN A CB    1 
ATOM   2405 C  CG    . GLN A 1 324 ? 27.002 -0.689  6.567   1.00 41.04 ?  304 GLN A CG    1 
ATOM   2406 C  CD    . GLN A 1 324 ? 25.619 -0.192  6.949   1.00 43.18 ?  304 GLN A CD    1 
ATOM   2407 O  OE1   . GLN A 1 324 ? 25.236 0.921   6.601   1.00 38.25 ?  304 GLN A OE1   1 
ATOM   2408 N  NE2   . GLN A 1 324 ? 24.871 -1.012  7.681   1.00 44.34 ?  304 GLN A NE2   1 
ATOM   2409 N  N     . ARG A 1 325 ? 30.670 0.448   6.124   1.00 30.73 ?  305 ARG A N     1 
ATOM   2410 C  CA    . ARG A 1 325 ? 31.369 0.909   4.923   1.00 34.45 ?  305 ARG A CA    1 
ATOM   2411 C  C     . ARG A 1 325 ? 32.493 -0.048  4.530   1.00 34.07 ?  305 ARG A C     1 
ATOM   2412 O  O     . ARG A 1 325 ? 32.699 -0.313  3.340   1.00 34.24 ?  305 ARG A O     1 
ATOM   2413 C  CB    . ARG A 1 325 ? 31.897 2.331   5.132   1.00 28.25 ?  305 ARG A CB    1 
ATOM   2414 C  CG    . ARG A 1 325 ? 30.779 3.312   5.501   1.00 32.62 ?  305 ARG A CG    1 
ATOM   2415 C  CD    . ARG A 1 325 ? 31.195 4.768   5.447   1.00 31.62 ?  305 ARG A CD    1 
ATOM   2416 N  NE    . ARG A 1 325 ? 32.227 5.088   6.428   1.00 43.42 ?  305 ARG A NE    1 
ATOM   2417 C  CZ    . ARG A 1 325 ? 32.005 5.288   7.723   1.00 42.60 ?  305 ARG A CZ    1 
ATOM   2418 N  NH1   . ARG A 1 325 ? 30.790 5.182   8.245   1.00 33.06 ?  305 ARG A NH1   1 
ATOM   2419 N  NH2   . ARG A 1 325 ? 33.028 5.605   8.514   1.00 37.37 ?  305 ARG A NH2   1 
ATOM   2420 N  N     . THR A 1 326 ? 33.199 -0.611  5.519   1.00 39.74 ?  306 THR A N     1 
ATOM   2421 C  CA    . THR A 1 326 ? 34.323 -1.501  5.239   1.00 36.18 ?  306 THR A CA    1 
ATOM   2422 C  C     . THR A 1 326 ? 33.873 -2.797  4.581   1.00 34.06 ?  306 THR A C     1 
ATOM   2423 O  O     . THR A 1 326 ? 34.595 -3.342  3.740   1.00 32.81 ?  306 THR A O     1 
ATOM   2424 C  CB    . THR A 1 326 ? 35.083 -1.815  6.531   1.00 32.51 ?  306 THR A CB    1 
ATOM   2425 O  OG1   . THR A 1 326 ? 35.788 -0.653  6.975   1.00 32.54 ?  306 THR A OG1   1 
ATOM   2426 C  CG2   . THR A 1 326 ? 36.090 -2.942  6.323   1.00 28.64 ?  306 THR A CG2   1 
ATOM   2427 N  N     . LEU A 1 327 ? 32.695 -3.296  4.948   1.00 31.74 ?  307 LEU A N     1 
ATOM   2428 C  CA    . LEU A 1 327 ? 32.182 -4.577  4.485   1.00 33.48 ?  307 LEU A CA    1 
ATOM   2429 C  C     . LEU A 1 327 ? 31.132 -4.438  3.380   1.00 31.49 ?  307 LEU A C     1 
ATOM   2430 O  O     . LEU A 1 327 ? 30.434 -5.406  3.068   1.00 32.76 ?  307 LEU A O     1 
ATOM   2431 C  CB    . LEU A 1 327 ? 31.610 -5.362  5.671   1.00 24.36 ?  307 LEU A CB    1 
ATOM   2432 C  CG    . LEU A 1 327 ? 32.645 -5.760  6.726   1.00 33.61 ?  307 LEU A CG    1 
ATOM   2433 C  CD1   . LEU A 1 327 ? 31.950 -6.140  8.030   1.00 33.52 ?  307 LEU A CD1   1 
ATOM   2434 C  CD2   . LEU A 1 327 ? 33.553 -6.899  6.256   1.00 25.66 ?  307 LEU A CD2   1 
ATOM   2435 N  N     . SER A 1 328 ? 30.991 -3.260  2.797   1.00 33.33 ?  308 SER A N     1 
ATOM   2436 C  CA    . SER A 1 328 ? 30.142 -3.125  1.626   1.00 34.79 ?  308 SER A CA    1 
ATOM   2437 C  C     . SER A 1 328 ? 30.784 -3.826  0.431   1.00 34.83 ?  308 SER A C     1 
ATOM   2438 O  O     . SER A 1 328 ? 31.996 -4.068  0.401   1.00 32.20 ?  308 SER A O     1 
ATOM   2439 C  CB    . SER A 1 328 ? 29.898 -1.651  1.320   1.00 31.01 ?  308 SER A CB    1 
ATOM   2440 O  OG    . SER A 1 328 ? 31.122 -0.968  1.126   1.00 33.79 ?  308 SER A OG    1 
ATOM   2441 N  N     . LYS A 1 329 ? 29.942 -4.175  -0.551  1.00 36.29 ?  309 LYS A N     1 
ATOM   2442 C  CA    . LYS A 1 329 ? 30.425 -4.829  -1.773  1.00 40.53 ?  309 LYS A CA    1 
ATOM   2443 C  C     . LYS A 1 329 ? 31.585 -4.067  -2.399  1.00 30.98 ?  309 LYS A C     1 
ATOM   2444 O  O     . LYS A 1 329 ? 32.524 -4.675  -2.921  1.00 30.37 ?  309 LYS A O     1 
ATOM   2445 C  CB    . LYS A 1 329 ? 29.283 -4.963  -2.787  1.00 36.27 ?  309 LYS A CB    1 
ATOM   2446 C  CG    . LYS A 1 329 ? 28.316 -6.110  -2.492  1.00 52.37 ?  309 LYS A CG    1 
ATOM   2447 C  CD    . LYS A 1 329 ? 28.069 -6.983  -3.715  1.00 60.45 ?  309 LYS A CD    1 
ATOM   2448 C  CE    . LYS A 1 329 ? 26.926 -7.967  -3.466  1.00 71.54 ?  309 LYS A CE    1 
ATOM   2449 N  NZ    . LYS A 1 329 ? 25.683 -7.293  -2.978  1.00 64.45 ?  309 LYS A NZ    1 
ATOM   2450 N  N     . GLU A 1 330 ? 31.555 -2.740  -2.303  1.00 29.69 ?  310 GLU A N     1 
ATOM   2451 C  CA    . GLU A 1 330 ? 32.589 -1.908  -2.887  1.00 27.33 ?  310 GLU A CA    1 
ATOM   2452 C  C     . GLU A 1 330 ? 33.911 -2.025  -2.140  1.00 38.77 ?  310 GLU A C     1 
ATOM   2453 O  O     . GLU A 1 330 ? 34.978 -2.079  -2.767  1.00 36.97 ?  310 GLU A O     1 
ATOM   2454 C  CB    . GLU A 1 330 ? 32.106 -0.462  -2.901  1.00 38.03 ?  310 GLU A CB    1 
ATOM   2455 C  CG    . GLU A 1 330 ? 33.200 0.569   -3.088  1.00 42.75 ?  310 GLU A CG    1 
ATOM   2456 C  CD    . GLU A 1 330 ? 32.651 1.983   -3.071  1.00 49.50 ?  310 GLU A CD    1 
ATOM   2457 O  OE1   . GLU A 1 330 ? 31.593 2.207   -2.421  1.00 48.96 ?  310 GLU A OE1   1 
ATOM   2458 O  OE2   . GLU A 1 330 ? 33.279 2.863   -3.707  1.00 38.25 ?  310 GLU A OE2   1 
ATOM   2459 N  N     . ASN A 1 331 ? 33.877 -2.037  -0.801  1.00 41.33 ?  311 ASN A N     1 
ATOM   2460 C  CA    . ASN A 1 331 ? 35.105 -1.899  -0.024  1.00 32.95 ?  311 ASN A CA    1 
ATOM   2461 C  C     . ASN A 1 331 ? 35.572 -3.165  0.683   1.00 30.19 ?  311 ASN A C     1 
ATOM   2462 O  O     . ASN A 1 331 ? 36.685 -3.160  1.215   1.00 29.04 ?  311 ASN A O     1 
ATOM   2463 C  CB    . ASN A 1 331 ? 34.955 -0.786  1.023   1.00 32.88 ?  311 ASN A CB    1 
ATOM   2464 C  CG    . ASN A 1 331 ? 34.632 0.567   0.407   1.00 40.41 ?  311 ASN A CG    1 
ATOM   2465 O  OD1   . ASN A 1 331 ? 35.280 1.021   -0.551  1.00 34.28 ?  311 ASN A OD1   1 
ATOM   2466 N  ND2   . ASN A 1 331 ? 33.627 1.230   0.976   1.00 38.79 ?  311 ASN A ND2   1 
ATOM   2467 N  N     . ARG A 1 332 ? 34.785 -4.249  0.678   1.00 30.71 ?  312 ARG A N     1 
ATOM   2468 C  CA    . ARG A 1 332 ? 35.076 -5.408  1.529   1.00 29.81 ?  312 ARG A CA    1 
ATOM   2469 C  C     . ARG A 1 332 ? 36.288 -6.227  1.091   1.00 29.78 ?  312 ARG A C     1 
ATOM   2470 O  O     . ARG A 1 332 ? 36.760 -7.058  1.880   1.00 32.25 ?  312 ARG A O     1 
ATOM   2471 C  CB    . ARG A 1 332 ? 33.855 -6.330  1.604   1.00 31.59 ?  312 ARG A CB    1 
ATOM   2472 C  CG    . ARG A 1 332 ? 33.460 -7.007  0.286   1.00 26.32 ?  312 ARG A CG    1 
ATOM   2473 C  CD    . ARG A 1 332 ? 32.308 -7.973  0.497   1.00 32.60 ?  312 ARG A CD    1 
ATOM   2474 N  NE    . ARG A 1 332 ? 31.750 -8.534  -0.730  1.00 42.82 ?  312 ARG A NE    1 
ATOM   2475 C  CZ    . ARG A 1 332 ? 30.678 -9.319  -0.776  1.00 57.60 ?  312 ARG A CZ    1 
ATOM   2476 N  NH1   . ARG A 1 332 ? 30.006 -9.644  0.321   1.00 47.76 ?  312 ARG A NH1   1 
ATOM   2477 N  NH2   . ARG A 1 332 ? 30.274 -9.802  -1.950  1.00 53.95 ?  312 ARG A NH2   1 
ATOM   2478 N  N     . GLY A 1 333 ? 36.785 -6.043  -0.136  1.00 31.77 ?  313 GLY A N     1 
ATOM   2479 C  CA    . GLY A 1 333 ? 37.892 -6.861  -0.624  1.00 23.30 ?  313 GLY A CA    1 
ATOM   2480 C  C     . GLY A 1 333 ? 37.547 -8.339  -0.587  1.00 30.05 ?  313 GLY A C     1 
ATOM   2481 O  O     . GLY A 1 333 ? 36.461 -8.766  -1.003  1.00 32.92 ?  313 GLY A O     1 
ATOM   2482 N  N     . ASN A 1 334 ? 38.455 -9.135  -0.031  1.00 28.34 ?  314 ASN A N     1 
ATOM   2483 C  CA    . ASN A 1 334 ? 38.310 -10.583 -0.002  1.00 22.73 ?  314 ASN A CA    1 
ATOM   2484 C  C     . ASN A 1 334 ? 37.697 -11.114 1.276   1.00 28.96 ?  314 ASN A C     1 
ATOM   2485 O  O     . ASN A 1 334 ? 37.740 -12.326 1.504   1.00 27.18 ?  314 ASN A O     1 
ATOM   2486 C  CB    . ASN A 1 334 ? 39.663 -11.242 -0.218  1.00 29.95 ?  314 ASN A CB    1 
ATOM   2487 C  CG    . ASN A 1 334 ? 40.171 -11.026 -1.610  1.00 34.45 ?  314 ASN A CG    1 
ATOM   2488 O  OD1   . ASN A 1 334 ? 39.391 -11.041 -2.566  1.00 34.55 ?  314 ASN A OD1   1 
ATOM   2489 N  ND2   . ASN A 1 334 ? 41.472 -10.798 -1.742  1.00 29.61 ?  314 ASN A ND2   1 
ATOM   2490 N  N     . TYR A 1 335 ? 37.104 -10.257 2.104   1.00 36.08 ?  315 TYR A N     1 
ATOM   2491 C  CA    . TYR A 1 335 ? 36.547 -10.700 3.369   1.00 28.48 ?  315 TYR A CA    1 
ATOM   2492 C  C     . TYR A 1 335 ? 35.091 -10.288 3.481   1.00 29.58 ?  315 TYR A C     1 
ATOM   2493 O  O     . TYR A 1 335 ? 34.657 -9.311  2.868   1.00 32.42 ?  315 TYR A O     1 
ATOM   2494 C  CB    . TYR A 1 335 ? 37.323 -10.122 4.538   1.00 27.21 ?  315 TYR A CB    1 
ATOM   2495 C  CG    . TYR A 1 335 ? 38.716 -10.664 4.666   1.00 29.23 ?  315 TYR A CG    1 
ATOM   2496 C  CD1   . TYR A 1 335 ? 39.768 -10.119 3.924   1.00 25.11 ?  315 TYR A CD1   1 
ATOM   2497 C  CD2   . TYR A 1 335 ? 38.991 -11.724 5.536   1.00 26.40 ?  315 TYR A CD2   1 
ATOM   2498 C  CE1   . TYR A 1 335 ? 41.053 -10.610 4.046   1.00 25.29 ?  315 TYR A CE1   1 
ATOM   2499 C  CE2   . TYR A 1 335 ? 40.275 -12.211 5.680   1.00 22.42 ?  315 TYR A CE2   1 
ATOM   2500 C  CZ    . TYR A 1 335 ? 41.299 -11.659 4.928   1.00 25.33 ?  315 TYR A CZ    1 
ATOM   2501 O  OH    . TYR A 1 335 ? 42.570 -12.154 5.067   1.00 33.54 ?  315 TYR A OH    1 
ATOM   2502 N  N     . THR A 1 336 ? 34.349 -11.054 4.285   1.00 31.51 ?  316 THR A N     1 
ATOM   2503 C  CA    . THR A 1 336 ? 33.006 -10.695 4.733   1.00 32.66 ?  316 THR A CA    1 
ATOM   2504 C  C     . THR A 1 336 ? 32.884 -10.685 6.256   1.00 31.33 ?  316 THR A C     1 
ATOM   2505 O  O     . THR A 1 336 ? 31.763 -10.574 6.778   1.00 27.38 ?  316 THR A O     1 
ATOM   2506 C  CB    . THR A 1 336 ? 31.963 -11.656 4.147   1.00 29.03 ?  316 THR A CB    1 
ATOM   2507 O  OG1   . THR A 1 336 ? 32.218 -12.987 4.618   1.00 28.34 ?  316 THR A OG1   1 
ATOM   2508 C  CG2   . THR A 1 336 ? 32.010 -11.636 2.658   1.00 24.77 ?  316 THR A CG2   1 
ATOM   2509 N  N     . THR A 1 337 ? 34.003 -10.811 6.978   1.00 29.43 ?  317 THR A N     1 
ATOM   2510 C  CA    . THR A 1 337 ? 34.003 -10.959 8.425   1.00 23.35 ?  317 THR A CA    1 
ATOM   2511 C  C     . THR A 1 337 ? 35.146 -10.155 9.028   1.00 28.79 ?  317 THR A C     1 
ATOM   2512 O  O     . THR A 1 337 ? 36.133 -9.835  8.350   1.00 24.03 ?  317 THR A O     1 
ATOM   2513 C  CB    . THR A 1 337 ? 34.159 -12.425 8.847   1.00 28.41 ?  317 THR A CB    1 
ATOM   2514 O  OG1   . THR A 1 337 ? 35.315 -12.991 8.207   1.00 29.50 ?  317 THR A OG1   1 
ATOM   2515 C  CG2   . THR A 1 337 ? 32.926 -13.224 8.472   1.00 26.12 ?  317 THR A CG2   1 
ATOM   2516 N  N     . GLY A 1 338 ? 35.001 -9.838  10.329  1.00 22.48 ?  318 GLY A N     1 
ATOM   2517 C  CA    . GLY A 1 338 ? 36.107 -9.340  11.121  1.00 19.39 ?  318 GLY A CA    1 
ATOM   2518 C  C     . GLY A 1 338 ? 37.004 -10.484 11.550  1.00 21.01 ?  318 GLY A C     1 
ATOM   2519 O  O     . GLY A 1 338 ? 36.723 -11.654 11.314  1.00 22.64 ?  318 GLY A O     1 
ATOM   2520 N  N     . SER A 1 339 ? 38.111 -10.140 12.203  1.00 25.76 ?  319 SER A N     1 
ATOM   2521 C  CA    . SER A 1 339 ? 39.084 -11.160 12.589  1.00 24.11 ?  319 SER A CA    1 
ATOM   2522 C  C     . SER A 1 339 ? 38.517 -12.201 13.564  1.00 26.10 ?  319 SER A C     1 
ATOM   2523 O  O     . SER A 1 339 ? 39.142 -13.250 13.762  1.00 23.82 ?  319 SER A O     1 
ATOM   2524 C  CB    . SER A 1 339 ? 40.317 -10.486 13.189  1.00 24.62 ?  319 SER A CB    1 
ATOM   2525 O  OG    . SER A 1 339 ? 39.986 -9.753  14.357  1.00 22.99 ?  319 SER A OG    1 
ATOM   2526 N  N     . ALA A 1 340 ? 37.361 -11.954 14.168  1.00 20.10 ?  320 ALA A N     1 
ATOM   2527 C  CA    . ALA A 1 340 ? 36.747 -12.936 15.048  1.00 27.68 ?  320 ALA A CA    1 
ATOM   2528 C  C     . ALA A 1 340 ? 35.671 -13.742 14.336  1.00 28.50 ?  320 ALA A C     1 
ATOM   2529 O  O     . ALA A 1 340 ? 34.997 -14.563 14.976  1.00 28.61 ?  320 ALA A O     1 
ATOM   2530 C  CB    . ALA A 1 340 ? 36.168 -12.256 16.316  1.00 19.25 ?  320 ALA A CB    1 
ATOM   2531 N  N     . GLY A 1 341 ? 35.487 -13.516 13.037  1.00 24.00 ?  321 GLY A N     1 
ATOM   2532 C  CA    . GLY A 1 341 ? 34.646 -14.372 12.218  1.00 24.61 ?  321 GLY A CA    1 
ATOM   2533 C  C     . GLY A 1 341 ? 33.193 -13.990 12.127  1.00 19.90 ?  321 GLY A C     1 
ATOM   2534 O  O     . GLY A 1 341 ? 32.371 -14.831 11.758  1.00 30.04 ?  321 GLY A O     1 
ATOM   2535 N  N     . TYR A 1 342 ? 32.851 -12.755 12.441  1.00 22.17 ?  322 TYR A N     1 
ATOM   2536 C  CA    . TYR A 1 342 ? 31.478 -12.285 12.441  1.00 25.15 ?  322 TYR A CA    1 
ATOM   2537 C  C     . TYR A 1 342 ? 31.303 -11.200 11.388  1.00 26.67 ?  322 TYR A C     1 
ATOM   2538 O  O     . TYR A 1 342 ? 32.259 -10.515 11.004  1.00 28.20 ?  322 TYR A O     1 
ATOM   2539 C  CB    . TYR A 1 342 ? 31.082 -11.730 13.825  1.00 24.04 ?  322 TYR A CB    1 
ATOM   2540 C  CG    . TYR A 1 342 ? 31.138 -12.725 14.963  1.00 25.15 ?  322 TYR A CG    1 
ATOM   2541 C  CD1   . TYR A 1 342 ? 32.306 -12.913 15.688  1.00 26.28 ?  322 TYR A CD1   1 
ATOM   2542 C  CD2   . TYR A 1 342 ? 30.015 -13.463 15.322  1.00 25.23 ?  322 TYR A CD2   1 
ATOM   2543 C  CE1   . TYR A 1 342 ? 32.356 -13.816 16.730  1.00 25.93 ?  322 TYR A CE1   1 
ATOM   2544 C  CE2   . TYR A 1 342 ? 30.052 -14.359 16.355  1.00 28.44 ?  322 TYR A CE2   1 
ATOM   2545 C  CZ    . TYR A 1 342 ? 31.226 -14.534 17.064  1.00 31.55 ?  322 TYR A CZ    1 
ATOM   2546 O  OH    . TYR A 1 342 ? 31.265 -15.431 18.111  1.00 35.48 ?  322 TYR A OH    1 
ATOM   2547 N  N     . THR A 1 343 ? 30.059 -11.045 10.934  1.00 22.68 ?  323 THR A N     1 
ATOM   2548 C  CA    . THR A 1 343 ? 29.681 -9.963  10.039  1.00 25.33 ?  323 THR A CA    1 
ATOM   2549 C  C     . THR A 1 343 ? 29.157 -8.782  10.851  1.00 31.76 ?  323 THR A C     1 
ATOM   2550 O  O     . THR A 1 343 ? 29.098 -8.813  12.084  1.00 29.39 ?  323 THR A O     1 
ATOM   2551 C  CB    . THR A 1 343 ? 28.628 -10.419 9.023   1.00 31.49 ?  323 THR A CB    1 
ATOM   2552 O  OG1   . THR A 1 343 ? 27.328 -10.443 9.636   1.00 30.87 ?  323 THR A OG1   1 
ATOM   2553 C  CG2   . THR A 1 343 ? 28.969 -11.810 8.452   1.00 25.13 ?  323 THR A CG2   1 
ATOM   2554 N  N     . ASN A 1 344 ? 28.746 -7.725  10.147  1.00 35.94 ?  324 ASN A N     1 
ATOM   2555 C  CA    . ASN A 1 344 ? 28.185 -6.567  10.827  1.00 32.03 ?  324 ASN A CA    1 
ATOM   2556 C  C     . ASN A 1 344 ? 26.887 -6.891  11.544  1.00 33.06 ?  324 ASN A C     1 
ATOM   2557 O  O     . ASN A 1 344 ? 26.451 -6.090  12.378  1.00 37.55 ?  324 ASN A O     1 
ATOM   2558 C  CB    . ASN A 1 344 ? 27.966 -5.421  9.846   1.00 31.51 ?  324 ASN A CB    1 
ATOM   2559 C  CG    . ASN A 1 344 ? 28.175 -4.067  10.490  1.00 35.53 ?  324 ASN A CG    1 
ATOM   2560 O  OD1   . ASN A 1 344 ? 29.078 -3.895  11.307  1.00 39.07 ?  324 ASN A OD1   1 
ATOM   2561 N  ND2   . ASN A 1 344 ? 27.346 -3.093  10.121  1.00 41.70 ?  324 ASN A ND2   1 
ATOM   2562 N  N     . SER A 1 345 ? 26.270 -8.041  11.245  1.00 32.65 ?  325 SER A N     1 
ATOM   2563 C  CA    . SER A 1 345 ? 25.095 -8.488  11.988  1.00 34.25 ?  325 SER A CA    1 
ATOM   2564 C  C     . SER A 1 345 ? 25.391 -8.583  13.483  1.00 36.81 ?  325 SER A C     1 
ATOM   2565 O  O     . SER A 1 345 ? 24.514 -8.310  14.315  1.00 32.44 ?  325 SER A O     1 
ATOM   2566 C  CB    . SER A 1 345 ? 24.631 -9.844  11.450  1.00 30.12 ?  325 SER A CB    1 
ATOM   2567 O  OG    . SER A 1 345 ? 24.468 -9.804  10.035  1.00 50.78 ?  325 SER A OG    1 
ATOM   2568 N  N     . PHE A 1 346 ? 26.625 -8.955  13.839  1.00 29.55 ?  326 PHE A N     1 
ATOM   2569 C  CA    . PHE A 1 346 ? 26.997 -9.065  15.242  1.00 31.68 ?  326 PHE A CA    1 
ATOM   2570 C  C     . PHE A 1 346 ? 26.959 -7.705  15.926  1.00 32.81 ?  326 PHE A C     1 
ATOM   2571 O  O     . PHE A 1 346 ? 26.400 -7.569  17.020  1.00 33.29 ?  326 PHE A O     1 
ATOM   2572 C  CB    . PHE A 1 346 ? 28.384 -9.690  15.357  1.00 35.27 ?  326 PHE A CB    1 
ATOM   2573 C  CG    . PHE A 1 346 ? 28.853 -9.887  16.771  1.00 29.43 ?  326 PHE A CG    1 
ATOM   2574 C  CD1   . PHE A 1 346 ? 28.402 -10.962 17.525  1.00 28.62 ?  326 PHE A CD1   1 
ATOM   2575 C  CD2   . PHE A 1 346 ? 29.752 -9.003  17.342  1.00 27.06 ?  326 PHE A CD2   1 
ATOM   2576 C  CE1   . PHE A 1 346 ? 28.840 -11.154 18.823  1.00 27.67 ?  326 PHE A CE1   1 
ATOM   2577 C  CE2   . PHE A 1 346 ? 30.200 -9.190  18.650  1.00 26.74 ?  326 PHE A CE2   1 
ATOM   2578 C  CZ    . PHE A 1 346 ? 29.740 -10.263 19.386  1.00 27.14 ?  326 PHE A CZ    1 
ATOM   2579 N  N     . ASN A 1 347 ? 27.560 -6.687  15.302  1.00 30.02 ?  327 ASN A N     1 
ATOM   2580 C  CA    . ASN A 1 347 ? 27.524 -5.349  15.878  1.00 27.02 ?  327 ASN A CA    1 
ATOM   2581 C  C     . ASN A 1 347 ? 26.101 -4.826  15.956  1.00 30.91 ?  327 ASN A C     1 
ATOM   2582 O  O     . ASN A 1 347 ? 25.710 -4.209  16.956  1.00 29.67 ?  327 ASN A O     1 
ATOM   2583 C  CB    . ASN A 1 347 ? 28.397 -4.410  15.064  1.00 32.89 ?  327 ASN A CB    1 
ATOM   2584 C  CG    . ASN A 1 347 ? 29.825 -4.859  15.022  1.00 30.10 ?  327 ASN A CG    1 
ATOM   2585 O  OD1   . ASN A 1 347 ? 30.365 -5.301  16.030  1.00 28.93 ?  327 ASN A OD1   1 
ATOM   2586 N  ND2   . ASN A 1 347 ? 30.454 -4.749  13.857  1.00 26.79 ?  327 ASN A ND2   1 
ATOM   2587 N  N     . HIS A 1 348 ? 25.302 -5.084  14.925  1.00 27.52 ?  328 HIS A N     1 
ATOM   2588 C  CA    . HIS A 1 348 ? 23.908 -4.675  14.981  1.00 36.33 ?  328 HIS A CA    1 
ATOM   2589 C  C     . HIS A 1 348 ? 23.205 -5.305  16.181  1.00 37.65 ?  328 HIS A C     1 
ATOM   2590 O  O     . HIS A 1 348 ? 22.369 -4.667  16.833  1.00 34.21 ?  328 HIS A O     1 
ATOM   2591 C  CB    . HIS A 1 348 ? 23.203 -5.039  13.672  1.00 39.12 ?  328 HIS A CB    1 
ATOM   2592 C  CG    . HIS A 1 348 ? 21.772 -4.611  13.626  1.00 45.54 ?  328 HIS A CG    1 
ATOM   2593 N  ND1   . HIS A 1 348 ? 21.397 -3.304  13.395  1.00 45.16 ?  328 HIS A ND1   1 
ATOM   2594 C  CD2   . HIS A 1 348 ? 20.626 -5.310  13.801  1.00 46.70 ?  328 HIS A CD2   1 
ATOM   2595 C  CE1   . HIS A 1 348 ? 20.079 -3.219  13.428  1.00 53.73 ?  328 HIS A CE1   1 
ATOM   2596 N  NE2   . HIS A 1 348 ? 19.588 -4.421  13.672  1.00 54.13 ?  328 HIS A NE2   1 
ATOM   2597 N  N     . MET A 1 349 ? 23.557 -6.546  16.510  1.00 34.89 ?  329 MET A N     1 
ATOM   2598 C  CA    . MET A 1 349 ? 22.907 -7.206  17.637  1.00 35.42 ?  329 MET A CA    1 
ATOM   2599 C  C     . MET A 1 349 ? 23.382 -6.634  18.978  1.00 36.29 ?  329 MET A C     1 
ATOM   2600 O  O     . MET A 1 349 ? 22.564 -6.388  19.872  1.00 37.08 ?  329 MET A O     1 
ATOM   2601 C  CB    . MET A 1 349 ? 23.139 -8.709  17.533  1.00 31.95 ?  329 MET A CB    1 
ATOM   2602 C  CG    . MET A 1 349 ? 22.670 -9.518  18.707  1.00 44.62 ?  329 MET A CG    1 
ATOM   2603 S  SD    . MET A 1 349 ? 23.997 -10.623 19.191  1.00 59.01 ?  329 MET A SD    1 
ATOM   2604 C  CE    . MET A 1 349 ? 25.038 -9.454  20.024  1.00 29.10 ?  329 MET A CE    1 
ATOM   2605 N  N     . VAL A 1 350 ? 24.690 -6.387  19.132  1.00 32.16 ?  330 VAL A N     1 
ATOM   2606 C  CA    . VAL A 1 350 ? 25.176 -5.763  20.362  1.00 28.26 ?  330 VAL A CA    1 
ATOM   2607 C  C     . VAL A 1 350 ? 24.582 -4.366  20.520  1.00 32.58 ?  330 VAL A C     1 
ATOM   2608 O  O     . VAL A 1 350 ? 24.218 -3.949  21.629  1.00 33.82 ?  330 VAL A O     1 
ATOM   2609 C  CB    . VAL A 1 350 ? 26.717 -5.718  20.394  1.00 23.28 ?  330 VAL A CB    1 
ATOM   2610 C  CG1   . VAL A 1 350 ? 27.182 -5.039  21.656  1.00 27.33 ?  330 VAL A CG1   1 
ATOM   2611 C  CG2   . VAL A 1 350 ? 27.326 -7.090  20.344  1.00 25.78 ?  330 VAL A CG2   1 
ATOM   2612 N  N     . LEU A 1 351 ? 24.484 -3.618  19.417  1.00 30.57 ?  331 LEU A N     1 
ATOM   2613 C  CA    . LEU A 1 351 ? 23.940 -2.264  19.467  1.00 29.20 ?  331 LEU A CA    1 
ATOM   2614 C  C     . LEU A 1 351 ? 22.457 -2.261  19.843  1.00 33.88 ?  331 LEU A C     1 
ATOM   2615 O  O     . LEU A 1 351 ? 22.019 -1.423  20.642  1.00 34.41 ?  331 LEU A O     1 
ATOM   2616 C  CB    . LEU A 1 351 ? 24.174 -1.569  18.122  1.00 32.36 ?  331 LEU A CB    1 
ATOM   2617 C  CG    . LEU A 1 351 ? 23.666 -0.151  17.841  1.00 37.48 ?  331 LEU A CG    1 
ATOM   2618 C  CD1   . LEU A 1 351 ? 24.225 0.854   18.834  1.00 25.91 ?  331 LEU A CD1   1 
ATOM   2619 C  CD2   . LEU A 1 351 ? 24.046 0.256   16.417  1.00 27.97 ?  331 LEU A CD2   1 
ATOM   2620 N  N     . GLU A 1 352 ? 21.671 -3.198  19.302  1.00 33.01 ?  332 GLU A N     1 
ATOM   2621 C  CA    . GLU A 1 352 ? 20.255 -3.255  19.659  1.00 37.63 ?  332 GLU A CA    1 
ATOM   2622 C  C     . GLU A 1 352 ? 20.058 -3.634  21.132  1.00 38.67 ?  332 GLU A C     1 
ATOM   2623 O  O     . GLU A 1 352 ? 19.210 -3.049  21.820  1.00 35.19 ?  332 GLU A O     1 
ATOM   2624 C  CB    . GLU A 1 352 ? 19.517 -4.230  18.740  1.00 32.16 ?  332 GLU A CB    1 
ATOM   2625 C  CG    . GLU A 1 352 ? 19.444 -3.813  17.249  1.00 50.43 ?  332 GLU A CG    1 
ATOM   2626 C  CD    . GLU A 1 352 ? 18.798 -2.443  17.007  1.00 59.85 ?  332 GLU A CD    1 
ATOM   2627 O  OE1   . GLU A 1 352 ? 18.029 -1.975  17.880  1.00 57.92 ?  332 GLU A OE1   1 
ATOM   2628 O  OE2   . GLU A 1 352 ? 19.056 -1.835  15.935  1.00 59.92 ?  332 GLU A OE2   1 
ATOM   2629 N  N     . PHE A 1 353 ? 20.809 -4.627  21.622  1.00 39.88 ?  333 PHE A N     1 
ATOM   2630 C  CA    . PHE A 1 353 ? 20.857 -4.923  23.052  1.00 33.14 ?  333 PHE A CA    1 
ATOM   2631 C  C     . PHE A 1 353 ? 21.045 -3.648  23.861  1.00 30.19 ?  333 PHE A C     1 
ATOM   2632 O  O     . PHE A 1 353 ? 20.281 -3.358  24.783  1.00 29.06 ?  333 PHE A O     1 
ATOM   2633 C  CB    . PHE A 1 353 ? 22.015 -5.884  23.336  1.00 41.00 ?  333 PHE A CB    1 
ATOM   2634 C  CG    . PHE A 1 353 ? 21.637 -7.339  23.357  1.00 43.60 ?  333 PHE A CG    1 
ATOM   2635 C  CD1   . PHE A 1 353 ? 20.570 -7.795  24.117  1.00 48.81 ?  333 PHE A CD1   1 
ATOM   2636 C  CD2   . PHE A 1 353 ? 22.361 -8.255  22.602  1.00 40.02 ?  333 PHE A CD2   1 
ATOM   2637 C  CE1   . PHE A 1 353 ? 20.231 -9.148  24.134  1.00 47.90 ?  333 PHE A CE1   1 
ATOM   2638 C  CE2   . PHE A 1 353 ? 22.025 -9.605  22.607  1.00 47.67 ?  333 PHE A CE2   1 
ATOM   2639 C  CZ    . PHE A 1 353 ? 20.956 -10.052 23.373  1.00 49.53 ?  333 PHE A CZ    1 
ATOM   2640 N  N     . THR A 1 354 ? 22.066 -2.867  23.509  1.00 31.78 ?  334 THR A N     1 
ATOM   2641 C  CA    . THR A 1 354 ? 22.385 -1.655  24.251  1.00 33.03 ?  334 THR A CA    1 
ATOM   2642 C  C     . THR A 1 354 ? 21.287 -0.606  24.110  1.00 34.37 ?  334 THR A C     1 
ATOM   2643 O  O     . THR A 1 354 ? 20.916 0.040   25.094  1.00 37.57 ?  334 THR A O     1 
ATOM   2644 C  CB    . THR A 1 354 ? 23.723 -1.103  23.768  1.00 33.54 ?  334 THR A CB    1 
ATOM   2645 O  OG1   . THR A 1 354 ? 24.651 -2.181  23.614  1.00 31.83 ?  334 THR A OG1   1 
ATOM   2646 C  CG2   . THR A 1 354 ? 24.279 -0.104  24.758  1.00 32.05 ?  334 THR A CG2   1 
ATOM   2647 N  N     . ILE A 1 355 ? 20.773 -0.409  22.891  1.00 36.14 ?  335 ILE A N     1 
ATOM   2648 C  CA    . ILE A 1 355 ? 19.644 0.499   22.677  1.00 35.37 ?  335 ILE A CA    1 
ATOM   2649 C  C     . ILE A 1 355 ? 18.463 0.101   23.560  1.00 34.88 ?  335 ILE A C     1 
ATOM   2650 O  O     . ILE A 1 355 ? 17.883 0.932   24.266  1.00 39.56 ?  335 ILE A O     1 
ATOM   2651 C  CB    . ILE A 1 355 ? 19.252 0.524   21.185  1.00 36.76 ?  335 ILE A CB    1 
ATOM   2652 C  CG1   . ILE A 1 355 ? 20.217 1.388   20.382  1.00 39.38 ?  335 ILE A CG1   1 
ATOM   2653 C  CG2   . ILE A 1 355 ? 17.842 1.046   20.992  1.00 30.42 ?  335 ILE A CG2   1 
ATOM   2654 C  CD1   . ILE A 1 355 ? 20.055 1.210   18.886  1.00 39.42 ?  335 ILE A CD1   1 
ATOM   2655 N  N     . GLU A 1 356 ? 18.091 -1.181  23.534  1.00 32.73 ?  336 GLU A N     1 
ATOM   2656 C  CA    . GLU A 1 356 ? 16.959 -1.648  24.328  1.00 34.39 ?  336 GLU A CA    1 
ATOM   2657 C  C     . GLU A 1 356 ? 17.172 -1.388  25.818  1.00 41.55 ?  336 GLU A C     1 
ATOM   2658 O  O     . GLU A 1 356 ? 16.213 -1.081  26.538  1.00 40.68 ?  336 GLU A O     1 
ATOM   2659 C  CB    . GLU A 1 356 ? 16.728 -3.135  24.048  1.00 32.99 ?  336 GLU A CB    1 
ATOM   2660 C  CG    . GLU A 1 356 ? 15.810 -3.877  25.013  1.00 36.18 ?  336 GLU A CG    1 
ATOM   2661 C  CD    . GLU A 1 356 ? 14.360 -3.416  24.965  1.00 46.95 ?  336 GLU A CD    1 
ATOM   2662 O  OE1   . GLU A 1 356 ? 13.873 -3.040  23.876  1.00 53.56 ?  336 GLU A OE1   1 
ATOM   2663 O  OE2   . GLU A 1 356 ? 13.700 -3.446  26.024  1.00 53.34 ?  336 GLU A OE2   1 
ATOM   2664 N  N     . VAL A 1 357 ? 18.416 -1.486  26.296  1.00 38.27 ?  337 VAL A N     1 
ATOM   2665 C  CA    . VAL A 1 357 ? 18.693 -1.183  27.695  1.00 35.05 ?  337 VAL A CA    1 
ATOM   2666 C  C     . VAL A 1 357 ? 18.395 0.284   27.979  1.00 45.76 ?  337 VAL A C     1 
ATOM   2667 O  O     . VAL A 1 357 ? 17.831 0.627   29.029  1.00 45.78 ?  337 VAL A O     1 
ATOM   2668 C  CB    . VAL A 1 357 ? 20.146 -1.557  28.051  1.00 36.78 ?  337 VAL A CB    1 
ATOM   2669 C  CG1   . VAL A 1 357 ? 20.571 -0.900  29.364  1.00 34.58 ?  337 VAL A CG1   1 
ATOM   2670 C  CG2   . VAL A 1 357 ? 20.308 -3.086  28.133  1.00 30.70 ?  337 VAL A CG2   1 
ATOM   2671 N  N     . GLU A 1 358 ? 18.736 1.170   27.034  1.00 40.50 ?  338 GLU A N     1 
ATOM   2672 C  CA    . GLU A 1 358 ? 18.435 2.588   27.202  1.00 39.25 ?  338 GLU A CA    1 
ATOM   2673 C  C     . GLU A 1 358 ? 16.931 2.847   27.232  1.00 40.28 ?  338 GLU A C     1 
ATOM   2674 O  O     . GLU A 1 358 ? 16.469 3.773   27.904  1.00 39.57 ?  338 GLU A O     1 
ATOM   2675 C  CB    . GLU A 1 358 ? 19.098 3.383   26.086  1.00 36.39 ?  338 GLU A CB    1 
ATOM   2676 C  CG    . GLU A 1 358 ? 18.876 4.880   26.138  1.00 38.35 ?  338 GLU A CG    1 
ATOM   2677 C  CD    . GLU A 1 358 ? 19.200 5.540   24.805  1.00 47.11 ?  338 GLU A CD    1 
ATOM   2678 O  OE1   . GLU A 1 358 ? 18.734 5.015   23.762  1.00 42.26 ?  338 GLU A OE1   1 
ATOM   2679 O  OE2   . GLU A 1 358 ? 19.926 6.562   24.796  1.00 41.90 ?  338 GLU A OE2   1 
ATOM   2680 N  N     . LYS A 1 359 ? 16.154 2.028   26.529  1.00 40.33 ?  339 LYS A N     1 
ATOM   2681 C  CA    . LYS A 1 359 ? 14.705 2.181   26.525  1.00 35.72 ?  339 LYS A CA    1 
ATOM   2682 C  C     . LYS A 1 359 ? 14.098 1.709   27.845  1.00 45.71 ?  339 LYS A C     1 
ATOM   2683 O  O     . LYS A 1 359 ? 13.138 2.310   28.342  1.00 46.67 ?  339 LYS A O     1 
ATOM   2684 C  CB    . LYS A 1 359 ? 14.141 1.413   25.326  1.00 38.11 ?  339 LYS A CB    1 
ATOM   2685 C  CG    . LYS A 1 359 ? 12.639 1.329   25.183  1.00 43.51 ?  339 LYS A CG    1 
ATOM   2686 C  CD    . LYS A 1 359 ? 12.280 0.075   24.389  1.00 42.31 ?  339 LYS A CD    1 
ATOM   2687 C  CE    . LYS A 1 359 ? 10.852 0.115   23.866  1.00 47.07 ?  339 LYS A CE    1 
ATOM   2688 N  NZ    . LYS A 1 359 ? 10.361 -1.254  23.519  1.00 56.95 ?  339 LYS A NZ    1 
ATOM   2689 N  N     . GLN A 1 360 ? 14.660 0.652   28.441  1.00 42.33 ?  340 GLN A N     1 
ATOM   2690 C  CA    . GLN A 1 360 ? 14.156 0.159   29.720  1.00 45.83 ?  340 GLN A CA    1 
ATOM   2691 C  C     . GLN A 1 360 ? 14.435 1.140   30.854  1.00 45.34 ?  340 GLN A C     1 
ATOM   2692 O  O     . GLN A 1 360 ? 13.621 1.278   31.774  1.00 44.11 ?  340 GLN A O     1 
ATOM   2693 C  CB    . GLN A 1 360 ? 14.778 -1.195  30.056  1.00 44.79 ?  340 GLN A CB    1 
ATOM   2694 C  CG    . GLN A 1 360 ? 14.407 -2.336  29.140  1.00 48.74 ?  340 GLN A CG    1 
ATOM   2695 C  CD    . GLN A 1 360 ? 14.607 -3.686  29.819  1.00 61.25 ?  340 GLN A CD    1 
ATOM   2696 O  OE1   . GLN A 1 360 ? 15.431 -3.823  30.731  1.00 61.54 ?  340 GLN A OE1   1 
ATOM   2697 N  NE2   . GLN A 1 360 ? 13.844 -4.686  29.385  1.00 55.85 ?  340 GLN A NE2   1 
ATOM   2698 N  N     . ILE A 1 361 ? 15.602 1.790   30.830  1.00 41.89 ?  341 ILE A N     1 
ATOM   2699 C  CA    . ILE A 1 361 ? 15.925 2.774   31.858  1.00 42.12 ?  341 ILE A CA    1 
ATOM   2700 C  C     . ILE A 1 361 ? 15.101 4.036   31.657  1.00 43.73 ?  341 ILE A C     1 
ATOM   2701 O  O     . ILE A 1 361 ? 14.652 4.660   32.624  1.00 45.53 ?  341 ILE A O     1 
ATOM   2702 C  CB    . ILE A 1 361 ? 17.429 3.097   31.856  1.00 45.40 ?  341 ILE A CB    1 
ATOM   2703 C  CG1   . ILE A 1 361 ? 18.280 1.841   32.066  1.00 43.14 ?  341 ILE A CG1   1 
ATOM   2704 C  CG2   . ILE A 1 361 ? 17.748 4.150   32.914  1.00 38.72 ?  341 ILE A CG2   1 
ATOM   2705 C  CD1   . ILE A 1 361 ? 19.774 2.134   32.022  1.00 32.47 ?  341 ILE A CD1   1 
ATOM   2706 N  N     . ARG A 1 362 ? 14.904 4.441   30.400  1.00 46.05 ?  342 ARG A N     1 
ATOM   2707 C  CA    . ARG A 1 362 ? 14.066 5.599   30.115  1.00 41.55 ?  342 ARG A CA    1 
ATOM   2708 C  C     . ARG A 1 362 ? 12.643 5.380   30.604  1.00 42.73 ?  342 ARG A C     1 
ATOM   2709 O  O     . ARG A 1 362 ? 11.957 6.341   30.964  1.00 46.10 ?  342 ARG A O     1 
ATOM   2710 C  CB    . ARG A 1 362 ? 14.070 5.897   28.615  1.00 42.89 ?  342 ARG A CB    1 
ATOM   2711 C  CG    . ARG A 1 362 ? 15.058 6.973   28.182  1.00 35.70 ?  342 ARG A CG    1 
ATOM   2712 C  CD    . ARG A 1 362 ? 15.261 6.912   26.688  1.00 39.48 ?  342 ARG A CD    1 
ATOM   2713 N  NE    . ARG A 1 362 ? 16.195 7.922   26.203  1.00 54.09 ?  342 ARG A NE    1 
ATOM   2714 C  CZ    . ARG A 1 362 ? 16.432 8.169   24.918  1.00 59.75 ?  342 ARG A CZ    1 
ATOM   2715 N  NH1   . ARG A 1 362 ? 15.820 7.493   23.954  1.00 41.55 ?  342 ARG A NH1   1 
ATOM   2716 N  NH2   . ARG A 1 362 ? 17.309 9.115   24.591  1.00 64.82 ?  342 ARG A NH2   1 
ATOM   2717 N  N     . ALA A 1 363 ? 12.194 4.124   30.635  1.00 43.13 ?  343 ALA A N     1 
ATOM   2718 C  CA    . ALA A 1 363 ? 10.844 3.798   31.081  1.00 48.04 ?  343 ALA A CA    1 
ATOM   2719 C  C     . ALA A 1 363 ? 10.733 3.872   32.598  1.00 48.33 ?  343 ALA A C     1 
ATOM   2720 O  O     . ALA A 1 363 ? 9.826  4.521   33.126  1.00 55.39 ?  343 ALA A O     1 
ATOM   2721 C  CB    . ALA A 1 363 ? 10.440 2.407   30.574  1.00 37.99 ?  343 ALA A CB    1 
ATOM   2722 N  N     . VAL A 1 364 ? 11.653 3.212   33.310  1.00 48.56 ?  344 VAL A N     1 
ATOM   2723 C  CA    . VAL A 1 364 ? 11.714 3.283   34.771  1.00 46.97 ?  344 VAL A CA    1 
ATOM   2724 C  C     . VAL A 1 364 ? 11.728 4.730   35.250  1.00 51.83 ?  344 VAL A C     1 
ATOM   2725 O  O     . VAL A 1 364 ? 11.163 5.053   36.305  1.00 51.55 ?  344 VAL A O     1 
ATOM   2726 C  CB    . VAL A 1 364 ? 12.953 2.502   35.282  1.00 41.30 ?  344 VAL A CB    1 
ATOM   2727 C  CG1   . VAL A 1 364 ? 13.196 2.743   36.764  1.00 40.82 ?  344 VAL A CG1   1 
ATOM   2728 C  CG2   . VAL A 1 364 ? 12.807 1.011   35.005  1.00 42.01 ?  344 VAL A CG2   1 
ATOM   2729 N  N     . LEU A 1 365 ? 12.348 5.625   34.477  1.00 45.27 ?  345 LEU A N     1 
ATOM   2730 C  CA    . LEU A 1 365 ? 12.540 7.012   34.877  1.00 47.33 ?  345 LEU A CA    1 
ATOM   2731 C  C     . LEU A 1 365 ? 11.406 7.939   34.452  1.00 55.21 ?  345 LEU A C     1 
ATOM   2732 O  O     . LEU A 1 365 ? 11.380 9.088   34.903  1.00 50.90 ?  345 LEU A O     1 
ATOM   2733 C  CB    . LEU A 1 365 ? 13.846 7.551   34.292  1.00 39.35 ?  345 LEU A CB    1 
ATOM   2734 C  CG    . LEU A 1 365 ? 15.152 7.394   35.061  1.00 40.43 ?  345 LEU A CG    1 
ATOM   2735 C  CD1   . LEU A 1 365 ? 16.131 8.407   34.518  1.00 43.25 ?  345 LEU A CD1   1 
ATOM   2736 C  CD2   . LEU A 1 365 ? 14.974 7.567   36.565  1.00 37.23 ?  345 LEU A CD2   1 
ATOM   2737 N  N     . ALA A 1 366 ? 10.482 7.479   33.605  1.00 58.65 ?  346 ALA A N     1 
ATOM   2738 C  CA    . ALA A 1 366 ? 9.513  8.382   32.983  1.00 54.86 ?  346 ALA A CA    1 
ATOM   2739 C  C     . ALA A 1 366 ? 8.745  9.251   33.974  1.00 59.75 ?  346 ALA A C     1 
ATOM   2740 O  O     . ALA A 1 366 ? 8.496  10.425  33.651  1.00 69.07 ?  346 ALA A O     1 
ATOM   2741 C  CB    . ALA A 1 366 ? 8.545  7.577   32.104  1.00 52.22 ?  346 ALA A CB    1 
ATOM   2742 N  N     . PRO A 1 367 ? 8.328  8.765   35.158  1.00 57.10 ?  347 PRO A N     1 
ATOM   2743 C  CA    . PRO A 1 367 ? 7.817  9.687   36.182  1.00 60.91 ?  347 PRO A CA    1 
ATOM   2744 C  C     . PRO A 1 367 ? 8.895  10.164  37.159  1.00 52.40 ?  347 PRO A C     1 
ATOM   2745 O  O     . PRO A 1 367 ? 9.519  11.192  36.889  1.00 54.15 ?  347 PRO A O     1 
ATOM   2746 C  CB    . PRO A 1 367 ? 6.758  8.846   36.915  1.00 59.73 ?  347 PRO A CB    1 
ATOM   2747 C  CG    . PRO A 1 367 ? 6.601  7.565   36.097  1.00 54.47 ?  347 PRO A CG    1 
ATOM   2748 C  CD    . PRO A 1 367 ? 7.933  7.377   35.455  1.00 60.06 ?  347 PRO A CD    1 
ATOM   2749 N  N     . GLN B 1 19  ? 53.253 -31.954 -34.259 1.00 65.08 ?  -1  GLN B N     1 
ATOM   2750 C  CA    . GLN B 1 19  ? 52.661 -32.653 -33.120 1.00 68.02 ?  -1  GLN B CA    1 
ATOM   2751 C  C     . GLN B 1 19  ? 52.738 -34.185 -33.273 1.00 72.14 ?  -1  GLN B C     1 
ATOM   2752 O  O     . GLN B 1 19  ? 52.934 -34.716 -34.370 1.00 78.41 ?  -1  GLN B O     1 
ATOM   2753 C  CB    . GLN B 1 19  ? 51.204 -32.199 -32.915 1.00 55.19 ?  -1  GLN B CB    1 
ATOM   2754 C  CG    . GLN B 1 19  ? 51.094 -30.851 -32.223 1.00 38.92 ?  -1  GLN B CG    1 
ATOM   2755 C  CD    . GLN B 1 19  ? 51.520 -30.917 -30.765 1.00 55.12 ?  -1  GLN B CD    1 
ATOM   2756 O  OE1   . GLN B 1 19  ? 51.484 -31.984 -30.145 1.00 57.74 ?  -1  GLN B OE1   1 
ATOM   2757 N  NE2   . GLN B 1 19  ? 51.976 -29.785 -30.224 1.00 46.38 ?  -1  GLN B NE2   1 
ATOM   2758 N  N     . GLY B 1 20  ? 52.586 -34.892 -32.157 1.00 65.54 ?  0   GLY B N     1 
ATOM   2759 C  CA    . GLY B 1 20  ? 52.765 -36.330 -32.157 1.00 75.07 ?  0   GLY B CA    1 
ATOM   2760 C  C     . GLY B 1 20  ? 53.730 -36.774 -31.076 1.00 72.36 ?  0   GLY B C     1 
ATOM   2761 O  O     . GLY B 1 20  ? 53.602 -36.354 -29.921 1.00 54.66 ?  0   GLY B O     1 
ATOM   2762 N  N     . MET B 1 21  ? 54.704 -37.616 -31.439 1.00 77.37 ?  1   MET B N     1 
ATOM   2763 C  CA    . MET B 1 21  ? 55.747 -38.066 -30.523 1.00 74.68 ?  1   MET B CA    1 
ATOM   2764 C  C     . MET B 1 21  ? 56.926 -37.096 -30.451 1.00 73.45 ?  1   MET B C     1 
ATOM   2765 O  O     . MET B 1 21  ? 58.003 -37.467 -29.960 1.00 62.69 ?  1   MET B O     1 
ATOM   2766 C  CB    . MET B 1 21  ? 56.224 -39.468 -30.908 1.00 82.42 ?  1   MET B CB    1 
ATOM   2767 C  CG    . MET B 1 21  ? 55.097 -40.371 -31.380 1.00 81.31 ?  1   MET B CG    1 
ATOM   2768 S  SD    . MET B 1 21  ? 54.018 -40.862 -30.019 1.00 87.59 ?  1   MET B SD    1 
ATOM   2769 C  CE    . MET B 1 21  ? 55.203 -41.086 -28.686 1.00 87.32 ?  1   MET B CE    1 
ATOM   2770 N  N     . ILE B 1 22  ? 56.737 -35.863 -30.940 1.00 71.07 ?  2   ILE B N     1 
ATOM   2771 C  CA    . ILE B 1 22  ? 57.558 -34.733 -30.524 1.00 63.34 ?  2   ILE B CA    1 
ATOM   2772 C  C     . ILE B 1 22  ? 57.509 -34.583 -29.013 1.00 52.60 ?  2   ILE B C     1 
ATOM   2773 O  O     . ILE B 1 22  ? 58.306 -33.837 -28.438 1.00 46.26 ?  2   ILE B O     1 
ATOM   2774 C  CB    . ILE B 1 22  ? 57.077 -33.435 -31.196 1.00 64.40 ?  2   ILE B CB    1 
ATOM   2775 C  CG1   . ILE B 1 22  ? 55.682 -33.077 -30.675 1.00 61.60 ?  2   ILE B CG1   1 
ATOM   2776 C  CG2   . ILE B 1 22  ? 57.046 -33.620 -32.707 1.00 54.45 ?  2   ILE B CG2   1 
ATOM   2777 C  CD1   . ILE B 1 22  ? 55.418 -31.601 -30.525 1.00 45.55 ?  2   ILE B CD1   1 
ATOM   2778 N  N     . SER B 1 23  ? 56.542 -35.246 -28.369 1.00 50.22 ?  3   SER B N     1 
ATOM   2779 C  CA    . SER B 1 23  ? 56.531 -35.423 -26.923 1.00 41.30 ?  3   SER B CA    1 
ATOM   2780 C  C     . SER B 1 23  ? 57.828 -36.041 -26.418 1.00 48.05 ?  3   SER B C     1 
ATOM   2781 O  O     . SER B 1 23  ? 58.294 -35.725 -25.314 1.00 44.79 ?  3   SER B O     1 
ATOM   2782 C  CB    . SER B 1 23  ? 55.351 -36.311 -26.550 1.00 44.49 ?  3   SER B CB    1 
ATOM   2783 O  OG    . SER B 1 23  ? 54.168 -35.836 -27.160 1.00 52.29 ?  3   SER B OG    1 
ATOM   2784 N  N     . ASN B 1 24  ? 58.411 -36.949 -27.208 1.00 56.53 ?  4   ASN B N     1 
ATOM   2785 C  CA    . ASN B 1 24  ? 59.651 -37.606 -26.820 1.00 44.12 ?  4   ASN B CA    1 
ATOM   2786 C  C     . ASN B 1 24  ? 60.806 -36.617 -26.771 1.00 42.46 ?  4   ASN B C     1 
ATOM   2787 O  O     . ASN B 1 24  ? 61.607 -36.644 -25.831 1.00 45.70 ?  4   ASN B O     1 
ATOM   2788 C  CB    . ASN B 1 24  ? 59.948 -38.739 -27.797 1.00 59.61 ?  4   ASN B CB    1 
ATOM   2789 C  CG    . ASN B 1 24  ? 59.559 -40.096 -27.247 1.00 74.61 ?  4   ASN B CG    1 
ATOM   2790 O  OD1   . ASN B 1 24  ? 59.460 -40.280 -26.025 1.00 65.39 ?  4   ASN B OD1   1 
ATOM   2791 N  ND2   . ASN B 1 24  ? 59.317 -41.054 -28.146 1.00 73.58 ?  4   ASN B ND2   1 
ATOM   2792 N  N     . GLU B 1 25  ? 60.899 -35.728 -27.767 1.00 40.64 ?  5   GLU B N     1 
ATOM   2793 C  CA    . GLU B 1 25  ? 61.978 -34.741 -27.791 1.00 45.06 ?  5   GLU B CA    1 
ATOM   2794 C  C     . GLU B 1 25  ? 61.881 -33.767 -26.618 1.00 35.29 ?  5   GLU B C     1 
ATOM   2795 O  O     . GLU B 1 25  ? 62.898 -33.234 -26.167 1.00 34.23 ?  5   GLU B O     1 
ATOM   2796 C  CB    . GLU B 1 25  ? 61.965 -33.964 -29.118 1.00 42.82 ?  5   GLU B CB    1 
ATOM   2797 C  CG    . GLU B 1 25  ? 62.600 -34.673 -30.348 1.00 47.31 ?  5   GLU B CG    1 
ATOM   2798 C  CD    . GLU B 1 25  ? 63.841 -35.516 -30.021 1.00 59.27 ?  5   GLU B CD    1 
ATOM   2799 O  OE1   . GLU B 1 25  ? 64.893 -34.943 -29.633 1.00 55.31 ?  5   GLU B OE1   1 
ATOM   2800 O  OE2   . GLU B 1 25  ? 63.763 -36.759 -30.161 1.00 53.11 ?  5   GLU B OE2   1 
ATOM   2801 N  N     . ILE B 1 26  ? 60.679 -33.516 -26.119 1.00 26.27 ?  6   ILE B N     1 
ATOM   2802 C  CA    . ILE B 1 26  ? 60.517 -32.561 -25.036 1.00 28.03 ?  6   ILE B CA    1 
ATOM   2803 C  C     . ILE B 1 26  ? 60.721 -33.219 -23.679 1.00 29.85 ?  6   ILE B C     1 
ATOM   2804 O  O     . ILE B 1 26  ? 61.393 -32.653 -22.814 1.00 28.74 ?  6   ILE B O     1 
ATOM   2805 C  CB    . ILE B 1 26  ? 59.143 -31.889 -25.145 1.00 26.76 ?  6   ILE B CB    1 
ATOM   2806 C  CG1   . ILE B 1 26  ? 59.103 -31.017 -26.389 1.00 23.13 ?  6   ILE B CG1   1 
ATOM   2807 C  CG2   . ILE B 1 26  ? 58.871 -31.026 -23.954 1.00 27.86 ?  6   ILE B CG2   1 
ATOM   2808 C  CD1   . ILE B 1 26  ? 57.723 -30.922 -26.959 1.00 26.87 ?  6   ILE B CD1   1 
ATOM   2809 N  N     . SER B 1 27  ? 60.185 -34.427 -23.483 1.00 28.15 ?  7   SER B N     1 
ATOM   2810 C  CA    . SER B 1 27  ? 60.261 -35.078 -22.174 1.00 29.07 ?  7   SER B CA    1 
ATOM   2811 C  C     . SER B 1 27  ? 61.690 -35.403 -21.758 1.00 30.91 ?  7   SER B C     1 
ATOM   2812 O  O     . SER B 1 27  ? 61.946 -35.588 -20.566 1.00 31.18 ?  7   SER B O     1 
ATOM   2813 C  CB    . SER B 1 27  ? 59.417 -36.359 -22.157 1.00 27.49 ?  7   SER B CB    1 
ATOM   2814 O  OG    . SER B 1 27  ? 59.938 -37.314 -23.063 1.00 37.52 ?  7   SER B OG    1 
ATOM   2815 N  N     . LYS B 1 28  ? 62.632 -35.454 -22.699 1.00 35.03 ?  8   LYS B N     1 
ATOM   2816 C  CA    . LYS B 1 28  ? 64.003 -35.836 -22.386 1.00 30.48 ?  8   LYS B CA    1 
ATOM   2817 C  C     . LYS B 1 28  ? 64.878 -34.653 -21.984 1.00 30.62 ?  8   LYS B C     1 
ATOM   2818 O  O     . LYS B 1 28  ? 66.023 -34.848 -21.563 1.00 31.83 ?  8   LYS B O     1 
ATOM   2819 C  CB    . LYS B 1 28  ? 64.609 -36.566 -23.586 1.00 28.64 ?  8   LYS B CB    1 
ATOM   2820 C  CG    . LYS B 1 28  ? 63.810 -37.816 -24.018 1.00 49.23 ?  8   LYS B CG    1 
ATOM   2821 C  CD    . LYS B 1 28  ? 63.123 -38.552 -22.829 1.00 46.12 ?  8   LYS B CD    1 
ATOM   2822 C  CE    . LYS B 1 28  ? 62.913 -40.052 -23.107 1.00 46.31 ?  8   LYS B CE    1 
ATOM   2823 N  NZ    . LYS B 1 28  ? 62.407 -40.367 -24.484 1.00 46.43 ?  8   LYS B NZ    1 
ATOM   2824 N  N     . LEU B 1 29  ? 64.362 -33.442 -22.073 1.00 28.20 ?  9   LEU B N     1 
ATOM   2825 C  CA    . LEU B 1 29  ? 65.171 -32.263 -21.856 1.00 24.46 ?  9   LEU B CA    1 
ATOM   2826 C  C     . LEU B 1 29  ? 65.126 -31.829 -20.399 1.00 30.79 ?  9   LEU B C     1 
ATOM   2827 O  O     . LEU B 1 29  ? 64.155 -32.065 -19.666 1.00 25.54 ?  9   LEU B O     1 
ATOM   2828 C  CB    . LEU B 1 29  ? 64.711 -31.122 -22.768 1.00 27.73 ?  9   LEU B CB    1 
ATOM   2829 C  CG    . LEU B 1 29  ? 64.870 -31.415 -24.270 1.00 27.86 ?  9   LEU B CG    1 
ATOM   2830 C  CD1   . LEU B 1 29  ? 64.362 -30.273 -25.129 1.00 19.93 ?  9   LEU B CD1   1 
ATOM   2831 C  CD2   . LEU B 1 29  ? 66.328 -31.714 -24.604 1.00 21.18 ?  9   LEU B CD2   1 
ATOM   2832 N  N     . ASP B 1 30  ? 66.220 -31.207 -19.985 1.00 27.87 ?  10  ASP B N     1 
ATOM   2833 C  CA    . ASP B 1 30  ? 66.333 -30.572 -18.681 1.00 25.01 ?  10  ASP B CA    1 
ATOM   2834 C  C     . ASP B 1 30  ? 67.043 -29.243 -18.891 1.00 26.20 ?  10  ASP B C     1 
ATOM   2835 O  O     . ASP B 1 30  ? 68.167 -29.032 -18.421 1.00 32.18 ?  10  ASP B O     1 
ATOM   2836 C  CB    . ASP B 1 30  ? 67.090 -31.479 -17.712 1.00 29.64 ?  10  ASP B CB    1 
ATOM   2837 C  CG    . ASP B 1 30  ? 67.027 -30.974 -16.285 1.00 34.24 ?  10  ASP B CG    1 
ATOM   2838 O  OD1   . ASP B 1 30  ? 66.109 -30.158 -15.990 1.00 30.18 ?  10  ASP B OD1   1 
ATOM   2839 O  OD2   . ASP B 1 30  ? 67.903 -31.376 -15.484 1.00 31.75 ?  10  ASP B OD2   1 
ATOM   2840 N  N     . PRO B 1 31  ? 66.410 -28.312 -19.605 1.00 24.33 ?  11  PRO B N     1 
ATOM   2841 C  CA    . PRO B 1 31  ? 67.138 -27.110 -20.055 1.00 27.72 ?  11  PRO B CA    1 
ATOM   2842 C  C     . PRO B 1 31  ? 67.565 -26.186 -18.923 1.00 28.98 ?  11  PRO B C     1 
ATOM   2843 O  O     . PRO B 1 31  ? 68.392 -25.292 -19.151 1.00 28.11 ?  11  PRO B O     1 
ATOM   2844 C  CB    . PRO B 1 31  ? 66.142 -26.411 -20.997 1.00 24.98 ?  11  PRO B CB    1 
ATOM   2845 C  CG    . PRO B 1 31  ? 64.797 -26.931 -20.620 1.00 31.48 ?  11  PRO B CG    1 
ATOM   2846 C  CD    . PRO B 1 31  ? 64.970 -28.269 -19.927 1.00 24.53 ?  11  PRO B CD    1 
ATOM   2847 N  N     . LEU B 1 32  ? 67.034 -26.372 -17.717 1.00 29.38 ?  12  LEU B N     1 
ATOM   2848 C  CA    . LEU B 1 32  ? 67.373 -25.534 -16.578 1.00 28.75 ?  12  LEU B CA    1 
ATOM   2849 C  C     . LEU B 1 32  ? 68.099 -26.321 -15.483 1.00 34.50 ?  12  LEU B C     1 
ATOM   2850 O  O     . LEU B 1 32  ? 68.204 -25.840 -14.349 1.00 32.41 ?  12  LEU B O     1 
ATOM   2851 C  CB    . LEU B 1 32  ? 66.111 -24.871 -16.032 1.00 22.69 ?  12  LEU B CB    1 
ATOM   2852 C  CG    . LEU B 1 32  ? 65.229 -24.045 -16.967 1.00 25.40 ?  12  LEU B CG    1 
ATOM   2853 C  CD1   . LEU B 1 32  ? 63.867 -23.878 -16.348 1.00 25.11 ?  12  LEU B CD1   1 
ATOM   2854 C  CD2   . LEU B 1 32  ? 65.823 -22.683 -17.277 1.00 23.60 ?  12  LEU B CD2   1 
ATOM   2855 N  N     . ASN B 1 33  ? 68.608 -27.512 -15.815 1.00 30.81 ?  13  ASN B N     1 
ATOM   2856 C  CA    . ASN B 1 33  ? 69.322 -28.401 -14.893 1.00 30.58 ?  13  ASN B CA    1 
ATOM   2857 C  C     . ASN B 1 33  ? 68.571 -28.566 -13.573 1.00 32.29 ?  13  ASN B C     1 
ATOM   2858 O  O     . ASN B 1 33  ? 69.096 -28.341 -12.479 1.00 37.06 ?  13  ASN B O     1 
ATOM   2859 C  CB    . ASN B 1 33  ? 70.758 -27.929 -14.658 1.00 30.80 ?  13  ASN B CB    1 
ATOM   2860 C  CG    . ASN B 1 33  ? 71.566 -28.932 -13.812 1.00 53.51 ?  13  ASN B CG    1 
ATOM   2861 O  OD1   . ASN B 1 33  ? 71.649 -30.122 -14.132 1.00 48.85 ?  13  ASN B OD1   1 
ATOM   2862 N  ND2   . ASN B 1 33  ? 72.130 -28.448 -12.699 1.00 54.95 ?  13  ASN B ND2   1 
ATOM   2863 N  N     . LEU B 1 34  ? 67.318 -28.986 -13.699 1.00 28.41 ?  14  LEU B N     1 
ATOM   2864 C  CA    . LEU B 1 34  ? 66.406 -29.086 -12.571 1.00 27.88 ?  14  LEU B CA    1 
ATOM   2865 C  C     . LEU B 1 34  ? 66.122 -30.524 -12.153 1.00 29.31 ?  14  LEU B C     1 
ATOM   2866 O  O     . LEU B 1 34  ? 65.275 -30.741 -11.280 1.00 32.17 ?  14  LEU B O     1 
ATOM   2867 C  CB    . LEU B 1 34  ? 65.090 -28.371 -12.900 1.00 22.71 ?  14  LEU B CB    1 
ATOM   2868 C  CG    . LEU B 1 34  ? 65.182 -26.855 -12.756 1.00 26.81 ?  14  LEU B CG    1 
ATOM   2869 C  CD1   . LEU B 1 34  ? 63.899 -26.147 -13.193 1.00 22.61 ?  14  LEU B CD1   1 
ATOM   2870 C  CD2   . LEU B 1 34  ? 65.569 -26.489 -11.310 1.00 30.52 ?  14  LEU B CD2   1 
ATOM   2871 N  N     . ASP B 1 35  ? 66.802 -31.510 -12.744 1.00 24.70 ?  15  ASP B N     1 
ATOM   2872 C  CA    . ASP B 1 35  ? 66.437 -32.903 -12.489 1.00 27.77 ?  15  ASP B CA    1 
ATOM   2873 C  C     . ASP B 1 35  ? 66.626 -33.271 -11.019 1.00 30.56 ?  15  ASP B C     1 
ATOM   2874 O  O     . ASP B 1 35  ? 65.717 -33.828 -10.388 1.00 34.53 ?  15  ASP B O     1 
ATOM   2875 C  CB    . ASP B 1 35  ? 67.245 -33.840 -13.387 1.00 26.28 ?  15  ASP B CB    1 
ATOM   2876 C  CG    . ASP B 1 35  ? 66.590 -34.064 -14.744 1.00 32.15 ?  15  ASP B CG    1 
ATOM   2877 O  OD1   . ASP B 1 35  ? 65.396 -33.702 -14.911 1.00 29.28 ?  15  ASP B OD1   1 
ATOM   2878 O  OD2   . ASP B 1 35  ? 67.283 -34.594 -15.645 1.00 31.85 ?  15  ASP B OD2   1 
ATOM   2879 N  N     . ALA B 1 36  ? 67.805 -32.982 -10.456 1.00 27.12 ?  16  ALA B N     1 
ATOM   2880 C  CA    . ALA B 1 36  ? 68.031 -33.270 -9.041  1.00 28.02 ?  16  ALA B CA    1 
ATOM   2881 C  C     . ALA B 1 36  ? 67.063 -32.486 -8.165  1.00 31.05 ?  16  ALA B C     1 
ATOM   2882 O  O     . ALA B 1 36  ? 66.547 -33.009 -7.172  1.00 29.35 ?  16  ALA B O     1 
ATOM   2883 C  CB    . ALA B 1 36  ? 69.476 -32.954 -8.647  1.00 18.78 ?  16  ALA B CB    1 
ATOM   2884 N  N     . PHE B 1 37  ? 66.794 -31.229 -8.524  1.00 28.54 ?  17  PHE B N     1 
ATOM   2885 C  CA    . PHE B 1 37  ? 65.807 -30.464 -7.781  1.00 24.65 ?  17  PHE B CA    1 
ATOM   2886 C  C     . PHE B 1 37  ? 64.432 -31.111 -7.848  1.00 26.87 ?  17  PHE B C     1 
ATOM   2887 O  O     . PHE B 1 37  ? 63.648 -30.981 -6.907  1.00 31.40 ?  17  PHE B O     1 
ATOM   2888 C  CB    . PHE B 1 37  ? 65.752 -29.032 -8.303  1.00 26.92 ?  17  PHE B CB    1 
ATOM   2889 C  CG    . PHE B 1 37  ? 64.695 -28.180 -7.644  1.00 30.40 ?  17  PHE B CG    1 
ATOM   2890 C  CD1   . PHE B 1 37  ? 63.372 -28.223 -8.075  1.00 27.28 ?  17  PHE B CD1   1 
ATOM   2891 C  CD2   . PHE B 1 37  ? 65.031 -27.311 -6.618  1.00 23.40 ?  17  PHE B CD2   1 
ATOM   2892 C  CE1   . PHE B 1 37  ? 62.414 -27.431 -7.494  1.00 22.49 ?  17  PHE B CE1   1 
ATOM   2893 C  CE2   . PHE B 1 37  ? 64.082 -26.523 -6.042  1.00 26.20 ?  17  PHE B CE2   1 
ATOM   2894 C  CZ    . PHE B 1 37  ? 62.764 -26.586 -6.484  1.00 26.14 ?  17  PHE B CZ    1 
ATOM   2895 N  N     . PHE B 1 38  ? 64.106 -31.805 -8.938  1.00 26.45 ?  18  PHE B N     1 
ATOM   2896 C  CA    . PHE B 1 38  ? 62.780 -32.409 -8.994  1.00 26.99 ?  18  PHE B CA    1 
ATOM   2897 C  C     . PHE B 1 38  ? 62.695 -33.716 -8.213  1.00 31.87 ?  18  PHE B C     1 
ATOM   2898 O  O     . PHE B 1 38  ? 61.586 -34.207 -7.961  1.00 27.35 ?  18  PHE B O     1 
ATOM   2899 C  CB    . PHE B 1 38  ? 62.333 -32.601 -10.450 1.00 24.35 ?  18  PHE B CB    1 
ATOM   2900 C  CG    . PHE B 1 38  ? 61.544 -31.429 -10.975 1.00 24.47 ?  18  PHE B CG    1 
ATOM   2901 C  CD1   . PHE B 1 38  ? 60.242 -31.208 -10.551 1.00 23.71 ?  18  PHE B CD1   1 
ATOM   2902 C  CD2   . PHE B 1 38  ? 62.131 -30.500 -11.818 1.00 19.72 ?  18  PHE B CD2   1 
ATOM   2903 C  CE1   . PHE B 1 38  ? 59.530 -30.106 -11.003 1.00 20.26 ?  18  PHE B CE1   1 
ATOM   2904 C  CE2   . PHE B 1 38  ? 61.426 -29.400 -12.258 1.00 22.25 ?  18  PHE B CE2   1 
ATOM   2905 C  CZ    . PHE B 1 38  ? 60.123 -29.205 -11.853 1.00 18.67 ?  18  PHE B CZ    1 
ATOM   2906 N  N     . ASN B 1 39  ? 63.822 -34.280 -7.794  1.00 26.96 ?  19  ASN B N     1 
ATOM   2907 C  CA    . ASN B 1 39  ? 63.731 -35.389 -6.863  1.00 31.64 ?  19  ASN B CA    1 
ATOM   2908 C  C     . ASN B 1 39  ? 63.482 -34.932 -5.434  1.00 29.29 ?  19  ASN B C     1 
ATOM   2909 O  O     . ASN B 1 39  ? 62.941 -35.713 -4.650  1.00 24.84 ?  19  ASN B O     1 
ATOM   2910 C  CB    . ASN B 1 39  ? 64.982 -36.243 -6.947  1.00 31.88 ?  19  ASN B CB    1 
ATOM   2911 C  CG    . ASN B 1 39  ? 65.074 -36.951 -8.265  1.00 41.36 ?  19  ASN B CG    1 
ATOM   2912 O  OD1   . ASN B 1 39  ? 64.055 -37.403 -8.821  1.00 40.35 ?  19  ASN B OD1   1 
ATOM   2913 N  ND2   . ASN B 1 39  ? 66.284 -37.035 -8.799  1.00 44.21 ?  19  ASN B ND2   1 
ATOM   2914 N  N     . GLN B 1 40  ? 63.826 -33.685 -5.091  1.00 27.07 ?  20  GLN B N     1 
ATOM   2915 C  CA    A GLN B 1 40  ? 63.513 -33.155 -3.774  0.54 24.87 ?  20  GLN B CA    1 
ATOM   2916 C  CA    B GLN B 1 40  ? 63.528 -33.117 -3.782  0.46 25.01 ?  20  GLN B CA    1 
ATOM   2917 C  C     . GLN B 1 40  ? 62.189 -32.401 -3.719  1.00 26.42 ?  20  GLN B C     1 
ATOM   2918 O  O     . GLN B 1 40  ? 61.753 -32.047 -2.623  1.00 35.14 ?  20  GLN B O     1 
ATOM   2919 C  CB    A GLN B 1 40  ? 64.639 -32.232 -3.286  0.54 27.57 ?  20  GLN B CB    1 
ATOM   2920 C  CB    B GLN B 1 40  ? 64.598 -32.109 -3.351  0.46 27.58 ?  20  GLN B CB    1 
ATOM   2921 C  CG    A GLN B 1 40  ? 66.018 -32.893 -3.113  0.54 27.97 ?  20  GLN B CG    1 
ATOM   2922 C  CG    B GLN B 1 40  ? 66.026 -32.436 -3.704  0.46 28.36 ?  20  GLN B CG    1 
ATOM   2923 C  CD    A GLN B 1 40  ? 65.977 -34.260 -2.432  0.54 28.45 ?  20  GLN B CD    1 
ATOM   2924 C  CD    B GLN B 1 40  ? 66.902 -31.202 -3.643  0.46 30.40 ?  20  GLN B CD    1 
ATOM   2925 O  OE1   A GLN B 1 40  ? 66.561 -35.224 -2.928  0.54 27.87 ?  20  GLN B OE1   1 
ATOM   2926 O  OE1   B GLN B 1 40  ? 67.790 -31.015 -4.475  0.46 32.82 ?  20  GLN B OE1   1 
ATOM   2927 N  NE2   A GLN B 1 40  ? 65.304 -34.344 -1.289  0.54 24.95 ?  20  GLN B NE2   1 
ATOM   2928 N  NE2   B GLN B 1 40  ? 66.646 -30.340 -2.657  0.46 30.59 ?  20  GLN B NE2   1 
ATOM   2929 N  N     . LEU B 1 41  ? 61.528 -32.153 -4.852  1.00 27.03 ?  21  LEU B N     1 
ATOM   2930 C  CA    . LEU B 1 41  ? 60.308 -31.343 -4.801  1.00 25.12 ?  21  LEU B CA    1 
ATOM   2931 C  C     . LEU B 1 41  ? 59.193 -31.946 -3.949  1.00 22.90 ?  21  LEU B C     1 
ATOM   2932 O  O     . LEU B 1 41  ? 58.582 -31.201 -3.166  1.00 26.71 ?  21  LEU B O     1 
ATOM   2933 C  CB    . LEU B 1 41  ? 59.801 -31.032 -6.212  1.00 18.83 ?  21  LEU B CB    1 
ATOM   2934 C  CG    . LEU B 1 41  ? 58.608 -30.061 -6.179  1.00 22.37 ?  21  LEU B CG    1 
ATOM   2935 C  CD1   . LEU B 1 41  ? 59.004 -28.715 -5.559  1.00 18.86 ?  21  LEU B CD1   1 
ATOM   2936 C  CD2   . LEU B 1 41  ? 57.945 -29.857 -7.541  1.00 20.00 ?  21  LEU B CD2   1 
ATOM   2937 N  N     . PRO B 1 42  ? 58.848 -33.228 -4.048  1.00 22.51 ?  22  PRO B N     1 
ATOM   2938 C  CA    . PRO B 1 42  ? 57.762 -33.726 -3.183  1.00 27.27 ?  22  PRO B CA    1 
ATOM   2939 C  C     . PRO B 1 42  ? 58.039 -33.513 -1.701  1.00 27.00 ?  22  PRO B C     1 
ATOM   2940 O  O     . PRO B 1 42  ? 57.100 -33.298 -0.916  1.00 27.72 ?  22  PRO B O     1 
ATOM   2941 C  CB    . PRO B 1 42  ? 57.675 -35.221 -3.539  1.00 28.57 ?  22  PRO B CB    1 
ATOM   2942 C  CG    . PRO B 1 42  ? 58.326 -35.340 -4.878  1.00 27.60 ?  22  PRO B CG    1 
ATOM   2943 C  CD    . PRO B 1 42  ? 59.409 -34.303 -4.888  1.00 25.60 ?  22  PRO B CD    1 
ATOM   2944 N  N     . SER B 1 43  ? 59.315 -33.550 -1.311  1.00 25.89 ?  23  SER B N     1 
ATOM   2945 C  CA    . SER B 1 43  ? 59.714 -33.353 0.074   1.00 29.03 ?  23  SER B CA    1 
ATOM   2946 C  C     . SER B 1 43  ? 59.719 -31.875 0.449   1.00 30.97 ?  23  SER B C     1 
ATOM   2947 O  O     . SER B 1 43  ? 59.305 -31.517 1.562   1.00 33.60 ?  23  SER B O     1 
ATOM   2948 C  CB    . SER B 1 43  ? 61.091 -33.982 0.314   1.00 30.12 ?  23  SER B CB    1 
ATOM   2949 O  OG    . SER B 1 43  ? 61.770 -33.379 1.403   1.00 30.12 ?  23  SER B OG    1 
ATOM   2950 N  N     . LEU B 1 44  ? 60.190 -31.013 -0.458  1.00 25.20 ?  24  LEU B N     1 
ATOM   2951 C  CA    . LEU B 1 44  ? 60.064 -29.571 -0.260  1.00 25.25 ?  24  LEU B CA    1 
ATOM   2952 C  C     . LEU B 1 44  ? 58.619 -29.173 -0.012  1.00 25.99 ?  24  LEU B C     1 
ATOM   2953 O  O     . LEU B 1 44  ? 58.323 -28.384 0.897   1.00 28.45 ?  24  LEU B O     1 
ATOM   2954 C  CB    . LEU B 1 44  ? 60.615 -28.812 -1.465  1.00 25.55 ?  24  LEU B CB    1 
ATOM   2955 C  CG    . LEU B 1 44  ? 62.098 -28.442 -1.550  1.00 32.93 ?  24  LEU B CG    1 
ATOM   2956 C  CD1   . LEU B 1 44  ? 63.011 -29.505 -0.959  1.00 34.85 ?  24  LEU B CD1   1 
ATOM   2957 C  CD2   . LEU B 1 44  ? 62.480 -28.155 -3.016  1.00 31.68 ?  24  LEU B CD2   1 
ATOM   2958 N  N     . ASN B 1 45  ? 57.706 -29.710 -0.815  1.00 25.07 ?  25  ASN B N     1 
ATOM   2959 C  CA    . ASN B 1 45  ? 56.306 -29.321 -0.706  1.00 28.39 ?  25  ASN B CA    1 
ATOM   2960 C  C     . ASN B 1 45  ? 55.660 -29.884 0.552   1.00 31.43 ?  25  ASN B C     1 
ATOM   2961 O  O     . ASN B 1 45  ? 54.772 -29.249 1.130   1.00 36.58 ?  25  ASN B O     1 
ATOM   2962 C  CB    . ASN B 1 45  ? 55.558 -29.763 -1.959  1.00 18.21 ?  25  ASN B CB    1 
ATOM   2963 C  CG    . ASN B 1 45  ? 55.850 -28.860 -3.129  1.00 23.58 ?  25  ASN B CG    1 
ATOM   2964 O  OD1   . ASN B 1 45  ? 56.167 -27.681 -2.947  1.00 23.08 ?  25  ASN B OD1   1 
ATOM   2965 N  ND2   . ASN B 1 45  ? 55.765 -29.396 -4.330  1.00 20.76 ?  25  ASN B ND2   1 
ATOM   2966 N  N     . GLN B 1 46  ? 56.096 -31.058 1.001   1.00 29.54 ?  26  GLN B N     1 
ATOM   2967 C  CA    . GLN B 1 46  ? 55.524 -31.625 2.212   1.00 29.32 ?  26  GLN B CA    1 
ATOM   2968 C  C     . GLN B 1 46  ? 55.992 -30.873 3.457   1.00 33.71 ?  26  GLN B C     1 
ATOM   2969 O  O     . GLN B 1 46  ? 55.254 -30.787 4.442   1.00 34.15 ?  26  GLN B O     1 
ATOM   2970 C  CB    . GLN B 1 46  ? 55.862 -33.115 2.259   1.00 27.53 ?  26  GLN B CB    1 
ATOM   2971 C  CG    . GLN B 1 46  ? 54.963 -33.939 3.110   1.00 28.85 ?  26  GLN B CG    1 
ATOM   2972 C  CD    . GLN B 1 46  ? 55.740 -34.684 4.168   1.00 56.89 ?  26  GLN B CD    1 
ATOM   2973 O  OE1   . GLN B 1 46  ? 56.938 -34.453 4.351   1.00 55.93 ?  26  GLN B OE1   1 
ATOM   2974 N  NE2   . GLN B 1 46  ? 55.062 -35.581 4.882   1.00 68.56 ?  26  GLN B NE2   1 
ATOM   2975 N  N     . ASN B 1 47  ? 57.180 -30.280 3.418   1.00 28.54 ?  27  ASN B N     1 
ATOM   2976 C  CA    . ASN B 1 47  ? 57.704 -29.540 4.550   1.00 23.65 ?  27  ASN B CA    1 
ATOM   2977 C  C     . ASN B 1 47  ? 57.482 -28.043 4.434   1.00 28.85 ?  27  ASN B C     1 
ATOM   2978 O  O     . ASN B 1 47  ? 58.070 -27.280 5.206   1.00 39.85 ?  27  ASN B O     1 
ATOM   2979 C  CB    . ASN B 1 47  ? 59.194 -29.846 4.731   1.00 30.13 ?  27  ASN B CB    1 
ATOM   2980 C  CG    . ASN B 1 47  ? 59.429 -31.263 5.214   1.00 35.00 ?  27  ASN B CG    1 
ATOM   2981 O  OD1   . ASN B 1 47  ? 58.718 -31.739 6.086   1.00 41.66 ?  27  ASN B OD1   1 
ATOM   2982 N  ND2   . ASN B 1 47  ? 60.413 -31.940 4.650   1.00 35.67 ?  27  ASN B ND2   1 
ATOM   2983 N  N     . LEU B 1 48  ? 56.641 -27.607 3.502   1.00 33.01 ?  28  LEU B N     1 
ATOM   2984 C  CA    . LEU B 1 48  ? 56.358 -26.182 3.275   1.00 36.41 ?  28  LEU B CA    1 
ATOM   2985 C  C     . LEU B 1 48  ? 57.625 -25.349 3.072   1.00 34.43 ?  28  LEU B C     1 
ATOM   2986 O  O     . LEU B 1 48  ? 57.700 -24.190 3.486   1.00 37.55 ?  28  LEU B O     1 
ATOM   2987 C  CB    . LEU B 1 48  ? 55.533 -25.595 4.416   1.00 24.65 ?  28  LEU B CB    1 
ATOM   2988 C  CG    . LEU B 1 48  ? 54.327 -26.343 4.953   1.00 31.04 ?  28  LEU B CG    1 
ATOM   2989 C  CD1   . LEU B 1 48  ? 53.539 -25.378 5.840   1.00 35.84 ?  28  LEU B CD1   1 
ATOM   2990 C  CD2   . LEU B 1 48  ? 53.482 -26.863 3.816   1.00 33.03 ?  28  LEU B CD2   1 
ATOM   2991 N  N     . GLU B 1 49  ? 58.631 -25.916 2.410   1.00 30.89 ?  29  GLU B N     1 
ATOM   2992 C  CA    . GLU B 1 49  ? 59.915 -25.226 2.338   1.00 29.23 ?  29  GLU B CA    1 
ATOM   2993 C  C     . GLU B 1 49  ? 59.889 -24.190 1.211   1.00 26.31 ?  29  GLU B C     1 
ATOM   2994 O  O     . GLU B 1 49  ? 60.523 -24.313 0.164   1.00 30.42 ?  29  GLU B O     1 
ATOM   2995 C  CB    . GLU B 1 49  ? 61.044 -26.236 2.221   1.00 28.21 ?  29  GLU B CB    1 
ATOM   2996 C  CG    . GLU B 1 49  ? 61.693 -26.498 3.587   1.00 30.04 ?  29  GLU B CG    1 
ATOM   2997 C  CD    . GLU B 1 49  ? 62.264 -27.891 3.713   1.00 43.93 ?  29  GLU B CD    1 
ATOM   2998 O  OE1   . GLU B 1 49  ? 61.935 -28.721 2.840   1.00 51.41 ?  29  GLU B OE1   1 
ATOM   2999 O  OE2   . GLU B 1 49  ? 63.025 -28.168 4.675   1.00 43.34 ?  29  GLU B OE2   1 
ATOM   3000 N  N     . VAL B 1 50  ? 59.162 -23.108 1.483   1.00 27.78 ?  30  VAL B N     1 
ATOM   3001 C  CA    . VAL B 1 50  ? 58.950 -22.065 0.489   1.00 29.58 ?  30  VAL B CA    1 
ATOM   3002 C  C     . VAL B 1 50  ? 60.236 -21.305 0.167   1.00 24.79 ?  30  VAL B C     1 
ATOM   3003 O  O     . VAL B 1 50  ? 60.412 -20.847 -0.967  1.00 30.77 ?  30  VAL B O     1 
ATOM   3004 C  CB    . VAL B 1 50  ? 57.835 -21.116 0.970   1.00 37.83 ?  30  VAL B CB    1 
ATOM   3005 C  CG1   . VAL B 1 50  ? 58.162 -20.518 2.343   1.00 24.55 ?  30  VAL B CG1   1 
ATOM   3006 C  CG2   . VAL B 1 50  ? 57.573 -20.022 -0.066  1.00 30.49 ?  30  VAL B CG2   1 
ATOM   3007 N  N     . SER B 1 51  ? 61.150 -21.152 1.130   1.00 27.07 ?  31  SER B N     1 
ATOM   3008 C  CA    . SER B 1 51  ? 62.396 -20.426 0.865   1.00 30.98 ?  31  SER B CA    1 
ATOM   3009 C  C     . SER B 1 51  ? 63.214 -21.101 -0.227  1.00 24.62 ?  31  SER B C     1 
ATOM   3010 O  O     . SER B 1 51  ? 63.883 -20.430 -1.015  1.00 27.75 ?  31  SER B O     1 
ATOM   3011 C  CB    . SER B 1 51  ? 63.253 -20.301 2.131   1.00 25.22 ?  31  SER B CB    1 
ATOM   3012 O  OG    . SER B 1 51  ? 62.678 -19.430 3.085   1.00 32.16 ?  31  SER B OG    1 
ATOM   3013 N  N     . LEU B 1 52  ? 63.208 -22.425 -0.263  1.00 22.28 ?  32  LEU B N     1 
ATOM   3014 C  CA    . LEU B 1 52  ? 63.963 -23.119 -1.295  1.00 22.00 ?  32  LEU B CA    1 
ATOM   3015 C  C     . LEU B 1 52  ? 63.294 -22.955 -2.658  1.00 26.73 ?  32  LEU B C     1 
ATOM   3016 O  O     . LEU B 1 52  ? 63.978 -22.727 -3.661  1.00 22.09 ?  32  LEU B O     1 
ATOM   3017 C  CB    . LEU B 1 52  ? 64.121 -24.589 -0.903  1.00 26.94 ?  32  LEU B CB    1 
ATOM   3018 C  CG    . LEU B 1 52  ? 64.865 -24.797 0.429   1.00 24.36 ?  32  LEU B CG    1 
ATOM   3019 C  CD1   . LEU B 1 52  ? 64.963 -26.269 0.814   1.00 24.09 ?  32  LEU B CD1   1 
ATOM   3020 C  CD2   . LEU B 1 52  ? 66.236 -24.191 0.331   1.00 18.19 ?  32  LEU B CD2   1 
ATOM   3021 N  N     . LEU B 1 53  ? 61.951 -23.032 -2.695  1.00 29.24 ?  33  LEU B N     1 
ATOM   3022 C  CA    . LEU B 1 53  ? 61.185 -22.743 -3.906  1.00 23.79 ?  33  LEU B CA    1 
ATOM   3023 C  C     . LEU B 1 53  ? 61.477 -21.345 -4.436  1.00 25.46 ?  33  LEU B C     1 
ATOM   3024 O  O     . LEU B 1 53  ? 61.741 -21.167 -5.631  1.00 27.07 ?  33  LEU B O     1 
ATOM   3025 C  CB    . LEU B 1 53  ? 59.688 -22.880 -3.637  1.00 21.16 ?  33  LEU B CB    1 
ATOM   3026 C  CG    . LEU B 1 53  ? 59.077 -24.228 -3.289  1.00 21.99 ?  33  LEU B CG    1 
ATOM   3027 C  CD1   . LEU B 1 53  ? 57.565 -24.056 -3.116  1.00 19.68 ?  33  LEU B CD1   1 
ATOM   3028 C  CD2   . LEU B 1 53  ? 59.398 -25.215 -4.377  1.00 20.08 ?  33  LEU B CD2   1 
ATOM   3029 N  N     . ILE B 1 54  ? 61.379 -20.333 -3.568  1.00 25.35 ?  34  ILE B N     1 
ATOM   3030 C  CA    . ILE B 1 54  ? 61.673 -18.960 -3.973  1.00 23.23 ?  34  ILE B CA    1 
ATOM   3031 C  C     . ILE B 1 54  ? 63.108 -18.851 -4.472  1.00 26.41 ?  34  ILE B C     1 
ATOM   3032 O  O     . ILE B 1 54  ? 63.385 -18.232 -5.510  1.00 25.98 ?  34  ILE B O     1 
ATOM   3033 C  CB    . ILE B 1 54  ? 61.409 -17.992 -2.802  1.00 29.46 ?  34  ILE B CB    1 
ATOM   3034 C  CG1   . ILE B 1 54  ? 59.928 -18.002 -2.456  1.00 27.21 ?  34  ILE B CG1   1 
ATOM   3035 C  CG2   . ILE B 1 54  ? 61.914 -16.552 -3.106  1.00 22.55 ?  34  ILE B CG2   1 
ATOM   3036 C  CD1   . ILE B 1 54  ? 59.112 -17.146 -3.362  1.00 28.48 ?  34  ILE B CD1   1 
ATOM   3037 N  N     . ASP B 1 55  ? 64.044 -19.442 -3.728  1.00 26.13 ?  35  ASP B N     1 
ATOM   3038 C  CA    . ASP B 1 55  ? 65.454 -19.310 -4.077  1.00 27.50 ?  35  ASP B CA    1 
ATOM   3039 C  C     . ASP B 1 55  ? 65.725 -19.916 -5.448  1.00 29.94 ?  35  ASP B C     1 
ATOM   3040 O  O     . ASP B 1 55  ? 66.510 -19.372 -6.234  1.00 25.40 ?  35  ASP B O     1 
ATOM   3041 C  CB    . ASP B 1 55  ? 66.313 -19.978 -3.003  1.00 27.87 ?  35  ASP B CB    1 
ATOM   3042 C  CG    . ASP B 1 55  ? 66.678 -19.027 -1.848  1.00 45.37 ?  35  ASP B CG    1 
ATOM   3043 O  OD1   . ASP B 1 55  ? 67.738 -19.232 -1.210  1.00 58.55 ?  35  ASP B OD1   1 
ATOM   3044 O  OD2   . ASP B 1 55  ? 65.922 -18.064 -1.577  1.00 49.33 ?  35  ASP B OD2   1 
ATOM   3045 N  N     . LYS B 1 56  ? 65.053 -21.031 -5.762  1.00 24.66 ?  36  LYS B N     1 
ATOM   3046 C  CA    . LYS B 1 56  ? 65.222 -21.662 -7.059  1.00 25.75 ?  36  LYS B CA    1 
ATOM   3047 C  C     . LYS B 1 56  ? 64.642 -20.796 -8.187  1.00 29.70 ?  36  LYS B C     1 
ATOM   3048 O  O     . LYS B 1 56  ? 65.208 -20.748 -9.278  1.00 21.67 ?  36  LYS B O     1 
ATOM   3049 C  CB    . LYS B 1 56  ? 64.598 -23.057 -7.025  1.00 18.37 ?  36  LYS B CB    1 
ATOM   3050 C  CG    . LYS B 1 56  ? 65.026 -23.964 -8.167  1.00 28.89 ?  36  LYS B CG    1 
ATOM   3051 C  CD    . LYS B 1 56  ? 66.528 -23.861 -8.465  1.00 31.89 ?  36  LYS B CD    1 
ATOM   3052 C  CE    . LYS B 1 56  ? 67.291 -25.067 -7.904  1.00 27.24 ?  36  LYS B CE    1 
ATOM   3053 N  NZ    . LYS B 1 56  ? 68.724 -25.055 -8.292  1.00 41.78 ?  36  LYS B NZ    1 
ATOM   3054 N  N     . LEU B 1 57  ? 63.549 -20.075 -7.932  1.00 26.43 ?  37  LEU B N     1 
ATOM   3055 C  CA    . LEU B 1 57  ? 63.024 -19.150 -8.931  1.00 28.28 ?  37  LEU B CA    1 
ATOM   3056 C  C     . LEU B 1 57  ? 63.985 -17.993 -9.180  1.00 30.08 ?  37  LEU B C     1 
ATOM   3057 O  O     . LEU B 1 57  ? 64.103 -17.506 -10.312 1.00 29.26 ?  37  LEU B O     1 
ATOM   3058 C  CB    . LEU B 1 57  ? 61.651 -18.624 -8.494  1.00 25.82 ?  37  LEU B CB    1 
ATOM   3059 C  CG    . LEU B 1 57  ? 60.535 -19.685 -8.531  1.00 30.04 ?  37  LEU B CG    1 
ATOM   3060 C  CD1   . LEU B 1 57  ? 59.202 -19.159 -8.003  1.00 18.57 ?  37  LEU B CD1   1 
ATOM   3061 C  CD2   . LEU B 1 57  ? 60.380 -20.287 -9.936  1.00 24.26 ?  37  LEU B CD2   1 
ATOM   3062 N  N     . ARG B 1 58  ? 64.676 -17.535 -8.134  1.00 32.54 ?  38  ARG B N     1 
ATOM   3063 C  CA    . ARG B 1 58  ? 65.620 -16.435 -8.298  1.00 27.84 ?  38  ARG B CA    1 
ATOM   3064 C  C     . ARG B 1 58  ? 66.890 -16.890 -9.009  1.00 31.26 ?  38  ARG B C     1 
ATOM   3065 O  O     . ARG B 1 58  ? 67.386 -16.190 -9.900  1.00 35.36 ?  38  ARG B O     1 
ATOM   3066 C  CB    . ARG B 1 58  ? 65.945 -15.819 -6.938  1.00 27.77 ?  38  ARG B CB    1 
ATOM   3067 C  CG    . ARG B 1 58  ? 64.851 -14.915 -6.399  1.00 21.29 ?  38  ARG B CG    1 
ATOM   3068 C  CD    . ARG B 1 58  ? 65.150 -14.549 -4.966  1.00 22.74 ?  38  ARG B CD    1 
ATOM   3069 N  NE    . ARG B 1 58  ? 64.141 -13.668 -4.388  1.00 27.46 ?  38  ARG B NE    1 
ATOM   3070 C  CZ    . ARG B 1 58  ? 63.939 -13.521 -3.083  1.00 29.68 ?  38  ARG B CZ    1 
ATOM   3071 N  NH1   . ARG B 1 58  ? 64.610 -14.240 -2.192  1.00 27.88 ?  38  ARG B NH1   1 
ATOM   3072 N  NH2   . ARG B 1 58  ? 63.042 -12.633 -2.660  1.00 29.26 ?  38  ARG B NH2   1 
ATOM   3073 N  N     . GLU B 1 59  ? 67.433 -18.056 -8.628  1.00 26.56 ?  39  GLU B N     1 
ATOM   3074 C  CA    . GLU B 1 59  ? 68.525 -18.660 -9.389  1.00 28.31 ?  39  GLU B CA    1 
ATOM   3075 C  C     . GLU B 1 59  ? 68.225 -18.712 -10.882 1.00 34.28 ?  39  GLU B C     1 
ATOM   3076 O  O     . GLU B 1 59  ? 69.090 -18.403 -11.709 1.00 32.50 ?  39  GLU B O     1 
ATOM   3077 C  CB    . GLU B 1 59  ? 68.810 -20.082 -8.909  1.00 33.68 ?  39  GLU B CB    1 
ATOM   3078 C  CG    . GLU B 1 59  ? 69.438 -20.275 -7.544  1.00 45.47 ?  39  GLU B CG    1 
ATOM   3079 C  CD    . GLU B 1 59  ? 69.412 -21.758 -7.164  1.00 53.34 ?  39  GLU B CD    1 
ATOM   3080 O  OE1   . GLU B 1 59  ? 68.824 -22.123 -6.106  1.00 44.13 ?  39  GLU B OE1   1 
ATOM   3081 O  OE2   . GLU B 1 59  ? 69.910 -22.562 -8.001  1.00 47.63 ?  39  GLU B OE2   1 
ATOM   3082 N  N     . ILE B 1 60  ? 67.008 -19.126 -11.245 1.00 34.30 ?  40  ILE B N     1 
ATOM   3083 C  CA    . ILE B 1 60  ? 66.696 -19.394 -12.642 1.00 28.01 ?  40  ILE B CA    1 
ATOM   3084 C  C     . ILE B 1 60  ? 66.653 -18.097 -13.438 1.00 33.05 ?  40  ILE B C     1 
ATOM   3085 O  O     . ILE B 1 60  ? 67.128 -18.041 -14.586 1.00 28.77 ?  40  ILE B O     1 
ATOM   3086 C  CB    . ILE B 1 60  ? 65.371 -20.171 -12.759 1.00 28.81 ?  40  ILE B CB    1 
ATOM   3087 C  CG1   . ILE B 1 60  ? 65.518 -21.594 -12.207 1.00 18.62 ?  40  ILE B CG1   1 
ATOM   3088 C  CG2   . ILE B 1 60  ? 64.869 -20.166 -14.233 1.00 22.33 ?  40  ILE B CG2   1 
ATOM   3089 C  CD1   . ILE B 1 60  ? 64.224 -22.331 -12.163 1.00 14.90 ?  40  ILE B CD1   1 
ATOM   3090 N  N     . THR B 1 61  ? 66.086 -17.032 -12.854 1.00 26.70 ?  41  THR B N     1 
ATOM   3091 C  CA    . THR B 1 61  ? 66.027 -15.781 -13.602 1.00 28.42 ?  41  THR B CA    1 
ATOM   3092 C  C     . THR B 1 61  ? 67.400 -15.151 -13.707 1.00 27.70 ?  41  THR B C     1 
ATOM   3093 O  O     . THR B 1 61  ? 67.669 -14.434 -14.673 1.00 39.57 ?  41  THR B O     1 
ATOM   3094 C  CB    . THR B 1 61  ? 65.033 -14.785 -12.988 1.00 33.15 ?  41  THR B CB    1 
ATOM   3095 O  OG1   . THR B 1 61  ? 65.384 -14.483 -11.630 1.00 31.66 ?  41  THR B OG1   1 
ATOM   3096 C  CG2   . THR B 1 61  ? 63.592 -15.336 -13.054 1.00 34.25 ?  41  THR B CG2   1 
ATOM   3097 N  N     . LYS B 1 62  ? 68.289 -15.444 -12.753 1.00 29.93 ?  42  LYS B N     1 
ATOM   3098 C  CA    . LYS B 1 62  ? 69.651 -14.929 -12.772 1.00 28.98 ?  42  LYS B CA    1 
ATOM   3099 C  C     . LYS B 1 62  ? 70.611 -15.779 -13.605 1.00 31.08 ?  42  LYS B C     1 
ATOM   3100 O  O     . LYS B 1 62  ? 71.639 -15.264 -14.058 1.00 27.76 ?  42  LYS B O     1 
ATOM   3101 C  CB    . LYS B 1 62  ? 70.174 -14.809 -11.338 1.00 23.77 ?  42  LYS B CB    1 
ATOM   3102 C  CG    . LYS B 1 62  ? 69.757 -13.517 -10.661 1.00 35.20 ?  42  LYS B CG    1 
ATOM   3103 C  CD    . LYS B 1 62  ? 69.675 -13.631 -9.144  1.00 34.60 ?  42  LYS B CD    1 
ATOM   3104 C  CE    . LYS B 1 62  ? 69.052 -12.368 -8.551  1.00 45.11 ?  42  LYS B CE    1 
ATOM   3105 N  NZ    . LYS B 1 62  ? 67.856 -12.626 -7.661  1.00 45.57 ?  42  LYS B NZ    1 
ATOM   3106 N  N     . SER B 1 63  ? 70.305 -17.056 -13.831 1.00 28.11 ?  43  SER B N     1 
ATOM   3107 C  CA    . SER B 1 63  ? 71.256 -17.954 -14.466 1.00 30.03 ?  43  SER B CA    1 
ATOM   3108 C  C     . SER B 1 63  ? 70.964 -18.231 -15.933 1.00 33.25 ?  43  SER B C     1 
ATOM   3109 O  O     . SER B 1 63  ? 71.853 -18.711 -16.640 1.00 34.97 ?  43  SER B O     1 
ATOM   3110 C  CB    . SER B 1 63  ? 71.297 -19.293 -13.730 1.00 28.73 ?  43  SER B CB    1 
ATOM   3111 O  OG    . SER B 1 63  ? 71.557 -19.100 -12.360 1.00 38.97 ?  43  SER B OG    1 
ATOM   3112 N  N     . TYR B 1 64  ? 69.750 -17.976 -16.403 1.00 30.65 ?  44  TYR B N     1 
ATOM   3113 C  CA    . TYR B 1 64  ? 69.358 -18.379 -17.742 1.00 29.65 ?  44  TYR B CA    1 
ATOM   3114 C  C     . TYR B 1 64  ? 68.806 -17.187 -18.508 1.00 35.53 ?  44  TYR B C     1 
ATOM   3115 O  O     . TYR B 1 64  ? 68.067 -16.359 -17.957 1.00 32.15 ?  44  TYR B O     1 
ATOM   3116 C  CB    . TYR B 1 64  ? 68.335 -19.525 -17.692 1.00 29.59 ?  44  TYR B CB    1 
ATOM   3117 C  CG    . TYR B 1 64  ? 68.976 -20.802 -17.219 1.00 29.72 ?  44  TYR B CG    1 
ATOM   3118 C  CD1   . TYR B 1 64  ? 69.691 -21.607 -18.100 1.00 21.42 ?  44  TYR B CD1   1 
ATOM   3119 C  CD2   . TYR B 1 64  ? 68.921 -21.175 -15.870 1.00 26.80 ?  44  TYR B CD2   1 
ATOM   3120 C  CE1   . TYR B 1 64  ? 70.300 -22.764 -17.666 1.00 24.63 ?  44  TYR B CE1   1 
ATOM   3121 C  CE2   . TYR B 1 64  ? 69.531 -22.330 -15.422 1.00 23.91 ?  44  TYR B CE2   1 
ATOM   3122 C  CZ    . TYR B 1 64  ? 70.217 -23.125 -16.321 1.00 31.73 ?  44  TYR B CZ    1 
ATOM   3123 O  OH    . TYR B 1 64  ? 70.828 -24.282 -15.878 1.00 32.18 ?  44  TYR B OH    1 
ATOM   3124 N  N     . LEU B 1 65  ? 69.227 -17.085 -19.772 1.00 35.94 ?  45  LEU B N     1 
ATOM   3125 C  CA    . LEU B 1 65  ? 68.673 -16.144 -20.736 1.00 31.20 ?  45  LEU B CA    1 
ATOM   3126 C  C     . LEU B 1 65  ? 67.874 -16.989 -21.705 1.00 32.34 ?  45  LEU B C     1 
ATOM   3127 O  O     . LEU B 1 65  ? 68.454 -17.584 -22.627 1.00 37.28 ?  45  LEU B O     1 
ATOM   3128 C  CB    . LEU B 1 65  ? 69.773 -15.366 -21.467 1.00 33.16 ?  45  LEU B CB    1 
ATOM   3129 C  CG    . LEU B 1 65  ? 70.516 -14.318 -20.636 1.00 33.44 ?  45  LEU B CG    1 
ATOM   3130 C  CD1   . LEU B 1 65  ? 71.607 -13.687 -21.459 1.00 29.69 ?  45  LEU B CD1   1 
ATOM   3131 C  CD2   . LEU B 1 65  ? 69.553 -13.263 -20.098 1.00 18.42 ?  45  LEU B CD2   1 
ATOM   3132 N  N     . PRO B 1 66  ? 66.553 -17.090 -21.538 1.00 36.57 ?  46  PRO B N     1 
ATOM   3133 C  CA    . PRO B 1 66  ? 65.780 -18.045 -22.347 1.00 31.89 ?  46  PRO B CA    1 
ATOM   3134 C  C     . PRO B 1 66  ? 65.942 -17.812 -23.825 1.00 38.92 ?  46  PRO B C     1 
ATOM   3135 O  O     . PRO B 1 66  ? 65.756 -18.745 -24.618 1.00 40.84 ?  46  PRO B O     1 
ATOM   3136 C  CB    . PRO B 1 66  ? 64.332 -17.795 -21.908 1.00 26.43 ?  46  PRO B CB    1 
ATOM   3137 C  CG    . PRO B 1 66  ? 64.415 -16.965 -20.702 1.00 28.02 ?  46  PRO B CG    1 
ATOM   3138 C  CD    . PRO B 1 66  ? 65.677 -16.182 -20.789 1.00 30.25 ?  46  PRO B CD    1 
ATOM   3139 N  N     . THR B 1 67  ? 66.314 -16.594 -24.218 1.00 35.21 ?  47  THR B N     1 
ATOM   3140 C  CA    . THR B 1 67  ? 66.467 -16.266 -25.623 1.00 33.55 ?  47  THR B CA    1 
ATOM   3141 C  C     . THR B 1 67  ? 67.439 -17.191 -26.343 1.00 35.60 ?  47  THR B C     1 
ATOM   3142 O  O     . THR B 1 67  ? 67.444 -17.224 -27.576 1.00 41.76 ?  47  THR B O     1 
ATOM   3143 C  CB    . THR B 1 67  ? 66.920 -14.824 -25.748 1.00 29.18 ?  47  THR B CB    1 
ATOM   3144 O  OG1   . THR B 1 67  ? 66.584 -14.362 -27.051 1.00 32.28 ?  47  THR B OG1   1 
ATOM   3145 C  CG2   . THR B 1 67  ? 68.413 -14.731 -25.538 1.00 26.89 ?  47  THR B CG2   1 
ATOM   3146 N  N     . THR B 1 68  ? 68.258 -17.946 -25.613 1.00 36.38 ?  48  THR B N     1 
ATOM   3147 C  CA    . THR B 1 68  ? 69.110 -18.947 -26.233 1.00 33.08 ?  48  THR B CA    1 
ATOM   3148 C  C     . THR B 1 68  ? 68.425 -20.305 -26.355 1.00 39.95 ?  48  THR B C     1 
ATOM   3149 O  O     . THR B 1 68  ? 69.070 -21.268 -26.785 1.00 35.13 ?  48  THR B O     1 
ATOM   3150 C  CB    . THR B 1 68  ? 70.425 -19.118 -25.446 1.00 37.54 ?  48  THR B CB    1 
ATOM   3151 O  OG1   . THR B 1 68  ? 70.168 -19.787 -24.204 1.00 35.74 ?  48  THR B OG1   1 
ATOM   3152 C  CG2   . THR B 1 68  ? 71.091 -17.775 -25.168 1.00 34.72 ?  48  THR B CG2   1 
ATOM   3153 N  N     . PHE B 1 69  ? 67.150 -20.421 -25.975 1.00 36.84 ?  49  PHE B N     1 
ATOM   3154 C  CA    . PHE B 1 69  ? 66.488 -21.720 -25.982 1.00 37.75 ?  49  PHE B CA    1 
ATOM   3155 C  C     . PHE B 1 69  ? 65.928 -22.013 -27.366 1.00 35.06 ?  49  PHE B C     1 
ATOM   3156 O  O     . PHE B 1 69  ? 65.411 -21.118 -28.041 1.00 34.14 ?  49  PHE B O     1 
ATOM   3157 C  CB    . PHE B 1 69  ? 65.341 -21.806 -24.961 1.00 34.06 ?  49  PHE B CB    1 
ATOM   3158 C  CG    . PHE B 1 69  ? 65.763 -21.693 -23.527 1.00 32.39 ?  49  PHE B CG    1 
ATOM   3159 C  CD1   . PHE B 1 69  ? 67.102 -21.627 -23.166 1.00 42.65 ?  49  PHE B CD1   1 
ATOM   3160 C  CD2   . PHE B 1 69  ? 64.810 -21.639 -22.531 1.00 29.05 ?  49  PHE B CD2   1 
ATOM   3161 C  CE1   . PHE B 1 69  ? 67.477 -21.502 -21.832 1.00 34.78 ?  49  PHE B CE1   1 
ATOM   3162 C  CE2   . PHE B 1 69  ? 65.182 -21.506 -21.194 1.00 33.24 ?  49  PHE B CE2   1 
ATOM   3163 C  CZ    . PHE B 1 69  ? 66.517 -21.444 -20.851 1.00 26.62 ?  49  PHE B CZ    1 
ATOM   3164 N  N     . SER B 1 70  ? 66.041 -23.278 -27.776 1.00 29.71 ?  50  SER B N     1 
ATOM   3165 C  CA    . SER B 1 70  ? 65.244 -23.808 -28.865 1.00 26.45 ?  50  SER B CA    1 
ATOM   3166 C  C     . SER B 1 70  ? 63.789 -23.914 -28.423 1.00 26.26 ?  50  SER B C     1 
ATOM   3167 O  O     . SER B 1 70  ? 63.470 -23.780 -27.245 1.00 28.50 ?  50  SER B O     1 
ATOM   3168 C  CB    . SER B 1 70  ? 65.758 -25.180 -29.280 1.00 26.20 ?  50  SER B CB    1 
ATOM   3169 O  OG    . SER B 1 70  ? 65.472 -26.137 -28.275 1.00 26.82 ?  50  SER B OG    1 
ATOM   3170 N  N     . ILE B 1 71  ? 62.893 -24.166 -29.383 1.00 32.52 ?  51  ILE B N     1 
ATOM   3171 C  CA    . ILE B 1 71  ? 61.477 -24.301 -29.046 1.00 25.52 ?  51  ILE B CA    1 
ATOM   3172 C  C     . ILE B 1 71  ? 61.268 -25.436 -28.048 1.00 25.88 ?  51  ILE B C     1 
ATOM   3173 O  O     . ILE B 1 71  ? 60.588 -25.268 -27.024 1.00 28.86 ?  51  ILE B O     1 
ATOM   3174 C  CB    . ILE B 1 71  ? 60.632 -24.497 -30.312 1.00 28.61 ?  51  ILE B CB    1 
ATOM   3175 C  CG1   . ILE B 1 71  ? 60.608 -23.195 -31.124 1.00 35.99 ?  51  ILE B CG1   1 
ATOM   3176 C  CG2   . ILE B 1 71  ? 59.242 -24.935 -29.939 1.00 17.32 ?  51  ILE B CG2   1 
ATOM   3177 C  CD1   . ILE B 1 71  ? 59.521 -23.128 -32.206 1.00 23.21 ?  51  ILE B CD1   1 
ATOM   3178 N  N     . ASN B 1 72  ? 61.872 -26.600 -28.306 1.00 23.37 ?  52  ASN B N     1 
ATOM   3179 C  CA    . ASN B 1 72  ? 61.699 -27.714 -27.377 1.00 25.12 ?  52  ASN B CA    1 
ATOM   3180 C  C     . ASN B 1 72  ? 62.204 -27.347 -25.987 1.00 21.22 ?  52  ASN B C     1 
ATOM   3181 O  O     . ASN B 1 72  ? 61.521 -27.598 -24.994 1.00 20.61 ?  52  ASN B O     1 
ATOM   3182 C  CB    . ASN B 1 72  ? 62.386 -28.968 -27.910 1.00 18.44 ?  52  ASN B CB    1 
ATOM   3183 C  CG    . ASN B 1 72  ? 61.637 -29.576 -29.125 1.00 31.15 ?  52  ASN B CG    1 
ATOM   3184 O  OD1   . ASN B 1 72  ? 60.472 -29.248 -29.390 1.00 22.73 ?  52  ASN B OD1   1 
ATOM   3185 N  ND2   . ASN B 1 72  ? 62.324 -30.443 -29.873 1.00 24.92 ?  52  ASN B ND2   1 
ATOM   3186 N  N     . ASP B 1 73  ? 63.374 -26.709 -25.908 1.00 24.46 ?  53  ASP B N     1 
ATOM   3187 C  CA    . ASP B 1 73  ? 63.893 -26.206 -24.640 1.00 21.61 ?  53  ASP B CA    1 
ATOM   3188 C  C     . ASP B 1 73  ? 62.891 -25.296 -23.933 1.00 27.32 ?  53  ASP B C     1 
ATOM   3189 O  O     . ASP B 1 73  ? 62.608 -25.467 -22.743 1.00 26.23 ?  53  ASP B O     1 
ATOM   3190 C  CB    . ASP B 1 73  ? 65.194 -25.445 -24.863 1.00 21.69 ?  53  ASP B CB    1 
ATOM   3191 C  CG    . ASP B 1 73  ? 66.357 -26.351 -25.146 1.00 33.43 ?  53  ASP B CG    1 
ATOM   3192 O  OD1   . ASP B 1 73  ? 66.320 -27.512 -24.678 1.00 32.61 ?  53  ASP B OD1   1 
ATOM   3193 O  OD2   . ASP B 1 73  ? 67.333 -25.883 -25.797 1.00 41.56 ?  53  ASP B OD2   1 
ATOM   3194 N  N     . ALA B 1 74  ? 62.379 -24.292 -24.639 1.00 21.06 ?  54  ALA B N     1 
ATOM   3195 C  CA    . ALA B 1 74  ? 61.385 -23.423 -24.031 1.00 25.62 ?  54  ALA B CA    1 
ATOM   3196 C  C     . ALA B 1 74  ? 60.125 -24.190 -23.649 1.00 24.55 ?  54  ALA B C     1 
ATOM   3197 O  O     . ALA B 1 74  ? 59.468 -23.840 -22.659 1.00 27.78 ?  54  ALA B O     1 
ATOM   3198 C  CB    . ALA B 1 74  ? 61.046 -22.265 -24.968 1.00 21.63 ?  54  ALA B CB    1 
ATOM   3199 N  N     . LEU B 1 75  ? 59.762 -25.227 -24.408 1.00 20.30 ?  55  LEU B N     1 
ATOM   3200 C  CA    . LEU B 1 75  ? 58.595 -26.018 -24.025 1.00 25.74 ?  55  LEU B CA    1 
ATOM   3201 C  C     . LEU B 1 75  ? 58.846 -26.754 -22.713 1.00 26.27 ?  55  LEU B C     1 
ATOM   3202 O  O     . LEU B 1 75  ? 58.011 -26.730 -21.800 1.00 20.36 ?  55  LEU B O     1 
ATOM   3203 C  CB    . LEU B 1 75  ? 58.226 -27.002 -25.134 1.00 19.81 ?  55  LEU B CB    1 
ATOM   3204 C  CG    . LEU B 1 75  ? 57.511 -26.391 -26.336 1.00 25.79 ?  55  LEU B CG    1 
ATOM   3205 C  CD1   . LEU B 1 75  ? 57.238 -27.470 -27.370 1.00 20.09 ?  55  LEU B CD1   1 
ATOM   3206 C  CD2   . LEU B 1 75  ? 56.223 -25.667 -25.916 1.00 18.31 ?  55  LEU B CD2   1 
ATOM   3207 N  N     . ALA B 1 76  ? 60.006 -27.402 -22.606 1.00 26.94 ?  56  ALA B N     1 
ATOM   3208 C  CA    . ALA B 1 76  ? 60.368 -28.129 -21.401 1.00 23.50 ?  56  ALA B CA    1 
ATOM   3209 C  C     . ALA B 1 76  ? 60.667 -27.180 -20.240 1.00 25.25 ?  56  ALA B C     1 
ATOM   3210 O  O     . ALA B 1 76  ? 60.469 -27.552 -19.075 1.00 27.53 ?  56  ALA B O     1 
ATOM   3211 C  CB    . ALA B 1 76  ? 61.565 -29.036 -21.695 1.00 19.30 ?  56  ALA B CB    1 
ATOM   3212 N  N     . ALA B 1 77  ? 61.138 -25.961 -20.525 1.00 17.84 ?  57  ALA B N     1 
ATOM   3213 C  CA    . ALA B 1 77  ? 61.366 -25.004 -19.452 1.00 18.17 ?  57  ALA B CA    1 
ATOM   3214 C  C     . ALA B 1 77  ? 60.049 -24.514 -18.871 1.00 21.61 ?  57  ALA B C     1 
ATOM   3215 O  O     . ALA B 1 77  ? 59.935 -24.334 -17.656 1.00 25.72 ?  57  ALA B O     1 
ATOM   3216 C  CB    . ALA B 1 77  ? 62.207 -23.834 -19.937 1.00 19.02 ?  57  ALA B CB    1 
ATOM   3217 N  N     . THR B 1 78  ? 59.032 -24.336 -19.710 1.00 22.76 ?  58  THR B N     1 
ATOM   3218 C  CA    . THR B 1 78  ? 57.714 -23.960 -19.203 1.00 20.82 ?  58  THR B CA    1 
ATOM   3219 C  C     . THR B 1 78  ? 57.132 -25.049 -18.313 1.00 25.02 ?  58  THR B C     1 
ATOM   3220 O  O     . THR B 1 78  ? 56.497 -24.754 -17.291 1.00 31.04 ?  58  THR B O     1 
ATOM   3221 C  CB    . THR B 1 78  ? 56.795 -23.657 -20.382 1.00 20.85 ?  58  THR B CB    1 
ATOM   3222 O  OG1   . THR B 1 78  ? 57.440 -22.673 -21.189 1.00 21.48 ?  58  THR B OG1   1 
ATOM   3223 C  CG2   . THR B 1 78  ? 55.412 -23.157 -19.953 1.00 12.26 ?  58  THR B CG2   1 
ATOM   3224 N  N     . ARG B 1 79  ? 57.338 -26.316 -18.684 1.00 24.10 ?  59  ARG B N     1 
ATOM   3225 C  CA    . ARG B 1 79  ? 56.940 -27.423 -17.818 1.00 23.71 ?  59  ARG B CA    1 
ATOM   3226 C  C     . ARG B 1 79  ? 57.571 -27.303 -16.427 1.00 24.78 ?  59  ARG B C     1 
ATOM   3227 O  O     . ARG B 1 79  ? 56.882 -27.417 -15.408 1.00 19.41 ?  59  ARG B O     1 
ATOM   3228 C  CB    . ARG B 1 79  ? 57.333 -28.755 -18.466 1.00 22.52 ?  59  ARG B CB    1 
ATOM   3229 C  CG    . ARG B 1 79  ? 57.315 -29.948 -17.490 1.00 20.09 ?  59  ARG B CG    1 
ATOM   3230 C  CD    . ARG B 1 79  ? 58.120 -31.095 -18.026 1.00 20.95 ?  59  ARG B CD    1 
ATOM   3231 N  NE    . ARG B 1 79  ? 59.548 -30.799 -18.043 1.00 19.10 ?  59  ARG B NE    1 
ATOM   3232 C  CZ    . ARG B 1 79  ? 60.402 -31.258 -18.950 1.00 22.51 ?  59  ARG B CZ    1 
ATOM   3233 N  NH1   . ARG B 1 79  ? 60.002 -32.032 -19.958 1.00 21.70 ?  59  ARG B NH1   1 
ATOM   3234 N  NH2   . ARG B 1 79  ? 61.688 -30.931 -18.850 1.00 22.05 ?  59  ARG B NH2   1 
ATOM   3235 N  N     . ASP B 1 80  ? 58.889 -27.072 -16.371 1.00 25.93 ?  60  ASP B N     1 
ATOM   3236 C  CA    . ASP B 1 80  ? 59.613 -27.151 -15.106 1.00 22.56 ?  60  ASP B CA    1 
ATOM   3237 C  C     . ASP B 1 80  ? 59.462 -25.869 -14.289 1.00 28.72 ?  60  ASP B C     1 
ATOM   3238 O  O     . ASP B 1 80  ? 59.056 -25.917 -13.118 1.00 26.96 ?  60  ASP B O     1 
ATOM   3239 C  CB    . ASP B 1 80  ? 61.082 -27.484 -15.367 1.00 17.09 ?  60  ASP B CB    1 
ATOM   3240 C  CG    . ASP B 1 80  ? 61.265 -28.903 -15.889 1.00 22.78 ?  60  ASP B CG    1 
ATOM   3241 O  OD1   . ASP B 1 80  ? 60.255 -29.628 -16.021 1.00 21.37 ?  60  ASP B OD1   1 
ATOM   3242 O  OD2   . ASP B 1 80  ? 62.409 -29.302 -16.176 1.00 23.55 ?  60  ASP B OD2   1 
ATOM   3243 N  N     . LEU B 1 81  ? 59.780 -24.717 -14.884 1.00 22.41 ?  61  LEU B N     1 
ATOM   3244 C  CA    . LEU B 1 81  ? 59.510 -23.455 -14.213 1.00 20.71 ?  61  LEU B CA    1 
ATOM   3245 C  C     . LEU B 1 81  ? 58.053 -23.378 -13.766 1.00 22.03 ?  61  LEU B C     1 
ATOM   3246 O  O     . LEU B 1 81  ? 57.759 -22.906 -12.666 1.00 25.30 ?  61  LEU B O     1 
ATOM   3247 C  CB    . LEU B 1 81  ? 59.845 -22.275 -15.136 1.00 25.43 ?  61  LEU B CB    1 
ATOM   3248 C  CG    . LEU B 1 81  ? 60.217 -20.947 -14.457 1.00 26.50 ?  61  LEU B CG    1 
ATOM   3249 C  CD1   . LEU B 1 81  ? 60.880 -21.234 -13.167 1.00 29.98 ?  61  LEU B CD1   1 
ATOM   3250 C  CD2   . LEU B 1 81  ? 61.098 -20.048 -15.288 1.00 30.15 ?  61  LEU B CD2   1 
ATOM   3251 N  N     . GLY B 1 82  ? 57.127 -23.846 -14.605 1.00 25.50 ?  62  GLY B N     1 
ATOM   3252 C  CA    . GLY B 1 82  ? 55.717 -23.718 -14.277 1.00 22.10 ?  62  GLY B CA    1 
ATOM   3253 C  C     . GLY B 1 82  ? 55.334 -24.510 -13.044 1.00 29.48 ?  62  GLY B C     1 
ATOM   3254 O  O     . GLY B 1 82  ? 54.542 -24.048 -12.218 1.00 33.88 ?  62  GLY B O     1 
ATOM   3255 N  N     . MET B 1 83  ? 55.890 -25.712 -12.892 1.00 25.39 ?  63  MET B N     1 
ATOM   3256 C  CA    . MET B 1 83  ? 55.535 -26.492 -11.720 1.00 26.73 ?  63  MET B CA    1 
ATOM   3257 C  C     . MET B 1 83  ? 56.156 -25.934 -10.448 1.00 25.23 ?  63  MET B C     1 
ATOM   3258 O  O     . MET B 1 83  ? 55.538 -26.020 -9.387  1.00 28.36 ?  63  MET B O     1 
ATOM   3259 C  CB    . MET B 1 83  ? 55.904 -27.955 -11.924 1.00 25.04 ?  63  MET B CB    1 
ATOM   3260 C  CG    . MET B 1 83  ? 54.974 -28.628 -12.906 1.00 25.57 ?  63  MET B CG    1 
ATOM   3261 S  SD    . MET B 1 83  ? 55.485 -30.299 -13.242 1.00 32.46 ?  63  MET B SD    1 
ATOM   3262 C  CE    . MET B 1 83  ? 54.882 -31.092 -11.720 1.00 24.34 ?  63  MET B CE    1 
ATOM   3263 N  N     . ILE B 1 84  ? 57.352 -25.351 -10.518 1.00 24.25 ?  64  ILE B N     1 
ATOM   3264 C  CA    . ILE B 1 84  ? 57.877 -24.653 -9.348  1.00 23.84 ?  64  ILE B CA    1 
ATOM   3265 C  C     . ILE B 1 84  ? 56.972 -23.477 -8.991  1.00 25.65 ?  64  ILE B C     1 
ATOM   3266 O  O     . ILE B 1 84  ? 56.594 -23.297 -7.828  1.00 25.84 ?  64  ILE B O     1 
ATOM   3267 C  CB    . ILE B 1 84  ? 59.328 -24.196 -9.572  1.00 20.21 ?  64  ILE B CB    1 
ATOM   3268 C  CG1   . ILE B 1 84  ? 60.260 -25.387 -9.717  1.00 15.92 ?  64  ILE B CG1   1 
ATOM   3269 C  CG2   . ILE B 1 84  ? 59.790 -23.433 -8.374  1.00 19.51 ?  64  ILE B CG2   1 
ATOM   3270 C  CD1   . ILE B 1 84  ? 61.570 -24.994 -10.309 1.00 16.82 ?  64  ILE B CD1   1 
ATOM   3271 N  N     . MET B 1 85  ? 56.594 -22.669 -9.992  1.00 19.13 ?  65  MET B N     1 
ATOM   3272 C  CA    . MET B 1 85  ? 55.622 -21.605 -9.748  1.00 22.62 ?  65  MET B CA    1 
ATOM   3273 C  C     . MET B 1 85  ? 54.341 -22.124 -9.109  1.00 21.56 ?  65  MET B C     1 
ATOM   3274 O  O     . MET B 1 85  ? 53.831 -21.509 -8.170  1.00 19.46 ?  65  MET B O     1 
ATOM   3275 C  CB    . MET B 1 85  ? 55.303 -20.833 -11.036 1.00 16.34 ?  65  MET B CB    1 
ATOM   3276 C  CG    . MET B 1 85  ? 56.507 -20.270 -11.799 1.00 25.41 ?  65  MET B CG    1 
ATOM   3277 S  SD    . MET B 1 85  ? 56.074 -18.962 -13.019 1.00 29.56 ?  65  MET B SD    1 
ATOM   3278 C  CE    . MET B 1 85  ? 55.198 -19.978 -14.224 1.00 19.21 ?  65  MET B CE    1 
ATOM   3279 N  N     . SER B 1 86  ? 53.800 -23.239 -9.606  1.00 22.88 ?  66  SER B N     1 
ATOM   3280 C  CA    . SER B 1 86  ? 52.551 -23.770 -9.049  1.00 29.88 ?  66  SER B CA    1 
ATOM   3281 C  C     . SER B 1 86  ? 52.702 -24.224 -7.595  1.00 26.92 ?  66  SER B C     1 
ATOM   3282 O  O     . SER B 1 86  ? 51.727 -24.195 -6.823  1.00 20.22 ?  66  SER B O     1 
ATOM   3283 C  CB    . SER B 1 86  ? 52.049 -24.932 -9.907  1.00 27.26 ?  66  SER B CB    1 
ATOM   3284 O  OG    . SER B 1 86  ? 51.702 -24.469 -11.192 1.00 27.37 ?  66  SER B OG    1 
ATOM   3285 N  N     . SER B 1 87  ? 53.908 -24.661 -7.217  1.00 23.42 ?  67  SER B N     1 
ATOM   3286 C  CA    . SER B 1 87  ? 54.187 -25.023 -5.832  1.00 25.90 ?  67  SER B CA    1 
ATOM   3287 C  C     . SER B 1 87  ? 54.181 -23.789 -4.927  1.00 25.54 ?  67  SER B C     1 
ATOM   3288 O  O     . SER B 1 87  ? 53.695 -23.840 -3.793  1.00 25.19 ?  67  SER B O     1 
ATOM   3289 C  CB    . SER B 1 87  ? 55.532 -25.748 -5.757  1.00 20.90 ?  67  SER B CB    1 
ATOM   3290 O  OG    . SER B 1 87  ? 55.575 -26.836 -6.666  1.00 16.87 ?  67  SER B OG    1 
ATOM   3291 N  N     . VAL B 1 88  ? 54.714 -22.671 -5.413  1.00 21.53 ?  68  VAL B N     1 
ATOM   3292 C  CA    . VAL B 1 88  ? 54.689 -21.438 -4.642  1.00 20.46 ?  68  VAL B CA    1 
ATOM   3293 C  C     . VAL B 1 88  ? 53.259 -20.944 -4.494  1.00 23.24 ?  68  VAL B C     1 
ATOM   3294 O  O     . VAL B 1 88  ? 52.800 -20.631 -3.387  1.00 30.73 ?  68  VAL B O     1 
ATOM   3295 C  CB    . VAL B 1 88  ? 55.595 -20.386 -5.305  1.00 21.71 ?  68  VAL B CB    1 
ATOM   3296 C  CG1   . VAL B 1 88  ? 55.463 -19.024 -4.603  1.00 22.55 ?  68  VAL B CG1   1 
ATOM   3297 C  CG2   . VAL B 1 88  ? 57.040 -20.881 -5.337  1.00 17.86 ?  68  VAL B CG2   1 
ATOM   3298 N  N     . ARG B 1 89  ? 52.522 -20.907 -5.601  1.00 19.85 ?  69  ARG B N     1 
ATOM   3299 C  CA    . ARG B 1 89  ? 51.122 -20.517 -5.554  1.00 23.45 ?  69  ARG B CA    1 
ATOM   3300 C  C     . ARG B 1 89  ? 50.302 -21.436 -4.637  1.00 23.94 ?  69  ARG B C     1 
ATOM   3301 O  O     . ARG B 1 89  ? 49.297 -21.004 -4.062  1.00 21.47 ?  69  ARG B O     1 
ATOM   3302 C  CB    . ARG B 1 89  ? 50.560 -20.497 -6.975  1.00 15.92 ?  69  ARG B CB    1 
ATOM   3303 C  CG    . ARG B 1 89  ? 49.058 -20.339 -7.048  1.00 18.91 ?  69  ARG B CG    1 
ATOM   3304 C  CD    . ARG B 1 89  ? 48.631 -18.970 -6.532  1.00 24.47 ?  69  ARG B CD    1 
ATOM   3305 N  NE    . ARG B 1 89  ? 47.181 -18.818 -6.519  1.00 28.05 ?  69  ARG B NE    1 
ATOM   3306 C  CZ    . ARG B 1 89  ? 46.398 -19.216 -5.523  1.00 32.33 ?  69  ARG B CZ    1 
ATOM   3307 N  NH1   . ARG B 1 89  ? 46.894 -19.804 -4.444  1.00 19.67 ?  69  ARG B NH1   1 
ATOM   3308 N  NH2   . ARG B 1 89  ? 45.086 -19.022 -5.615  1.00 33.66 ?  69  ARG B NH2   1 
ATOM   3309 N  N     . LYS B 1 90  ? 50.714 -22.694 -4.472  1.00 24.76 ?  70  LYS B N     1 
ATOM   3310 C  CA    . LYS B 1 90  ? 49.966 -23.588 -3.587  1.00 26.80 ?  70  LYS B CA    1 
ATOM   3311 C  C     . LYS B 1 90  ? 49.958 -23.064 -2.151  1.00 23.97 ?  70  LYS B C     1 
ATOM   3312 O  O     . LYS B 1 90  ? 48.951 -23.176 -1.440  1.00 24.71 ?  70  LYS B O     1 
ATOM   3313 C  CB    . LYS B 1 90  ? 50.550 -25.003 -3.665  1.00 24.99 ?  70  LYS B CB    1 
ATOM   3314 C  CG    . LYS B 1 90  ? 49.938 -26.014 -2.739  1.00 19.58 ?  70  LYS B CG    1 
ATOM   3315 C  CD    . LYS B 1 90  ? 50.946 -26.443 -1.710  1.00 25.52 ?  70  LYS B CD    1 
ATOM   3316 C  CE    . LYS B 1 90  ? 50.264 -27.126 -0.531  1.00 35.00 ?  70  LYS B CE    1 
ATOM   3317 N  NZ    . LYS B 1 90  ? 51.219 -27.374 0.586   1.00 39.72 ?  70  LYS B NZ    1 
ATOM   3318 N  N     . LEU B 1 91  ? 51.058 -22.460 -1.719  1.00 27.96 ?  71  LEU B N     1 
ATOM   3319 C  CA    . LEU B 1 91  ? 51.130 -21.920 -0.370  1.00 23.95 ?  71  LEU B CA    1 
ATOM   3320 C  C     . LEU B 1 91  ? 50.336 -20.633 -0.199  1.00 24.29 ?  71  LEU B C     1 
ATOM   3321 O  O     . LEU B 1 91  ? 50.169 -20.179 0.936   1.00 33.23 ?  71  LEU B O     1 
ATOM   3322 C  CB    . LEU B 1 91  ? 52.589 -21.686 0.007   1.00 30.38 ?  71  LEU B CB    1 
ATOM   3323 C  CG    . LEU B 1 91  ? 53.462 -22.921 -0.188  1.00 28.17 ?  71  LEU B CG    1 
ATOM   3324 C  CD1   . LEU B 1 91  ? 54.918 -22.568 -0.039  1.00 28.70 ?  71  LEU B CD1   1 
ATOM   3325 C  CD2   . LEU B 1 91  ? 53.068 -23.967 0.801   1.00 29.70 ?  71  LEU B CD2   1 
ATOM   3326 N  N     . GLY B 1 92  ? 49.847 -20.038 -1.285  1.00 27.33 ?  72  GLY B N     1 
ATOM   3327 C  CA    . GLY B 1 92  ? 49.069 -18.815 -1.243  1.00 19.84 ?  72  GLY B CA    1 
ATOM   3328 C  C     . GLY B 1 92  ? 49.765 -17.613 -1.841  1.00 22.57 ?  72  GLY B C     1 
ATOM   3329 O  O     . GLY B 1 92  ? 49.109 -16.590 -2.053  1.00 23.89 ?  72  GLY B O     1 
ATOM   3330 N  N     . ILE B 1 93  ? 51.066 -17.703 -2.126  1.00 22.40 ?  73  ILE B N     1 
ATOM   3331 C  CA    . ILE B 1 93  ? 51.851 -16.572 -2.609  1.00 18.72 ?  73  ILE B CA    1 
ATOM   3332 C  C     . ILE B 1 93  ? 51.790 -16.507 -4.123  1.00 24.07 ?  73  ILE B C     1 
ATOM   3333 O  O     . ILE B 1 93  ? 52.097 -17.497 -4.809  1.00 23.11 ?  73  ILE B O     1 
ATOM   3334 C  CB    . ILE B 1 93  ? 53.315 -16.682 -2.153  1.00 24.70 ?  73  ILE B CB    1 
ATOM   3335 C  CG1   . ILE B 1 93  ? 53.431 -16.425 -0.641  1.00 28.83 ?  73  ILE B CG1   1 
ATOM   3336 C  CG2   . ILE B 1 93  ? 54.188 -15.692 -2.946  1.00 19.58 ?  73  ILE B CG2   1 
ATOM   3337 C  CD1   . ILE B 1 93  ? 54.355 -17.369 0.069   1.00 23.58 ?  73  ILE B CD1   1 
ATOM   3338 N  N     . GLN B 1 94  ? 51.443 -15.335 -4.651  1.00 24.02 ?  74  GLN B N     1 
ATOM   3339 C  CA    . GLN B 1 94  ? 51.563 -15.118 -6.095  1.00 21.64 ?  74  GLN B CA    1 
ATOM   3340 C  C     . GLN B 1 94  ? 53.031 -15.131 -6.513  1.00 26.06 ?  74  GLN B C     1 
ATOM   3341 O  O     . GLN B 1 94  ? 53.754 -14.165 -6.221  1.00 25.32 ?  74  GLN B O     1 
ATOM   3342 C  CB    . GLN B 1 94  ? 50.906 -13.810 -6.498  1.00 16.96 ?  74  GLN B CB    1 
ATOM   3343 C  CG    . GLN B 1 94  ? 49.429 -13.945 -6.790  1.00 20.42 ?  74  GLN B CG    1 
ATOM   3344 C  CD    . GLN B 1 94  ? 49.137 -14.908 -7.933  1.00 26.60 ?  74  GLN B CD    1 
ATOM   3345 O  OE1   . GLN B 1 94  ? 49.990 -15.160 -8.788  1.00 27.28 ?  74  GLN B OE1   1 
ATOM   3346 N  NE2   . GLN B 1 94  ? 47.919 -15.437 -7.962  1.00 22.83 ?  74  GLN B NE2   1 
ATOM   3347 N  N     . PRO B 1 95  ? 53.502 -16.157 -7.237  1.00 24.57 ?  75  PRO B N     1 
ATOM   3348 C  CA    . PRO B 1 95  ? 54.959 -16.307 -7.436  1.00 22.32 ?  75  PRO B CA    1 
ATOM   3349 C  C     . PRO B 1 95  ? 55.605 -15.220 -8.296  1.00 26.43 ?  75  PRO B C     1 
ATOM   3350 O  O     . PRO B 1 95  ? 56.792 -14.929 -8.094  1.00 28.56 ?  75  PRO B O     1 
ATOM   3351 C  CB    . PRO B 1 95  ? 55.088 -17.705 -8.076  1.00 17.30 ?  75  PRO B CB    1 
ATOM   3352 C  CG    . PRO B 1 95  ? 53.784 -17.976 -8.688  1.00 19.77 ?  75  PRO B CG    1 
ATOM   3353 C  CD    . PRO B 1 95  ? 52.734 -17.233 -7.890  1.00 22.37 ?  75  PRO B CD    1 
ATOM   3354 N  N     . VAL B 1 96  ? 54.884 -14.619 -9.250  1.00 23.00 ?  76  VAL B N     1 
ATOM   3355 C  CA    . VAL B 1 96  ? 55.475 -13.536 -10.034 1.00 25.80 ?  76  VAL B CA    1 
ATOM   3356 C  C     . VAL B 1 96  ? 55.548 -12.248 -9.231  1.00 32.50 ?  76  VAL B C     1 
ATOM   3357 O  O     . VAL B 1 96  ? 56.393 -11.391 -9.518  1.00 35.29 ?  76  VAL B O     1 
ATOM   3358 C  CB    . VAL B 1 96  ? 54.707 -13.279 -11.346 1.00 28.53 ?  76  VAL B CB    1 
ATOM   3359 C  CG1   . VAL B 1 96  ? 55.515 -12.366 -12.246 1.00 32.10 ?  76  VAL B CG1   1 
ATOM   3360 C  CG2   . VAL B 1 96  ? 54.371 -14.600 -12.066 1.00 27.83 ?  76  VAL B CG2   1 
ATOM   3361 N  N     . SER B 1 97  ? 54.686 -12.095 -8.220  1.00 31.94 ?  77  SER B N     1 
ATOM   3362 C  CA    . SER B 1 97  ? 54.793 -10.961 -7.310  1.00 22.96 ?  77  SER B CA    1 
ATOM   3363 C  C     . SER B 1 97  ? 56.012 -11.069 -6.398  1.00 29.41 ?  77  SER B C     1 
ATOM   3364 O  O     . SER B 1 97  ? 56.624 -10.046 -6.067  1.00 38.16 ?  77  SER B O     1 
ATOM   3365 C  CB    . SER B 1 97  ? 53.514 -10.842 -6.482  1.00 32.62 ?  77  SER B CB    1 
ATOM   3366 O  OG    . SER B 1 97  ? 52.368 -10.677 -7.313  1.00 32.77 ?  77  SER B OG    1 
ATOM   3367 N  N     . ALA B 1 98  ? 56.384 -12.286 -5.981  1.00 28.44 ?  78  ALA B N     1 
ATOM   3368 C  CA    . ALA B 1 98  ? 57.521 -12.453 -5.078  1.00 25.03 ?  78  ALA B CA    1 
ATOM   3369 C  C     . ALA B 1 98  ? 58.838 -12.324 -5.819  1.00 24.83 ?  78  ALA B C     1 
ATOM   3370 O  O     . ALA B 1 98  ? 59.751 -11.640 -5.356  1.00 31.92 ?  78  ALA B O     1 
ATOM   3371 C  CB    . ALA B 1 98  ? 57.457 -13.808 -4.376  1.00 25.78 ?  78  ALA B CB    1 
ATOM   3372 N  N     . VAL B 1 99  ? 58.960 -13.005 -6.956  1.00 31.96 ?  79  VAL B N     1 
ATOM   3373 C  CA    . VAL B 1 99  ? 60.139 -12.928 -7.814  1.00 25.64 ?  79  VAL B CA    1 
ATOM   3374 C  C     . VAL B 1 99  ? 59.757 -12.148 -9.059  1.00 28.39 ?  79  VAL B C     1 
ATOM   3375 O  O     . VAL B 1 99  ? 59.407 -12.736 -10.093 1.00 32.84 ?  79  VAL B O     1 
ATOM   3376 C  CB    . VAL B 1 99  ? 60.660 -14.331 -8.173  1.00 27.46 ?  79  VAL B CB    1 
ATOM   3377 C  CG1   . VAL B 1 99  ? 62.029 -14.226 -8.791  1.00 31.26 ?  79  VAL B CG1   1 
ATOM   3378 C  CG2   . VAL B 1 99  ? 60.701 -15.224 -6.946  1.00 16.80 ?  79  VAL B CG2   1 
ATOM   3379 N  N     . SER B 1 100 ? 59.802 -10.816 -8.973  1.00 28.25 ?  80  SER B N     1 
ATOM   3380 C  CA    . SER B 1 100 ? 59.272 -9.997  -10.061 1.00 38.27 ?  80  SER B CA    1 
ATOM   3381 C  C     . SER B 1 100 ? 60.083 -10.116 -11.347 1.00 33.23 ?  80  SER B C     1 
ATOM   3382 O  O     . SER B 1 100 ? 59.600 -9.684  -12.396 1.00 28.40 ?  80  SER B O     1 
ATOM   3383 C  CB    . SER B 1 100 ? 59.197 -8.529  -9.640  1.00 35.33 ?  80  SER B CB    1 
ATOM   3384 O  OG    . SER B 1 100 ? 60.487 -7.949  -9.653  1.00 42.63 ?  80  SER B OG    1 
ATOM   3385 N  N     . ASP B 1 101 ? 61.294 -10.681 -11.292 1.00 27.88 ?  81  ASP B N     1 
ATOM   3386 C  CA    . ASP B 1 101 ? 62.073 -10.900 -12.501 1.00 28.88 ?  81  ASP B CA    1 
ATOM   3387 C  C     . ASP B 1 101 ? 61.531 -12.052 -13.342 1.00 32.48 ?  81  ASP B C     1 
ATOM   3388 O  O     . ASP B 1 101 ? 61.924 -12.187 -14.505 1.00 30.14 ?  81  ASP B O     1 
ATOM   3389 C  CB    . ASP B 1 101 ? 63.534 -11.181 -12.154 1.00 31.27 ?  81  ASP B CB    1 
ATOM   3390 C  CG    . ASP B 1 101 ? 64.308 -9.927  -11.730 1.00 43.45 ?  81  ASP B CG    1 
ATOM   3391 O  OD1   . ASP B 1 101 ? 63.732 -8.806  -11.685 1.00 40.20 ?  81  ASP B OD1   1 
ATOM   3392 O  OD2   . ASP B 1 101 ? 65.526 -10.075 -11.469 1.00 38.29 ?  81  ASP B OD2   1 
ATOM   3393 N  N     . LEU B 1 102 ? 60.665 -12.904 -12.781 1.00 29.34 ?  82  LEU B N     1 
ATOM   3394 C  CA    . LEU B 1 102 ? 60.031 -13.942 -13.589 1.00 25.27 ?  82  LEU B CA    1 
ATOM   3395 C  C     . LEU B 1 102 ? 59.156 -13.368 -14.702 1.00 28.26 ?  82  LEU B C     1 
ATOM   3396 O  O     . LEU B 1 102 ? 58.899 -14.058 -15.695 1.00 30.97 ?  82  LEU B O     1 
ATOM   3397 C  CB    . LEU B 1 102 ? 59.175 -14.861 -12.726 1.00 25.36 ?  82  LEU B CB    1 
ATOM   3398 C  CG    . LEU B 1 102 ? 59.833 -16.000 -11.954 1.00 29.16 ?  82  LEU B CG    1 
ATOM   3399 C  CD1   . LEU B 1 102 ? 58.926 -16.416 -10.818 1.00 22.05 ?  82  LEU B CD1   1 
ATOM   3400 C  CD2   . LEU B 1 102 ? 60.119 -17.178 -12.860 1.00 29.21 ?  82  LEU B CD2   1 
ATOM   3401 N  N     . GLU B 1 103 ? 58.692 -12.129 -14.577 1.00 23.77 ?  83  GLU B N     1 
ATOM   3402 C  CA    . GLU B 1 103 ? 57.751 -11.631 -15.573 1.00 36.05 ?  83  GLU B CA    1 
ATOM   3403 C  C     . GLU B 1 103 ? 58.403 -11.505 -16.952 1.00 36.45 ?  83  GLU B C     1 
ATOM   3404 O  O     . GLU B 1 103 ? 57.791 -11.870 -17.961 1.00 31.48 ?  83  GLU B O     1 
ATOM   3405 C  CB    . GLU B 1 103 ? 57.173 -10.298 -15.117 1.00 35.46 ?  83  GLU B CB    1 
ATOM   3406 C  CG    . GLU B 1 103 ? 55.728 -10.109 -15.498 1.00 44.04 ?  83  GLU B CG    1 
ATOM   3407 C  CD    . GLU B 1 103 ? 55.351 -8.657  -15.583 1.00 53.31 ?  83  GLU B CD    1 
ATOM   3408 O  OE1   . GLU B 1 103 ? 55.118 -8.052  -14.515 1.00 57.33 ?  83  GLU B OE1   1 
ATOM   3409 O  OE2   . GLU B 1 103 ? 55.284 -8.122  -16.708 1.00 65.96 ?  83  GLU B OE2   1 
ATOM   3410 N  N     . VAL B 1 104 ? 59.640 -10.998 -17.013 1.00 27.99 ?  84  VAL B N     1 
ATOM   3411 C  CA    . VAL B 1 104 ? 60.326 -10.813 -18.288 1.00 31.35 ?  84  VAL B CA    1 
ATOM   3412 C  C     . VAL B 1 104 ? 60.776 -12.157 -18.848 1.00 30.67 ?  84  VAL B C     1 
ATOM   3413 O  O     . VAL B 1 104 ? 60.627 -12.429 -20.050 1.00 27.41 ?  84  VAL B O     1 
ATOM   3414 C  CB    . VAL B 1 104 ? 61.500 -9.827  -18.100 1.00 34.77 ?  84  VAL B CB    1 
ATOM   3415 C  CG1   . VAL B 1 104 ? 62.483 -9.899  -19.259 1.00 29.58 ?  84  VAL B CG1   1 
ATOM   3416 C  CG2   . VAL B 1 104 ? 60.971 -8.401  -17.945 1.00 27.17 ?  84  VAL B CG2   1 
ATOM   3417 N  N     . PHE B 1 105 ? 61.312 -13.009 -17.968 1.00 28.37 ?  85  PHE B N     1 
ATOM   3418 C  CA    . PHE B 1 105 ? 61.653 -14.389 -18.293 1.00 25.94 ?  85  PHE B CA    1 
ATOM   3419 C  C     . PHE B 1 105 ? 60.474 -15.140 -18.917 1.00 24.51 ?  85  PHE B C     1 
ATOM   3420 O  O     . PHE B 1 105 ? 60.628 -15.817 -19.934 1.00 24.33 ?  85  PHE B O     1 
ATOM   3421 C  CB    . PHE B 1 105 ? 62.119 -15.083 -17.010 1.00 22.49 ?  85  PHE B CB    1 
ATOM   3422 C  CG    . PHE B 1 105 ? 62.913 -16.337 -17.234 1.00 23.62 ?  85  PHE B CG    1 
ATOM   3423 C  CD1   . PHE B 1 105 ? 62.284 -17.541 -17.494 1.00 20.54 ?  85  PHE B CD1   1 
ATOM   3424 C  CD2   . PHE B 1 105 ? 64.285 -16.323 -17.137 1.00 24.29 ?  85  PHE B CD2   1 
ATOM   3425 C  CE1   . PHE B 1 105 ? 63.015 -18.696 -17.687 1.00 23.34 ?  85  PHE B CE1   1 
ATOM   3426 C  CE2   . PHE B 1 105 ? 65.017 -17.482 -17.326 1.00 26.90 ?  85  PHE B CE2   1 
ATOM   3427 C  CZ    . PHE B 1 105 ? 64.380 -18.669 -17.597 1.00 26.23 ?  85  PHE B CZ    1 
ATOM   3428 N  N     . LEU B 1 106 ? 59.296 -15.072 -18.290 1.00 25.76 ?  86  LEU B N     1 
ATOM   3429 C  CA    . LEU B 1 106 ? 58.144 -15.809 -18.807 1.00 23.63 ?  86  LEU B CA    1 
ATOM   3430 C  C     . LEU B 1 106 ? 57.584 -15.152 -20.059 1.00 27.91 ?  86  LEU B C     1 
ATOM   3431 O  O     . LEU B 1 106 ? 57.013 -15.832 -20.917 1.00 31.21 ?  86  LEU B O     1 
ATOM   3432 C  CB    . LEU B 1 106 ? 57.044 -15.923 -17.746 1.00 19.07 ?  86  LEU B CB    1 
ATOM   3433 C  CG    . LEU B 1 106 ? 57.267 -16.818 -16.521 1.00 19.51 ?  86  LEU B CG    1 
ATOM   3434 C  CD1   . LEU B 1 106 ? 56.349 -16.399 -15.361 1.00 17.90 ?  86  LEU B CD1   1 
ATOM   3435 C  CD2   . LEU B 1 106 ? 57.081 -18.294 -16.858 1.00 19.02 ?  86  LEU B CD2   1 
ATOM   3436 N  N     . GLU B 1 107 ? 57.698 -13.830 -20.152 1.00 29.32 ?  87  GLU B N     1 
ATOM   3437 C  CA    . GLU B 1 107 ? 57.428 -13.130 -21.398 1.00 28.63 ?  87  GLU B CA    1 
ATOM   3438 C  C     . GLU B 1 107 ? 58.330 -13.653 -22.514 1.00 30.09 ?  87  GLU B C     1 
ATOM   3439 O  O     . GLU B 1 107 ? 57.852 -14.039 -23.588 1.00 32.33 ?  87  GLU B O     1 
ATOM   3440 C  CB    . GLU B 1 107 ? 57.617 -11.630 -21.166 1.00 30.85 ?  87  GLU B CB    1 
ATOM   3441 C  CG    . GLU B 1 107 ? 57.837 -10.785 -22.395 1.00 43.22 ?  87  GLU B CG    1 
ATOM   3442 C  CD    . GLU B 1 107 ? 58.854 -9.657  -22.151 1.00 57.60 ?  87  GLU B CD    1 
ATOM   3443 O  OE1   . GLU B 1 107 ? 58.468 -8.616  -21.550 1.00 44.53 ?  87  GLU B OE1   1 
ATOM   3444 O  OE2   . GLU B 1 107 ? 60.039 -9.831  -22.565 1.00 53.87 ?  87  GLU B OE2   1 
ATOM   3445 N  N     . THR B 1 108 ? 59.640 -13.716 -22.258 1.00 29.27 ?  88  THR B N     1 
ATOM   3446 C  CA    . THR B 1 108 ? 60.574 -14.229 -23.260 1.00 26.39 ?  88  THR B CA    1 
ATOM   3447 C  C     . THR B 1 108 ? 60.291 -15.695 -23.599 1.00 26.18 ?  88  THR B C     1 
ATOM   3448 O  O     . THR B 1 108 ? 60.372 -16.098 -24.763 1.00 33.67 ?  88  THR B O     1 
ATOM   3449 C  CB    . THR B 1 108 ? 62.003 -14.046 -22.754 1.00 25.70 ?  88  THR B CB    1 
ATOM   3450 O  OG1   . THR B 1 108 ? 62.295 -12.648 -22.652 1.00 32.14 ?  88  THR B OG1   1 
ATOM   3451 C  CG2   . THR B 1 108 ? 62.998 -14.678 -23.690 1.00 30.76 ?  88  THR B CG2   1 
ATOM   3452 N  N     . LEU B 1 109 ? 59.939 -16.498 -22.596 1.00 26.27 ?  89  LEU B N     1 
ATOM   3453 C  CA    . LEU B 1 109 ? 59.630 -17.911 -22.805 1.00 25.53 ?  89  LEU B CA    1 
ATOM   3454 C  C     . LEU B 1 109 ? 58.386 -18.085 -23.664 1.00 28.11 ?  89  LEU B C     1 
ATOM   3455 O  O     . LEU B 1 109 ? 58.321 -18.979 -24.519 1.00 31.01 ?  89  LEU B O     1 
ATOM   3456 C  CB    . LEU B 1 109 ? 59.424 -18.584 -21.448 1.00 22.16 ?  89  LEU B CB    1 
ATOM   3457 C  CG    . LEU B 1 109 ? 59.943 -19.989 -21.203 1.00 22.36 ?  89  LEU B CG    1 
ATOM   3458 C  CD1   . LEU B 1 109 ? 61.342 -20.140 -21.759 1.00 24.70 ?  89  LEU B CD1   1 
ATOM   3459 C  CD2   . LEU B 1 109 ? 59.907 -20.295 -19.709 1.00 20.16 ?  89  LEU B CD2   1 
ATOM   3460 N  N     . SER B 1 110 ? 57.381 -17.248 -23.430 1.00 25.59 ?  90  SER B N     1 
ATOM   3461 C  CA    . SER B 1 110 ? 56.134 -17.305 -24.179 1.00 23.34 ?  90  SER B CA    1 
ATOM   3462 C  C     . SER B 1 110 ? 56.315 -16.892 -25.642 1.00 29.41 ?  90  SER B C     1 
ATOM   3463 O  O     . SER B 1 110 ? 55.535 -17.304 -26.512 1.00 27.82 ?  90  SER B O     1 
ATOM   3464 C  CB    . SER B 1 110 ? 55.119 -16.388 -23.507 1.00 22.63 ?  90  SER B CB    1 
ATOM   3465 O  OG    . SER B 1 110 ? 53.839 -16.966 -23.527 1.00 30.45 ?  90  SER B OG    1 
ATOM   3466 N  N     . GLU B 1 111 ? 57.304 -16.050 -25.923 1.00 25.36 ?  91  GLU B N     1 
ATOM   3467 C  CA    . GLU B 1 111 ? 57.505 -15.575 -27.280 1.00 23.86 ?  91  GLU B CA    1 
ATOM   3468 C  C     . GLU B 1 111 ? 58.041 -16.680 -28.176 1.00 27.58 ?  91  GLU B C     1 
ATOM   3469 O  O     . GLU B 1 111 ? 57.821 -16.651 -29.395 1.00 25.63 ?  91  GLU B O     1 
ATOM   3470 C  CB    . GLU B 1 111 ? 58.476 -14.397 -27.271 1.00 19.96 ?  91  GLU B CB    1 
ATOM   3471 C  CG    . GLU B 1 111 ? 57.910 -13.106 -26.762 1.00 25.58 ?  91  GLU B CG    1 
ATOM   3472 C  CD    . GLU B 1 111 ? 58.994 -12.061 -26.540 1.00 38.51 ?  91  GLU B CD    1 
ATOM   3473 O  OE1   . GLU B 1 111 ? 60.060 -12.161 -27.190 1.00 29.34 ?  91  GLU B OE1   1 
ATOM   3474 O  OE2   . GLU B 1 111 ? 58.779 -11.150 -25.708 1.00 48.63 ?  91  GLU B OE2   1 
ATOM   3475 N  N     . ILE B 1 112 ? 58.778 -17.625 -27.594 1.00 20.51 ?  92  ILE B N     1 
ATOM   3476 C  CA    . ILE B 1 112 ? 59.415 -18.709 -28.336 1.00 19.74 ?  92  ILE B CA    1 
ATOM   3477 C  C     . ILE B 1 112 ? 58.453 -19.864 -28.541 1.00 26.13 ?  92  ILE B C     1 
ATOM   3478 O  O     . ILE B 1 112 ? 58.387 -20.417 -29.638 1.00 38.41 ?  92  ILE B O     1 
ATOM   3479 C  CB    . ILE B 1 112 ? 60.684 -19.170 -27.584 1.00 22.54 ?  92  ILE B CB    1 
ATOM   3480 C  CG1   . ILE B 1 112 ? 61.744 -18.079 -27.577 1.00 20.48 ?  92  ILE B CG1   1 
ATOM   3481 C  CG2   . ILE B 1 112 ? 61.226 -20.477 -28.119 1.00 19.45 ?  92  ILE B CG2   1 
ATOM   3482 C  CD1   . ILE B 1 112 ? 62.784 -18.286 -26.514 1.00 28.71 ?  92  ILE B CD1   1 
ATOM   3483 N  N     . THR B 1 113 ? 57.723 -20.239 -27.475 1.00 28.56 ?  93  THR B N     1 
ATOM   3484 C  CA    . THR B 1 113 ? 56.733 -21.311 -27.485 1.00 24.06 ?  93  THR B CA    1 
ATOM   3485 C  C     . THR B 1 113 ? 55.445 -20.910 -28.189 1.00 29.38 ?  93  THR B C     1 
ATOM   3486 O  O     . THR B 1 113 ? 54.677 -21.787 -28.611 1.00 26.25 ?  93  THR B O     1 
ATOM   3487 C  CB    . THR B 1 113 ? 56.350 -21.718 -26.048 1.00 27.13 ?  93  THR B CB    1 
ATOM   3488 O  OG1   . THR B 1 113 ? 55.833 -20.575 -25.355 1.00 23.44 ?  93  THR B OG1   1 
ATOM   3489 C  CG2   . THR B 1 113 ? 57.534 -22.308 -25.255 1.00 22.20 ?  93  THR B CG2   1 
ATOM   3490 N  N     . ASN B 1 114 ? 55.160 -19.611 -28.267 1.00 26.11 ?  94  ASN B N     1 
ATOM   3491 C  CA    . ASN B 1 114 ? 53.863 -19.149 -28.732 1.00 23.19 ?  94  ASN B CA    1 
ATOM   3492 C  C     . ASN B 1 114 ? 52.732 -19.834 -27.949 1.00 24.34 ?  94  ASN B C     1 
ATOM   3493 O  O     . ASN B 1 114 ? 51.671 -20.155 -28.487 1.00 25.44 ?  94  ASN B O     1 
ATOM   3494 C  CB    . ASN B 1 114 ? 53.741 -19.365 -30.244 1.00 30.45 ?  94  ASN B CB    1 
ATOM   3495 C  CG    . ASN B 1 114 ? 55.035 -18.971 -31.014 1.00 42.99 ?  94  ASN B CG    1 
ATOM   3496 O  OD1   . ASN B 1 114 ? 55.772 -19.833 -31.520 1.00 42.05 ?  94  ASN B OD1   1 
ATOM   3497 N  ND2   . ASN B 1 114 ? 55.297 -17.661 -31.108 1.00 41.47 ?  94  ASN B ND2   1 
ATOM   3498 N  N     . MET B 1 115 ? 52.975 -20.078 -26.655 1.00 25.37 ?  95  MET B N     1 
ATOM   3499 C  CA    . MET B 1 115 ? 52.006 -20.642 -25.717 1.00 17.70 ?  95  MET B CA    1 
ATOM   3500 C  C     . MET B 1 115 ? 51.947 -19.774 -24.456 1.00 20.46 ?  95  MET B C     1 
ATOM   3501 O  O     . MET B 1 115 ? 52.762 -18.874 -24.255 1.00 23.72 ?  95  MET B O     1 
ATOM   3502 C  CB    . MET B 1 115 ? 52.356 -22.092 -25.356 1.00 17.21 ?  95  MET B CB    1 
ATOM   3503 C  CG    . MET B 1 115 ? 52.284 -23.081 -26.530 1.00 18.16 ?  95  MET B CG    1 
ATOM   3504 S  SD    . MET B 1 115 ? 52.643 -24.793 -26.078 1.00 21.78 ?  95  MET B SD    1 
ATOM   3505 C  CE    . MET B 1 115 ? 51.177 -25.194 -25.144 1.00 15.55 ?  95  MET B CE    1 
ATOM   3506 N  N     . VAL B 1 116 ? 50.967 -20.032 -23.599 1.00 18.29 ?  96  VAL B N     1 
ATOM   3507 C  CA    . VAL B 1 116 ? 50.865 -19.341 -22.313 1.00 16.43 ?  96  VAL B CA    1 
ATOM   3508 C  C     . VAL B 1 116 ? 52.122 -19.582 -21.477 1.00 19.13 ?  96  VAL B C     1 
ATOM   3509 O  O     . VAL B 1 116 ? 52.800 -20.602 -21.659 1.00 20.23 ?  96  VAL B O     1 
ATOM   3510 C  CB    . VAL B 1 116 ? 49.610 -19.800 -21.559 1.00 22.83 ?  96  VAL B CB    1 
ATOM   3511 C  CG1   . VAL B 1 116 ? 48.346 -19.135 -22.136 1.00 19.10 ?  96  VAL B CG1   1 
ATOM   3512 C  CG2   . VAL B 1 116 ? 49.500 -21.329 -21.579 1.00 15.71 ?  96  VAL B CG2   1 
ATOM   3513 N  N     . PRO B 1 117 ? 52.501 -18.650 -20.549 1.00 25.33 ?  97  PRO B N     1 
ATOM   3514 C  CA    . PRO B 1 117 ? 53.656 -18.849 -19.665 1.00 21.20 ?  97  PRO B CA    1 
ATOM   3515 C  C     . PRO B 1 117 ? 53.307 -19.613 -18.383 1.00 27.44 ?  97  PRO B C     1 
ATOM   3516 O  O     . PRO B 1 117 ? 53.641 -19.198 -17.269 1.00 29.28 ?  97  PRO B O     1 
ATOM   3517 C  CB    . PRO B 1 117 ? 54.095 -17.412 -19.361 1.00 20.55 ?  97  PRO B CB    1 
ATOM   3518 C  CG    . PRO B 1 117 ? 52.803 -16.661 -19.339 1.00 20.47 ?  97  PRO B CG    1 
ATOM   3519 C  CD    . PRO B 1 117 ? 51.891 -17.319 -20.350 1.00 25.19 ?  97  PRO B CD    1 
ATOM   3520 N  N     . ARG B 1 118 ? 52.617 -20.733 -18.547 1.00 23.78 ?  98  ARG B N     1 
ATOM   3521 C  CA    . ARG B 1 118 ? 52.236 -21.601 -17.450 1.00 29.38 ?  98  ARG B CA    1 
ATOM   3522 C  C     . ARG B 1 118 ? 52.135 -23.010 -18.021 1.00 25.41 ?  98  ARG B C     1 
ATOM   3523 O  O     . ARG B 1 118 ? 51.842 -23.187 -19.204 1.00 28.62 ?  98  ARG B O     1 
ATOM   3524 C  CB    . ARG B 1 118 ? 50.912 -21.135 -16.828 1.00 29.98 ?  98  ARG B CB    1 
ATOM   3525 C  CG    . ARG B 1 118 ? 50.359 -22.044 -15.758 1.00 24.69 ?  98  ARG B CG    1 
ATOM   3526 C  CD    . ARG B 1 118 ? 51.013 -21.734 -14.455 1.00 31.40 ?  98  ARG B CD    1 
ATOM   3527 N  NE    . ARG B 1 118 ? 50.526 -22.545 -13.348 1.00 26.99 ?  98  ARG B NE    1 
ATOM   3528 C  CZ    . ARG B 1 118 ? 49.382 -22.342 -12.708 1.00 27.05 ?  98  ARG B CZ    1 
ATOM   3529 N  NH1   . ARG B 1 118 ? 48.493 -21.461 -13.136 1.00 17.52 ?  98  ARG B NH1   1 
ATOM   3530 N  NH2   . ARG B 1 118 ? 49.136 -23.025 -11.589 1.00 32.61 ?  98  ARG B NH2   1 
ATOM   3531 N  N     . GLU B 1 119 ? 52.407 -24.007 -17.191 1.00 18.33 ?  99  GLU B N     1 
ATOM   3532 C  CA    . GLU B 1 119 ? 52.294 -25.378 -17.652 1.00 19.29 ?  99  GLU B CA    1 
ATOM   3533 C  C     . GLU B 1 119 ? 50.816 -25.768 -17.814 1.00 21.53 ?  99  GLU B C     1 
ATOM   3534 O  O     . GLU B 1 119 ? 49.912 -25.169 -17.230 1.00 21.93 ?  99  GLU B O     1 
ATOM   3535 C  CB    . GLU B 1 119 ? 53.040 -26.318 -16.690 1.00 22.75 ?  99  GLU B CB    1 
ATOM   3536 C  CG    . GLU B 1 119 ? 52.283 -26.785 -15.432 1.00 22.79 ?  99  GLU B CG    1 
ATOM   3537 C  CD    . GLU B 1 119 ? 52.111 -25.711 -14.343 1.00 26.39 ?  99  GLU B CD    1 
ATOM   3538 O  OE1   . GLU B 1 119 ? 52.350 -24.515 -14.607 1.00 26.74 ?  99  GLU B OE1   1 
ATOM   3539 O  OE2   . GLU B 1 119 ? 51.739 -26.075 -13.198 1.00 30.54 ?  99  GLU B OE2   1 
ATOM   3540 N  N     . THR B 1 120 ? 50.572 -26.758 -18.672 1.00 20.17 ?  100 THR B N     1 
ATOM   3541 C  CA    . THR B 1 120 ? 49.231 -27.292 -18.886 1.00 17.11 ?  100 THR B CA    1 
ATOM   3542 C  C     . THR B 1 120 ? 49.310 -28.806 -18.796 1.00 17.67 ?  100 THR B C     1 
ATOM   3543 O  O     . THR B 1 120 ? 50.381 -29.358 -18.532 1.00 19.45 ?  100 THR B O     1 
ATOM   3544 C  CB    . THR B 1 120 ? 48.655 -26.877 -20.256 1.00 21.96 ?  100 THR B CB    1 
ATOM   3545 O  OG1   . THR B 1 120 ? 49.516 -27.335 -21.318 1.00 27.75 ?  100 THR B OG1   1 
ATOM   3546 C  CG2   . THR B 1 120 ? 48.460 -25.362 -20.367 1.00 21.21 ?  100 THR B CG2   1 
ATOM   3547 N  N     . SER B 1 121 ? 48.207 -29.497 -19.065 1.00 15.98 ?  101 SER B N     1 
ATOM   3548 C  CA    . SER B 1 121 ? 48.250 -30.950 -19.052 1.00 20.67 ?  101 SER B CA    1 
ATOM   3549 C  C     . SER B 1 121 ? 49.210 -31.534 -20.095 1.00 25.51 ?  101 SER B C     1 
ATOM   3550 O  O     . SER B 1 121 ? 49.679 -32.666 -19.928 1.00 20.82 ?  101 SER B O     1 
ATOM   3551 C  CB    . SER B 1 121 ? 46.844 -31.479 -19.244 1.00 22.79 ?  101 SER B CB    1 
ATOM   3552 O  OG    . SER B 1 121 ? 46.153 -31.379 -18.008 1.00 29.42 ?  101 SER B OG    1 
ATOM   3553 N  N     . TYR B 1 122 ? 49.537 -30.783 -21.150 1.00 24.80 ?  102 TYR B N     1 
ATOM   3554 C  CA    . TYR B 1 122 ? 50.532 -31.246 -22.110 1.00 21.93 ?  102 TYR B CA    1 
ATOM   3555 C  C     . TYR B 1 122 ? 51.906 -31.394 -21.469 1.00 24.25 ?  102 TYR B C     1 
ATOM   3556 O  O     . TYR B 1 122 ? 52.614 -32.382 -21.727 1.00 28.25 ?  102 TYR B O     1 
ATOM   3557 C  CB    . TYR B 1 122 ? 50.607 -30.275 -23.288 1.00 23.98 ?  102 TYR B CB    1 
ATOM   3558 C  CG    . TYR B 1 122 ? 49.708 -30.640 -24.434 1.00 22.89 ?  102 TYR B CG    1 
ATOM   3559 C  CD1   . TYR B 1 122 ? 48.389 -30.207 -24.460 1.00 19.97 ?  102 TYR B CD1   1 
ATOM   3560 C  CD2   . TYR B 1 122 ? 50.178 -31.410 -25.498 1.00 20.59 ?  102 TYR B CD2   1 
ATOM   3561 C  CE1   . TYR B 1 122 ? 47.556 -30.539 -25.505 1.00 22.99 ?  102 TYR B CE1   1 
ATOM   3562 C  CE2   . TYR B 1 122 ? 49.351 -31.746 -26.542 1.00 26.27 ?  102 TYR B CE2   1 
ATOM   3563 C  CZ    . TYR B 1 122 ? 48.034 -31.313 -26.541 1.00 25.23 ?  102 TYR B CZ    1 
ATOM   3564 O  OH    . TYR B 1 122 ? 47.196 -31.630 -27.590 1.00 26.73 ?  102 TYR B OH    1 
ATOM   3565 N  N     . HIS B 1 123 ? 52.320 -30.404 -20.661 1.00 19.99 ?  103 HIS B N     1 
ATOM   3566 C  CA    . HIS B 1 123 ? 53.629 -30.463 -20.015 1.00 20.68 ?  103 HIS B CA    1 
ATOM   3567 C  C     . HIS B 1 123 ? 53.643 -31.476 -18.882 1.00 20.16 ?  103 HIS B C     1 
ATOM   3568 O  O     . HIS B 1 123 ? 54.682 -32.086 -18.600 1.00 18.44 ?  103 HIS B O     1 
ATOM   3569 C  CB    . HIS B 1 123 ? 54.028 -29.104 -19.449 1.00 17.44 ?  103 HIS B CB    1 
ATOM   3570 C  CG    . HIS B 1 123 ? 53.864 -27.958 -20.392 1.00 18.74 ?  103 HIS B CG    1 
ATOM   3571 N  ND1   . HIS B 1 123 ? 52.632 -27.507 -20.813 1.00 18.67 ?  103 HIS B ND1   1 
ATOM   3572 C  CD2   . HIS B 1 123 ? 54.775 -27.122 -20.935 1.00 18.65 ?  103 HIS B CD2   1 
ATOM   3573 C  CE1   . HIS B 1 123 ? 52.793 -26.455 -21.589 1.00 20.32 ?  103 HIS B CE1   1 
ATOM   3574 N  NE2   . HIS B 1 123 ? 54.086 -26.205 -21.685 1.00 23.10 ?  103 HIS B NE2   1 
ATOM   3575 N  N     . TYR B 1 124 ? 52.500 -31.647 -18.219 1.00 21.75 ?  104 TYR B N     1 
ATOM   3576 C  CA    . TYR B 1 124 ? 52.353 -32.520 -17.060 1.00 20.14 ?  104 TYR B CA    1 
ATOM   3577 C  C     . TYR B 1 124 ? 52.248 -33.988 -17.440 1.00 24.17 ?  104 TYR B C     1 
ATOM   3578 O  O     . TYR B 1 124 ? 52.564 -34.857 -16.617 1.00 27.70 ?  104 TYR B O     1 
ATOM   3579 C  CB    . TYR B 1 124 ? 51.105 -32.090 -16.291 1.00 21.94 ?  104 TYR B CB    1 
ATOM   3580 C  CG    . TYR B 1 124 ? 50.945 -32.573 -14.867 1.00 19.49 ?  104 TYR B CG    1 
ATOM   3581 C  CD1   . TYR B 1 124 ? 52.011 -32.597 -13.978 1.00 22.05 ?  104 TYR B CD1   1 
ATOM   3582 C  CD2   . TYR B 1 124 ? 49.699 -32.957 -14.404 1.00 19.57 ?  104 TYR B CD2   1 
ATOM   3583 C  CE1   . TYR B 1 124 ? 51.839 -33.015 -12.666 1.00 21.57 ?  104 TYR B CE1   1 
ATOM   3584 C  CE2   . TYR B 1 124 ? 49.516 -33.378 -13.118 1.00 26.30 ?  104 TYR B CE2   1 
ATOM   3585 C  CZ    . TYR B 1 124 ? 50.582 -33.409 -12.245 1.00 24.32 ?  104 TYR B CZ    1 
ATOM   3586 O  OH    . TYR B 1 124 ? 50.354 -33.838 -10.953 1.00 30.82 ?  104 TYR B OH    1 
ATOM   3587 N  N     . GLY B 1 125 ? 51.811 -34.282 -18.662 1.00 24.73 ?  105 GLY B N     1 
ATOM   3588 C  CA    . GLY B 1 125 ? 51.566 -35.642 -19.072 1.00 24.12 ?  105 GLY B CA    1 
ATOM   3589 C  C     . GLY B 1 125 ? 52.493 -36.066 -20.183 1.00 23.80 ?  105 GLY B C     1 
ATOM   3590 O  O     . GLY B 1 125 ? 53.586 -36.597 -19.949 1.00 29.10 ?  105 GLY B O     1 
ATOM   3591 N  N     . PRO B 1 126 ? 52.078 -35.811 -21.424 1.00 25.29 ?  106 PRO B N     1 
ATOM   3592 C  CA    . PRO B 1 126 ? 52.904 -36.226 -22.578 1.00 23.94 ?  106 PRO B CA    1 
ATOM   3593 C  C     . PRO B 1 126 ? 54.299 -35.619 -22.603 1.00 25.53 ?  106 PRO B C     1 
ATOM   3594 O  O     . PRO B 1 126 ? 55.238 -36.299 -23.022 1.00 28.98 ?  106 PRO B O     1 
ATOM   3595 C  CB    . PRO B 1 126 ? 52.069 -35.776 -23.786 1.00 24.40 ?  106 PRO B CB    1 
ATOM   3596 C  CG    . PRO B 1 126 ? 51.046 -34.786 -23.223 1.00 26.32 ?  106 PRO B CG    1 
ATOM   3597 C  CD    . PRO B 1 126 ? 50.802 -35.198 -21.823 1.00 21.32 ?  106 PRO B CD    1 
ATOM   3598 N  N     . TRP B 1 127 ? 54.484 -34.362 -22.190 1.00 25.27 ?  107 TRP B N     1 
ATOM   3599 C  CA    . TRP B 1 127 ? 55.832 -33.797 -22.208 1.00 26.08 ?  107 TRP B CA    1 
ATOM   3600 C  C     . TRP B 1 127 ? 56.599 -34.093 -20.932 1.00 23.33 ?  107 TRP B C     1 
ATOM   3601 O  O     . TRP B 1 127 ? 57.764 -33.707 -20.812 1.00 27.26 ?  107 TRP B O     1 
ATOM   3602 C  CB    . TRP B 1 127 ? 55.777 -32.286 -22.481 1.00 24.33 ?  107 TRP B CB    1 
ATOM   3603 C  CG    . TRP B 1 127 ? 55.112 -31.978 -23.831 1.00 29.32 ?  107 TRP B CG    1 
ATOM   3604 C  CD1   . TRP B 1 127 ? 54.840 -32.881 -24.827 1.00 24.98 ?  107 TRP B CD1   1 
ATOM   3605 C  CD2   . TRP B 1 127 ? 54.614 -30.712 -24.298 1.00 21.43 ?  107 TRP B CD2   1 
ATOM   3606 N  NE1   . TRP B 1 127 ? 54.216 -32.257 -25.877 1.00 30.63 ?  107 TRP B NE1   1 
ATOM   3607 C  CE2   . TRP B 1 127 ? 54.058 -30.929 -25.582 1.00 30.38 ?  107 TRP B CE2   1 
ATOM   3608 C  CE3   . TRP B 1 127 ? 54.579 -29.424 -23.761 1.00 24.03 ?  107 TRP B CE3   1 
ATOM   3609 C  CZ2   . TRP B 1 127 ? 53.487 -29.899 -26.343 1.00 24.98 ?  107 TRP B CZ2   1 
ATOM   3610 C  CZ3   . TRP B 1 127 ? 54.003 -28.400 -24.513 1.00 25.02 ?  107 TRP B CZ3   1 
ATOM   3611 C  CH2   . TRP B 1 127 ? 53.463 -28.649 -25.792 1.00 25.41 ?  107 TRP B CH2   1 
ATOM   3612 N  N     . ASN B 1 128 ? 55.965 -34.777 -19.994 1.00 21.30 ?  108 ASN B N     1 
ATOM   3613 C  CA    . ASN B 1 128 ? 56.552 -35.127 -18.712 1.00 20.43 ?  108 ASN B CA    1 
ATOM   3614 C  C     . ASN B 1 128 ? 57.201 -36.501 -18.836 1.00 23.43 ?  108 ASN B C     1 
ATOM   3615 O  O     . ASN B 1 128 ? 56.506 -37.467 -19.186 1.00 19.80 ?  108 ASN B O     1 
ATOM   3616 C  CB    . ASN B 1 128 ? 55.449 -35.136 -17.666 1.00 24.05 ?  108 ASN B CB    1 
ATOM   3617 C  CG    . ASN B 1 128 ? 55.938 -35.239 -16.245 1.00 18.86 ?  108 ASN B CG    1 
ATOM   3618 O  OD1   . ASN B 1 128 ? 57.129 -35.307 -15.957 1.00 21.68 ?  108 ASN B OD1   1 
ATOM   3619 N  ND2   . ASN B 1 128 ? 54.989 -35.249 -15.334 1.00 18.65 ?  108 ASN B ND2   1 
ATOM   3620 N  N     . PRO B 1 129 ? 58.512 -36.639 -18.591 1.00 23.63 ?  109 PRO B N     1 
ATOM   3621 C  CA    . PRO B 1 129 ? 59.174 -37.935 -18.811 1.00 20.07 ?  109 PRO B CA    1 
ATOM   3622 C  C     . PRO B 1 129 ? 58.683 -39.022 -17.862 1.00 23.26 ?  109 PRO B C     1 
ATOM   3623 O  O     . PRO B 1 129 ? 58.209 -38.759 -16.756 1.00 20.21 ?  109 PRO B O     1 
ATOM   3624 C  CB    . PRO B 1 129 ? 60.658 -37.626 -18.566 1.00 21.82 ?  109 PRO B CB    1 
ATOM   3625 C  CG    . PRO B 1 129 ? 60.676 -36.355 -17.771 1.00 19.07 ?  109 PRO B CG    1 
ATOM   3626 C  CD    . PRO B 1 129 ? 59.451 -35.595 -18.135 1.00 15.76 ?  109 PRO B CD    1 
ATOM   3627 N  N     . ILE B 1 130 ? 58.792 -40.261 -18.321 1.00 32.16 ?  110 ILE B N     1 
ATOM   3628 C  CA    . ILE B 1 130 ? 58.494 -41.418 -17.491 1.00 27.49 ?  110 ILE B CA    1 
ATOM   3629 C  C     . ILE B 1 130 ? 59.735 -41.787 -16.692 1.00 32.77 ?  110 ILE B C     1 
ATOM   3630 O  O     . ILE B 1 130 ? 60.874 -41.526 -17.109 1.00 33.29 ?  110 ILE B O     1 
ATOM   3631 C  CB    . ILE B 1 130 ? 58.004 -42.603 -18.348 1.00 36.34 ?  110 ILE B CB    1 
ATOM   3632 C  CG1   . ILE B 1 130 ? 57.016 -42.146 -19.419 1.00 26.38 ?  110 ILE B CG1   1 
ATOM   3633 C  CG2   . ILE B 1 130 ? 57.392 -43.692 -17.479 1.00 48.89 ?  110 ILE B CG2   1 
ATOM   3634 C  CD1   . ILE B 1 130 ? 57.153 -42.929 -20.704 1.00 39.55 ?  110 ILE B CD1   1 
ATOM   3635 N  N     . GLY B 1 131 ? 59.508 -42.358 -15.505 1.00 36.50 ?  111 GLY B N     1 
ATOM   3636 C  CA    . GLY B 1 131 ? 60.575 -42.928 -14.704 1.00 30.29 ?  111 GLY B CA    1 
ATOM   3637 C  C     . GLY B 1 131 ? 61.173 -42.010 -13.658 1.00 32.97 ?  111 GLY B C     1 
ATOM   3638 O  O     . GLY B 1 131 ? 60.486 -41.126 -13.136 1.00 33.70 ?  111 GLY B O     1 
ATOM   3639 N  N     . GLU B 1 132 ? 62.463 -42.219 -13.354 1.00 31.87 ?  112 GLU B N     1 
ATOM   3640 C  CA    . GLU B 1 132 ? 63.122 -41.483 -12.282 1.00 34.86 ?  112 GLU B CA    1 
ATOM   3641 C  C     . GLU B 1 132 ? 62.955 -39.981 -12.460 1.00 32.57 ?  112 GLU B C     1 
ATOM   3642 O  O     . GLU B 1 132 ? 62.788 -39.246 -11.480 1.00 42.22 ?  112 GLU B O     1 
ATOM   3643 C  CB    . GLU B 1 132 ? 64.608 -41.853 -12.234 1.00 39.33 ?  112 GLU B CB    1 
ATOM   3644 C  CG    . GLU B 1 132 ? 65.035 -42.772 -11.078 1.00 57.49 ?  112 GLU B CG    1 
ATOM   3645 C  CD    . GLU B 1 132 ? 64.259 -42.549 -9.769  1.00 73.32 ?  112 GLU B CD    1 
ATOM   3646 O  OE1   . GLU B 1 132 ? 64.371 -41.451 -9.163  1.00 69.39 ?  112 GLU B OE1   1 
ATOM   3647 O  OE2   . GLU B 1 132 ? 63.539 -43.486 -9.344  1.00 68.46 ?  112 GLU B OE2   1 
ATOM   3648 N  N     . ARG B 1 133 ? 62.968 -39.512 -13.710 1.00 29.73 ?  113 ARG B N     1 
ATOM   3649 C  CA    . ARG B 1 133 ? 62.950 -38.085 -14.007 1.00 30.65 ?  113 ARG B CA    1 
ATOM   3650 C  C     . ARG B 1 133 ? 61.566 -37.456 -13.891 1.00 24.78 ?  113 ARG B C     1 
ATOM   3651 O  O     . ARG B 1 133 ? 61.487 -36.223 -13.857 1.00 24.78 ?  113 ARG B O     1 
ATOM   3652 C  CB    . ARG B 1 133 ? 63.526 -37.830 -15.415 1.00 25.41 ?  113 ARG B CB    1 
ATOM   3653 C  CG    . ARG B 1 133 ? 65.055 -37.976 -15.497 1.00 23.76 ?  113 ARG B CG    1 
ATOM   3654 C  CD    . ARG B 1 133 ? 65.673 -37.543 -16.831 1.00 27.59 ?  113 ARG B CD    1 
ATOM   3655 N  NE    . ARG B 1 133 ? 65.522 -36.113 -17.060 1.00 28.96 ?  113 ARG B NE    1 
ATOM   3656 C  CZ    . ARG B 1 133 ? 64.676 -35.596 -17.936 1.00 26.91 ?  113 ARG B CZ    1 
ATOM   3657 N  NH1   . ARG B 1 133 ? 63.947 -36.369 -18.725 1.00 23.73 ?  113 ARG B NH1   1 
ATOM   3658 N  NH2   . ARG B 1 133 ? 64.542 -34.273 -18.007 1.00 24.03 ?  113 ARG B NH2   1 
ATOM   3659 N  N     . GLU B 1 134 ? 60.500 -38.257 -13.793 1.00 18.87 ?  114 GLU B N     1 
ATOM   3660 C  CA    . GLU B 1 134 ? 59.131 -37.742 -13.824 1.00 25.66 ?  114 GLU B CA    1 
ATOM   3661 C  C     . GLU B 1 134 ? 58.914 -36.621 -12.812 1.00 27.28 ?  114 GLU B C     1 
ATOM   3662 O  O     . GLU B 1 134 ? 59.255 -36.756 -11.636 1.00 26.79 ?  114 GLU B O     1 
ATOM   3663 C  CB    . GLU B 1 134 ? 58.123 -38.872 -13.568 1.00 22.84 ?  114 GLU B CB    1 
ATOM   3664 C  CG    . GLU B 1 134 ? 56.683 -38.484 -13.927 1.00 20.53 ?  114 GLU B CG    1 
ATOM   3665 C  CD    . GLU B 1 134 ? 55.697 -39.639 -13.870 1.00 29.46 ?  114 GLU B CD    1 
ATOM   3666 O  OE1   . GLU B 1 134 ? 55.688 -40.501 -14.782 1.00 35.98 ?  114 GLU B OE1   1 
ATOM   3667 O  OE2   . GLU B 1 134 ? 54.899 -39.686 -12.918 1.00 43.77 ?  114 GLU B OE2   1 
ATOM   3668 N  N     . ARG B 1 135 ? 58.331 -35.514 -13.279 1.00 26.81 ?  115 ARG B N     1 
ATOM   3669 C  CA    . ARG B 1 135 ? 58.080 -34.340 -12.444 1.00 24.50 ?  115 ARG B CA    1 
ATOM   3670 C  C     . ARG B 1 135 ? 56.735 -34.480 -11.740 1.00 27.86 ?  115 ARG B C     1 
ATOM   3671 O  O     . ARG B 1 135 ? 55.693 -34.594 -12.395 1.00 29.49 ?  115 ARG B O     1 
ATOM   3672 C  CB    . ARG B 1 135 ? 58.105 -33.064 -13.280 1.00 23.82 ?  115 ARG B CB    1 
ATOM   3673 C  CG    . ARG B 1 135 ? 59.493 -32.576 -13.593 1.00 26.29 ?  115 ARG B CG    1 
ATOM   3674 C  CD    . ARG B 1 135 ? 60.021 -33.108 -14.911 1.00 21.14 ?  115 ARG B CD    1 
ATOM   3675 N  NE    . ARG B 1 135 ? 61.191 -32.328 -15.282 1.00 22.86 ?  115 ARG B NE    1 
ATOM   3676 C  CZ    . ARG B 1 135 ? 62.444 -32.700 -15.077 1.00 21.81 ?  115 ARG B CZ    1 
ATOM   3677 N  NH1   . ARG B 1 135 ? 62.741 -33.869 -14.538 1.00 20.07 ?  115 ARG B NH1   1 
ATOM   3678 N  NH2   . ARG B 1 135 ? 63.425 -31.880 -15.432 1.00 23.54 ?  115 ARG B NH2   1 
ATOM   3679 N  N     . ARG B 1 136 ? 56.761 -34.462 -10.405 1.00 27.79 ?  116 ARG B N     1 
ATOM   3680 C  CA    . ARG B 1 136 ? 55.580 -34.647 -9.579  1.00 24.36 ?  116 ARG B CA    1 
ATOM   3681 C  C     . ARG B 1 136 ? 55.613 -33.641 -8.442  1.00 24.47 ?  116 ARG B C     1 
ATOM   3682 O  O     . ARG B 1 136 ? 56.678 -33.291 -7.932  1.00 19.97 ?  116 ARG B O     1 
ATOM   3683 C  CB    . ARG B 1 136 ? 55.483 -36.081 -9.023  1.00 27.05 ?  116 ARG B CB    1 
ATOM   3684 C  CG    . ARG B 1 136 ? 54.701 -37.007 -9.943  1.00 26.59 ?  116 ARG B CG    1 
ATOM   3685 C  CD    . ARG B 1 136 ? 54.666 -38.427 -9.471  1.00 28.32 ?  116 ARG B CD    1 
ATOM   3686 N  NE    . ARG B 1 136 ? 55.878 -39.131 -9.868  1.00 49.62 ?  116 ARG B NE    1 
ATOM   3687 C  CZ    . ARG B 1 136 ? 56.371 -40.202 -9.258  1.00 53.98 ?  116 ARG B CZ    1 
ATOM   3688 N  NH1   . ARG B 1 136 ? 55.753 -40.757 -8.228  1.00 50.43 ?  116 ARG B NH1   1 
ATOM   3689 N  NH2   . ARG B 1 136 ? 57.515 -40.729 -9.692  1.00 55.61 ?  116 ARG B NH2   1 
ATOM   3690 N  N     . PHE B 1 137 ? 54.426 -33.157 -8.081  1.00 21.51 ?  117 PHE B N     1 
ATOM   3691 C  CA    . PHE B 1 137 ? 54.265 -32.220 -6.979  1.00 22.65 ?  117 PHE B CA    1 
ATOM   3692 C  C     . PHE B 1 137 ? 54.426 -32.887 -5.607  1.00 30.07 ?  117 PHE B C     1 
ATOM   3693 O  O     . PHE B 1 137 ? 54.926 -32.262 -4.662  1.00 22.15 ?  117 PHE B O     1 
ATOM   3694 C  CB    . PHE B 1 137 ? 52.875 -31.585 -7.053  1.00 26.88 ?  117 PHE B CB    1 
ATOM   3695 C  CG    . PHE B 1 137 ? 52.687 -30.610 -8.177  1.00 24.87 ?  117 PHE B CG    1 
ATOM   3696 C  CD1   . PHE B 1 137 ? 53.480 -29.466 -8.277  1.00 24.94 ?  117 PHE B CD1   1 
ATOM   3697 C  CD2   . PHE B 1 137 ? 51.672 -30.795 -9.092  1.00 21.50 ?  117 PHE B CD2   1 
ATOM   3698 C  CE1   . PHE B 1 137 ? 53.286 -28.545 -9.298  1.00 23.63 ?  117 PHE B CE1   1 
ATOM   3699 C  CE2   . PHE B 1 137 ? 51.471 -29.873 -10.110 1.00 25.64 ?  117 PHE B CE2   1 
ATOM   3700 C  CZ    . PHE B 1 137 ? 52.283 -28.742 -10.206 1.00 21.82 ?  117 PHE B CZ    1 
ATOM   3701 N  N     . THR B 1 138 ? 53.989 -34.137 -5.469  1.00 28.60 ?  118 THR B N     1 
ATOM   3702 C  CA    . THR B 1 138 ? 53.879 -34.785 -4.175  1.00 29.97 ?  118 THR B CA    1 
ATOM   3703 C  C     . THR B 1 138 ? 54.502 -36.173 -4.223  1.00 32.70 ?  118 THR B C     1 
ATOM   3704 O  O     . THR B 1 138 ? 54.880 -36.683 -5.285  1.00 31.97 ?  118 THR B O     1 
ATOM   3705 C  CB    . THR B 1 138 ? 52.420 -34.926 -3.758  1.00 34.53 ?  118 THR B CB    1 
ATOM   3706 O  OG1   . THR B 1 138 ? 51.752 -35.769 -4.709  1.00 33.50 ?  118 THR B OG1   1 
ATOM   3707 C  CG2   . THR B 1 138 ? 51.737 -33.551 -3.715  1.00 31.66 ?  118 THR B CG2   1 
ATOM   3708 N  N     . HIS B 1 139 ? 54.572 -36.790 -3.046  1.00 30.54 ?  119 HIS B N     1 
ATOM   3709 C  CA    . HIS B 1 139 ? 54.934 -38.193 -2.891  1.00 27.95 ?  119 HIS B CA    1 
ATOM   3710 C  C     . HIS B 1 139 ? 53.744 -39.127 -3.029  1.00 27.41 ?  119 HIS B C     1 
ATOM   3711 O  O     . HIS B 1 139 ? 53.948 -40.339 -3.107  1.00 33.01 ?  119 HIS B O     1 
ATOM   3712 C  CB    . HIS B 1 139 ? 55.579 -38.411 -1.522  1.00 33.31 ?  119 HIS B CB    1 
ATOM   3713 C  CG    . HIS B 1 139 ? 54.776 -37.839 -0.389  1.00 42.10 ?  119 HIS B CG    1 
ATOM   3714 N  ND1   . HIS B 1 139 ? 53.973 -38.614 0.423   1.00 39.73 ?  119 HIS B ND1   1 
ATOM   3715 C  CD2   . HIS B 1 139 ? 54.624 -36.561 0.043   1.00 45.48 ?  119 HIS B CD2   1 
ATOM   3716 C  CE1   . HIS B 1 139 ? 53.380 -37.842 1.320   1.00 44.22 ?  119 HIS B CE1   1 
ATOM   3717 N  NE2   . HIS B 1 139 ? 53.756 -36.592 1.110   1.00 46.55 ?  119 HIS B NE2   1 
ATOM   3718 N  N     . PHE B 1 140 ? 52.517 -38.595 -3.061  1.00 29.67 ?  120 PHE B N     1 
ATOM   3719 C  CA    . PHE B 1 140 ? 51.313 -39.433 -3.067  1.00 26.79 ?  120 PHE B CA    1 
ATOM   3720 C  C     . PHE B 1 140 ? 51.192 -40.221 -4.367  1.00 34.00 ?  120 PHE B C     1 
ATOM   3721 O  O     . PHE B 1 140 ? 51.274 -39.636 -5.457  1.00 36.30 ?  120 PHE B O     1 
ATOM   3722 C  CB    . PHE B 1 140 ? 50.068 -38.578 -2.879  1.00 26.59 ?  120 PHE B CB    1 
ATOM   3723 C  CG    . PHE B 1 140 ? 50.016 -37.862 -1.561  1.00 33.68 ?  120 PHE B CG    1 
ATOM   3724 C  CD1   . PHE B 1 140 ? 50.603 -36.618 -1.409  1.00 34.11 ?  120 PHE B CD1   1 
ATOM   3725 C  CD2   . PHE B 1 140 ? 49.368 -38.430 -0.467  1.00 38.84 ?  120 PHE B CD2   1 
ATOM   3726 C  CE1   . PHE B 1 140 ? 50.550 -35.950 -0.187  1.00 40.81 ?  120 PHE B CE1   1 
ATOM   3727 C  CE2   . PHE B 1 140 ? 49.314 -37.773 0.762   1.00 30.26 ?  120 PHE B CE2   1 
ATOM   3728 C  CZ    . PHE B 1 140 ? 49.906 -36.536 0.902   1.00 37.75 ?  120 PHE B CZ    1 
ATOM   3729 N  N     . PRO B 1 141 ? 50.975 -41.538 -4.302  1.00 37.53 ?  121 PRO B N     1 
ATOM   3730 C  CA    . PRO B 1 141 ? 50.782 -42.312 -5.540  1.00 28.80 ?  121 PRO B CA    1 
ATOM   3731 C  C     . PRO B 1 141 ? 49.539 -41.901 -6.296  1.00 30.58 ?  121 PRO B C     1 
ATOM   3732 O  O     . PRO B 1 141 ? 49.435 -42.186 -7.499  1.00 28.21 ?  121 PRO B O     1 
ATOM   3733 C  CB    . PRO B 1 141 ? 50.670 -43.760 -5.044  1.00 26.30 ?  121 PRO B CB    1 
ATOM   3734 C  CG    . PRO B 1 141 ? 51.094 -43.728 -3.620  1.00 27.74 ?  121 PRO B CG    1 
ATOM   3735 C  CD    . PRO B 1 141 ? 50.830 -42.367 -3.101  1.00 23.67 ?  121 PRO B CD    1 
ATOM   3736 N  N     . ASP B 1 142 ? 48.590 -41.252 -5.609  1.00 28.84 ?  122 ASP B N     1 
ATOM   3737 C  CA    . ASP B 1 142 ? 47.391 -40.738 -6.253  1.00 27.20 ?  122 ASP B CA    1 
ATOM   3738 C  C     . ASP B 1 142 ? 47.716 -39.754 -7.369  1.00 32.37 ?  122 ASP B C     1 
ATOM   3739 O  O     . ASP B 1 142 ? 46.934 -39.616 -8.318  1.00 27.88 ?  122 ASP B O     1 
ATOM   3740 C  CB    . ASP B 1 142 ? 46.504 -40.062 -5.216  1.00 26.27 ?  122 ASP B CB    1 
ATOM   3741 C  CG    . ASP B 1 142 ? 46.237 -40.936 -4.014  1.00 31.80 ?  122 ASP B CG    1 
ATOM   3742 O  OD1   . ASP B 1 142 ? 47.169 -41.163 -3.207  1.00 38.24 ?  122 ASP B OD1   1 
ATOM   3743 O  OD2   . ASP B 1 142 ? 45.076 -41.377 -3.867  1.00 35.60 ?  122 ASP B OD2   1 
ATOM   3744 N  N     . GLU B 1 143 ? 48.841 -39.038 -7.260  1.00 27.73 ?  123 GLU B N     1 
ATOM   3745 C  CA    . GLU B 1 143 ? 49.177 -38.065 -8.286  1.00 26.63 ?  123 GLU B CA    1 
ATOM   3746 C  C     . GLU B 1 143 ? 49.436 -38.728 -9.623  1.00 23.87 ?  123 GLU B C     1 
ATOM   3747 O  O     . GLU B 1 143 ? 49.178 -38.130 -10.670 1.00 25.60 ?  123 GLU B O     1 
ATOM   3748 C  CB    . GLU B 1 143 ? 50.393 -37.245 -7.874  1.00 32.49 ?  123 GLU B CB    1 
ATOM   3749 C  CG    . GLU B 1 143 ? 50.633 -36.084 -8.835  1.00 26.24 ?  123 GLU B CG    1 
ATOM   3750 C  CD    . GLU B 1 143 ? 51.726 -35.165 -8.387  1.00 27.09 ?  123 GLU B CD    1 
ATOM   3751 O  OE1   . GLU B 1 143 ? 52.170 -35.303 -7.231  1.00 35.20 ?  123 GLU B OE1   1 
ATOM   3752 O  OE2   . GLU B 1 143 ? 52.142 -34.300 -9.185  1.00 30.67 ?  123 GLU B OE2   1 
ATOM   3753 N  N     . ARG B 1 144 ? 49.935 -39.961 -9.610  1.00 28.44 ?  124 ARG B N     1 
ATOM   3754 C  CA    . ARG B 1 144 ? 50.148 -40.683 -10.853 1.00 30.27 ?  124 ARG B CA    1 
ATOM   3755 C  C     . ARG B 1 144 ? 48.849 -40.913 -11.619 1.00 28.53 ?  124 ARG B C     1 
ATOM   3756 O  O     . ARG B 1 144 ? 48.883 -41.062 -12.843 1.00 31.70 ?  124 ARG B O     1 
ATOM   3757 C  CB    . ARG B 1 144 ? 50.874 -42.002 -10.566 1.00 32.59 ?  124 ARG B CB    1 
ATOM   3758 C  CG    . ARG B 1 144 ? 52.271 -41.789 -9.974  1.00 36.94 ?  124 ARG B CG    1 
ATOM   3759 C  CD    . ARG B 1 144 ? 53.201 -42.996 -10.181 1.00 41.20 ?  124 ARG B CD    1 
ATOM   3760 N  NE    . ARG B 1 144 ? 52.485 -44.227 -10.523 1.00 63.13 ?  124 ARG B NE    1 
ATOM   3761 C  CZ    . ARG B 1 144 ? 52.507 -44.846 -11.702 1.00 64.83 ?  124 ARG B CZ    1 
ATOM   3762 N  NH1   . ARG B 1 144 ? 53.148 -44.339 -12.750 1.00 58.60 ?  124 ARG B NH1   1 
ATOM   3763 N  NH2   . ARG B 1 144 ? 51.858 -46.001 -11.837 1.00 49.93 ?  124 ARG B NH2   1 
ATOM   3764 N  N     . GLY B 1 145 ? 47.703 -40.904 -10.943 1.00 24.81 ?  125 GLY B N     1 
ATOM   3765 C  CA    . GLY B 1 145 ? 46.445 -41.103 -11.641 1.00 26.13 ?  125 GLY B CA    1 
ATOM   3766 C  C     . GLY B 1 145 ? 46.066 -39.965 -12.569 1.00 25.83 ?  125 GLY B C     1 
ATOM   3767 O  O     . GLY B 1 145 ? 45.343 -40.176 -13.549 1.00 26.62 ?  125 GLY B O     1 
ATOM   3768 N  N     . LEU B 1 146 ? 46.525 -38.750 -12.275 1.00 23.20 ?  126 LEU B N     1 
ATOM   3769 C  CA    . LEU B 1 146 ? 46.283 -37.621 -13.170 1.00 25.67 ?  126 LEU B CA    1 
ATOM   3770 C  C     . LEU B 1 146 ? 47.289 -37.607 -14.317 1.00 23.80 ?  126 LEU B C     1 
ATOM   3771 O  O     . LEU B 1 146 ? 46.920 -37.421 -15.485 1.00 21.58 ?  126 LEU B O     1 
ATOM   3772 C  CB    . LEU B 1 146 ? 46.359 -36.300 -12.391 1.00 25.74 ?  126 LEU B CB    1 
ATOM   3773 C  CG    . LEU B 1 146 ? 45.570 -36.130 -11.088 1.00 27.53 ?  126 LEU B CG    1 
ATOM   3774 C  CD1   . LEU B 1 146 ? 45.910 -34.791 -10.419 1.00 26.15 ?  126 LEU B CD1   1 
ATOM   3775 C  CD2   . LEU B 1 146 ? 44.071 -36.232 -11.352 1.00 25.79 ?  126 LEU B CD2   1 
ATOM   3776 N  N     . ILE B 1 147 ? 48.568 -37.793 -13.985 1.00 24.81 ?  127 ILE B N     1 
ATOM   3777 C  CA    . ILE B 1 147 ? 49.633 -37.755 -14.977 1.00 23.77 ?  127 ILE B CA    1 
ATOM   3778 C  C     . ILE B 1 147 ? 49.457 -38.875 -15.990 1.00 28.69 ?  127 ILE B C     1 
ATOM   3779 O  O     . ILE B 1 147 ? 49.552 -38.650 -17.202 1.00 28.31 ?  127 ILE B O     1 
ATOM   3780 C  CB    . ILE B 1 147 ? 51.000 -37.827 -14.275 1.00 26.68 ?  127 ILE B CB    1 
ATOM   3781 C  CG1   . ILE B 1 147 ? 51.145 -36.630 -13.322 1.00 19.01 ?  127 ILE B CG1   1 
ATOM   3782 C  CG2   . ILE B 1 147 ? 52.127 -37.936 -15.300 1.00 25.36 ?  127 ILE B CG2   1 
ATOM   3783 C  CD1   . ILE B 1 147 ? 52.409 -36.603 -12.557 1.00 18.27 ?  127 ILE B CD1   1 
ATOM   3784 N  N     . GLU B 1 148 ? 49.162 -40.089 -15.517 1.00 27.41 ?  128 GLU B N     1 
ATOM   3785 C  CA    . GLU B 1 148 ? 48.900 -41.182 -16.443 1.00 24.49 ?  128 GLU B CA    1 
ATOM   3786 C  C     . GLU B 1 148 ? 47.670 -40.891 -17.281 1.00 25.16 ?  128 GLU B C     1 
ATOM   3787 O  O     . GLU B 1 148 ? 47.655 -41.162 -18.489 1.00 27.40 ?  128 GLU B O     1 
ATOM   3788 C  CB    . GLU B 1 148 ? 48.723 -42.500 -15.695 1.00 27.57 ?  128 GLU B CB    1 
ATOM   3789 C  CG    . GLU B 1 148 ? 49.998 -42.995 -15.070 1.00 34.50 ?  128 GLU B CG    1 
ATOM   3790 C  CD    . GLU B 1 148 ? 51.134 -43.080 -16.057 1.00 38.04 ?  128 GLU B CD    1 
ATOM   3791 O  OE1   . GLU B 1 148 ? 50.894 -43.398 -17.241 1.00 41.30 ?  128 GLU B OE1   1 
ATOM   3792 O  OE2   . GLU B 1 148 ? 52.282 -42.803 -15.644 1.00 46.88 ?  128 GLU B OE2   1 
ATOM   3793 N  N     . GLY B 1 149 ? 46.636 -40.335 -16.661 1.00 17.78 ?  129 GLY B N     1 
ATOM   3794 C  CA    . GLY B 1 149 ? 45.426 -39.984 -17.373 1.00 17.92 ?  129 GLY B CA    1 
ATOM   3795 C  C     . GLY B 1 149 ? 45.694 -39.165 -18.619 1.00 26.55 ?  129 GLY B C     1 
ATOM   3796 O  O     . GLY B 1 149 ? 45.367 -39.606 -19.727 1.00 26.23 ?  129 GLY B O     1 
ATOM   3797 N  N     . VAL B 1 150 ? 46.334 -37.999 -18.463 1.00 23.81 ?  130 VAL B N     1 
ATOM   3798 C  CA    . VAL B 1 150 ? 46.524 -37.114 -19.612 1.00 23.81 ?  130 VAL B CA    1 
ATOM   3799 C  C     . VAL B 1 150 ? 47.607 -37.639 -20.543 1.00 24.28 ?  130 VAL B C     1 
ATOM   3800 O  O     . VAL B 1 150 ? 47.512 -37.469 -21.763 1.00 29.19 ?  130 VAL B O     1 
ATOM   3801 C  CB    . VAL B 1 150 ? 46.817 -35.665 -19.164 1.00 23.16 ?  130 VAL B CB    1 
ATOM   3802 C  CG1   . VAL B 1 150 ? 45.641 -35.113 -18.383 1.00 21.57 ?  130 VAL B CG1   1 
ATOM   3803 C  CG2   . VAL B 1 150 ? 48.068 -35.592 -18.341 1.00 23.48 ?  130 VAL B CG2   1 
ATOM   3804 N  N     . ARG B 1 151 ? 48.635 -38.297 -20.007 1.00 24.28 ?  131 ARG B N     1 
ATOM   3805 C  CA    . ARG B 1 151 ? 49.684 -38.839 -20.863 1.00 20.83 ?  131 ARG B CA    1 
ATOM   3806 C  C     . ARG B 1 151 ? 49.132 -39.900 -21.810 1.00 25.19 ?  131 ARG B C     1 
ATOM   3807 O  O     . ARG B 1 151 ? 49.532 -39.968 -22.975 1.00 25.12 ?  131 ARG B O     1 
ATOM   3808 C  CB    . ARG B 1 151 ? 50.801 -39.403 -20.005 1.00 20.75 ?  131 ARG B CB    1 
ATOM   3809 C  CG    . ARG B 1 151 ? 51.896 -40.068 -20.747 1.00 18.63 ?  131 ARG B CG    1 
ATOM   3810 C  CD    . ARG B 1 151 ? 52.859 -40.758 -19.775 1.00 29.14 ?  131 ARG B CD    1 
ATOM   3811 N  NE    . ARG B 1 151 ? 53.812 -39.839 -19.155 1.00 30.58 ?  131 ARG B NE    1 
ATOM   3812 C  CZ    . ARG B 1 151 ? 54.124 -39.843 -17.863 1.00 33.62 ?  131 ARG B CZ    1 
ATOM   3813 N  NH1   . ARG B 1 151 ? 53.556 -40.690 -17.016 1.00 33.33 ?  131 ARG B NH1   1 
ATOM   3814 N  NH2   . ARG B 1 151 ? 55.044 -38.991 -17.411 1.00 25.03 ?  131 ARG B NH2   1 
ATOM   3815 N  N     . ILE B 1 152 ? 48.182 -40.709 -21.347 1.00 25.19 ?  132 ILE B N     1 
ATOM   3816 C  CA    . ILE B 1 152 ? 47.546 -41.683 -22.232 1.00 24.55 ?  132 ILE B CA    1 
ATOM   3817 C  C     . ILE B 1 152 ? 46.522 -41.007 -23.141 1.00 22.23 ?  132 ILE B C     1 
ATOM   3818 O  O     . ILE B 1 152 ? 46.420 -41.329 -24.330 1.00 34.50 ?  132 ILE B O     1 
ATOM   3819 C  CB    . ILE B 1 152 ? 46.901 -42.822 -21.409 1.00 27.55 ?  132 ILE B CB    1 
ATOM   3820 C  CG1   . ILE B 1 152 ? 47.957 -43.694 -20.723 1.00 21.79 ?  132 ILE B CG1   1 
ATOM   3821 C  CG2   . ILE B 1 152 ? 45.994 -43.674 -22.274 1.00 26.44 ?  132 ILE B CG2   1 
ATOM   3822 C  CD1   . ILE B 1 152 ? 47.443 -44.424 -19.514 1.00 24.77 ?  132 ILE B CD1   1 
ATOM   3823 N  N     . ALA B 1 153 ? 45.747 -40.068 -22.612 1.00 23.16 ?  133 ALA B N     1 
ATOM   3824 C  CA    . ALA B 1 153 ? 44.620 -39.543 -23.373 1.00 24.28 ?  133 ALA B CA    1 
ATOM   3825 C  C     . ALA B 1 153 ? 45.079 -38.667 -24.532 1.00 26.54 ?  133 ALA B C     1 
ATOM   3826 O  O     . ALA B 1 153 ? 44.505 -38.724 -25.621 1.00 29.80 ?  133 ALA B O     1 
ATOM   3827 C  CB    . ALA B 1 153 ? 43.684 -38.755 -22.457 1.00 23.08 ?  133 ALA B CB    1 
ATOM   3828 N  N     . ILE B 1 154 ? 46.112 -37.863 -24.329 1.00 27.14 ?  134 ILE B N     1 
ATOM   3829 C  CA    . ILE B 1 154 ? 46.360 -36.754 -25.243 1.00 27.66 ?  134 ILE B CA    1 
ATOM   3830 C  C     . ILE B 1 154 ? 46.809 -37.271 -26.606 1.00 24.61 ?  134 ILE B C     1 
ATOM   3831 O  O     . ILE B 1 154 ? 46.230 -36.847 -27.613 1.00 27.22 ?  134 ILE B O     1 
ATOM   3832 C  CB    . ILE B 1 154 ? 47.345 -35.742 -24.636 1.00 28.91 ?  134 ILE B CB    1 
ATOM   3833 C  CG1   . ILE B 1 154 ? 46.626 -34.944 -23.537 1.00 25.52 ?  134 ILE B CG1   1 
ATOM   3834 C  CG2   . ILE B 1 154 ? 47.944 -34.849 -25.740 1.00 25.26 ?  134 ILE B CG2   1 
ATOM   3835 C  CD1   . ILE B 1 154 ? 47.471 -33.941 -22.843 1.00 20.65 ?  134 ILE B CD1   1 
ATOM   3836 N  N     . PRO B 1 155 ? 47.800 -38.170 -26.705 1.00 27.75 ?  135 PRO B N     1 
ATOM   3837 C  CA    . PRO B 1 155 ? 48.092 -38.791 -28.023 1.00 23.20 ?  135 PRO B CA    1 
ATOM   3838 C  C     . PRO B 1 155 ? 46.875 -39.324 -28.775 1.00 24.23 ?  135 PRO B C     1 
ATOM   3839 O  O     . PRO B 1 155 ? 46.673 -38.988 -29.946 1.00 27.69 ?  135 PRO B O     1 
ATOM   3840 C  CB    . PRO B 1 155 ? 49.057 -39.921 -27.649 1.00 20.43 ?  135 PRO B CB    1 
ATOM   3841 C  CG    . PRO B 1 155 ? 49.782 -39.402 -26.459 1.00 23.33 ?  135 PRO B CG    1 
ATOM   3842 C  CD    . PRO B 1 155 ? 48.863 -38.462 -25.725 1.00 21.94 ?  135 PRO B CD    1 
ATOM   3843 N  N     . GLY B 1 156 ? 46.052 -40.150 -28.132 1.00 25.87 ?  136 GLY B N     1 
ATOM   3844 C  CA    . GLY B 1 156 ? 44.917 -40.725 -28.831 1.00 23.41 ?  136 GLY B CA    1 
ATOM   3845 C  C     . GLY B 1 156 ? 43.969 -39.679 -29.385 1.00 23.53 ?  136 GLY B C     1 
ATOM   3846 O  O     . GLY B 1 156 ? 43.576 -39.744 -30.550 1.00 24.72 ?  136 GLY B O     1 
ATOM   3847 N  N     . ILE B 1 157 ? 43.567 -38.713 -28.544 1.00 27.74 ?  137 ILE B N     1 
ATOM   3848 C  CA    . ILE B 1 157 ? 42.645 -37.655 -28.973 1.00 26.84 ?  137 ILE B CA    1 
ATOM   3849 C  C     . ILE B 1 157 ? 43.211 -36.916 -30.178 1.00 23.33 ?  137 ILE B C     1 
ATOM   3850 O  O     . ILE B 1 157 ? 42.469 -36.467 -31.053 1.00 22.12 ?  137 ILE B O     1 
ATOM   3851 C  CB    . ILE B 1 157 ? 42.360 -36.684 -27.803 1.00 18.51 ?  137 ILE B CB    1 
ATOM   3852 C  CG1   . ILE B 1 157 ? 41.846 -37.440 -26.598 1.00 20.89 ?  137 ILE B CG1   1 
ATOM   3853 C  CG2   . ILE B 1 157 ? 41.329 -35.637 -28.167 1.00 18.66 ?  137 ILE B CG2   1 
ATOM   3854 C  CD1   . ILE B 1 157 ? 41.915 -36.611 -25.358 1.00 27.73 ?  137 ILE B CD1   1 
ATOM   3855 N  N     . GLU B 1 158 ? 44.532 -36.807 -30.254 1.00 23.98 ?  138 GLU B N     1 
ATOM   3856 C  CA    . GLU B 1 158 ? 45.155 -35.997 -31.283 1.00 21.71 ?  138 GLU B CA    1 
ATOM   3857 C  C     . GLU B 1 158 ? 45.091 -36.687 -32.636 1.00 25.84 ?  138 GLU B C     1 
ATOM   3858 O  O     . GLU B 1 158 ? 44.719 -36.066 -33.636 1.00 31.77 ?  138 GLU B O     1 
ATOM   3859 C  CB    . GLU B 1 158 ? 46.586 -35.697 -30.871 1.00 21.14 ?  138 GLU B CB    1 
ATOM   3860 C  CG    . GLU B 1 158 ? 46.716 -34.372 -30.169 1.00 26.08 ?  138 GLU B CG    1 
ATOM   3861 C  CD    . GLU B 1 158 ? 48.150 -34.043 -29.892 1.00 35.23 ?  138 GLU B CD    1 
ATOM   3862 O  OE1   . GLU B 1 158 ? 48.934 -35.018 -29.823 1.00 38.10 ?  138 GLU B OE1   1 
ATOM   3863 O  OE2   . GLU B 1 158 ? 48.490 -32.842 -29.741 1.00 30.74 ?  138 GLU B OE2   1 
ATOM   3864 N  N     . LEU B 1 159 ? 45.455 -37.972 -32.688 1.00 27.75 ?  139 LEU B N     1 
ATOM   3865 C  CA    . LEU B 1 159 ? 45.242 -38.757 -33.896 1.00 23.11 ?  139 LEU B CA    1 
ATOM   3866 C  C     . LEU B 1 159 ? 43.776 -38.755 -34.288 1.00 26.72 ?  139 LEU B C     1 
ATOM   3867 O  O     . LEU B 1 159 ? 43.441 -38.694 -35.477 1.00 33.08 ?  139 LEU B O     1 
ATOM   3868 C  CB    . LEU B 1 159 ? 45.721 -40.188 -33.694 1.00 21.87 ?  139 LEU B CB    1 
ATOM   3869 C  CG    . LEU B 1 159 ? 47.209 -40.343 -33.463 1.00 26.52 ?  139 LEU B CG    1 
ATOM   3870 C  CD1   . LEU B 1 159 ? 47.489 -41.639 -32.749 1.00 25.36 ?  139 LEU B CD1   1 
ATOM   3871 C  CD2   . LEU B 1 159 ? 47.946 -40.295 -34.759 1.00 28.31 ?  139 LEU B CD2   1 
ATOM   3872 N  N     . ALA B 1 160 ? 42.884 -38.808 -33.302 1.00 25.14 ?  140 ALA B N     1 
ATOM   3873 C  CA    . ALA B 1 160 ? 41.460 -38.806 -33.611 1.00 30.76 ?  140 ALA B CA    1 
ATOM   3874 C  C     . ALA B 1 160 ? 41.051 -37.497 -34.262 1.00 24.50 ?  140 ALA B C     1 
ATOM   3875 O  O     . ALA B 1 160 ? 40.195 -37.480 -35.149 1.00 25.96 ?  140 ALA B O     1 
ATOM   3876 C  CB    . ALA B 1 160 ? 40.639 -39.060 -32.346 1.00 22.19 ?  140 ALA B CB    1 
ATOM   3877 N  N     . ILE B 1 161 ? 41.666 -36.392 -33.844 1.00 25.33 ?  141 ILE B N     1 
ATOM   3878 C  CA    . ILE B 1 161 ? 41.323 -35.090 -34.402 1.00 23.31 ?  141 ILE B CA    1 
ATOM   3879 C  C     . ILE B 1 161 ? 41.652 -35.052 -35.888 1.00 30.56 ?  141 ILE B C     1 
ATOM   3880 O  O     . ILE B 1 161 ? 40.830 -34.632 -36.716 1.00 30.58 ?  141 ILE B O     1 
ATOM   3881 C  CB    . ILE B 1 161 ? 42.045 -33.982 -33.616 1.00 22.11 ?  141 ILE B CB    1 
ATOM   3882 C  CG1   . ILE B 1 161 ? 41.340 -33.777 -32.269 1.00 21.50 ?  141 ILE B CG1   1 
ATOM   3883 C  CG2   . ILE B 1 161 ? 42.094 -32.684 -34.421 1.00 16.56 ?  141 ILE B CG2   1 
ATOM   3884 C  CD1   . ILE B 1 161 ? 42.155 -33.045 -31.210 1.00 17.30 ?  141 ILE B CD1   1 
ATOM   3885 N  N     . ARG B 1 162 ? 42.836 -35.551 -36.255 1.00 29.97 ?  142 ARG B N     1 
ATOM   3886 C  CA    . ARG B 1 162 ? 43.236 -35.587 -37.655 1.00 33.54 ?  142 ARG B CA    1 
ATOM   3887 C  C     . ARG B 1 162 ? 42.343 -36.508 -38.487 1.00 29.89 ?  142 ARG B C     1 
ATOM   3888 O  O     . ARG B 1 162 ? 42.104 -36.230 -39.666 1.00 31.76 ?  142 ARG B O     1 
ATOM   3889 C  CB    . ARG B 1 162 ? 44.709 -35.996 -37.752 1.00 36.29 ?  142 ARG B CB    1 
ATOM   3890 C  CG    . ARG B 1 162 ? 45.680 -34.923 -37.216 1.00 43.57 ?  142 ARG B CG    1 
ATOM   3891 C  CD    . ARG B 1 162 ? 46.949 -35.464 -36.496 1.00 51.88 ?  142 ARG B CD    1 
ATOM   3892 N  NE    . ARG B 1 162 ? 47.765 -36.369 -37.304 1.00 53.36 ?  142 ARG B NE    1 
ATOM   3893 C  CZ    . ARG B 1 162 ? 47.524 -37.661 -37.495 1.00 59.24 ?  142 ARG B CZ    1 
ATOM   3894 N  NH1   . ARG B 1 162 ? 46.535 -38.278 -36.870 1.00 52.00 ?  142 ARG B NH1   1 
ATOM   3895 N  NH2   . ARG B 1 162 ? 48.298 -38.351 -38.333 1.00 61.51 ?  142 ARG B NH2   1 
ATOM   3896 N  N     . GLU B 1 163 ? 41.827 -37.585 -37.895 1.00 27.06 ?  143 GLU B N     1 
ATOM   3897 C  CA    . GLU B 1 163 ? 40.966 -38.511 -38.623 1.00 25.38 ?  143 GLU B CA    1 
ATOM   3898 C  C     . GLU B 1 163 ? 39.558 -37.951 -38.798 1.00 33.12 ?  143 GLU B C     1 
ATOM   3899 O  O     . GLU B 1 163 ? 38.987 -38.025 -39.895 1.00 31.16 ?  143 GLU B O     1 
ATOM   3900 C  CB    . GLU B 1 163 ? 40.935 -39.855 -37.906 1.00 23.62 ?  143 GLU B CB    1 
ATOM   3901 C  CG    . GLU B 1 163 ? 42.235 -40.611 -38.081 1.00 28.25 ?  143 GLU B CG    1 
ATOM   3902 C  CD    . GLU B 1 163 ? 42.513 -41.653 -37.002 1.00 32.57 ?  143 GLU B CD    1 
ATOM   3903 O  OE1   . GLU B 1 163 ? 42.066 -41.485 -35.845 1.00 32.76 ?  143 GLU B OE1   1 
ATOM   3904 O  OE2   . GLU B 1 163 ? 43.204 -42.647 -37.323 1.00 42.28 ?  143 GLU B OE2   1 
ATOM   3905 N  N     . ILE B 1 164 ? 38.983 -37.384 -37.732 1.00 29.61 ?  144 ILE B N     1 
ATOM   3906 C  CA    . ILE B 1 164 ? 37.671 -36.749 -37.844 1.00 29.74 ?  144 ILE B CA    1 
ATOM   3907 C  C     . ILE B 1 164 ? 37.717 -35.603 -38.835 1.00 34.22 ?  144 ILE B C     1 
ATOM   3908 O  O     . ILE B 1 164 ? 36.744 -35.338 -39.547 1.00 30.31 ?  144 ILE B O     1 
ATOM   3909 C  CB    . ILE B 1 164 ? 37.181 -36.287 -36.455 1.00 30.21 ?  144 ILE B CB    1 
ATOM   3910 C  CG1   . ILE B 1 164 ? 37.104 -37.484 -35.497 1.00 28.43 ?  144 ILE B CG1   1 
ATOM   3911 C  CG2   . ILE B 1 164 ? 35.856 -35.516 -36.539 1.00 26.68 ?  144 ILE B CG2   1 
ATOM   3912 C  CD1   . ILE B 1 164 ? 36.416 -37.180 -34.180 1.00 31.65 ?  144 ILE B CD1   1 
ATOM   3913 N  N     . ASN B 1 165 ? 38.853 -34.922 -38.915 1.00 41.27 ?  145 ASN B N     1 
ATOM   3914 C  CA    . ASN B 1 165 ? 38.986 -33.794 -39.825 1.00 39.10 ?  145 ASN B CA    1 
ATOM   3915 C  C     . ASN B 1 165 ? 38.787 -34.225 -41.284 1.00 36.80 ?  145 ASN B C     1 
ATOM   3916 O  O     . ASN B 1 165 ? 38.143 -33.515 -42.072 1.00 33.86 ?  145 ASN B O     1 
ATOM   3917 C  CB    . ASN B 1 165 ? 40.354 -33.158 -39.583 1.00 34.08 ?  145 ASN B CB    1 
ATOM   3918 C  CG    . ASN B 1 165 ? 40.563 -31.902 -40.363 1.00 39.44 ?  145 ASN B CG    1 
ATOM   3919 O  OD1   . ASN B 1 165 ? 39.777 -30.956 -40.275 1.00 42.61 ?  145 ASN B OD1   1 
ATOM   3920 N  ND2   . ASN B 1 165 ? 41.652 -31.867 -41.121 1.00 37.43 ?  145 ASN B ND2   1 
ATOM   3921 N  N     . GLN B 1 166 ? 39.293 -35.409 -41.642 1.00 30.00 ?  146 GLN B N     1 
ATOM   3922 C  CA    . GLN B 1 166 ? 39.167 -35.946 -42.990 1.00 32.35 ?  146 GLN B CA    1 
ATOM   3923 C  C     . GLN B 1 166 ? 37.742 -36.351 -43.337 1.00 33.09 ?  146 GLN B C     1 
ATOM   3924 O  O     . GLN B 1 166 ? 37.460 -36.600 -44.514 1.00 44.08 ?  146 GLN B O     1 
ATOM   3925 C  CB    . GLN B 1 166 ? 40.093 -37.157 -43.166 1.00 34.61 ?  146 GLN B CB    1 
ATOM   3926 C  CG    . GLN B 1 166 ? 41.590 -36.838 -43.237 1.00 33.20 ?  146 GLN B CG    1 
ATOM   3927 C  CD    . GLN B 1 166 ? 42.455 -38.072 -43.088 1.00 33.77 ?  146 GLN B CD    1 
ATOM   3928 O  OE1   . GLN B 1 166 ? 42.582 -38.862 -44.017 1.00 43.80 ?  146 GLN B OE1   1 
ATOM   3929 N  NE2   . GLN B 1 166 ? 43.044 -38.256 -41.906 1.00 39.18 ?  146 GLN B NE2   1 
ATOM   3930 N  N     . LEU B 1 167 ? 36.846 -36.414 -42.352 1.00 34.23 ?  147 LEU B N     1 
ATOM   3931 C  CA    . LEU B 1 167 ? 35.494 -36.898 -42.597 1.00 35.05 ?  147 LEU B CA    1 
ATOM   3932 C  C     . LEU B 1 167 ? 34.662 -35.890 -43.370 1.00 38.95 ?  147 LEU B C     1 
ATOM   3933 O  O     . LEU B 1 167 ? 33.710 -36.278 -44.059 1.00 38.79 ?  147 LEU B O     1 
ATOM   3934 C  CB    . LEU B 1 167 ? 34.799 -37.226 -41.275 1.00 35.07 ?  147 LEU B CB    1 
ATOM   3935 C  CG    . LEU B 1 167 ? 35.294 -38.386 -40.408 1.00 35.35 ?  147 LEU B CG    1 
ATOM   3936 C  CD1   . LEU B 1 167 ? 34.412 -38.527 -39.153 1.00 34.54 ?  147 LEU B CD1   1 
ATOM   3937 C  CD2   . LEU B 1 167 ? 35.346 -39.691 -41.209 1.00 32.84 ?  147 LEU B CD2   1 
ATOM   3938 N  N     . SER B 1 168 ? 34.985 -34.598 -43.250 1.00 40.62 ?  148 SER B N     1 
ATOM   3939 C  CA    . SER B 1 168 ? 34.233 -33.577 -43.973 1.00 45.86 ?  148 SER B CA    1 
ATOM   3940 C  C     . SER B 1 168 ? 34.240 -33.836 -45.476 1.00 43.80 ?  148 SER B C     1 
ATOM   3941 O  O     . SER B 1 168 ? 33.235 -33.607 -46.157 1.00 43.32 ?  148 SER B O     1 
ATOM   3942 C  CB    . SER B 1 168 ? 34.800 -32.191 -43.665 1.00 49.34 ?  148 SER B CB    1 
ATOM   3943 O  OG    . SER B 1 168 ? 34.184 -31.619 -42.526 1.00 56.81 ?  148 SER B OG    1 
ATOM   3944 N  N     . ASN B 1 169 ? 35.355 -34.337 -46.004 1.00 43.55 ?  149 ASN B N     1 
ATOM   3945 C  CA    . ASN B 1 169 ? 35.571 -34.454 -47.441 1.00 46.68 ?  149 ASN B CA    1 
ATOM   3946 C  C     . ASN B 1 169 ? 35.437 -35.892 -47.938 1.00 52.77 ?  149 ASN B C     1 
ATOM   3947 O  O     . ASN B 1 169 ? 36.072 -36.269 -48.924 1.00 59.21 ?  149 ASN B O     1 
ATOM   3948 C  CB    . ASN B 1 169 ? 36.941 -33.889 -47.805 1.00 51.54 ?  149 ASN B CB    1 
ATOM   3949 C  CG    . ASN B 1 169 ? 36.970 -32.367 -47.770 1.00 60.79 ?  149 ASN B CG    1 
ATOM   3950 O  OD1   . ASN B 1 169 ? 37.014 -31.767 -46.692 1.00 66.33 ?  149 ASN B OD1   1 
ATOM   3951 N  ND2   . ASN B 1 169 ? 36.943 -31.737 -48.943 1.00 60.91 ?  149 ASN B ND2   1 
ATOM   3952 N  N     . LEU B 1 170 ? 34.626 -36.706 -47.256 1.00 51.62 ?  150 LEU B N     1 
ATOM   3953 C  CA    . LEU B 1 170 ? 34.290 -38.057 -47.684 1.00 39.46 ?  150 LEU B CA    1 
ATOM   3954 C  C     . LEU B 1 170 ? 32.779 -38.228 -47.612 1.00 40.21 ?  150 LEU B C     1 
ATOM   3955 O  O     . LEU B 1 170 ? 32.095 -37.520 -46.871 1.00 33.61 ?  150 LEU B O     1 
ATOM   3956 C  CB    . LEU B 1 170 ? 34.987 -39.121 -46.823 1.00 35.56 ?  150 LEU B CB    1 
ATOM   3957 C  CG    . LEU B 1 170 ? 36.518 -39.076 -46.830 1.00 41.33 ?  150 LEU B CG    1 
ATOM   3958 C  CD1   . LEU B 1 170 ? 37.132 -40.140 -45.924 1.00 31.36 ?  150 LEU B CD1   1 
ATOM   3959 C  CD2   . LEU B 1 170 ? 37.019 -39.250 -48.253 1.00 50.56 ?  150 LEU B CD2   1 
ATOM   3960 N  N     . SER B 1 171 ? 32.256 -39.165 -48.403 1.00 42.92 ?  151 SER B N     1 
ATOM   3961 C  CA    . SER B 1 171 ? 30.828 -39.452 -48.422 1.00 37.50 ?  151 SER B CA    1 
ATOM   3962 C  C     . SER B 1 171 ? 30.506 -40.660 -47.554 1.00 37.15 ?  151 SER B C     1 
ATOM   3963 O  O     . SER B 1 171 ? 31.331 -41.559 -47.365 1.00 38.45 ?  151 SER B O     1 
ATOM   3964 C  CB    . SER B 1 171 ? 30.336 -39.718 -49.839 1.00 47.28 ?  151 SER B CB    1 
ATOM   3965 O  OG    . SER B 1 171 ? 31.332 -40.405 -50.572 1.00 58.90 ?  151 SER B OG    1 
ATOM   3966 N  N     . LEU B 1 172 ? 29.282 -40.675 -47.034 1.00 38.75 ?  152 LEU B N     1 
ATOM   3967 C  CA    . LEU B 1 172 ? 28.836 -41.796 -46.222 1.00 36.56 ?  152 LEU B CA    1 
ATOM   3968 C  C     . LEU B 1 172 ? 28.844 -43.097 -47.009 1.00 41.87 ?  152 LEU B C     1 
ATOM   3969 O  O     . LEU B 1 172 ? 28.840 -44.176 -46.410 1.00 44.77 ?  152 LEU B O     1 
ATOM   3970 C  CB    . LEU B 1 172 ? 27.440 -41.506 -45.674 1.00 37.21 ?  152 LEU B CB    1 
ATOM   3971 C  CG    . LEU B 1 172 ? 27.350 -40.277 -44.761 1.00 45.98 ?  152 LEU B CG    1 
ATOM   3972 C  CD1   . LEU B 1 172 ? 25.911 -39.750 -44.673 1.00 42.45 ?  152 LEU B CD1   1 
ATOM   3973 C  CD2   . LEU B 1 172 ? 27.912 -40.591 -43.366 1.00 32.26 ?  152 LEU B CD2   1 
ATOM   3974 N  N     . ASN B 1 173 ? 28.861 -43.019 -48.339 1.00 46.81 ?  153 ASN B N     1 
ATOM   3975 C  CA    . ASN B 1 173 ? 28.942 -44.207 -49.168 1.00 38.23 ?  153 ASN B CA    1 
ATOM   3976 C  C     . ASN B 1 173 ? 30.380 -44.650 -49.405 1.00 38.14 ?  153 ASN B C     1 
ATOM   3977 O  O     . ASN B 1 173 ? 30.615 -45.832 -49.668 1.00 41.28 ?  153 ASN B O     1 
ATOM   3978 C  CB    . ASN B 1 173 ? 28.248 -43.947 -50.501 1.00 42.16 ?  153 ASN B CB    1 
ATOM   3979 C  CG    . ASN B 1 173 ? 27.688 -45.200 -51.115 1.00 50.07 ?  153 ASN B CG    1 
ATOM   3980 O  OD1   . ASN B 1 173 ? 28.279 -46.274 -51.024 1.00 55.02 ?  153 ASN B OD1   1 
ATOM   3981 N  ND2   . ASN B 1 173 ? 26.530 -45.072 -51.742 1.00 55.89 ?  153 ASN B ND2   1 
ATOM   3982 N  N     . ASP B 1 174 ? 31.341 -43.743 -49.308 1.00 38.59 ?  154 ASP B N     1 
ATOM   3983 C  CA    . ASP B 1 174 ? 32.744 -44.111 -49.427 1.00 30.29 ?  154 ASP B CA    1 
ATOM   3984 C  C     . ASP B 1 174 ? 33.140 -44.972 -48.234 1.00 39.57 ?  154 ASP B C     1 
ATOM   3985 O  O     . ASP B 1 174 ? 32.986 -44.535 -47.085 1.00 40.79 ?  154 ASP B O     1 
ATOM   3986 C  CB    . ASP B 1 174 ? 33.616 -42.858 -49.512 1.00 30.35 ?  154 ASP B CB    1 
ATOM   3987 C  CG    . ASP B 1 174 ? 35.089 -43.167 -49.778 1.00 35.19 ?  154 ASP B CG    1 
ATOM   3988 O  OD1   . ASP B 1 174 ? 35.491 -44.347 -49.722 1.00 40.06 ?  154 ASP B OD1   1 
ATOM   3989 O  OD2   . ASP B 1 174 ? 35.866 -42.219 -50.039 1.00 40.34 ?  154 ASP B OD2   1 
ATOM   3990 N  N     . PRO B 1 175 ? 33.630 -46.193 -48.451 1.00 44.93 ?  155 PRO B N     1 
ATOM   3991 C  CA    . PRO B 1 175 ? 34.103 -47.009 -47.322 1.00 46.17 ?  155 PRO B CA    1 
ATOM   3992 C  C     . PRO B 1 175 ? 35.229 -46.371 -46.535 1.00 41.28 ?  155 PRO B C     1 
ATOM   3993 O  O     . PRO B 1 175 ? 35.457 -46.765 -45.384 1.00 39.55 ?  155 PRO B O     1 
ATOM   3994 C  CB    . PRO B 1 175 ? 34.567 -48.308 -48.000 1.00 37.26 ?  155 PRO B CB    1 
ATOM   3995 C  CG    . PRO B 1 175 ? 33.758 -48.372 -49.250 1.00 39.15 ?  155 PRO B CG    1 
ATOM   3996 C  CD    . PRO B 1 175 ? 33.588 -46.961 -49.709 1.00 43.20 ?  155 PRO B CD    1 
ATOM   3997 N  N     . ALA B 1 176 ? 35.961 -45.421 -47.119 1.00 39.70 ?  156 ALA B N     1 
ATOM   3998 C  CA    . ALA B 1 176 ? 37.058 -44.808 -46.379 1.00 43.62 ?  156 ALA B CA    1 
ATOM   3999 C  C     . ALA B 1 176 ? 36.539 -43.954 -45.228 1.00 37.27 ?  156 ALA B C     1 
ATOM   4000 O  O     . ALA B 1 176 ? 37.241 -43.784 -44.224 1.00 35.97 ?  156 ALA B O     1 
ATOM   4001 C  CB    . ALA B 1 176 ? 37.937 -43.984 -47.319 1.00 28.99 ?  156 ALA B CB    1 
ATOM   4002 N  N     . PHE B 1 177 ? 35.318 -43.428 -45.357 1.00 31.27 ?  157 PHE B N     1 
ATOM   4003 C  CA    . PHE B 1 177 ? 34.658 -42.734 -44.255 1.00 29.00 ?  157 PHE B CA    1 
ATOM   4004 C  C     . PHE B 1 177 ? 34.483 -43.658 -43.053 1.00 36.41 ?  157 PHE B C     1 
ATOM   4005 O  O     . PHE B 1 177 ? 34.987 -43.375 -41.961 1.00 36.16 ?  157 PHE B O     1 
ATOM   4006 C  CB    . PHE B 1 177 ? 33.308 -42.196 -44.729 1.00 31.05 ?  157 PHE B CB    1 
ATOM   4007 C  CG    . PHE B 1 177 ? 32.563 -41.390 -43.700 1.00 40.57 ?  157 PHE B CG    1 
ATOM   4008 C  CD1   . PHE B 1 177 ? 31.924 -42.006 -42.626 1.00 33.85 ?  157 PHE B CD1   1 
ATOM   4009 C  CD2   . PHE B 1 177 ? 32.470 -40.015 -43.825 1.00 36.94 ?  157 PHE B CD2   1 
ATOM   4010 C  CE1   . PHE B 1 177 ? 31.229 -41.269 -41.702 1.00 30.14 ?  157 PHE B CE1   1 
ATOM   4011 C  CE2   . PHE B 1 177 ? 31.777 -39.269 -42.893 1.00 36.43 ?  157 PHE B CE2   1 
ATOM   4012 C  CZ    . PHE B 1 177 ? 31.153 -39.897 -41.830 1.00 36.44 ?  157 PHE B CZ    1 
ATOM   4013 N  N     . GLU B 1 178 ? 33.757 -44.769 -43.236 1.00 37.00 ?  158 GLU B N     1 
ATOM   4014 C  CA    . GLU B 1 178 ? 33.546 -45.711 -42.139 1.00 35.54 ?  158 GLU B CA    1 
ATOM   4015 C  C     . GLU B 1 178 ? 34.864 -46.124 -41.500 1.00 39.40 ?  158 GLU B C     1 
ATOM   4016 O  O     . GLU B 1 178 ? 34.980 -46.174 -40.262 1.00 33.02 ?  158 GLU B O     1 
ATOM   4017 C  CB    . GLU B 1 178 ? 32.801 -46.953 -42.623 1.00 38.26 ?  158 GLU B CB    1 
ATOM   4018 C  CG    . GLU B 1 178 ? 32.506 -47.944 -41.491 1.00 41.14 ?  158 GLU B CG    1 
ATOM   4019 C  CD    . GLU B 1 178 ? 32.245 -49.367 -41.969 1.00 46.78 ?  158 GLU B CD    1 
ATOM   4020 O  OE1   . GLU B 1 178 ? 32.457 -49.647 -43.169 1.00 44.62 ?  158 GLU B OE1   1 
ATOM   4021 O  OE2   . GLU B 1 178 ? 31.832 -50.207 -41.136 1.00 48.49 ?  158 GLU B OE2   1 
ATOM   4022 N  N     . SER B 1 179 ? 35.872 -46.417 -42.327 1.00 29.12 ?  159 SER B N     1 
ATOM   4023 C  CA    . SER B 1 179 ? 37.161 -46.832 -41.786 1.00 27.32 ?  159 SER B CA    1 
ATOM   4024 C  C     . SER B 1 179 ? 37.721 -45.766 -40.861 1.00 36.58 ?  159 SER B C     1 
ATOM   4025 O  O     . SER B 1 179 ? 38.183 -46.067 -39.755 1.00 31.41 ?  159 SER B O     1 
ATOM   4026 C  CB    . SER B 1 179 ? 38.144 -47.113 -42.913 1.00 27.91 ?  159 SER B CB    1 
ATOM   4027 O  OG    . SER B 1 179 ? 37.498 -47.830 -43.950 1.00 60.36 ?  159 SER B OG    1 
ATOM   4028 N  N     . LEU B 1 180 ? 37.653 -44.505 -41.299 1.00 28.81 ?  160 LEU B N     1 
ATOM   4029 C  CA    . LEU B 1 180 ? 38.316 -43.415 -40.598 1.00 32.83 ?  160 LEU B CA    1 
ATOM   4030 C  C     . LEU B 1 180 ? 37.614 -43.106 -39.283 1.00 29.57 ?  160 LEU B C     1 
ATOM   4031 O  O     . LEU B 1 180 ? 38.270 -42.882 -38.261 1.00 29.92 ?  160 LEU B O     1 
ATOM   4032 C  CB    . LEU B 1 180 ? 38.334 -42.192 -41.511 1.00 32.97 ?  160 LEU B CB    1 
ATOM   4033 C  CG    . LEU B 1 180 ? 39.529 -41.265 -41.617 1.00 29.70 ?  160 LEU B CG    1 
ATOM   4034 C  CD1   . LEU B 1 180 ? 40.835 -41.997 -41.422 1.00 25.31 ?  160 LEU B CD1   1 
ATOM   4035 C  CD2   . LEU B 1 180 ? 39.464 -40.706 -43.027 1.00 42.68 ?  160 LEU B CD2   1 
ATOM   4036 N  N     . ALA B 1 181 ? 36.279 -43.097 -39.305 1.00 26.10 ?  161 ALA B N     1 
ATOM   4037 C  CA    . ALA B 1 181 ? 35.496 -42.910 -38.098 1.00 31.84 ?  161 ALA B CA    1 
ATOM   4038 C  C     . ALA B 1 181 ? 35.716 -44.051 -37.104 1.00 37.52 ?  161 ALA B C     1 
ATOM   4039 O  O     . ALA B 1 181 ? 35.576 -43.854 -35.885 1.00 31.48 ?  161 ALA B O     1 
ATOM   4040 C  CB    . ALA B 1 181 ? 34.020 -42.769 -38.472 1.00 25.52 ?  161 ALA B CB    1 
ATOM   4041 N  N     . LYS B 1 182 ? 36.073 -45.243 -37.601 1.00 30.90 ?  162 LYS B N     1 
ATOM   4042 C  CA    . LYS B 1 182 ? 36.356 -46.366 -36.715 1.00 32.55 ?  162 LYS B CA    1 
ATOM   4043 C  C     . LYS B 1 182 ? 37.747 -46.257 -36.117 1.00 31.91 ?  162 LYS B C     1 
ATOM   4044 O  O     . LYS B 1 182 ? 37.941 -46.561 -34.933 1.00 37.48 ?  162 LYS B O     1 
ATOM   4045 C  CB    . LYS B 1 182 ? 36.204 -47.693 -37.463 1.00 30.16 ?  162 LYS B CB    1 
ATOM   4046 C  CG    . LYS B 1 182 ? 34.765 -48.203 -37.549 1.00 32.93 ?  162 LYS B CG    1 
ATOM   4047 C  CD    . LYS B 1 182 ? 34.761 -49.606 -38.126 1.00 36.56 ?  162 LYS B CD    1 
ATOM   4048 C  CE    . LYS B 1 182 ? 33.443 -50.310 -37.914 1.00 39.83 ?  162 LYS B CE    1 
ATOM   4049 N  NZ    . LYS B 1 182 ? 33.326 -51.480 -38.822 1.00 44.03 ?  162 LYS B NZ    1 
ATOM   4050 N  N     . SER B 1 183 ? 38.721 -45.838 -36.924 1.00 22.18 ?  163 SER B N     1 
ATOM   4051 C  CA    . SER B 1 183 ? 40.037 -45.522 -36.393 1.00 25.23 ?  163 SER B CA    1 
ATOM   4052 C  C     . SER B 1 183 ? 39.962 -44.404 -35.359 1.00 32.59 ?  163 SER B C     1 
ATOM   4053 O  O     . SER B 1 183 ? 40.687 -44.422 -34.358 1.00 24.51 ?  163 SER B O     1 
ATOM   4054 C  CB    . SER B 1 183 ? 40.971 -45.114 -37.521 1.00 25.40 ?  163 SER B CB    1 
ATOM   4055 O  OG    . SER B 1 183 ? 42.263 -44.902 -36.995 1.00 32.02 ?  163 SER B OG    1 
ATOM   4056 N  N     . ALA B 1 184 ? 39.112 -43.404 -35.599 1.00 27.52 ?  164 ALA B N     1 
ATOM   4057 C  CA    . ALA B 1 184 ? 38.999 -42.309 -34.652 1.00 26.74 ?  164 ALA B CA    1 
ATOM   4058 C  C     . ALA B 1 184 ? 38.381 -42.793 -33.347 1.00 32.70 ?  164 ALA B C     1 
ATOM   4059 O  O     . ALA B 1 184 ? 38.927 -42.548 -32.261 1.00 27.55 ?  164 ALA B O     1 
ATOM   4060 C  CB    . ALA B 1 184 ? 38.180 -41.174 -35.262 1.00 22.47 ?  164 ALA B CB    1 
ATOM   4061 N  N     . ALA B 1 185 ? 37.246 -43.501 -33.441 1.00 30.34 ?  165 ALA B N     1 
ATOM   4062 C  CA    . ALA B 1 185 ? 36.637 -44.090 -32.253 1.00 32.68 ?  165 ALA B CA    1 
ATOM   4063 C  C     . ALA B 1 185 ? 37.645 -44.929 -31.479 1.00 30.18 ?  165 ALA B C     1 
ATOM   4064 O  O     . ALA B 1 185 ? 37.669 -44.907 -30.244 1.00 32.91 ?  165 ALA B O     1 
ATOM   4065 C  CB    . ALA B 1 185 ? 35.426 -44.939 -32.639 1.00 33.79 ?  165 ALA B CB    1 
ATOM   4066 N  N     . LEU B 1 186 ? 38.499 -45.660 -32.190 1.00 27.12 ?  166 LEU B N     1 
ATOM   4067 C  CA    . LEU B 1 186 ? 39.532 -46.430 -31.514 1.00 29.42 ?  166 LEU B CA    1 
ATOM   4068 C  C     . LEU B 1 186 ? 40.505 -45.517 -30.792 1.00 29.32 ?  166 LEU B C     1 
ATOM   4069 O  O     . LEU B 1 186 ? 40.926 -45.809 -29.667 1.00 32.96 ?  166 LEU B O     1 
ATOM   4070 C  CB    . LEU B 1 186 ? 40.267 -47.307 -32.519 1.00 29.47 ?  166 LEU B CB    1 
ATOM   4071 C  CG    . LEU B 1 186 ? 41.123 -48.446 -31.989 1.00 26.35 ?  166 LEU B CG    1 
ATOM   4072 C  CD1   . LEU B 1 186 ? 40.283 -49.393 -31.131 1.00 26.56 ?  166 LEU B CD1   1 
ATOM   4073 C  CD2   . LEU B 1 186 ? 41.725 -49.165 -33.167 1.00 20.47 ?  166 LEU B CD2   1 
ATOM   4074 N  N     . HIS B 1 187 ? 40.876 -44.406 -31.425 1.00 28.91 ?  167 HIS B N     1 
ATOM   4075 C  CA    . HIS B 1 187 ? 41.856 -43.506 -30.831 1.00 27.65 ?  167 HIS B CA    1 
ATOM   4076 C  C     . HIS B 1 187 ? 41.266 -42.747 -29.644 1.00 31.13 ?  167 HIS B C     1 
ATOM   4077 O  O     . HIS B 1 187 ? 41.964 -42.473 -28.663 1.00 25.98 ?  167 HIS B O     1 
ATOM   4078 C  CB    . HIS B 1 187 ? 42.382 -42.546 -31.893 1.00 22.92 ?  167 HIS B CB    1 
ATOM   4079 C  CG    . HIS B 1 187 ? 43.444 -43.141 -32.764 1.00 30.21 ?  167 HIS B CG    1 
ATOM   4080 N  ND1   . HIS B 1 187 ? 43.332 -43.216 -34.141 1.00 30.77 ?  167 HIS B ND1   1 
ATOM   4081 C  CD2   . HIS B 1 187 ? 44.645 -43.685 -32.454 1.00 26.79 ?  167 HIS B CD2   1 
ATOM   4082 C  CE1   . HIS B 1 187 ? 44.416 -43.785 -34.639 1.00 28.60 ?  167 HIS B CE1   1 
ATOM   4083 N  NE2   . HIS B 1 187 ? 45.228 -44.081 -33.637 1.00 31.77 ?  167 HIS B NE2   1 
ATOM   4084 N  N     . VAL B 1 188 ? 39.984 -42.392 -29.722 1.00 28.11 ?  168 VAL B N     1 
ATOM   4085 C  CA    . VAL B 1 188 ? 39.305 -41.792 -28.585 1.00 25.57 ?  168 VAL B CA    1 
ATOM   4086 C  C     . VAL B 1 188 ? 39.265 -42.756 -27.405 1.00 33.08 ?  168 VAL B C     1 
ATOM   4087 O  O     . VAL B 1 188 ? 39.181 -42.331 -26.243 1.00 34.51 ?  168 VAL B O     1 
ATOM   4088 C  CB    . VAL B 1 188 ? 37.894 -41.352 -29.011 1.00 29.55 ?  168 VAL B CB    1 
ATOM   4089 C  CG1   . VAL B 1 188 ? 37.154 -40.704 -27.864 1.00 26.74 ?  168 VAL B CG1   1 
ATOM   4090 C  CG2   . VAL B 1 188 ? 37.988 -40.410 -30.164 1.00 31.05 ?  168 VAL B CG2   1 
ATOM   4091 N  N     . TYR B 1 189 ? 39.334 -44.063 -27.666 1.00 27.75 ?  169 TYR B N     1 
ATOM   4092 C  CA    . TYR B 1 189 ? 39.307 -45.004 -26.556 1.00 28.79 ?  169 TYR B CA    1 
ATOM   4093 C  C     . TYR B 1 189 ? 40.511 -44.815 -25.647 1.00 30.19 ?  169 TYR B C     1 
ATOM   4094 O  O     . TYR B 1 189 ? 40.455 -45.154 -24.459 1.00 32.74 ?  169 TYR B O     1 
ATOM   4095 C  CB    . TYR B 1 189 ? 39.250 -46.439 -27.069 1.00 34.49 ?  169 TYR B CB    1 
ATOM   4096 C  CG    . TYR B 1 189 ? 37.931 -47.125 -26.806 1.00 33.74 ?  169 TYR B CG    1 
ATOM   4097 C  CD1   . TYR B 1 189 ? 37.585 -47.546 -25.518 1.00 30.50 ?  169 TYR B CD1   1 
ATOM   4098 C  CD2   . TYR B 1 189 ? 37.043 -47.388 -27.850 1.00 32.96 ?  169 TYR B CD2   1 
ATOM   4099 C  CE1   . TYR B 1 189 ? 36.374 -48.184 -25.278 1.00 34.19 ?  169 TYR B CE1   1 
ATOM   4100 C  CE2   . TYR B 1 189 ? 35.840 -48.022 -27.621 1.00 28.84 ?  169 TYR B CE2   1 
ATOM   4101 C  CZ    . TYR B 1 189 ? 35.510 -48.422 -26.338 1.00 35.41 ?  169 TYR B CZ    1 
ATOM   4102 O  OH    . TYR B 1 189 ? 34.310 -49.052 -26.121 1.00 37.87 ?  169 TYR B OH    1 
ATOM   4103 N  N     . GLN B 1 190 ? 41.599 -44.270 -26.186 1.00 30.41 ?  170 GLN B N     1 
ATOM   4104 C  CA    . GLN B 1 190 ? 42.759 -43.909 -25.378 1.00 35.19 ?  170 GLN B CA    1 
ATOM   4105 C  C     . GLN B 1 190 ? 42.381 -43.032 -24.187 1.00 37.35 ?  170 GLN B C     1 
ATOM   4106 O  O     . GLN B 1 190 ? 42.948 -43.171 -23.094 1.00 33.06 ?  170 GLN B O     1 
ATOM   4107 C  CB    . GLN B 1 190 ? 43.764 -43.181 -26.257 1.00 35.98 ?  170 GLN B CB    1 
ATOM   4108 C  CG    . GLN B 1 190 ? 44.552 -44.107 -27.115 1.00 36.24 ?  170 GLN B CG    1 
ATOM   4109 C  CD    . GLN B 1 190 ? 45.616 -44.776 -26.313 1.00 47.96 ?  170 GLN B CD    1 
ATOM   4110 O  OE1   . GLN B 1 190 ? 45.537 -45.973 -26.030 1.00 50.64 ?  170 GLN B OE1   1 
ATOM   4111 N  NE2   . GLN B 1 190 ? 46.620 -43.995 -25.898 1.00 50.39 ?  170 GLN B NE2   1 
ATOM   4112 N  N     . ALA B 1 191 ? 41.444 -42.101 -24.388 1.00 29.59 ?  171 ALA B N     1 
ATOM   4113 C  CA    . ALA B 1 191 ? 40.995 -41.267 -23.279 1.00 26.23 ?  171 ALA B CA    1 
ATOM   4114 C  C     . ALA B 1 191 ? 40.229 -42.084 -22.241 1.00 34.48 ?  171 ALA B C     1 
ATOM   4115 O  O     . ALA B 1 191 ? 40.363 -41.849 -21.032 1.00 28.01 ?  171 ALA B O     1 
ATOM   4116 C  CB    . ALA B 1 191 ? 40.124 -40.128 -23.802 1.00 22.18 ?  171 ALA B CB    1 
ATOM   4117 N  N     . VAL B 1 192 ? 39.392 -43.020 -22.701 1.00 33.38 ?  172 VAL B N     1 
ATOM   4118 C  CA    . VAL B 1 192 ? 38.684 -43.914 -21.794 1.00 28.19 ?  172 VAL B CA    1 
ATOM   4119 C  C     . VAL B 1 192 ? 39.677 -44.667 -20.923 1.00 25.61 ?  172 VAL B C     1 
ATOM   4120 O  O     . VAL B 1 192 ? 39.539 -44.719 -19.698 1.00 27.03 ?  172 VAL B O     1 
ATOM   4121 C  CB    . VAL B 1 192 ? 37.782 -44.869 -22.595 1.00 29.28 ?  172 VAL B CB    1 
ATOM   4122 C  CG1   . VAL B 1 192 ? 37.024 -45.799 -21.675 1.00 17.89 ?  172 VAL B CG1   1 
ATOM   4123 C  CG2   . VAL B 1 192 ? 36.814 -44.055 -23.450 1.00 30.61 ?  172 VAL B CG2   1 
ATOM   4124 N  N     . ASP B 1 193 ? 40.716 -45.230 -21.536 1.00 25.85 ?  173 ASP B N     1 
ATOM   4125 C  CA    . ASP B 1 193 ? 41.728 -45.912 -20.739 1.00 30.00 ?  173 ASP B CA    1 
ATOM   4126 C  C     . ASP B 1 193 ? 42.412 -44.947 -19.786 1.00 32.34 ?  173 ASP B C     1 
ATOM   4127 O  O     . ASP B 1 193 ? 42.730 -45.311 -18.651 1.00 38.16 ?  173 ASP B O     1 
ATOM   4128 C  CB    . ASP B 1 193 ? 42.758 -46.582 -21.639 1.00 28.04 ?  173 ASP B CB    1 
ATOM   4129 C  CG    . ASP B 1 193 ? 42.138 -47.622 -22.543 1.00 42.78 ?  173 ASP B CG    1 
ATOM   4130 O  OD1   . ASP B 1 193 ? 41.077 -48.185 -22.167 1.00 42.29 ?  173 ASP B OD1   1 
ATOM   4131 O  OD2   . ASP B 1 193 ? 42.708 -47.873 -23.634 1.00 46.26 ?  173 ASP B OD2   1 
ATOM   4132 N  N     . GLY B 1 194 ? 42.638 -43.708 -20.229 1.00 33.23 ?  174 GLY B N     1 
ATOM   4133 C  CA    . GLY B 1 194 ? 43.270 -42.725 -19.363 1.00 31.32 ?  174 GLY B CA    1 
ATOM   4134 C  C     . GLY B 1 194 ? 42.455 -42.424 -18.118 1.00 31.37 ?  174 GLY B C     1 
ATOM   4135 O  O     . GLY B 1 194 ? 42.968 -42.499 -16.999 1.00 31.27 ?  174 GLY B O     1 
ATOM   4136 N  N     . ILE B 1 195 ? 41.169 -42.087 -18.293 1.00 21.97 ?  175 ILE B N     1 
ATOM   4137 C  CA    . ILE B 1 195 ? 40.344 -41.801 -17.129 1.00 21.84 ?  175 ILE B CA    1 
ATOM   4138 C  C     . ILE B 1 195 ? 40.167 -43.064 -16.296 1.00 34.71 ?  175 ILE B C     1 
ATOM   4139 O  O     . ILE B 1 195 ? 40.041 -42.991 -15.066 1.00 35.16 ?  175 ILE B O     1 
ATOM   4140 C  CB    . ILE B 1 195 ? 38.998 -41.159 -17.532 1.00 21.05 ?  175 ILE B CB    1 
ATOM   4141 C  CG1   . ILE B 1 195 ? 38.419 -40.348 -16.374 1.00 26.21 ?  175 ILE B CG1   1 
ATOM   4142 C  CG2   . ILE B 1 195 ? 37.975 -42.183 -17.904 1.00 22.79 ?  175 ILE B CG2   1 
ATOM   4143 C  CD1   . ILE B 1 195 ? 39.349 -39.311 -15.803 1.00 24.61 ?  175 ILE B CD1   1 
ATOM   4144 N  N     . GLY B 1 196 ? 40.212 -44.238 -16.932 1.00 30.09 ?  176 GLY B N     1 
ATOM   4145 C  CA    . GLY B 1 196 ? 40.204 -45.472 -16.170 1.00 27.62 ?  176 GLY B CA    1 
ATOM   4146 C  C     . GLY B 1 196 ? 41.381 -45.583 -15.216 1.00 33.29 ?  176 GLY B C     1 
ATOM   4147 O  O     . GLY B 1 196 ? 41.214 -45.960 -14.055 1.00 33.02 ?  176 GLY B O     1 
ATOM   4148 N  N     . GLU B 1 197 ? 42.595 -45.270 -15.696 1.00 28.86 ?  177 GLU B N     1 
ATOM   4149 C  CA    . GLU B 1 197 ? 43.755 -45.271 -14.808 1.00 27.11 ?  177 GLU B CA    1 
ATOM   4150 C  C     . GLU B 1 197 ? 43.588 -44.274 -13.656 1.00 32.19 ?  177 GLU B C     1 
ATOM   4151 O  O     . GLU B 1 197 ? 44.112 -44.495 -12.558 1.00 27.77 ?  177 GLU B O     1 
ATOM   4152 C  CB    . GLU B 1 197 ? 45.025 -44.954 -15.594 1.00 25.04 ?  177 GLU B CB    1 
ATOM   4153 C  CG    . GLU B 1 197 ? 45.643 -46.105 -16.401 1.00 38.71 ?  177 GLU B CG    1 
ATOM   4154 C  CD    . GLU B 1 197 ? 45.730 -47.435 -15.650 1.00 49.97 ?  177 GLU B CD    1 
ATOM   4155 O  OE1   . GLU B 1 197 ? 46.715 -47.632 -14.904 1.00 51.34 ?  177 GLU B OE1   1 
ATOM   4156 O  OE2   . GLU B 1 197 ? 44.837 -48.299 -15.829 1.00 50.97 ?  177 GLU B OE2   1 
ATOM   4157 N  N     . THR B 1 198 ? 42.877 -43.170 -13.884 1.00 27.67 ?  178 THR B N     1 
ATOM   4158 C  CA    . THR B 1 198 ? 42.667 -42.202 -12.814 1.00 29.90 ?  178 THR B CA    1 
ATOM   4159 C  C     . THR B 1 198 ? 41.712 -42.750 -11.762 1.00 32.77 ?  178 THR B C     1 
ATOM   4160 O  O     . THR B 1 198 ? 41.958 -42.613 -10.553 1.00 27.16 ?  178 THR B O     1 
ATOM   4161 C  CB    . THR B 1 198 ? 42.134 -40.890 -13.397 1.00 25.44 ?  178 THR B CB    1 
ATOM   4162 O  OG1   . THR B 1 198 ? 42.990 -40.481 -14.466 1.00 24.29 ?  178 THR B OG1   1 
ATOM   4163 C  CG2   . THR B 1 198 ? 42.082 -39.789 -12.338 1.00 24.08 ?  178 THR B CG2   1 
ATOM   4164 N  N     . ILE B 1 199 ? 40.621 -43.377 -12.214 1.00 31.00 ?  179 ILE B N     1 
ATOM   4165 C  CA    . ILE B 1 199 ? 39.650 -43.986 -11.315 1.00 32.93 ?  179 ILE B CA    1 
ATOM   4166 C  C     . ILE B 1 199 ? 40.297 -45.085 -10.493 1.00 24.47 ?  179 ILE B C     1 
ATOM   4167 O  O     . ILE B 1 199 ? 39.974 -45.265 -9.317  1.00 28.07 ?  179 ILE B O     1 
ATOM   4168 C  CB    . ILE B 1 199 ? 38.455 -44.494 -12.139 1.00 33.21 ?  179 ILE B CB    1 
ATOM   4169 C  CG1   . ILE B 1 199 ? 37.732 -43.292 -12.751 1.00 28.41 ?  179 ILE B CG1   1 
ATOM   4170 C  CG2   . ILE B 1 199 ? 37.510 -45.312 -11.282 1.00 24.74 ?  179 ILE B CG2   1 
ATOM   4171 C  CD1   . ILE B 1 199 ? 36.703 -43.640 -13.791 1.00 17.87 ?  179 ILE B CD1   1 
ATOM   4172 N  N     . LYS B 1 200 ? 41.265 -45.784 -11.069 1.00 27.50 ?  180 LYS B N     1 
ATOM   4173 C  CA    . LYS B 1 200 ? 41.996 -46.811 -10.337 1.00 27.72 ?  180 LYS B CA    1 
ATOM   4174 C  C     . LYS B 1 200 ? 42.931 -46.202 -9.297  1.00 30.04 ?  180 LYS B C     1 
ATOM   4175 O  O     . LYS B 1 200 ? 43.005 -46.680 -8.163  1.00 31.73 ?  180 LYS B O     1 
ATOM   4176 C  CB    . LYS B 1 200 ? 42.799 -47.651 -11.318 1.00 28.69 ?  180 LYS B CB    1 
ATOM   4177 C  CG    . LYS B 1 200 ? 42.349 -49.063 -11.532 1.00 34.35 ?  180 LYS B CG    1 
ATOM   4178 C  CD    . LYS B 1 200 ? 42.897 -49.519 -12.890 1.00 40.53 ?  180 LYS B CD    1 
ATOM   4179 C  CE    . LYS B 1 200 ? 44.250 -50.220 -12.745 1.00 43.20 ?  180 LYS B CE    1 
ATOM   4180 N  NZ    . LYS B 1 200 ? 44.798 -50.668 -14.070 1.00 43.34 ?  180 LYS B NZ    1 
ATOM   4181 N  N     . LYS B 1 201 ? 43.681 -45.162 -9.668  1.00 31.10 ?  181 LYS B N     1 
ATOM   4182 C  CA    . LYS B 1 201 ? 44.820 -44.751 -8.857  1.00 27.77 ?  181 LYS B CA    1 
ATOM   4183 C  C     . LYS B 1 201 ? 44.578 -43.528 -7.982  1.00 31.82 ?  181 LYS B C     1 
ATOM   4184 O  O     . LYS B 1 201 ? 45.320 -43.332 -7.017  1.00 33.78 ?  181 LYS B O     1 
ATOM   4185 C  CB    . LYS B 1 201 ? 46.036 -44.485 -9.743  1.00 21.06 ?  181 LYS B CB    1 
ATOM   4186 C  CG    . LYS B 1 201 ? 46.729 -45.747 -10.176 1.00 29.85 ?  181 LYS B CG    1 
ATOM   4187 C  CD    . LYS B 1 201 ? 47.352 -45.614 -11.560 1.00 36.72 ?  181 LYS B CD    1 
ATOM   4188 C  CE    . LYS B 1 201 ? 48.584 -46.480 -11.675 1.00 39.40 ?  181 LYS B CE    1 
ATOM   4189 N  NZ    . LYS B 1 201 ? 48.511 -47.359 -12.867 1.00 41.87 ?  181 LYS B NZ    1 
ATOM   4190 N  N     . THR B 1 202 ? 43.582 -42.705 -8.261  1.00 31.37 ?  182 THR B N     1 
ATOM   4191 C  CA    . THR B 1 202 ? 43.443 -41.436 -7.552  1.00 31.85 ?  182 THR B CA    1 
ATOM   4192 C  C     . THR B 1 202 ? 42.235 -41.494 -6.628  1.00 24.68 ?  182 THR B C     1 
ATOM   4193 O  O     . THR B 1 202 ? 41.092 -41.594 -7.089  1.00 22.92 ?  182 THR B O     1 
ATOM   4194 C  CB    . THR B 1 202 ? 43.348 -40.274 -8.542  1.00 27.74 ?  182 THR B CB    1 
ATOM   4195 O  OG1   . THR B 1 202 ? 44.558 -40.229 -9.299  1.00 23.95 ?  182 THR B OG1   1 
ATOM   4196 C  CG2   . THR B 1 202 ? 43.188 -38.957 -7.815  1.00 24.07 ?  182 THR B CG2   1 
ATOM   4197 N  N     . ASP B 1 203 ? 42.496 -41.415 -5.326  1.00 32.58 ?  183 ASP B N     1 
ATOM   4198 C  CA    . ASP B 1 203 ? 41.426 -41.357 -4.336  1.00 25.49 ?  183 ASP B CA    1 
ATOM   4199 C  C     . ASP B 1 203 ? 40.836 -39.952 -4.280  1.00 24.60 ?  183 ASP B C     1 
ATOM   4200 O  O     . ASP B 1 203 ? 41.577 -38.984 -4.089  1.00 28.05 ?  183 ASP B O     1 
ATOM   4201 C  CB    . ASP B 1 203 ? 41.930 -41.749 -2.957  1.00 26.09 ?  183 ASP B CB    1 
ATOM   4202 C  CG    . ASP B 1 203 ? 40.897 -41.491 -1.883  1.00 24.44 ?  183 ASP B CG    1 
ATOM   4203 O  OD1   . ASP B 1 203 ? 39.945 -42.288 -1.760  1.00 24.00 ?  183 ASP B OD1   1 
ATOM   4204 O  OD2   . ASP B 1 203 ? 41.012 -40.463 -1.189  1.00 28.79 ?  183 ASP B OD2   1 
ATOM   4205 N  N     . PRO B 1 204 ? 39.517 -39.809 -4.427  1.00 25.40 ?  184 PRO B N     1 
ATOM   4206 C  CA    . PRO B 1 204 ? 38.915 -38.465 -4.446  1.00 27.24 ?  184 PRO B CA    1 
ATOM   4207 C  C     . PRO B 1 204 ? 39.342 -37.547 -3.311  1.00 30.92 ?  184 PRO B C     1 
ATOM   4208 O  O     . PRO B 1 204 ? 39.707 -36.388 -3.558  1.00 34.95 ?  184 PRO B O     1 
ATOM   4209 C  CB    . PRO B 1 204 ? 37.416 -38.777 -4.393  1.00 29.91 ?  184 PRO B CB    1 
ATOM   4210 C  CG    . PRO B 1 204 ? 37.291 -40.087 -5.129  1.00 27.65 ?  184 PRO B CG    1 
ATOM   4211 C  CD    . PRO B 1 204 ? 38.560 -40.857 -4.836  1.00 28.43 ?  184 PRO B CD    1 
ATOM   4212 N  N     . TYR B 1 205 ? 39.294 -38.034 -2.070  1.00 35.32 ?  185 TYR B N     1 
ATOM   4213 C  CA    . TYR B 1 205 ? 39.633 -37.204 -0.918  1.00 28.50 ?  185 TYR B CA    1 
ATOM   4214 C  C     . TYR B 1 205 ? 41.100 -36.787 -0.959  1.00 27.37 ?  185 TYR B C     1 
ATOM   4215 O  O     . TYR B 1 205 ? 41.424 -35.625 -0.694  1.00 28.16 ?  185 TYR B O     1 
ATOM   4216 C  CB    . TYR B 1 205 ? 39.290 -37.960 0.382   1.00 27.78 ?  185 TYR B CB    1 
ATOM   4217 C  CG    . TYR B 1 205 ? 39.596 -37.197 1.672   1.00 26.35 ?  185 TYR B CG    1 
ATOM   4218 C  CD1   . TYR B 1 205 ? 40.909 -37.054 2.116   1.00 23.67 ?  185 TYR B CD1   1 
ATOM   4219 C  CD2   . TYR B 1 205 ? 38.577 -36.631 2.440   1.00 23.11 ?  185 TYR B CD2   1 
ATOM   4220 C  CE1   . TYR B 1 205 ? 41.209 -36.357 3.261   1.00 34.38 ?  185 TYR B CE1   1 
ATOM   4221 C  CE2   . TYR B 1 205 ? 38.865 -35.926 3.598   1.00 24.04 ?  185 TYR B CE2   1 
ATOM   4222 C  CZ    . TYR B 1 205 ? 40.193 -35.800 4.008   1.00 34.11 ?  185 TYR B CZ    1 
ATOM   4223 O  OH    . TYR B 1 205 ? 40.544 -35.118 5.154   1.00 37.34 ?  185 TYR B OH    1 
ATOM   4224 N  N     . VAL B 1 206 ? 42.005 -37.719 -1.281  1.00 28.47 ?  186 VAL B N     1 
ATOM   4225 C  CA    . VAL B 1 206 ? 43.416 -37.356 -1.433  1.00 30.06 ?  186 VAL B CA    1 
ATOM   4226 C  C     . VAL B 1 206 ? 43.571 -36.257 -2.480  1.00 32.40 ?  186 VAL B C     1 
ATOM   4227 O  O     . VAL B 1 206 ? 44.313 -35.284 -2.277  1.00 28.79 ?  186 VAL B O     1 
ATOM   4228 C  CB    . VAL B 1 206 ? 44.266 -38.591 -1.791  1.00 27.47 ?  186 VAL B CB    1 
ATOM   4229 C  CG1   . VAL B 1 206 ? 45.738 -38.204 -1.909  1.00 27.01 ?  186 VAL B CG1   1 
ATOM   4230 C  CG2   . VAL B 1 206 ? 44.084 -39.692 -0.766  1.00 17.40 ?  186 VAL B CG2   1 
ATOM   4231 N  N     . PHE B 1 207 ? 42.863 -36.390 -3.613  1.00 28.15 ?  187 PHE B N     1 
ATOM   4232 C  CA    . PHE B 1 207 ? 42.957 -35.381 -4.663  1.00 30.98 ?  187 PHE B CA    1 
ATOM   4233 C  C     . PHE B 1 207 ? 42.602 -33.999 -4.126  1.00 29.32 ?  187 PHE B C     1 
ATOM   4234 O  O     . PHE B 1 207 ? 43.344 -33.030 -4.332  1.00 25.03 ?  187 PHE B O     1 
ATOM   4235 C  CB    . PHE B 1 207 ? 42.045 -35.722 -5.844  1.00 24.42 ?  187 PHE B CB    1 
ATOM   4236 C  CG    . PHE B 1 207 ? 41.849 -34.560 -6.787  1.00 27.12 ?  187 PHE B CG    1 
ATOM   4237 C  CD1   . PHE B 1 207 ? 42.759 -34.315 -7.804  1.00 24.99 ?  187 PHE B CD1   1 
ATOM   4238 C  CD2   . PHE B 1 207 ? 40.791 -33.672 -6.623  1.00 29.83 ?  187 PHE B CD2   1 
ATOM   4239 C  CE1   . PHE B 1 207 ? 42.602 -33.240 -8.657  1.00 21.55 ?  187 PHE B CE1   1 
ATOM   4240 C  CE2   . PHE B 1 207 ? 40.636 -32.581 -7.483  1.00 28.28 ?  187 PHE B CE2   1 
ATOM   4241 C  CZ    . PHE B 1 207 ? 41.543 -32.377 -8.503  1.00 19.83 ?  187 PHE B CZ    1 
ATOM   4242 N  N     . SER B 1 208 ? 41.440 -33.884 -3.473  1.00 29.40 ?  188 SER B N     1 
ATOM   4243 C  CA    . SER B 1 208 ? 40.977 -32.582 -3.013  1.00 29.18 ?  188 SER B CA    1 
ATOM   4244 C  C     . SER B 1 208 ? 41.936 -32.007 -1.989  1.00 24.79 ?  188 SER B C     1 
ATOM   4245 O  O     . SER B 1 208 ? 42.243 -30.814 -2.011  1.00 27.37 ?  188 SER B O     1 
ATOM   4246 C  CB    . SER B 1 208 ? 39.572 -32.697 -2.431  1.00 27.22 ?  188 SER B CB    1 
ATOM   4247 O  OG    . SER B 1 208 ? 38.678 -33.324 -3.352  1.00 28.87 ?  188 SER B OG    1 
ATOM   4248 N  N     . HIS B 1 209 ? 42.468 -32.850 -1.130  1.00 25.45 ?  189 HIS B N     1 
ATOM   4249 C  CA    . HIS B 1 209 ? 43.243 -32.341 -0.018  1.00 36.23 ?  189 HIS B CA    1 
ATOM   4250 C  C     . HIS B 1 209 ? 44.708 -32.145 -0.383  1.00 31.88 ?  189 HIS B C     1 
ATOM   4251 O  O     . HIS B 1 209 ? 45.328 -31.171 0.056   1.00 28.35 ?  189 HIS B O     1 
ATOM   4252 C  CB    . HIS B 1 209 ? 43.068 -33.287 1.184   1.00 30.23 ?  189 HIS B CB    1 
ATOM   4253 C  CG    . HIS B 1 209 ? 41.742 -33.133 1.870   1.00 31.37 ?  189 HIS B CG    1 
ATOM   4254 N  ND1   . HIS B 1 209 ? 41.610 -32.566 3.119   1.00 35.72 ?  189 HIS B ND1   1 
ATOM   4255 C  CD2   . HIS B 1 209 ? 40.483 -33.412 1.453   1.00 35.17 ?  189 HIS B CD2   1 
ATOM   4256 C  CE1   . HIS B 1 209 ? 40.331 -32.533 3.456   1.00 32.76 ?  189 HIS B CE1   1 
ATOM   4257 N  NE2   . HIS B 1 209 ? 39.624 -33.036 2.461   1.00 31.43 ?  189 HIS B NE2   1 
ATOM   4258 N  N     . GLU B 1 210 ? 45.271 -33.039 -1.195  1.00 27.12 ?  190 GLU B N     1 
ATOM   4259 C  CA    . GLU B 1 210 ? 46.700 -33.027 -1.461  1.00 29.64 ?  190 GLU B CA    1 
ATOM   4260 C  C     . GLU B 1 210 ? 47.082 -32.556 -2.852  1.00 31.84 ?  190 GLU B C     1 
ATOM   4261 O  O     . GLU B 1 210 ? 48.213 -32.092 -3.030  1.00 31.51 ?  190 GLU B O     1 
ATOM   4262 C  CB    . GLU B 1 210 ? 47.291 -34.428 -1.259  1.00 30.56 ?  190 GLU B CB    1 
ATOM   4263 C  CG    . GLU B 1 210 ? 46.946 -35.008 0.063   1.00 33.92 ?  190 GLU B CG    1 
ATOM   4264 C  CD    . GLU B 1 210 ? 47.425 -34.122 1.187   1.00 42.08 ?  190 GLU B CD    1 
ATOM   4265 O  OE1   . GLU B 1 210 ? 48.590 -33.650 1.135   1.00 33.99 ?  190 GLU B OE1   1 
ATOM   4266 O  OE2   . GLU B 1 210 ? 46.618 -33.883 2.110   1.00 52.79 ?  190 GLU B OE2   1 
ATOM   4267 N  N     . LEU B 1 211 ? 46.190 -32.679 -3.838  1.00 28.69 ?  191 LEU B N     1 
ATOM   4268 C  CA    . LEU B 1 211 ? 46.543 -32.469 -5.234  1.00 27.18 ?  191 LEU B CA    1 
ATOM   4269 C  C     . LEU B 1 211 ? 45.960 -31.182 -5.801  1.00 25.91 ?  191 LEU B C     1 
ATOM   4270 O  O     . LEU B 1 211 ? 46.720 -30.315 -6.242  1.00 27.75 ?  191 LEU B O     1 
ATOM   4271 C  CB    . LEU B 1 211 ? 46.099 -33.672 -6.065  1.00 28.42 ?  191 LEU B CB    1 
ATOM   4272 C  CG    . LEU B 1 211 ? 46.661 -35.024 -5.640  1.00 28.09 ?  191 LEU B CG    1 
ATOM   4273 C  CD1   . LEU B 1 211 ? 46.359 -36.043 -6.724  1.00 27.88 ?  191 LEU B CD1   1 
ATOM   4274 C  CD2   . LEU B 1 211 ? 48.151 -34.934 -5.365  1.00 23.62 ?  191 LEU B CD2   1 
ATOM   4275 N  N     . ARG B 1 212 ? 44.629 -31.032 -5.790  1.00 22.04 ?  192 ARG B N     1 
ATOM   4276 C  CA    . ARG B 1 212 ? 43.932 -29.848 -6.289  1.00 18.67 ?  192 ARG B CA    1 
ATOM   4277 C  C     . ARG B 1 212 ? 44.569 -28.505 -5.906  1.00 21.37 ?  192 ARG B C     1 
ATOM   4278 O  O     . ARG B 1 212 ? 44.545 -27.582 -6.725  1.00 25.35 ?  192 ARG B O     1 
ATOM   4279 C  CB    . ARG B 1 212 ? 42.475 -29.873 -5.835  1.00 16.88 ?  192 ARG B CB    1 
ATOM   4280 C  CG    . ARG B 1 212 ? 41.700 -28.599 -6.152  1.00 22.41 ?  192 ARG B CG    1 
ATOM   4281 C  CD    . ARG B 1 212 ? 41.362 -28.488 -7.639  1.00 23.11 ?  192 ARG B CD    1 
ATOM   4282 N  NE    . ARG B 1 212 ? 40.540 -27.323 -7.941  1.00 19.16 ?  192 ARG B NE    1 
ATOM   4283 C  CZ    . ARG B 1 212 ? 41.011 -26.095 -8.097  1.00 22.46 ?  192 ARG B CZ    1 
ATOM   4284 N  NH1   . ARG B 1 212 ? 42.301 -25.825 -7.955  1.00 23.37 ?  192 ARG B NH1   1 
ATOM   4285 N  NH2   . ARG B 1 212 ? 40.166 -25.107 -8.379  1.00 21.36 ?  192 ARG B NH2   1 
ATOM   4286 N  N     . PRO B 1 213 ? 45.149 -28.322 -4.711  1.00 26.02 ?  193 PRO B N     1 
ATOM   4287 C  CA    . PRO B 1 213 ? 45.755 -27.013 -4.407  1.00 26.19 ?  193 PRO B CA    1 
ATOM   4288 C  C     . PRO B 1 213 ? 46.935 -26.643 -5.296  1.00 30.62 ?  193 PRO B C     1 
ATOM   4289 O  O     . PRO B 1 213 ? 47.375 -25.485 -5.249  1.00 27.97 ?  193 PRO B O     1 
ATOM   4290 C  CB    . PRO B 1 213 ? 46.194 -27.158 -2.947  1.00 22.29 ?  193 PRO B CB    1 
ATOM   4291 C  CG    . PRO B 1 213 ? 45.299 -28.191 -2.398  1.00 23.71 ?  193 PRO B CG    1 
ATOM   4292 C  CD    . PRO B 1 213 ? 45.064 -29.154 -3.491  1.00 24.86 ?  193 PRO B CD    1 
ATOM   4293 N  N     . PHE B 1 214 ? 47.464 -27.574 -6.088  1.00 25.92 ?  194 PHE B N     1 
ATOM   4294 C  CA    . PHE B 1 214 ? 48.609 -27.291 -6.939  1.00 25.82 ?  194 PHE B CA    1 
ATOM   4295 C  C     . PHE B 1 214 ? 48.222 -26.798 -8.325  1.00 25.61 ?  194 PHE B C     1 
ATOM   4296 O  O     . PHE B 1 214 ? 49.106 -26.534 -9.137  1.00 24.58 ?  194 PHE B O     1 
ATOM   4297 C  CB    . PHE B 1 214 ? 49.485 -28.530 -7.069  1.00 25.42 ?  194 PHE B CB    1 
ATOM   4298 C  CG    . PHE B 1 214 ? 50.350 -28.768 -5.878  1.00 26.60 ?  194 PHE B CG    1 
ATOM   4299 C  CD1   . PHE B 1 214 ? 51.508 -28.030 -5.689  1.00 24.04 ?  194 PHE B CD1   1 
ATOM   4300 C  CD2   . PHE B 1 214 ? 50.000 -29.720 -4.932  1.00 26.67 ?  194 PHE B CD2   1 
ATOM   4301 C  CE1   . PHE B 1 214 ? 52.315 -28.249 -4.577  1.00 25.11 ?  194 PHE B CE1   1 
ATOM   4302 C  CE2   . PHE B 1 214 ? 50.800 -29.944 -3.820  1.00 27.43 ?  194 PHE B CE2   1 
ATOM   4303 C  CZ    . PHE B 1 214 ? 51.957 -29.205 -3.644  1.00 25.79 ?  194 PHE B CZ    1 
ATOM   4304 N  N     . PHE B 1 215 ? 46.940 -26.619 -8.592  1.00 26.08 ?  195 PHE B N     1 
ATOM   4305 C  CA    . PHE B 1 215 ? 46.442 -26.272 -9.909  1.00 25.30 ?  195 PHE B CA    1 
ATOM   4306 C  C     . PHE B 1 215 ? 45.623 -24.986 -9.869  1.00 25.27 ?  195 PHE B C     1 
ATOM   4307 O  O     . PHE B 1 215 ? 44.591 -24.865 -10.534 1.00 28.07 ?  195 PHE B O     1 
ATOM   4308 C  CB    . PHE B 1 215 ? 45.635 -27.439 -10.473 1.00 22.19 ?  195 PHE B CB    1 
ATOM   4309 C  CG    . PHE B 1 215 ? 46.378 -28.747 -10.419 1.00 23.55 ?  195 PHE B CG    1 
ATOM   4310 C  CD1   . PHE B 1 215 ? 47.345 -29.050 -11.363 1.00 22.29 ?  195 PHE B CD1   1 
ATOM   4311 C  CD2   . PHE B 1 215 ? 46.138 -29.663 -9.394  1.00 26.68 ?  195 PHE B CD2   1 
ATOM   4312 C  CE1   . PHE B 1 215 ? 48.049 -30.250 -11.302 1.00 26.26 ?  195 PHE B CE1   1 
ATOM   4313 C  CE2   . PHE B 1 215 ? 46.830 -30.854 -9.327  1.00 21.07 ?  195 PHE B CE2   1 
ATOM   4314 C  CZ    . PHE B 1 215 ? 47.787 -31.155 -10.284 1.00 23.57 ?  195 PHE B CZ    1 
ATOM   4315 N  N     . ASP B 1 216 ? 46.087 -24.005 -9.100  1.00 25.45 ?  196 ASP B N     1 
ATOM   4316 C  CA    . ASP B 1 216 ? 45.409 -22.734 -8.859  1.00 23.36 ?  196 ASP B CA    1 
ATOM   4317 C  C     . ASP B 1 216 ? 45.938 -21.635 -9.786  1.00 23.72 ?  196 ASP B C     1 
ATOM   4318 O  O     . ASP B 1 216 ? 47.067 -21.709 -10.285 1.00 16.42 ?  196 ASP B O     1 
ATOM   4319 C  CB    . ASP B 1 216 ? 45.592 -22.311 -7.395  1.00 24.20 ?  196 ASP B CB    1 
ATOM   4320 C  CG    . ASP B 1 216 ? 44.587 -22.983 -6.436  1.00 32.74 ?  196 ASP B CG    1 
ATOM   4321 O  OD1   . ASP B 1 216 ? 43.459 -23.316 -6.861  1.00 27.70 ?  196 ASP B OD1   1 
ATOM   4322 O  OD2   . ASP B 1 216 ? 44.940 -23.169 -5.240  1.00 36.24 ?  196 ASP B OD2   1 
ATOM   4323 N  N     . PRO B 1 217 ? 45.148 -20.582 -10.018 1.00 28.36 ?  197 PRO B N     1 
ATOM   4324 C  CA    . PRO B 1 217 ? 45.541 -19.560 -11.005 1.00 29.27 ?  197 PRO B CA    1 
ATOM   4325 C  C     . PRO B 1 217 ? 46.781 -18.776 -10.598 1.00 21.95 ?  197 PRO B C     1 
ATOM   4326 O  O     . PRO B 1 217 ? 47.070 -18.589 -9.419  1.00 28.74 ?  197 PRO B O     1 
ATOM   4327 C  CB    . PRO B 1 217 ? 44.313 -18.645 -11.078 1.00 26.02 ?  197 PRO B CB    1 
ATOM   4328 C  CG    . PRO B 1 217 ? 43.183 -19.472 -10.513 1.00 22.24 ?  197 PRO B CG    1 
ATOM   4329 C  CD    . PRO B 1 217 ? 43.784 -20.363 -9.502  1.00 22.31 ?  197 PRO B CD    1 
ATOM   4330 N  N     . ILE B 1 218 ? 47.516 -18.302 -11.599 1.00 23.57 ?  198 ILE B N     1 
ATOM   4331 C  CA    . ILE B 1 218 ? 48.748 -17.553 -11.383 1.00 26.50 ?  198 ILE B CA    1 
ATOM   4332 C  C     . ILE B 1 218 ? 48.700 -16.259 -12.195 1.00 29.62 ?  198 ILE B C     1 
ATOM   4333 O  O     . ILE B 1 218 ? 48.445 -16.287 -13.411 1.00 20.80 ?  198 ILE B O     1 
ATOM   4334 C  CB    . ILE B 1 218 ? 49.993 -18.383 -11.754 1.00 25.53 ?  198 ILE B CB    1 
ATOM   4335 C  CG1   . ILE B 1 218 ? 50.230 -19.490 -10.726 1.00 22.35 ?  198 ILE B CG1   1 
ATOM   4336 C  CG2   . ILE B 1 218 ? 51.218 -17.490 -11.831 1.00 26.24 ?  198 ILE B CG2   1 
ATOM   4337 C  CD1   . ILE B 1 218 ? 51.535 -20.220 -10.931 1.00 18.71 ?  198 ILE B CD1   1 
ATOM   4338 N  N     . ARG B 1 219 ? 48.972 -15.130 -11.523 1.00 29.58 ?  199 ARG B N     1 
ATOM   4339 C  CA    . ARG B 1 219 ? 48.968 -13.816 -12.165 1.00 30.81 ?  199 ARG B CA    1 
ATOM   4340 C  C     . ARG B 1 219 ? 50.313 -13.543 -12.825 1.00 27.84 ?  199 ARG B C     1 
ATOM   4341 O  O     . ARG B 1 219 ? 51.345 -13.477 -12.148 1.00 25.31 ?  199 ARG B O     1 
ATOM   4342 C  CB    . ARG B 1 219 ? 48.633 -12.702 -11.174 1.00 26.52 ?  199 ARG B CB    1 
ATOM   4343 C  CG    . ARG B 1 219 ? 47.842 -11.553 -11.816 1.00 42.82 ?  199 ARG B CG    1 
ATOM   4344 C  CD    . ARG B 1 219 ? 46.323 -11.796 -11.752 1.00 48.00 ?  199 ARG B CD    1 
ATOM   4345 N  NE    . ARG B 1 219 ? 45.527 -10.762 -12.418 1.00 49.21 ?  199 ARG B NE    1 
ATOM   4346 C  CZ    . ARG B 1 219 ? 44.197 -10.764 -12.470 1.00 60.70 ?  199 ARG B CZ    1 
ATOM   4347 N  NH1   . ARG B 1 219 ? 43.479 -11.678 -11.826 1.00 63.84 ?  199 ARG B NH1   1 
ATOM   4348 N  NH2   . ARG B 1 219 ? 43.569 -9.831  -13.189 1.00 46.30 ?  199 ARG B NH2   1 
ATOM   4349 N  N     . ILE B 1 220 ? 50.287 -13.367 -14.146 1.00 27.33 ?  200 ILE B N     1 
ATOM   4350 C  CA    . ILE B 1 220 ? 51.476 -13.118 -14.961 1.00 31.72 ?  200 ILE B CA    1 
ATOM   4351 C  C     . ILE B 1 220 ? 51.149 -11.977 -15.914 1.00 35.93 ?  200 ILE B C     1 
ATOM   4352 O  O     . ILE B 1 220 ? 50.160 -12.048 -16.658 1.00 38.02 ?  200 ILE B O     1 
ATOM   4353 C  CB    . ILE B 1 220 ? 51.920 -14.368 -15.750 1.00 29.95 ?  200 ILE B CB    1 
ATOM   4354 C  CG1   . ILE B 1 220 ? 52.066 -15.584 -14.826 1.00 23.85 ?  200 ILE B CG1   1 
ATOM   4355 C  CG2   . ILE B 1 220 ? 53.209 -14.110 -16.482 1.00 26.13 ?  200 ILE B CG2   1 
ATOM   4356 C  CD1   . ILE B 1 220 ? 52.211 -16.895 -15.573 1.00 24.98 ?  200 ILE B CD1   1 
ATOM   4357 N  N     . GLY B 1 221 ? 51.968 -10.929 -15.891 1.00 38.56 ?  201 GLY B N     1 
ATOM   4358 C  CA    . GLY B 1 221 ? 51.739 -9.766  -16.723 1.00 43.14 ?  201 GLY B CA    1 
ATOM   4359 C  C     . GLY B 1 221 ? 50.305 -9.258  -16.775 1.00 47.69 ?  201 GLY B C     1 
ATOM   4360 O  O     . GLY B 1 221 ? 49.774 -8.991  -17.864 1.00 51.18 ?  201 GLY B O     1 
ATOM   4361 N  N     . GLY B 1 222 ? 49.659 -9.123  -15.618 1.00 28.79 ?  202 GLY B N     1 
ATOM   4362 C  CA    . GLY B 1 222 ? 48.341 -8.525  -15.576 1.00 34.31 ?  202 GLY B CA    1 
ATOM   4363 C  C     . GLY B 1 222 ? 47.204 -9.400  -16.056 1.00 42.59 ?  202 GLY B C     1 
ATOM   4364 O  O     . GLY B 1 222 ? 46.063 -8.919  -16.133 1.00 33.70 ?  202 GLY B O     1 
ATOM   4365 N  N     . LYS B 1 223 ? 47.469 -10.659 -16.396 1.00 34.83 ?  203 LYS B N     1 
ATOM   4366 C  CA    . LYS B 1 223 ? 46.418 -11.610 -16.708 1.00 29.87 ?  203 LYS B CA    1 
ATOM   4367 C  C     . LYS B 1 223 ? 46.569 -12.798 -15.763 1.00 32.57 ?  203 LYS B C     1 
ATOM   4368 O  O     . LYS B 1 223 ? 47.637 -13.047 -15.191 1.00 28.29 ?  203 LYS B O     1 
ATOM   4369 C  CB    . LYS B 1 223 ? 46.461 -12.014 -18.202 1.00 38.08 ?  203 LYS B CB    1 
ATOM   4370 C  CG    . LYS B 1 223 ? 45.881 -13.381 -18.602 1.00 38.92 ?  203 LYS B CG    1 
ATOM   4371 C  CD    . LYS B 1 223 ? 46.053 -13.667 -20.114 1.00 46.81 ?  203 LYS B CD    1 
ATOM   4372 C  CE    . LYS B 1 223 ? 44.739 -14.124 -20.796 1.00 66.30 ?  203 LYS B CE    1 
ATOM   4373 N  NZ    . LYS B 1 223 ? 44.882 -15.092 -21.947 1.00 54.13 ?  203 LYS B NZ    1 
ATOM   4374 N  N     . SER B 1 224 ? 45.471 -13.499 -15.548 1.00 33.61 ?  204 SER B N     1 
ATOM   4375 C  CA    . SER B 1 224 ? 45.458 -14.659 -14.677 1.00 36.57 ?  204 SER B CA    1 
ATOM   4376 C  C     . SER B 1 224 ? 45.367 -15.926 -15.533 1.00 32.26 ?  204 SER B C     1 
ATOM   4377 O  O     . SER B 1 224 ? 44.519 -16.019 -16.427 1.00 34.69 ?  204 SER B O     1 
ATOM   4378 C  CB    . SER B 1 224 ? 44.298 -14.546 -13.684 1.00 24.72 ?  204 SER B CB    1 
ATOM   4379 O  OG    . SER B 1 224 ? 44.208 -15.707 -12.889 1.00 43.66 ?  204 SER B OG    1 
ATOM   4380 N  N     . TYR B 1 225 ? 46.250 -16.889 -15.271 1.00 24.30 ?  205 TYR B N     1 
ATOM   4381 C  CA    . TYR B 1 225 ? 46.300 -18.141 -16.017 1.00 25.23 ?  205 TYR B CA    1 
ATOM   4382 C  C     . TYR B 1 225 ? 45.902 -19.310 -15.129 1.00 23.17 ?  205 TYR B C     1 
ATOM   4383 O  O     . TYR B 1 225 ? 46.571 -19.593 -14.130 1.00 24.75 ?  205 TYR B O     1 
ATOM   4384 C  CB    . TYR B 1 225 ? 47.692 -18.364 -16.593 1.00 26.48 ?  205 TYR B CB    1 
ATOM   4385 C  CG    . TYR B 1 225 ? 48.087 -17.292 -17.578 1.00 28.00 ?  205 TYR B CG    1 
ATOM   4386 C  CD1   . TYR B 1 225 ? 48.629 -16.080 -17.143 1.00 29.17 ?  205 TYR B CD1   1 
ATOM   4387 C  CD2   . TYR B 1 225 ? 47.883 -17.472 -18.942 1.00 29.18 ?  205 TYR B CD2   1 
ATOM   4388 C  CE1   . TYR B 1 225 ? 48.981 -15.098 -18.034 1.00 25.73 ?  205 TYR B CE1   1 
ATOM   4389 C  CE2   . TYR B 1 225 ? 48.236 -16.493 -19.844 1.00 29.14 ?  205 TYR B CE2   1 
ATOM   4390 C  CZ    . TYR B 1 225 ? 48.791 -15.318 -19.386 1.00 28.63 ?  205 TYR B CZ    1 
ATOM   4391 O  OH    . TYR B 1 225 ? 49.142 -14.354 -20.286 1.00 30.80 ?  205 TYR B OH    1 
ATOM   4392 N  N     . ILE B 1 226 ? 44.815 -19.989 -15.497 1.00 19.71 ?  206 ILE B N     1 
ATOM   4393 C  CA    . ILE B 1 226 ? 44.422 -21.177 -14.758 1.00 19.16 ?  206 ILE B CA    1 
ATOM   4394 C  C     . ILE B 1 226 ? 45.545 -22.217 -14.752 1.00 21.01 ?  206 ILE B C     1 
ATOM   4395 O  O     . ILE B 1 226 ? 46.412 -22.255 -15.635 1.00 21.73 ?  206 ILE B O     1 
ATOM   4396 C  CB    . ILE B 1 226 ? 43.130 -21.772 -15.334 1.00 18.81 ?  206 ILE B CB    1 
ATOM   4397 C  CG1   . ILE B 1 226 ? 43.345 -22.291 -16.758 1.00 21.71 ?  206 ILE B CG1   1 
ATOM   4398 C  CG2   . ILE B 1 226 ? 42.050 -20.738 -15.344 1.00 17.98 ?  206 ILE B CG2   1 
ATOM   4399 C  CD1   . ILE B 1 226 ? 42.153 -23.062 -17.267 1.00 16.58 ?  206 ILE B CD1   1 
ATOM   4400 N  N     . GLY B 1 227 ? 45.522 -23.078 -13.727 1.00 23.06 ?  207 GLY B N     1 
ATOM   4401 C  CA    . GLY B 1 227 ? 46.442 -24.195 -13.670 1.00 19.92 ?  207 GLY B CA    1 
ATOM   4402 C  C     . GLY B 1 227 ? 46.032 -25.344 -14.582 1.00 21.44 ?  207 GLY B C     1 
ATOM   4403 O  O     . GLY B 1 227 ? 44.950 -25.340 -15.175 1.00 19.17 ?  207 GLY B O     1 
ATOM   4404 N  N     . ALA B 1 228 ? 46.923 -26.336 -14.683 1.00 22.09 ?  208 ALA B N     1 
ATOM   4405 C  CA    . ALA B 1 228 ? 46.666 -27.513 -15.508 1.00 20.41 ?  208 ALA B CA    1 
ATOM   4406 C  C     . ALA B 1 228 ? 45.373 -28.208 -15.084 1.00 24.79 ?  208 ALA B C     1 
ATOM   4407 O  O     . ALA B 1 228 ? 44.971 -28.176 -13.916 1.00 22.04 ?  208 ALA B O     1 
ATOM   4408 C  CB    . ALA B 1 228 ? 47.833 -28.495 -15.425 1.00 16.44 ?  208 ALA B CB    1 
ATOM   4409 N  N     . GLY B 1 229 ? 44.706 -28.819 -16.056 1.00 19.18 ?  209 GLY B N     1 
ATOM   4410 C  CA    . GLY B 1 229 ? 43.425 -29.450 -15.814 1.00 19.59 ?  209 GLY B CA    1 
ATOM   4411 C  C     . GLY B 1 229 ? 43.186 -30.556 -16.818 1.00 23.52 ?  209 GLY B C     1 
ATOM   4412 O  O     . GLY B 1 229 ? 43.772 -30.573 -17.908 1.00 19.09 ?  209 GLY B O     1 
ATOM   4413 N  N     . GLY B 1 230 ? 42.312 -31.493 -16.430 1.00 19.31 ?  210 GLY B N     1 
ATOM   4414 C  CA    . GLY B 1 230 ? 41.890 -32.529 -17.359 1.00 18.73 ?  210 GLY B CA    1 
ATOM   4415 C  C     . GLY B 1 230 ? 41.281 -31.954 -18.621 1.00 19.81 ?  210 GLY B C     1 
ATOM   4416 O  O     . GLY B 1 230 ? 41.601 -32.391 -19.731 1.00 16.77 ?  210 GLY B O     1 
ATOM   4417 N  N     . GLY B 1 231 ? 40.424 -30.938 -18.468 1.00 19.63 ?  211 GLY B N     1 
ATOM   4418 C  CA    . GLY B 1 231 ? 39.787 -30.251 -19.585 1.00 21.57 ?  211 GLY B CA    1 
ATOM   4419 C  C     . GLY B 1 231 ? 40.750 -29.659 -20.617 1.00 25.24 ?  211 GLY B C     1 
ATOM   4420 O  O     . GLY B 1 231 ? 40.296 -29.197 -21.674 1.00 17.58 ?  211 GLY B O     1 
ATOM   4421 N  N     . GLN B 1 232 ? 42.055 -29.651 -20.338 1.00 22.65 ?  212 GLN B N     1 
ATOM   4422 C  CA    . GLN B 1 232 ? 43.023 -29.191 -21.327 1.00 21.18 ?  212 GLN B CA    1 
ATOM   4423 C  C     . GLN B 1 232 ? 43.429 -30.265 -22.331 1.00 20.09 ?  212 GLN B C     1 
ATOM   4424 O  O     . GLN B 1 232 ? 44.064 -29.929 -23.337 1.00 24.55 ?  212 GLN B O     1 
ATOM   4425 C  CB    . GLN B 1 232 ? 44.267 -28.630 -20.627 1.00 20.01 ?  212 GLN B CB    1 
ATOM   4426 C  CG    . GLN B 1 232 ? 43.934 -27.531 -19.646 1.00 19.61 ?  212 GLN B CG    1 
ATOM   4427 C  CD    . GLN B 1 232 ? 45.156 -26.972 -18.996 1.00 25.17 ?  212 GLN B CD    1 
ATOM   4428 O  OE1   . GLN B 1 232 ? 46.064 -27.717 -18.638 1.00 26.64 ?  212 GLN B OE1   1 
ATOM   4429 N  NE2   . GLN B 1 232 ? 45.212 -25.644 -18.860 1.00 26.84 ?  212 GLN B NE2   1 
ATOM   4430 N  N     . ILE B 1 233 ? 43.088 -31.532 -22.099 1.00 22.37 ?  213 ILE B N     1 
ATOM   4431 C  CA    . ILE B 1 233 ? 43.228 -32.471 -23.219 1.00 19.83 ?  213 ILE B CA    1 
ATOM   4432 C  C     . ILE B 1 233 ? 42.313 -32.007 -24.338 1.00 21.55 ?  213 ILE B C     1 
ATOM   4433 O  O     . ILE B 1 233 ? 41.214 -31.484 -24.059 1.00 21.14 ?  213 ILE B O     1 
ATOM   4434 C  CB    . ILE B 1 233 ? 42.904 -33.926 -22.802 1.00 24.41 ?  213 ILE B CB    1 
ATOM   4435 C  CG1   . ILE B 1 233 ? 41.401 -34.143 -22.584 1.00 20.44 ?  213 ILE B CG1   1 
ATOM   4436 C  CG2   . ILE B 1 233 ? 43.698 -34.357 -21.571 1.00 21.20 ?  213 ILE B CG2   1 
ATOM   4437 C  CD1   . ILE B 1 233 ? 41.037 -35.501 -22.092 1.00 24.46 ?  213 ILE B CD1   1 
ATOM   4438 N  N     . PRO B 1 234 ? 42.711 -32.134 -25.608 1.00 21.86 ?  214 PRO B N     1 
ATOM   4439 C  CA    . PRO B 1 234 ? 41.977 -31.463 -26.688 1.00 17.72 ?  214 PRO B CA    1 
ATOM   4440 C  C     . PRO B 1 234 ? 40.708 -32.193 -27.101 1.00 24.75 ?  214 PRO B C     1 
ATOM   4441 O  O     . PRO B 1 234 ? 40.330 -32.219 -28.283 1.00 30.71 ?  214 PRO B O     1 
ATOM   4442 C  CB    . PRO B 1 234 ? 43.008 -31.420 -27.821 1.00 19.27 ?  214 PRO B CB    1 
ATOM   4443 C  CG    . PRO B 1 234 ? 43.856 -32.594 -27.596 1.00 17.68 ?  214 PRO B CG    1 
ATOM   4444 C  CD    . PRO B 1 234 ? 43.924 -32.808 -26.096 1.00 25.29 ?  214 PRO B CD    1 
ATOM   4445 N  N     . LEU B 1 235 ? 40.044 -32.801 -26.117 1.00 22.04 ?  215 LEU B N     1 
ATOM   4446 C  CA    . LEU B 1 235 ? 38.791 -33.484 -26.389 1.00 20.20 ?  215 LEU B CA    1 
ATOM   4447 C  C     . LEU B 1 235 ? 37.753 -32.514 -26.937 1.00 21.47 ?  215 LEU B C     1 
ATOM   4448 O  O     . LEU B 1 235 ? 37.041 -32.834 -27.892 1.00 29.23 ?  215 LEU B O     1 
ATOM   4449 C  CB    . LEU B 1 235 ? 38.287 -34.176 -25.125 1.00 16.17 ?  215 LEU B CB    1 
ATOM   4450 C  CG    . LEU B 1 235 ? 37.138 -35.147 -25.381 1.00 21.39 ?  215 LEU B CG    1 
ATOM   4451 C  CD1   . LEU B 1 235 ? 37.565 -36.265 -26.332 1.00 21.00 ?  215 LEU B CD1   1 
ATOM   4452 C  CD2   . LEU B 1 235 ? 36.636 -35.729 -24.079 1.00 22.51 ?  215 LEU B CD2   1 
ATOM   4453 N  N     . PHE B 1 236 ? 37.670 -31.315 -26.364 1.00 23.88 ?  216 PHE B N     1 
ATOM   4454 C  CA    . PHE B 1 236 ? 36.708 -30.335 -26.845 1.00 24.10 ?  216 PHE B CA    1 
ATOM   4455 C  C     . PHE B 1 236 ? 36.949 -30.010 -28.317 1.00 24.43 ?  216 PHE B C     1 
ATOM   4456 O  O     . PHE B 1 236 ? 36.008 -29.652 -29.031 1.00 28.53 ?  216 PHE B O     1 
ATOM   4457 C  CB    . PHE B 1 236 ? 36.746 -29.069 -25.958 1.00 22.78 ?  216 PHE B CB    1 
ATOM   4458 C  CG    . PHE B 1 236 ? 37.997 -28.226 -26.123 1.00 25.31 ?  216 PHE B CG    1 
ATOM   4459 C  CD1   . PHE B 1 236 ? 38.130 -27.335 -27.205 1.00 21.96 ?  216 PHE B CD1   1 
ATOM   4460 C  CD2   . PHE B 1 236 ? 39.045 -28.333 -25.211 1.00 19.76 ?  216 PHE B CD2   1 
ATOM   4461 C  CE1   . PHE B 1 236 ? 39.286 -26.572 -27.372 1.00 22.89 ?  216 PHE B CE1   1 
ATOM   4462 C  CE2   . PHE B 1 236 ? 40.203 -27.575 -25.361 1.00 23.48 ?  216 PHE B CE2   1 
ATOM   4463 C  CZ    . PHE B 1 236 ? 40.323 -26.681 -26.445 1.00 28.14 ?  216 PHE B CZ    1 
ATOM   4464 N  N     . VAL B 1 237 ? 38.189 -30.152 -28.798 1.00 25.54 ?  217 VAL B N     1 
ATOM   4465 C  CA    . VAL B 1 237 ? 38.442 -29.987 -30.227 1.00 22.57 ?  217 VAL B CA    1 
ATOM   4466 C  C     . VAL B 1 237 ? 37.748 -31.092 -31.025 1.00 25.16 ?  217 VAL B C     1 
ATOM   4467 O  O     . VAL B 1 237 ? 37.144 -30.822 -32.073 1.00 27.81 ?  217 VAL B O     1 
ATOM   4468 C  CB    . VAL B 1 237 ? 39.955 -29.933 -30.509 1.00 26.31 ?  217 VAL B CB    1 
ATOM   4469 C  CG1   . VAL B 1 237 ? 40.236 -29.626 -32.004 1.00 21.51 ?  217 VAL B CG1   1 
ATOM   4470 C  CG2   . VAL B 1 237 ? 40.602 -28.902 -29.634 1.00 23.18 ?  217 VAL B CG2   1 
ATOM   4471 N  N     . VAL B 1 238 ? 37.819 -32.349 -30.550 1.00 18.91 ?  218 VAL B N     1 
ATOM   4472 C  CA    . VAL B 1 238 ? 36.977 -33.402 -31.119 1.00 19.56 ?  218 VAL B CA    1 
ATOM   4473 C  C     . VAL B 1 238 ? 35.506 -32.975 -31.123 1.00 24.50 ?  218 VAL B C     1 
ATOM   4474 O  O     . VAL B 1 238 ? 34.785 -33.181 -32.105 1.00 19.00 ?  218 VAL B O     1 
ATOM   4475 C  CB    . VAL B 1 238 ? 37.183 -34.734 -30.363 1.00 27.29 ?  218 VAL B CB    1 
ATOM   4476 C  CG1   . VAL B 1 238 ? 36.078 -35.744 -30.714 1.00 22.04 ?  218 VAL B CG1   1 
ATOM   4477 C  CG2   . VAL B 1 238 ? 38.552 -35.355 -30.666 1.00 21.70 ?  218 VAL B CG2   1 
ATOM   4478 N  N     . ASP B 1 239 ? 35.041 -32.351 -30.036 1.00 27.05 ?  219 ASP B N     1 
ATOM   4479 C  CA    . ASP B 1 239 ? 33.621 -32.013 -29.926 1.00 27.70 ?  219 ASP B CA    1 
ATOM   4480 C  C     . ASP B 1 239 ? 33.197 -31.033 -31.005 1.00 31.07 ?  219 ASP B C     1 
ATOM   4481 O  O     . ASP B 1 239 ? 32.229 -31.273 -31.741 1.00 31.04 ?  219 ASP B O     1 
ATOM   4482 C  CB    . ASP B 1 239 ? 33.309 -31.423 -28.551 1.00 29.01 ?  219 ASP B CB    1 
ATOM   4483 C  CG    . ASP B 1 239 ? 33.168 -32.483 -27.485 1.00 34.09 ?  219 ASP B CG    1 
ATOM   4484 O  OD1   . ASP B 1 239 ? 32.624 -33.563 -27.810 1.00 25.95 ?  219 ASP B OD1   1 
ATOM   4485 O  OD2   . ASP B 1 239 ? 33.617 -32.233 -26.336 1.00 31.86 ?  219 ASP B OD2   1 
ATOM   4486 N  N     . VAL B 1 240 ? 33.907 -29.910 -31.102 1.00 29.04 ?  220 VAL B N     1 
ATOM   4487 C  CA    . VAL B 1 240 ? 33.480 -28.838 -31.988 1.00 28.94 ?  220 VAL B CA    1 
ATOM   4488 C  C     . VAL B 1 240 ? 33.454 -29.318 -33.437 1.00 27.82 ?  220 VAL B C     1 
ATOM   4489 O  O     . VAL B 1 240 ? 32.495 -29.057 -34.170 1.00 29.78 ?  220 VAL B O     1 
ATOM   4490 C  CB    . VAL B 1 240 ? 34.387 -27.610 -31.786 1.00 30.46 ?  220 VAL B CB    1 
ATOM   4491 C  CG1   . VAL B 1 240 ? 34.115 -27.000 -30.444 1.00 27.48 ?  220 VAL B CG1   1 
ATOM   4492 C  CG2   . VAL B 1 240 ? 35.844 -28.004 -31.852 1.00 29.32 ?  220 VAL B CG2   1 
ATOM   4493 N  N     . LYS B 1 241 ? 34.490 -30.045 -33.865 1.00 25.46 ?  221 LYS B N     1 
ATOM   4494 C  CA    . LYS B 1 241 ? 34.492 -30.622 -35.206 1.00 30.64 ?  221 LYS B CA    1 
ATOM   4495 C  C     . LYS B 1 241 ? 33.337 -31.610 -35.402 1.00 34.77 ?  221 LYS B C     1 
ATOM   4496 O  O     . LYS B 1 241 ? 32.600 -31.535 -36.395 1.00 29.12 ?  221 LYS B O     1 
ATOM   4497 C  CB    . LYS B 1 241 ? 35.830 -31.305 -35.467 1.00 27.86 ?  221 LYS B CB    1 
ATOM   4498 C  CG    . LYS B 1 241 ? 36.034 -31.698 -36.926 1.00 34.70 ?  221 LYS B CG    1 
ATOM   4499 C  CD    . LYS B 1 241 ? 36.746 -30.588 -37.699 1.00 39.71 ?  221 LYS B CD    1 
ATOM   4500 C  CE    . LYS B 1 241 ? 36.823 -30.912 -39.187 1.00 45.93 ?  221 LYS B CE    1 
ATOM   4501 N  NZ    . LYS B 1 241 ? 36.350 -29.785 -40.046 1.00 45.99 ?  221 LYS B NZ    1 
ATOM   4502 N  N     . LEU B 1 242 ? 33.141 -32.523 -34.440 1.00 29.71 ?  222 LEU B N     1 
ATOM   4503 C  CA    . LEU B 1 242 ? 32.247 -33.656 -34.641 1.00 22.13 ?  222 LEU B CA    1 
ATOM   4504 C  C     . LEU B 1 242 ? 30.774 -33.291 -34.447 1.00 27.85 ?  222 LEU B C     1 
ATOM   4505 O  O     . LEU B 1 242 ? 29.930 -33.673 -35.265 1.00 31.34 ?  222 LEU B O     1 
ATOM   4506 C  CB    . LEU B 1 242 ? 32.656 -34.801 -33.719 1.00 21.79 ?  222 LEU B CB    1 
ATOM   4507 C  CG    . LEU B 1 242 ? 31.812 -36.076 -33.708 1.00 27.14 ?  222 LEU B CG    1 
ATOM   4508 C  CD1   . LEU B 1 242 ? 31.969 -36.907 -34.974 1.00 30.04 ?  222 LEU B CD1   1 
ATOM   4509 C  CD2   . LEU B 1 242 ? 32.176 -36.899 -32.501 1.00 28.91 ?  222 LEU B CD2   1 
ATOM   4510 N  N     . TRP B 1 243 ? 30.422 -32.573 -33.377 1.00 26.65 ?  223 TRP B N     1 
ATOM   4511 C  CA    . TRP B 1 243 ? 28.997 -32.334 -33.152 1.00 24.20 ?  223 TRP B CA    1 
ATOM   4512 C  C     . TRP B 1 243 ? 28.639 -30.913 -32.744 1.00 30.20 ?  223 TRP B C     1 
ATOM   4513 O  O     . TRP B 1 243 ? 27.520 -30.482 -33.037 1.00 31.76 ?  223 TRP B O     1 
ATOM   4514 C  CB    . TRP B 1 243 ? 28.432 -33.302 -32.095 1.00 28.36 ?  223 TRP B CB    1 
ATOM   4515 C  CG    . TRP B 1 243 ? 29.106 -33.245 -30.753 1.00 24.86 ?  223 TRP B CG    1 
ATOM   4516 C  CD1   . TRP B 1 243 ? 30.154 -34.010 -30.335 1.00 25.15 ?  223 TRP B CD1   1 
ATOM   4517 C  CD2   . TRP B 1 243 ? 28.777 -32.382 -29.652 1.00 27.24 ?  223 TRP B CD2   1 
ATOM   4518 N  NE1   . TRP B 1 243 ? 30.498 -33.684 -29.041 1.00 25.25 ?  223 TRP B NE1   1 
ATOM   4519 C  CE2   . TRP B 1 243 ? 29.669 -32.687 -28.600 1.00 27.82 ?  223 TRP B CE2   1 
ATOM   4520 C  CE3   . TRP B 1 243 ? 27.808 -31.394 -29.447 1.00 29.91 ?  223 TRP B CE3   1 
ATOM   4521 C  CZ2   . TRP B 1 243 ? 29.628 -32.029 -27.371 1.00 25.49 ?  223 TRP B CZ2   1 
ATOM   4522 C  CZ3   . TRP B 1 243 ? 27.765 -30.751 -28.219 1.00 29.54 ?  223 TRP B CZ3   1 
ATOM   4523 C  CH2   . TRP B 1 243 ? 28.673 -31.069 -27.203 1.00 27.93 ?  223 TRP B CH2   1 
ATOM   4524 N  N     . LEU B 1 244 ? 29.521 -30.165 -32.090 1.00 29.39 ?  224 LEU B N     1 
ATOM   4525 C  CA    . LEU B 1 244 ? 29.115 -28.851 -31.605 1.00 33.38 ?  224 LEU B CA    1 
ATOM   4526 C  C     . LEU B 1 244 ? 29.103 -27.818 -32.726 1.00 35.90 ?  224 LEU B C     1 
ATOM   4527 O  O     . LEU B 1 244 ? 28.120 -27.085 -32.884 1.00 39.19 ?  224 LEU B O     1 
ATOM   4528 C  CB    . LEU B 1 244 ? 30.030 -28.398 -30.466 1.00 33.83 ?  224 LEU B CB    1 
ATOM   4529 C  CG    . LEU B 1 244 ? 29.799 -26.967 -29.984 1.00 28.91 ?  224 LEU B CG    1 
ATOM   4530 C  CD1   . LEU B 1 244 ? 28.448 -26.801 -29.291 1.00 33.15 ?  224 LEU B CD1   1 
ATOM   4531 C  CD2   . LEU B 1 244 ? 30.926 -26.583 -29.067 1.00 29.49 ?  224 LEU B CD2   1 
ATOM   4532 N  N     . GLY B 1 245 ? 30.191 -27.745 -33.499 1.00 33.46 ?  225 GLY B N     1 
ATOM   4533 C  CA    . GLY B 1 245 ? 30.268 -26.836 -34.636 1.00 34.16 ?  225 GLY B CA    1 
ATOM   4534 C  C     . GLY B 1 245 ? 29.971 -25.405 -34.244 1.00 36.60 ?  225 GLY B C     1 
ATOM   4535 O  O     . GLY B 1 245 ? 30.476 -24.891 -33.237 1.00 34.93 ?  225 GLY B O     1 
ATOM   4536 N  N     . ASN B 1 246 ? 29.124 -24.751 -35.034 1.00 38.60 ?  226 ASN B N     1 
ATOM   4537 C  CA    . ASN B 1 246 ? 28.698 -23.377 -34.794 1.00 39.33 ?  226 ASN B CA    1 
ATOM   4538 C  C     . ASN B 1 246 ? 27.204 -23.304 -34.516 1.00 38.90 ?  226 ASN B C     1 
ATOM   4539 O  O     . ASN B 1 246 ? 26.516 -22.401 -34.985 1.00 44.26 ?  226 ASN B O     1 
ATOM   4540 C  CB    . ASN B 1 246 ? 29.058 -22.480 -35.976 1.00 32.48 ?  226 ASN B CB    1 
ATOM   4541 C  CG    . ASN B 1 246 ? 28.363 -22.887 -37.255 1.00 35.22 ?  226 ASN B CG    1 
ATOM   4542 O  OD1   . ASN B 1 246 ? 27.664 -23.899 -37.300 1.00 38.99 ?  226 ASN B OD1   1 
ATOM   4543 N  ND2   . ASN B 1 246 ? 28.548 -22.096 -38.308 1.00 38.60 ?  226 ASN B ND2   1 
ATOM   4544 N  N     . HIS B 1 247 ? 26.678 -24.254 -33.742 1.00 42.70 ?  227 HIS B N     1 
ATOM   4545 C  CA    . HIS B 1 247 ? 25.236 -24.333 -33.541 1.00 46.63 ?  227 HIS B CA    1 
ATOM   4546 C  C     . HIS B 1 247 ? 24.747 -23.828 -32.186 1.00 46.72 ?  227 HIS B C     1 
ATOM   4547 O  O     . HIS B 1 247 ? 23.547 -23.557 -32.058 1.00 53.72 ?  227 HIS B O     1 
ATOM   4548 C  CB    . HIS B 1 247 ? 24.740 -25.773 -33.765 1.00 45.13 ?  227 HIS B CB    1 
ATOM   4549 C  CG    . HIS B 1 247 ? 25.290 -26.415 -35.005 1.00 54.61 ?  227 HIS B CG    1 
ATOM   4550 N  ND1   . HIS B 1 247 ? 24.717 -26.236 -36.248 1.00 49.42 ?  227 HIS B ND1   1 
ATOM   4551 C  CD2   . HIS B 1 247 ? 26.324 -27.273 -35.193 1.00 52.01 ?  227 HIS B CD2   1 
ATOM   4552 C  CE1   . HIS B 1 247 ? 25.393 -26.928 -37.149 1.00 42.69 ?  227 HIS B CE1   1 
ATOM   4553 N  NE2   . HIS B 1 247 ? 26.369 -27.572 -36.536 1.00 41.14 ?  227 HIS B NE2   1 
ATOM   4554 N  N     . SER B 1 248 ? 25.619 -23.664 -31.188 1.00 40.99 ?  228 SER B N     1 
ATOM   4555 C  CA    . SER B 1 248 ? 25.223 -23.195 -29.856 1.00 34.86 ?  228 SER B CA    1 
ATOM   4556 C  C     . SER B 1 248 ? 25.978 -21.921 -29.482 1.00 43.37 ?  228 SER B C     1 
ATOM   4557 O  O     . SER B 1 248 ? 26.733 -21.894 -28.496 1.00 33.56 ?  228 SER B O     1 
ATOM   4558 C  CB    . SER B 1 248 ? 25.446 -24.280 -28.806 1.00 42.32 ?  228 SER B CB    1 
ATOM   4559 O  OG    . SER B 1 248 ? 24.908 -25.522 -29.235 1.00 42.13 ?  228 SER B OG    1 
ATOM   4560 N  N     . PRO B 1 249 ? 25.754 -20.831 -30.230 1.00 44.29 ?  229 PRO B N     1 
ATOM   4561 C  CA    . PRO B 1 249 ? 26.647 -19.662 -30.133 1.00 40.67 ?  229 PRO B CA    1 
ATOM   4562 C  C     . PRO B 1 249 ? 26.808 -19.079 -28.732 1.00 43.48 ?  229 PRO B C     1 
ATOM   4563 O  O     . PRO B 1 249 ? 27.857 -18.481 -28.448 1.00 46.12 ?  229 PRO B O     1 
ATOM   4564 C  CB    . PRO B 1 249 ? 25.992 -18.652 -31.090 1.00 35.02 ?  229 PRO B CB    1 
ATOM   4565 C  CG    . PRO B 1 249 ? 24.588 -19.133 -31.270 1.00 31.05 ?  229 PRO B CG    1 
ATOM   4566 C  CD    . PRO B 1 249 ? 24.692 -20.614 -31.224 1.00 34.47 ?  229 PRO B CD    1 
ATOM   4567 N  N     . ASN B 1 250 ? 25.824 -19.215 -27.844 1.00 28.46 ?  230 ASN B N     1 
ATOM   4568 C  CA    . ASN B 1 250 ? 25.932 -18.555 -26.546 1.00 39.65 ?  230 ASN B CA    1 
ATOM   4569 C  C     . ASN B 1 250 ? 25.919 -19.531 -25.367 1.00 37.19 ?  230 ASN B C     1 
ATOM   4570 O  O     . ASN B 1 250 ? 25.732 -19.105 -24.224 1.00 32.42 ?  230 ASN B O     1 
ATOM   4571 C  CB    . ASN B 1 250 ? 24.830 -17.504 -26.389 1.00 37.12 ?  230 ASN B CB    1 
ATOM   4572 C  CG    . ASN B 1 250 ? 25.040 -16.287 -27.293 1.00 41.24 ?  230 ASN B CG    1 
ATOM   4573 O  OD1   . ASN B 1 250 ? 26.050 -15.580 -27.204 1.00 40.54 ?  230 ASN B OD1   1 
ATOM   4574 N  ND2   . ASN B 1 250 ? 24.073 -16.033 -28.155 1.00 43.83 ?  230 ASN B ND2   1 
ATOM   4575 N  N     . SER B 1 251 ? 26.133 -20.823 -25.612 1.00 39.27 ?  231 SER B N     1 
ATOM   4576 C  CA    . SER B 1 251 ? 26.181 -21.799 -24.534 1.00 31.60 ?  231 SER B CA    1 
ATOM   4577 C  C     . SER B 1 251 ? 27.427 -21.595 -23.680 1.00 31.50 ?  231 SER B C     1 
ATOM   4578 O  O     . SER B 1 251 ? 28.375 -20.910 -24.068 1.00 38.92 ?  231 SER B O     1 
ATOM   4579 C  CB    . SER B 1 251 ? 26.174 -23.220 -25.089 1.00 39.69 ?  231 SER B CB    1 
ATOM   4580 O  OG    . SER B 1 251 ? 27.160 -23.367 -26.091 1.00 39.48 ?  231 SER B OG    1 
ATOM   4581 N  N     . GLU B 1 252 ? 27.421 -22.212 -22.497 1.00 32.57 ?  232 GLU B N     1 
ATOM   4582 C  CA    . GLU B 1 252 ? 28.564 -22.085 -21.598 1.00 33.50 ?  232 GLU B CA    1 
ATOM   4583 C  C     . GLU B 1 252 ? 29.742 -22.924 -22.098 1.00 34.72 ?  232 GLU B C     1 
ATOM   4584 O  O     . GLU B 1 252 ? 30.906 -22.576 -21.857 1.00 32.81 ?  232 GLU B O     1 
ATOM   4585 C  CB    . GLU B 1 252 ? 28.106 -22.438 -20.163 1.00 29.61 ?  232 GLU B CB    1 
ATOM   4586 C  CG    . GLU B 1 252 ? 29.044 -23.203 -19.214 1.00 42.11 ?  232 GLU B CG    1 
ATOM   4587 C  CD    . GLU B 1 252 ? 28.550 -23.199 -17.720 1.00 67.48 ?  232 GLU B CD    1 
ATOM   4588 O  OE1   . GLU B 1 252 ? 28.569 -22.123 -17.070 1.00 67.65 ?  232 GLU B OE1   1 
ATOM   4589 O  OE2   . GLU B 1 252 ? 28.159 -24.275 -17.185 1.00 62.66 ?  232 GLU B OE2   1 
ATOM   4590 N  N     . TYR B 1 253 ? 29.462 -23.987 -22.859 1.00 32.17 ?  233 TYR B N     1 
ATOM   4591 C  CA    . TYR B 1 253 ? 30.538 -24.803 -23.411 1.00 26.34 ?  233 TYR B CA    1 
ATOM   4592 C  C     . TYR B 1 253 ? 31.360 -24.035 -24.450 1.00 29.38 ?  233 TYR B C     1 
ATOM   4593 O  O     . TYR B 1 253 ? 32.597 -24.134 -24.464 1.00 27.29 ?  233 TYR B O     1 
ATOM   4594 C  CB    . TYR B 1 253 ? 29.957 -26.079 -24.012 1.00 27.20 ?  233 TYR B CB    1 
ATOM   4595 C  CG    . TYR B 1 253 ? 30.982 -27.148 -24.269 1.00 23.82 ?  233 TYR B CG    1 
ATOM   4596 C  CD1   . TYR B 1 253 ? 32.125 -27.223 -23.495 1.00 22.53 ?  233 TYR B CD1   1 
ATOM   4597 C  CD2   . TYR B 1 253 ? 30.815 -28.080 -25.297 1.00 26.87 ?  233 TYR B CD2   1 
ATOM   4598 C  CE1   . TYR B 1 253 ? 33.077 -28.190 -23.713 1.00 23.74 ?  233 TYR B CE1   1 
ATOM   4599 C  CE2   . TYR B 1 253 ? 31.772 -29.064 -25.525 1.00 27.94 ?  233 TYR B CE2   1 
ATOM   4600 C  CZ    . TYR B 1 253 ? 32.905 -29.110 -24.717 1.00 27.69 ?  233 TYR B CZ    1 
ATOM   4601 O  OH    . TYR B 1 253 ? 33.874 -30.073 -24.903 1.00 29.18 ?  233 TYR B OH    1 
ATOM   4602 N  N     . VAL B 1 254 ? 30.699 -23.277 -25.338 1.00 26.84 ?  234 VAL B N     1 
ATOM   4603 C  CA    . VAL B 1 254 ? 31.452 -22.464 -26.300 1.00 30.62 ?  234 VAL B CA    1 
ATOM   4604 C  C     . VAL B 1 254 ? 32.295 -21.423 -25.567 1.00 26.23 ?  234 VAL B C     1 
ATOM   4605 O  O     . VAL B 1 254 ? 33.396 -21.067 -26.012 1.00 24.17 ?  234 VAL B O     1 
ATOM   4606 C  CB    . VAL B 1 254 ? 30.504 -21.812 -27.340 1.00 31.66 ?  234 VAL B CB    1 
ATOM   4607 C  CG1   . VAL B 1 254 ? 31.254 -20.799 -28.216 1.00 19.79 ?  234 VAL B CG1   1 
ATOM   4608 C  CG2   . VAL B 1 254 ? 29.847 -22.878 -28.211 1.00 26.80 ?  234 VAL B CG2   1 
ATOM   4609 N  N     . SER B 1 255 ? 31.815 -20.940 -24.421 1.00 26.95 ?  235 SER B N     1 
ATOM   4610 C  CA    . SER B 1 255 ? 32.604 -19.988 -23.650 1.00 24.48 ?  235 SER B CA    1 
ATOM   4611 C  C     . SER B 1 255 ? 33.868 -20.645 -23.096 1.00 25.99 ?  235 SER B C     1 
ATOM   4612 O  O     . SER B 1 255 ? 34.967 -20.081 -23.183 1.00 25.92 ?  235 SER B O     1 
ATOM   4613 C  CB    . SER B 1 255 ? 31.747 -19.393 -22.544 1.00 22.21 ?  235 SER B CB    1 
ATOM   4614 O  OG    . SER B 1 255 ? 32.304 -18.169 -22.119 1.00 35.79 ?  235 SER B OG    1 
ATOM   4615 N  N     . PHE B 1 256 ? 33.730 -21.851 -22.546 1.00 23.24 ?  236 PHE B N     1 
ATOM   4616 C  CA    . PHE B 1 256 ? 34.888 -22.611 -22.090 1.00 21.39 ?  236 PHE B CA    1 
ATOM   4617 C  C     . PHE B 1 256 ? 35.861 -22.860 -23.233 1.00 21.92 ?  236 PHE B C     1 
ATOM   4618 O  O     . PHE B 1 256 ? 37.067 -22.630 -23.097 1.00 22.75 ?  236 PHE B O     1 
ATOM   4619 C  CB    . PHE B 1 256 ? 34.401 -23.920 -21.475 1.00 21.97 ?  236 PHE B CB    1 
ATOM   4620 C  CG    . PHE B 1 256 ? 35.458 -24.963 -21.289 1.00 23.59 ?  236 PHE B CG    1 
ATOM   4621 C  CD1   . PHE B 1 256 ? 36.156 -25.054 -20.069 1.00 18.64 ?  236 PHE B CD1   1 
ATOM   4622 C  CD2   . PHE B 1 256 ? 35.693 -25.918 -22.284 1.00 20.12 ?  236 PHE B CD2   1 
ATOM   4623 C  CE1   . PHE B 1 256 ? 37.109 -26.041 -19.869 1.00 19.31 ?  236 PHE B CE1   1 
ATOM   4624 C  CE2   . PHE B 1 256 ? 36.656 -26.911 -22.096 1.00 20.96 ?  236 PHE B CE2   1 
ATOM   4625 C  CZ    . PHE B 1 256 ? 37.370 -26.974 -20.883 1.00 19.26 ?  236 PHE B CZ    1 
ATOM   4626 N  N     . ILE B 1 257 ? 35.351 -23.324 -24.377 1.00 24.00 ?  237 ILE B N     1 
ATOM   4627 C  CA    . ILE B 1 257 ? 36.216 -23.550 -25.533 1.00 21.59 ?  237 ILE B CA    1 
ATOM   4628 C  C     . ILE B 1 257 ? 36.910 -22.254 -25.926 1.00 23.61 ?  237 ILE B C     1 
ATOM   4629 O  O     . ILE B 1 257 ? 38.120 -22.228 -26.193 1.00 19.90 ?  237 ILE B O     1 
ATOM   4630 C  CB    . ILE B 1 257 ? 35.407 -24.132 -26.706 1.00 19.67 ?  237 ILE B CB    1 
ATOM   4631 C  CG1   . ILE B 1 257 ? 34.911 -25.521 -26.351 1.00 22.83 ?  237 ILE B CG1   1 
ATOM   4632 C  CG2   . ILE B 1 257 ? 36.247 -24.161 -27.966 1.00 18.09 ?  237 ILE B CG2   1 
ATOM   4633 C  CD1   . ILE B 1 257 ? 33.704 -25.914 -27.084 1.00 22.07 ?  237 ILE B CD1   1 
ATOM   4634 N  N     . LYS B 1 258 ? 36.148 -21.155 -25.959 1.00 19.74 ?  238 LYS B N     1 
ATOM   4635 C  CA    . LYS B 1 258 ? 36.718 -19.857 -26.303 1.00 19.58 ?  238 LYS B CA    1 
ATOM   4636 C  C     . LYS B 1 258 ? 37.912 -19.516 -25.412 1.00 24.12 ?  238 LYS B C     1 
ATOM   4637 O  O     . LYS B 1 258 ? 38.928 -18.995 -25.891 1.00 24.64 ?  238 LYS B O     1 
ATOM   4638 C  CB    . LYS B 1 258 ? 35.644 -18.771 -26.198 1.00 21.92 ?  238 LYS B CB    1 
ATOM   4639 C  CG    . LYS B 1 258 ? 36.228 -17.369 -26.240 1.00 23.25 ?  238 LYS B CG    1 
ATOM   4640 C  CD    . LYS B 1 258 ? 35.204 -16.322 -25.961 1.00 20.04 ?  238 LYS B CD    1 
ATOM   4641 C  CE    . LYS B 1 258 ? 35.074 -16.105 -24.474 1.00 22.75 ?  238 LYS B CE    1 
ATOM   4642 N  NZ    . LYS B 1 258 ? 33.738 -15.500 -24.159 1.00 24.95 ?  238 LYS B NZ    1 
ATOM   4643 N  N     . ASP B 1 259 ? 37.820 -19.828 -24.113 1.00 20.95 ?  239 ASP B N     1 
ATOM   4644 C  CA    . ASP B 1 259 ? 38.913 -19.546 -23.199 1.00 21.02 ?  239 ASP B CA    1 
ATOM   4645 C  C     . ASP B 1 259 ? 40.067 -20.519 -23.347 1.00 23.68 ?  239 ASP B C     1 
ATOM   4646 O  O     . ASP B 1 259 ? 41.189 -20.177 -22.956 1.00 29.71 ?  239 ASP B O     1 
ATOM   4647 C  CB    . ASP B 1 259 ? 38.413 -19.546 -21.746 1.00 23.79 ?  239 ASP B CB    1 
ATOM   4648 C  CG    . ASP B 1 259 ? 37.306 -18.520 -21.504 1.00 27.68 ?  239 ASP B CG    1 
ATOM   4649 O  OD1   . ASP B 1 259 ? 37.409 -17.378 -22.013 1.00 24.22 ?  239 ASP B OD1   1 
ATOM   4650 O  OD2   . ASP B 1 259 ? 36.317 -18.868 -20.814 1.00 38.11 ?  239 ASP B OD2   1 
ATOM   4651 N  N     . SER B 1 260 ? 39.830 -21.711 -23.907 1.00 24.18 ?  240 SER B N     1 
ATOM   4652 C  CA    . SER B 1 260 ? 40.874 -22.729 -24.035 1.00 24.57 ?  240 SER B CA    1 
ATOM   4653 C  C     . SER B 1 260 ? 41.697 -22.613 -25.320 1.00 25.76 ?  240 SER B C     1 
ATOM   4654 O  O     . SER B 1 260 ? 42.813 -23.154 -25.365 1.00 23.80 ?  240 SER B O     1 
ATOM   4655 C  CB    . SER B 1 260 ? 40.258 -24.136 -23.986 1.00 24.48 ?  240 SER B CB    1 
ATOM   4656 O  OG    . SER B 1 260 ? 39.356 -24.280 -22.904 1.00 24.49 ?  240 SER B OG    1 
ATOM   4657 N  N     . VAL B 1 261 ? 41.179 -21.923 -26.350 1.00 21.42 ?  241 VAL B N     1 
ATOM   4658 C  CA    . VAL B 1 261 ? 41.799 -21.949 -27.680 1.00 23.64 ?  241 VAL B CA    1 
ATOM   4659 C  C     . VAL B 1 261 ? 43.289 -21.642 -27.590 1.00 20.41 ?  241 VAL B C     1 
ATOM   4660 O  O     . VAL B 1 261 ? 44.122 -22.342 -28.182 1.00 19.67 ?  241 VAL B O     1 
ATOM   4661 C  CB    . VAL B 1 261 ? 41.084 -20.971 -28.642 1.00 26.13 ?  241 VAL B CB    1 
ATOM   4662 C  CG1   . VAL B 1 261 ? 41.816 -20.900 -29.990 1.00 20.28 ?  241 VAL B CG1   1 
ATOM   4663 C  CG2   . VAL B 1 261 ? 39.620 -21.355 -28.857 1.00 19.15 ?  241 VAL B CG2   1 
ATOM   4664 N  N     . PHE B 1 262 ? 43.654 -20.600 -26.842 1.00 15.02 ?  242 PHE B N     1 
ATOM   4665 C  CA    . PHE B 1 262 ? 45.042 -20.156 -26.869 1.00 20.58 ?  242 PHE B CA    1 
ATOM   4666 C  C     . PHE B 1 262 ? 45.893 -20.812 -25.796 1.00 21.78 ?  242 PHE B C     1 
ATOM   4667 O  O     . PHE B 1 262 ? 47.096 -20.537 -25.721 1.00 18.94 ?  242 PHE B O     1 
ATOM   4668 C  CB    . PHE B 1 262 ? 45.095 -18.621 -26.828 1.00 12.18 ?  242 PHE B CB    1 
ATOM   4669 C  CG    . PHE B 1 262 ? 44.547 -18.016 -28.094 1.00 23.88 ?  242 PHE B CG    1 
ATOM   4670 C  CD1   . PHE B 1 262 ? 45.298 -18.034 -29.267 1.00 20.58 ?  242 PHE B CD1   1 
ATOM   4671 C  CD2   . PHE B 1 262 ? 43.235 -17.566 -28.162 1.00 25.72 ?  242 PHE B CD2   1 
ATOM   4672 C  CE1   . PHE B 1 262 ? 44.783 -17.535 -30.458 1.00 20.41 ?  242 PHE B CE1   1 
ATOM   4673 C  CE2   . PHE B 1 262 ? 42.709 -17.079 -29.358 1.00 25.45 ?  242 PHE B CE2   1 
ATOM   4674 C  CZ    . PHE B 1 262 ? 43.489 -17.055 -30.502 1.00 25.72 ?  242 PHE B CZ    1 
ATOM   4675 N  N     . TYR B 1 263 ? 45.305 -21.724 -25.014 1.00 23.58 ?  243 TYR B N     1 
ATOM   4676 C  CA    . TYR B 1 263 ? 46.085 -22.619 -24.169 1.00 19.59 ?  243 TYR B CA    1 
ATOM   4677 C  C     . TYR B 1 263 ? 46.623 -23.800 -24.962 1.00 20.82 ?  243 TYR B C     1 
ATOM   4678 O  O     . TYR B 1 263 ? 47.730 -24.276 -24.690 1.00 21.42 ?  243 TYR B O     1 
ATOM   4679 C  CB    . TYR B 1 263 ? 45.232 -23.116 -22.999 1.00 22.59 ?  243 TYR B CB    1 
ATOM   4680 C  CG    . TYR B 1 263 ? 45.148 -22.168 -21.812 1.00 22.40 ?  243 TYR B CG    1 
ATOM   4681 C  CD1   . TYR B 1 263 ? 44.346 -21.026 -21.855 1.00 24.29 ?  243 TYR B CD1   1 
ATOM   4682 C  CD2   . TYR B 1 263 ? 45.885 -22.409 -20.657 1.00 20.37 ?  243 TYR B CD2   1 
ATOM   4683 C  CE1   . TYR B 1 263 ? 44.269 -20.166 -20.774 1.00 20.03 ?  243 TYR B CE1   1 
ATOM   4684 C  CE2   . TYR B 1 263 ? 45.828 -21.552 -19.570 1.00 16.98 ?  243 TYR B CE2   1 
ATOM   4685 C  CZ    . TYR B 1 263 ? 45.005 -20.443 -19.623 1.00 28.36 ?  243 TYR B CZ    1 
ATOM   4686 O  OH    . TYR B 1 263 ? 44.927 -19.601 -18.520 1.00 30.53 ?  243 TYR B OH    1 
ATOM   4687 N  N     . LEU B 1 264 ? 45.853 -24.284 -25.942 1.00 23.78 ?  244 LEU B N     1 
ATOM   4688 C  CA    . LEU B 1 264 ? 46.251 -25.348 -26.852 1.00 18.99 ?  244 LEU B CA    1 
ATOM   4689 C  C     . LEU B 1 264 ? 47.605 -25.064 -27.482 1.00 18.75 ?  244 LEU B C     1 
ATOM   4690 O  O     . LEU B 1 264 ? 47.971 -23.899 -27.675 1.00 15.48 ?  244 LEU B O     1 
ATOM   4691 C  CB    . LEU B 1 264 ? 45.222 -25.509 -27.965 1.00 20.35 ?  244 LEU B CB    1 
ATOM   4692 C  CG    . LEU B 1 264 ? 43.941 -26.259 -27.632 1.00 22.86 ?  244 LEU B CG    1 
ATOM   4693 C  CD1   . LEU B 1 264 ? 42.956 -26.021 -28.759 1.00 20.53 ?  244 LEU B CD1   1 
ATOM   4694 C  CD2   . LEU B 1 264 ? 44.240 -27.747 -27.435 1.00 21.81 ?  244 LEU B CD2   1 
ATOM   4695 N  N     . PRO B 1 265 ? 48.372 -26.096 -27.816 1.00 22.11 ?  245 PRO B N     1 
ATOM   4696 C  CA    . PRO B 1 265 ? 49.548 -25.907 -28.690 1.00 20.12 ?  245 PRO B CA    1 
ATOM   4697 C  C     . PRO B 1 265 ? 49.165 -25.199 -29.980 1.00 21.34 ?  245 PRO B C     1 
ATOM   4698 O  O     . PRO B 1 265 ? 48.062 -25.407 -30.513 1.00 15.99 ?  245 PRO B O     1 
ATOM   4699 C  CB    . PRO B 1 265 ? 50.016 -27.338 -28.959 1.00 19.13 ?  245 PRO B CB    1 
ATOM   4700 C  CG    . PRO B 1 265 ? 49.481 -28.135 -27.768 1.00 20.99 ?  245 PRO B CG    1 
ATOM   4701 C  CD    . PRO B 1 265 ? 48.306 -27.441 -27.209 1.00 17.32 ?  245 PRO B CD    1 
ATOM   4702 N  N     . PRO B 1 266 ? 50.045 -24.339 -30.506 1.00 21.22 ?  246 PRO B N     1 
ATOM   4703 C  CA    . PRO B 1 266 ? 49.703 -23.591 -31.733 1.00 22.53 ?  246 PRO B CA    1 
ATOM   4704 C  C     . PRO B 1 266 ? 49.183 -24.474 -32.850 1.00 22.51 ?  246 PRO B C     1 
ATOM   4705 O  O     . PRO B 1 266 ? 48.231 -24.098 -33.546 1.00 26.14 ?  246 PRO B O     1 
ATOM   4706 C  CB    . PRO B 1 266 ? 51.030 -22.927 -32.120 1.00 21.93 ?  246 PRO B CB    1 
ATOM   4707 C  CG    . PRO B 1 266 ? 51.867 -22.962 -30.869 1.00 24.38 ?  246 PRO B CG    1 
ATOM   4708 C  CD    . PRO B 1 266 ? 51.446 -24.145 -30.092 1.00 18.97 ?  246 PRO B CD    1 
ATOM   4709 N  N     . GLU B 1 267 ? 49.733 -25.683 -32.977 1.00 26.68 ?  247 GLU B N     1 
ATOM   4710 C  CA    . GLU B 1 267 ? 49.400 -26.574 -34.080 1.00 26.11 ?  247 GLU B CA    1 
ATOM   4711 C  C     . GLU B 1 267 ? 47.888 -26.879 -34.170 1.00 26.79 ?  247 GLU B C     1 
ATOM   4712 O  O     . GLU B 1 267 ? 47.402 -27.203 -35.257 1.00 30.31 ?  247 GLU B O     1 
ATOM   4713 C  CB    . GLU B 1 267 ? 50.252 -27.873 -33.966 1.00 28.20 ?  247 GLU B CB    1 
ATOM   4714 C  CG    . GLU B 1 267 ? 51.890 -27.763 -33.857 1.00 28.56 ?  247 GLU B CG    1 
ATOM   4715 C  CD    . GLU B 1 267 ? 52.478 -27.423 -32.425 1.00 40.67 ?  247 GLU B CD    1 
ATOM   4716 O  OE1   . GLU B 1 267 ? 51.740 -26.729 -31.695 1.00 41.41 ?  247 GLU B OE1   1 
ATOM   4717 O  OE2   . GLU B 1 267 ? 53.650 -27.820 -32.020 1.00 28.83 ?  247 GLU B OE2   1 
ATOM   4718 N  N     . LEU B 1 268 ? 47.118 -26.721 -33.080 1.00 25.18 ?  248 LEU B N     1 
ATOM   4719 C  CA    . LEU B 1 268 ? 45.701 -27.109 -33.007 1.00 21.28 ?  248 LEU B CA    1 
ATOM   4720 C  C     . LEU B 1 268 ? 44.710 -25.951 -33.071 1.00 22.47 ?  248 LEU B C     1 
ATOM   4721 O  O     . LEU B 1 268 ? 43.504 -26.204 -33.129 1.00 18.69 ?  248 LEU B O     1 
ATOM   4722 C  CB    . LEU B 1 268 ? 45.402 -27.879 -31.694 1.00 21.74 ?  248 LEU B CB    1 
ATOM   4723 C  CG    . LEU B 1 268 ? 45.612 -29.392 -31.599 1.00 25.79 ?  248 LEU B CG    1 
ATOM   4724 C  CD1   . LEU B 1 268 ? 45.722 -29.812 -30.159 1.00 28.53 ?  248 LEU B CD1   1 
ATOM   4725 C  CD2   . LEU B 1 268 ? 44.485 -30.164 -32.292 1.00 25.77 ?  248 LEU B CD2   1 
ATOM   4726 N  N     . ARG B 1 269 ? 45.164 -24.702 -33.013 1.00 23.65 ?  249 ARG B N     1 
ATOM   4727 C  CA    . ARG B 1 269 ? 44.253 -23.566 -32.907 1.00 19.03 ?  249 ARG B CA    1 
ATOM   4728 C  C     . ARG B 1 269 ? 43.446 -23.318 -34.189 1.00 23.47 ?  249 ARG B C     1 
ATOM   4729 O  O     . ARG B 1 269 ? 42.245 -23.005 -34.109 1.00 18.89 ?  249 ARG B O     1 
ATOM   4730 C  CB    . ARG B 1 269 ? 45.043 -22.313 -32.507 1.00 24.04 ?  249 ARG B CB    1 
ATOM   4731 C  CG    . ARG B 1 269 ? 45.688 -22.409 -31.117 1.00 20.68 ?  249 ARG B CG    1 
ATOM   4732 C  CD    . ARG B 1 269 ? 46.681 -21.302 -30.813 1.00 18.39 ?  249 ARG B CD    1 
ATOM   4733 N  NE    . ARG B 1 269 ? 47.467 -21.644 -29.637 1.00 22.73 ?  249 ARG B NE    1 
ATOM   4734 C  CZ    . ARG B 1 269 ? 48.576 -21.032 -29.241 1.00 16.74 ?  249 ARG B CZ    1 
ATOM   4735 N  NH1   . ARG B 1 269 ? 49.026 -19.957 -29.846 1.00 14.39 ?  249 ARG B NH1   1 
ATOM   4736 N  NH2   . ARG B 1 269 ? 49.245 -21.515 -28.202 1.00 16.29 ?  249 ARG B NH2   1 
ATOM   4737 N  N     . PRO B 1 270 ? 44.042 -23.425 -35.386 1.00 23.52 ?  250 PRO B N     1 
ATOM   4738 C  CA    . PRO B 1 270 ? 43.224 -23.202 -36.594 1.00 17.80 ?  250 PRO B CA    1 
ATOM   4739 C  C     . PRO B 1 270 ? 42.083 -24.200 -36.745 1.00 23.81 ?  250 PRO B C     1 
ATOM   4740 O  O     . PRO B 1 270 ? 40.945 -23.787 -37.024 1.00 22.33 ?  250 PRO B O     1 
ATOM   4741 C  CB    . PRO B 1 270 ? 44.253 -23.291 -37.715 1.00 15.67 ?  250 PRO B CB    1 
ATOM   4742 C  CG    . PRO B 1 270 ? 45.553 -22.962 -37.060 1.00 20.09 ?  250 PRO B CG    1 
ATOM   4743 C  CD    . PRO B 1 270 ? 45.480 -23.524 -35.719 1.00 21.68 ?  250 PRO B CD    1 
ATOM   4744 N  N     . ILE B 1 271 ? 42.329 -25.500 -36.535 1.00 22.11 ?  251 ILE B N     1 
ATOM   4745 C  CA    . ILE B 1 271 ? 41.237 -26.455 -36.703 1.00 21.77 ?  251 ILE B CA    1 
ATOM   4746 C  C     . ILE B 1 271 ? 40.148 -26.181 -35.691 1.00 25.87 ?  251 ILE B C     1 
ATOM   4747 O  O     . ILE B 1 271 ? 38.955 -26.268 -36.005 1.00 26.59 ?  251 ILE B O     1 
ATOM   4748 C  CB    . ILE B 1 271 ? 41.725 -27.917 -36.630 1.00 28.78 ?  251 ILE B CB    1 
ATOM   4749 C  CG1   . ILE B 1 271 ? 40.527 -28.845 -36.384 1.00 34.89 ?  251 ILE B CG1   1 
ATOM   4750 C  CG2   . ILE B 1 271 ? 42.786 -28.111 -35.580 1.00 29.60 ?  251 ILE B CG2   1 
ATOM   4751 C  CD1   . ILE B 1 271 ? 40.810 -30.323 -36.589 1.00 37.28 ?  251 ILE B CD1   1 
ATOM   4752 N  N     . CYS B 1 272 ? 40.537 -25.796 -34.473 1.00 25.85 ?  252 CYS B N     1 
ATOM   4753 C  CA    . CYS B 1 272 ? 39.551 -25.470 -33.451 1.00 23.48 ?  252 CYS B CA    1 
ATOM   4754 C  C     . CYS B 1 272 ? 38.780 -24.204 -33.811 1.00 21.43 ?  252 CYS B C     1 
ATOM   4755 O  O     . CYS B 1 272 ? 37.544 -24.167 -33.717 1.00 23.20 ?  252 CYS B O     1 
ATOM   4756 C  CB    . CYS B 1 272 ? 40.236 -25.330 -32.091 1.00 25.97 ?  252 CYS B CB    1 
ATOM   4757 S  SG    . CYS B 1 272 ? 39.058 -25.137 -30.759 1.00 32.01 ?  252 CYS B SG    1 
ATOM   4758 N  N     . VAL B 1 273 ? 39.494 -23.156 -34.233 1.00 24.19 ?  253 VAL B N     1 
ATOM   4759 C  CA    . VAL B 1 273 ? 38.828 -21.924 -34.668 1.00 25.63 ?  253 VAL B CA    1 
ATOM   4760 C  C     . VAL B 1 273 ? 37.892 -22.211 -35.840 1.00 28.27 ?  253 VAL B C     1 
ATOM   4761 O  O     . VAL B 1 273 ? 36.711 -21.853 -35.806 1.00 28.67 ?  253 VAL B O     1 
ATOM   4762 C  CB    . VAL B 1 273 ? 39.864 -20.837 -35.031 1.00 24.77 ?  253 VAL B CB    1 
ATOM   4763 C  CG1   . VAL B 1 273 ? 39.187 -19.695 -35.821 1.00 20.26 ?  253 VAL B CG1   1 
ATOM   4764 C  CG2   . VAL B 1 273 ? 40.555 -20.303 -33.793 1.00 19.07 ?  253 VAL B CG2   1 
ATOM   4765 N  N     . ASP B 1 274 ? 38.414 -22.873 -36.890 1.00 22.71 ?  254 ASP B N     1 
ATOM   4766 C  CA    . ASP B 1 274 ? 37.614 -23.229 -38.063 1.00 24.17 ?  254 ASP B CA    1 
ATOM   4767 C  C     . ASP B 1 274 ? 36.351 -23.992 -37.689 1.00 29.02 ?  254 ASP B C     1 
ATOM   4768 O  O     . ASP B 1 274 ? 35.260 -23.696 -38.188 1.00 32.18 ?  254 ASP B O     1 
ATOM   4769 C  CB    . ASP B 1 274 ? 38.437 -24.093 -39.016 1.00 33.88 ?  254 ASP B CB    1 
ATOM   4770 C  CG    . ASP B 1 274 ? 39.531 -23.324 -39.735 1.00 30.06 ?  254 ASP B CG    1 
ATOM   4771 O  OD1   . ASP B 1 274 ? 39.834 -22.157 -39.387 1.00 30.61 ?  254 ASP B OD1   1 
ATOM   4772 O  OD2   . ASP B 1 274 ? 40.126 -23.937 -40.632 1.00 34.89 ?  254 ASP B OD2   1 
ATOM   4773 N  N     . SER B 1 275 ? 36.494 -25.027 -36.854 1.00 27.03 ?  255 SER B N     1 
ATOM   4774 C  CA    . SER B 1 275 ? 35.342 -25.840 -36.473 1.00 25.72 ?  255 SER B CA    1 
ATOM   4775 C  C     . SER B 1 275 ? 34.295 -24.998 -35.765 1.00 29.95 ?  255 SER B C     1 
ATOM   4776 O  O     . SER B 1 275 ? 33.089 -25.204 -35.953 1.00 30.79 ?  255 SER B O     1 
ATOM   4777 C  CB    . SER B 1 275 ? 35.782 -26.997 -35.575 1.00 25.66 ?  255 SER B CB    1 
ATOM   4778 O  OG    . SER B 1 275 ? 36.760 -27.801 -36.209 1.00 28.09 ?  255 SER B OG    1 
ATOM   4779 N  N     . LEU B 1 276 ? 34.744 -24.044 -34.941 1.00 23.38 ?  256 LEU B N     1 
ATOM   4780 C  CA    . LEU B 1 276 ? 33.835 -23.147 -34.239 1.00 28.80 ?  256 LEU B CA    1 
ATOM   4781 C  C     . LEU B 1 276 ? 33.001 -22.302 -35.191 1.00 30.76 ?  256 LEU B C     1 
ATOM   4782 O  O     . LEU B 1 276 ? 31.915 -21.857 -34.812 1.00 33.06 ?  256 LEU B O     1 
ATOM   4783 C  CB    . LEU B 1 276 ? 34.630 -22.232 -33.291 1.00 29.48 ?  256 LEU B CB    1 
ATOM   4784 C  CG    . LEU B 1 276 ? 35.044 -22.810 -31.920 1.00 24.46 ?  256 LEU B CG    1 
ATOM   4785 C  CD1   . LEU B 1 276 ? 35.772 -21.763 -31.124 1.00 23.89 ?  256 LEU B CD1   1 
ATOM   4786 C  CD2   . LEU B 1 276 ? 33.848 -23.349 -31.142 1.00 16.02 ?  256 LEU B CD2   1 
ATOM   4787 N  N     . LEU B 1 277 ? 33.476 -22.076 -36.415 1.00 25.05 ?  257 LEU B N     1 
ATOM   4788 C  CA    . LEU B 1 277 ? 32.839 -21.146 -37.327 1.00 30.96 ?  257 LEU B CA    1 
ATOM   4789 C  C     . LEU B 1 277 ? 32.169 -21.843 -38.498 1.00 31.78 ?  257 LEU B C     1 
ATOM   4790 O  O     . LEU B 1 277 ? 31.747 -21.170 -39.439 1.00 31.81 ?  257 LEU B O     1 
ATOM   4791 C  CB    . LEU B 1 277 ? 33.865 -20.123 -37.824 1.00 29.66 ?  257 LEU B CB    1 
ATOM   4792 C  CG    . LEU B 1 277 ? 34.522 -19.306 -36.706 1.00 25.03 ?  257 LEU B CG    1 
ATOM   4793 C  CD1   . LEU B 1 277 ? 35.633 -18.424 -37.238 1.00 24.70 ?  257 LEU B CD1   1 
ATOM   4794 C  CD2   . LEU B 1 277 ? 33.479 -18.483 -35.972 1.00 24.88 ?  257 LEU B CD2   1 
ATOM   4795 N  N     . GLU B 1 278 ? 32.046 -23.163 -38.446 1.00 33.65 ?  258 GLU B N     1 
ATOM   4796 C  CA    . GLU B 1 278 ? 31.535 -24.004 -39.518 1.00 33.01 ?  258 GLU B CA    1 
ATOM   4797 C  C     . GLU B 1 278 ? 30.549 -24.995 -38.924 1.00 36.18 ?  258 GLU B C     1 
ATOM   4798 O  O     . GLU B 1 278 ? 30.601 -25.288 -37.724 1.00 36.31 ?  258 GLU B O     1 
ATOM   4799 C  CB    . GLU B 1 278 ? 32.680 -24.755 -40.219 1.00 28.71 ?  258 GLU B CB    1 
ATOM   4800 C  CG    . GLU B 1 278 ? 33.578 -23.854 -41.075 1.00 31.06 ?  258 GLU B CG    1 
ATOM   4801 C  CD    . GLU B 1 278 ? 34.854 -24.538 -41.582 1.00 40.65 ?  258 GLU B CD    1 
ATOM   4802 O  OE1   . GLU B 1 278 ? 35.007 -25.769 -41.400 1.00 43.19 ?  258 GLU B OE1   1 
ATOM   4803 O  OE2   . GLU B 1 278 ? 35.708 -23.840 -42.179 1.00 31.89 ?  258 GLU B OE2   1 
ATOM   4804 N  N     . PRO B 1 279 ? 29.632 -25.528 -39.730 1.00 46.12 ?  259 PRO B N     1 
ATOM   4805 C  CA    . PRO B 1 279 ? 28.755 -26.592 -39.223 1.00 41.69 ?  259 PRO B CA    1 
ATOM   4806 C  C     . PRO B 1 279 ? 29.557 -27.844 -38.910 1.00 38.73 ?  259 PRO B C     1 
ATOM   4807 O  O     . PRO B 1 279 ? 30.585 -28.116 -39.537 1.00 41.86 ?  259 PRO B O     1 
ATOM   4808 C  CB    . PRO B 1 279 ? 27.780 -26.832 -40.378 1.00 43.40 ?  259 PRO B CB    1 
ATOM   4809 C  CG    . PRO B 1 279 ? 28.526 -26.360 -41.593 1.00 39.51 ?  259 PRO B CG    1 
ATOM   4810 C  CD    . PRO B 1 279 ? 29.336 -25.188 -41.132 1.00 33.17 ?  259 PRO B CD    1 
ATOM   4811 N  N     . SER B 1 280 ? 29.068 -28.615 -37.938 1.00 32.73 ?  260 SER B N     1 
ATOM   4812 C  CA    . SER B 1 280 ? 29.758 -29.828 -37.510 1.00 32.80 ?  260 SER B CA    1 
ATOM   4813 C  C     . SER B 1 280 ? 29.661 -30.952 -38.548 1.00 36.26 ?  260 SER B C     1 
ATOM   4814 O  O     . SER B 1 280 ? 28.775 -30.987 -39.405 1.00 34.73 ?  260 SER B O     1 
ATOM   4815 C  CB    . SER B 1 280 ? 29.187 -30.335 -36.197 1.00 33.46 ?  260 SER B CB    1 
ATOM   4816 O  OG    . SER B 1 280 ? 27.964 -31.001 -36.428 1.00 34.31 ?  260 SER B OG    1 
ATOM   4817 N  N     . VAL B 1 281 ? 30.591 -31.903 -38.428 1.00 34.84 ?  261 VAL B N     1 
ATOM   4818 C  CA    . VAL B 1 281 ? 30.628 -33.053 -39.327 1.00 30.13 ?  261 VAL B CA    1 
ATOM   4819 C  C     . VAL B 1 281 ? 29.315 -33.831 -39.279 1.00 36.99 ?  261 VAL B C     1 
ATOM   4820 O  O     . VAL B 1 281 ? 28.790 -34.248 -40.315 1.00 38.76 ?  261 VAL B O     1 
ATOM   4821 C  CB    . VAL B 1 281 ? 31.833 -33.949 -38.983 1.00 30.62 ?  261 VAL B CB    1 
ATOM   4822 C  CG1   . VAL B 1 281 ? 31.715 -35.308 -39.687 1.00 29.52 ?  261 VAL B CG1   1 
ATOM   4823 C  CG2   . VAL B 1 281 ? 33.138 -33.252 -39.356 1.00 26.02 ?  261 VAL B CG2   1 
ATOM   4824 N  N     . ILE B 1 282 ? 28.760 -34.044 -38.083 1.00 37.94 ?  262 ILE B N     1 
ATOM   4825 C  CA    . ILE B 1 282 ? 27.502 -34.782 -37.988 1.00 37.41 ?  262 ILE B CA    1 
ATOM   4826 C  C     . ILE B 1 282 ? 26.351 -33.963 -38.568 1.00 38.39 ?  262 ILE B C     1 
ATOM   4827 O  O     . ILE B 1 282 ? 25.452 -34.503 -39.221 1.00 37.81 ?  262 ILE B O     1 
ATOM   4828 C  CB    . ILE B 1 282 ? 27.241 -35.201 -36.533 1.00 26.62 ?  262 ILE B CB    1 
ATOM   4829 C  CG1   . ILE B 1 282 ? 28.207 -36.315 -36.139 1.00 34.35 ?  262 ILE B CG1   1 
ATOM   4830 C  CG2   . ILE B 1 282 ? 25.801 -35.646 -36.332 1.00 21.03 ?  262 ILE B CG2   1 
ATOM   4831 C  CD1   . ILE B 1 282 ? 28.299 -36.539 -34.634 1.00 31.81 ?  262 ILE B CD1   1 
ATOM   4832 N  N     . ASN B 1 283 ? 26.363 -32.651 -38.350 1.00 37.78 ?  263 ASN B N     1 
ATOM   4833 C  CA    . ASN B 1 283 ? 25.374 -31.783 -38.979 1.00 37.57 ?  263 ASN B CA    1 
ATOM   4834 C  C     . ASN B 1 283 ? 25.386 -31.929 -40.501 1.00 43.95 ?  263 ASN B C     1 
ATOM   4835 O  O     . ASN B 1 283 ? 24.327 -32.032 -41.132 1.00 40.89 ?  263 ASN B O     1 
ATOM   4836 C  CB    . ASN B 1 283 ? 25.644 -30.339 -38.584 1.00 44.55 ?  263 ASN B CB    1 
ATOM   4837 C  CG    . ASN B 1 283 ? 24.487 -29.438 -38.884 1.00 52.12 ?  263 ASN B CG    1 
ATOM   4838 O  OD1   . ASN B 1 283 ? 23.647 -29.190 -38.015 1.00 55.33 ?  263 ASN B OD1   1 
ATOM   4839 N  ND2   . ASN B 1 283 ? 24.429 -28.931 -40.114 1.00 42.96 ?  263 ASN B ND2   1 
ATOM   4840 N  N     . GLN B 1 284 ? 26.582 -31.929 -41.109 1.00 39.83 ?  264 GLN B N     1 
ATOM   4841 C  CA    . GLN B 1 284 ? 26.690 -32.107 -42.554 1.00 34.86 ?  264 GLN B CA    1 
ATOM   4842 C  C     . GLN B 1 284 ? 26.195 -33.476 -42.980 1.00 43.26 ?  264 GLN B C     1 
ATOM   4843 O  O     . GLN B 1 284 ? 25.545 -33.608 -44.028 1.00 39.83 ?  264 GLN B O     1 
ATOM   4844 C  CB    . GLN B 1 284 ? 28.133 -31.938 -43.019 1.00 37.76 ?  264 GLN B CB    1 
ATOM   4845 C  CG    . GLN B 1 284 ? 28.619 -30.517 -43.092 1.00 44.95 ?  264 GLN B CG    1 
ATOM   4846 C  CD    . GLN B 1 284 ? 30.009 -30.389 -42.502 1.00 59.00 ?  264 GLN B CD    1 
ATOM   4847 O  OE1   . GLN B 1 284 ? 30.352 -29.367 -41.900 1.00 61.57 ?  264 GLN B OE1   1 
ATOM   4848 N  NE2   . GLN B 1 284 ? 30.820 -31.441 -42.660 1.00 55.45 ?  264 GLN B NE2   1 
ATOM   4849 N  N     . LYS B 1 285 ? 26.517 -34.513 -42.193 1.00 37.29 ?  265 LYS B N     1 
ATOM   4850 C  CA    . LYS B 1 285 ? 26.183 -35.877 -42.578 1.00 33.72 ?  265 LYS B CA    1 
ATOM   4851 C  C     . LYS B 1 285 ? 24.725 -36.196 -42.308 1.00 35.12 ?  265 LYS B C     1 
ATOM   4852 O  O     . LYS B 1 285 ? 24.146 -37.035 -43.000 1.00 50.58 ?  265 LYS B O     1 
ATOM   4853 C  CB    . LYS B 1 285 ? 27.080 -36.878 -41.857 1.00 33.61 ?  265 LYS B CB    1 
ATOM   4854 C  CG    . LYS B 1 285 ? 28.566 -36.768 -42.181 1.00 30.49 ?  265 LYS B CG    1 
ATOM   4855 C  CD    . LYS B 1 285 ? 28.828 -36.935 -43.656 1.00 43.06 ?  265 LYS B CD    1 
ATOM   4856 C  CE    . LYS B 1 285 ? 29.867 -35.952 -44.149 1.00 41.97 ?  265 LYS B CE    1 
ATOM   4857 N  NZ    . LYS B 1 285 ? 30.172 -36.184 -45.591 1.00 42.52 ?  265 LYS B NZ    1 
ATOM   4858 N  N     . PHE B 1 286 ? 24.117 -35.557 -41.312 1.00 41.54 ?  266 PHE B N     1 
ATOM   4859 C  CA    . PHE B 1 286 ? 22.667 -35.636 -41.185 1.00 41.79 ?  266 PHE B CA    1 
ATOM   4860 C  C     . PHE B 1 286 ? 21.999 -35.143 -42.460 1.00 45.87 ?  266 PHE B C     1 
ATOM   4861 O  O     . PHE B 1 286 ? 21.033 -35.749 -42.939 1.00 49.22 ?  266 PHE B O     1 
ATOM   4862 C  CB    . PHE B 1 286 ? 22.190 -34.821 -39.979 1.00 31.07 ?  266 PHE B CB    1 
ATOM   4863 C  CG    . PHE B 1 286 ? 22.207 -35.583 -38.675 1.00 39.96 ?  266 PHE B CG    1 
ATOM   4864 C  CD1   . PHE B 1 286 ? 22.661 -36.893 -38.619 1.00 45.71 ?  266 PHE B CD1   1 
ATOM   4865 C  CD2   . PHE B 1 286 ? 21.766 -34.989 -37.505 1.00 35.16 ?  266 PHE B CD2   1 
ATOM   4866 C  CE1   . PHE B 1 286 ? 22.681 -37.591 -37.414 1.00 42.39 ?  266 PHE B CE1   1 
ATOM   4867 C  CE2   . PHE B 1 286 ? 21.782 -35.679 -36.306 1.00 42.30 ?  266 PHE B CE2   1 
ATOM   4868 C  CZ    . PHE B 1 286 ? 22.238 -36.982 -36.263 1.00 36.40 ?  266 PHE B CZ    1 
ATOM   4869 N  N     . ALA B 1 287 ? 22.520 -34.054 -43.033 1.00 40.13 ?  267 ALA B N     1 
ATOM   4870 C  CA    . ALA B 1 287 ? 21.956 -33.495 -44.256 1.00 46.34 ?  267 ALA B CA    1 
ATOM   4871 C  C     . ALA B 1 287 ? 22.074 -34.483 -45.409 1.00 49.05 ?  267 ALA B C     1 
ATOM   4872 O  O     . ALA B 1 287 ? 21.073 -34.875 -46.019 1.00 53.01 ?  267 ALA B O     1 
ATOM   4873 C  CB    . ALA B 1 287 ? 22.659 -32.181 -44.603 1.00 37.44 ?  267 ALA B CB    1 
ATOM   4874 N  N     . GLU B 1 288 ? 23.301 -34.904 -45.709 1.00 42.19 ?  268 GLU B N     1 
ATOM   4875 C  CA    . GLU B 1 288 ? 23.533 -35.788 -46.842 1.00 50.42 ?  268 GLU B CA    1 
ATOM   4876 C  C     . GLU B 1 288 ? 22.873 -37.153 -46.651 1.00 52.92 ?  268 GLU B C     1 
ATOM   4877 O  O     . GLU B 1 288 ? 22.563 -37.817 -47.641 1.00 50.27 ?  268 GLU B O     1 
ATOM   4878 C  CB    . GLU B 1 288 ? 25.045 -35.906 -47.073 1.00 48.17 ?  268 GLU B CB    1 
ATOM   4879 C  CG    . GLU B 1 288 ? 25.542 -37.231 -47.635 1.00 45.59 ?  268 GLU B CG    1 
ATOM   4880 C  CD    . GLU B 1 288 ? 27.053 -37.243 -47.800 1.00 51.59 ?  268 GLU B CD    1 
ATOM   4881 O  OE1   . GLU B 1 288 ? 27.663 -36.151 -47.670 1.00 56.10 ?  268 GLU B OE1   1 
ATOM   4882 O  OE2   . GLU B 1 288 ? 27.622 -38.332 -48.060 1.00 42.99 ?  268 GLU B OE2   1 
ATOM   4883 N  N     . PHE B 1 289 ? 22.615 -37.573 -45.407 1.00 52.26 ?  269 PHE B N     1 
ATOM   4884 C  CA    . PHE B 1 289 ? 21.903 -38.829 -45.182 1.00 46.90 ?  269 PHE B CA    1 
ATOM   4885 C  C     . PHE B 1 289 ? 20.428 -38.717 -45.559 1.00 55.28 ?  269 PHE B C     1 
ATOM   4886 O  O     . PHE B 1 289 ? 19.819 -39.714 -45.965 1.00 59.59 ?  269 PHE B O     1 
ATOM   4887 C  CB    . PHE B 1 289 ? 22.070 -39.263 -43.724 1.00 47.65 ?  269 PHE B CB    1 
ATOM   4888 C  CG    . PHE B 1 289 ? 21.476 -40.611 -43.400 1.00 45.18 ?  269 PHE B CG    1 
ATOM   4889 C  CD1   . PHE B 1 289 ? 22.291 -41.729 -43.304 1.00 50.33 ?  269 PHE B CD1   1 
ATOM   4890 C  CD2   . PHE B 1 289 ? 20.128 -40.750 -43.108 1.00 50.35 ?  269 PHE B CD2   1 
ATOM   4891 C  CE1   . PHE B 1 289 ? 21.761 -42.977 -42.992 1.00 52.09 ?  269 PHE B CE1   1 
ATOM   4892 C  CE2   . PHE B 1 289 ? 19.589 -41.992 -42.790 1.00 56.36 ?  269 PHE B CE2   1 
ATOM   4893 C  CZ    . PHE B 1 289 ? 20.408 -43.105 -42.727 1.00 58.14 ?  269 PHE B CZ    1 
ATOM   4894 N  N     . GLY B 1 290 ? 19.840 -37.527 -45.446 1.00 49.68 ?  270 GLY B N     1 
ATOM   4895 C  CA    . GLY B 1 290 ? 18.450 -37.341 -45.819 1.00 50.05 ?  270 GLY B CA    1 
ATOM   4896 C  C     . GLY B 1 290 ? 18.233 -36.926 -47.265 1.00 56.29 ?  270 GLY B C     1 
ATOM   4897 O  O     . GLY B 1 290 ? 17.141 -36.473 -47.626 1.00 55.74 ?  270 GLY B O     1 
ATOM   4898 N  N     . SER B 1 291 ? 19.256 -37.083 -48.108 1.00 47.51 ?  271 SER B N     1 
ATOM   4899 C  CA    . SER B 1 291 ? 19.162 -36.647 -49.498 1.00 54.18 ?  271 SER B CA    1 
ATOM   4900 C  C     . SER B 1 291 ? 19.854 -37.556 -50.509 1.00 55.84 ?  271 SER B C     1 
ATOM   4901 O  O     . SER B 1 291 ? 19.680 -37.334 -51.711 1.00 61.84 ?  271 SER B O     1 
ATOM   4902 C  CB    . SER B 1 291 ? 19.724 -35.222 -49.642 1.00 50.33 ?  271 SER B CB    1 
ATOM   4903 O  OG    . SER B 1 291 ? 21.141 -35.227 -49.717 1.00 53.89 ?  271 SER B OG    1 
ATOM   4904 N  N     . VAL B 1 292 ? 20.615 -38.562 -50.088 1.00 55.80 ?  272 VAL B N     1 
ATOM   4905 C  CA    . VAL B 1 292 ? 21.309 -39.450 -51.005 1.00 54.24 ?  272 VAL B CA    1 
ATOM   4906 C  C     . VAL B 1 292 ? 20.658 -40.831 -50.962 1.00 58.99 ?  272 VAL B C     1 
ATOM   4907 O  O     . VAL B 1 292 ? 19.766 -41.104 -50.156 1.00 56.18 ?  272 VAL B O     1 
ATOM   4908 C  CB    . VAL B 1 292 ? 22.823 -39.531 -50.707 1.00 49.76 ?  272 VAL B CB    1 
ATOM   4909 C  CG1   . VAL B 1 292 ? 23.410 -38.142 -50.569 1.00 45.60 ?  272 VAL B CG1   1 
ATOM   4910 C  CG2   . VAL B 1 292 ? 23.095 -40.358 -49.459 1.00 55.28 ?  272 VAL B CG2   1 
ATOM   4911 N  N     . GLU B 1 293 ? 21.106 -41.705 -51.863 1.00 60.77 ?  273 GLU B N     1 
ATOM   4912 C  CA    . GLU B 1 293 ? 20.607 -43.076 -51.908 1.00 70.42 ?  273 GLU B CA    1 
ATOM   4913 C  C     . GLU B 1 293 ? 21.189 -43.856 -50.735 1.00 65.59 ?  273 GLU B C     1 
ATOM   4914 O  O     . GLU B 1 293 ? 22.386 -44.161 -50.709 1.00 62.48 ?  273 GLU B O     1 
ATOM   4915 C  CB    . GLU B 1 293 ? 20.957 -43.732 -53.243 1.00 81.34 ?  273 GLU B CB    1 
ATOM   4916 C  CG    . GLU B 1 293 ? 19.973 -43.441 -54.392 1.00 85.95 ?  273 GLU B CG    1 
ATOM   4917 C  CD    . GLU B 1 293 ? 18.520 -43.794 -54.059 1.00 89.97 ?  273 GLU B CD    1 
ATOM   4918 O  OE1   . GLU B 1 293 ? 17.823 -42.979 -53.407 1.00 84.48 ?  273 GLU B OE1   1 
ATOM   4919 O  OE2   . GLU B 1 293 ? 18.075 -44.894 -54.452 1.00 96.52 ?  273 GLU B OE2   1 
ATOM   4920 N  N     . ILE B 1 294 ? 20.339 -44.179 -49.762 1.00 59.94 ?  274 ILE B N     1 
ATOM   4921 C  CA    . ILE B 1 294 ? 20.761 -44.803 -48.515 1.00 56.09 ?  274 ILE B CA    1 
ATOM   4922 C  C     . ILE B 1 294 ? 21.169 -46.257 -48.749 1.00 58.61 ?  274 ILE B C     1 
ATOM   4923 O  O     . ILE B 1 294 ? 20.365 -47.178 -48.574 1.00 59.81 ?  274 ILE B O     1 
ATOM   4924 C  CB    . ILE B 1 294 ? 19.639 -44.666 -47.466 1.00 62.27 ?  274 ILE B CB    1 
ATOM   4925 C  CG1   . ILE B 1 294 ? 19.367 -43.176 -47.216 1.00 60.20 ?  274 ILE B CG1   1 
ATOM   4926 C  CG2   . ILE B 1 294 ? 19.973 -45.401 -46.154 1.00 58.79 ?  274 ILE B CG2   1 
ATOM   4927 C  CD1   . ILE B 1 294 ? 18.238 -42.900 -46.256 1.00 59.99 ?  274 ILE B CD1   1 
ATOM   4928 N  N     . THR B 1 295 ? 22.422 -46.476 -49.149 1.00 54.19 ?  275 THR B N     1 
ATOM   4929 C  CA    . THR B 1 295 ? 22.901 -47.830 -49.376 1.00 47.03 ?  275 THR B CA    1 
ATOM   4930 C  C     . THR B 1 295 ? 23.283 -48.484 -48.053 1.00 48.36 ?  275 THR B C     1 
ATOM   4931 O  O     . THR B 1 295 ? 23.096 -47.925 -46.970 1.00 50.89 ?  275 THR B O     1 
ATOM   4932 C  CB    . THR B 1 295 ? 24.094 -47.842 -50.329 1.00 48.98 ?  275 THR B CB    1 
ATOM   4933 O  OG1   . THR B 1 295 ? 25.249 -47.324 -49.661 1.00 54.52 ?  275 THR B OG1   1 
ATOM   4934 C  CG2   . THR B 1 295 ? 23.810 -47.007 -51.570 1.00 50.07 ?  275 THR B CG2   1 
ATOM   4935 N  N     . ASP B 1 296 ? 23.823 -49.699 -48.148 1.00 50.66 ?  276 ASP B N     1 
ATOM   4936 C  CA    . ASP B 1 296 ? 24.309 -50.392 -46.961 1.00 49.89 ?  276 ASP B CA    1 
ATOM   4937 C  C     . ASP B 1 296 ? 25.493 -49.655 -46.352 1.00 47.08 ?  276 ASP B C     1 
ATOM   4938 O  O     . ASP B 1 296 ? 25.570 -49.487 -45.130 1.00 47.01 ?  276 ASP B O     1 
ATOM   4939 C  CB    . ASP B 1 296 ? 24.707 -51.828 -47.317 1.00 56.07 ?  276 ASP B CB    1 
ATOM   4940 C  CG    . ASP B 1 296 ? 23.510 -52.754 -47.462 1.00 65.02 ?  276 ASP B CG    1 
ATOM   4941 O  OD1   . ASP B 1 296 ? 22.415 -52.400 -46.967 1.00 62.63 ?  276 ASP B OD1   1 
ATOM   4942 O  OD2   . ASP B 1 296 ? 23.671 -53.834 -48.075 1.00 59.60 ?  276 ASP B OD2   1 
ATOM   4943 N  N     . GLN B 1 297 ? 26.427 -49.214 -47.197 1.00 43.95 ?  277 GLN B N     1 
ATOM   4944 C  CA    . GLN B 1 297 ? 27.610 -48.510 -46.725 1.00 45.76 ?  277 GLN B CA    1 
ATOM   4945 C  C     . GLN B 1 297 ? 27.253 -47.150 -46.129 1.00 47.47 ?  277 GLN B C     1 
ATOM   4946 O  O     . GLN B 1 297 ? 27.951 -46.666 -45.231 1.00 40.96 ?  277 GLN B O     1 
ATOM   4947 C  CB    . GLN B 1 297 ? 28.603 -48.373 -47.879 1.00 37.38 ?  277 GLN B CB    1 
ATOM   4948 C  CG    . GLN B 1 297 ? 29.963 -47.808 -47.511 1.00 40.09 ?  277 GLN B CG    1 
ATOM   4949 C  CD    . GLN B 1 297 ? 30.751 -48.680 -46.556 1.00 49.36 ?  277 GLN B CD    1 
ATOM   4950 O  OE1   . GLN B 1 297 ? 31.184 -49.780 -46.908 1.00 54.62 ?  277 GLN B OE1   1 
ATOM   4951 N  NE2   . GLN B 1 297 ? 30.971 -48.177 -45.343 1.00 45.53 ?  277 GLN B NE2   1 
ATOM   4952 N  N     . VAL B 1 298 ? 26.167 -46.532 -46.595 1.00 40.64 ?  278 VAL B N     1 
ATOM   4953 C  CA    . VAL B 1 298 ? 25.739 -45.256 -46.031 1.00 39.69 ?  278 VAL B CA    1 
ATOM   4954 C  C     . VAL B 1 298 ? 25.297 -45.431 -44.583 1.00 43.44 ?  278 VAL B C     1 
ATOM   4955 O  O     . VAL B 1 298 ? 25.619 -44.609 -43.717 1.00 41.78 ?  278 VAL B O     1 
ATOM   4956 C  CB    . VAL B 1 298 ? 24.626 -44.644 -46.901 1.00 47.47 ?  278 VAL B CB    1 
ATOM   4957 C  CG1   . VAL B 1 298 ? 23.826 -43.612 -46.113 1.00 46.48 ?  278 VAL B CG1   1 
ATOM   4958 C  CG2   . VAL B 1 298 ? 25.220 -44.033 -48.169 1.00 48.26 ?  278 VAL B CG2   1 
ATOM   4959 N  N     . ILE B 1 299 ? 24.555 -46.501 -44.297 1.00 42.79 ?  279 ILE B N     1 
ATOM   4960 C  CA    . ILE B 1 299 ? 24.179 -46.797 -42.919 1.00 45.29 ?  279 ILE B CA    1 
ATOM   4961 C  C     . ILE B 1 299 ? 25.415 -47.119 -42.094 1.00 45.13 ?  279 ILE B C     1 
ATOM   4962 O  O     . ILE B 1 299 ? 25.583 -46.614 -40.978 1.00 48.48 ?  279 ILE B O     1 
ATOM   4963 C  CB    . ILE B 1 299 ? 23.157 -47.945 -42.873 1.00 46.35 ?  279 ILE B CB    1 
ATOM   4964 C  CG1   . ILE B 1 299 ? 21.763 -47.412 -43.183 1.00 50.67 ?  279 ILE B CG1   1 
ATOM   4965 C  CG2   . ILE B 1 299 ? 23.155 -48.608 -41.513 1.00 43.17 ?  279 ILE B CG2   1 
ATOM   4966 C  CD1   . ILE B 1 299 ? 20.868 -48.437 -43.803 1.00 50.18 ?  279 ILE B CD1   1 
ATOM   4967 N  N     . LYS B 1 300 ? 26.299 -47.962 -42.629 1.00 40.93 ?  280 LYS B N     1 
ATOM   4968 C  CA    . LYS B 1 300 ? 27.546 -48.247 -41.933 1.00 39.75 ?  280 LYS B CA    1 
ATOM   4969 C  C     . LYS B 1 300 ? 28.318 -46.962 -41.636 1.00 45.32 ?  280 LYS B C     1 
ATOM   4970 O  O     . LYS B 1 300 ? 28.862 -46.798 -40.537 1.00 38.58 ?  280 LYS B O     1 
ATOM   4971 C  CB    . LYS B 1 300 ? 28.386 -49.225 -42.752 1.00 43.33 ?  280 LYS B CB    1 
ATOM   4972 C  CG    . LYS B 1 300 ? 27.716 -50.578 -42.967 1.00 43.51 ?  280 LYS B CG    1 
ATOM   4973 C  CD    . LYS B 1 300 ? 28.634 -51.730 -42.579 1.00 48.91 ?  280 LYS B CD    1 
ATOM   4974 C  CE    . LYS B 1 300 ? 29.575 -52.131 -43.713 1.00 51.94 ?  280 LYS B CE    1 
ATOM   4975 N  NZ    . LYS B 1 300 ? 30.855 -52.727 -43.215 1.00 56.06 ?  280 LYS B NZ    1 
ATOM   4976 N  N     . GLY B 1 301 ? 28.343 -46.024 -42.591 1.00 45.55 ?  281 GLY B N     1 
ATOM   4977 C  CA    . GLY B 1 301 ? 29.011 -44.750 -42.360 1.00 38.91 ?  281 GLY B CA    1 
ATOM   4978 C  C     . GLY B 1 301 ? 28.367 -43.947 -41.244 1.00 45.95 ?  281 GLY B C     1 
ATOM   4979 O  O     . GLY B 1 301 ? 29.046 -43.451 -40.339 1.00 39.15 ?  281 GLY B O     1 
ATOM   4980 N  N     . MET B 1 302 ? 27.043 -43.805 -41.289 1.00 44.93 ?  282 MET B N     1 
ATOM   4981 C  CA    . MET B 1 302 ? 26.371 -43.116 -40.200 1.00 39.89 ?  282 MET B CA    1 
ATOM   4982 C  C     . MET B 1 302 ? 26.484 -43.882 -38.892 1.00 42.78 ?  282 MET B C     1 
ATOM   4983 O  O     . MET B 1 302 ? 26.437 -43.276 -37.815 1.00 47.12 ?  282 MET B O     1 
ATOM   4984 C  CB    . MET B 1 302 ? 24.910 -42.845 -40.557 1.00 41.06 ?  282 MET B CB    1 
ATOM   4985 C  CG    . MET B 1 302 ? 24.137 -42.173 -39.421 1.00 44.23 ?  282 MET B CG    1 
ATOM   4986 S  SD    . MET B 1 302 ? 24.509 -40.411 -39.295 1.00 54.79 ?  282 MET B SD    1 
ATOM   4987 C  CE    . MET B 1 302 ? 23.504 -39.640 -40.555 1.00 48.47 ?  282 MET B CE    1 
ATOM   4988 N  N     . GLU B 1 303 ? 26.657 -45.196 -38.954 1.00 39.17 ?  283 GLU B N     1 
ATOM   4989 C  CA    . GLU B 1 303 ? 26.814 -45.947 -37.719 1.00 43.89 ?  283 GLU B CA    1 
ATOM   4990 C  C     . GLU B 1 303 ? 28.201 -45.780 -37.108 1.00 42.59 ?  283 GLU B C     1 
ATOM   4991 O  O     . GLU B 1 303 ? 28.360 -45.988 -35.902 1.00 37.76 ?  283 GLU B O     1 
ATOM   4992 C  CB    . GLU B 1 303 ? 26.506 -47.421 -37.960 1.00 45.56 ?  283 GLU B CB    1 
ATOM   4993 C  CG    . GLU B 1 303 ? 25.061 -47.749 -37.670 1.00 51.09 ?  283 GLU B CG    1 
ATOM   4994 C  CD    . GLU B 1 303 ? 24.699 -49.193 -37.947 1.00 62.07 ?  283 GLU B CD    1 
ATOM   4995 O  OE1   . GLU B 1 303 ? 25.538 -49.948 -38.500 1.00 53.18 ?  283 GLU B OE1   1 
ATOM   4996 O  OE2   . GLU B 1 303 ? 23.566 -49.573 -37.580 1.00 64.93 ?  283 GLU B OE2   1 
ATOM   4997 N  N     . SER B 1 304 ? 29.205 -45.402 -37.899 1.00 41.15 ?  284 SER B N     1 
ATOM   4998 C  CA    . SER B 1 304 ? 30.524 -45.179 -37.325 1.00 36.51 ?  284 SER B CA    1 
ATOM   4999 C  C     . SER B 1 304 ? 30.634 -43.818 -36.649 1.00 35.05 ?  284 SER B C     1 
ATOM   5000 O  O     . SER B 1 304 ? 31.469 -43.655 -35.756 1.00 35.44 ?  284 SER B O     1 
ATOM   5001 C  CB    . SER B 1 304 ? 31.606 -45.339 -38.397 1.00 34.83 ?  284 SER B CB    1 
ATOM   5002 O  OG    . SER B 1 304 ? 31.501 -44.326 -39.386 1.00 35.94 ?  284 SER B OG    1 
ATOM   5003 N  N     . LEU B 1 305 ? 29.810 -42.846 -37.045 1.00 32.40 ?  285 LEU B N     1 
ATOM   5004 C  CA    . LEU B 1 305 ? 29.732 -41.607 -36.290 1.00 27.10 ?  285 LEU B CA    1 
ATOM   5005 C  C     . LEU B 1 305 ? 29.129 -41.855 -34.921 1.00 34.06 ?  285 LEU B C     1 
ATOM   5006 O  O     . LEU B 1 305 ? 29.586 -41.287 -33.922 1.00 36.63 ?  285 LEU B O     1 
ATOM   5007 C  CB    . LEU B 1 305 ? 28.917 -40.575 -37.055 1.00 28.93 ?  285 LEU B CB    1 
ATOM   5008 C  CG    . LEU B 1 305 ? 29.624 -40.015 -38.285 1.00 33.87 ?  285 LEU B CG    1 
ATOM   5009 C  CD1   . LEU B 1 305 ? 28.715 -39.050 -39.030 1.00 28.99 ?  285 LEU B CD1   1 
ATOM   5010 C  CD2   . LEU B 1 305 ? 30.927 -39.344 -37.872 1.00 30.95 ?  285 LEU B CD2   1 
ATOM   5011 N  N     . LEU B 1 306 ? 28.126 -42.735 -34.851 1.00 39.99 ?  286 LEU B N     1 
ATOM   5012 C  CA    . LEU B 1 306 ? 27.546 -43.113 -33.562 1.00 44.19 ?  286 LEU B CA    1 
ATOM   5013 C  C     . LEU B 1 306 ? 28.531 -43.874 -32.678 1.00 36.20 ?  286 LEU B C     1 
ATOM   5014 O  O     . LEU B 1 306 ? 28.421 -43.816 -31.450 1.00 39.76 ?  286 LEU B O     1 
ATOM   5015 C  CB    . LEU B 1 306 ? 26.280 -43.942 -33.779 1.00 45.41 ?  286 LEU B CB    1 
ATOM   5016 C  CG    . LEU B 1 306 ? 25.622 -44.482 -32.510 1.00 48.51 ?  286 LEU B CG    1 
ATOM   5017 C  CD1   . LEU B 1 306 ? 24.536 -43.526 -32.053 1.00 48.46 ?  286 LEU B CD1   1 
ATOM   5018 C  CD2   . LEU B 1 306 ? 25.034 -45.868 -32.756 1.00 46.21 ?  286 LEU B CD2   1 
ATOM   5019 N  N     . SER B 1 307 ? 29.495 -44.579 -33.273 1.00 28.56 ?  287 SER B N     1 
ATOM   5020 C  CA    . SER B 1 307 ? 30.512 -45.272 -32.487 1.00 32.88 ?  287 SER B CA    1 
ATOM   5021 C  C     . SER B 1 307 ? 31.530 -44.306 -31.891 1.00 36.23 ?  287 SER B C     1 
ATOM   5022 O  O     . SER B 1 307 ? 32.073 -44.570 -30.812 1.00 37.33 ?  287 SER B O     1 
ATOM   5023 C  CB    . SER B 1 307 ? 31.234 -46.310 -33.345 1.00 34.19 ?  287 SER B CB    1 
ATOM   5024 O  OG    . SER B 1 307 ? 30.351 -47.343 -33.747 1.00 40.97 ?  287 SER B OG    1 
ATOM   5025 N  N     . VAL B 1 308 ? 31.823 -43.201 -32.576 1.00 35.32 ?  288 VAL B N     1 
ATOM   5026 C  CA    . VAL B 1 308 ? 32.692 -42.192 -31.982 1.00 37.37 ?  288 VAL B CA    1 
ATOM   5027 C  C     . VAL B 1 308 ? 31.987 -41.521 -30.812 1.00 36.29 ?  288 VAL B C     1 
ATOM   5028 O  O     . VAL B 1 308 ? 32.526 -41.419 -29.700 1.00 30.96 ?  288 VAL B O     1 
ATOM   5029 C  CB    . VAL B 1 308 ? 33.122 -41.161 -33.035 1.00 34.45 ?  288 VAL B CB    1 
ATOM   5030 C  CG1   . VAL B 1 308 ? 33.672 -39.919 -32.330 1.00 27.65 ?  288 VAL B CG1   1 
ATOM   5031 C  CG2   . VAL B 1 308 ? 34.147 -41.775 -33.972 1.00 34.91 ?  288 VAL B CG2   1 
ATOM   5032 N  N     . ILE B 1 309 ? 30.757 -41.073 -31.048 1.00 32.84 ?  289 ILE B N     1 
ATOM   5033 C  CA    . ILE B 1 309 ? 29.989 -40.417 -30.003 1.00 30.01 ?  289 ILE B CA    1 
ATOM   5034 C  C     . ILE B 1 309 ? 29.870 -41.324 -28.783 1.00 29.29 ?  289 ILE B C     1 
ATOM   5035 O  O     . ILE B 1 309 ? 29.956 -40.868 -27.637 1.00 33.36 ?  289 ILE B O     1 
ATOM   5036 C  CB    . ILE B 1 309 ? 28.617 -40.007 -30.571 1.00 34.26 ?  289 ILE B CB    1 
ATOM   5037 C  CG1   . ILE B 1 309 ? 28.812 -38.878 -31.587 1.00 30.81 ?  289 ILE B CG1   1 
ATOM   5038 C  CG2   . ILE B 1 309 ? 27.640 -39.640 -29.461 1.00 39.57 ?  289 ILE B CG2   1 
ATOM   5039 C  CD1   . ILE B 1 309 ? 28.813 -37.499 -30.994 1.00 30.99 ?  289 ILE B CD1   1 
ATOM   5040 N  N     . GLN B 1 310 ? 29.713 -42.627 -29.006 1.00 37.25 ?  290 GLN B N     1 
ATOM   5041 C  CA    . GLN B 1 310 ? 29.513 -43.539 -27.891 1.00 30.43 ?  290 GLN B CA    1 
ATOM   5042 C  C     . GLN B 1 310 ? 30.797 -43.864 -27.155 1.00 33.18 ?  290 GLN B C     1 
ATOM   5043 O  O     . GLN B 1 310 ? 30.720 -44.232 -25.979 1.00 38.83 ?  290 GLN B O     1 
ATOM   5044 C  CB    . GLN B 1 310 ? 28.844 -44.823 -28.364 1.00 32.12 ?  290 GLN B CB    1 
ATOM   5045 C  CG    . GLN B 1 310 ? 27.347 -44.672 -28.452 1.00 33.18 ?  290 GLN B CG    1 
ATOM   5046 C  CD    . GLN B 1 310 ? 26.656 -45.896 -28.996 1.00 38.77 ?  290 GLN B CD    1 
ATOM   5047 O  OE1   . GLN B 1 310 ? 27.250 -46.691 -29.734 1.00 33.76 ?  290 GLN B OE1   1 
ATOM   5048 N  NE2   . GLN B 1 310 ? 25.381 -46.040 -28.662 1.00 35.34 ?  290 GLN B NE2   1 
ATOM   5049 N  N     . VAL B 1 311 ? 31.966 -43.724 -27.794 1.00 30.66 ?  291 VAL B N     1 
ATOM   5050 C  CA    . VAL B 1 311 ? 33.212 -43.781 -27.020 1.00 26.03 ?  291 VAL B CA    1 
ATOM   5051 C  C     . VAL B 1 311 ? 33.347 -42.545 -26.139 1.00 34.81 ?  291 VAL B C     1 
ATOM   5052 O  O     . VAL B 1 311 ? 33.883 -42.626 -25.023 1.00 33.06 ?  291 VAL B O     1 
ATOM   5053 C  CB    . VAL B 1 311 ? 34.449 -43.947 -27.923 1.00 32.21 ?  291 VAL B CB    1 
ATOM   5054 C  CG1   . VAL B 1 311 ? 35.676 -44.103 -27.092 1.00 25.69 ?  291 VAL B CG1   1 
ATOM   5055 C  CG2   . VAL B 1 311 ? 34.319 -45.174 -28.832 1.00 41.10 ?  291 VAL B CG2   1 
ATOM   5056 N  N     . LEU B 1 312 ? 32.860 -41.388 -26.603 1.00 29.91 ?  292 LEU B N     1 
ATOM   5057 C  CA    . LEU B 1 312 ? 32.884 -40.198 -25.756 1.00 26.71 ?  292 LEU B CA    1 
ATOM   5058 C  C     . LEU B 1 312 ? 32.083 -40.425 -24.469 1.00 32.99 ?  292 LEU B C     1 
ATOM   5059 O  O     . LEU B 1 312 ? 32.469 -39.961 -23.385 1.00 27.34 ?  292 LEU B O     1 
ATOM   5060 C  CB    . LEU B 1 312 ? 32.350 -38.990 -26.539 1.00 26.97 ?  292 LEU B CB    1 
ATOM   5061 C  CG    . LEU B 1 312 ? 33.223 -38.446 -27.681 1.00 27.81 ?  292 LEU B CG    1 
ATOM   5062 C  CD1   . LEU B 1 312 ? 32.443 -37.562 -28.672 1.00 22.30 ?  292 LEU B CD1   1 
ATOM   5063 C  CD2   . LEU B 1 312 ? 34.440 -37.721 -27.131 1.00 27.05 ?  292 LEU B CD2   1 
ATOM   5064 N  N     . LEU B 1 313 ? 30.975 -41.163 -24.564 1.00 31.96 ?  293 LEU B N     1 
ATOM   5065 C  CA    . LEU B 1 313 ? 30.148 -41.390 -23.387 1.00 31.82 ?  293 LEU B CA    1 
ATOM   5066 C  C     . LEU B 1 313 ? 30.834 -42.327 -22.397 1.00 29.91 ?  293 LEU B C     1 
ATOM   5067 O  O     . LEU B 1 313 ? 30.798 -42.090 -21.183 1.00 32.73 ?  293 LEU B O     1 
ATOM   5068 C  CB    . LEU B 1 313 ? 28.794 -41.933 -23.818 1.00 24.23 ?  293 LEU B CB    1 
ATOM   5069 C  CG    . LEU B 1 313 ? 28.061 -40.961 -24.719 1.00 23.47 ?  293 LEU B CG    1 
ATOM   5070 C  CD1   . LEU B 1 313 ? 26.994 -41.685 -25.502 1.00 28.62 ?  293 LEU B CD1   1 
ATOM   5071 C  CD2   . LEU B 1 313 ? 27.468 -39.824 -23.898 1.00 30.27 ?  293 LEU B CD2   1 
ATOM   5072 N  N     . LYS B 1 314 ? 31.466 -43.390 -22.896 1.00 28.57 ?  294 LYS B N     1 
ATOM   5073 C  CA    . LYS B 1 314 ? 32.316 -44.236 -22.065 1.00 31.16 ?  294 LYS B CA    1 
ATOM   5074 C  C     . LYS B 1 314 ? 33.365 -43.431 -21.305 1.00 26.10 ?  294 LYS B C     1 
ATOM   5075 O  O     . LYS B 1 314 ? 33.937 -43.928 -20.334 1.00 27.56 ?  294 LYS B O     1 
ATOM   5076 C  CB    . LYS B 1 314 ? 33.004 -45.291 -22.951 1.00 28.12 ?  294 LYS B CB    1 
ATOM   5077 C  CG    . LYS B 1 314 ? 32.233 -46.582 -23.049 1.00 37.76 ?  294 LYS B CG    1 
ATOM   5078 C  CD    . LYS B 1 314 ? 31.464 -46.679 -24.364 1.00 39.00 ?  294 LYS B CD    1 
ATOM   5079 C  CE    . LYS B 1 314 ? 31.015 -48.110 -24.633 1.00 43.40 ?  294 LYS B CE    1 
ATOM   5080 N  NZ    . LYS B 1 314 ? 30.307 -48.327 -25.933 1.00 51.26 ?  294 LYS B NZ    1 
ATOM   5081 N  N     . PHE B 1 315 ? 33.664 -42.219 -21.750 1.00 26.83 ?  295 PHE B N     1 
ATOM   5082 C  CA    . PHE B 1 315 ? 34.576 -41.368 -21.006 1.00 28.90 ?  295 PHE B CA    1 
ATOM   5083 C  C     . PHE B 1 315 ? 33.812 -40.448 -20.068 1.00 26.92 ?  295 PHE B C     1 
ATOM   5084 O  O     . PHE B 1 315 ? 34.205 -40.275 -18.914 1.00 28.81 ?  295 PHE B O     1 
ATOM   5085 C  CB    . PHE B 1 315 ? 35.455 -40.507 -21.938 1.00 29.47 ?  295 PHE B CB    1 
ATOM   5086 C  CG    . PHE B 1 315 ? 36.139 -39.378 -21.211 1.00 26.03 ?  295 PHE B CG    1 
ATOM   5087 C  CD1   . PHE B 1 315 ? 35.502 -38.147 -21.030 1.00 29.48 ?  295 PHE B CD1   1 
ATOM   5088 C  CD2   . PHE B 1 315 ? 37.390 -39.562 -20.655 1.00 25.28 ?  295 PHE B CD2   1 
ATOM   5089 C  CE1   . PHE B 1 315 ? 36.103 -37.120 -20.303 1.00 28.92 ?  295 PHE B CE1   1 
ATOM   5090 C  CE2   . PHE B 1 315 ? 38.007 -38.534 -19.932 1.00 28.07 ?  295 PHE B CE2   1 
ATOM   5091 C  CZ    . PHE B 1 315 ? 37.358 -37.309 -19.754 1.00 23.91 ?  295 PHE B CZ    1 
ATOM   5092 N  N     . ARG B 1 316 ? 32.745 -39.817 -20.562 1.00 20.06 ?  296 ARG B N     1 
ATOM   5093 C  CA    . ARG B 1 316 ? 32.137 -38.747 -19.788 1.00 26.68 ?  296 ARG B CA    1 
ATOM   5094 C  C     . ARG B 1 316 ? 31.319 -39.288 -18.610 1.00 32.93 ?  296 ARG B C     1 
ATOM   5095 O  O     . ARG B 1 316 ? 31.301 -38.671 -17.537 1.00 25.86 ?  296 ARG B O     1 
ATOM   5096 C  CB    . ARG B 1 316 ? 31.298 -37.868 -20.702 1.00 26.33 ?  296 ARG B CB    1 
ATOM   5097 C  CG    . ARG B 1 316 ? 32.126 -37.194 -21.766 1.00 27.83 ?  296 ARG B CG    1 
ATOM   5098 C  CD    . ARG B 1 316 ? 31.453 -35.960 -22.334 1.00 25.30 ?  296 ARG B CD    1 
ATOM   5099 N  NE    . ARG B 1 316 ? 32.460 -35.051 -22.855 1.00 24.81 ?  296 ARG B NE    1 
ATOM   5100 C  CZ    . ARG B 1 316 ? 32.620 -34.766 -24.138 1.00 30.34 ?  296 ARG B CZ    1 
ATOM   5101 N  NH1   . ARG B 1 316 ? 31.760 -35.186 -25.053 1.00 32.30 ?  296 ARG B NH1   1 
ATOM   5102 N  NH2   . ARG B 1 316 ? 33.675 -34.047 -24.516 1.00 29.48 ?  296 ARG B NH2   1 
ATOM   5103 N  N     . LYS B 1 317 ? 30.659 -40.447 -18.779 1.00 31.33 ?  297 LYS B N     1 
ATOM   5104 C  CA    . LYS B 1 317 ? 29.872 -41.020 -17.683 1.00 27.29 ?  297 LYS B CA    1 
ATOM   5105 C  C     . LYS B 1 317 ? 30.719 -41.342 -16.461 1.00 31.69 ?  297 LYS B C     1 
ATOM   5106 O  O     . LYS B 1 317 ? 30.406 -40.840 -15.362 1.00 33.41 ?  297 LYS B O     1 
ATOM   5107 C  CB    . LYS B 1 317 ? 29.106 -42.245 -18.181 1.00 23.90 ?  297 LYS B CB    1 
ATOM   5108 C  CG    . LYS B 1 317 ? 27.799 -41.908 -18.836 1.00 29.19 ?  297 LYS B CG    1 
ATOM   5109 C  CD    . LYS B 1 317 ? 27.426 -42.969 -19.842 1.00 32.46 ?  297 LYS B CD    1 
ATOM   5110 C  CE    . LYS B 1 317 ? 26.022 -42.780 -20.398 1.00 33.55 ?  297 LYS B CE    1 
ATOM   5111 N  NZ    . LYS B 1 317 ? 25.736 -43.806 -21.450 1.00 40.04 ?  297 LYS B NZ    1 
ATOM   5112 N  N     . PRO B 1 318 ? 31.774 -42.163 -16.546 1.00 32.42 ?  298 PRO B N     1 
ATOM   5113 C  CA    . PRO B 1 318 ? 32.574 -42.400 -15.334 1.00 24.64 ?  298 PRO B CA    1 
ATOM   5114 C  C     . PRO B 1 318 ? 33.283 -41.147 -14.861 1.00 28.00 ?  298 PRO B C     1 
ATOM   5115 O  O     . PRO B 1 318 ? 33.437 -40.969 -13.649 1.00 30.47 ?  298 PRO B O     1 
ATOM   5116 C  CB    . PRO B 1 318 ? 33.559 -43.498 -15.759 1.00 21.70 ?  298 PRO B CB    1 
ATOM   5117 C  CG    . PRO B 1 318 ? 33.687 -43.328 -17.236 1.00 28.41 ?  298 PRO B CG    1 
ATOM   5118 C  CD    . PRO B 1 318 ? 32.329 -42.878 -17.714 1.00 27.06 ?  298 PRO B CD    1 
ATOM   5119 N  N     . HIS B 1 319 ? 33.692 -40.264 -15.786 1.00 34.24 ?  299 HIS B N     1 
ATOM   5120 C  CA    . HIS B 1 319 ? 34.286 -38.986 -15.398 1.00 26.37 ?  299 HIS B CA    1 
ATOM   5121 C  C     . HIS B 1 319 ? 33.329 -38.181 -14.530 1.00 25.64 ?  299 HIS B C     1 
ATOM   5122 O  O     . HIS B 1 319 ? 33.744 -37.551 -13.548 1.00 23.99 ?  299 HIS B O     1 
ATOM   5123 C  CB    . HIS B 1 319 ? 34.692 -38.180 -16.639 1.00 21.98 ?  299 HIS B CB    1 
ATOM   5124 C  CG    . HIS B 1 319 ? 35.322 -36.856 -16.319 1.00 21.05 ?  299 HIS B CG    1 
ATOM   5125 N  ND1   . HIS B 1 319 ? 34.588 -35.699 -16.177 1.00 20.84 ?  299 HIS B ND1   1 
ATOM   5126 C  CD2   . HIS B 1 319 ? 36.612 -36.512 -16.092 1.00 19.41 ?  299 HIS B CD2   1 
ATOM   5127 C  CE1   . HIS B 1 319 ? 35.396 -34.700 -15.865 1.00 22.30 ?  299 HIS B CE1   1 
ATOM   5128 N  NE2   . HIS B 1 319 ? 36.630 -35.168 -15.808 1.00 22.22 ?  299 HIS B NE2   1 
ATOM   5129 N  N     . PHE B 1 320 ? 32.045 -38.192 -14.875 1.00 24.16 ?  300 PHE B N     1 
ATOM   5130 C  CA    . PHE B 1 320 ? 31.055 -37.498 -14.063 1.00 27.76 ?  300 PHE B CA    1 
ATOM   5131 C  C     . PHE B 1 320 ? 31.005 -38.080 -12.649 1.00 32.73 ?  300 PHE B C     1 
ATOM   5132 O  O     . PHE B 1 320 ? 31.034 -37.341 -11.656 1.00 34.51 ?  300 PHE B O     1 
ATOM   5133 C  CB    . PHE B 1 320 ? 29.689 -37.573 -14.750 1.00 30.11 ?  300 PHE B CB    1 
ATOM   5134 C  CG    . PHE B 1 320 ? 28.624 -36.769 -14.071 1.00 32.90 ?  300 PHE B CG    1 
ATOM   5135 C  CD1   . PHE B 1 320 ? 28.507 -35.409 -14.310 1.00 30.63 ?  300 PHE B CD1   1 
ATOM   5136 C  CD2   . PHE B 1 320 ? 27.743 -37.372 -13.183 1.00 35.37 ?  300 PHE B CD2   1 
ATOM   5137 C  CE1   . PHE B 1 320 ? 27.534 -34.654 -13.676 1.00 33.48 ?  300 PHE B CE1   1 
ATOM   5138 C  CE2   . PHE B 1 320 ? 26.759 -36.617 -12.541 1.00 43.45 ?  300 PHE B CE2   1 
ATOM   5139 C  CZ    . PHE B 1 320 ? 26.656 -35.254 -12.792 1.00 39.28 ?  300 PHE B CZ    1 
ATOM   5140 N  N     . GLN B 1 321 ? 30.962 -39.410 -12.537 1.00 29.75 ?  301 GLN B N     1 
ATOM   5141 C  CA    . GLN B 1 321 ? 30.908 -40.028 -11.216 1.00 29.78 ?  301 GLN B CA    1 
ATOM   5142 C  C     . GLN B 1 321 ? 32.154 -39.700 -10.407 1.00 30.22 ?  301 GLN B C     1 
ATOM   5143 O  O     . GLN B 1 321 ? 32.063 -39.420 -9.207  1.00 32.20 ?  301 GLN B O     1 
ATOM   5144 C  CB    . GLN B 1 321 ? 30.736 -41.545 -11.343 1.00 30.31 ?  301 GLN B CB    1 
ATOM   5145 C  CG    . GLN B 1 321 ? 29.407 -41.994 -11.956 1.00 23.20 ?  301 GLN B CG    1 
ATOM   5146 C  CD    . GLN B 1 321 ? 28.199 -41.387 -11.248 1.00 34.44 ?  301 GLN B CD    1 
ATOM   5147 O  OE1   . GLN B 1 321 ? 27.273 -40.898 -11.896 1.00 28.53 ?  301 GLN B OE1   1 
ATOM   5148 N  NE2   . GLN B 1 321 ? 28.209 -41.414 -9.905  1.00 36.82 ?  301 GLN B NE2   1 
ATOM   5149 N  N     . LEU B 1 322 ? 33.326 -39.720 -11.049 1.00 25.58 ?  302 LEU B N     1 
ATOM   5150 C  CA    . LEU B 1 322 ? 34.564 -39.404 -10.341 1.00 27.94 ?  302 LEU B CA    1 
ATOM   5151 C  C     . LEU B 1 322 ? 34.588 -37.951 -9.860  1.00 31.60 ?  302 LEU B C     1 
ATOM   5152 O  O     . LEU B 1 322 ? 34.949 -37.675 -8.712  1.00 30.54 ?  302 LEU B O     1 
ATOM   5153 C  CB    . LEU B 1 322 ? 35.762 -39.683 -11.233 1.00 25.87 ?  302 LEU B CB    1 
ATOM   5154 C  CG    . LEU B 1 322 ? 37.041 -39.076 -10.669 1.00 28.41 ?  302 LEU B CG    1 
ATOM   5155 C  CD1   . LEU B 1 322 ? 37.483 -39.785 -9.398  1.00 22.30 ?  302 LEU B CD1   1 
ATOM   5156 C  CD2   . LEU B 1 322 ? 38.132 -39.129 -11.713 1.00 35.68 ?  302 LEU B CD2   1 
ATOM   5157 N  N     . ALA B 1 323 ? 34.221 -37.000 -10.721 1.00 24.02 ?  303 ALA B N     1 
ATOM   5158 C  CA    . ALA B 1 323 ? 34.143 -35.625 -10.248 1.00 27.98 ?  303 ALA B CA    1 
ATOM   5159 C  C     . ALA B 1 323 ? 33.061 -35.461 -9.183  1.00 37.28 ?  303 ALA B C     1 
ATOM   5160 O  O     . ALA B 1 323 ? 33.188 -34.619 -8.281  1.00 33.48 ?  303 ALA B O     1 
ATOM   5161 C  CB    . ALA B 1 323 ? 33.898 -34.672 -11.410 1.00 27.64 ?  303 ALA B CB    1 
ATOM   5162 N  N     . GLN B 1 324 ? 31.997 -36.256 -9.256  1.00 34.33 ?  304 GLN B N     1 
ATOM   5163 C  CA    . GLN B 1 324 ? 30.963 -36.143 -8.239  1.00 33.21 ?  304 GLN B CA    1 
ATOM   5164 C  C     . GLN B 1 324 ? 31.459 -36.649 -6.890  1.00 36.34 ?  304 GLN B C     1 
ATOM   5165 O  O     . GLN B 1 324 ? 31.200 -36.020 -5.860  1.00 32.69 ?  304 GLN B O     1 
ATOM   5166 C  CB    . GLN B 1 324 ? 29.711 -36.896 -8.665  1.00 33.67 ?  304 GLN B CB    1 
ATOM   5167 C  CG    . GLN B 1 324 ? 28.491 -36.529 -7.831  1.00 35.88 ?  304 GLN B CG    1 
ATOM   5168 C  CD    . GLN B 1 324 ? 27.210 -37.117 -8.389  1.00 40.20 ?  304 GLN B CD    1 
ATOM   5169 O  OE1   . GLN B 1 324 ? 27.003 -38.328 -8.342  1.00 41.12 ?  304 GLN B OE1   1 
ATOM   5170 N  NE2   . GLN B 1 324 ? 26.353 -36.264 -8.938  1.00 36.49 ?  304 GLN B NE2   1 
ATOM   5171 N  N     . ARG B 1 325 ? 32.165 -37.787 -6.874  1.00 34.65 ?  305 ARG B N     1 
ATOM   5172 C  CA    . ARG B 1 325 ? 32.687 -38.319 -5.617  1.00 30.21 ?  305 ARG B CA    1 
ATOM   5173 C  C     . ARG B 1 325 ? 33.730 -37.398 -4.997  1.00 32.91 ?  305 ARG B C     1 
ATOM   5174 O  O     . ARG B 1 325 ? 33.870 -37.364 -3.772  1.00 41.47 ?  305 ARG B O     1 
ATOM   5175 C  CB    . ARG B 1 325 ? 33.267 -39.709 -5.847  1.00 29.69 ?  305 ARG B CB    1 
ATOM   5176 C  CG    . ARG B 1 325 ? 32.245 -40.669 -6.436  1.00 38.01 ?  305 ARG B CG    1 
ATOM   5177 C  CD    . ARG B 1 325 ? 32.675 -42.102 -6.258  1.00 35.46 ?  305 ARG B CD    1 
ATOM   5178 N  NE    . ARG B 1 325 ? 33.943 -42.338 -6.936  1.00 40.64 ?  305 ARG B NE    1 
ATOM   5179 C  CZ    . ARG B 1 325 ? 34.060 -42.675 -8.214  1.00 37.29 ?  305 ARG B CZ    1 
ATOM   5180 N  NH1   . ARG B 1 325 ? 32.997 -42.858 -8.986  1.00 28.45 ?  305 ARG B NH1   1 
ATOM   5181 N  NH2   . ARG B 1 325 ? 35.275 -42.838 -8.729  1.00 29.68 ?  305 ARG B NH2   1 
ATOM   5182 N  N     . THR B 1 326 ? 34.436 -36.625 -5.819  1.00 37.84 ?  306 THR B N     1 
ATOM   5183 C  CA    . THR B 1 326 ? 35.494 -35.737 -5.352  1.00 34.94 ?  306 THR B CA    1 
ATOM   5184 C  C     . THR B 1 326 ? 34.941 -34.463 -4.728  1.00 34.46 ?  306 THR B C     1 
ATOM   5185 O  O     . THR B 1 326 ? 35.521 -33.927 -3.774  1.00 25.05 ?  306 THR B O     1 
ATOM   5186 C  CB    . THR B 1 326 ? 36.395 -35.378 -6.531  1.00 31.23 ?  306 THR B CB    1 
ATOM   5187 O  OG1   . THR B 1 326 ? 36.940 -36.578 -7.087  1.00 30.55 ?  306 THR B OG1   1 
ATOM   5188 C  CG2   . THR B 1 326 ? 37.525 -34.427 -6.105  1.00 29.30 ?  306 THR B CG2   1 
ATOM   5189 N  N     . LEU B 1 327 ? 33.847 -33.950 -5.287  1.00 39.93 ?  307 LEU B N     1 
ATOM   5190 C  CA    . LEU B 1 327 ? 33.272 -32.667 -4.908  1.00 35.19 ?  307 LEU B CA    1 
ATOM   5191 C  C     . LEU B 1 327 ? 32.122 -32.808 -3.919  1.00 30.85 ?  307 LEU B C     1 
ATOM   5192 O  O     . LEU B 1 327 ? 31.430 -31.826 -3.643  1.00 32.65 ?  307 LEU B O     1 
ATOM   5193 C  CB    . LEU B 1 327 ? 32.809 -31.913 -6.161  1.00 24.18 ?  307 LEU B CB    1 
ATOM   5194 C  CG    . LEU B 1 327 ? 33.898 -31.333 -7.081  1.00 30.79 ?  307 LEU B CG    1 
ATOM   5195 C  CD1   . LEU B 1 327 ? 33.291 -30.472 -8.194  1.00 25.19 ?  307 LEU B CD1   1 
ATOM   5196 C  CD2   . LEU B 1 327 ? 34.960 -30.548 -6.320  1.00 28.53 ?  307 LEU B CD2   1 
ATOM   5197 N  N     . SER B 1 328 ? 31.887 -34.009 -3.403  1.00 39.23 ?  308 SER B N     1 
ATOM   5198 C  CA    . SER B 1 328 ? 30.900 -34.198 -2.348  1.00 32.22 ?  308 SER B CA    1 
ATOM   5199 C  C     . SER B 1 328 ? 31.353 -33.470 -1.095  1.00 33.33 ?  308 SER B C     1 
ATOM   5200 O  O     . SER B 1 328 ? 32.548 -33.230 -0.902  1.00 36.08 ?  308 SER B O     1 
ATOM   5201 C  CB    . SER B 1 328 ? 30.723 -35.687 -2.063  1.00 32.74 ?  308 SER B CB    1 
ATOM   5202 O  OG    . SER B 1 328 ? 31.983 -36.328 -1.942  1.00 36.14 ?  308 SER B OG    1 
ATOM   5203 N  N     . LYS B 1 329 ? 30.392 -33.114 -0.232  1.00 39.47 ?  309 LYS B N     1 
ATOM   5204 C  CA    . LYS B 1 329 ? 30.760 -32.412 1.003   1.00 38.98 ?  309 LYS B CA    1 
ATOM   5205 C  C     . LYS B 1 329 ? 31.771 -33.207 1.813   1.00 37.01 ?  309 LYS B C     1 
ATOM   5206 O  O     . LYS B 1 329 ? 32.666 -32.620 2.430   1.00 44.12 ?  309 LYS B O     1 
ATOM   5207 C  CB    . LYS B 1 329 ? 29.524 -32.099 1.845   1.00 37.95 ?  309 LYS B CB    1 
ATOM   5208 C  CG    . LYS B 1 329 ? 28.783 -30.843 1.361   1.00 54.29 ?  309 LYS B CG    1 
ATOM   5209 C  CD    . LYS B 1 329 ? 28.245 -29.990 2.504   1.00 54.55 ?  309 LYS B CD    1 
ATOM   5210 C  CE    . LYS B 1 329 ? 27.072 -29.126 2.038   1.00 60.80 ?  309 LYS B CE    1 
ATOM   5211 N  NZ    . LYS B 1 329 ? 27.342 -27.652 2.133   1.00 64.82 ?  309 LYS B NZ    1 
ATOM   5212 N  N     . GLU B 1 330 ? 31.684 -34.539 1.769   1.00 31.74 ?  310 GLU B N     1 
ATOM   5213 C  CA    . GLU B 1 330 ? 32.648 -35.383 2.461   1.00 36.04 ?  310 GLU B CA    1 
ATOM   5214 C  C     . GLU B 1 330 ? 34.052 -35.269 1.884   1.00 37.37 ?  310 GLU B C     1 
ATOM   5215 O  O     . GLU B 1 330 ? 35.033 -35.405 2.621   1.00 34.26 ?  310 GLU B O     1 
ATOM   5216 C  CB    . GLU B 1 330 ? 32.196 -36.835 2.403   1.00 37.31 ?  310 GLU B CB    1 
ATOM   5217 C  CG    . GLU B 1 330 ? 30.722 -37.002 2.684   1.00 51.13 ?  310 GLU B CG    1 
ATOM   5218 C  CD    . GLU B 1 330 ? 29.877 -36.907 1.428   1.00 51.12 ?  310 GLU B CD    1 
ATOM   5219 O  OE1   . GLU B 1 330 ? 30.005 -37.810 0.562   1.00 53.93 ?  310 GLU B OE1   1 
ATOM   5220 O  OE2   . GLU B 1 330 ? 29.095 -35.929 1.310   1.00 43.17 ?  310 GLU B OE2   1 
ATOM   5221 N  N     . ASN B 1 331 ? 34.185 -35.058 0.575   1.00 38.94 ?  311 ASN B N     1 
ATOM   5222 C  CA    . ASN B 1 331 ? 35.495 -35.196 -0.045  1.00 31.43 ?  311 ASN B CA    1 
ATOM   5223 C  C     . ASN B 1 331 ? 36.095 -33.897 -0.572  1.00 28.92 ?  311 ASN B C     1 
ATOM   5224 O  O     . ASN B 1 331 ? 37.304 -33.864 -0.813  1.00 24.93 ?  311 ASN B O     1 
ATOM   5225 C  CB    . ASN B 1 331 ? 35.424 -36.224 -1.179  1.00 29.43 ?  311 ASN B CB    1 
ATOM   5226 C  CG    . ASN B 1 331 ? 35.206 -37.640 -0.678  1.00 37.15 ?  311 ASN B CG    1 
ATOM   5227 O  OD1   . ASN B 1 331 ? 35.785 -38.071 0.331   1.00 31.07 ?  311 ASN B OD1   1 
ATOM   5228 N  ND2   . ASN B 1 331 ? 34.367 -38.382 -1.396  1.00 42.49 ?  311 ASN B ND2   1 
ATOM   5229 N  N     . ARG B 1 332 ? 35.305 -32.821 -0.686  1.00 26.80 ?  312 ARG B N     1 
ATOM   5230 C  CA    . ARG B 1 332 ? 35.649 -31.688 -1.544  1.00 30.41 ?  312 ARG B CA    1 
ATOM   5231 C  C     . ARG B 1 332 ? 36.751 -30.796 -0.987  1.00 33.85 ?  312 ARG B C     1 
ATOM   5232 O  O     . ARG B 1 332 ? 37.293 -29.973 -1.742  1.00 32.57 ?  312 ARG B O     1 
ATOM   5233 C  CB    . ARG B 1 332 ? 34.405 -30.844 -1.806  1.00 32.53 ?  312 ARG B CB    1 
ATOM   5234 C  CG    . ARG B 1 332 ? 33.897 -30.051 -0.613  1.00 23.70 ?  312 ARG B CG    1 
ATOM   5235 C  CD    . ARG B 1 332 ? 32.548 -29.448 -0.939  1.00 28.22 ?  312 ARG B CD    1 
ATOM   5236 N  NE    . ARG B 1 332 ? 32.208 -28.324 -0.076  1.00 36.14 ?  312 ARG B NE    1 
ATOM   5237 C  CZ    . ARG B 1 332 ? 30.985 -27.822 0.039   1.00 47.52 ?  312 ARG B CZ    1 
ATOM   5238 N  NH1   . ARG B 1 332 ? 29.965 -28.331 -0.634  1.00 44.95 ?  312 ARG B NH1   1 
ATOM   5239 N  NH2   . ARG B 1 332 ? 30.783 -26.775 0.840   1.00 49.17 ?  312 ARG B NH2   1 
ATOM   5240 N  N     . GLY B 1 333 ? 37.076 -30.917 0.300   1.00 28.62 ?  313 GLY B N     1 
ATOM   5241 C  CA    . GLY B 1 333 ? 38.136 -30.113 0.885   1.00 21.89 ?  313 GLY B CA    1 
ATOM   5242 C  C     . GLY B 1 333 ? 37.820 -28.637 0.801   1.00 25.24 ?  313 GLY B C     1 
ATOM   5243 O  O     . GLY B 1 333 ? 36.692 -28.200 1.037   1.00 25.26 ?  313 GLY B O     1 
ATOM   5244 N  N     . ASN B 1 334 ? 38.816 -27.854 0.407   1.00 29.20 ?  314 ASN B N     1 
ATOM   5245 C  CA    . ASN B 1 334 ? 38.682 -26.409 0.389   1.00 24.92 ?  314 ASN B CA    1 
ATOM   5246 C  C     . ASN B 1 334 ? 38.215 -25.876 -0.942  1.00 26.66 ?  314 ASN B C     1 
ATOM   5247 O  O     . ASN B 1 334 ? 38.292 -24.667 -1.168  1.00 31.82 ?  314 ASN B O     1 
ATOM   5248 C  CB    . ASN B 1 334 ? 40.009 -25.754 0.779   1.00 34.30 ?  314 ASN B CB    1 
ATOM   5249 C  CG    . ASN B 1 334 ? 40.288 -25.882 2.266   1.00 33.60 ?  314 ASN B CG    1 
ATOM   5250 O  OD1   . ASN B 1 334 ? 39.363 -25.901 3.073   1.00 43.22 ?  314 ASN B OD1   1 
ATOM   5251 N  ND2   . ASN B 1 334 ? 41.555 -25.992 2.631   1.00 34.88 ?  314 ASN B ND2   1 
ATOM   5252 N  N     . TYR B 1 335 ? 37.710 -26.731 -1.820  1.00 33.74 ?  315 TYR B N     1 
ATOM   5253 C  CA    . TYR B 1 335 ? 37.364 -26.320 -3.169  1.00 26.01 ?  315 TYR B CA    1 
ATOM   5254 C  C     . TYR B 1 335 ? 35.955 -26.766 -3.515  1.00 27.42 ?  315 TYR B C     1 
ATOM   5255 O  O     . TYR B 1 335 ? 35.487 -27.808 -3.053  1.00 33.37 ?  315 TYR B O     1 
ATOM   5256 C  CB    . TYR B 1 335 ? 38.328 -26.912 -4.183  1.00 28.58 ?  315 TYR B CB    1 
ATOM   5257 C  CG    . TYR B 1 335 ? 39.731 -26.363 -4.115  1.00 30.04 ?  315 TYR B CG    1 
ATOM   5258 C  CD1   . TYR B 1 335 ? 40.102 -25.253 -4.874  1.00 24.94 ?  315 TYR B CD1   1 
ATOM   5259 C  CD2   . TYR B 1 335 ? 40.691 -26.958 -3.300  1.00 23.97 ?  315 TYR B CD2   1 
ATOM   5260 C  CE1   . TYR B 1 335 ? 41.384 -24.762 -4.831  1.00 20.19 ?  315 TYR B CE1   1 
ATOM   5261 C  CE2   . TYR B 1 335 ? 41.978 -26.467 -3.246  1.00 23.26 ?  315 TYR B CE2   1 
ATOM   5262 C  CZ    . TYR B 1 335 ? 42.319 -25.366 -4.015  1.00 24.41 ?  315 TYR B CZ    1 
ATOM   5263 O  OH    . TYR B 1 335 ? 43.600 -24.870 -3.968  1.00 27.17 ?  315 TYR B OH    1 
ATOM   5264 N  N     . THR B 1 336 ? 35.293 -25.969 -4.356  1.00 27.72 ?  316 THR B N     1 
ATOM   5265 C  CA    . THR B 1 336 ? 34.024 -26.344 -4.960  1.00 28.57 ?  316 THR B CA    1 
ATOM   5266 C  C     . THR B 1 336 ? 34.106 -26.478 -6.479  1.00 32.13 ?  316 THR B C     1 
ATOM   5267 O  O     . THR B 1 336 ? 33.068 -26.710 -7.118  1.00 27.74 ?  316 THR B O     1 
ATOM   5268 C  CB    . THR B 1 336 ? 32.929 -25.323 -4.599  1.00 27.25 ?  316 THR B CB    1 
ATOM   5269 O  OG1   . THR B 1 336 ? 33.255 -24.039 -5.151  1.00 29.06 ?  316 THR B OG1   1 
ATOM   5270 C  CG2   . THR B 1 336 ? 32.789 -25.198 -3.107  1.00 24.07 ?  316 THR B CG2   1 
ATOM   5271 N  N     . THR B 1 337 ? 35.301 -26.335 -7.073  1.00 31.34 ?  317 THR B N     1 
ATOM   5272 C  CA    . THR B 1 337 ? 35.465 -26.223 -8.517  1.00 21.79 ?  317 THR B CA    1 
ATOM   5273 C  C     . THR B 1 337 ? 36.716 -26.962 -8.971  1.00 30.82 ?  317 THR B C     1 
ATOM   5274 O  O     . THR B 1 337 ? 37.627 -27.241 -8.180  1.00 28.69 ?  317 THR B O     1 
ATOM   5275 C  CB    . THR B 1 337 ? 35.585 -24.770 -8.970  1.00 26.01 ?  317 THR B CB    1 
ATOM   5276 O  OG1   . THR B 1 337 ? 36.656 -24.128 -8.251  1.00 22.69 ?  317 THR B OG1   1 
ATOM   5277 C  CG2   . THR B 1 337 ? 34.263 -24.023 -8.776  1.00 22.79 ?  317 THR B CG2   1 
ATOM   5278 N  N     . GLY B 1 338 ? 36.761 -27.259 -10.274 1.00 21.50 ?  318 GLY B N     1 
ATOM   5279 C  CA    . GLY B 1 338 ? 37.986 -27.716 -10.890 1.00 22.05 ?  318 GLY B CA    1 
ATOM   5280 C  C     . GLY B 1 338 ? 38.949 -26.569 -11.143 1.00 20.55 ?  318 GLY B C     1 
ATOM   5281 O  O     . GLY B 1 338 ? 38.649 -25.397 -10.936 1.00 22.46 ?  318 GLY B O     1 
ATOM   5282 N  N     . SER B 1 339 ? 40.139 -26.918 -11.622 1.00 21.96 ?  319 SER B N     1 
ATOM   5283 C  CA    . SER B 1 339 ? 41.157 -25.899 -11.851 1.00 21.50 ?  319 SER B CA    1 
ATOM   5284 C  C     . SER B 1 339 ? 40.728 -24.851 -12.884 1.00 21.83 ?  319 SER B C     1 
ATOM   5285 O  O     . SER B 1 339 ? 41.311 -23.761 -12.929 1.00 24.03 ?  319 SER B O     1 
ATOM   5286 C  CB    . SER B 1 339 ? 42.462 -26.570 -12.277 1.00 24.64 ?  319 SER B CB    1 
ATOM   5287 O  OG    . SER B 1 339 ? 42.294 -27.318 -13.475 1.00 26.75 ?  319 SER B OG    1 
ATOM   5288 N  N     . ALA B 1 340 ? 39.719 -25.132 -13.703 1.00 18.64 ?  320 ALA B N     1 
ATOM   5289 C  CA    . ALA B 1 340 ? 39.250 -24.156 -14.675 1.00 29.86 ?  320 ALA B CA    1 
ATOM   5290 C  C     . ALA B 1 340 ? 38.053 -23.359 -14.162 1.00 28.26 ?  320 ALA B C     1 
ATOM   5291 O  O     . ALA B 1 340 ? 37.457 -22.586 -14.928 1.00 30.85 ?  320 ALA B O     1 
ATOM   5292 C  CB    . ALA B 1 340 ? 38.919 -24.836 -16.022 1.00 21.86 ?  320 ALA B CB    1 
ATOM   5293 N  N     . GLY B 1 341 ? 37.686 -23.537 -12.892 1.00 28.69 ?  321 GLY B N     1 
ATOM   5294 C  CA    . GLY B 1 341 ? 36.676 -22.710 -12.253 1.00 25.46 ?  321 GLY B CA    1 
ATOM   5295 C  C     . GLY B 1 341 ? 35.243 -23.149 -12.429 1.00 23.58 ?  321 GLY B C     1 
ATOM   5296 O  O     . GLY B 1 341 ? 34.340 -22.321 -12.277 1.00 27.04 ?  321 GLY B O     1 
ATOM   5297 N  N     . TYR B 1 342 ? 35.002 -24.418 -12.732 1.00 20.09 ?  322 TYR B N     1 
ATOM   5298 C  CA    . TYR B 1 342 ? 33.665 -24.946 -12.950 1.00 22.79 ?  322 TYR B CA    1 
ATOM   5299 C  C     . TYR B 1 342 ? 33.371 -26.033 -11.921 1.00 27.67 ?  322 TYR B C     1 
ATOM   5300 O  O     . TYR B 1 342 ? 34.286 -26.693 -11.416 1.00 31.44 ?  322 TYR B O     1 
ATOM   5301 C  CB    . TYR B 1 342 ? 33.520 -25.527 -14.379 1.00 22.42 ?  322 TYR B CB    1 
ATOM   5302 C  CG    . TYR B 1 342 ? 33.711 -24.525 -15.508 1.00 21.73 ?  322 TYR B CG    1 
ATOM   5303 C  CD1   . TYR B 1 342 ? 32.651 -23.770 -15.976 1.00 25.05 ?  322 TYR B CD1   1 
ATOM   5304 C  CD2   . TYR B 1 342 ? 34.947 -24.340 -16.099 1.00 21.42 ?  322 TYR B CD2   1 
ATOM   5305 C  CE1   . TYR B 1 342 ? 32.810 -22.860 -17.003 1.00 27.93 ?  322 TYR B CE1   1 
ATOM   5306 C  CE2   . TYR B 1 342 ? 35.119 -23.435 -17.125 1.00 23.99 ?  322 TYR B CE2   1 
ATOM   5307 C  CZ    . TYR B 1 342 ? 34.045 -22.694 -17.580 1.00 28.29 ?  322 TYR B CZ    1 
ATOM   5308 O  OH    . TYR B 1 342 ? 34.199 -21.783 -18.612 1.00 29.94 ?  322 TYR B OH    1 
ATOM   5309 N  N     . THR B 1 343 ? 32.084 -26.214 -11.610 1.00 22.84 ?  323 THR B N     1 
ATOM   5310 C  CA    . THR B 1 343 ? 31.634 -27.323 -10.781 1.00 24.04 ?  323 THR B CA    1 
ATOM   5311 C  C     . THR B 1 343 ? 31.224 -28.489 -11.680 1.00 31.84 ?  323 THR B C     1 
ATOM   5312 O  O     . THR B 1 343 ? 31.370 -28.436 -12.907 1.00 28.44 ?  323 THR B O     1 
ATOM   5313 C  CB    . THR B 1 343 ? 30.457 -26.914 -9.902  1.00 30.60 ?  323 THR B CB    1 
ATOM   5314 O  OG1   . THR B 1 343 ? 29.286 -26.765 -10.724 1.00 34.80 ?  323 THR B OG1   1 
ATOM   5315 C  CG2   . THR B 1 343 ? 30.745 -25.603 -9.156  1.00 21.81 ?  323 THR B CG2   1 
ATOM   5316 N  N     . ASN B 1 344 ? 30.654 -29.544 -11.080 1.00 31.81 ?  324 ASN B N     1 
ATOM   5317 C  CA    . ASN B 1 344 ? 30.235 -30.703 -11.859 1.00 29.51 ?  324 ASN B CA    1 
ATOM   5318 C  C     . ASN B 1 344 ? 29.033 -30.422 -12.752 1.00 31.70 ?  324 ASN B C     1 
ATOM   5319 O  O     . ASN B 1 344 ? 28.762 -31.230 -13.649 1.00 35.13 ?  324 ASN B O     1 
ATOM   5320 C  CB    . ASN B 1 344 ? 29.929 -31.891 -10.952 1.00 27.73 ?  324 ASN B CB    1 
ATOM   5321 C  CG    . ASN B 1 344 ? 30.410 -33.210 -11.552 1.00 34.44 ?  324 ASN B CG    1 
ATOM   5322 O  OD1   . ASN B 1 344 ? 31.415 -33.243 -12.255 1.00 34.09 ?  324 ASN B OD1   1 
ATOM   5323 N  ND2   . ASN B 1 344 ? 29.693 -34.294 -11.283 1.00 33.30 ?  324 ASN B ND2   1 
ATOM   5324 N  N     . SER B 1 345 ? 28.317 -29.309 -12.538 1.00 28.67 ?  325 SER B N     1 
ATOM   5325 C  CA    . SER B 1 345 ? 27.260 -28.904 -13.468 1.00 37.21 ?  325 SER B CA    1 
ATOM   5326 C  C     . SER B 1 345 ? 27.807 -28.724 -14.888 1.00 30.19 ?  325 SER B C     1 
ATOM   5327 O  O     . SER B 1 345 ? 27.124 -29.049 -15.867 1.00 29.13 ?  325 SER B O     1 
ATOM   5328 C  CB    . SER B 1 345 ? 26.582 -27.612 -12.990 1.00 27.98 ?  325 SER B CB    1 
ATOM   5329 O  OG    . SER B 1 345 ? 26.499 -27.556 -11.573 1.00 45.43 ?  325 SER B OG    1 
ATOM   5330 N  N     . PHE B 1 346 ? 29.040 -28.222 -15.019 1.00 25.94 ?  326 PHE B N     1 
ATOM   5331 C  CA    . PHE B 1 346 ? 29.647 -28.112 -16.344 1.00 34.10 ?  326 PHE B CA    1 
ATOM   5332 C  C     . PHE B 1 346 ? 29.779 -29.483 -16.993 1.00 29.03 ?  326 PHE B C     1 
ATOM   5333 O  O     . PHE B 1 346 ? 29.358 -29.683 -18.136 1.00 33.73 ?  326 PHE B O     1 
ATOM   5334 C  CB    . PHE B 1 346 ? 31.013 -27.419 -16.257 1.00 32.69 ?  326 PHE B CB    1 
ATOM   5335 C  CG    . PHE B 1 346 ? 31.693 -27.210 -17.597 1.00 24.85 ?  326 PHE B CG    1 
ATOM   5336 C  CD1   . PHE B 1 346 ? 31.396 -26.104 -18.381 1.00 26.79 ?  326 PHE B CD1   1 
ATOM   5337 C  CD2   . PHE B 1 346 ? 32.658 -28.105 -18.056 1.00 30.00 ?  326 PHE B CD2   1 
ATOM   5338 C  CE1   . PHE B 1 346 ? 32.022 -25.907 -19.610 1.00 28.38 ?  326 PHE B CE1   1 
ATOM   5339 C  CE2   . PHE B 1 346 ? 33.290 -27.914 -19.291 1.00 28.12 ?  326 PHE B CE2   1 
ATOM   5340 C  CZ    . PHE B 1 346 ? 32.965 -26.816 -20.067 1.00 23.29 ?  326 PHE B CZ    1 
ATOM   5341 N  N     . ASN B 1 347 ? 30.366 -30.444 -16.276 1.00 33.04 ?  327 ASN B N     1 
ATOM   5342 C  CA    . ASN B 1 347 ? 30.507 -31.786 -16.829 1.00 30.76 ?  327 ASN B CA    1 
ATOM   5343 C  C     . ASN B 1 347 ? 29.147 -32.374 -17.151 1.00 29.38 ?  327 ASN B C     1 
ATOM   5344 O  O     . ASN B 1 347 ? 28.966 -33.013 -18.196 1.00 26.34 ?  327 ASN B O     1 
ATOM   5345 C  CB    . ASN B 1 347 ? 31.256 -32.687 -15.854 1.00 29.48 ?  327 ASN B CB    1 
ATOM   5346 C  CG    . ASN B 1 347 ? 32.717 -32.326 -15.736 1.00 28.81 ?  327 ASN B CG    1 
ATOM   5347 O  OD1   . ASN B 1 347 ? 33.352 -31.921 -16.713 1.00 31.39 ?  327 ASN B OD1   1 
ATOM   5348 N  ND2   . ASN B 1 347 ? 33.269 -32.487 -14.540 1.00 27.09 ?  327 ASN B ND2   1 
ATOM   5349 N  N     . HIS B 1 348 ? 28.170 -32.134 -16.277 1.00 31.14 ?  328 HIS B N     1 
ATOM   5350 C  CA    . HIS B 1 348 ? 26.829 -32.630 -16.541 1.00 38.65 ?  328 HIS B CA    1 
ATOM   5351 C  C     . HIS B 1 348 ? 26.288 -32.081 -17.857 1.00 33.84 ?  328 HIS B C     1 
ATOM   5352 O  O     . HIS B 1 348 ? 25.623 -32.804 -18.607 1.00 30.68 ?  328 HIS B O     1 
ATOM   5353 C  CB    . HIS B 1 348 ? 25.888 -32.292 -15.378 1.00 38.52 ?  328 HIS B CB    1 
ATOM   5354 C  CG    . HIS B 1 348 ? 24.640 -33.115 -15.385 1.00 43.26 ?  328 HIS B CG    1 
ATOM   5355 N  ND1   . HIS B 1 348 ? 23.402 -32.588 -15.692 1.00 46.11 ?  328 HIS B ND1   1 
ATOM   5356 C  CD2   . HIS B 1 348 ? 24.451 -34.443 -15.201 1.00 39.56 ?  328 HIS B CD2   1 
ATOM   5357 C  CE1   . HIS B 1 348 ? 22.502 -33.555 -15.674 1.00 51.87 ?  328 HIS B CE1   1 
ATOM   5358 N  NE2   . HIS B 1 348 ? 23.113 -34.690 -15.382 1.00 52.34 ?  328 HIS B NE2   1 
ATOM   5359 N  N     . MET B 1 349 ? 26.593 -30.815 -18.170 1.00 28.32 ?  329 MET B N     1 
ATOM   5360 C  CA    . MET B 1 349 ? 26.073 -30.214 -19.395 1.00 30.08 ?  329 MET B CA    1 
ATOM   5361 C  C     . MET B 1 349 ? 26.791 -30.751 -20.637 1.00 31.57 ?  329 MET B C     1 
ATOM   5362 O  O     . MET B 1 349 ? 26.151 -31.004 -21.664 1.00 28.40 ?  329 MET B O     1 
ATOM   5363 C  CB    . MET B 1 349 ? 26.174 -28.687 -19.314 1.00 30.82 ?  329 MET B CB    1 
ATOM   5364 C  CG    . MET B 1 349 ? 26.350 -27.956 -20.657 1.00 34.00 ?  329 MET B CG    1 
ATOM   5365 S  SD    . MET B 1 349 ? 27.505 -26.581 -20.549 1.00 56.44 ?  329 MET B SD    1 
ATOM   5366 C  CE    . MET B 1 349 ? 29.034 -27.487 -20.589 1.00 32.79 ?  329 MET B CE    1 
ATOM   5367 N  N     . VAL B 1 350 ? 28.116 -30.930 -20.576 1.00 31.14 ?  330 VAL B N     1 
ATOM   5368 C  CA    . VAL B 1 350 ? 28.796 -31.560 -21.705 1.00 28.06 ?  330 VAL B CA    1 
ATOM   5369 C  C     . VAL B 1 350 ? 28.269 -32.976 -21.915 1.00 27.45 ?  330 VAL B C     1 
ATOM   5370 O  O     . VAL B 1 350 ? 28.035 -33.397 -23.053 1.00 28.34 ?  330 VAL B O     1 
ATOM   5371 C  CB    . VAL B 1 350 ? 30.324 -31.552 -21.517 1.00 25.01 ?  330 VAL B CB    1 
ATOM   5372 C  CG1   . VAL B 1 350 ? 30.971 -32.356 -22.631 1.00 23.72 ?  330 VAL B CG1   1 
ATOM   5373 C  CG2   . VAL B 1 350 ? 30.873 -30.146 -21.552 1.00 26.84 ?  330 VAL B CG2   1 
ATOM   5374 N  N     . LEU B 1 351 ? 28.066 -33.733 -20.823 1.00 28.19 ?  331 LEU B N     1 
ATOM   5375 C  CA    . LEU B 1 351 ? 27.578 -35.107 -20.951 1.00 31.22 ?  331 LEU B CA    1 
ATOM   5376 C  C     . LEU B 1 351 ? 26.180 -35.148 -21.570 1.00 35.36 ?  331 LEU B C     1 
ATOM   5377 O  O     . LEU B 1 351 ? 25.913 -35.968 -22.459 1.00 29.48 ?  331 LEU B O     1 
ATOM   5378 C  CB    . LEU B 1 351 ? 27.592 -35.818 -19.586 1.00 30.73 ?  331 LEU B CB    1 
ATOM   5379 C  CG    . LEU B 1 351 ? 27.064 -37.267 -19.455 1.00 29.95 ?  331 LEU B CG    1 
ATOM   5380 C  CD1   . LEU B 1 351 ? 27.799 -38.272 -20.323 1.00 26.80 ?  331 LEU B CD1   1 
ATOM   5381 C  CD2   . LEU B 1 351 ? 27.143 -37.736 -18.028 1.00 30.19 ?  331 LEU B CD2   1 
ATOM   5382 N  N     . GLU B 1 352 ? 25.280 -34.261 -21.126 1.00 34.81 ?  332 GLU B N     1 
ATOM   5383 C  CA    . GLU B 1 352 ? 23.928 -34.229 -21.682 1.00 34.06 ?  332 GLU B CA    1 
ATOM   5384 C  C     . GLU B 1 352 ? 23.953 -33.874 -23.170 1.00 34.14 ?  332 GLU B C     1 
ATOM   5385 O  O     . GLU B 1 352 ? 23.262 -34.502 -23.982 1.00 38.46 ?  332 GLU B O     1 
ATOM   5386 C  CB    . GLU B 1 352 ? 23.063 -33.238 -20.897 1.00 30.58 ?  332 GLU B CB    1 
ATOM   5387 C  CG    . GLU B 1 352 ? 22.279 -33.819 -19.696 1.00 53.48 ?  332 GLU B CG    1 
ATOM   5388 C  CD    . GLU B 1 352 ? 21.707 -35.234 -19.910 1.00 62.00 ?  332 GLU B CD    1 
ATOM   5389 O  OE1   . GLU B 1 352 ? 21.723 -36.037 -18.943 1.00 54.84 ?  332 GLU B OE1   1 
ATOM   5390 O  OE2   . GLU B 1 352 ? 21.208 -35.532 -21.023 1.00 68.67 ?  332 GLU B OE2   1 
ATOM   5391 N  N     . PHE B 1 353 ? 24.741 -32.859 -23.538 1.00 30.35 ?  333 PHE B N     1 
ATOM   5392 C  CA    . PHE B 1 353 ? 24.978 -32.526 -24.941 1.00 30.48 ?  333 PHE B CA    1 
ATOM   5393 C  C     . PHE B 1 353 ? 25.332 -33.771 -25.744 1.00 33.49 ?  333 PHE B C     1 
ATOM   5394 O  O     . PHE B 1 353 ? 24.773 -34.022 -26.814 1.00 34.57 ?  333 PHE B O     1 
ATOM   5395 C  CB    . PHE B 1 353 ? 26.118 -31.505 -25.029 1.00 32.64 ?  333 PHE B CB    1 
ATOM   5396 C  CG    . PHE B 1 353 ? 25.680 -30.080 -25.276 1.00 40.76 ?  333 PHE B CG    1 
ATOM   5397 C  CD1   . PHE B 1 353 ? 24.797 -29.757 -26.302 1.00 50.45 ?  333 PHE B CD1   1 
ATOM   5398 C  CD2   . PHE B 1 353 ? 26.165 -29.056 -24.470 1.00 37.18 ?  333 PHE B CD2   1 
ATOM   5399 C  CE1   . PHE B 1 353 ? 24.414 -28.435 -26.526 1.00 47.98 ?  333 PHE B CE1   1 
ATOM   5400 C  CE2   . PHE B 1 353 ? 25.782 -27.740 -24.676 1.00 43.22 ?  333 PHE B CE2   1 
ATOM   5401 C  CZ    . PHE B 1 353 ? 24.906 -27.425 -25.707 1.00 52.47 ?  333 PHE B CZ    1 
ATOM   5402 N  N     . THR B 1 354 ? 26.260 -34.574 -25.225 1.00 33.05 ?  334 THR B N     1 
ATOM   5403 C  CA    . THR B 1 354 ? 26.759 -35.725 -25.965 1.00 35.23 ?  334 THR B CA    1 
ATOM   5404 C  C     . THR B 1 354 ? 25.733 -36.855 -26.000 1.00 39.65 ?  334 THR B C     1 
ATOM   5405 O  O     . THR B 1 354 ? 25.609 -37.554 -27.015 1.00 35.61 ?  334 THR B O     1 
ATOM   5406 C  CB    . THR B 1 354 ? 28.072 -36.192 -25.337 1.00 36.34 ?  334 THR B CB    1 
ATOM   5407 O  OG1   . THR B 1 354 ? 28.909 -35.056 -25.113 1.00 29.53 ?  334 THR B OG1   1 
ATOM   5408 C  CG2   . THR B 1 354 ? 28.799 -37.183 -26.237 1.00 32.95 ?  334 THR B CG2   1 
ATOM   5409 N  N     . ILE B 1 355 ? 25.007 -37.057 -24.893 1.00 37.69 ?  335 ILE B N     1 
ATOM   5410 C  CA    . ILE B 1 355 ? 23.898 -38.011 -24.859 1.00 33.69 ?  335 ILE B CA    1 
ATOM   5411 C  C     . ILE B 1 355 ? 22.862 -37.646 -25.912 1.00 35.30 ?  335 ILE B C     1 
ATOM   5412 O  O     . ILE B 1 355 ? 22.365 -38.507 -26.647 1.00 42.37 ?  335 ILE B O     1 
ATOM   5413 C  CB    . ILE B 1 355 ? 23.286 -38.058 -23.439 1.00 35.62 ?  335 ILE B CB    1 
ATOM   5414 C  CG1   . ILE B 1 355 ? 24.204 -38.808 -22.481 1.00 32.46 ?  335 ILE B CG1   1 
ATOM   5415 C  CG2   . ILE B 1 355 ? 21.920 -38.716 -23.411 1.00 29.16 ?  335 ILE B CG2   1 
ATOM   5416 C  CD1   . ILE B 1 355 ? 23.801 -38.663 -21.038 1.00 32.72 ?  335 ILE B CD1   1 
ATOM   5417 N  N     . GLU B 1 356 ? 22.543 -36.360 -26.021 1.00 35.25 ?  336 GLU B N     1 
ATOM   5418 C  CA    . GLU B 1 356 ? 21.553 -35.920 -26.995 1.00 36.37 ?  336 GLU B CA    1 
ATOM   5419 C  C     . GLU B 1 356 ? 22.033 -36.111 -28.440 1.00 42.79 ?  336 GLU B C     1 
ATOM   5420 O  O     . GLU B 1 356 ? 21.217 -36.392 -29.327 1.00 44.28 ?  336 GLU B O     1 
ATOM   5421 C  CB    . GLU B 1 356 ? 21.185 -34.460 -26.712 1.00 33.25 ?  336 GLU B CB    1 
ATOM   5422 C  CG    . GLU B 1 356 ? 20.548 -33.721 -27.864 1.00 39.65 ?  336 GLU B CG    1 
ATOM   5423 C  CD    . GLU B 1 356 ? 19.044 -33.983 -27.986 1.00 58.39 ?  336 GLU B CD    1 
ATOM   5424 O  OE1   . GLU B 1 356 ? 18.505 -34.816 -27.220 1.00 57.09 ?  336 GLU B OE1   1 
ATOM   5425 O  OE2   . GLU B 1 356 ? 18.400 -33.359 -28.861 1.00 63.07 ?  336 GLU B OE2   1 
ATOM   5426 N  N     . VAL B 1 357 ? 23.332 -35.972 -28.714 1.00 34.88 ?  337 VAL B N     1 
ATOM   5427 C  CA    . VAL B 1 357 ? 23.782 -36.240 -30.074 1.00 37.26 ?  337 VAL B CA    1 
ATOM   5428 C  C     . VAL B 1 357 ? 23.606 -37.716 -30.394 1.00 41.01 ?  337 VAL B C     1 
ATOM   5429 O  O     . VAL B 1 357 ? 23.197 -38.081 -31.500 1.00 43.50 ?  337 VAL B O     1 
ATOM   5430 C  CB    . VAL B 1 357 ? 25.237 -35.784 -30.289 1.00 35.07 ?  337 VAL B CB    1 
ATOM   5431 C  CG1   . VAL B 1 357 ? 25.750 -36.334 -31.591 1.00 29.26 ?  337 VAL B CG1   1 
ATOM   5432 C  CG2   . VAL B 1 357 ? 25.322 -34.269 -30.308 1.00 26.95 ?  337 VAL B CG2   1 
ATOM   5433 N  N     . GLU B 1 358 ? 23.871 -38.585 -29.419 1.00 42.62 ?  338 GLU B N     1 
ATOM   5434 C  CA    . GLU B 1 358 ? 23.641 -40.010 -29.616 1.00 38.97 ?  338 GLU B CA    1 
ATOM   5435 C  C     . GLU B 1 358 ? 22.165 -40.311 -29.847 1.00 43.30 ?  338 GLU B C     1 
ATOM   5436 O  O     . GLU B 1 358 ? 21.818 -41.194 -30.643 1.00 37.63 ?  338 GLU B O     1 
ATOM   5437 C  CB    . GLU B 1 358 ? 24.150 -40.788 -28.417 1.00 30.52 ?  338 GLU B CB    1 
ATOM   5438 C  CG    . GLU B 1 358 ? 23.770 -42.226 -28.480 1.00 38.93 ?  338 GLU B CG    1 
ATOM   5439 C  CD    . GLU B 1 358 ? 23.937 -42.914 -27.157 1.00 43.92 ?  338 GLU B CD    1 
ATOM   5440 O  OE1   . GLU B 1 358 ? 23.412 -42.387 -26.148 1.00 40.81 ?  338 GLU B OE1   1 
ATOM   5441 O  OE2   . GLU B 1 358 ? 24.594 -43.978 -27.129 1.00 43.16 ?  338 GLU B OE2   1 
ATOM   5442 N  N     . LYS B 1 359 ? 21.283 -39.592 -29.149 1.00 43.83 ?  339 LYS B N     1 
ATOM   5443 C  CA    . LYS B 1 359 ? 19.851 -39.759 -29.369 1.00 37.90 ?  339 LYS B CA    1 
ATOM   5444 C  C     . LYS B 1 359 ? 19.466 -39.405 -30.799 1.00 41.09 ?  339 LYS B C     1 
ATOM   5445 O  O     . LYS B 1 359 ? 18.701 -40.137 -31.436 1.00 47.00 ?  339 LYS B O     1 
ATOM   5446 C  CB    . LYS B 1 359 ? 19.068 -38.907 -28.371 1.00 41.02 ?  339 LYS B CB    1 
ATOM   5447 C  CG    . LYS B 1 359 ? 17.592 -39.224 -28.289 1.00 41.26 ?  339 LYS B CG    1 
ATOM   5448 C  CD    . LYS B 1 359 ? 16.931 -38.436 -27.188 1.00 38.46 ?  339 LYS B CD    1 
ATOM   5449 C  CE    . LYS B 1 359 ? 15.754 -37.640 -27.723 1.00 49.66 ?  339 LYS B CE    1 
ATOM   5450 N  NZ    . LYS B 1 359 ? 15.779 -36.223 -27.246 1.00 55.44 ?  339 LYS B NZ    1 
ATOM   5451 N  N     . GLN B 1 360 ? 19.997 -38.295 -31.325 1.00 42.28 ?  340 GLN B N     1 
ATOM   5452 C  CA    . GLN B 1 360 ? 19.655 -37.866 -32.681 1.00 45.27 ?  340 GLN B CA    1 
ATOM   5453 C  C     . GLN B 1 360 ? 20.154 -38.855 -33.726 1.00 43.43 ?  340 GLN B C     1 
ATOM   5454 O  O     . GLN B 1 360 ? 19.463 -39.125 -34.714 1.00 45.74 ?  340 GLN B O     1 
ATOM   5455 C  CB    . GLN B 1 360 ? 20.251 -36.494 -32.979 1.00 39.92 ?  340 GLN B CB    1 
ATOM   5456 C  CG    . GLN B 1 360 ? 19.933 -35.428 -31.988 1.00 48.18 ?  340 GLN B CG    1 
ATOM   5457 C  CD    . GLN B 1 360 ? 20.746 -34.180 -32.252 1.00 53.39 ?  340 GLN B CD    1 
ATOM   5458 O  OE1   . GLN B 1 360 ? 21.873 -34.257 -32.737 1.00 58.95 ?  340 GLN B OE1   1 
ATOM   5459 N  NE2   . GLN B 1 360 ? 20.185 -33.025 -31.925 1.00 50.54 ?  340 GLN B NE2   1 
ATOM   5460 N  N     . ILE B 1 361 ? 21.374 -39.361 -33.554 1.00 33.69 ?  341 ILE B N     1 
ATOM   5461 C  CA    . ILE B 1 361 ? 21.911 -40.337 -34.494 1.00 40.78 ?  341 ILE B CA    1 
ATOM   5462 C  C     . ILE B 1 361 ? 21.026 -41.573 -34.532 1.00 47.46 ?  341 ILE B C     1 
ATOM   5463 O  O     . ILE B 1 361 ? 20.653 -42.060 -35.607 1.00 45.50 ?  341 ILE B O     1 
ATOM   5464 C  CB    . ILE B 1 361 ? 23.358 -40.703 -34.124 1.00 46.29 ?  341 ILE B CB    1 
ATOM   5465 C  CG1   . ILE B 1 361 ? 24.223 -39.443 -33.959 1.00 41.42 ?  341 ILE B CG1   1 
ATOM   5466 C  CG2   . ILE B 1 361 ? 23.926 -41.677 -35.155 1.00 50.08 ?  341 ILE B CG2   1 
ATOM   5467 C  CD1   . ILE B 1 361 ? 25.724 -39.704 -33.949 1.00 34.85 ?  341 ILE B CD1   1 
ATOM   5468 N  N     . ARG B 1 362 ? 20.687 -42.101 -33.352 1.00 44.25 ?  342 ARG B N     1 
ATOM   5469 C  CA    . ARG B 1 362 ? 19.830 -43.277 -33.258 1.00 41.68 ?  342 ARG B CA    1 
ATOM   5470 C  C     . ARG B 1 362 ? 18.467 -43.044 -33.902 1.00 47.87 ?  342 ARG B C     1 
ATOM   5471 O  O     . ARG B 1 362 ? 17.891 -43.969 -34.489 1.00 46.98 ?  342 ARG B O     1 
ATOM   5472 C  CB    . ARG B 1 362 ? 19.657 -43.664 -31.793 1.00 42.13 ?  342 ARG B CB    1 
ATOM   5473 C  CG    . ARG B 1 362 ? 20.819 -44.441 -31.210 1.00 46.07 ?  342 ARG B CG    1 
ATOM   5474 C  CD    . ARG B 1 362 ? 20.580 -44.721 -29.737 1.00 46.05 ?  342 ARG B CD    1 
ATOM   5475 N  NE    . ARG B 1 362 ? 21.542 -45.658 -29.171 1.00 46.10 ?  342 ARG B NE    1 
ATOM   5476 C  CZ    . ARG B 1 362 ? 21.730 -45.821 -27.868 1.00 57.26 ?  342 ARG B CZ    1 
ATOM   5477 N  NH1   . ARG B 1 362 ? 21.073 -45.087 -26.977 1.00 52.75 ?  342 ARG B NH1   1 
ATOM   5478 N  NH2   . ARG B 1 362 ? 22.605 -46.732 -27.446 1.00 56.08 ?  342 ARG B NH2   1 
ATOM   5479 N  N     . ALA B 1 363 ? 17.930 -41.824 -33.791 1.00 39.38 ?  343 ALA B N     1 
ATOM   5480 C  CA    . ALA B 1 363 ? 16.666 -41.517 -34.453 1.00 42.90 ?  343 ALA B CA    1 
ATOM   5481 C  C     . ALA B 1 363 ? 16.806 -41.599 -35.970 1.00 50.82 ?  343 ALA B C     1 
ATOM   5482 O  O     . ALA B 1 363 ? 15.940 -42.163 -36.651 1.00 49.44 ?  343 ALA B O     1 
ATOM   5483 C  CB    . ALA B 1 363 ? 16.173 -40.132 -34.032 1.00 32.47 ?  343 ALA B CB    1 
ATOM   5484 N  N     . VAL B 1 364 ? 17.898 -41.054 -36.515 1.00 46.24 ?  344 VAL B N     1 
ATOM   5485 C  CA    . VAL B 1 364 ? 18.096 -41.052 -37.958 1.00 45.81 ?  344 VAL B CA    1 
ATOM   5486 C  C     . VAL B 1 364 ? 18.290 -42.475 -38.476 1.00 48.62 ?  344 VAL B C     1 
ATOM   5487 O  O     . VAL B 1 364 ? 17.798 -42.831 -39.553 1.00 54.59 ?  344 VAL B O     1 
ATOM   5488 C  CB    . VAL B 1 364 ? 19.273 -40.126 -38.322 1.00 42.04 ?  344 VAL B CB    1 
ATOM   5489 C  CG1   . VAL B 1 364 ? 19.790 -40.424 -39.713 1.00 43.74 ?  344 VAL B CG1   1 
ATOM   5490 C  CG2   . VAL B 1 364 ? 18.837 -38.684 -38.236 1.00 37.12 ?  344 VAL B CG2   1 
ATOM   5491 N  N     . LEU B 1 365 ? 18.976 -43.320 -37.711 1.00 47.52 ?  345 LEU B N     1 
ATOM   5492 C  CA    . LEU B 1 365 ? 19.176 -44.699 -38.137 1.00 45.43 ?  345 LEU B CA    1 
ATOM   5493 C  C     . LEU B 1 365 ? 17.945 -45.576 -37.936 1.00 54.79 ?  345 LEU B C     1 
ATOM   5494 O  O     . LEU B 1 365 ? 17.848 -46.625 -38.582 1.00 58.75 ?  345 LEU B O     1 
ATOM   5495 C  CB    . LEU B 1 365 ? 20.359 -45.306 -37.390 1.00 42.97 ?  345 LEU B CB    1 
ATOM   5496 C  CG    . LEU B 1 365 ? 21.725 -45.011 -37.990 1.00 41.21 ?  345 LEU B CG    1 
ATOM   5497 C  CD1   . LEU B 1 365 ? 22.798 -45.267 -36.961 1.00 41.24 ?  345 LEU B CD1   1 
ATOM   5498 C  CD2   . LEU B 1 365 ? 21.936 -45.887 -39.199 1.00 48.27 ?  345 LEU B CD2   1 
ATOM   5499 N  N     . ALA B 1 366 ? 17.005 -45.159 -37.080 1.00 62.59 ?  346 ALA B N     1 
ATOM   5500 C  CA    . ALA B 1 366 ? 15.876 -45.998 -36.667 1.00 55.92 ?  346 ALA B CA    1 
ATOM   5501 C  C     . ALA B 1 366 ? 15.138 -46.682 -37.814 1.00 62.11 ?  346 ALA B C     1 
ATOM   5502 O  O     . ALA B 1 366 ? 14.956 -47.909 -37.750 1.00 62.49 ?  346 ALA B O     1 
ATOM   5503 C  CB    . ALA B 1 366 ? 14.905 -45.156 -35.828 1.00 45.68 ?  346 ALA B CB    1 
ATOM   5504 N  N     . PRO B 1 367 ? 14.702 -45.983 -38.889 1.00 58.47 ?  347 PRO B N     1 
ATOM   5505 C  CA    . PRO B 1 367 ? 13.926 -46.673 -39.930 1.00 55.52 ?  347 PRO B CA    1 
ATOM   5506 C  C     . PRO B 1 367 ? 14.753 -47.643 -40.758 1.00 60.93 ?  347 PRO B C     1 
ATOM   5507 O  O     . PRO B 1 367 ? 14.378 -47.965 -41.890 1.00 68.75 ?  347 PRO B O     1 
ATOM   5508 C  CB    . PRO B 1 367 ? 13.401 -45.520 -40.800 1.00 60.82 ?  347 PRO B CB    1 
ATOM   5509 C  CG    . PRO B 1 367 ? 13.591 -44.274 -39.972 1.00 57.80 ?  347 PRO B CG    1 
ATOM   5510 C  CD    . PRO B 1 367 ? 14.835 -44.548 -39.199 1.00 60.03 ?  347 PRO B CD    1 
ATOM   5511 N  N     . TYR B 1 368 ? 15.880 -48.104 -40.220 1.00 63.40 ?  348 TYR B N     1 
ATOM   5512 C  CA    . TYR B 1 368 ? 16.788 -48.980 -40.952 1.00 57.88 ?  348 TYR B CA    1 
ATOM   5513 C  C     . TYR B 1 368 ? 17.448 -49.982 -40.015 1.00 50.47 ?  348 TYR B C     1 
ATOM   5514 O  O     . TYR B 1 368 ? 16.901 -50.310 -38.960 1.00 62.25 ?  348 TYR B O     1 
ATOM   5515 C  CB    . TYR B 1 368 ? 17.858 -48.162 -41.691 1.00 62.94 ?  348 TYR B CB    1 
ATOM   5516 C  CG    . TYR B 1 368 ? 17.332 -46.943 -42.429 1.00 60.30 ?  348 TYR B CG    1 
ATOM   5517 C  CD1   . TYR B 1 368 ? 17.080 -46.990 -43.799 1.00 55.31 ?  348 TYR B CD1   1 
ATOM   5518 C  CD2   . TYR B 1 368 ? 17.102 -45.740 -41.758 1.00 61.61 ?  348 TYR B CD2   1 
ATOM   5519 C  CE1   . TYR B 1 368 ? 16.597 -45.876 -44.482 1.00 56.30 ?  348 TYR B CE1   1 
ATOM   5520 C  CE2   . TYR B 1 368 ? 16.618 -44.624 -42.429 1.00 62.42 ?  348 TYR B CE2   1 
ATOM   5521 C  CZ    . TYR B 1 368 ? 16.370 -44.695 -43.791 1.00 64.50 ?  348 TYR B CZ    1 
ATOM   5522 O  OH    . TYR B 1 368 ? 15.892 -43.584 -44.454 1.00 56.46 ?  348 TYR B OH    1 
HETATM 5523 C  CHA   . HEM C 2 .   ? 33.621 -6.064  16.718  1.00 18.60 ?  401 HEM A CHA   1 
HETATM 5524 C  CHB   . HEM C 2 .   ? 34.726 -4.311  12.278  1.00 23.74 ?  401 HEM A CHB   1 
HETATM 5525 C  CHC   . HEM C 2 .   ? 37.747 -0.979  14.169  1.00 24.63 ?  401 HEM A CHC   1 
HETATM 5526 C  CHD   . HEM C 2 .   ? 35.994 -2.251  18.557  1.00 18.16 ?  401 HEM A CHD   1 
HETATM 5527 C  C1A   . HEM C 2 .   ? 33.769 -5.952  15.344  1.00 21.84 ?  401 HEM A C1A   1 
HETATM 5528 C  C2A   . HEM C 2 .   ? 33.345 -6.909  14.340  1.00 18.95 ?  401 HEM A C2A   1 
HETATM 5529 C  C3A   . HEM C 2 .   ? 33.650 -6.418  13.124  1.00 27.88 ?  401 HEM A C3A   1 
HETATM 5530 C  C4A   . HEM C 2 .   ? 34.277 -5.128  13.304  1.00 27.29 ?  401 HEM A C4A   1 
HETATM 5531 C  CMA   . HEM C 2 .   ? 33.397 -7.070  11.740  1.00 21.96 ?  401 HEM A CMA   1 
HETATM 5532 C  CAA   . HEM C 2 .   ? 32.676 -8.266  14.644  1.00 23.12 ?  401 HEM A CAA   1 
HETATM 5533 C  CBA   . HEM C 2 .   ? 33.654 -9.164  15.413  1.00 20.85 ?  401 HEM A CBA   1 
HETATM 5534 C  CGA   . HEM C 2 .   ? 34.693 -9.702  14.465  1.00 21.54 ?  401 HEM A CGA   1 
HETATM 5535 O  O1A   . HEM C 2 .   ? 34.316 -10.504 13.574  1.00 25.59 ?  401 HEM A O1A   1 
HETATM 5536 O  O2A   . HEM C 2 .   ? 35.900 -9.372  14.593  1.00 20.11 ?  401 HEM A O2A   1 
HETATM 5537 C  C1B   . HEM C 2 .   ? 35.642 -3.278  12.372  1.00 24.07 ?  401 HEM A C1B   1 
HETATM 5538 C  C2B   . HEM C 2 .   ? 36.248 -2.547  11.270  1.00 33.84 ?  401 HEM A C2B   1 
HETATM 5539 C  C3B   . HEM C 2 .   ? 37.089 -1.614  11.787  1.00 25.31 ?  401 HEM A C3B   1 
HETATM 5540 C  C4B   . HEM C 2 .   ? 37.039 -1.723  13.231  1.00 27.52 ?  401 HEM A C4B   1 
HETATM 5541 C  CMB   . HEM C 2 .   ? 35.914 -2.852  9.783   1.00 23.59 ?  401 HEM A CMB   1 
HETATM 5542 C  CAB   . HEM C 2 .   ? 37.986 -0.580  11.060  1.00 25.63 ?  401 HEM A CAB   1 
HETATM 5543 C  CBB   . HEM C 2 .   ? 38.101 -0.453  9.739   1.00 18.56 ?  401 HEM A CBB   1 
HETATM 5544 C  C1C   . HEM C 2 .   ? 37.583 -1.088  15.548  1.00 23.50 ?  401 HEM A C1C   1 
HETATM 5545 C  C2C   . HEM C 2 .   ? 38.351 -0.404  16.573  1.00 20.88 ?  401 HEM A C2C   1 
HETATM 5546 C  C3C   . HEM C 2 .   ? 37.876 -0.767  17.795  1.00 19.50 ?  401 HEM A C3C   1 
HETATM 5547 C  C4C   . HEM C 2 .   ? 36.760 -1.664  17.581  1.00 19.23 ?  401 HEM A C4C   1 
HETATM 5548 C  CMC   . HEM C 2 .   ? 39.534 0.528   16.232  1.00 21.14 ?  401 HEM A CMC   1 
HETATM 5549 C  CAC   . HEM C 2 .   ? 38.339 -0.311  19.205  1.00 21.87 ?  401 HEM A CAC   1 
HETATM 5550 C  CBC   . HEM C 2 .   ? 38.944 0.870   19.439  1.00 20.39 ?  401 HEM A CBC   1 
HETATM 5551 C  C1D   . HEM C 2 .   ? 35.167 -3.350  18.438  1.00 18.79 ?  401 HEM A C1D   1 
HETATM 5552 C  C2D   . HEM C 2 .   ? 34.325 -3.899  19.483  1.00 22.95 ?  401 HEM A C2D   1 
HETATM 5553 C  C3D   . HEM C 2 .   ? 33.649 -4.953  18.994  1.00 27.32 ?  401 HEM A C3D   1 
HETATM 5554 C  C4D   . HEM C 2 .   ? 34.049 -5.109  17.603  1.00 21.50 ?  401 HEM A C4D   1 
HETATM 5555 C  CMD   . HEM C 2 .   ? 34.226 -3.362  20.923  1.00 21.98 ?  401 HEM A CMD   1 
HETATM 5556 C  CAD   . HEM C 2 .   ? 32.643 -5.841  19.790  1.00 25.63 ?  401 HEM A CAD   1 
HETATM 5557 C  CBD   . HEM C 2 .   ? 31.194 -5.516  19.409  1.00 27.80 ?  401 HEM A CBD   1 
HETATM 5558 C  CGD   . HEM C 2 .   ? 30.716 -4.243  20.079  1.00 32.57 ?  401 HEM A CGD   1 
HETATM 5559 O  O1D   . HEM C 2 .   ? 30.016 -3.416  19.428  1.00 31.62 ?  401 HEM A O1D   1 
HETATM 5560 O  O2D   . HEM C 2 .   ? 31.033 -4.038  21.279  1.00 29.70 ?  401 HEM A O2D   1 
HETATM 5561 N  NA    . HEM C 2 .   ? 34.328 -4.877  14.672  1.00 23.86 ?  401 HEM A NA    1 
HETATM 5562 N  NB    . HEM C 2 .   ? 36.147 -2.746  13.540  1.00 28.57 ?  401 HEM A NB    1 
HETATM 5563 N  NC    . HEM C 2 .   ? 36.618 -1.845  16.204  1.00 25.34 ?  401 HEM A NC    1 
HETATM 5564 N  ND    . HEM C 2 .   ? 34.972 -4.118  17.309  1.00 19.00 ?  401 HEM A ND    1 
HETATM 5565 FE FE    . HEM C 2 .   ? 35.384 -3.270  15.383  1.00 24.76 ?  401 HEM A FE    1 
HETATM 5566 C  "C1'" . IOP D 3 .   ? 37.689 -6.360  14.048  1.00 29.97 ?  402 IOP A "C1'" 1 
HETATM 5567 O  O1    . IOP D 3 .   ? 37.740 -5.718  15.139  1.00 32.36 ?  402 IOP A O1    1 
HETATM 5568 O  O2    . IOP D 3 .   ? 37.396 -7.581  14.029  1.00 33.29 -1 402 IOP A O2    1 
HETATM 5569 C  "C2'" . IOP D 3 .   ? 38.015 -5.642  12.755  1.00 23.36 ?  402 IOP A "C2'" 1 
HETATM 5570 C  "C3'" . IOP D 3 .   ? 38.857 -4.449  13.149  1.00 25.32 ?  402 IOP A "C3'" 1 
HETATM 5571 N  N1    . IOP D 3 .   ? 42.161 -5.986  13.563  1.00 26.70 ?  402 IOP A N1    1 
HETATM 5572 C  C2    . IOP D 3 .   ? 40.960 -5.970  12.994  1.00 25.77 ?  402 IOP A C2    1 
HETATM 5573 C  C3    . IOP D 3 .   ? 40.261 -4.883  13.506  1.00 24.54 ?  402 IOP A C3    1 
HETATM 5574 C  C3A   . IOP D 3 .   ? 41.103 -4.244  14.421  1.00 23.02 ?  402 IOP A C3A   1 
HETATM 5575 C  C4    . IOP D 3 .   ? 40.953 -3.111  15.227  1.00 21.71 ?  402 IOP A C4    1 
HETATM 5576 C  C5    . IOP D 3 .   ? 42.005 -2.723  16.044  1.00 25.26 ?  402 IOP A C5    1 
HETATM 5577 C  C6    . IOP D 3 .   ? 43.202 -3.435  16.066  1.00 22.20 ?  402 IOP A C6    1 
HETATM 5578 C  C7    . IOP D 3 .   ? 43.342 -4.559  15.264  1.00 26.66 ?  402 IOP A C7    1 
HETATM 5579 C  C7A   . IOP D 3 .   ? 42.281 -4.965  14.431  1.00 25.03 ?  402 IOP A C7A   1 
HETATM 5580 C  C1    . GOL E 4 .   ? 66.839 -15.814 2.913   1.00 46.67 ?  403 GOL A C1    1 
HETATM 5581 O  O1    . GOL E 4 .   ? 66.309 -14.968 1.898   1.00 53.47 ?  403 GOL A O1    1 
HETATM 5582 C  C2    . GOL E 4 .   ? 67.216 -17.202 2.261   1.00 56.55 ?  403 GOL A C2    1 
HETATM 5583 O  O2    . GOL E 4 .   ? 66.724 -17.349 0.933   1.00 52.84 ?  403 GOL A O2    1 
HETATM 5584 C  C3    . GOL E 4 .   ? 66.662 -18.276 3.244   1.00 40.38 ?  403 GOL A C3    1 
HETATM 5585 O  O3    . GOL E 4 .   ? 66.402 -19.423 2.477   1.00 50.83 ?  403 GOL A O3    1 
HETATM 5586 C  C1    . GOL F 4 .   ? 69.029 -20.329 9.699   1.00 52.31 ?  404 GOL A C1    1 
HETATM 5587 O  O1    . GOL F 4 .   ? 68.354 -20.146 10.926  1.00 47.97 ?  404 GOL A O1    1 
HETATM 5588 C  C2    . GOL F 4 .   ? 68.318 -19.415 8.670   1.00 55.84 ?  404 GOL A C2    1 
HETATM 5589 O  O2    . GOL F 4 .   ? 66.974 -19.236 8.996   1.00 54.57 ?  404 GOL A O2    1 
HETATM 5590 C  C3    . GOL F 4 .   ? 69.123 -18.063 8.671   1.00 53.55 ?  404 GOL A C3    1 
HETATM 5591 O  O3    . GOL F 4 .   ? 69.108 -17.556 9.987   1.00 43.87 ?  404 GOL A O3    1 
HETATM 5592 C  C1    . GOL G 4 .   ? 31.581 -19.187 14.527  1.00 58.05 ?  405 GOL A C1    1 
HETATM 5593 O  O1    . GOL G 4 .   ? 32.090 -18.776 15.769  1.00 51.56 ?  405 GOL A O1    1 
HETATM 5594 C  C2    . GOL G 4 .   ? 31.471 -17.904 13.640  1.00 61.83 ?  405 GOL A C2    1 
HETATM 5595 O  O2    . GOL G 4 .   ? 30.391 -17.092 14.027  1.00 53.99 ?  405 GOL A O2    1 
HETATM 5596 C  C3    . GOL G 4 .   ? 32.827 -17.186 13.842  1.00 49.03 ?  405 GOL A C3    1 
HETATM 5597 O  O3    . GOL G 4 .   ? 32.793 -16.696 15.160  1.00 42.44 ?  405 GOL A O3    1 
HETATM 5598 C  CHA   . HEM H 2 .   ? 36.635 -31.114 -16.722 1.00 22.14 ?  401 HEM B CHA   1 
HETATM 5599 C  CHB   . HEM H 2 .   ? 37.082 -32.867 -12.183 1.00 20.12 ?  401 HEM B CHB   1 
HETATM 5600 C  CHC   . HEM H 2 .   ? 40.427 -36.058 -13.672 1.00 23.58 ?  401 HEM B CHC   1 
HETATM 5601 C  CHD   . HEM H 2 .   ? 39.337 -34.830 -18.252 1.00 18.77 ?  401 HEM B CHD   1 
HETATM 5602 C  C1A   . HEM H 2 .   ? 36.560 -31.243 -15.347 1.00 24.50 ?  401 HEM B C1A   1 
HETATM 5603 C  C2A   . HEM H 2 .   ? 35.893 -30.335 -14.427 1.00 21.57 ?  401 HEM B C2A   1 
HETATM 5604 C  C3A   . HEM H 2 .   ? 36.014 -30.819 -13.179 1.00 24.96 ?  401 HEM B C3A   1 
HETATM 5605 C  C4A   . HEM H 2 .   ? 36.763 -32.057 -13.257 1.00 23.48 ?  401 HEM B C4A   1 
HETATM 5606 C  CMA   . HEM H 2 .   ? 35.471 -30.185 -11.879 1.00 19.64 ?  401 HEM B CMA   1 
HETATM 5607 C  CAA   . HEM H 2 .   ? 35.206 -29.020 -14.829 1.00 20.56 ?  401 HEM B CAA   1 
HETATM 5608 C  CBA   . HEM H 2 .   ? 36.258 -28.082 -15.448 1.00 24.54 ?  401 HEM B CBA   1 
HETATM 5609 C  CGA   . HEM H 2 .   ? 37.066 -27.378 -14.386 1.00 24.17 ?  401 HEM B CGA   1 
HETATM 5610 O  O1A   . HEM H 2 .   ? 36.481 -26.569 -13.625 1.00 24.37 ?  401 HEM B O1A   1 
HETATM 5611 O  O2A   . HEM H 2 .   ? 38.301 -27.601 -14.304 1.00 23.64 ?  401 HEM B O2A   1 
HETATM 5612 C  C1B   . HEM H 2 .   ? 38.041 -33.858 -12.164 1.00 22.03 ?  401 HEM B C1B   1 
HETATM 5613 C  C2B   . HEM H 2 .   ? 38.563 -34.528 -10.992 1.00 25.10 ?  401 HEM B C2B   1 
HETATM 5614 C  C3B   . HEM H 2 .   ? 39.499 -35.415 -11.396 1.00 25.08 ?  401 HEM B C3B   1 
HETATM 5615 C  C4B   . HEM H 2 .   ? 39.586 -35.338 -12.843 1.00 25.74 ?  401 HEM B C4B   1 
HETATM 5616 C  CMB   . HEM H 2 .   ? 38.074 -34.214 -9.560  1.00 18.18 ?  401 HEM B CMB   1 
HETATM 5617 C  CAB   . HEM H 2 .   ? 40.342 -36.405 -10.552 1.00 25.90 ?  401 HEM B CAB   1 
HETATM 5618 C  CBB   . HEM H 2 .   ? 40.114 -36.689 -9.264  1.00 23.84 ?  401 HEM B CBB   1 
HETATM 5619 C  C1C   . HEM H 2 .   ? 40.476 -35.948 -15.048 1.00 22.16 ?  401 HEM B C1C   1 
HETATM 5620 C  C2C   . HEM H 2 .   ? 41.439 -36.583 -15.930 1.00 18.69 ?  401 HEM B C2C   1 
HETATM 5621 C  C3C   . HEM H 2 .   ? 41.147 -36.236 -17.208 1.00 16.50 ?  401 HEM B C3C   1 
HETATM 5622 C  C4C   . HEM H 2 .   ? 39.970 -35.393 -17.163 1.00 19.33 ?  401 HEM B C4C   1 
HETATM 5623 C  CMC   . HEM H 2 .   ? 42.587 -37.459 -15.380 1.00 18.35 ?  401 HEM B CMC   1 
HETATM 5624 C  CAC   . HEM H 2 .   ? 41.827 -36.637 -18.551 1.00 21.93 ?  401 HEM B CAC   1 
HETATM 5625 C  CBC   . HEM H 2 .   ? 42.565 -37.747 -18.720 1.00 20.41 ?  401 HEM B CBC   1 
HETATM 5626 C  C1D   . HEM H 2 .   ? 38.462 -33.761 -18.250 1.00 18.34 ?  401 HEM B C1D   1 
HETATM 5627 C  C2D   . HEM H 2 .   ? 37.773 -33.210 -19.400 1.00 21.01 ?  401 HEM B C2D   1 
HETATM 5628 C  C3D   . HEM H 2 .   ? 37.010 -32.185 -18.999 1.00 23.53 ?  401 HEM B C3D   1 
HETATM 5629 C  C4D   . HEM H 2 .   ? 37.201 -32.048 -17.561 1.00 24.03 ?  401 HEM B C4D   1 
HETATM 5630 C  CMD   . HEM H 2 .   ? 37.923 -33.724 -20.841 1.00 21.07 ?  401 HEM B CMD   1 
HETATM 5631 C  CAD   . HEM H 2 .   ? 36.119 -31.296 -19.909 1.00 27.43 ?  401 HEM B CAD   1 
HETATM 5632 C  CBD   . HEM H 2 .   ? 34.641 -31.702 -19.838 1.00 28.16 ?  401 HEM B CBD   1 
HETATM 5633 C  CGD   . HEM H 2 .   ? 34.394 -32.914 -20.714 1.00 33.39 ?  401 HEM B CGD   1 
HETATM 5634 O  O1D   . HEM H 2 .   ? 33.545 -33.769 -20.324 1.00 35.27 ?  401 HEM B O1D   1 
HETATM 5635 O  O2D   . HEM H 2 .   ? 35.050 -33.047 -21.790 1.00 22.30 ?  401 HEM B O2D   1 
HETATM 5636 N  NA    . HEM H 2 .   ? 37.065 -32.297 -14.601 1.00 22.47 ?  401 HEM B NA    1 
HETATM 5637 N  NB    . HEM H 2 .   ? 38.690 -34.379 -13.271 1.00 25.50 ?  401 HEM B NB    1 
HETATM 5638 N  NC    . HEM H 2 .   ? 39.590 -35.235 -15.831 1.00 23.14 ?  401 HEM B NC    1 
HETATM 5639 N  ND    . HEM H 2 .   ? 38.089 -33.026 -17.147 1.00 19.34 ?  401 HEM B ND    1 
HETATM 5640 FE FE    . HEM H 2 .   ? 38.202 -33.869 -15.218 1.00 21.04 ?  401 HEM B FE    1 
HETATM 5641 C  "C1'" . IOP I 3 .   ? 39.982 -30.676 -13.125 1.00 32.75 ?  402 IOP B "C1'" 1 
HETATM 5642 O  O1    . IOP I 3 .   ? 39.270 -29.660 -12.880 1.00 36.25 ?  402 IOP B O1    1 
HETATM 5643 O  O2    . IOP I 3 .   ? 40.260 -31.024 -14.306 1.00 33.31 -1 402 IOP B O2    1 
HETATM 5644 C  "C2'" . IOP I 3 .   ? 40.514 -31.505 -11.971 1.00 27.23 ?  402 IOP B "C2'" 1 
HETATM 5645 C  "C3'" . IOP I 3 .   ? 41.365 -32.629 -12.510 1.00 22.09 ?  402 IOP B "C3'" 1 
HETATM 5646 N  N1    . IOP I 3 .   ? 44.615 -30.988 -12.275 1.00 25.56 ?  402 IOP B N1    1 
HETATM 5647 C  C2    . IOP I 3 .   ? 43.344 -31.075 -11.916 1.00 26.75 ?  402 IOP B C2    1 
HETATM 5648 C  C3    . IOP I 3 .   ? 42.783 -32.140 -12.599 1.00 25.10 ?  402 IOP B C3    1 
HETATM 5649 C  C3A   . IOP I 3 .   ? 43.776 -32.692 -13.404 1.00 26.02 ?  402 IOP B C3A   1 
HETATM 5650 C  C4    . IOP I 3 .   ? 43.785 -33.776 -14.289 1.00 19.07 ?  402 IOP B C4    1 
HETATM 5651 C  C5    . IOP I 3 .   ? 44.970 -34.076 -14.943 1.00 24.23 ?  402 IOP B C5    1 
HETATM 5652 C  C6    . IOP I 3 .   ? 46.131 -33.327 -14.728 1.00 27.38 ?  402 IOP B C6    1 
HETATM 5653 C  C7    . IOP I 3 .   ? 46.115 -32.257 -13.844 1.00 27.20 ?  402 IOP B C7    1 
HETATM 5654 C  C7A   . IOP I 3 .   ? 44.916 -31.942 -13.172 1.00 27.17 ?  402 IOP B C7A   1 
HETATM 5655 C  C     . TRS J 5 .   ? 57.676 -33.461 8.649   1.00 69.24 ?  403 TRS B C     1 
HETATM 5656 C  C1    . TRS J 5 .   ? 58.520 -34.298 7.686   1.00 68.71 ?  403 TRS B C1    1 
HETATM 5657 C  C2    . TRS J 5 .   ? 58.430 -32.208 9.119   1.00 61.76 ?  403 TRS B C2    1 
HETATM 5658 C  C3    . TRS J 5 .   ? 57.328 -34.339 9.854   1.00 61.83 ?  403 TRS B C3    1 
HETATM 5659 N  N     . TRS J 5 .   ? 56.442 -33.054 7.951   1.00 64.28 ?  403 TRS B N     1 
HETATM 5660 O  O1    . TRS J 5 .   ? 57.753 -34.645 6.551   1.00 50.01 ?  403 TRS B O1    1 
HETATM 5661 O  O2    . TRS J 5 .   ? 58.093 -31.062 8.350   1.00 44.72 ?  403 TRS B O2    1 
HETATM 5662 O  O3    . TRS J 5 .   ? 56.964 -33.531 10.950  1.00 63.38 ?  403 TRS B O3    1 
HETATM 5663 O  O     . HOH K 6 .   ? 61.952 -8.142  20.953  1.00 22.65 ?  501 HOH A O     1 
HETATM 5664 O  O     . HOH K 6 .   ? 63.691 -17.898 -0.549  1.00 40.33 ?  502 HOH A O     1 
HETATM 5665 O  O     . HOH K 6 .   ? 29.086 -7.022  45.046  1.00 48.47 ?  503 HOH A O     1 
HETATM 5666 O  O     . HOH K 6 .   ? 50.551 5.465   16.257  1.00 45.92 ?  504 HOH A O     1 
HETATM 5667 O  O     . HOH K 6 .   ? 34.917 -16.563 39.214  1.00 27.27 ?  505 HOH A O     1 
HETATM 5668 O  O     . HOH K 6 .   ? 67.948 -14.620 6.301   1.00 36.80 ?  506 HOH A O     1 
HETATM 5669 O  O     . HOH K 6 .   ? 59.775 2.179   13.398  1.00 33.23 ?  507 HOH A O     1 
HETATM 5670 O  O     . HOH K 6 .   ? 53.262 -17.168 34.902  1.00 31.07 ?  508 HOH A O     1 
HETATM 5671 O  O     . HOH K 6 .   ? 47.357 10.523  16.690  1.00 43.15 ?  509 HOH A O     1 
HETATM 5672 O  O     . HOH K 6 .   ? 56.681 -2.038  11.907  1.00 23.34 ?  510 HOH A O     1 
HETATM 5673 O  O     . HOH K 6 .   ? 28.386 -3.112  4.231   1.00 33.95 ?  511 HOH A O     1 
HETATM 5674 O  O     . HOH K 6 .   ? 61.533 -0.907  15.863  1.00 28.35 ?  512 HOH A O     1 
HETATM 5675 O  O     . HOH K 6 .   ? 63.850 -23.585 14.919  1.00 41.47 ?  513 HOH A O     1 
HETATM 5676 O  O     . HOH K 6 .   ? 59.935 -0.565  6.094   1.00 28.04 ?  514 HOH A O     1 
HETATM 5677 O  O     . HOH K 6 .   ? 47.288 -10.297 14.629  1.00 31.43 ?  515 HOH A O     1 
HETATM 5678 O  O     . HOH K 6 .   ? 46.648 -20.670 4.914   1.00 39.29 ?  516 HOH A O     1 
HETATM 5679 O  O     . HOH K 6 .   ? 53.898 -2.636  4.127   1.00 30.07 ?  517 HOH A O     1 
HETATM 5680 O  O     . HOH K 6 .   ? 39.793 -19.629 14.601  1.00 35.73 ?  518 HOH A O     1 
HETATM 5681 O  O     . HOH K 6 .   ? 36.800 -10.569 22.757  1.00 13.79 ?  519 HOH A O     1 
HETATM 5682 O  O     . HOH K 6 .   ? 62.051 -24.155 19.553  1.00 36.74 ?  520 HOH A O     1 
HETATM 5683 O  O     . HOH K 6 .   ? 61.323 -25.825 13.340  1.00 29.56 ?  521 HOH A O     1 
HETATM 5684 O  O     . HOH K 6 .   ? 37.211 3.652   1.515   1.00 34.67 ?  522 HOH A O     1 
HETATM 5685 O  O     . HOH K 6 .   ? 23.451 8.051   43.777  1.00 34.82 ?  523 HOH A O     1 
HETATM 5686 O  O     . HOH K 6 .   ? 51.775 2.472   9.251   1.00 32.34 ?  524 HOH A O     1 
HETATM 5687 O  O     . HOH K 6 .   ? 48.969 -5.002  2.952   1.00 27.78 ?  525 HOH A O     1 
HETATM 5688 O  O     . HOH K 6 .   ? 43.140 -19.957 9.035   1.00 20.88 ?  526 HOH A O     1 
HETATM 5689 O  O     . HOH K 6 .   ? 44.885 -6.003  32.310  1.00 37.49 ?  527 HOH A O     1 
HETATM 5690 O  O     . HOH K 6 .   ? 29.117 -1.197  16.545  1.00 24.36 ?  528 HOH A O     1 
HETATM 5691 O  O     . HOH K 6 .   ? 64.551 -21.894 22.103  1.00 29.29 ?  529 HOH A O     1 
HETATM 5692 O  O     . HOH K 6 .   ? 50.830 -22.200 12.162  1.00 19.66 ?  530 HOH A O     1 
HETATM 5693 O  O     . HOH K 6 .   ? 24.819 15.738  36.738  1.00 36.32 ?  531 HOH A O     1 
HETATM 5694 O  O     . HOH K 6 .   ? 18.861 -4.867  43.692  1.00 39.68 ?  532 HOH A O     1 
HETATM 5695 O  O     . HOH K 6 .   ? 44.956 -14.892 26.621  1.00 13.97 ?  533 HOH A O     1 
HETATM 5696 O  O     . HOH K 6 .   ? 59.830 -29.095 16.317  1.00 36.57 ?  534 HOH A O     1 
HETATM 5697 O  O     . HOH K 6 .   ? 44.065 -10.003 25.330  1.00 19.72 ?  535 HOH A O     1 
HETATM 5698 O  O     . HOH K 6 .   ? 34.266 -5.852  23.881  1.00 24.43 ?  536 HOH A O     1 
HETATM 5699 O  O     . HOH K 6 .   ? 57.266 2.388   13.720  1.00 27.96 ?  537 HOH A O     1 
HETATM 5700 O  O     . HOH K 6 .   ? 50.900 -12.527 26.018  1.00 20.81 ?  538 HOH A O     1 
HETATM 5701 O  O     . HOH K 6 .   ? 29.561 8.966   18.194  1.00 28.64 ?  539 HOH A O     1 
HETATM 5702 O  O     . HOH K 6 .   ? 53.826 -10.695 4.428   1.00 31.77 ?  540 HOH A O     1 
HETATM 5703 O  O     . HOH K 6 .   ? 68.507 -12.998 14.407  1.00 32.60 ?  541 HOH A O     1 
HETATM 5704 O  O     . HOH K 6 .   ? 34.329 -10.330 40.018  1.00 34.66 ?  542 HOH A O     1 
HETATM 5705 O  O     . HOH K 6 .   ? 36.470 -8.215  16.994  1.00 23.98 ?  543 HOH A O     1 
HETATM 5706 O  O     . HOH K 6 .   ? 39.665 -11.054 16.738  1.00 21.34 ?  544 HOH A O     1 
HETATM 5707 O  O     . HOH K 6 .   ? 47.317 -20.975 1.843   1.00 35.93 ?  545 HOH A O     1 
HETATM 5708 O  O     . HOH K 6 .   ? 66.126 -6.528  15.092  1.00 27.69 ?  546 HOH A O     1 
HETATM 5709 O  O     . HOH K 6 .   ? 47.558 -12.923 8.941   1.00 26.10 ?  547 HOH A O     1 
HETATM 5710 O  O     . HOH K 6 .   ? 51.877 -15.917 25.474  1.00 19.85 ?  548 HOH A O     1 
HETATM 5711 O  O     . HOH K 6 .   ? 46.728 4.788   2.491   1.00 32.84 ?  549 HOH A O     1 
HETATM 5712 O  O     . HOH K 6 .   ? 29.409 -9.451  5.795   1.00 24.39 ?  550 HOH A O     1 
HETATM 5713 O  O     . HOH K 6 .   ? 31.694 -6.299  23.000  1.00 21.86 ?  551 HOH A O     1 
HETATM 5714 O  O     . HOH K 6 .   ? 59.714 4.627   20.676  1.00 30.04 ?  552 HOH A O     1 
HETATM 5715 O  O     . HOH K 6 .   ? 58.171 -27.356 18.632  1.00 38.49 ?  553 HOH A O     1 
HETATM 5716 O  O     . HOH K 6 .   ? 36.602 -15.139 9.445   1.00 28.44 ?  554 HOH A O     1 
HETATM 5717 O  O     . HOH K 6 .   ? 41.611 -14.279 12.732  1.00 17.36 ?  555 HOH A O     1 
HETATM 5718 O  O     . HOH K 6 .   ? 59.544 -27.183 10.323  1.00 26.12 ?  556 HOH A O     1 
HETATM 5719 O  O     . HOH K 6 .   ? 55.126 1.739   9.315   1.00 24.44 ?  557 HOH A O     1 
HETATM 5720 O  O     . HOH K 6 .   ? 44.233 -12.561 19.257  1.00 26.06 ?  558 HOH A O     1 
HETATM 5721 O  O     . HOH K 6 .   ? 59.279 -4.525  33.202  1.00 37.89 ?  559 HOH A O     1 
HETATM 5722 O  O     . HOH K 6 .   ? 38.909 2.385   38.203  1.00 36.50 ?  560 HOH A O     1 
HETATM 5723 O  O     . HOH K 6 .   ? 24.271 12.296  26.006  1.00 35.65 ?  561 HOH A O     1 
HETATM 5724 O  O     . HOH K 6 .   ? 35.974 -13.555 5.492   1.00 25.07 ?  562 HOH A O     1 
HETATM 5725 O  O     . HOH K 6 .   ? 37.937 -18.310 26.062  1.00 24.49 ?  563 HOH A O     1 
HETATM 5726 O  O     . HOH K 6 .   ? 59.338 -0.352  14.478  1.00 34.85 ?  564 HOH A O     1 
HETATM 5727 O  O     . HOH K 6 .   ? 21.456 -14.571 19.720  1.00 36.29 ?  565 HOH A O     1 
HETATM 5728 O  O     . HOH K 6 .   ? 41.251 -8.353  1.086   1.00 25.30 ?  566 HOH A O     1 
HETATM 5729 O  O     . HOH K 6 .   ? 63.346 -5.438  1.610   1.00 44.13 ?  567 HOH A O     1 
HETATM 5730 O  O     . HOH K 6 .   ? 62.462 -8.592  -3.414  1.00 28.34 ?  568 HOH A O     1 
HETATM 5731 O  O     . HOH K 6 .   ? 51.814 2.352   24.722  1.00 23.88 ?  569 HOH A O     1 
HETATM 5732 O  O     . HOH K 6 .   ? 48.550 -13.373 24.600  1.00 18.90 ?  570 HOH A O     1 
HETATM 5733 O  O     . HOH K 6 .   ? 38.137 -15.321 20.939  1.00 21.16 ?  571 HOH A O     1 
HETATM 5734 O  O     . HOH K 6 .   ? 39.696 -11.642 -5.400  1.00 45.13 ?  572 HOH A O     1 
HETATM 5735 O  O     . HOH K 6 .   ? 37.077 -7.366  7.125   1.00 24.18 ?  573 HOH A O     1 
HETATM 5736 O  O     . HOH K 6 .   ? 38.695 11.239  18.742  1.00 30.94 ?  574 HOH A O     1 
HETATM 5737 O  O     . HOH K 6 .   ? 53.085 6.589   17.572  1.00 37.79 ?  575 HOH A O     1 
HETATM 5738 O  O     . HOH K 6 .   ? 60.439 -17.750 34.410  1.00 34.20 ?  576 HOH A O     1 
HETATM 5739 O  O     . HOH K 6 .   ? 59.840 -25.183 6.464   1.00 23.35 ?  577 HOH A O     1 
HETATM 5740 O  O     . HOH K 6 .   ? 24.436 3.374   13.521  1.00 31.22 ?  578 HOH A O     1 
HETATM 5741 O  O     . HOH K 6 .   ? 71.255 -23.772 12.755  1.00 35.87 ?  579 HOH A O     1 
HETATM 5742 O  O     . HOH K 6 .   ? 49.675 -27.116 15.392  1.00 39.17 ?  580 HOH A O     1 
HETATM 5743 O  O     . HOH K 6 .   ? 64.598 -5.463  26.413  1.00 21.67 ?  581 HOH A O     1 
HETATM 5744 O  O     . HOH K 6 .   ? 25.339 -8.089  7.758   1.00 44.35 ?  582 HOH A O     1 
HETATM 5745 O  O     . HOH K 6 .   ? 50.311 -23.707 5.404   1.00 22.50 ?  583 HOH A O     1 
HETATM 5746 O  O     . HOH K 6 .   ? 26.477 -9.132  36.588  1.00 38.51 ?  584 HOH A O     1 
HETATM 5747 O  O     . HOH K 6 .   ? 61.940 -24.901 10.092  1.00 16.58 ?  585 HOH A O     1 
HETATM 5748 O  O     . HOH K 6 .   ? 68.687 -15.102 0.023   1.00 37.71 ?  586 HOH A O     1 
HETATM 5749 O  O     . HOH K 6 .   ? 43.229 -16.281 4.992   1.00 48.53 ?  587 HOH A O     1 
HETATM 5750 O  O     . HOH K 6 .   ? 40.982 -9.873  25.035  1.00 20.73 ?  588 HOH A O     1 
HETATM 5751 O  O     . HOH K 6 .   ? 28.001 -7.602  7.194   1.00 30.06 ?  589 HOH A O     1 
HETATM 5752 O  O     . HOH K 6 .   ? 25.362 -4.028  7.843   1.00 39.18 ?  590 HOH A O     1 
HETATM 5753 O  O     . HOH K 6 .   ? 58.877 -3.824  -5.658  1.00 46.83 ?  591 HOH A O     1 
HETATM 5754 O  O     . HOH K 6 .   ? 54.258 -28.103 22.548  1.00 45.31 ?  592 HOH A O     1 
HETATM 5755 O  O     . HOH K 6 .   ? 27.258 2.761   5.186   1.00 42.23 ?  593 HOH A O     1 
HETATM 5756 O  O     . HOH K 6 .   ? 39.564 -13.120 21.405  1.00 20.84 ?  594 HOH A O     1 
HETATM 5757 O  O     . HOH K 6 .   ? 27.668 -12.592 12.115  1.00 21.55 ?  595 HOH A O     1 
HETATM 5758 O  O     . HOH K 6 .   ? 36.083 -14.199 20.473  1.00 23.02 ?  596 HOH A O     1 
HETATM 5759 O  O     . HOH K 6 .   ? 69.581 -15.058 24.779  1.00 29.89 ?  597 HOH A O     1 
HETATM 5760 O  O     . HOH K 6 .   ? 67.628 -16.199 26.257  1.00 28.10 ?  598 HOH A O     1 
HETATM 5761 O  O     . HOH K 6 .   ? 59.973 2.899   23.947  1.00 26.46 ?  599 HOH A O     1 
HETATM 5762 O  O     . HOH K 6 .   ? 59.557 -29.996 11.028  1.00 29.22 ?  600 HOH A O     1 
HETATM 5763 O  O     . HOH K 6 .   ? 43.531 -21.541 11.688  1.00 15.10 ?  601 HOH A O     1 
HETATM 5764 O  O     . HOH K 6 .   ? 34.178 -16.875 10.164  1.00 40.34 ?  602 HOH A O     1 
HETATM 5765 O  O     . HOH K 6 .   ? 57.401 -26.875 28.489  1.00 56.65 ?  603 HOH A O     1 
HETATM 5766 O  O     . HOH K 6 .   ? 57.781 -9.183  35.090  1.00 26.26 ?  604 HOH A O     1 
HETATM 5767 O  O     . HOH K 6 .   ? 30.354 2.114   1.257   1.00 35.97 ?  605 HOH A O     1 
HETATM 5768 O  O     . HOH K 6 .   ? 15.313 10.916  32.693  1.00 37.81 ?  606 HOH A O     1 
HETATM 5769 O  O     . HOH K 6 .   ? 48.683 -0.323  32.938  1.00 33.42 ?  607 HOH A O     1 
HETATM 5770 O  O     . HOH K 6 .   ? 47.607 1.670   28.566  1.00 34.39 ?  608 HOH A O     1 
HETATM 5771 O  O     . HOH K 6 .   ? 63.567 -23.712 3.856   1.00 20.90 ?  609 HOH A O     1 
HETATM 5772 O  O     . HOH K 6 .   ? 28.075 4.798   6.343   1.00 35.73 ?  610 HOH A O     1 
HETATM 5773 O  O     . HOH K 6 .   ? 37.988 10.693  29.200  1.00 35.93 ?  611 HOH A O     1 
HETATM 5774 O  O     . HOH K 6 .   ? 63.612 -22.425 26.847  1.00 28.53 ?  612 HOH A O     1 
HETATM 5775 O  O     . HOH K 6 .   ? 65.452 -1.788  23.070  1.00 39.15 ?  613 HOH A O     1 
HETATM 5776 O  O     . HOH K 6 .   ? 17.349 10.434  27.996  1.00 30.10 ?  614 HOH A O     1 
HETATM 5777 O  O     . HOH K 6 .   ? 38.384 -9.392  18.446  1.00 22.19 ?  615 HOH A O     1 
HETATM 5778 O  O     . HOH K 6 .   ? 52.520 -7.173  34.927  1.00 42.12 ?  616 HOH A O     1 
HETATM 5779 O  O     . HOH K 6 .   ? 22.125 -2.759  47.624  1.00 39.16 ?  617 HOH A O     1 
HETATM 5780 O  O     . HOH K 6 .   ? 41.514 8.581   6.093   1.00 25.35 ?  618 HOH A O     1 
HETATM 5781 O  O     . HOH K 6 .   ? 61.769 -23.371 22.378  1.00 36.25 ?  619 HOH A O     1 
HETATM 5782 O  O     . HOH K 6 .   ? 62.717 -1.701  -0.623  1.00 41.83 ?  620 HOH A O     1 
HETATM 5783 O  O     . HOH K 6 .   ? 39.763 -28.977 15.081  1.00 42.18 ?  621 HOH A O     1 
HETATM 5784 O  O     . HOH K 6 .   ? 43.744 -10.157 0.849   1.00 27.67 ?  622 HOH A O     1 
HETATM 5785 O  O     . HOH K 6 .   ? 39.071 -11.177 23.804  1.00 17.27 ?  623 HOH A O     1 
HETATM 5786 O  O     . HOH K 6 .   ? 60.008 3.129   10.930  1.00 39.78 ?  624 HOH A O     1 
HETATM 5787 O  O     . HOH K 6 .   ? 31.773 4.055   2.114   1.00 25.25 ?  625 HOH A O     1 
HETATM 5788 O  O     . HOH K 6 .   ? 49.420 -26.030 6.843   1.00 35.72 ?  626 HOH A O     1 
HETATM 5789 O  O     . HOH K 6 .   ? 28.421 1.086   2.793   1.00 36.65 ?  627 HOH A O     1 
HETATM 5790 O  O     . HOH K 6 .   ? 24.015 -5.623  9.682   1.00 33.20 ?  628 HOH A O     1 
HETATM 5791 O  O     . HOH K 6 .   ? 60.801 -25.650 30.172  1.00 33.95 ?  629 HOH A O     1 
HETATM 5792 O  O     . HOH K 6 .   ? 38.890 8.128   6.111   1.00 29.90 ?  630 HOH A O     1 
HETATM 5793 O  O     . HOH K 6 .   ? 36.303 -16.053 41.708  1.00 33.72 ?  631 HOH A O     1 
HETATM 5794 O  O     . HOH K 6 .   ? 49.107 -11.478 -0.169  1.00 39.70 ?  632 HOH A O     1 
HETATM 5795 O  O     . HOH K 6 .   ? 57.253 1.042   11.110  1.00 23.59 ?  633 HOH A O     1 
HETATM 5796 O  O     . HOH K 6 .   ? 48.921 -6.857  37.945  1.00 45.95 ?  634 HOH A O     1 
HETATM 5797 O  O     . HOH K 6 .   ? 27.576 -4.979  6.131   1.00 37.06 ?  635 HOH A O     1 
HETATM 5798 O  O     . HOH K 6 .   ? 42.222 -12.522 -5.779  1.00 45.80 ?  636 HOH A O     1 
HETATM 5799 O  O     . HOH K 6 .   ? 33.723 -22.587 18.615  1.00 48.72 ?  637 HOH A O     1 
HETATM 5800 O  O     . HOH K 6 .   ? 27.664 -11.078 5.080   1.00 30.11 ?  638 HOH A O     1 
HETATM 5801 O  O     . HOH K 6 .   ? 48.965 -12.567 36.891  1.00 34.54 ?  639 HOH A O     1 
HETATM 5802 O  O     . HOH K 6 .   ? 48.586 -9.906  38.805  1.00 40.48 ?  640 HOH A O     1 
HETATM 5803 O  O     . HOH K 6 .   ? 45.610 -9.265  -3.739  1.00 39.09 ?  641 HOH A O     1 
HETATM 5804 O  O     . HOH K 6 .   ? 46.541 -10.131 0.012   1.00 36.44 ?  642 HOH A O     1 
HETATM 5805 O  O     . HOH K 6 .   ? 48.070 -8.960  -2.355  1.00 41.92 ?  643 HOH A O     1 
HETATM 5806 O  O     . HOH K 6 .   ? 38.500 2.928   -5.357  1.00 39.03 ?  644 HOH A O     1 
HETATM 5807 O  O     . HOH K 6 .   ? 25.774 -8.241  3.867   1.00 43.67 ?  645 HOH A O     1 
HETATM 5808 O  O     . HOH L 6 .   ? 55.564 -11.651 -18.279 1.00 29.65 ?  501 HOH B O     1 
HETATM 5809 O  O     . HOH L 6 .   ? 45.306 -40.162 -37.153 1.00 32.79 ?  502 HOH B O     1 
HETATM 5810 O  O     . HOH L 6 .   ? 29.650 -34.389 -5.523  1.00 27.30 ?  503 HOH B O     1 
HETATM 5811 O  O     . HOH L 6 .   ? 66.622 -16.003 -2.487  1.00 35.83 ?  504 HOH B O     1 
HETATM 5812 O  O     . HOH L 6 .   ? 22.038 -31.436 -41.288 1.00 41.57 ?  505 HOH B O     1 
HETATM 5813 O  O     . HOH L 6 .   ? 65.274 -12.765 -9.968  1.00 39.37 ?  506 HOH B O     1 
HETATM 5814 O  O     . HOH L 6 .   ? 37.946 -40.953 -1.353  1.00 27.83 ?  507 HOH B O     1 
HETATM 5815 O  O     . HOH L 6 .   ? 36.707 -40.197 1.127   1.00 35.31 ?  508 HOH B O     1 
HETATM 5816 O  O     . HOH L 6 .   ? 62.856 -31.314 2.239   1.00 30.12 ?  509 HOH B O     1 
HETATM 5817 O  O     . HOH L 6 .   ? 64.156 -11.799 -15.613 1.00 35.01 ?  510 HOH B O     1 
HETATM 5818 O  O     . HOH L 6 .   ? 31.510 -53.127 -38.226 1.00 34.43 ?  511 HOH B O     1 
HETATM 5819 O  O     . HOH L 6 .   ? 52.302 -14.457 -9.513  1.00 17.57 ?  512 HOH B O     1 
HETATM 5820 O  O     . HOH L 6 .   ? 35.729 -30.903 -23.355 1.00 20.96 ?  513 HOH B O     1 
HETATM 5821 O  O     . HOH L 6 .   ? 58.810 -34.557 -8.575  1.00 25.04 ?  514 HOH B O     1 
HETATM 5822 O  O     . HOH L 6 .   ? 60.496 -8.825  -14.652 1.00 28.53 ?  515 HOH B O     1 
HETATM 5823 O  O     . HOH L 6 .   ? 27.044 -33.845 -9.492  1.00 28.28 ?  516 HOH B O     1 
HETATM 5824 O  O     . HOH L 6 .   ? 69.571 -32.820 -4.947  1.00 35.51 ?  517 HOH B O     1 
HETATM 5825 O  O     . HOH L 6 .   ? 40.078 -26.652 -22.193 1.00 19.71 ?  518 HOH B O     1 
HETATM 5826 O  O     . HOH L 6 .   ? 53.110 -41.831 -13.399 1.00 35.81 ?  519 HOH B O     1 
HETATM 5827 O  O     . HOH L 6 .   ? 32.102 -36.217 -17.441 1.00 19.99 ?  520 HOH B O     1 
HETATM 5828 O  O     . HOH L 6 .   ? 39.003 -43.014 -7.705  1.00 28.13 ?  521 HOH B O     1 
HETATM 5829 O  O     . HOH L 6 .   ? 37.724 -30.529 -4.265  1.00 28.02 ?  522 HOH B O     1 
HETATM 5830 O  O     . HOH L 6 .   ? 34.862 -27.381 -39.338 1.00 35.98 ?  523 HOH B O     1 
HETATM 5831 O  O     . HOH L 6 .   ? 53.561 -39.029 -6.621  1.00 28.92 ?  524 HOH B O     1 
HETATM 5832 O  O     . HOH L 6 .   ? 49.327 -22.145 -24.774 1.00 15.34 ?  525 HOH B O     1 
HETATM 5833 O  O     . HOH L 6 .   ? 30.612 -27.555 -6.519  1.00 27.02 ?  526 HOH B O     1 
HETATM 5834 O  O     . HOH L 6 .   ? 46.772 -21.655 -1.681  1.00 36.71 ?  527 HOH B O     1 
HETATM 5835 O  O     . HOH L 6 .   ? 35.383 -29.850 -45.802 1.00 46.28 ?  528 HOH B O     1 
HETATM 5836 O  O     . HOH L 6 .   ? 38.332 -31.193 -23.774 1.00 20.66 ?  529 HOH B O     1 
HETATM 5837 O  O     . HOH L 6 .   ? 68.625 -29.771 -9.827  1.00 34.76 ?  530 HOH B O     1 
HETATM 5838 O  O     . HOH L 6 .   ? 59.762 -38.700 -9.852  1.00 36.49 ?  531 HOH B O     1 
HETATM 5839 O  O     . HOH L 6 .   ? 21.164 -40.971 -25.724 1.00 32.14 ?  532 HOH B O     1 
HETATM 5840 O  O     . HOH L 6 .   ? 43.616 -22.610 -11.658 1.00 17.44 ?  533 HOH B O     1 
HETATM 5841 O  O     . HOH L 6 .   ? 16.936 -40.698 -52.254 1.00 52.60 ?  534 HOH B O     1 
HETATM 5842 O  O     . HOH L 6 .   ? 42.413 -26.041 -15.884 1.00 21.19 ?  535 HOH B O     1 
HETATM 5843 O  O     . HOH L 6 .   ? 66.772 -18.803 -29.696 1.00 38.00 ?  536 HOH B O     1 
HETATM 5844 O  O     . HOH L 6 .   ? 42.121 -17.301 -13.674 1.00 38.23 ?  537 HOH B O     1 
HETATM 5845 O  O     . HOH L 6 .   ? 61.726 -35.921 -10.788 1.00 30.04 ?  538 HOH B O     1 
HETATM 5846 O  O     . HOH L 6 .   ? 64.762 -27.880 -16.736 1.00 24.59 ?  539 HOH B O     1 
HETATM 5847 O  O     . HOH L 6 .   ? 68.423 -24.452 -11.966 1.00 32.46 ?  540 HOH B O     1 
HETATM 5848 O  O     . HOH L 6 .   ? 52.367 -23.301 -22.121 1.00 20.22 ?  541 HOH B O     1 
HETATM 5849 O  O     . HOH L 6 .   ? 36.877 -21.065 -18.576 1.00 26.04 ?  542 HOH B O     1 
HETATM 5850 O  O     . HOH L 6 .   ? 49.628 -10.508 -7.705  1.00 37.11 ?  543 HOH B O     1 
HETATM 5851 O  O     . HOH L 6 .   ? 49.753 -31.899 -0.674  1.00 33.62 ?  544 HOH B O     1 
HETATM 5852 O  O     . HOH L 6 .   ? 32.474 -20.105 -41.898 1.00 31.74 ?  545 HOH B O     1 
HETATM 5853 O  O     . HOH L 6 .   ? 62.198 -39.370 -8.172  1.00 49.79 ?  546 HOH B O     1 
HETATM 5854 O  O     . HOH L 6 .   ? 39.389 -28.862 -16.539 1.00 25.76 ?  547 HOH B O     1 
HETATM 5855 O  O     . HOH L 6 .   ? 45.041 -15.197 -10.277 1.00 20.82 ?  548 HOH B O     1 
HETATM 5856 O  O     . HOH L 6 .   ? 31.165 -34.638 -19.146 1.00 31.71 ?  549 HOH B O     1 
HETATM 5857 O  O     . HOH L 6 .   ? 31.078 -45.333 -45.200 1.00 33.16 ?  550 HOH B O     1 
HETATM 5858 O  O     . HOH L 6 .   ? 22.901 -47.746 -30.439 1.00 25.03 ?  551 HOH B O     1 
HETATM 5859 O  O     . HOH L 6 .   ? 27.554 -41.007 -14.684 1.00 25.36 ?  552 HOH B O     1 
HETATM 5860 O  O     . HOH L 6 .   ? 61.231 -21.607 4.122   1.00 31.29 ?  553 HOH B O     1 
HETATM 5861 O  O     . HOH L 6 .   ? 55.777 -20.827 -22.514 1.00 19.41 ?  554 HOH B O     1 
HETATM 5862 O  O     . HOH L 6 .   ? 69.381 -27.751 -7.804  1.00 37.51 ?  555 HOH B O     1 
HETATM 5863 O  O     . HOH L 6 .   ? 60.522 -9.168  -6.475  1.00 25.10 ?  556 HOH B O     1 
HETATM 5864 O  O     . HOH L 6 .   ? 47.263 -24.210 -17.556 1.00 16.95 ?  557 HOH B O     1 
HETATM 5865 O  O     . HOH L 6 .   ? 47.747 -26.881 -23.598 1.00 22.68 ?  558 HOH B O     1 
HETATM 5866 O  O     . HOH L 6 .   ? 64.102 -35.612 -11.880 1.00 22.95 ?  559 HOH B O     1 
HETATM 5867 O  O     . HOH L 6 .   ? 54.498 -25.899 -1.483  1.00 28.97 ?  560 HOH B O     1 
HETATM 5868 O  O     . HOH L 6 .   ? 36.449 -23.528 -5.274  1.00 20.11 ?  561 HOH B O     1 
HETATM 5869 O  O     . HOH L 6 .   ? 68.457 -33.469 -21.001 1.00 36.73 ?  562 HOH B O     1 
HETATM 5870 O  O     . HOH L 6 .   ? 31.124 -39.053 -1.936  1.00 32.47 ?  563 HOH B O     1 
HETATM 5871 O  O     . HOH L 6 .   ? 56.989 -38.507 -5.924  1.00 28.96 ?  564 HOH B O     1 
HETATM 5872 O  O     . HOH L 6 .   ? 68.371 -30.439 -21.715 1.00 23.76 ?  565 HOH B O     1 
HETATM 5873 O  O     . HOH L 6 .   ? 52.786 -16.546 -30.287 1.00 31.87 ?  566 HOH B O     1 
HETATM 5874 O  O     . HOH L 6 .   ? 59.211 -22.866 5.533   1.00 28.55 ?  567 HOH B O     1 
HETATM 5875 O  O     . HOH L 6 .   ? 44.177 -24.506 -1.182  1.00 26.28 ?  568 HOH B O     1 
HETATM 5876 O  O     . HOH L 6 .   ? 51.471 -9.298  -13.400 1.00 40.59 ?  569 HOH B O     1 
HETATM 5877 O  O     . HOH L 6 .   ? 54.747 -24.083 -23.510 1.00 22.65 ?  570 HOH B O     1 
HETATM 5878 O  O     . HOH L 6 .   ? 68.006 -34.799 -5.456  1.00 33.60 ?  571 HOH B O     1 
HETATM 5879 O  O     . HOH L 6 .   ? 63.351 -11.340 -5.891  1.00 12.34 ?  572 HOH B O     1 
HETATM 5880 O  O     . HOH L 6 .   ? 64.201 -39.003 -19.874 1.00 29.31 ?  573 HOH B O     1 
HETATM 5881 O  O     . HOH L 6 .   ? 62.715 -10.910 -8.784  1.00 29.73 ?  574 HOH B O     1 
HETATM 5882 O  O     . HOH L 6 .   ? 22.124 -37.312 -16.102 1.00 40.73 ?  575 HOH B O     1 
HETATM 5883 O  O     . HOH L 6 .   ? 45.169 -27.267 -23.733 1.00 18.75 ?  576 HOH B O     1 
HETATM 5884 O  O     . HOH L 6 .   ? 60.785 -29.983 8.637   1.00 36.83 ?  577 HOH B O     1 
HETATM 5885 O  O     . HOH L 6 .   ? 42.391 -18.602 -25.131 1.00 26.27 ?  578 HOH B O     1 
HETATM 5886 O  O     . HOH L 6 .   ? 42.996 -24.317 -20.247 1.00 20.82 ?  579 HOH B O     1 
HETATM 5887 O  O     . HOH L 6 .   ? 61.248 -35.799 -2.257  1.00 25.05 ?  580 HOH B O     1 
HETATM 5888 O  O     . HOH L 6 .   ? 43.883 -16.921 -19.148 1.00 37.80 ?  581 HOH B O     1 
HETATM 5889 O  O     . HOH L 6 .   ? 48.751 -23.879 -7.304  1.00 21.06 ?  582 HOH B O     1 
HETATM 5890 O  O     . HOH L 6 .   ? 33.442 -21.979 -3.035  1.00 38.98 ?  583 HOH B O     1 
HETATM 5891 O  O     . HOH L 6 .   ? 28.757 -30.642 -2.041  1.00 41.26 ?  584 HOH B O     1 
HETATM 5892 O  O     . HOH L 6 .   ? 38.430 -29.846 -7.004  1.00 29.72 ?  585 HOH B O     1 
HETATM 5893 O  O     . HOH L 6 .   ? 30.593 -48.474 -36.483 1.00 40.15 ?  586 HOH B O     1 
HETATM 5894 O  O     . HOH L 6 .   ? 24.852 -23.693 -22.205 1.00 44.03 ?  587 HOH B O     1 
HETATM 5895 O  O     . HOH L 6 .   ? 18.800 -49.375 -36.854 1.00 49.16 ?  588 HOH B O     1 
HETATM 5896 O  O     . HOH L 6 .   ? 17.749 -36.861 -35.650 1.00 38.06 ?  589 HOH B O     1 
HETATM 5897 O  O     . HOH L 6 .   ? 23.674 -31.711 -28.414 1.00 34.52 ?  590 HOH B O     1 
HETATM 5898 O  O     . HOH L 6 .   ? 32.500 -27.973 -37.193 1.00 34.88 ?  591 HOH B O     1 
HETATM 5899 O  O     . HOH L 6 .   ? 63.962 -24.020 -32.216 1.00 27.87 ?  592 HOH B O     1 
HETATM 5900 O  O     . HOH L 6 .   ? 55.373 -7.663  -4.626  1.00 39.78 ?  593 HOH B O     1 
HETATM 5901 O  O     . HOH L 6 .   ? 60.254 -41.934 -8.921  1.00 41.30 ?  594 HOH B O     1 
HETATM 5902 O  O     . HOH L 6 .   ? 29.505 -29.852 -8.219  1.00 23.07 ?  595 HOH B O     1 
HETATM 5903 O  O     . HOH L 6 .   ? 38.802 -47.857 -13.626 1.00 29.61 ?  596 HOH B O     1 
HETATM 5904 O  O     . HOH L 6 .   ? 56.765 -7.216  -7.323  1.00 37.55 ?  597 HOH B O     1 
HETATM 5905 O  O     . HOH L 6 .   ? 34.842 -19.548 -10.965 1.00 36.26 ?  598 HOH B O     1 
HETATM 5906 O  O     . HOH L 6 .   ? 43.765 -26.507 0.453   1.00 28.49 ?  599 HOH B O     1 
HETATM 5907 O  O     . HOH L 6 .   ? 50.529 -12.847 -2.945  1.00 16.80 ?  600 HOH B O     1 
HETATM 5908 O  O     . HOH L 6 .   ? 29.897 -24.550 -13.177 1.00 30.02 ?  601 HOH B O     1 
HETATM 5909 O  O     . HOH L 6 .   ? 48.186 -18.371 -32.459 1.00 4.66  ?  602 HOH B O     1 
HETATM 5910 O  O     . HOH L 6 .   ? 42.265 -48.319 -17.690 1.00 30.03 ?  603 HOH B O     1 
HETATM 5911 O  O     . HOH L 6 .   ? 27.530 -29.187 -9.046  1.00 31.05 ?  604 HOH B O     1 
HETATM 5912 O  O     . HOH L 6 .   ? 34.320 -28.592 -43.496 1.00 42.34 ?  605 HOH B O     1 
HETATM 5913 O  O     . HOH L 6 .   ? 59.918 -6.408  -6.886  1.00 31.31 ?  606 HOH B O     1 
HETATM 5914 O  O     . HOH L 6 .   ? 40.090 -22.030 -9.356  1.00 27.26 ?  607 HOH B O     1 
HETATM 5915 O  O     . HOH L 6 .   ? 44.216 -16.917 -7.963  1.00 25.84 ?  608 HOH B O     1 
HETATM 5916 O  O     . HOH L 6 .   ? 34.531 -20.208 -14.768 1.00 30.00 ?  609 HOH B O     1 
HETATM 5917 O  O     . HOH L 6 .   ? 33.166 -17.579 -19.003 1.00 38.35 ?  610 HOH B O     1 
HETATM 5918 O  O     . HOH L 6 .   ? 66.453 -13.745 -22.578 1.00 31.08 ?  611 HOH B O     1 
HETATM 5919 O  O     . HOH L 6 .   ? 42.046 -45.262 -5.351  1.00 35.16 ?  612 HOH B O     1 
HETATM 5920 O  O     . HOH L 6 .   ? 39.487 -33.751 -45.767 1.00 37.58 ?  613 HOH B O     1 
HETATM 5921 O  O     . HOH L 6 .   ? 26.313 -31.528 -11.081 1.00 31.30 ?  614 HOH B O     1 
HETATM 5922 O  O     . HOH L 6 .   ? 45.556 -39.492 -40.080 1.00 29.91 ?  615 HOH B O     1 
HETATM 5923 O  O     . HOH L 6 .   ? 32.761 -41.101 -2.508  1.00 23.97 ?  616 HOH B O     1 
HETATM 5924 O  O     . HOH L 6 .   ? 64.195 -44.385 -15.244 1.00 32.88 ?  617 HOH B O     1 
HETATM 5925 O  O     . HOH L 6 .   ? 29.060 -40.530 -6.710  1.00 36.38 ?  618 HOH B O     1 
HETATM 5926 O  O     . HOH L 6 .   ? 63.619 -12.609 0.726   1.00 13.81 ?  619 HOH B O     1 
HETATM 5927 O  O     . HOH L 6 .   ? 41.273 -27.545 -17.718 1.00 18.73 ?  620 HOH B O     1 
HETATM 5928 O  O     . HOH L 6 .   ? 43.050 -25.715 -23.058 1.00 19.98 ?  621 HOH B O     1 
HETATM 5929 O  O     . HOH L 6 .   ? 69.307 -36.344 -7.178  1.00 28.87 ?  622 HOH B O     1 
HETATM 5930 O  O     . HOH L 6 .   ? 37.393 -16.998 -18.043 1.00 38.37 ?  623 HOH B O     1 
HETATM 5931 O  O     . HOH L 6 .   ? 39.795 -45.272 0.091   1.00 30.35 ?  624 HOH B O     1 
HETATM 5932 O  O     . HOH L 6 .   ? 62.450 -14.651 -27.956 1.00 34.81 ?  625 HOH B O     1 
HETATM 5933 O  O     . HOH L 6 .   ? 53.584 -14.514 -27.576 1.00 27.89 ?  626 HOH B O     1 
HETATM 5934 O  O     . HOH L 6 .   ? 21.201 -48.246 -35.066 1.00 39.65 ?  627 HOH B O     1 
HETATM 5935 O  O     . HOH L 6 .   ? 58.915 -37.284 -7.974  1.00 24.96 ?  628 HOH B O     1 
HETATM 5936 O  O     . HOH L 6 .   ? 25.744 -33.469 -49.473 1.00 43.35 ?  629 HOH B O     1 
HETATM 5937 O  O     . HOH L 6 .   ? 37.662 -30.642 4.639   1.00 28.39 ?  630 HOH B O     1 
HETATM 5938 O  O     . HOH L 6 .   ? 26.086 -21.257 -14.315 1.00 38.35 ?  631 HOH B O     1 
HETATM 5939 O  O     . HOH L 6 .   ? 42.669 -13.594 -18.731 1.00 44.20 ?  632 HOH B O     1 
HETATM 5940 O  O     . HOH L 6 .   ? 49.350 -30.098 2.545   1.00 51.58 ?  633 HOH B O     1 
HETATM 5941 O  O     . HOH L 6 .   ? 40.176 -23.574 -44.489 1.00 45.83 ?  634 HOH B O     1 
HETATM 5942 O  O     . HOH L 6 .   ? 49.357 -27.901 3.956   1.00 35.46 ?  635 HOH B O     1 
HETATM 5943 O  O     . HOH L 6 .   ? 35.336 -41.961 -2.647  1.00 21.45 ?  636 HOH B O     1 
HETATM 5944 O  O     . HOH L 6 .   ? 36.581 -43.840 -4.148  1.00 30.82 ?  637 HOH B O     1 
HETATM 5945 O  O     . HOH L 6 .   ? 59.089 -37.661 -1.844  1.00 36.62 ?  638 HOH B O     1 
HETATM 5946 O  O     . HOH L 6 .   ? 73.425 -22.200 -5.462  1.00 34.94 ?  639 HOH B O     1 
HETATM 5947 O  O     . HOH L 6 .   ? 46.029 -18.494 0.837   1.00 29.79 ?  640 HOH B O     1 
HETATM 5948 O  O     . HOH L 6 .   ? 40.548 -25.864 -45.507 1.00 40.86 ?  641 HOH B O     1 
HETATM 5949 O  O     . HOH L 6 .   ? 43.234 -35.428 -48.167 1.00 40.24 ?  642 HOH B O     1 
HETATM 5950 O  O     . HOH L 6 .   ? 26.918 -20.976 -12.028 1.00 44.02 ?  643 HOH B O     1 
HETATM 5951 O  O     . HOH L 6 .   ? 63.813 -6.184  -18.885 1.00 35.23 ?  644 HOH B O     1 
HETATM 5952 O  O     . HOH L 6 .   ? 41.924 -25.596 -47.796 1.00 47.27 ?  645 HOH B O     1 
# 
