data_9EPK
# 
_entry.id   9EPK 
# 
_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   9EPK         pdb_00009epk 10.2210/pdb9epk/pdb 
WWPDB D_1292137380 ?            ?                   
# 
_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       2025-03-26 
_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                        9EPK 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.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              robin.owen@diamond.ac.uk 
_pdbx_contact_author.name_first         Robin 
_pdbx_contact_author.name_last          Owen 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2104-7057 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Williams, L.J.'  1 0009-0002-4066-3899 
'Owen, R.L.'      2 0000-0002-2104-7057 
'Worrall, J.A.R.' 3 0000-0002-1863-834X 
'Hough, M.A.'     4 0000-0001-7377-6713 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'DtpAa Y389F 22 fs 100 microjoules XFEL Pulse Data Collection' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Williams, L.J.'  1 0009-0002-4066-3899 
primary 'Owen, R.L.'      2 0000-0002-2104-7057 
primary 'Worrall, J.A.R.' 3 0000-0002-1863-834X 
primary 'Hough, M.A.'     4 0000-0001-7377-6713 
# 
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 Deferrochelatase                  40240.020 2   ? ? ? ? 
2 non-polymer nat 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   2   ? ? ? ? 
3 water       nat water                             18.015    557 ? ? ? ? 
# 
_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       
;DPAGADAGSAVPFHGAHQAGIATPVQDRLHFAAFDVTTEDRAAFVALLKEWTAAARRLTAGHAVGEGAYGGLPEAPPDDT
GEALGLKPSRLTLTIGFGPSLFTRFGLADLRPEALADLPKFPGDNLDRARSGGDLCVQACADDPQVAVHAIRNLARIGFG
KVVVRWSQLGFGKTSSTTPDKQTPRNLLGFKDGTRNIAGTEKDRLDRFVWAAEKDGTPWMTGGSYLVARRIRMHIETWDR
ASLQEQEDVFGRDKGEGAPVGKAKERDEPFLKAMKPDAHVRLAHPDSNGGATLLRRGYSFTDGTDGLGRLDAGLFFLAYQ
RDIRTGFVPVQRNLATDALNEFIQHVGSAVFAVPPGVRDADDWWGSTLFGKEA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DPAGADAGSAVPFHGAHQAGIATPVQDRLHFAAFDVTTEDRAAFVALLKEWTAAARRLTAGHAVGEGAYGGLPEAPPDDT
GEALGLKPSRLTLTIGFGPSLFTRFGLADLRPEALADLPKFPGDNLDRARSGGDLCVQACADDPQVAVHAIRNLARIGFG
KVVVRWSQLGFGKTSSTTPDKQTPRNLLGFKDGTRNIAGTEKDRLDRFVWAAEKDGTPWMTGGSYLVARRIRMHIETWDR
ASLQEQEDVFGRDKGEGAPVGKAKERDEPFLKAMKPDAHVRLAHPDSNGGATLLRRGYSFTDGTDGLGRLDAGLFFLAYQ
RDIRTGFVPVQRNLATDALNEFIQHVGSAVFAVPPGVRDADDWWGSTLFGKEA
;
_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 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   PRO n 
1 3   ALA n 
1 4   GLY n 
1 5   ALA n 
1 6   ASP n 
1 7   ALA n 
1 8   GLY n 
1 9   SER n 
1 10  ALA n 
1 11  VAL n 
1 12  PRO n 
1 13  PHE n 
1 14  HIS n 
1 15  GLY n 
1 16  ALA n 
1 17  HIS n 
1 18  GLN n 
1 19  ALA n 
1 20  GLY n 
1 21  ILE n 
1 22  ALA n 
1 23  THR n 
1 24  PRO n 
1 25  VAL n 
1 26  GLN n 
1 27  ASP n 
1 28  ARG n 
1 29  LEU n 
1 30  HIS n 
1 31  PHE n 
1 32  ALA n 
1 33  ALA n 
1 34  PHE n 
1 35  ASP n 
1 36  VAL n 
1 37  THR n 
1 38  THR n 
1 39  GLU n 
1 40  ASP n 
1 41  ARG n 
1 42  ALA n 
1 43  ALA n 
1 44  PHE n 
1 45  VAL n 
1 46  ALA n 
1 47  LEU n 
1 48  LEU n 
1 49  LYS n 
1 50  GLU n 
1 51  TRP n 
1 52  THR n 
1 53  ALA n 
1 54  ALA n 
1 55  ALA n 
1 56  ARG n 
1 57  ARG n 
1 58  LEU n 
1 59  THR n 
1 60  ALA n 
1 61  GLY n 
1 62  HIS n 
1 63  ALA n 
1 64  VAL n 
1 65  GLY n 
1 66  GLU n 
1 67  GLY n 
1 68  ALA n 
1 69  TYR n 
1 70  GLY n 
1 71  GLY n 
1 72  LEU n 
1 73  PRO n 
1 74  GLU n 
1 75  ALA n 
1 76  PRO n 
1 77  PRO n 
1 78  ASP n 
1 79  ASP n 
1 80  THR n 
1 81  GLY n 
1 82  GLU n 
1 83  ALA n 
1 84  LEU n 
1 85  GLY n 
1 86  LEU n 
1 87  LYS n 
1 88  PRO n 
1 89  SER n 
1 90  ARG n 
1 91  LEU n 
1 92  THR n 
1 93  LEU n 
1 94  THR n 
1 95  ILE n 
1 96  GLY n 
1 97  PHE n 
1 98  GLY n 
1 99  PRO n 
1 100 SER n 
1 101 LEU n 
1 102 PHE n 
1 103 THR n 
1 104 ARG n 
1 105 PHE n 
1 106 GLY n 
1 107 LEU n 
1 108 ALA n 
1 109 ASP n 
1 110 LEU n 
1 111 ARG n 
1 112 PRO n 
1 113 GLU n 
1 114 ALA n 
1 115 LEU n 
1 116 ALA n 
1 117 ASP n 
1 118 LEU n 
1 119 PRO n 
1 120 LYS n 
1 121 PHE n 
1 122 PRO n 
1 123 GLY n 
1 124 ASP n 
1 125 ASN n 
1 126 LEU n 
1 127 ASP n 
1 128 ARG n 
1 129 ALA n 
1 130 ARG n 
1 131 SER n 
1 132 GLY n 
1 133 GLY n 
1 134 ASP n 
1 135 LEU n 
1 136 CYS n 
1 137 VAL n 
1 138 GLN n 
1 139 ALA n 
1 140 CYS n 
1 141 ALA n 
1 142 ASP n 
1 143 ASP n 
1 144 PRO n 
1 145 GLN n 
1 146 VAL n 
1 147 ALA n 
1 148 VAL n 
1 149 HIS n 
1 150 ALA n 
1 151 ILE n 
1 152 ARG n 
1 153 ASN n 
1 154 LEU n 
1 155 ALA n 
1 156 ARG n 
1 157 ILE n 
1 158 GLY n 
1 159 PHE n 
1 160 GLY n 
1 161 LYS n 
1 162 VAL n 
1 163 VAL n 
1 164 VAL n 
1 165 ARG n 
1 166 TRP n 
1 167 SER n 
1 168 GLN n 
1 169 LEU n 
1 170 GLY n 
1 171 PHE n 
1 172 GLY n 
1 173 LYS n 
1 174 THR n 
1 175 SER n 
1 176 SER n 
1 177 THR n 
1 178 THR n 
1 179 PRO n 
1 180 ASP n 
1 181 LYS n 
1 182 GLN n 
1 183 THR n 
1 184 PRO n 
1 185 ARG n 
1 186 ASN n 
1 187 LEU n 
1 188 LEU n 
1 189 GLY n 
1 190 PHE n 
1 191 LYS n 
1 192 ASP n 
1 193 GLY n 
1 194 THR n 
1 195 ARG n 
1 196 ASN n 
1 197 ILE n 
1 198 ALA n 
1 199 GLY n 
1 200 THR n 
1 201 GLU n 
1 202 LYS n 
1 203 ASP n 
1 204 ARG n 
1 205 LEU n 
1 206 ASP n 
1 207 ARG n 
1 208 PHE n 
1 209 VAL n 
1 210 TRP n 
1 211 ALA n 
1 212 ALA n 
1 213 GLU n 
1 214 LYS n 
1 215 ASP n 
1 216 GLY n 
1 217 THR n 
1 218 PRO n 
1 219 TRP n 
1 220 MET n 
1 221 THR n 
1 222 GLY n 
1 223 GLY n 
1 224 SER n 
1 225 TYR n 
1 226 LEU n 
1 227 VAL n 
1 228 ALA n 
1 229 ARG n 
1 230 ARG n 
1 231 ILE n 
1 232 ARG n 
1 233 MET n 
1 234 HIS n 
1 235 ILE n 
1 236 GLU n 
1 237 THR n 
1 238 TRP n 
1 239 ASP n 
1 240 ARG n 
1 241 ALA n 
1 242 SER n 
1 243 LEU n 
1 244 GLN n 
1 245 GLU n 
1 246 GLN n 
1 247 GLU n 
1 248 ASP n 
1 249 VAL n 
1 250 PHE n 
1 251 GLY n 
1 252 ARG n 
1 253 ASP n 
1 254 LYS n 
1 255 GLY n 
1 256 GLU n 
1 257 GLY n 
1 258 ALA n 
1 259 PRO n 
1 260 VAL n 
1 261 GLY n 
1 262 LYS n 
1 263 ALA n 
1 264 LYS n 
1 265 GLU n 
1 266 ARG n 
1 267 ASP n 
1 268 GLU n 
1 269 PRO n 
1 270 PHE n 
1 271 LEU n 
1 272 LYS n 
1 273 ALA n 
1 274 MET n 
1 275 LYS n 
1 276 PRO n 
1 277 ASP n 
1 278 ALA n 
1 279 HIS n 
1 280 VAL n 
1 281 ARG n 
1 282 LEU n 
1 283 ALA n 
1 284 HIS n 
1 285 PRO n 
1 286 ASP n 
1 287 SER n 
1 288 ASN n 
1 289 GLY n 
1 290 GLY n 
1 291 ALA n 
1 292 THR n 
1 293 LEU n 
1 294 LEU n 
1 295 ARG n 
1 296 ARG n 
1 297 GLY n 
1 298 TYR n 
1 299 SER n 
1 300 PHE n 
1 301 THR n 
1 302 ASP n 
1 303 GLY n 
1 304 THR n 
1 305 ASP n 
1 306 GLY n 
1 307 LEU n 
1 308 GLY n 
1 309 ARG n 
1 310 LEU n 
1 311 ASP n 
1 312 ALA n 
1 313 GLY n 
1 314 LEU n 
1 315 PHE n 
1 316 PHE n 
1 317 LEU n 
1 318 ALA n 
1 319 TYR n 
1 320 GLN n 
1 321 ARG n 
1 322 ASP n 
1 323 ILE n 
1 324 ARG n 
1 325 THR n 
1 326 GLY n 
1 327 PHE n 
1 328 VAL n 
1 329 PRO n 
1 330 VAL n 
1 331 GLN n 
1 332 ARG n 
1 333 ASN n 
1 334 LEU n 
1 335 ALA n 
1 336 THR n 
1 337 ASP n 
1 338 ALA n 
1 339 LEU n 
1 340 ASN n 
1 341 GLU n 
1 342 PHE n 
1 343 ILE n 
1 344 GLN n 
1 345 HIS n 
1 346 VAL n 
1 347 GLY n 
1 348 SER n 
1 349 ALA n 
1 350 VAL n 
1 351 PHE n 
1 352 ALA n 
1 353 VAL n 
1 354 PRO n 
1 355 PRO n 
1 356 GLY n 
1 357 VAL n 
1 358 ARG n 
1 359 ASP n 
1 360 ALA n 
1 361 ASP n 
1 362 ASP n 
1 363 TRP n 
1 364 TRP n 
1 365 GLY n 
1 366 SER n 
1 367 THR n 
1 368 LEU n 
1 369 PHE n 
1 370 GLY n 
1 371 LYS n 
1 372 GLU n 
1 373 ALA 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                   373 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SLI_2602 
_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      'Streptomyces lividans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1916 
_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              C43 
_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  
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 
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 
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   ASP 1   48  ?   ?   ?   A . n 
A 1 2   PRO 2   49  ?   ?   ?   A . n 
A 1 3   ALA 3   50  ?   ?   ?   A . n 
A 1 4   GLY 4   51  ?   ?   ?   A . n 
A 1 5   ALA 5   52  ?   ?   ?   A . n 
A 1 6   ASP 6   53  ?   ?   ?   A . n 
A 1 7   ALA 7   54  ?   ?   ?   A . n 
A 1 8   GLY 8   55  55  GLY GLY A . n 
A 1 9   SER 9   56  56  SER SER A . n 
A 1 10  ALA 10  57  57  ALA ALA A . n 
A 1 11  VAL 11  58  58  VAL VAL A . n 
A 1 12  PRO 12  59  59  PRO PRO A . n 
A 1 13  PHE 13  60  60  PHE PHE A . n 
A 1 14  HIS 14  61  61  HIS HIS A . n 
A 1 15  GLY 15  62  62  GLY GLY A . n 
A 1 16  ALA 16  63  63  ALA ALA A . n 
A 1 17  HIS 17  64  64  HIS HIS A . n 
A 1 18  GLN 18  65  65  GLN GLN A . n 
A 1 19  ALA 19  66  66  ALA ALA A . n 
A 1 20  GLY 20  67  67  GLY GLY A . n 
A 1 21  ILE 21  68  68  ILE ILE A . n 
A 1 22  ALA 22  69  69  ALA ALA A . n 
A 1 23  THR 23  70  70  THR THR A . n 
A 1 24  PRO 24  71  71  PRO PRO A . n 
A 1 25  VAL 25  72  72  VAL VAL A . n 
A 1 26  GLN 26  73  73  GLN GLN A . n 
A 1 27  ASP 27  74  74  ASP ASP A . n 
A 1 28  ARG 28  75  75  ARG ARG A . n 
A 1 29  LEU 29  76  76  LEU LEU A . n 
A 1 30  HIS 30  77  77  HIS HIS A . n 
A 1 31  PHE 31  78  78  PHE PHE A . n 
A 1 32  ALA 32  79  79  ALA ALA A . n 
A 1 33  ALA 33  80  80  ALA ALA A . n 
A 1 34  PHE 34  81  81  PHE PHE A . n 
A 1 35  ASP 35  82  82  ASP ASP A . n 
A 1 36  VAL 36  83  83  VAL VAL A . n 
A 1 37  THR 37  84  84  THR THR A . n 
A 1 38  THR 38  85  85  THR THR A . n 
A 1 39  GLU 39  86  86  GLU GLU A . n 
A 1 40  ASP 40  87  87  ASP ASP A . n 
A 1 41  ARG 41  88  88  ARG ARG A . n 
A 1 42  ALA 42  89  89  ALA ALA A . n 
A 1 43  ALA 43  90  90  ALA ALA A . n 
A 1 44  PHE 44  91  91  PHE PHE A . n 
A 1 45  VAL 45  92  92  VAL VAL A . n 
A 1 46  ALA 46  93  93  ALA ALA A . n 
A 1 47  LEU 47  94  94  LEU LEU A . n 
A 1 48  LEU 48  95  95  LEU LEU A . n 
A 1 49  LYS 49  96  96  LYS LYS A . n 
A 1 50  GLU 50  97  97  GLU GLU A . n 
A 1 51  TRP 51  98  98  TRP TRP A . n 
A 1 52  THR 52  99  99  THR THR A . n 
A 1 53  ALA 53  100 100 ALA ALA A . n 
A 1 54  ALA 54  101 101 ALA ALA A . n 
A 1 55  ALA 55  102 102 ALA ALA A . n 
A 1 56  ARG 56  103 103 ARG ARG A . n 
A 1 57  ARG 57  104 104 ARG ARG A . n 
A 1 58  LEU 58  105 105 LEU LEU A . n 
A 1 59  THR 59  106 106 THR THR A . n 
A 1 60  ALA 60  107 107 ALA ALA A . n 
A 1 61  GLY 61  108 108 GLY GLY A . n 
A 1 62  HIS 62  109 109 HIS HIS A . n 
A 1 63  ALA 63  110 110 ALA ALA A . n 
A 1 64  VAL 64  111 111 VAL VAL A . n 
A 1 65  GLY 65  112 112 GLY GLY A . n 
A 1 66  GLU 66  113 113 GLU GLU A . n 
A 1 67  GLY 67  114 114 GLY GLY A . n 
A 1 68  ALA 68  115 115 ALA ALA A . n 
A 1 69  TYR 69  116 116 TYR TYR A . n 
A 1 70  GLY 70  117 117 GLY GLY A . n 
A 1 71  GLY 71  118 118 GLY GLY A . n 
A 1 72  LEU 72  119 119 LEU LEU A . n 
A 1 73  PRO 73  120 120 PRO PRO A . n 
A 1 74  GLU 74  121 121 GLU GLU A . n 
A 1 75  ALA 75  122 122 ALA ALA A . n 
A 1 76  PRO 76  123 123 PRO PRO A . n 
A 1 77  PRO 77  124 124 PRO PRO A . n 
A 1 78  ASP 78  125 125 ASP ASP A . n 
A 1 79  ASP 79  126 126 ASP ASP A . n 
A 1 80  THR 80  127 127 THR THR A . n 
A 1 81  GLY 81  128 128 GLY GLY A . n 
A 1 82  GLU 82  129 129 GLU GLU A . n 
A 1 83  ALA 83  130 130 ALA ALA A . n 
A 1 84  LEU 84  131 131 LEU LEU A . n 
A 1 85  GLY 85  132 132 GLY GLY A . n 
A 1 86  LEU 86  133 133 LEU LEU A . n 
A 1 87  LYS 87  134 134 LYS LYS A . n 
A 1 88  PRO 88  135 135 PRO PRO A . n 
A 1 89  SER 89  136 136 SER SER A . n 
A 1 90  ARG 90  137 137 ARG ARG A . n 
A 1 91  LEU 91  138 138 LEU LEU A . n 
A 1 92  THR 92  139 139 THR THR A . n 
A 1 93  LEU 93  140 140 LEU LEU A . n 
A 1 94  THR 94  141 141 THR THR A . n 
A 1 95  ILE 95  142 142 ILE ILE A . n 
A 1 96  GLY 96  143 143 GLY GLY A . n 
A 1 97  PHE 97  144 144 PHE PHE A . n 
A 1 98  GLY 98  145 145 GLY GLY A . n 
A 1 99  PRO 99  146 146 PRO PRO A . n 
A 1 100 SER 100 147 147 SER SER A . n 
A 1 101 LEU 101 148 148 LEU LEU A . n 
A 1 102 PHE 102 149 149 PHE PHE A . n 
A 1 103 THR 103 150 150 THR THR A . n 
A 1 104 ARG 104 151 151 ARG ARG A . n 
A 1 105 PHE 105 152 152 PHE PHE A . n 
A 1 106 GLY 106 153 153 GLY GLY A . n 
A 1 107 LEU 107 154 154 LEU LEU A . n 
A 1 108 ALA 108 155 155 ALA ALA A . n 
A 1 109 ASP 109 156 156 ASP ASP A . n 
A 1 110 LEU 110 157 157 LEU LEU A . n 
A 1 111 ARG 111 158 158 ARG ARG A . n 
A 1 112 PRO 112 159 159 PRO PRO A . n 
A 1 113 GLU 113 160 160 GLU GLU A . n 
A 1 114 ALA 114 161 161 ALA ALA A . n 
A 1 115 LEU 115 162 162 LEU LEU A . n 
A 1 116 ALA 116 163 163 ALA ALA A . n 
A 1 117 ASP 117 164 164 ASP ASP A . n 
A 1 118 LEU 118 165 165 LEU LEU A . n 
A 1 119 PRO 119 166 166 PRO PRO A . n 
A 1 120 LYS 120 167 167 LYS LYS A . n 
A 1 121 PHE 121 168 168 PHE PHE A . n 
A 1 122 PRO 122 169 169 PRO PRO A . n 
A 1 123 GLY 123 170 170 GLY GLY A . n 
A 1 124 ASP 124 171 171 ASP ASP A . n 
A 1 125 ASN 125 172 172 ASN ASN A . n 
A 1 126 LEU 126 173 173 LEU LEU A . n 
A 1 127 ASP 127 174 174 ASP ASP A . n 
A 1 128 ARG 128 175 175 ARG ARG A . n 
A 1 129 ALA 129 176 176 ALA ALA A . n 
A 1 130 ARG 130 177 177 ARG ARG A . n 
A 1 131 SER 131 178 178 SER SER A . n 
A 1 132 GLY 132 179 179 GLY GLY A . n 
A 1 133 GLY 133 180 180 GLY GLY A . n 
A 1 134 ASP 134 181 181 ASP ASP A . n 
A 1 135 LEU 135 182 182 LEU LEU A . n 
A 1 136 CYS 136 183 183 CYS CYS A . n 
A 1 137 VAL 137 184 184 VAL VAL A . n 
A 1 138 GLN 138 185 185 GLN GLN A . n 
A 1 139 ALA 139 186 186 ALA ALA A . n 
A 1 140 CYS 140 187 187 CYS CYS A . n 
A 1 141 ALA 141 188 188 ALA ALA A . n 
A 1 142 ASP 142 189 189 ASP ASP A . n 
A 1 143 ASP 143 190 190 ASP ASP A . n 
A 1 144 PRO 144 191 191 PRO PRO A . n 
A 1 145 GLN 145 192 192 GLN GLN A . n 
A 1 146 VAL 146 193 193 VAL VAL A . n 
A 1 147 ALA 147 194 194 ALA ALA A . n 
A 1 148 VAL 148 195 195 VAL VAL A . n 
A 1 149 HIS 149 196 196 HIS HIS A . n 
A 1 150 ALA 150 197 197 ALA ALA A . n 
A 1 151 ILE 151 198 198 ILE ILE A . n 
A 1 152 ARG 152 199 199 ARG ARG A . n 
A 1 153 ASN 153 200 200 ASN ASN A . n 
A 1 154 LEU 154 201 201 LEU LEU A . n 
A 1 155 ALA 155 202 202 ALA ALA A . n 
A 1 156 ARG 156 203 203 ARG ARG A . n 
A 1 157 ILE 157 204 204 ILE ILE A . n 
A 1 158 GLY 158 205 205 GLY GLY A . n 
A 1 159 PHE 159 206 206 PHE PHE A . n 
A 1 160 GLY 160 207 207 GLY GLY A . n 
A 1 161 LYS 161 208 208 LYS LYS A . n 
A 1 162 VAL 162 209 209 VAL VAL A . n 
A 1 163 VAL 163 210 210 VAL VAL A . n 
A 1 164 VAL 164 211 211 VAL VAL A . n 
A 1 165 ARG 165 212 212 ARG ARG A . n 
A 1 166 TRP 166 213 213 TRP TRP A . n 
A 1 167 SER 167 214 214 SER SER A . n 
A 1 168 GLN 168 215 215 GLN GLN A . n 
A 1 169 LEU 169 216 216 LEU LEU A . n 
A 1 170 GLY 170 217 217 GLY GLY A . n 
A 1 171 PHE 171 218 218 PHE PHE A . n 
A 1 172 GLY 172 219 219 GLY GLY A . n 
A 1 173 LYS 173 220 220 LYS LYS A . n 
A 1 174 THR 174 221 221 THR THR A . n 
A 1 175 SER 175 222 222 SER SER A . n 
A 1 176 SER 176 223 223 SER SER A . n 
A 1 177 THR 177 224 224 THR THR A . n 
A 1 178 THR 178 225 225 THR THR A . n 
A 1 179 PRO 179 226 226 PRO PRO A . n 
A 1 180 ASP 180 227 227 ASP ASP A . n 
A 1 181 LYS 181 228 228 LYS LYS A . n 
A 1 182 GLN 182 229 229 GLN GLN A . n 
A 1 183 THR 183 230 230 THR THR A . n 
A 1 184 PRO 184 231 231 PRO PRO A . n 
A 1 185 ARG 185 232 232 ARG ARG A . n 
A 1 186 ASN 186 233 233 ASN ASN A . n 
A 1 187 LEU 187 234 234 LEU LEU A . n 
A 1 188 LEU 188 235 235 LEU LEU A . n 
A 1 189 GLY 189 236 236 GLY GLY A . n 
A 1 190 PHE 190 237 237 PHE PHE A . n 
A 1 191 LYS 191 238 238 LYS LYS A . n 
A 1 192 ASP 192 239 239 ASP ASP A . n 
A 1 193 GLY 193 240 240 GLY GLY A . n 
A 1 194 THR 194 241 241 THR THR A . n 
A 1 195 ARG 195 242 242 ARG ARG A . n 
A 1 196 ASN 196 243 243 ASN ASN A . n 
A 1 197 ILE 197 244 244 ILE ILE A . n 
A 1 198 ALA 198 245 245 ALA ALA A . n 
A 1 199 GLY 199 246 246 GLY GLY A . n 
A 1 200 THR 200 247 247 THR THR A . n 
A 1 201 GLU 201 248 248 GLU GLU A . n 
A 1 202 LYS 202 249 249 LYS LYS A . n 
A 1 203 ASP 203 250 250 ASP ASP A . n 
A 1 204 ARG 204 251 251 ARG ARG A . n 
A 1 205 LEU 205 252 252 LEU LEU A . n 
A 1 206 ASP 206 253 253 ASP ASP A . n 
A 1 207 ARG 207 254 254 ARG ARG A . n 
A 1 208 PHE 208 255 255 PHE PHE A . n 
A 1 209 VAL 209 256 256 VAL VAL A . n 
A 1 210 TRP 210 257 257 TRP TRP A . n 
A 1 211 ALA 211 258 258 ALA ALA A . n 
A 1 212 ALA 212 259 259 ALA ALA A . n 
A 1 213 GLU 213 260 260 GLU GLU A . n 
A 1 214 LYS 214 261 261 LYS LYS A . n 
A 1 215 ASP 215 262 262 ASP ASP A . n 
A 1 216 GLY 216 263 263 GLY GLY A . n 
A 1 217 THR 217 264 264 THR THR A . n 
A 1 218 PRO 218 265 265 PRO PRO A . n 
A 1 219 TRP 219 266 266 TRP TRP A . n 
A 1 220 MET 220 267 267 MET MET A . n 
A 1 221 THR 221 268 268 THR THR A . n 
A 1 222 GLY 222 269 269 GLY GLY A . n 
A 1 223 GLY 223 270 270 GLY GLY A . n 
A 1 224 SER 224 271 271 SER SER A . n 
A 1 225 TYR 225 272 272 TYR TYR A . n 
A 1 226 LEU 226 273 273 LEU LEU A . n 
A 1 227 VAL 227 274 274 VAL VAL A . n 
A 1 228 ALA 228 275 275 ALA ALA A . n 
A 1 229 ARG 229 276 276 ARG ARG A . n 
A 1 230 ARG 230 277 277 ARG ARG A . n 
A 1 231 ILE 231 278 278 ILE ILE A . n 
A 1 232 ARG 232 279 279 ARG ARG A . n 
A 1 233 MET 233 280 280 MET MET A . n 
A 1 234 HIS 234 281 281 HIS HIS A . n 
A 1 235 ILE 235 282 282 ILE ILE A . n 
A 1 236 GLU 236 283 283 GLU GLU A . n 
A 1 237 THR 237 284 284 THR THR A . n 
A 1 238 TRP 238 285 285 TRP TRP A . n 
A 1 239 ASP 239 286 286 ASP ASP A . n 
A 1 240 ARG 240 287 287 ARG ARG A . n 
A 1 241 ALA 241 288 288 ALA ALA A . n 
A 1 242 SER 242 289 289 SER SER A . n 
A 1 243 LEU 243 290 290 LEU LEU A . n 
A 1 244 GLN 244 291 291 GLN GLN A . n 
A 1 245 GLU 245 292 292 GLU GLU A . n 
A 1 246 GLN 246 293 293 GLN GLN A . n 
A 1 247 GLU 247 294 294 GLU GLU A . n 
A 1 248 ASP 248 295 295 ASP ASP A . n 
A 1 249 VAL 249 296 296 VAL VAL A . n 
A 1 250 PHE 250 297 297 PHE PHE A . n 
A 1 251 GLY 251 298 298 GLY GLY A . n 
A 1 252 ARG 252 299 299 ARG ARG A . n 
A 1 253 ASP 253 300 300 ASP ASP A . n 
A 1 254 LYS 254 301 301 LYS LYS A . n 
A 1 255 GLY 255 302 302 GLY GLY A . n 
A 1 256 GLU 256 303 303 GLU GLU A . n 
A 1 257 GLY 257 304 304 GLY GLY A . n 
A 1 258 ALA 258 305 305 ALA ALA A . n 
A 1 259 PRO 259 306 306 PRO PRO A . n 
A 1 260 VAL 260 307 307 VAL VAL A . n 
A 1 261 GLY 261 308 308 GLY GLY A . n 
A 1 262 LYS 262 309 309 LYS LYS A . n 
A 1 263 ALA 263 310 310 ALA ALA A . n 
A 1 264 LYS 264 311 311 LYS LYS A . n 
A 1 265 GLU 265 312 312 GLU GLU A . n 
A 1 266 ARG 266 313 313 ARG ARG A . n 
A 1 267 ASP 267 314 314 ASP ASP A . n 
A 1 268 GLU 268 315 315 GLU GLU A . n 
A 1 269 PRO 269 316 316 PRO PRO A . n 
A 1 270 PHE 270 317 317 PHE PHE A . n 
A 1 271 LEU 271 318 318 LEU LEU A . n 
A 1 272 LYS 272 319 319 LYS LYS A . n 
A 1 273 ALA 273 320 320 ALA ALA A . n 
A 1 274 MET 274 321 321 MET MET A . n 
A 1 275 LYS 275 322 322 LYS LYS A . n 
A 1 276 PRO 276 323 323 PRO PRO A . n 
A 1 277 ASP 277 324 324 ASP ASP A . n 
A 1 278 ALA 278 325 325 ALA ALA A . n 
A 1 279 HIS 279 326 326 HIS HIS A . n 
A 1 280 VAL 280 327 327 VAL VAL A . n 
A 1 281 ARG 281 328 328 ARG ARG A . n 
A 1 282 LEU 282 329 329 LEU LEU A . n 
A 1 283 ALA 283 330 330 ALA ALA A . n 
A 1 284 HIS 284 331 331 HIS HIS A . n 
A 1 285 PRO 285 332 332 PRO PRO A . n 
A 1 286 ASP 286 333 333 ASP ASP A . n 
A 1 287 SER 287 334 334 SER SER A . n 
A 1 288 ASN 288 335 335 ASN ASN A . n 
A 1 289 GLY 289 336 336 GLY GLY A . n 
A 1 290 GLY 290 337 337 GLY GLY A . n 
A 1 291 ALA 291 338 338 ALA ALA A . n 
A 1 292 THR 292 339 339 THR THR A . n 
A 1 293 LEU 293 340 340 LEU LEU A . n 
A 1 294 LEU 294 341 341 LEU LEU A . n 
A 1 295 ARG 295 342 342 ARG ARG A . n 
A 1 296 ARG 296 343 343 ARG ARG A . n 
A 1 297 GLY 297 344 344 GLY GLY A . n 
A 1 298 TYR 298 345 345 TYR TYR A . n 
A 1 299 SER 299 346 346 SER SER A . n 
A 1 300 PHE 300 347 347 PHE PHE A . n 
A 1 301 THR 301 348 348 THR THR A . n 
A 1 302 ASP 302 349 349 ASP ASP A . n 
A 1 303 GLY 303 350 350 GLY GLY A . n 
A 1 304 THR 304 351 351 THR THR A . n 
A 1 305 ASP 305 352 352 ASP ASP A . n 
A 1 306 GLY 306 353 353 GLY GLY A . n 
A 1 307 LEU 307 354 354 LEU LEU A . n 
A 1 308 GLY 308 355 355 GLY GLY A . n 
A 1 309 ARG 309 356 356 ARG ARG A . n 
A 1 310 LEU 310 357 357 LEU LEU A . n 
A 1 311 ASP 311 358 358 ASP ASP A . n 
A 1 312 ALA 312 359 359 ALA ALA A . n 
A 1 313 GLY 313 360 360 GLY GLY A . n 
A 1 314 LEU 314 361 361 LEU LEU A . n 
A 1 315 PHE 315 362 362 PHE PHE A . n 
A 1 316 PHE 316 363 363 PHE PHE A . n 
A 1 317 LEU 317 364 364 LEU LEU A . n 
A 1 318 ALA 318 365 365 ALA ALA A . n 
A 1 319 TYR 319 366 366 TYR TYR A . n 
A 1 320 GLN 320 367 367 GLN GLN A . n 
A 1 321 ARG 321 368 368 ARG ARG A . n 
A 1 322 ASP 322 369 369 ASP ASP A . n 
A 1 323 ILE 323 370 370 ILE ILE A . n 
A 1 324 ARG 324 371 371 ARG ARG A . n 
A 1 325 THR 325 372 372 THR THR A . n 
A 1 326 GLY 326 373 373 GLY GLY A . n 
A 1 327 PHE 327 374 374 PHE PHE A . n 
A 1 328 VAL 328 375 375 VAL VAL A . n 
A 1 329 PRO 329 376 376 PRO PRO A . n 
A 1 330 VAL 330 377 377 VAL VAL A . n 
A 1 331 GLN 331 378 378 GLN GLN A . n 
A 1 332 ARG 332 379 379 ARG ARG A . n 
A 1 333 ASN 333 380 380 ASN ASN A . n 
A 1 334 LEU 334 381 381 LEU LEU A . n 
A 1 335 ALA 335 382 382 ALA ALA A . n 
A 1 336 THR 336 383 383 THR THR A . n 
A 1 337 ASP 337 384 384 ASP ASP A . n 
A 1 338 ALA 338 385 385 ALA ALA A . n 
A 1 339 LEU 339 386 386 LEU LEU A . n 
A 1 340 ASN 340 387 387 ASN ASN A . n 
A 1 341 GLU 341 388 388 GLU GLU A . n 
A 1 342 PHE 342 389 389 PHE PHE A . n 
A 1 343 ILE 343 390 390 ILE ILE A . n 
A 1 344 GLN 344 391 391 GLN GLN A . n 
A 1 345 HIS 345 392 392 HIS HIS A . n 
A 1 346 VAL 346 393 393 VAL VAL A . n 
A 1 347 GLY 347 394 394 GLY GLY A . n 
A 1 348 SER 348 395 395 SER SER A . n 
A 1 349 ALA 349 396 396 ALA ALA A . n 
A 1 350 VAL 350 397 397 VAL VAL A . n 
A 1 351 PHE 351 398 398 PHE PHE A . n 
A 1 352 ALA 352 399 399 ALA ALA A . n 
A 1 353 VAL 353 400 400 VAL VAL A . n 
A 1 354 PRO 354 401 401 PRO PRO A . n 
A 1 355 PRO 355 402 402 PRO PRO A . n 
A 1 356 GLY 356 403 403 GLY GLY A . n 
A 1 357 VAL 357 404 404 VAL VAL A . n 
A 1 358 ARG 358 405 405 ARG ARG A . n 
A 1 359 ASP 359 406 406 ASP ASP A . n 
A 1 360 ALA 360 407 407 ALA ALA A . n 
A 1 361 ASP 361 408 408 ASP ASP A . n 
A 1 362 ASP 362 409 409 ASP ASP A . n 
A 1 363 TRP 363 410 410 TRP TRP A . n 
A 1 364 TRP 364 411 411 TRP TRP A . n 
A 1 365 GLY 365 412 412 GLY GLY A . n 
A 1 366 SER 366 413 413 SER SER A . n 
A 1 367 THR 367 414 414 THR THR A . n 
A 1 368 LEU 368 415 415 LEU LEU A . n 
A 1 369 PHE 369 416 416 PHE PHE A . n 
A 1 370 GLY 370 417 ?   ?   ?   A . n 
A 1 371 LYS 371 418 ?   ?   ?   A . n 
A 1 372 GLU 372 419 ?   ?   ?   A . n 
A 1 373 ALA 373 420 ?   ?   ?   A . n 
B 1 1   ASP 1   48  ?   ?   ?   B . n 
B 1 2   PRO 2   49  ?   ?   ?   B . n 
B 1 3   ALA 3   50  ?   ?   ?   B . n 
B 1 4   GLY 4   51  ?   ?   ?   B . n 
B 1 5   ALA 5   52  ?   ?   ?   B . n 
B 1 6   ASP 6   53  ?   ?   ?   B . n 
B 1 7   ALA 7   54  ?   ?   ?   B . n 
B 1 8   GLY 8   55  ?   ?   ?   B . n 
B 1 9   SER 9   56  56  SER SER B . n 
B 1 10  ALA 10  57  57  ALA ALA B . n 
B 1 11  VAL 11  58  58  VAL VAL B . n 
B 1 12  PRO 12  59  59  PRO PRO B . n 
B 1 13  PHE 13  60  60  PHE PHE B . n 
B 1 14  HIS 14  61  61  HIS HIS B . n 
B 1 15  GLY 15  62  62  GLY GLY B . n 
B 1 16  ALA 16  63  63  ALA ALA B . n 
B 1 17  HIS 17  64  64  HIS HIS B . n 
B 1 18  GLN 18  65  65  GLN GLN B . n 
B 1 19  ALA 19  66  66  ALA ALA B . n 
B 1 20  GLY 20  67  67  GLY GLY B . n 
B 1 21  ILE 21  68  68  ILE ILE B . n 
B 1 22  ALA 22  69  69  ALA ALA B . n 
B 1 23  THR 23  70  70  THR THR B . n 
B 1 24  PRO 24  71  71  PRO PRO B . n 
B 1 25  VAL 25  72  72  VAL VAL B . n 
B 1 26  GLN 26  73  73  GLN GLN B . n 
B 1 27  ASP 27  74  74  ASP ASP B . n 
B 1 28  ARG 28  75  75  ARG ARG B . n 
B 1 29  LEU 29  76  76  LEU LEU B . n 
B 1 30  HIS 30  77  77  HIS HIS B . n 
B 1 31  PHE 31  78  78  PHE PHE B . n 
B 1 32  ALA 32  79  79  ALA ALA B . n 
B 1 33  ALA 33  80  80  ALA ALA B . n 
B 1 34  PHE 34  81  81  PHE PHE B . n 
B 1 35  ASP 35  82  82  ASP ASP B . n 
B 1 36  VAL 36  83  83  VAL VAL B . n 
B 1 37  THR 37  84  84  THR THR B . n 
B 1 38  THR 38  85  85  THR THR B . n 
B 1 39  GLU 39  86  86  GLU GLU B . n 
B 1 40  ASP 40  87  87  ASP ASP B . n 
B 1 41  ARG 41  88  88  ARG ARG B . n 
B 1 42  ALA 42  89  89  ALA ALA B . n 
B 1 43  ALA 43  90  90  ALA ALA B . n 
B 1 44  PHE 44  91  91  PHE PHE B . n 
B 1 45  VAL 45  92  92  VAL VAL B . n 
B 1 46  ALA 46  93  93  ALA ALA B . n 
B 1 47  LEU 47  94  94  LEU LEU B . n 
B 1 48  LEU 48  95  95  LEU LEU B . n 
B 1 49  LYS 49  96  96  LYS LYS B . n 
B 1 50  GLU 50  97  97  GLU GLU B . n 
B 1 51  TRP 51  98  98  TRP TRP B . n 
B 1 52  THR 52  99  99  THR THR B . n 
B 1 53  ALA 53  100 100 ALA ALA B . n 
B 1 54  ALA 54  101 101 ALA ALA B . n 
B 1 55  ALA 55  102 102 ALA ALA B . n 
B 1 56  ARG 56  103 103 ARG ARG B . n 
B 1 57  ARG 57  104 104 ARG ARG B . n 
B 1 58  LEU 58  105 105 LEU LEU B . n 
B 1 59  THR 59  106 106 THR THR B . n 
B 1 60  ALA 60  107 107 ALA ALA B . n 
B 1 61  GLY 61  108 108 GLY GLY B . n 
B 1 62  HIS 62  109 109 HIS HIS B . n 
B 1 63  ALA 63  110 110 ALA ALA B . n 
B 1 64  VAL 64  111 111 VAL VAL B . n 
B 1 65  GLY 65  112 112 GLY GLY B . n 
B 1 66  GLU 66  113 113 GLU GLU B . n 
B 1 67  GLY 67  114 114 GLY GLY B . n 
B 1 68  ALA 68  115 115 ALA ALA B . n 
B 1 69  TYR 69  116 116 TYR TYR B . n 
B 1 70  GLY 70  117 117 GLY GLY B . n 
B 1 71  GLY 71  118 118 GLY GLY B . n 
B 1 72  LEU 72  119 119 LEU LEU B . n 
B 1 73  PRO 73  120 120 PRO PRO B . n 
B 1 74  GLU 74  121 121 GLU GLU B . n 
B 1 75  ALA 75  122 122 ALA ALA B . n 
B 1 76  PRO 76  123 123 PRO PRO B . n 
B 1 77  PRO 77  124 124 PRO PRO B . n 
B 1 78  ASP 78  125 125 ASP ASP B . n 
B 1 79  ASP 79  126 126 ASP ASP B . n 
B 1 80  THR 80  127 127 THR THR B . n 
B 1 81  GLY 81  128 128 GLY GLY B . n 
B 1 82  GLU 82  129 129 GLU GLU B . n 
B 1 83  ALA 83  130 130 ALA ALA B . n 
B 1 84  LEU 84  131 131 LEU LEU B . n 
B 1 85  GLY 85  132 132 GLY GLY B . n 
B 1 86  LEU 86  133 133 LEU LEU B . n 
B 1 87  LYS 87  134 134 LYS LYS B . n 
B 1 88  PRO 88  135 135 PRO PRO B . n 
B 1 89  SER 89  136 136 SER SER B . n 
B 1 90  ARG 90  137 137 ARG ARG B . n 
B 1 91  LEU 91  138 138 LEU LEU B . n 
B 1 92  THR 92  139 139 THR THR B . n 
B 1 93  LEU 93  140 140 LEU LEU B . n 
B 1 94  THR 94  141 141 THR THR B . n 
B 1 95  ILE 95  142 142 ILE ILE B . n 
B 1 96  GLY 96  143 143 GLY GLY B . n 
B 1 97  PHE 97  144 144 PHE PHE B . n 
B 1 98  GLY 98  145 145 GLY GLY B . n 
B 1 99  PRO 99  146 146 PRO PRO B . n 
B 1 100 SER 100 147 147 SER SER B . n 
B 1 101 LEU 101 148 148 LEU LEU B . n 
B 1 102 PHE 102 149 149 PHE PHE B . n 
B 1 103 THR 103 150 150 THR THR B . n 
B 1 104 ARG 104 151 151 ARG ARG B . n 
B 1 105 PHE 105 152 152 PHE PHE B . n 
B 1 106 GLY 106 153 153 GLY GLY B . n 
B 1 107 LEU 107 154 154 LEU LEU B . n 
B 1 108 ALA 108 155 155 ALA ALA B . n 
B 1 109 ASP 109 156 156 ASP ASP B . n 
B 1 110 LEU 110 157 157 LEU LEU B . n 
B 1 111 ARG 111 158 158 ARG ARG B . n 
B 1 112 PRO 112 159 159 PRO PRO B . n 
B 1 113 GLU 113 160 160 GLU GLU B . n 
B 1 114 ALA 114 161 161 ALA ALA B . n 
B 1 115 LEU 115 162 162 LEU LEU B . n 
B 1 116 ALA 116 163 163 ALA ALA B . n 
B 1 117 ASP 117 164 164 ASP ASP B . n 
B 1 118 LEU 118 165 165 LEU LEU B . n 
B 1 119 PRO 119 166 166 PRO PRO B . n 
B 1 120 LYS 120 167 167 LYS LYS B . n 
B 1 121 PHE 121 168 168 PHE PHE B . n 
B 1 122 PRO 122 169 169 PRO PRO B . n 
B 1 123 GLY 123 170 170 GLY GLY B . n 
B 1 124 ASP 124 171 171 ASP ASP B . n 
B 1 125 ASN 125 172 172 ASN ASN B . n 
B 1 126 LEU 126 173 173 LEU LEU B . n 
B 1 127 ASP 127 174 174 ASP ASP B . n 
B 1 128 ARG 128 175 175 ARG ARG B . n 
B 1 129 ALA 129 176 176 ALA ALA B . n 
B 1 130 ARG 130 177 177 ARG ARG B . n 
B 1 131 SER 131 178 178 SER SER B . n 
B 1 132 GLY 132 179 179 GLY GLY B . n 
B 1 133 GLY 133 180 180 GLY GLY B . n 
B 1 134 ASP 134 181 181 ASP ASP B . n 
B 1 135 LEU 135 182 182 LEU LEU B . n 
B 1 136 CYS 136 183 183 CYS CYS B . n 
B 1 137 VAL 137 184 184 VAL VAL B . n 
B 1 138 GLN 138 185 185 GLN GLN B . n 
B 1 139 ALA 139 186 186 ALA ALA B . n 
B 1 140 CYS 140 187 187 CYS CYS B . n 
B 1 141 ALA 141 188 188 ALA ALA B . n 
B 1 142 ASP 142 189 189 ASP ASP B . n 
B 1 143 ASP 143 190 190 ASP ASP B . n 
B 1 144 PRO 144 191 191 PRO PRO B . n 
B 1 145 GLN 145 192 192 GLN GLN B . n 
B 1 146 VAL 146 193 193 VAL VAL B . n 
B 1 147 ALA 147 194 194 ALA ALA B . n 
B 1 148 VAL 148 195 195 VAL VAL B . n 
B 1 149 HIS 149 196 196 HIS HIS B . n 
B 1 150 ALA 150 197 197 ALA ALA B . n 
B 1 151 ILE 151 198 198 ILE ILE B . n 
B 1 152 ARG 152 199 199 ARG ARG B . n 
B 1 153 ASN 153 200 200 ASN ASN B . n 
B 1 154 LEU 154 201 201 LEU LEU B . n 
B 1 155 ALA 155 202 202 ALA ALA B . n 
B 1 156 ARG 156 203 203 ARG ARG B . n 
B 1 157 ILE 157 204 204 ILE ILE B . n 
B 1 158 GLY 158 205 205 GLY GLY B . n 
B 1 159 PHE 159 206 206 PHE PHE B . n 
B 1 160 GLY 160 207 207 GLY GLY B . n 
B 1 161 LYS 161 208 208 LYS LYS B . n 
B 1 162 VAL 162 209 209 VAL VAL B . n 
B 1 163 VAL 163 210 210 VAL VAL B . n 
B 1 164 VAL 164 211 211 VAL VAL B . n 
B 1 165 ARG 165 212 212 ARG ARG B . n 
B 1 166 TRP 166 213 213 TRP TRP B . n 
B 1 167 SER 167 214 214 SER SER B . n 
B 1 168 GLN 168 215 215 GLN GLN B . n 
B 1 169 LEU 169 216 216 LEU LEU B . n 
B 1 170 GLY 170 217 217 GLY GLY B . n 
B 1 171 PHE 171 218 218 PHE PHE B . n 
B 1 172 GLY 172 219 219 GLY GLY B . n 
B 1 173 LYS 173 220 220 LYS LYS B . n 
B 1 174 THR 174 221 221 THR THR B . n 
B 1 175 SER 175 222 222 SER SER B . n 
B 1 176 SER 176 223 223 SER SER B . n 
B 1 177 THR 177 224 224 THR THR B . n 
B 1 178 THR 178 225 225 THR THR B . n 
B 1 179 PRO 179 226 226 PRO PRO B . n 
B 1 180 ASP 180 227 227 ASP ASP B . n 
B 1 181 LYS 181 228 228 LYS LYS B . n 
B 1 182 GLN 182 229 229 GLN GLN B . n 
B 1 183 THR 183 230 230 THR THR B . n 
B 1 184 PRO 184 231 231 PRO PRO B . n 
B 1 185 ARG 185 232 232 ARG ARG B . n 
B 1 186 ASN 186 233 233 ASN ASN B . n 
B 1 187 LEU 187 234 234 LEU LEU B . n 
B 1 188 LEU 188 235 235 LEU LEU B . n 
B 1 189 GLY 189 236 236 GLY GLY B . n 
B 1 190 PHE 190 237 237 PHE PHE B . n 
B 1 191 LYS 191 238 238 LYS LYS B . n 
B 1 192 ASP 192 239 239 ASP ASP B . n 
B 1 193 GLY 193 240 240 GLY GLY B . n 
B 1 194 THR 194 241 241 THR THR B . n 
B 1 195 ARG 195 242 242 ARG ARG B . n 
B 1 196 ASN 196 243 243 ASN ASN B . n 
B 1 197 ILE 197 244 244 ILE ILE B . n 
B 1 198 ALA 198 245 245 ALA ALA B . n 
B 1 199 GLY 199 246 246 GLY GLY B . n 
B 1 200 THR 200 247 247 THR THR B . n 
B 1 201 GLU 201 248 248 GLU GLU B . n 
B 1 202 LYS 202 249 249 LYS LYS B . n 
B 1 203 ASP 203 250 250 ASP ASP B . n 
B 1 204 ARG 204 251 251 ARG ARG B . n 
B 1 205 LEU 205 252 252 LEU LEU B . n 
B 1 206 ASP 206 253 253 ASP ASP B . n 
B 1 207 ARG 207 254 254 ARG ARG B . n 
B 1 208 PHE 208 255 255 PHE PHE B . n 
B 1 209 VAL 209 256 256 VAL VAL B . n 
B 1 210 TRP 210 257 257 TRP TRP B . n 
B 1 211 ALA 211 258 258 ALA ALA B . n 
B 1 212 ALA 212 259 259 ALA ALA B . n 
B 1 213 GLU 213 260 260 GLU GLU B . n 
B 1 214 LYS 214 261 261 LYS LYS B . n 
B 1 215 ASP 215 262 262 ASP ASP B . n 
B 1 216 GLY 216 263 263 GLY GLY B . n 
B 1 217 THR 217 264 264 THR THR B . n 
B 1 218 PRO 218 265 265 PRO PRO B . n 
B 1 219 TRP 219 266 266 TRP TRP B . n 
B 1 220 MET 220 267 267 MET MET B . n 
B 1 221 THR 221 268 268 THR THR B . n 
B 1 222 GLY 222 269 269 GLY GLY B . n 
B 1 223 GLY 223 270 270 GLY GLY B . n 
B 1 224 SER 224 271 271 SER SER B . n 
B 1 225 TYR 225 272 272 TYR TYR B . n 
B 1 226 LEU 226 273 273 LEU LEU B . n 
B 1 227 VAL 227 274 274 VAL VAL B . n 
B 1 228 ALA 228 275 275 ALA ALA B . n 
B 1 229 ARG 229 276 276 ARG ARG B . n 
B 1 230 ARG 230 277 277 ARG ARG B . n 
B 1 231 ILE 231 278 278 ILE ILE B . n 
B 1 232 ARG 232 279 279 ARG ARG B . n 
B 1 233 MET 233 280 280 MET MET B . n 
B 1 234 HIS 234 281 281 HIS HIS B . n 
B 1 235 ILE 235 282 282 ILE ILE B . n 
B 1 236 GLU 236 283 283 GLU GLU B . n 
B 1 237 THR 237 284 284 THR THR B . n 
B 1 238 TRP 238 285 285 TRP TRP B . n 
B 1 239 ASP 239 286 286 ASP ASP B . n 
B 1 240 ARG 240 287 287 ARG ARG B . n 
B 1 241 ALA 241 288 288 ALA ALA B . n 
B 1 242 SER 242 289 289 SER SER B . n 
B 1 243 LEU 243 290 290 LEU LEU B . n 
B 1 244 GLN 244 291 291 GLN GLN B . n 
B 1 245 GLU 245 292 292 GLU GLU B . n 
B 1 246 GLN 246 293 293 GLN GLN B . n 
B 1 247 GLU 247 294 294 GLU GLU B . n 
B 1 248 ASP 248 295 295 ASP ASP B . n 
B 1 249 VAL 249 296 296 VAL VAL B . n 
B 1 250 PHE 250 297 297 PHE PHE B . n 
B 1 251 GLY 251 298 298 GLY GLY B . n 
B 1 252 ARG 252 299 299 ARG ARG B . n 
B 1 253 ASP 253 300 300 ASP ASP B . n 
B 1 254 LYS 254 301 301 LYS LYS B . n 
B 1 255 GLY 255 302 302 GLY GLY B . n 
B 1 256 GLU 256 303 303 GLU GLU B . n 
B 1 257 GLY 257 304 304 GLY GLY B . n 
B 1 258 ALA 258 305 305 ALA ALA B . n 
B 1 259 PRO 259 306 306 PRO PRO B . n 
B 1 260 VAL 260 307 307 VAL VAL B . n 
B 1 261 GLY 261 308 308 GLY GLY B . n 
B 1 262 LYS 262 309 309 LYS LYS B . n 
B 1 263 ALA 263 310 310 ALA ALA B . n 
B 1 264 LYS 264 311 311 LYS LYS B . n 
B 1 265 GLU 265 312 312 GLU GLU B . n 
B 1 266 ARG 266 313 313 ARG ARG B . n 
B 1 267 ASP 267 314 314 ASP ASP B . n 
B 1 268 GLU 268 315 315 GLU GLU B . n 
B 1 269 PRO 269 316 316 PRO PRO B . n 
B 1 270 PHE 270 317 317 PHE PHE B . n 
B 1 271 LEU 271 318 318 LEU LEU B . n 
B 1 272 LYS 272 319 319 LYS LYS B . n 
B 1 273 ALA 273 320 320 ALA ALA B . n 
B 1 274 MET 274 321 321 MET MET B . n 
B 1 275 LYS 275 322 322 LYS LYS B . n 
B 1 276 PRO 276 323 323 PRO PRO B . n 
B 1 277 ASP 277 324 324 ASP ASP B . n 
B 1 278 ALA 278 325 325 ALA ALA B . n 
B 1 279 HIS 279 326 326 HIS HIS B . n 
B 1 280 VAL 280 327 327 VAL VAL B . n 
B 1 281 ARG 281 328 328 ARG ARG B . n 
B 1 282 LEU 282 329 329 LEU LEU B . n 
B 1 283 ALA 283 330 330 ALA ALA B . n 
B 1 284 HIS 284 331 331 HIS HIS B . n 
B 1 285 PRO 285 332 332 PRO PRO B . n 
B 1 286 ASP 286 333 333 ASP ASP B . n 
B 1 287 SER 287 334 334 SER SER B . n 
B 1 288 ASN 288 335 335 ASN ASN B . n 
B 1 289 GLY 289 336 336 GLY GLY B . n 
B 1 290 GLY 290 337 337 GLY GLY B . n 
B 1 291 ALA 291 338 338 ALA ALA B . n 
B 1 292 THR 292 339 339 THR THR B . n 
B 1 293 LEU 293 340 340 LEU LEU B . n 
B 1 294 LEU 294 341 341 LEU LEU B . n 
B 1 295 ARG 295 342 342 ARG ARG B . n 
B 1 296 ARG 296 343 343 ARG ARG B . n 
B 1 297 GLY 297 344 344 GLY GLY B . n 
B 1 298 TYR 298 345 345 TYR TYR B . n 
B 1 299 SER 299 346 346 SER SER B . n 
B 1 300 PHE 300 347 347 PHE PHE B . n 
B 1 301 THR 301 348 348 THR THR B . n 
B 1 302 ASP 302 349 349 ASP ASP B . n 
B 1 303 GLY 303 350 350 GLY GLY B . n 
B 1 304 THR 304 351 351 THR THR B . n 
B 1 305 ASP 305 352 352 ASP ASP B . n 
B 1 306 GLY 306 353 353 GLY GLY B . n 
B 1 307 LEU 307 354 354 LEU LEU B . n 
B 1 308 GLY 308 355 355 GLY GLY B . n 
B 1 309 ARG 309 356 356 ARG ARG B . n 
B 1 310 LEU 310 357 357 LEU LEU B . n 
B 1 311 ASP 311 358 358 ASP ASP B . n 
B 1 312 ALA 312 359 359 ALA ALA B . n 
B 1 313 GLY 313 360 360 GLY GLY B . n 
B 1 314 LEU 314 361 361 LEU LEU B . n 
B 1 315 PHE 315 362 362 PHE PHE B . n 
B 1 316 PHE 316 363 363 PHE PHE B . n 
B 1 317 LEU 317 364 364 LEU LEU B . n 
B 1 318 ALA 318 365 365 ALA ALA B . n 
B 1 319 TYR 319 366 366 TYR TYR B . n 
B 1 320 GLN 320 367 367 GLN GLN B . n 
B 1 321 ARG 321 368 368 ARG ARG B . n 
B 1 322 ASP 322 369 369 ASP ASP B . n 
B 1 323 ILE 323 370 370 ILE ILE B . n 
B 1 324 ARG 324 371 371 ARG ARG B . n 
B 1 325 THR 325 372 372 THR THR B . n 
B 1 326 GLY 326 373 373 GLY GLY B . n 
B 1 327 PHE 327 374 374 PHE PHE B . n 
B 1 328 VAL 328 375 375 VAL VAL B . n 
B 1 329 PRO 329 376 376 PRO PRO B . n 
B 1 330 VAL 330 377 377 VAL VAL B . n 
B 1 331 GLN 331 378 378 GLN GLN B . n 
B 1 332 ARG 332 379 379 ARG ARG B . n 
B 1 333 ASN 333 380 380 ASN ASN B . n 
B 1 334 LEU 334 381 381 LEU LEU B . n 
B 1 335 ALA 335 382 382 ALA ALA B . n 
B 1 336 THR 336 383 383 THR THR B . n 
B 1 337 ASP 337 384 384 ASP ASP B . n 
B 1 338 ALA 338 385 385 ALA ALA B . n 
B 1 339 LEU 339 386 386 LEU LEU B . n 
B 1 340 ASN 340 387 387 ASN ASN B . n 
B 1 341 GLU 341 388 388 GLU GLU B . n 
B 1 342 PHE 342 389 389 PHE PHE B . n 
B 1 343 ILE 343 390 390 ILE ILE B . n 
B 1 344 GLN 344 391 391 GLN GLN B . n 
B 1 345 HIS 345 392 392 HIS HIS B . n 
B 1 346 VAL 346 393 393 VAL VAL B . n 
B 1 347 GLY 347 394 394 GLY GLY B . n 
B 1 348 SER 348 395 395 SER SER B . n 
B 1 349 ALA 349 396 396 ALA ALA B . n 
B 1 350 VAL 350 397 397 VAL VAL B . n 
B 1 351 PHE 351 398 398 PHE PHE B . n 
B 1 352 ALA 352 399 399 ALA ALA B . n 
B 1 353 VAL 353 400 400 VAL VAL B . n 
B 1 354 PRO 354 401 401 PRO PRO B . n 
B 1 355 PRO 355 402 402 PRO PRO B . n 
B 1 356 GLY 356 403 403 GLY GLY B . n 
B 1 357 VAL 357 404 404 VAL VAL B . n 
B 1 358 ARG 358 405 405 ARG ARG B . n 
B 1 359 ASP 359 406 406 ASP ASP B . n 
B 1 360 ALA 360 407 407 ALA ALA B . n 
B 1 361 ASP 361 408 408 ASP ASP B . n 
B 1 362 ASP 362 409 409 ASP ASP B . n 
B 1 363 TRP 363 410 410 TRP TRP B . n 
B 1 364 TRP 364 411 411 TRP TRP B . n 
B 1 365 GLY 365 412 412 GLY GLY B . n 
B 1 366 SER 366 413 413 SER SER B . n 
B 1 367 THR 367 414 414 THR THR B . n 
B 1 368 LEU 368 415 415 LEU LEU B . n 
B 1 369 PHE 369 416 416 PHE PHE B . n 
B 1 370 GLY 370 417 417 GLY GLY B . n 
B 1 371 LYS 371 418 ?   ?   ?   B . n 
B 1 372 GLU 372 419 ?   ?   ?   B . n 
B 1 373 ALA 373 420 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEM 1   501 501  HEM HEM A . 
D 2 HEM 1   501 501  HEM HEM B . 
E 3 HOH 1   601 824  HOH HOH A . 
E 3 HOH 2   602 44   HOH HOH A . 
E 3 HOH 3   603 811  HOH HOH A . 
E 3 HOH 4   604 666  HOH HOH A . 
E 3 HOH 5   605 710  HOH HOH A . 
E 3 HOH 6   606 64   HOH HOH A . 
E 3 HOH 7   607 23   HOH HOH A . 
E 3 HOH 8   608 50   HOH HOH A . 
E 3 HOH 9   609 648  HOH HOH A . 
E 3 HOH 10  610 17   HOH HOH A . 
E 3 HOH 11  611 633  HOH HOH A . 
E 3 HOH 12  612 41   HOH HOH A . 
E 3 HOH 13  613 46   HOH HOH A . 
E 3 HOH 14  614 636  HOH HOH A . 
E 3 HOH 15  615 614  HOH HOH A . 
E 3 HOH 16  616 840  HOH HOH A . 
E 3 HOH 17  617 972  HOH HOH A . 
E 3 HOH 18  618 677  HOH HOH A . 
E 3 HOH 19  619 708  HOH HOH A . 
E 3 HOH 20  620 606  HOH HOH A . 
E 3 HOH 21  621 21   HOH HOH A . 
E 3 HOH 22  622 9    HOH HOH A . 
E 3 HOH 23  623 842  HOH HOH A . 
E 3 HOH 24  624 723  HOH HOH A . 
E 3 HOH 25  625 40   HOH HOH A . 
E 3 HOH 26  626 690  HOH HOH A . 
E 3 HOH 27  627 631  HOH HOH A . 
E 3 HOH 28  628 711  HOH HOH A . 
E 3 HOH 29  629 33   HOH HOH A . 
E 3 HOH 30  630 629  HOH HOH A . 
E 3 HOH 31  631 694  HOH HOH A . 
E 3 HOH 32  632 799  HOH HOH A . 
E 3 HOH 33  633 730  HOH HOH A . 
E 3 HOH 34  634 720  HOH HOH A . 
E 3 HOH 35  635 675  HOH HOH A . 
E 3 HOH 36  636 626  HOH HOH A . 
E 3 HOH 37  637 643  HOH HOH A . 
E 3 HOH 38  638 625  HOH HOH A . 
E 3 HOH 39  639 1    HOH HOH A . 
E 3 HOH 40  640 37   HOH HOH A . 
E 3 HOH 41  641 681  HOH HOH A . 
E 3 HOH 42  642 662  HOH HOH A . 
E 3 HOH 43  643 714  HOH HOH A . 
E 3 HOH 44  644 728  HOH HOH A . 
E 3 HOH 45  645 611  HOH HOH A . 
E 3 HOH 46  646 6    HOH HOH A . 
E 3 HOH 47  647 661  HOH HOH A . 
E 3 HOH 48  648 913  HOH HOH A . 
E 3 HOH 49  649 685  HOH HOH A . 
E 3 HOH 50  650 853  HOH HOH A . 
E 3 HOH 51  651 642  HOH HOH A . 
E 3 HOH 52  652 613  HOH HOH A . 
E 3 HOH 53  653 743  HOH HOH A . 
E 3 HOH 54  654 61   HOH HOH A . 
E 3 HOH 55  655 734  HOH HOH A . 
E 3 HOH 56  656 716  HOH HOH A . 
E 3 HOH 57  657 668  HOH HOH A . 
E 3 HOH 58  658 692  HOH HOH A . 
E 3 HOH 59  659 875  HOH HOH A . 
E 3 HOH 60  660 776  HOH HOH A . 
E 3 HOH 61  661 45   HOH HOH A . 
E 3 HOH 62  662 721  HOH HOH A . 
E 3 HOH 63  663 654  HOH HOH A . 
E 3 HOH 64  664 674  HOH HOH A . 
E 3 HOH 65  665 749  HOH HOH A . 
E 3 HOH 66  666 755  HOH HOH A . 
E 3 HOH 67  667 738  HOH HOH A . 
E 3 HOH 68  668 650  HOH HOH A . 
E 3 HOH 69  669 639  HOH HOH A . 
E 3 HOH 70  670 712  HOH HOH A . 
E 3 HOH 71  671 51   HOH HOH A . 
E 3 HOH 72  672 621  HOH HOH A . 
E 3 HOH 73  673 740  HOH HOH A . 
E 3 HOH 74  674 783  HOH HOH A . 
E 3 HOH 75  675 669  HOH HOH A . 
E 3 HOH 76  676 656  HOH HOH A . 
E 3 HOH 77  677 630  HOH HOH A . 
E 3 HOH 78  678 27   HOH HOH A . 
E 3 HOH 79  679 900  HOH HOH A . 
E 3 HOH 80  680 765  HOH HOH A . 
E 3 HOH 81  681 839  HOH HOH A . 
E 3 HOH 82  682 647  HOH HOH A . 
E 3 HOH 83  683 14   HOH HOH A . 
E 3 HOH 84  684 684  HOH HOH A . 
E 3 HOH 85  685 19   HOH HOH A . 
E 3 HOH 86  686 696  HOH HOH A . 
E 3 HOH 87  687 704  HOH HOH A . 
E 3 HOH 88  688 944  HOH HOH A . 
E 3 HOH 89  689 739  HOH HOH A . 
E 3 HOH 90  690 718  HOH HOH A . 
E 3 HOH 91  691 699  HOH HOH A . 
E 3 HOH 92  692 705  HOH HOH A . 
E 3 HOH 93  693 719  HOH HOH A . 
E 3 HOH 94  694 641  HOH HOH A . 
E 3 HOH 95  695 800  HOH HOH A . 
E 3 HOH 96  696 698  HOH HOH A . 
E 3 HOH 97  697 807  HOH HOH A . 
E 3 HOH 98  698 789  HOH HOH A . 
E 3 HOH 99  699 818  HOH HOH A . 
E 3 HOH 100 700 702  HOH HOH A . 
E 3 HOH 101 701 937  HOH HOH A . 
E 3 HOH 102 702 794  HOH HOH A . 
E 3 HOH 103 703 847  HOH HOH A . 
E 3 HOH 104 704 623  HOH HOH A . 
E 3 HOH 105 705 49   HOH HOH A . 
E 3 HOH 106 706 874  HOH HOH A . 
E 3 HOH 107 707 790  HOH HOH A . 
E 3 HOH 108 708 727  HOH HOH A . 
E 3 HOH 109 709 737  HOH HOH A . 
E 3 HOH 110 710 1016 HOH HOH A . 
E 3 HOH 111 711 851  HOH HOH A . 
E 3 HOH 112 712 759  HOH HOH A . 
E 3 HOH 113 713 795  HOH HOH A . 
E 3 HOH 114 714 695  HOH HOH A . 
E 3 HOH 115 715 754  HOH HOH A . 
E 3 HOH 116 716 709  HOH HOH A . 
E 3 HOH 117 717 733  HOH HOH A . 
E 3 HOH 118 718 3    HOH HOH A . 
E 3 HOH 119 719 672  HOH HOH A . 
E 3 HOH 120 720 706  HOH HOH A . 
E 3 HOH 121 721 827  HOH HOH A . 
E 3 HOH 122 722 990  HOH HOH A . 
E 3 HOH 123 723 663  HOH HOH A . 
E 3 HOH 124 724 69   HOH HOH A . 
E 3 HOH 125 725 676  HOH HOH A . 
E 3 HOH 126 726 933  HOH HOH A . 
E 3 HOH 127 727 893  HOH HOH A . 
E 3 HOH 128 728 805  HOH HOH A . 
E 3 HOH 129 729 745  HOH HOH A . 
E 3 HOH 130 730 822  HOH HOH A . 
E 3 HOH 131 731 744  HOH HOH A . 
E 3 HOH 132 732 680  HOH HOH A . 
E 3 HOH 133 733 736  HOH HOH A . 
E 3 HOH 134 734 686  HOH HOH A . 
E 3 HOH 135 735 12   HOH HOH A . 
E 3 HOH 136 736 801  HOH HOH A . 
E 3 HOH 137 737 791  HOH HOH A . 
E 3 HOH 138 738 804  HOH HOH A . 
E 3 HOH 139 739 775  HOH HOH A . 
E 3 HOH 140 740 928  HOH HOH A . 
E 3 HOH 141 741 897  HOH HOH A . 
E 3 HOH 142 742 752  HOH HOH A . 
E 3 HOH 143 743 28   HOH HOH A . 
E 3 HOH 144 744 63   HOH HOH A . 
E 3 HOH 145 745 817  HOH HOH A . 
E 3 HOH 146 746 649  HOH HOH A . 
E 3 HOH 147 747 724  HOH HOH A . 
E 3 HOH 148 748 707  HOH HOH A . 
E 3 HOH 149 749 863  HOH HOH A . 
E 3 HOH 150 750 815  HOH HOH A . 
E 3 HOH 151 751 751  HOH HOH A . 
E 3 HOH 152 752 769  HOH HOH A . 
E 3 HOH 153 753 806  HOH HOH A . 
E 3 HOH 154 754 42   HOH HOH A . 
E 3 HOH 155 755 803  HOH HOH A . 
E 3 HOH 156 756 829  HOH HOH A . 
E 3 HOH 157 757 60   HOH HOH A . 
E 3 HOH 158 758 793  HOH HOH A . 
E 3 HOH 159 759 688  HOH HOH A . 
E 3 HOH 160 760 652  HOH HOH A . 
E 3 HOH 161 761 673  HOH HOH A . 
E 3 HOH 162 762 798  HOH HOH A . 
E 3 HOH 163 763 871  HOH HOH A . 
E 3 HOH 164 764 683  HOH HOH A . 
E 3 HOH 165 765 713  HOH HOH A . 
E 3 HOH 166 766 836  HOH HOH A . 
E 3 HOH 167 767 2    HOH HOH A . 
E 3 HOH 168 768 864  HOH HOH A . 
E 3 HOH 169 769 748  HOH HOH A . 
E 3 HOH 170 770 778  HOH HOH A . 
E 3 HOH 171 771 59   HOH HOH A . 
E 3 HOH 172 772 858  HOH HOH A . 
E 3 HOH 173 773 865  HOH HOH A . 
E 3 HOH 174 774 762  HOH HOH A . 
E 3 HOH 175 775 834  HOH HOH A . 
E 3 HOH 176 776 819  HOH HOH A . 
E 3 HOH 177 777 679  HOH HOH A . 
E 3 HOH 178 778 860  HOH HOH A . 
E 3 HOH 179 779 854  HOH HOH A . 
E 3 HOH 180 780 848  HOH HOH A . 
E 3 HOH 181 781 922  HOH HOH A . 
E 3 HOH 182 782 20   HOH HOH A . 
E 3 HOH 183 783 788  HOH HOH A . 
E 3 HOH 184 784 849  HOH HOH A . 
E 3 HOH 185 785 820  HOH HOH A . 
E 3 HOH 186 786 823  HOH HOH A . 
E 3 HOH 187 787 810  HOH HOH A . 
E 3 HOH 188 788 808  HOH HOH A . 
E 3 HOH 189 789 701  HOH HOH A . 
E 3 HOH 190 790 909  HOH HOH A . 
E 3 HOH 191 791 924  HOH HOH A . 
E 3 HOH 192 792 838  HOH HOH A . 
E 3 HOH 193 793 756  HOH HOH A . 
E 3 HOH 194 794 651  HOH HOH A . 
E 3 HOH 195 795 832  HOH HOH A . 
E 3 HOH 196 796 855  HOH HOH A . 
E 3 HOH 197 797 899  HOH HOH A . 
E 3 HOH 198 798 892  HOH HOH A . 
E 3 HOH 199 799 938  HOH HOH A . 
E 3 HOH 200 800 890  HOH HOH A . 
E 3 HOH 201 801 802  HOH HOH A . 
E 3 HOH 202 802 772  HOH HOH A . 
E 3 HOH 203 803 18   HOH HOH A . 
E 3 HOH 204 804 916  HOH HOH A . 
E 3 HOH 205 805 841  HOH HOH A . 
E 3 HOH 206 806 889  HOH HOH A . 
E 3 HOH 207 807 917  HOH HOH A . 
E 3 HOH 208 808 30   HOH HOH A . 
E 3 HOH 209 809 878  HOH HOH A . 
E 3 HOH 210 810 798  HOH HOH A . 
E 3 HOH 211 811 812  HOH HOH A . 
E 3 HOH 212 812 920  HOH HOH A . 
E 3 HOH 213 813 895  HOH HOH A . 
E 3 HOH 214 814 52   HOH HOH A . 
E 3 HOH 215 815 54   HOH HOH A . 
E 3 HOH 216 816 68   HOH HOH A . 
E 3 HOH 217 817 905  HOH HOH A . 
E 3 HOH 218 818 884  HOH HOH A . 
E 3 HOH 219 819 48   HOH HOH A . 
E 3 HOH 220 820 38   HOH HOH A . 
E 3 HOH 221 821 948  HOH HOH A . 
E 3 HOH 222 822 921  HOH HOH A . 
E 3 HOH 223 823 911  HOH HOH A . 
E 3 HOH 224 824 986  HOH HOH A . 
E 3 HOH 225 825 845  HOH HOH A . 
E 3 HOH 226 826 869  HOH HOH A . 
E 3 HOH 227 827 843  HOH HOH A . 
E 3 HOH 228 828 8    HOH HOH A . 
E 3 HOH 229 829 877  HOH HOH A . 
E 3 HOH 230 830 946  HOH HOH A . 
E 3 HOH 231 831 809  HOH HOH A . 
E 3 HOH 232 832 919  HOH HOH A . 
E 3 HOH 233 833 968  HOH HOH A . 
E 3 HOH 234 834 879  HOH HOH A . 
E 3 HOH 235 835 996  HOH HOH A . 
E 3 HOH 236 836 957  HOH HOH A . 
E 3 HOH 237 837 7    HOH HOH A . 
E 3 HOH 238 838 954  HOH HOH A . 
E 3 HOH 239 839 955  HOH HOH A . 
E 3 HOH 240 840 969  HOH HOH A . 
E 3 HOH 241 841 988  HOH HOH A . 
E 3 HOH 242 842 872  HOH HOH A . 
E 3 HOH 243 843 1006 HOH HOH A . 
E 3 HOH 244 844 687  HOH HOH A . 
E 3 HOH 245 845 962  HOH HOH A . 
E 3 HOH 246 846 1003 HOH HOH A . 
E 3 HOH 247 847 982  HOH HOH A . 
E 3 HOH 248 848 998  HOH HOH A . 
E 3 HOH 249 849 1020 HOH HOH A . 
E 3 HOH 250 850 1017 HOH HOH A . 
E 3 HOH 251 851 928  HOH HOH A . 
E 3 HOH 252 852 992  HOH HOH A . 
E 3 HOH 253 853 615  HOH HOH A . 
E 3 HOH 254 854 1036 HOH HOH A . 
E 3 HOH 255 855 965  HOH HOH A . 
E 3 HOH 256 856 773  HOH HOH A . 
F 3 HOH 1   601 874  HOH HOH B . 
F 3 HOH 2   602 766  HOH HOH B . 
F 3 HOH 3   603 710  HOH HOH B . 
F 3 HOH 4   604 658  HOH HOH B . 
F 3 HOH 5   605 845  HOH HOH B . 
F 3 HOH 6   606 609  HOH HOH B . 
F 3 HOH 7   607 775  HOH HOH B . 
F 3 HOH 8   608 672  HOH HOH B . 
F 3 HOH 9   609 719  HOH HOH B . 
F 3 HOH 10  610 726  HOH HOH B . 
F 3 HOH 11  611 861  HOH HOH B . 
F 3 HOH 12  612 601  HOH HOH B . 
F 3 HOH 13  613 765  HOH HOH B . 
F 3 HOH 14  614 746  HOH HOH B . 
F 3 HOH 15  615 67   HOH HOH B . 
F 3 HOH 16  616 43   HOH HOH B . 
F 3 HOH 17  617 624  HOH HOH B . 
F 3 HOH 18  618 618  HOH HOH B . 
F 3 HOH 19  619 714  HOH HOH B . 
F 3 HOH 20  620 637  HOH HOH B . 
F 3 HOH 21  621 664  HOH HOH B . 
F 3 HOH 22  622 829  HOH HOH B . 
F 3 HOH 23  623 611  HOH HOH B . 
F 3 HOH 24  624 865  HOH HOH B . 
F 3 HOH 25  625 24   HOH HOH B . 
F 3 HOH 26  626 638  HOH HOH B . 
F 3 HOH 27  627 688  HOH HOH B . 
F 3 HOH 28  628 606  HOH HOH B . 
F 3 HOH 29  629 720  HOH HOH B . 
F 3 HOH 30  630 754  HOH HOH B . 
F 3 HOH 31  631 771  HOH HOH B . 
F 3 HOH 32  632 26   HOH HOH B . 
F 3 HOH 33  633 612  HOH HOH B . 
F 3 HOH 34  634 654  HOH HOH B . 
F 3 HOH 35  635 817  HOH HOH B . 
F 3 HOH 36  636 956  HOH HOH B . 
F 3 HOH 37  637 621  HOH HOH B . 
F 3 HOH 38  638 772  HOH HOH B . 
F 3 HOH 39  639 610  HOH HOH B . 
F 3 HOH 40  640 645  HOH HOH B . 
F 3 HOH 41  641 826  HOH HOH B . 
F 3 HOH 42  642 66   HOH HOH B . 
F 3 HOH 43  643 713  HOH HOH B . 
F 3 HOH 44  644 752  HOH HOH B . 
F 3 HOH 45  645 619  HOH HOH B . 
F 3 HOH 46  646 36   HOH HOH B . 
F 3 HOH 47  647 738  HOH HOH B . 
F 3 HOH 48  648 16   HOH HOH B . 
F 3 HOH 49  649 614  HOH HOH B . 
F 3 HOH 50  650 35   HOH HOH B . 
F 3 HOH 51  651 698  HOH HOH B . 
F 3 HOH 52  652 607  HOH HOH B . 
F 3 HOH 53  653 696  HOH HOH B . 
F 3 HOH 54  654 652  HOH HOH B . 
F 3 HOH 55  655 794  HOH HOH B . 
F 3 HOH 56  656 668  HOH HOH B . 
F 3 HOH 57  657 748  HOH HOH B . 
F 3 HOH 58  658 25   HOH HOH B . 
F 3 HOH 59  659 699  HOH HOH B . 
F 3 HOH 60  660 682  HOH HOH B . 
F 3 HOH 61  661 616  HOH HOH B . 
F 3 HOH 62  662 702  HOH HOH B . 
F 3 HOH 63  663 641  HOH HOH B . 
F 3 HOH 64  664 728  HOH HOH B . 
F 3 HOH 65  665 695  HOH HOH B . 
F 3 HOH 66  666 646  HOH HOH B . 
F 3 HOH 67  667 657  HOH HOH B . 
F 3 HOH 68  668 806  HOH HOH B . 
F 3 HOH 69  669 657  HOH HOH B . 
F 3 HOH 70  670 685  HOH HOH B . 
F 3 HOH 71  671 923  HOH HOH B . 
F 3 HOH 72  672 947  HOH HOH B . 
F 3 HOH 73  673 650  HOH HOH B . 
F 3 HOH 74  674 818  HOH HOH B . 
F 3 HOH 75  675 662  HOH HOH B . 
F 3 HOH 76  676 737  HOH HOH B . 
F 3 HOH 77  677 34   HOH HOH B . 
F 3 HOH 78  678 625  HOH HOH B . 
F 3 HOH 79  679 655  HOH HOH B . 
F 3 HOH 80  680 763  HOH HOH B . 
F 3 HOH 81  681 816  HOH HOH B . 
F 3 HOH 82  682 636  HOH HOH B . 
F 3 HOH 83  683 651  HOH HOH B . 
F 3 HOH 84  684 853  HOH HOH B . 
F 3 HOH 85  685 801  HOH HOH B . 
F 3 HOH 86  686 797  HOH HOH B . 
F 3 HOH 87  687 755  HOH HOH B . 
F 3 HOH 88  688 693  HOH HOH B . 
F 3 HOH 89  689 840  HOH HOH B . 
F 3 HOH 90  690 736  HOH HOH B . 
F 3 HOH 91  691 5    HOH HOH B . 
F 3 HOH 92  692 642  HOH HOH B . 
F 3 HOH 93  693 800  HOH HOH B . 
F 3 HOH 94  694 758  HOH HOH B . 
F 3 HOH 95  695 769  HOH HOH B . 
F 3 HOH 96  696 629  HOH HOH B . 
F 3 HOH 97  697 862  HOH HOH B . 
F 3 HOH 98  698 678  HOH HOH B . 
F 3 HOH 99  699 708  HOH HOH B . 
F 3 HOH 100 700 707  HOH HOH B . 
F 3 HOH 101 701 10   HOH HOH B . 
F 3 HOH 102 702 730  HOH HOH B . 
F 3 HOH 103 703 630  HOH HOH B . 
F 3 HOH 104 704 732  HOH HOH B . 
F 3 HOH 105 705 780  HOH HOH B . 
F 3 HOH 106 706 57   HOH HOH B . 
F 3 HOH 107 707 70   HOH HOH B . 
F 3 HOH 108 708 644  HOH HOH B . 
F 3 HOH 109 709 770  HOH HOH B . 
F 3 HOH 110 710 700  HOH HOH B . 
F 3 HOH 111 711 762  HOH HOH B . 
F 3 HOH 112 712 674  HOH HOH B . 
F 3 HOH 113 713 866  HOH HOH B . 
F 3 HOH 114 714 676  HOH HOH B . 
F 3 HOH 115 715 767  HOH HOH B . 
F 3 HOH 116 716 743  HOH HOH B . 
F 3 HOH 117 717 832  HOH HOH B . 
F 3 HOH 118 718 751  HOH HOH B . 
F 3 HOH 119 719 32   HOH HOH B . 
F 3 HOH 120 720 727  HOH HOH B . 
F 3 HOH 121 721 785  HOH HOH B . 
F 3 HOH 122 722 740  HOH HOH B . 
F 3 HOH 123 723 628  HOH HOH B . 
F 3 HOH 124 724 704  HOH HOH B . 
F 3 HOH 125 725 725  HOH HOH B . 
F 3 HOH 126 726 631  HOH HOH B . 
F 3 HOH 127 727 640  HOH HOH B . 
F 3 HOH 128 728 887  HOH HOH B . 
F 3 HOH 129 729 735  HOH HOH B . 
F 3 HOH 130 730 782  HOH HOH B . 
F 3 HOH 131 731 15   HOH HOH B . 
F 3 HOH 132 732 724  HOH HOH B . 
F 3 HOH 133 733 855  HOH HOH B . 
F 3 HOH 134 734 666  HOH HOH B . 
F 3 HOH 135 735 757  HOH HOH B . 
F 3 HOH 136 736 796  HOH HOH B . 
F 3 HOH 137 737 690  HOH HOH B . 
F 3 HOH 138 738 703  HOH HOH B . 
F 3 HOH 139 739 683  HOH HOH B . 
F 3 HOH 140 740 648  HOH HOH B . 
F 3 HOH 141 741 834  HOH HOH B . 
F 3 HOH 142 742 58   HOH HOH B . 
F 3 HOH 143 743 739  HOH HOH B . 
F 3 HOH 144 744 776  HOH HOH B . 
F 3 HOH 145 745 786  HOH HOH B . 
F 3 HOH 146 746 904  HOH HOH B . 
F 3 HOH 147 747 706  HOH HOH B . 
F 3 HOH 148 748 822  HOH HOH B . 
F 3 HOH 149 749 799  HOH HOH B . 
F 3 HOH 150 750 742  HOH HOH B . 
F 3 HOH 151 751 819  HOH HOH B . 
F 3 HOH 152 752 633  HOH HOH B . 
F 3 HOH 153 753 792  HOH HOH B . 
F 3 HOH 154 754 709  HOH HOH B . 
F 3 HOH 155 755 963  HOH HOH B . 
F 3 HOH 156 756 848  HOH HOH B . 
F 3 HOH 157 757 753  HOH HOH B . 
F 3 HOH 158 758 756  HOH HOH B . 
F 3 HOH 159 759 774  HOH HOH B . 
F 3 HOH 160 760 793  HOH HOH B . 
F 3 HOH 161 761 813  HOH HOH B . 
F 3 HOH 162 762 749  HOH HOH B . 
F 3 HOH 163 763 803  HOH HOH B . 
F 3 HOH 164 764 759  HOH HOH B . 
F 3 HOH 165 765 779  HOH HOH B . 
F 3 HOH 166 766 741  HOH HOH B . 
F 3 HOH 167 767 47   HOH HOH B . 
F 3 HOH 168 768 747  HOH HOH B . 
F 3 HOH 169 769 718  HOH HOH B . 
F 3 HOH 170 770 770  HOH HOH B . 
F 3 HOH 171 771 837  HOH HOH B . 
F 3 HOH 172 772 701  HOH HOH B . 
F 3 HOH 173 773 802  HOH HOH B . 
F 3 HOH 174 774 639  HOH HOH B . 
F 3 HOH 175 775 649  HOH HOH B . 
F 3 HOH 176 776 634  HOH HOH B . 
F 3 HOH 177 777 768  HOH HOH B . 
F 3 HOH 178 778 792  HOH HOH B . 
F 3 HOH 179 779 716  HOH HOH B . 
F 3 HOH 180 780 824  HOH HOH B . 
F 3 HOH 181 781 860  HOH HOH B . 
F 3 HOH 182 782 791  HOH HOH B . 
F 3 HOH 183 783 839  HOH HOH B . 
F 3 HOH 184 784 873  HOH HOH B . 
F 3 HOH 185 785 870  HOH HOH B . 
F 3 HOH 186 786 812  HOH HOH B . 
F 3 HOH 187 787 715  HOH HOH B . 
F 3 HOH 188 788 673  HOH HOH B . 
F 3 HOH 189 789 815  HOH HOH B . 
F 3 HOH 190 790 959  HOH HOH B . 
F 3 HOH 191 791 656  HOH HOH B . 
F 3 HOH 192 792 863  HOH HOH B . 
F 3 HOH 193 793 797  HOH HOH B . 
F 3 HOH 194 794 844  HOH HOH B . 
F 3 HOH 195 795 823  HOH HOH B . 
F 3 HOH 196 796 773  HOH HOH B . 
F 3 HOH 197 797 663  HOH HOH B . 
F 3 HOH 198 798 838  HOH HOH B . 
F 3 HOH 199 799 623  HOH HOH B . 
F 3 HOH 200 800 608  HOH HOH B . 
F 3 HOH 201 801 29   HOH HOH B . 
F 3 HOH 202 802 882  HOH HOH B . 
F 3 HOH 203 803 888  HOH HOH B . 
F 3 HOH 204 804 781  HOH HOH B . 
F 3 HOH 205 805 761  HOH HOH B . 
F 3 HOH 206 806 857  HOH HOH B . 
F 3 HOH 207 807 681  HOH HOH B . 
F 3 HOH 208 808 912  HOH HOH B . 
F 3 HOH 209 809 777  HOH HOH B . 
F 3 HOH 210 810 795  HOH HOH B . 
F 3 HOH 211 811 809  HOH HOH B . 
F 3 HOH 212 812 864  HOH HOH B . 
F 3 HOH 213 813 784  HOH HOH B . 
F 3 HOH 214 814 854  HOH HOH B . 
F 3 HOH 215 815 731  HOH HOH B . 
F 3 HOH 216 816 827  HOH HOH B . 
F 3 HOH 217 817 789  HOH HOH B . 
F 3 HOH 218 818 856  HOH HOH B . 
F 3 HOH 219 819 760  HOH HOH B . 
F 3 HOH 220 820 909  HOH HOH B . 
F 3 HOH 221 821 852  HOH HOH B . 
F 3 HOH 222 822 804  HOH HOH B . 
F 3 HOH 223 823 868  HOH HOH B . 
F 3 HOH 224 824 896  HOH HOH B . 
F 3 HOH 225 825 691  HOH HOH B . 
F 3 HOH 226 826 55   HOH HOH B . 
F 3 HOH 227 827 843  HOH HOH B . 
F 3 HOH 228 828 810  HOH HOH B . 
F 3 HOH 229 829 828  HOH HOH B . 
F 3 HOH 230 830 831  HOH HOH B . 
F 3 HOH 231 831 878  HOH HOH B . 
F 3 HOH 232 832 850  HOH HOH B . 
F 3 HOH 233 833 22   HOH HOH B . 
F 3 HOH 234 834 851  HOH HOH B . 
F 3 HOH 235 835 935  HOH HOH B . 
F 3 HOH 236 836 886  HOH HOH B . 
F 3 HOH 237 837 907  HOH HOH B . 
F 3 HOH 238 838 905  HOH HOH B . 
F 3 HOH 239 839 891  HOH HOH B . 
F 3 HOH 240 840 872  HOH HOH B . 
F 3 HOH 241 841 745  HOH HOH B . 
F 3 HOH 242 842 901  HOH HOH B . 
F 3 HOH 243 843 903  HOH HOH B . 
F 3 HOH 244 844 56   HOH HOH B . 
F 3 HOH 245 845 53   HOH HOH B . 
F 3 HOH 246 846 744  HOH HOH B . 
F 3 HOH 247 847 830  HOH HOH B . 
F 3 HOH 248 848 889  HOH HOH B . 
F 3 HOH 249 849 859  HOH HOH B . 
F 3 HOH 250 850 932  HOH HOH B . 
F 3 HOH 251 851 880  HOH HOH B . 
F 3 HOH 252 852 39   HOH HOH B . 
F 3 HOH 253 853 622  HOH HOH B . 
F 3 HOH 254 854 875  HOH HOH B . 
F 3 HOH 255 855 892  HOH HOH B . 
F 3 HOH 256 856 913  HOH HOH B . 
F 3 HOH 257 857 877  HOH HOH B . 
F 3 HOH 258 858 31   HOH HOH B . 
F 3 HOH 259 859 4    HOH HOH B . 
F 3 HOH 260 860 807  HOH HOH B . 
F 3 HOH 261 861 62   HOH HOH B . 
F 3 HOH 262 862 920  HOH HOH B . 
F 3 HOH 263 863 933  HOH HOH B . 
F 3 HOH 264 864 966  HOH HOH B . 
F 3 HOH 265 865 899  HOH HOH B . 
F 3 HOH 266 866 931  HOH HOH B . 
F 3 HOH 267 867 881  HOH HOH B . 
F 3 HOH 268 868 910  HOH HOH B . 
F 3 HOH 269 869 660  HOH HOH B . 
F 3 HOH 270 870 763  HOH HOH B . 
F 3 HOH 271 871 895  HOH HOH B . 
F 3 HOH 272 872 65   HOH HOH B . 
F 3 HOH 273 873 917  HOH HOH B . 
F 3 HOH 274 874 712  HOH HOH B . 
F 3 HOH 275 875 808  HOH HOH B . 
F 3 HOH 276 876 950  HOH HOH B . 
F 3 HOH 277 877 944  HOH HOH B . 
F 3 HOH 278 878 937  HOH HOH B . 
F 3 HOH 279 879 963  HOH HOH B . 
F 3 HOH 280 880 955  HOH HOH B . 
F 3 HOH 281 881 971  HOH HOH B . 
F 3 HOH 282 882 916  HOH HOH B . 
F 3 HOH 283 883 983  HOH HOH B . 
F 3 HOH 284 884 958  HOH HOH B . 
F 3 HOH 285 885 973  HOH HOH B . 
F 3 HOH 286 886 949  HOH HOH B . 
F 3 HOH 287 887 604  HOH HOH B . 
F 3 HOH 288 888 982  HOH HOH B . 
F 3 HOH 289 889 841  HOH HOH B . 
F 3 HOH 290 890 981  HOH HOH B . 
F 3 HOH 291 891 991  HOH HOH B . 
F 3 HOH 292 892 939  HOH HOH B . 
F 3 HOH 293 893 733  HOH HOH B . 
F 3 HOH 294 894 929  HOH HOH B . 
F 3 HOH 295 895 1004 HOH HOH B . 
F 3 HOH 296 896 1009 HOH HOH B . 
F 3 HOH 297 897 1000 HOH HOH B . 
F 3 HOH 298 898 1001 HOH HOH B . 
F 3 HOH 299 899 1005 HOH HOH B . 
F 3 HOH 300 900 1007 HOH HOH B . 
F 3 HOH 301 901 1002 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0419 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .        3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? .        4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? .        5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   105.60 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EPK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.720 
_cell.length_a_esd                 ? 
_cell.length_b                     68.200 
_cell.length_b_esd                 ? 
_cell.length_c                     74.600 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9EPK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   9EPK 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.44 
_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          'BATCH MODE' 
_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    '12% v/v PEG 3350, 100 mM HEPES pH 7.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     294.15 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'PSI JUNGFRAU 8M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-05 
_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   1.03 
_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                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SwissFEL ARAMIS BEAMLINE ESA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ESA 
_diffrn_source.pdbx_synchrotron_site       'SwissFEL ARAMIS' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EPK 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.30 
_reflns.d_resolution_low                               35.05 
_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                                     172313 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                523.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.61 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.974 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                        ? 
# 
_reflns_shell.d_res_high                                    1.30 
_reflns_shell.d_res_low                                     1.33 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.75 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8552 
_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                               326.7 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.360 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_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               ? 
# 
_refine.aniso_B[1][1]                            0.21 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.03 
_refine.aniso_B[2][2]                            -0.24 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.01 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               17.228 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.972 
_refine.correlation_coeff_Fo_to_Fc_free          0.968 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9EPK 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.30 
_refine.ls_d_res_low                             35.05 
_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                     163665 
_refine.ls_number_reflns_R_free                  8593 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16144 
_refine.ls_R_factor_R_free                       0.17833 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16056 
_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                    MASK 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.045 
_refine.pdbx_overall_ESU_R_Free                  0.046 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_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                 ? 
_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                             0.831 
_refine.overall_SU_ML                            0.035 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.30 
_refine_hist.d_res_low                        35.05 
_refine_hist.number_atoms_solvent             557 
_refine_hist.number_atoms_total               6187 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5544 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         86 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.012  0.012  5829  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  5428  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.840  1.850  7940  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.620  1.789  12433 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.413  5.000  734   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.593  5.000  64    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.047 10.000 881   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.094  0.200  826   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  7248  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  1482  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.584  1.597  2906  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.582  1.596  2905  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.318  2.865  3632  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.319  2.865  3633  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.892  1.924  2923  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.893  1.924  2921  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.406  3.355  4302  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.495  17.60  6462  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.429  17.47  6418  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.300 
_refine_ls_shell.d_res_low                        1.334 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             626 
_refine_ls_shell.number_reflns_R_work             12114 
_refine_ls_shell.percent_reflns_obs               99.99 
_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                  0.304 
_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   20 
_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                  0.327 
# 
_struct.entry_id                     9EPK 
_struct.title                        'DtpAa Y389F 24 fs 100 microjoules XFEL Pulse Data Collection' 
_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        9EPK 
_struct_keywords.text            'peroxidase, heme, 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 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A7U9DT46_STRLI 
_struct_ref.pdbx_db_accession          A0A7U9DT46 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DPAGADAGSAVPFHGAHQAGIATPVQDRLHFAAFDVTTEDRAAFVALLKEWTAAARRLTAGHAVGEGAYGGLPEAPPDDT
GEALGLKPSRLTLTIGFGPSLFTRFGLADLRPEALADLPKFPGDNLDRARSGGDLCVQACADDPQVAVHAIRNLARIGFG
KVVVRWSQLGFGKTSSTTPDKQTPRNLLGFKDGTRNIAGTEKDRLDRFVWAAEKDGTPWMTGGSYLVARRIRMHIETWDR
ASLQEQEDVFGRDKGEGAPVGKAKERDEPFLKAMKPDAHVRLAHPDSNGGATLLRRGYSFTDGTDGLGRLDAGLFFLAYQ
RDIRTGFVPVQRNLATDALNEYIQHVGSAVFAVPPGVRDADDWWGSTLFGKEA
;
_struct_ref.pdbx_align_begin           48 
# 
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 9EPK A 1 ? 373 ? A0A7U9DT46 48 ? 420 ? 48 420 
2 1 9EPK B 1 ? 373 ? A0A7U9DT46 48 ? 420 ? 48 420 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EPK PHE A 342 ? UNP A0A7U9DT46 TYR 389 'engineered mutation' 389 1 
2 9EPK PHE B 342 ? UNP A0A7U9DT46 TYR 389 'engineered mutation' 389 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6950  ? 
1 MORE         -63   ? 
1 'SSA (A^2)'  26930 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'equilibrium centrifugation' 
_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 ASP A 40  ? ALA A 60  ? ASP A 87  ALA A 107 1 ? 21 
HELX_P HELX_P2  AA2 PRO A 99  ? ARG A 104 ? PRO A 146 ARG A 151 5 ? 6  
HELX_P HELX_P3  AA3 LEU A 107 ? ARG A 111 ? LEU A 154 ARG A 158 5 ? 5  
HELX_P HELX_P4  AA4 ASP A 127 ? SER A 131 ? ASP A 174 SER A 178 5 ? 5  
HELX_P HELX_P5  AA5 ASP A 143 ? GLY A 158 ? ASP A 190 GLY A 205 1 ? 16 
HELX_P HELX_P6  AA6 GLU A 201 ? VAL A 209 ? GLU A 248 VAL A 256 1 ? 9  
HELX_P HELX_P7  AA7 ALA A 212 ? GLY A 216 ? ALA A 259 GLY A 263 5 ? 5  
HELX_P HELX_P8  AA8 THR A 217 ? THR A 221 ? THR A 264 THR A 268 5 ? 5  
HELX_P HELX_P9  AA9 HIS A 234 ? ARG A 240 ? HIS A 281 ARG A 287 1 ? 7  
HELX_P HELX_P10 AB1 SER A 242 ? GLY A 251 ? SER A 289 GLY A 298 1 ? 10 
HELX_P HELX_P11 AB2 PHE A 270 ? MET A 274 ? PHE A 317 MET A 321 5 ? 5  
HELX_P HELX_P12 AB3 ALA A 278 ? HIS A 284 ? ALA A 325 HIS A 331 1 ? 7  
HELX_P HELX_P13 AB4 PRO A 285 ? ASN A 288 ? PRO A 332 ASN A 335 5 ? 4  
HELX_P HELX_P14 AB5 ASP A 322 ? THR A 325 ? ASP A 369 THR A 372 5 ? 4  
HELX_P HELX_P15 AB6 GLY A 326 ? LEU A 334 ? GLY A 373 LEU A 381 1 ? 9  
HELX_P HELX_P16 AB7 ALA A 335 ? GLU A 341 ? ALA A 382 GLU A 388 5 ? 7  
HELX_P HELX_P17 AB8 ASP B 40  ? ALA B 60  ? ASP B 87  ALA B 107 1 ? 21 
HELX_P HELX_P18 AB9 PRO B 99  ? ARG B 104 ? PRO B 146 ARG B 151 5 ? 6  
HELX_P HELX_P19 AC1 LEU B 107 ? ARG B 111 ? LEU B 154 ARG B 158 5 ? 5  
HELX_P HELX_P20 AC2 ASP B 127 ? SER B 131 ? ASP B 174 SER B 178 5 ? 5  
HELX_P HELX_P21 AC3 ASP B 143 ? GLY B 158 ? ASP B 190 GLY B 205 1 ? 16 
HELX_P HELX_P22 AC4 GLU B 201 ? VAL B 209 ? GLU B 248 VAL B 256 1 ? 9  
HELX_P HELX_P23 AC5 ALA B 212 ? GLY B 216 ? ALA B 259 GLY B 263 5 ? 5  
HELX_P HELX_P24 AC6 THR B 217 ? THR B 221 ? THR B 264 THR B 268 5 ? 5  
HELX_P HELX_P25 AC7 HIS B 234 ? ASP B 239 ? HIS B 281 ASP B 286 1 ? 6  
HELX_P HELX_P26 AC8 SER B 242 ? GLY B 251 ? SER B 289 GLY B 298 1 ? 10 
HELX_P HELX_P27 AC9 PHE B 270 ? MET B 274 ? PHE B 317 MET B 321 5 ? 5  
HELX_P HELX_P28 AD1 ALA B 278 ? HIS B 284 ? ALA B 325 HIS B 331 1 ? 7  
HELX_P HELX_P29 AD2 PRO B 285 ? ASN B 288 ? PRO B 332 ASN B 335 5 ? 4  
HELX_P HELX_P30 AD3 ASP B 322 ? THR B 325 ? ASP B 369 THR B 372 5 ? 4  
HELX_P HELX_P31 AD4 GLY B 326 ? LEU B 334 ? GLY B 373 LEU B 381 1 ? 9  
HELX_P HELX_P32 AD5 ALA B 335 ? GLU B 341 ? ALA B 382 GLU B 388 5 ? 7  
HELX_P HELX_P33 AD6 GLY B 365 ? GLY B 370 ? GLY B 412 GLY B 417 1 ? 6  
# 
_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 279 NE2 ? ? ? 1_555 C HEM . FE ? ? A HIS 326 A HEM 501 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc2 metalc ? ? C HEM .   FE  ? ? ? 1_555 E HOH . O  ? ? A HEM 501 A HOH 724 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc3 metalc ? ? B HIS 279 NE2 ? ? ? 1_555 D HEM . FE ? ? B HIS 326 B HEM 501 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
metalc4 metalc ? ? D HEM .   FE  ? ? ? 1_555 F HOH . O  A ? B HEM 501 B HOH 707 1_555 ? ? ? ? ? ? ? 2.214 ? ? 
# 
_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 279 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NA ? C HEM . ? A HEM 501 ? 1_555 92.9  ? 
2  NE2 ? A HIS 279 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 91.0  ? 
3  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 89.8  ? 
4  NE2 ? A HIS 279 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 93.8  ? 
5  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 173.1 ? 
6  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 88.4  ? 
7  NE2 ? A HIS 279 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 96.7  ? 
8  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 90.7  ? 
9  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 172.3 ? 
10 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 90.1  ? 
11 NE2 ? A HIS 279 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 724 ? 1_555 170.0 ? 
12 NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 724 ? 1_555 81.0  ? 
13 NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 724 ? 1_555 81.1  ? 
14 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 724 ? 1_555 92.1  ? 
15 ND  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 724 ? 1_555 91.3  ? 
16 NE2 ? B HIS 279 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NA ? D HEM . ? B HEM 501 ? 1_555 94.8  ? 
17 NE2 ? B HIS 279 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NB ? D HEM . ? B HEM 501 ? 1_555 91.6  ? 
18 NA  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NB ? D HEM . ? B HEM 501 ? 1_555 90.1  ? 
19 NE2 ? B HIS 279 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NC ? D HEM . ? B HEM 501 ? 1_555 95.8  ? 
20 NA  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NC ? D HEM . ? B HEM 501 ? 1_555 169.3 ? 
21 NB  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NC ? D HEM . ? B HEM 501 ? 1_555 87.9  ? 
22 NE2 ? B HIS 279 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 100.0 ? 
23 NA  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 89.4  ? 
24 NB  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 168.5 ? 
25 NC  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 90.4  ? 
26 NE2 ? B HIS 279 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  A F HOH . ? B HOH 707 ? 1_555 172.4 ? 
27 NA  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  A F HOH . ? B HOH 707 ? 1_555 83.3  ? 
28 NB  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  A F HOH . ? B HOH 707 ? 1_555 81.1  ? 
29 NC  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  A F HOH . ? B HOH 707 ? 1_555 86.0  ? 
30 ND  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  A F HOH . ? B HOH 707 ? 1_555 87.4  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 4 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? 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 THR A 92  ? PHE A 97  ? THR A 139 PHE A 144 
AA1 2 LEU A 135 ? ALA A 141 ? LEU A 182 ALA A 188 
AA1 3 ARG A 28  ? VAL A 36  ? ARG A 75  VAL A 83  
AA1 4 VAL A 162 ? GLY A 170 ? VAL A 209 GLY A 217 
AA2 1 GLY A 172 ? LYS A 173 ? GLY A 219 LYS A 220 
AA2 2 TYR A 298 ? PHE A 300 ? TYR A 345 PHE A 347 
AA2 3 GLY A 313 ? GLN A 320 ? GLY A 360 GLN A 367 
AA2 4 LEU A 294 ? ARG A 295 ? LEU A 341 ARG A 342 
AA3 1 GLY A 172 ? LYS A 173 ? GLY A 219 LYS A 220 
AA3 2 TYR A 298 ? PHE A 300 ? TYR A 345 PHE A 347 
AA3 3 GLY A 313 ? GLN A 320 ? GLY A 360 GLN A 367 
AA3 4 SER A 224 ? MET A 233 ? SER A 271 MET A 280 
AA3 5 ILE A 343 ? VAL A 353 ? ILE A 390 VAL A 400 
AA4 1 THR B 92  ? PHE B 97  ? THR B 139 PHE B 144 
AA4 2 LEU B 135 ? ALA B 141 ? LEU B 182 ALA B 188 
AA4 3 ARG B 28  ? VAL B 36  ? ARG B 75  VAL B 83  
AA4 4 VAL B 162 ? PHE B 171 ? VAL B 209 PHE B 218 
AA5 1 LEU B 294 ? ARG B 295 ? LEU B 341 ARG B 342 
AA5 2 LEU B 310 ? GLN B 320 ? LEU B 357 GLN B 367 
AA5 3 TYR B 298 ? THR B 304 ? TYR B 345 THR B 351 
AA6 1 LEU B 294 ? ARG B 295 ? LEU B 341 ARG B 342 
AA6 2 LEU B 310 ? GLN B 320 ? LEU B 357 GLN B 367 
AA6 3 SER B 224 ? MET B 233 ? SER B 271 MET B 280 
AA6 4 ILE B 343 ? VAL B 353 ? ILE B 390 VAL B 400 
# 
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 THR A 94  ? N THR A 141 O GLN A 138 ? O GLN A 185 
AA1 2 3 O ALA A 139 ? O ALA A 186 N HIS A 30  ? N HIS A 77  
AA1 3 4 N ALA A 33  ? N ALA A 80  O TRP A 166 ? O TRP A 213 
AA2 1 2 N GLY A 172 ? N GLY A 219 O SER A 299 ? O SER A 346 
AA2 2 3 N TYR A 298 ? N TYR A 345 O PHE A 315 ? O PHE A 362 
AA2 3 4 O TYR A 319 ? O TYR A 366 N LEU A 294 ? N LEU A 341 
AA3 1 2 N GLY A 172 ? N GLY A 219 O SER A 299 ? O SER A 346 
AA3 2 3 N TYR A 298 ? N TYR A 345 O PHE A 315 ? O PHE A 362 
AA3 3 4 O PHE A 316 ? O PHE A 363 N ARG A 229 ? N ARG A 276 
AA3 4 5 N LEU A 226 ? N LEU A 273 O PHE A 351 ? O PHE A 398 
AA4 1 2 N THR B 94  ? N THR B 141 O GLN B 138 ? O GLN B 185 
AA4 2 3 O ALA B 139 ? O ALA B 186 N HIS B 30  ? N HIS B 77  
AA4 3 4 N PHE B 31  ? N PHE B 78  O GLN B 168 ? O GLN B 215 
AA5 1 2 N LEU B 294 ? N LEU B 341 O TYR B 319 ? O TYR B 366 
AA5 2 3 O PHE B 315 ? O PHE B 362 N TYR B 298 ? N TYR B 345 
AA6 1 2 N LEU B 294 ? N LEU B 341 O TYR B 319 ? O TYR B 366 
AA6 2 3 O ALA B 312 ? O ALA B 359 N MET B 233 ? N MET B 280 
AA6 3 4 N SER B 224 ? N SER B 271 O VAL B 353 ? O VAL B 400 
# 
_pdbx_entry_details.entry_id                   9EPK 
_pdbx_entry_details.has_ligand_of_interest     N 
_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 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 777 ? ? O B HOH 770 ? ? 1.75 
2 1 O A HOH 844 ? ? O A HOH 851 ? ? 2.05 
3 1 O A HOH 646 ? ? O A HOH 760 ? ? 2.17 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 NE A ARG 75  ? B CZ A ARG 75  ? B NH2 A ARG 75  ? B 114.13 120.30 -6.17 0.50 N 
2  1 NE A ARG 103 ? ? CZ A ARG 103 ? ? NH2 A ARG 103 ? ? 115.61 120.30 -4.69 0.50 N 
3  1 NE A ARG 104 ? A CZ A ARG 104 ? A NH2 A ARG 104 ? A 117.16 120.30 -3.14 0.50 N 
4  1 NE B ARG 88  ? ? CZ B ARG 88  ? ? NH2 B ARG 88  ? ? 117.27 120.30 -3.03 0.50 N 
5  1 NE B ARG 137 ? ? CZ B ARG 137 ? ? NH1 B ARG 137 ? ? 124.30 120.30 4.00  0.50 N 
6  1 NE B ARG 203 ? ? CZ B ARG 203 ? ? NH2 B ARG 203 ? ? 116.68 120.30 -3.62 0.50 N 
7  1 CD B ARG 251 ? ? NE B ARG 251 ? ? CZ  B ARG 251 ? ? 134.00 123.60 10.40 1.40 N 
8  1 NE B ARG 251 ? ? CZ B ARG 251 ? ? NH1 B ARG 251 ? ? 125.64 120.30 5.34  0.50 N 
9  1 NE B ARG 251 ? ? CZ B ARG 251 ? ? NH2 B ARG 251 ? ? 115.63 120.30 -4.67 0.50 N 
10 1 NE B ARG 276 ? ? CZ B ARG 276 ? ? NH1 B ARG 276 ? ? 123.94 120.30 3.64  0.50 N 
11 1 NE B ARG 276 ? ? CZ B ARG 276 ? ? NH2 B ARG 276 ? ? 116.38 120.30 -3.92 0.50 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 ILE A 68  ? ? -119.70 -71.48  
2 1 ASN A 243 ? ? -114.64 -155.66 
3 1 ARG A 343 ? ? -148.58 39.03   
4 1 VAL B 256 ? ? -123.94 -50.93  
5 1 ARG B 343 ? ? -145.59 42.49   
6 1 PRO B 402 ? ? -59.68  170.93  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 104 ? ? 0.083 'SIDE CHAIN' 
2 1 ARG A 242 ? ? 0.091 'SIDE CHAIN' 
3 1 ARG A 277 ? ? 0.166 'SIDE CHAIN' 
4 1 ARG B 242 ? ? 0.101 'SIDE CHAIN' 
5 1 ARG B 251 ? ? 0.093 'SIDE CHAIN' 
6 1 ARG B 313 ? ? 0.077 'SIDE CHAIN' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       856 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.29 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 ASP 48  ? A ASP 1   
2  1 Y 1 A PRO 49  ? A PRO 2   
3  1 Y 1 A ALA 50  ? A ALA 3   
4  1 Y 1 A GLY 51  ? A GLY 4   
5  1 Y 1 A ALA 52  ? A ALA 5   
6  1 Y 1 A ASP 53  ? A ASP 6   
7  1 Y 1 A ALA 54  ? A ALA 7   
8  1 Y 1 A GLY 417 ? A GLY 370 
9  1 Y 1 A LYS 418 ? A LYS 371 
10 1 Y 1 A GLU 419 ? A GLU 372 
11 1 Y 1 A ALA 420 ? A ALA 373 
12 1 Y 1 B ASP 48  ? B ASP 1   
13 1 Y 1 B PRO 49  ? B PRO 2   
14 1 Y 1 B ALA 50  ? B ALA 3   
15 1 Y 1 B GLY 51  ? B GLY 4   
16 1 Y 1 B ALA 52  ? B ALA 5   
17 1 Y 1 B ASP 53  ? B ASP 6   
18 1 Y 1 B ALA 54  ? B ALA 7   
19 1 Y 1 B GLY 55  ? B GLY 8   
20 1 Y 1 B LYS 418 ? B LYS 371 
21 1 Y 1 B GLU 419 ? B GLU 372 
22 1 Y 1 B ALA 420 ? B ALA 373 
# 
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 
HEM CHA  C  N N 137 
HEM CHB  C  N N 138 
HEM CHC  C  N N 139 
HEM CHD  C  N N 140 
HEM C1A  C  Y N 141 
HEM C2A  C  Y N 142 
HEM C3A  C  Y N 143 
HEM C4A  C  Y N 144 
HEM CMA  C  N N 145 
HEM CAA  C  N N 146 
HEM CBA  C  N N 147 
HEM CGA  C  N N 148 
HEM O1A  O  N N 149 
HEM O2A  O  N N 150 
HEM C1B  C  N N 151 
HEM C2B  C  N N 152 
HEM C3B  C  N N 153 
HEM C4B  C  N N 154 
HEM CMB  C  N N 155 
HEM CAB  C  N N 156 
HEM CBB  C  N N 157 
HEM C1C  C  Y N 158 
HEM C2C  C  Y N 159 
HEM C3C  C  Y N 160 
HEM C4C  C  Y N 161 
HEM CMC  C  N N 162 
HEM CAC  C  N N 163 
HEM CBC  C  N N 164 
HEM C1D  C  N N 165 
HEM C2D  C  N N 166 
HEM C3D  C  N N 167 
HEM C4D  C  N N 168 
HEM CMD  C  N N 169 
HEM CAD  C  N N 170 
HEM CBD  C  N N 171 
HEM CGD  C  N N 172 
HEM O1D  O  N N 173 
HEM O2D  O  N N 174 
HEM NA   N  Y N 175 
HEM NB   N  N N 176 
HEM NC   N  Y N 177 
HEM ND   N  N N 178 
HEM FE   FE N N 179 
HEM HHB  H  N N 180 
HEM HHC  H  N N 181 
HEM HHD  H  N N 182 
HEM HMA  H  N N 183 
HEM HMAA H  N N 184 
HEM HMAB H  N N 185 
HEM HAA  H  N N 186 
HEM HAAA H  N N 187 
HEM HBA  H  N N 188 
HEM HBAA H  N N 189 
HEM HMB  H  N N 190 
HEM HMBA H  N N 191 
HEM HMBB H  N N 192 
HEM HAB  H  N N 193 
HEM HBB  H  N N 194 
HEM HBBA H  N N 195 
HEM HMC  H  N N 196 
HEM HMCA H  N N 197 
HEM HMCB H  N N 198 
HEM HAC  H  N N 199 
HEM HBC  H  N N 200 
HEM HBCA H  N N 201 
HEM HMD  H  N N 202 
HEM HMDA H  N N 203 
HEM HMDB H  N N 204 
HEM HAD  H  N N 205 
HEM HADA H  N N 206 
HEM HBD  H  N N 207 
HEM HBDA H  N N 208 
HEM H2A  H  N N 209 
HEM H2D  H  N N 210 
HEM HHA  H  N N 211 
HIS N    N  N N 212 
HIS CA   C  N S 213 
HIS C    C  N N 214 
HIS O    O  N N 215 
HIS CB   C  N N 216 
HIS CG   C  Y N 217 
HIS ND1  N  Y N 218 
HIS CD2  C  Y N 219 
HIS CE1  C  Y N 220 
HIS NE2  N  Y N 221 
HIS OXT  O  N N 222 
HIS H    H  N N 223 
HIS H2   H  N N 224 
HIS HA   H  N N 225 
HIS HB2  H  N N 226 
HIS HB3  H  N N 227 
HIS HD1  H  N N 228 
HIS HD2  H  N N 229 
HIS HE1  H  N N 230 
HIS HE2  H  N N 231 
HIS HXT  H  N N 232 
HOH O    O  N N 233 
HOH H1   H  N N 234 
HOH H2   H  N N 235 
ILE N    N  N N 236 
ILE CA   C  N S 237 
ILE C    C  N N 238 
ILE O    O  N N 239 
ILE CB   C  N S 240 
ILE CG1  C  N N 241 
ILE CG2  C  N N 242 
ILE CD1  C  N N 243 
ILE OXT  O  N N 244 
ILE H    H  N N 245 
ILE H2   H  N N 246 
ILE HA   H  N N 247 
ILE HB   H  N N 248 
ILE HG12 H  N N 249 
ILE HG13 H  N N 250 
ILE HG21 H  N N 251 
ILE HG22 H  N N 252 
ILE HG23 H  N N 253 
ILE HD11 H  N N 254 
ILE HD12 H  N N 255 
ILE HD13 H  N N 256 
ILE HXT  H  N N 257 
LEU N    N  N N 258 
LEU CA   C  N S 259 
LEU C    C  N N 260 
LEU O    O  N N 261 
LEU CB   C  N N 262 
LEU CG   C  N N 263 
LEU CD1  C  N N 264 
LEU CD2  C  N N 265 
LEU OXT  O  N N 266 
LEU H    H  N N 267 
LEU H2   H  N N 268 
LEU HA   H  N N 269 
LEU HB2  H  N N 270 
LEU HB3  H  N N 271 
LEU HG   H  N N 272 
LEU HD11 H  N N 273 
LEU HD12 H  N N 274 
LEU HD13 H  N N 275 
LEU HD21 H  N N 276 
LEU HD22 H  N N 277 
LEU HD23 H  N N 278 
LEU HXT  H  N N 279 
LYS N    N  N N 280 
LYS CA   C  N S 281 
LYS C    C  N N 282 
LYS O    O  N N 283 
LYS CB   C  N N 284 
LYS CG   C  N N 285 
LYS CD   C  N N 286 
LYS CE   C  N N 287 
LYS NZ   N  N N 288 
LYS OXT  O  N N 289 
LYS H    H  N N 290 
LYS H2   H  N N 291 
LYS HA   H  N N 292 
LYS HB2  H  N N 293 
LYS HB3  H  N N 294 
LYS HG2  H  N N 295 
LYS HG3  H  N N 296 
LYS HD2  H  N N 297 
LYS HD3  H  N N 298 
LYS HE2  H  N N 299 
LYS HE3  H  N N 300 
LYS HZ1  H  N N 301 
LYS HZ2  H  N N 302 
LYS HZ3  H  N N 303 
LYS HXT  H  N N 304 
MET N    N  N N 305 
MET CA   C  N S 306 
MET C    C  N N 307 
MET O    O  N N 308 
MET CB   C  N N 309 
MET CG   C  N N 310 
MET SD   S  N N 311 
MET CE   C  N N 312 
MET OXT  O  N N 313 
MET H    H  N N 314 
MET H2   H  N N 315 
MET HA   H  N N 316 
MET HB2  H  N N 317 
MET HB3  H  N N 318 
MET HG2  H  N N 319 
MET HG3  H  N N 320 
MET HE1  H  N N 321 
MET HE2  H  N N 322 
MET HE3  H  N N 323 
MET HXT  H  N N 324 
PHE N    N  N N 325 
PHE CA   C  N S 326 
PHE C    C  N N 327 
PHE O    O  N N 328 
PHE CB   C  N N 329 
PHE CG   C  Y N 330 
PHE CD1  C  Y N 331 
PHE CD2  C  Y N 332 
PHE CE1  C  Y N 333 
PHE CE2  C  Y N 334 
PHE CZ   C  Y N 335 
PHE OXT  O  N N 336 
PHE H    H  N N 337 
PHE H2   H  N N 338 
PHE HA   H  N N 339 
PHE HB2  H  N N 340 
PHE HB3  H  N N 341 
PHE HD1  H  N N 342 
PHE HD2  H  N N 343 
PHE HE1  H  N N 344 
PHE HE2  H  N N 345 
PHE HZ   H  N N 346 
PHE HXT  H  N N 347 
PRO N    N  N N 348 
PRO CA   C  N S 349 
PRO C    C  N N 350 
PRO O    O  N N 351 
PRO CB   C  N N 352 
PRO CG   C  N N 353 
PRO CD   C  N N 354 
PRO OXT  O  N N 355 
PRO H    H  N N 356 
PRO HA   H  N N 357 
PRO HB2  H  N N 358 
PRO HB3  H  N N 359 
PRO HG2  H  N N 360 
PRO HG3  H  N N 361 
PRO HD2  H  N N 362 
PRO HD3  H  N N 363 
PRO HXT  H  N N 364 
SER N    N  N N 365 
SER CA   C  N S 366 
SER C    C  N N 367 
SER O    O  N N 368 
SER CB   C  N N 369 
SER OG   O  N N 370 
SER OXT  O  N N 371 
SER H    H  N N 372 
SER H2   H  N N 373 
SER HA   H  N N 374 
SER HB2  H  N N 375 
SER HB3  H  N N 376 
SER HG   H  N N 377 
SER HXT  H  N N 378 
THR N    N  N N 379 
THR CA   C  N S 380 
THR C    C  N N 381 
THR O    O  N N 382 
THR CB   C  N R 383 
THR OG1  O  N N 384 
THR CG2  C  N N 385 
THR OXT  O  N N 386 
THR H    H  N N 387 
THR H2   H  N N 388 
THR HA   H  N N 389 
THR HB   H  N N 390 
THR HG1  H  N N 391 
THR HG21 H  N N 392 
THR HG22 H  N N 393 
THR HG23 H  N N 394 
THR HXT  H  N N 395 
TRP N    N  N N 396 
TRP CA   C  N S 397 
TRP C    C  N N 398 
TRP O    O  N N 399 
TRP CB   C  N N 400 
TRP CG   C  Y N 401 
TRP CD1  C  Y N 402 
TRP CD2  C  Y N 403 
TRP NE1  N  Y N 404 
TRP CE2  C  Y N 405 
TRP CE3  C  Y N 406 
TRP CZ2  C  Y N 407 
TRP CZ3  C  Y N 408 
TRP CH2  C  Y N 409 
TRP OXT  O  N N 410 
TRP H    H  N N 411 
TRP H2   H  N N 412 
TRP HA   H  N N 413 
TRP HB2  H  N N 414 
TRP HB3  H  N N 415 
TRP HD1  H  N N 416 
TRP HE1  H  N N 417 
TRP HE3  H  N N 418 
TRP HZ2  H  N N 419 
TRP HZ3  H  N N 420 
TRP HH2  H  N N 421 
TRP HXT  H  N N 422 
TYR N    N  N N 423 
TYR CA   C  N S 424 
TYR C    C  N N 425 
TYR O    O  N N 426 
TYR CB   C  N N 427 
TYR CG   C  Y N 428 
TYR CD1  C  Y N 429 
TYR CD2  C  Y N 430 
TYR CE1  C  Y N 431 
TYR CE2  C  Y N 432 
TYR CZ   C  Y N 433 
TYR OH   O  N N 434 
TYR OXT  O  N N 435 
TYR H    H  N N 436 
TYR H2   H  N N 437 
TYR HA   H  N N 438 
TYR HB2  H  N N 439 
TYR HB3  H  N N 440 
TYR HD1  H  N N 441 
TYR HD2  H  N N 442 
TYR HE1  H  N N 443 
TYR HE2  H  N N 444 
TYR HH   H  N N 445 
TYR HXT  H  N N 446 
VAL N    N  N N 447 
VAL CA   C  N S 448 
VAL C    C  N N 449 
VAL O    O  N N 450 
VAL CB   C  N N 451 
VAL CG1  C  N N 452 
VAL CG2  C  N N 453 
VAL OXT  O  N N 454 
VAL H    H  N N 455 
VAL H2   H  N N 456 
VAL HA   H  N N 457 
VAL HB   H  N N 458 
VAL HG11 H  N N 459 
VAL HG12 H  N N 460 
VAL HG13 H  N N 461 
VAL HG21 H  N N 462 
VAL HG22 H  N N 463 
VAL HG23 H  N N 464 
VAL HXT  H  N N 465 
# 
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 
HEM CHA C1A  sing N N 129 
HEM CHA C4D  doub N N 130 
HEM CHA HHA  sing N N 131 
HEM CHB C4A  sing N N 132 
HEM CHB C1B  doub N N 133 
HEM CHB HHB  sing N N 134 
HEM CHC C4B  sing N N 135 
HEM CHC C1C  doub N N 136 
HEM CHC HHC  sing N N 137 
HEM CHD C4C  doub N N 138 
HEM CHD C1D  sing N N 139 
HEM CHD HHD  sing N N 140 
HEM C1A C2A  doub Y N 141 
HEM C1A NA   sing Y N 142 
HEM C2A C3A  sing Y N 143 
HEM C2A CAA  sing N N 144 
HEM C3A C4A  doub Y N 145 
HEM C3A CMA  sing N N 146 
HEM C4A NA   sing Y N 147 
HEM CMA HMA  sing N N 148 
HEM CMA HMAA sing N N 149 
HEM CMA HMAB sing N N 150 
HEM CAA CBA  sing N N 151 
HEM CAA HAA  sing N N 152 
HEM CAA HAAA sing N N 153 
HEM CBA CGA  sing N N 154 
HEM CBA HBA  sing N N 155 
HEM CBA HBAA sing N N 156 
HEM CGA O1A  doub N N 157 
HEM CGA O2A  sing N N 158 
HEM C1B C2B  sing N N 159 
HEM C1B NB   sing N N 160 
HEM C2B C3B  doub N N 161 
HEM C2B CMB  sing N N 162 
HEM C3B C4B  sing N N 163 
HEM C3B CAB  sing N N 164 
HEM C4B NB   doub N N 165 
HEM CMB HMB  sing N N 166 
HEM CMB HMBA sing N N 167 
HEM CMB HMBB sing N N 168 
HEM CAB CBB  doub N N 169 
HEM CAB HAB  sing N N 170 
HEM CBB HBB  sing N N 171 
HEM CBB HBBA sing N N 172 
HEM C1C C2C  sing Y N 173 
HEM C1C NC   sing Y N 174 
HEM C2C C3C  doub Y N 175 
HEM C2C CMC  sing N N 176 
HEM C3C C4C  sing Y N 177 
HEM C3C CAC  sing N N 178 
HEM C4C NC   sing Y N 179 
HEM CMC HMC  sing N N 180 
HEM CMC HMCA sing N N 181 
HEM CMC HMCB sing N N 182 
HEM CAC CBC  doub N N 183 
HEM CAC HAC  sing N N 184 
HEM CBC HBC  sing N N 185 
HEM CBC HBCA sing N N 186 
HEM C1D C2D  sing N N 187 
HEM C1D ND   doub N N 188 
HEM C2D C3D  doub N N 189 
HEM C2D CMD  sing N N 190 
HEM C3D C4D  sing N N 191 
HEM C3D CAD  sing N N 192 
HEM C4D ND   sing N N 193 
HEM CMD HMD  sing N N 194 
HEM CMD HMDA sing N N 195 
HEM CMD HMDB sing N N 196 
HEM CAD CBD  sing N N 197 
HEM CAD HAD  sing N N 198 
HEM CAD HADA sing N N 199 
HEM CBD CGD  sing N N 200 
HEM CBD HBD  sing N N 201 
HEM CBD HBDA sing N N 202 
HEM CGD O1D  doub N N 203 
HEM CGD O2D  sing N N 204 
HEM O2A H2A  sing N N 205 
HEM O2D H2D  sing N N 206 
HEM FE  NA   sing N N 207 
HEM FE  NB   sing N N 208 
HEM FE  NC   sing N N 209 
HEM FE  ND   sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
HOH O   H1   sing N N 232 
HOH O   H2   sing N N 233 
ILE N   CA   sing N N 234 
ILE N   H    sing N N 235 
ILE N   H2   sing N N 236 
ILE CA  C    sing N N 237 
ILE CA  CB   sing N N 238 
ILE CA  HA   sing N N 239 
ILE C   O    doub N N 240 
ILE C   OXT  sing N N 241 
ILE CB  CG1  sing N N 242 
ILE CB  CG2  sing N N 243 
ILE CB  HB   sing N N 244 
ILE CG1 CD1  sing N N 245 
ILE CG1 HG12 sing N N 246 
ILE CG1 HG13 sing N N 247 
ILE CG2 HG21 sing N N 248 
ILE CG2 HG22 sing N N 249 
ILE CG2 HG23 sing N N 250 
ILE CD1 HD11 sing N N 251 
ILE CD1 HD12 sing N N 252 
ILE CD1 HD13 sing N N 253 
ILE OXT HXT  sing N N 254 
LEU N   CA   sing N N 255 
LEU N   H    sing N N 256 
LEU N   H2   sing N N 257 
LEU CA  C    sing N N 258 
LEU CA  CB   sing N N 259 
LEU CA  HA   sing N N 260 
LEU C   O    doub N N 261 
LEU C   OXT  sing N N 262 
LEU CB  CG   sing N N 263 
LEU CB  HB2  sing N N 264 
LEU CB  HB3  sing N N 265 
LEU CG  CD1  sing N N 266 
LEU CG  CD2  sing N N 267 
LEU CG  HG   sing N N 268 
LEU CD1 HD11 sing N N 269 
LEU CD1 HD12 sing N N 270 
LEU CD1 HD13 sing N N 271 
LEU CD2 HD21 sing N N 272 
LEU CD2 HD22 sing N N 273 
LEU CD2 HD23 sing N N 274 
LEU OXT HXT  sing N N 275 
LYS N   CA   sing N N 276 
LYS N   H    sing N N 277 
LYS N   H2   sing N N 278 
LYS CA  C    sing N N 279 
LYS CA  CB   sing N N 280 
LYS CA  HA   sing N N 281 
LYS C   O    doub N N 282 
LYS C   OXT  sing N N 283 
LYS CB  CG   sing N N 284 
LYS CB  HB2  sing N N 285 
LYS CB  HB3  sing N N 286 
LYS CG  CD   sing N N 287 
LYS CG  HG2  sing N N 288 
LYS CG  HG3  sing N N 289 
LYS CD  CE   sing N N 290 
LYS CD  HD2  sing N N 291 
LYS CD  HD3  sing N N 292 
LYS CE  NZ   sing N N 293 
LYS CE  HE2  sing N N 294 
LYS CE  HE3  sing N N 295 
LYS NZ  HZ1  sing N N 296 
LYS NZ  HZ2  sing N N 297 
LYS NZ  HZ3  sing N N 298 
LYS OXT HXT  sing N N 299 
MET N   CA   sing N N 300 
MET N   H    sing N N 301 
MET N   H2   sing N N 302 
MET CA  C    sing N N 303 
MET CA  CB   sing N N 304 
MET CA  HA   sing N N 305 
MET C   O    doub N N 306 
MET C   OXT  sing N N 307 
MET CB  CG   sing N N 308 
MET CB  HB2  sing N N 309 
MET CB  HB3  sing N N 310 
MET CG  SD   sing N N 311 
MET CG  HG2  sing N N 312 
MET CG  HG3  sing N N 313 
MET SD  CE   sing N N 314 
MET CE  HE1  sing N N 315 
MET CE  HE2  sing N N 316 
MET CE  HE3  sing N N 317 
MET OXT HXT  sing N N 318 
PHE N   CA   sing N N 319 
PHE N   H    sing N N 320 
PHE N   H2   sing N N 321 
PHE CA  C    sing N N 322 
PHE CA  CB   sing N N 323 
PHE CA  HA   sing N N 324 
PHE C   O    doub N N 325 
PHE C   OXT  sing N N 326 
PHE CB  CG   sing N N 327 
PHE CB  HB2  sing N N 328 
PHE CB  HB3  sing N N 329 
PHE CG  CD1  doub Y N 330 
PHE CG  CD2  sing Y N 331 
PHE CD1 CE1  sing Y N 332 
PHE CD1 HD1  sing N N 333 
PHE CD2 CE2  doub Y N 334 
PHE CD2 HD2  sing N N 335 
PHE CE1 CZ   doub Y N 336 
PHE CE1 HE1  sing N N 337 
PHE CE2 CZ   sing Y N 338 
PHE CE2 HE2  sing N N 339 
PHE CZ  HZ   sing N N 340 
PHE OXT HXT  sing N N 341 
PRO N   CA   sing N N 342 
PRO N   CD   sing N N 343 
PRO N   H    sing N N 344 
PRO CA  C    sing N N 345 
PRO CA  CB   sing N N 346 
PRO CA  HA   sing N N 347 
PRO C   O    doub N N 348 
PRO C   OXT  sing N N 349 
PRO CB  CG   sing N N 350 
PRO CB  HB2  sing N N 351 
PRO CB  HB3  sing N N 352 
PRO CG  CD   sing N N 353 
PRO CG  HG2  sing N N 354 
PRO CG  HG3  sing N N 355 
PRO CD  HD2  sing N N 356 
PRO CD  HD3  sing N N 357 
PRO OXT HXT  sing N N 358 
SER N   CA   sing N N 359 
SER N   H    sing N N 360 
SER N   H2   sing N N 361 
SER CA  C    sing N N 362 
SER CA  CB   sing N N 363 
SER CA  HA   sing N N 364 
SER C   O    doub N N 365 
SER C   OXT  sing N N 366 
SER CB  OG   sing N N 367 
SER CB  HB2  sing N N 368 
SER CB  HB3  sing N N 369 
SER OG  HG   sing N N 370 
SER OXT HXT  sing N N 371 
THR N   CA   sing N N 372 
THR N   H    sing N N 373 
THR N   H2   sing N N 374 
THR CA  C    sing N N 375 
THR CA  CB   sing N N 376 
THR CA  HA   sing N N 377 
THR C   O    doub N N 378 
THR C   OXT  sing N N 379 
THR CB  OG1  sing N N 380 
THR CB  CG2  sing N N 381 
THR CB  HB   sing N N 382 
THR OG1 HG1  sing N N 383 
THR CG2 HG21 sing N N 384 
THR CG2 HG22 sing N N 385 
THR CG2 HG23 sing N N 386 
THR OXT HXT  sing N N 387 
TRP N   CA   sing N N 388 
TRP N   H    sing N N 389 
TRP N   H2   sing N N 390 
TRP CA  C    sing N N 391 
TRP CA  CB   sing N N 392 
TRP CA  HA   sing N N 393 
TRP C   O    doub N N 394 
TRP C   OXT  sing N N 395 
TRP CB  CG   sing N N 396 
TRP CB  HB2  sing N N 397 
TRP CB  HB3  sing N N 398 
TRP CG  CD1  doub Y N 399 
TRP CG  CD2  sing Y N 400 
TRP CD1 NE1  sing Y N 401 
TRP CD1 HD1  sing N N 402 
TRP CD2 CE2  doub Y N 403 
TRP CD2 CE3  sing Y N 404 
TRP NE1 CE2  sing Y N 405 
TRP NE1 HE1  sing N N 406 
TRP CE2 CZ2  sing Y N 407 
TRP CE3 CZ3  doub Y N 408 
TRP CE3 HE3  sing N N 409 
TRP CZ2 CH2  doub Y N 410 
TRP CZ2 HZ2  sing N N 411 
TRP CZ3 CH2  sing Y N 412 
TRP CZ3 HZ3  sing N N 413 
TRP CH2 HH2  sing N N 414 
TRP OXT HXT  sing N N 415 
TYR N   CA   sing N N 416 
TYR N   H    sing N N 417 
TYR N   H2   sing N N 418 
TYR CA  C    sing N N 419 
TYR CA  CB   sing N N 420 
TYR CA  HA   sing N N 421 
TYR C   O    doub N N 422 
TYR C   OXT  sing N N 423 
TYR CB  CG   sing N N 424 
TYR CB  HB2  sing N N 425 
TYR CB  HB3  sing N N 426 
TYR CG  CD1  doub Y N 427 
TYR CG  CD2  sing Y N 428 
TYR CD1 CE1  sing Y N 429 
TYR CD1 HD1  sing N N 430 
TYR CD2 CE2  doub Y N 431 
TYR CD2 HD2  sing N N 432 
TYR CE1 CZ   doub Y N 433 
TYR CE1 HE1  sing N N 434 
TYR CE2 CZ   sing Y N 435 
TYR CE2 HE2  sing N N 436 
TYR CZ  OH   sing N N 437 
TYR OH  HH   sing N N 438 
TYR OXT HXT  sing N N 439 
VAL N   CA   sing N N 440 
VAL N   H    sing N N 441 
VAL N   H2   sing N N 442 
VAL CA  C    sing N N 443 
VAL CA  CB   sing N N 444 
VAL CA  HA   sing N N 445 
VAL C   O    doub N N 446 
VAL C   OXT  sing N N 447 
VAL CB  CG1  sing N N 448 
VAL CB  CG2  sing N N 449 
VAL CB  HB   sing N N 450 
VAL CG1 HG11 sing N N 451 
VAL CG1 HG12 sing N N 452 
VAL CG1 HG13 sing N N 453 
VAL CG2 HG21 sing N N 454 
VAL CG2 HG22 sing N N 455 
VAL CG2 HG23 sing N N 456 
VAL OXT HXT  sing N N 457 
# 
_pdbx_audit_support.funding_organization   'Diamond Light Source' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           STU0436 
_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   6I43 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_measurement.diffrn_id                    1 
_pdbx_serial_crystallography_measurement.pulse_energy                 100 
_pdbx_serial_crystallography_measurement.pulse_duration               22 
_pdbx_serial_crystallography_measurement.xfel_pulse_repetition_rate   ? 
_pdbx_serial_crystallography_measurement.pulse_photon_energy          ? 
_pdbx_serial_crystallography_measurement.photons_per_pulse            ? 
_pdbx_serial_crystallography_measurement.source_size                  ? 
_pdbx_serial_crystallography_measurement.source_distance              ? 
_pdbx_serial_crystallography_measurement.focal_spot_size              ? 
_pdbx_serial_crystallography_measurement.collimation                  ? 
_pdbx_serial_crystallography_measurement.collection_time_total        ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_atom_sites.entry_id                    9EPK 
_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]   0.013751 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003839 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014663 
_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]   0.013918 
_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   . GLY A 1 8   ? 17.300  -18.368 23.356  1.00 32.32 ? 55  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 8   ? 18.237  -17.966 24.422  1.00 29.56 ? 55  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 8   ? 19.686  -18.329 24.111  1.00 25.65 ? 55  GLY A C   1 
ATOM   4    O  O   . GLY A 1 8   ? 20.566  -17.798 24.778  1.00 23.80 ? 55  GLY A O   1 
ATOM   5    N  N   . SER A 1 9   ? 19.907  -19.159 23.079  1.00 25.75 ? 56  SER A N   1 
ATOM   6    C  CA  . SER A 1 9   ? 21.194  -19.777 22.800  1.00 25.11 ? 56  SER A CA  1 
ATOM   7    C  C   . SER A 1 9   ? 22.149  -18.728 22.239  1.00 21.16 ? 56  SER A C   1 
ATOM   8    O  O   . SER A 1 9   ? 21.753  -17.613 21.878  1.00 20.28 ? 56  SER A O   1 
ATOM   9    C  CB  . SER A 1 9   ? 21.031  -20.970 21.872  1.00 27.29 ? 56  SER A CB  1 
ATOM   10   O  OG  . SER A 1 9   ? 20.483  -20.577 20.618  1.00 32.57 ? 56  SER A OG  1 
ATOM   11   N  N   . ALA A 1 10  ? 23.445  -19.035 22.265  1.00 19.65 ? 57  ALA A N   1 
ATOM   12   C  CA  . ALA A 1 10  ? 24.477  -18.232 21.654  1.00 19.40 ? 57  ALA A CA  1 
ATOM   13   C  C   . ALA A 1 10  ? 24.590  -18.593 20.172  1.00 18.58 ? 57  ALA A C   1 
ATOM   14   O  O   . ALA A 1 10  ? 24.360  -19.716 19.734  1.00 21.98 ? 57  ALA A O   1 
ATOM   15   C  CB  . ALA A 1 10  ? 25.788  -18.447 22.357  1.00 21.99 ? 57  ALA A CB  1 
ATOM   16   N  N   . VAL A 1 11  ? 24.914  -17.577 19.383  1.00 15.60 ? 58  VAL A N   1 
ATOM   17   C  CA  . VAL A 1 11  ? 25.286  -17.723 17.996  1.00 15.12 ? 58  VAL A CA  1 
ATOM   18   C  C   . VAL A 1 11  ? 26.794  -17.658 17.974  1.00 13.34 ? 58  VAL A C   1 
ATOM   19   O  O   . VAL A 1 11  ? 27.367  -16.724 18.512  1.00 14.57 ? 58  VAL A O   1 
ATOM   20   C  CB  . VAL A 1 11  ? 24.658  -16.632 17.126  1.00 16.03 ? 58  VAL A CB  1 
ATOM   21   C  CG1 . VAL A 1 11  ? 25.190  -16.680 15.708  1.00 16.12 ? 58  VAL A CG1 1 
ATOM   22   C  CG2 . VAL A 1 11  ? 23.131  -16.706 17.152  1.00 19.24 ? 58  VAL A CG2 1 
ATOM   23   N  N   . PRO A 1 12  ? 27.470  -18.657 17.386  1.00 13.64 ? 59  PRO A N   1 
ATOM   24   C  CA  . PRO A 1 12  ? 28.928  -18.614 17.343  1.00 15.51 ? 59  PRO A CA  1 
ATOM   25   C  C   . PRO A 1 12  ? 29.418  -17.312 16.745  1.00 15.37 ? 59  PRO A C   1 
ATOM   26   O  O   . PRO A 1 12  ? 28.928  -16.854 15.712  1.00 16.44 ? 59  PRO A O   1 
ATOM   27   C  CB  . PRO A 1 12  ? 29.290  -19.821 16.472  1.00 17.90 ? 59  PRO A CB  1 
ATOM   28   C  CG  . PRO A 1 12  ? 28.107  -20.740 16.572  1.00 18.97 ? 59  PRO A CG  1 
ATOM   29   C  CD  . PRO A 1 12  ? 26.882  -19.835 16.724  1.00 16.61 ? 59  PRO A CD  1 
ATOM   30   N  N   . PHE A 1 13  ? 30.462  -16.761 17.325  1.00 14.58 ? 60  PHE A N   1 
ATOM   31   C  CA  . PHE A 1 13  ? 31.017  -15.490 16.927  1.00 14.00 ? 60  PHE A CA  1 
ATOM   32   C  C   . PHE A 1 13  ? 32.074  -15.621 15.838  1.00 14.81 ? 60  PHE A C   1 
ATOM   33   O  O   . PHE A 1 13  ? 32.166  -14.779 14.961  1.00 15.02 ? 60  PHE A O   1 
ATOM   34   C  CB  . PHE A 1 13  ? 31.618  -14.817 18.157  1.00 15.42 ? 60  PHE A CB  1 
ATOM   35   C  CG  . PHE A 1 13  ? 32.309  -13.504 17.887  1.00 16.06 ? 60  PHE A CG  1 
ATOM   36   C  CD1 . PHE A 1 13  ? 31.582  -12.362 17.590  1.00 15.90 ? 60  PHE A CD1 1 
ATOM   37   C  CD2 . PHE A 1 13  ? 33.684  -13.391 17.877  1.00 17.87 ? 60  PHE A CD2 1 
ATOM   38   C  CE1 . PHE A 1 13  ? 32.214  -11.177 17.313  1.00 16.85 ? 60  PHE A CE1 1 
ATOM   39   C  CE2 . PHE A 1 13  ? 34.298  -12.183 17.610  1.00 18.41 ? 60  PHE A CE2 1 
ATOM   40   C  CZ  . PHE A 1 13  ? 33.550  -11.078 17.320  1.00 18.59 ? 60  PHE A CZ  1 
ATOM   41   N  N   . HIS A 1 14  ? 32.882  -16.667 15.903  1.00 14.12 ? 61  HIS A N   1 
ATOM   42   C  CA  . HIS A 1 14  ? 33.949  -16.865 14.954  1.00 13.99 ? 61  HIS A CA  1 
ATOM   43   C  C   . HIS A 1 14  ? 33.429  -17.537 13.693  1.00 14.94 ? 61  HIS A C   1 
ATOM   44   O  O   . HIS A 1 14  ? 32.458  -18.310 13.695  1.00 18.03 ? 61  HIS A O   1 
ATOM   45   C  CB  . HIS A 1 14  ? 35.014  -17.791 15.572  1.00 14.17 ? 61  HIS A CB  1 
ATOM   46   C  CG  . HIS A 1 14  ? 35.733  -17.145 16.699  1.00 14.62 ? 61  HIS A CG  1 
ATOM   47   N  ND1 . HIS A 1 14  ? 36.155  -17.921 17.771  1.00 17.60 ? 61  HIS A ND1 1 
ATOM   48   C  CD2 . HIS A 1 14  ? 36.156  -15.945 16.972  1.00 15.10 ? 61  HIS A CD2 1 
ATOM   49   C  CE1 . HIS A 1 14  ? 36.822  -17.124 18.612  1.00 17.34 ? 61  HIS A CE1 1 
ATOM   50   N  NE2 . HIS A 1 14  ? 36.845  -15.910 18.154  1.00 15.63 ? 61  HIS A NE2 1 
ATOM   51   N  N   . GLY A 1 15  ? 34.105  -17.275 12.595  1.00 15.87 ? 62  GLY A N   1 
ATOM   52   C  CA  . GLY A 1 15  ? 33.747  -17.892 11.341  1.00 16.81 ? 62  GLY A CA  1 
ATOM   53   C  C   . GLY A 1 15  ? 34.451  -17.210 10.187  1.00 16.21 ? 62  GLY A C   1 
ATOM   54   O  O   . GLY A 1 15  ? 35.114  -16.192 10.360  1.00 16.62 ? 62  GLY A O   1 
ATOM   55   N  N   . ALA A 1 16  ? 34.261  -17.790 9.004   1.00 17.13 ? 63  ALA A N   1 
ATOM   56   C  CA  . ALA A 1 16  ? 34.774  -17.184 7.796   1.00 17.70 ? 63  ALA A CA  1 
ATOM   57   C  C   . ALA A 1 16  ? 34.057  -15.866 7.522   1.00 16.19 ? 63  ALA A C   1 
ATOM   58   O  O   . ALA A 1 16  ? 34.632  -14.978 6.949   1.00 15.68 ? 63  ALA A O   1 
ATOM   59   C  CB  . ALA A 1 16  ? 34.589  -18.134 6.643   1.00 20.51 ? 63  ALA A CB  1 
ATOM   60   N  N   . HIS A 1 17  ? 32.788  -15.796 7.923   1.00 14.96 ? 64  HIS A N   1 
ATOM   61   C  CA  . HIS A 1 17  ? 31.956  -14.629 7.747   1.00 15.25 ? 64  HIS A CA  1 
ATOM   62   C  C   . HIS A 1 17  ? 31.550  -14.148 9.133   1.00 13.87 ? 64  HIS A C   1 
ATOM   63   O  O   . HIS A 1 17  ? 31.492  -14.925 10.086  1.00 15.44 ? 64  HIS A O   1 
ATOM   64   C  CB  . HIS A 1 17  ? 30.698  -14.961 6.960   1.00 15.41 ? 64  HIS A CB  1 
ATOM   65   C  CG  . HIS A 1 17  ? 30.979  -15.682 5.677   1.00 15.27 ? 64  HIS A CG  1 
ATOM   66   N  ND1 . HIS A 1 17  ? 31.712  -15.100 4.672   1.00 15.70 ? 64  HIS A ND1 1 
ATOM   67   C  CD2 . HIS A 1 17  ? 30.648  -16.921 5.287   1.00 18.38 ? 64  HIS A CD2 1 
ATOM   68   C  CE1 . HIS A 1 17  ? 31.805  -15.995 3.682   1.00 17.35 ? 64  HIS A CE1 1 
ATOM   69   N  NE2 . HIS A 1 17  ? 31.154  -17.075 4.036   1.00 18.82 ? 64  HIS A NE2 1 
ATOM   70   N  N   . GLN A 1 18  ? 31.264  -12.855 9.261   1.00 13.17 ? 65  GLN A N   1 
ATOM   71   C  CA  . GLN A 1 18  ? 30.649  -12.365 10.475  1.00 12.26 ? 65  GLN A CA  1 
ATOM   72   C  C   . GLN A 1 18  ? 29.243  -12.906 10.569  1.00 12.54 ? 65  GLN A C   1 
ATOM   73   O  O   . GLN A 1 18  ? 28.548  -13.047 9.584   1.00 13.64 ? 65  GLN A O   1 
ATOM   74   C  CB  . GLN A 1 18  ? 30.551  -10.842 10.444  1.00 12.62 ? 65  GLN A CB  1 
ATOM   75   C  CG  . GLN A 1 18  ? 31.910  -10.185 10.552  1.00 13.25 ? 65  GLN A CG  1 
ATOM   76   C  CD  . GLN A 1 18  ? 31.760  -8.707  10.763  1.00 13.84 ? 65  GLN A CD  1 
ATOM   77   O  OE1 . GLN A 1 18  ? 31.297  -8.285  11.815  1.00 13.51 ? 65  GLN A OE1 1 
ATOM   78   N  NE2 . GLN A 1 18  ? 32.148  -7.878  9.814   1.00 14.18 ? 65  GLN A NE2 1 
ATOM   79   N  N   . ALA A 1 19  ? 28.844  -13.238 11.787  1.00 12.42 ? 66  ALA A N   1 
ATOM   80   C  CA  . ALA A 1 19  ? 27.443  -13.518 12.081  1.00 12.76 ? 66  ALA A CA  1 
ATOM   81   C  C   . ALA A 1 19  ? 26.606  -12.253 11.979  1.00 12.56 ? 66  ALA A C   1 
ATOM   82   O  O   . ALA A 1 19  ? 27.155  -11.165 11.921  1.00 14.73 ? 66  ALA A O   1 
ATOM   83   C  CB  . ALA A 1 19  ? 27.344  -14.089 13.476  1.00 14.06 ? 66  ALA A CB  1 
ATOM   84   N  N   . GLY A 1 20  ? 25.289  -12.448 11.926  1.00 12.46 ? 67  GLY A N   1 
ATOM   85   C  CA  . GLY A 1 20  ? 24.363  -11.329 11.876  1.00 13.18 ? 67  GLY A CA  1 
ATOM   86   C  C   . GLY A 1 20  ? 23.930  -10.987 10.462  1.00 13.48 ? 67  GLY A C   1 
ATOM   87   O  O   . GLY A 1 20  ? 23.284  -9.955  10.279  1.00 13.50 ? 67  GLY A O   1 
ATOM   88   N  N   . ILE A 1 21  ? 24.258  -11.835 9.485   1.00 12.23 ? 68  ILE A N   1 
ATOM   89   C  CA  . ILE A 1 21  ? 23.939  -11.596 8.088   1.00 12.72 ? 68  ILE A CA  1 
ATOM   90   C  C   . ILE A 1 21  ? 23.056  -12.724 7.601   1.00 13.60 ? 68  ILE A C   1 
ATOM   91   O  O   . ILE A 1 21  ? 21.851  -12.570 7.464   1.00 14.69 ? 68  ILE A O   1 
ATOM   92   C  CB  . ILE A 1 21  ? 25.206  -11.383 7.260   1.00 13.90 ? 68  ILE A CB  1 
ATOM   93   C  CG1 . ILE A 1 21  ? 26.034  -10.224 7.816   1.00 16.05 ? 68  ILE A CG1 1 
ATOM   94   C  CG2 . ILE A 1 21  ? 24.837  -11.143 5.793   1.00 15.87 ? 68  ILE A CG2 1 
ATOM   95   C  CD1 . ILE A 1 21  ? 27.459  -10.160 7.268   1.00 19.54 ? 68  ILE A CD1 1 
ATOM   96   N  N   . ALA A 1 22  ? 23.622  -13.912 7.439   1.00 13.07 ? 69  ALA A N   1 
ATOM   97   C  CA  . ALA A 1 22  ? 22.902  -15.108 7.082   1.00 13.90 ? 69  ALA A CA  1 
ATOM   98   C  C   . ALA A 1 22  ? 22.185  -15.753 8.252   1.00 15.06 ? 69  ALA A C   1 
ATOM   99   O  O   . ALA A 1 22  ? 21.310  -16.583 8.038   1.00 17.68 ? 69  ALA A O   1 
ATOM   100  C  CB  . ALA A 1 22  ? 23.880  -16.104 6.489   1.00 15.88 ? 69  ALA A CB  1 
ATOM   101  N  N   . THR A 1 23  ? 22.597  -15.406 9.458   1.00 13.92 ? 70  THR A N   1 
ATOM   102  C  CA  . THR A 1 23  ? 22.045  -15.857 10.712  1.00 14.89 ? 70  THR A CA  1 
ATOM   103  C  C   . THR A 1 23  ? 20.556  -15.658 10.679  1.00 13.98 ? 70  THR A C   1 
ATOM   104  O  O   . THR A 1 23  ? 20.070  -14.625 10.204  1.00 12.66 ? 70  THR A O   1 
ATOM   105  C  CB  . THR A 1 23  ? 22.573  -14.965 11.842  1.00 15.45 ? 70  THR A CB  1 
ATOM   106  O  OG1 . THR A 1 23  ? 23.972  -14.931 11.757  1.00 17.59 ? 70  THR A OG1 1 
ATOM   107  C  CG2 . THR A 1 23  ? 22.156  -15.477 13.208  1.00 17.61 ? 70  THR A CG2 1 
ATOM   108  N  N   . PRO A 1 24  ? 19.765  -16.542 11.303  1.00 12.94 ? 71  PRO A N   1 
ATOM   109  C  CA  . PRO A 1 24  ? 18.343  -16.287 11.492  1.00 13.42 ? 71  PRO A CA  1 
ATOM   110  C  C   . PRO A 1 24  ? 18.138  -14.907 12.102  1.00 12.14 ? 71  PRO A C   1 
ATOM   111  O  O   . PRO A 1 24  ? 18.852  -14.440 12.996  1.00 13.28 ? 71  PRO A O   1 
ATOM   112  C  CB  . PRO A 1 24  ? 17.897  -17.407 12.431  1.00 14.42 ? 71  PRO A CB  1 
ATOM   113  C  CG  . PRO A 1 24  ? 18.824  -18.544 12.030  1.00 14.92 ? 71  PRO A CG  1 
ATOM   114  C  CD  . PRO A 1 24  ? 20.155  -17.892 11.762  1.00 14.29 ? 71  PRO A CD  1 
ATOM   115  N  N   . VAL A 1 25  ? 17.093  -14.222 11.633  1.00 12.10 ? 72  VAL A N   1 
ATOM   116  C  CA  . VAL A 1 25  ? 16.865  -12.846 12.019  1.00 11.51 ? 72  VAL A CA  1 
ATOM   117  C  C   . VAL A 1 25  ? 16.265  -12.760 13.414  1.00 11.30 ? 72  VAL A C   1 
ATOM   118  O  O   . VAL A 1 25  ? 15.218  -13.344 13.685  1.00 13.24 ? 72  VAL A O   1 
ATOM   119  C  CB  . VAL A 1 25  ? 15.982  -12.100 11.032  1.00 12.64 ? 72  VAL A CB  1 
ATOM   120  C  CG1 . VAL A 1 25  ? 15.796  -10.656 11.445  1.00 12.63 ? 72  VAL A CG1 1 
ATOM   121  C  CG2 . VAL A 1 25  ? 16.567  -12.170 9.650   1.00 13.05 ? 72  VAL A CG2 1 
ATOM   122  N  N   . GLN A 1 26  ? 16.961  -12.077 14.307  1.00 11.97 ? 73  GLN A N   1 
ATOM   123  C  CA  . GLN A 1 26  ? 16.547  -11.982 15.696  1.00 11.07 ? 73  GLN A CA  1 
ATOM   124  C  C   . GLN A 1 26  ? 15.486  -10.904 15.867  1.00 12.86 ? 73  GLN A C   1 
ATOM   125  O  O   . GLN A 1 26  ? 15.262  -10.048 15.010  1.00 12.93 ? 73  GLN A O   1 
ATOM   126  C  CB  . GLN A 1 26  ? 17.775  -11.679 16.560  1.00 11.81 ? 73  GLN A CB  1 
ATOM   127  C  CG  . GLN A 1 26  ? 18.940  -12.642 16.331  1.00 11.90 ? 73  GLN A CG  1 
ATOM   128  C  CD  . GLN A 1 26  ? 20.000  -12.094 15.402  1.00 12.35 ? 73  GLN A CD  1 
ATOM   129  O  OE1 . GLN A 1 26  ? 19.719  -11.528 14.348  1.00 12.14 ? 73  GLN A OE1 1 
ATOM   130  N  NE2 . GLN A 1 26  ? 21.246  -12.212 15.807  1.00 12.89 ? 73  GLN A NE2 1 
ATOM   131  N  N   . ASP A 1 27  ? 14.868  -10.863 17.039  1.00 12.96 ? 74  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 27  ? 13.691  -10.036 17.157  1.00 14.19 ? 74  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 27  ? 14.022  -8.572  17.263  1.00 13.29 ? 74  ASP A C   1 
ATOM   134  O  O   . ASP A 1 27  ? 13.144  -7.746  16.946  1.00 15.87 ? 74  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 27  ? 12.894  -10.481 18.369  1.00 16.17 ? 74  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 27  ? 12.172  -11.804 18.228  1.00 21.18 ? 74  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 27  ? 11.994  -12.267 17.114  1.00 22.50 ? 74  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 27  ? 11.868  -12.399 19.283  1.00 27.76 ? 74  ASP A OD2 1 
ATOM   139  N  N   . ARG A 1 28  ? 15.171  -8.179  17.758  1.00 12.71 ? 75  ARG A N   1 
ATOM   140  C  CA  A ARG A 1 28  ? 15.431  -6.784  18.070  0.50 12.10 ? 75  ARG A CA  1 
ATOM   141  C  CA  B ARG A 1 28  ? 15.426  -6.788  18.068  0.50 13.49 ? 75  ARG A CA  1 
ATOM   142  C  C   . ARG A 1 28  ? 16.722  -6.332  17.416  1.00 12.56 ? 75  ARG A C   1 
ATOM   143  O  O   . ARG A 1 28  ? 17.676  -7.103  17.262  1.00 13.99 ? 75  ARG A O   1 
ATOM   144  C  CB  A ARG A 1 28  ? 15.663  -6.522  19.571  0.50 12.55 ? 75  ARG A CB  1 
ATOM   145  C  CB  B ARG A 1 28  ? 15.568  -6.667  19.594  0.50 16.35 ? 75  ARG A CB  1 
ATOM   146  C  CG  A ARG A 1 28  ? 14.469  -6.849  20.443  0.50 13.57 ? 75  ARG A CG  1 
ATOM   147  C  CG  B ARG A 1 28  ? 14.663  -7.584  20.400  0.50 20.96 ? 75  ARG A CG  1 
ATOM   148  C  CD  A ARG A 1 28  ? 13.282  -5.958  20.186  0.50 14.79 ? 75  ARG A CD  1 
ATOM   149  C  CD  B ARG A 1 28  ? 13.358  -6.944  20.660  0.50 23.06 ? 75  ARG A CD  1 
ATOM   150  N  NE  A ARG A 1 28  ? 13.554  -4.571  20.549  0.50 13.81 ? 75  ARG A NE  1 
ATOM   151  N  NE  B ARG A 1 28  ? 12.328  -7.403  19.747  0.50 23.31 ? 75  ARG A NE  1 
ATOM   152  C  CZ  A ARG A 1 28  ? 12.744  -3.785  21.227  0.50 14.78 ? 75  ARG A CZ  1 
ATOM   153  C  CZ  B ARG A 1 28  ? 11.090  -7.759  20.098  0.50 19.64 ? 75  ARG A CZ  1 
ATOM   154  N  NH1 A ARG A 1 28  ? 11.603  -4.257  21.688  0.50 16.48 ? 75  ARG A NH1 1 
ATOM   155  N  NH1 B ARG A 1 28  ? 10.699  -7.675  21.392  0.50 15.83 ? 75  ARG A NH1 1 
ATOM   156  N  NH2 A ARG A 1 28  ? 13.141  -2.563  21.452  0.50 15.38 ? 75  ARG A NH2 1 
ATOM   157  N  NH2 B ARG A 1 28  ? 10.271  -7.953  19.074  0.50 12.05 ? 75  ARG A NH2 1 
ATOM   158  N  N   . LEU A 1 29  ? 16.809  -5.050  17.142  1.00 11.78 ? 76  LEU A N   1 
ATOM   159  C  CA  . LEU A 1 29  ? 17.960  -4.410  16.592  1.00 11.63 ? 76  LEU A CA  1 
ATOM   160  C  C   . LEU A 1 29  ? 18.342  -3.202  17.408  1.00 12.61 ? 76  LEU A C   1 
ATOM   161  O  O   . LEU A 1 29  ? 17.490  -2.368  17.768  1.00 13.35 ? 76  LEU A O   1 
ATOM   162  C  CB  . LEU A 1 29  ? 17.603  -3.936  15.187  1.00 12.92 ? 76  LEU A CB  1 
ATOM   163  C  CG  . LEU A 1 29  ? 18.643  -3.063  14.478  1.00 13.84 ? 76  LEU A CG  1 
ATOM   164  C  CD1 . LEU A 1 29  ? 19.872  -3.888  14.145  1.00 16.41 ? 76  LEU A CD1 1 
ATOM   165  C  CD2 . LEU A 1 29  ? 18.083  -2.344  13.269  1.00 14.74 ? 76  LEU A CD2 1 
ATOM   166  N  N   . HIS A 1 30  ? 19.638  -2.990  17.619  1.00 11.78 ? 77  HIS A N   1 
ATOM   167  C  CA  . HIS A 1 30  ? 20.186  -1.721  18.000  1.00 11.67 ? 77  HIS A CA  1 
ATOM   168  C  C   . HIS A 1 30  ? 21.360  -1.472  17.090  1.00 12.39 ? 77  HIS A C   1 
ATOM   169  O  O   . HIS A 1 30  ? 22.374  -2.172  17.142  1.00 13.72 ? 77  HIS A O   1 
ATOM   170  C  CB  . HIS A 1 30  ? 20.587  -1.747  19.465  1.00 13.85 ? 77  HIS A CB  1 
ATOM   171  C  CG  . HIS A 1 30  ? 20.913  -0.433  19.983  1.00 15.95 ? 77  HIS A CG  1 
ATOM   172  N  ND1 . HIS A 1 30  ? 20.834  -0.241  21.338  1.00 20.32 ? 77  HIS A ND1 1 
ATOM   173  C  CD2 . HIS A 1 30  ? 21.397  0.663   19.480  1.00 17.23 ? 77  HIS A CD2 1 
ATOM   174  C  CE1 . HIS A 1 30  ? 21.183  1.013   21.603  1.00 21.39 ? 77  HIS A CE1 1 
ATOM   175  N  NE2 . HIS A 1 30  ? 21.575  1.592   20.520  1.00 21.49 ? 77  HIS A NE2 1 
ATOM   176  N  N   . PHE A 1 31  ? 21.250  -0.504  16.200  1.00 12.41 ? 78  PHE A N   1 
ATOM   177  C  CA  . PHE A 1 31  ? 22.250  -0.195  15.206  1.00 12.33 ? 78  PHE A CA  1 
ATOM   178  C  C   . PHE A 1 31  ? 22.894  1.126   15.566  1.00 12.62 ? 78  PHE A C   1 
ATOM   179  O  O   . PHE A 1 31  ? 22.173  2.090   15.819  1.00 15.34 ? 78  PHE A O   1 
ATOM   180  C  CB  . PHE A 1 31  ? 21.562  -0.062  13.851  1.00 13.37 ? 78  PHE A CB  1 
ATOM   181  C  CG  . PHE A 1 31  ? 22.512  -0.032  12.692  1.00 13.09 ? 78  PHE A CG  1 
ATOM   182  C  CD1 . PHE A 1 31  ? 23.163  1.142   12.328  1.00 15.29 ? 78  PHE A CD1 1 
ATOM   183  C  CD2 . PHE A 1 31  ? 22.748  -1.163  11.939  1.00 14.15 ? 78  PHE A CD2 1 
ATOM   184  C  CE1 . PHE A 1 31  ? 24.013  1.171   11.215  1.00 15.45 ? 78  PHE A CE1 1 
ATOM   185  C  CE2 . PHE A 1 31  ? 23.603  -1.105  10.859  1.00 16.02 ? 78  PHE A CE2 1 
ATOM   186  C  CZ  . PHE A 1 31  ? 24.247  0.043   10.534  1.00 16.81 ? 78  PHE A CZ  1 
ATOM   187  N  N   . ALA A 1 32  ? 24.201  1.195   15.614  1.00 13.14 ? 79  ALA A N   1 
ATOM   188  C  CA  . ALA A 1 32  ? 24.869  2.423   15.907  1.00 13.72 ? 79  ALA A CA  1 
ATOM   189  C  C   . ALA A 1 32  ? 25.902  2.717   14.848  1.00 13.79 ? 79  ALA A C   1 
ATOM   190  O  O   . ALA A 1 32  ? 26.680  1.852   14.464  1.00 14.54 ? 79  ALA A O   1 
ATOM   191  C  CB  . ALA A 1 32  ? 25.509  2.378   17.278  1.00 14.55 ? 79  ALA A CB  1 
ATOM   192  N  N   . ALA A 1 33  ? 25.938  3.969   14.403  1.00 13.53 ? 80  ALA A N   1 
ATOM   193  C  CA  . ALA A 1 33  ? 27.008  4.456   13.561  1.00 13.66 ? 80  ALA A CA  1 
ATOM   194  C  C   . ALA A 1 33  ? 27.923  5.341   14.395  1.00 14.09 ? 80  ALA A C   1 
ATOM   195  O  O   . ALA A 1 33  ? 27.452  6.138   15.185  1.00 16.67 ? 80  ALA A O   1 
ATOM   196  C  CB  . ALA A 1 33  ? 26.401  5.218   12.380  1.00 15.93 ? 80  ALA A CB  1 
ATOM   197  N  N   . PHE A 1 34  ? 29.210  5.175   14.206  1.00 15.03 ? 81  PHE A N   1 
ATOM   198  C  CA  . PHE A 1 34  ? 30.229  5.879   14.972  1.00 15.30 ? 81  PHE A CA  1 
ATOM   199  C  C   . PHE A 1 34  ? 31.128  6.654   14.028  1.00 16.83 ? 81  PHE A C   1 
ATOM   200  O  O   . PHE A 1 34  ? 31.379  6.224   12.925  1.00 17.15 ? 81  PHE A O   1 
ATOM   201  C  CB  . PHE A 1 34  ? 31.153  4.925   15.731  1.00 16.75 ? 81  PHE A CB  1 
ATOM   202  C  CG  . PHE A 1 34  ? 30.493  4.060   16.778  1.00 16.46 ? 81  PHE A CG  1 
ATOM   203  C  CD1 . PHE A 1 34  ? 29.839  2.880   16.422  1.00 18.41 ? 81  PHE A CD1 1 
ATOM   204  C  CD2 . PHE A 1 34  ? 30.626  4.365   18.124  1.00 18.69 ? 81  PHE A CD2 1 
ATOM   205  C  CE1 . PHE A 1 34  ? 29.323  2.055   17.411  1.00 19.77 ? 81  PHE A CE1 1 
ATOM   206  C  CE2 . PHE A 1 34  ? 30.079  3.556   19.094  1.00 19.76 ? 81  PHE A CE2 1 
ATOM   207  C  CZ  . PHE A 1 34  ? 29.416  2.418   18.732  1.00 20.62 ? 81  PHE A CZ  1 
ATOM   208  N  N   . ASP A 1 35  ? 31.603  7.807   14.514  1.00 16.68 ? 82  ASP A N   1 
ATOM   209  C  CA  . ASP A 1 35  ? 32.675  8.544   13.852  1.00 17.35 ? 82  ASP A CA  1 
ATOM   210  C  C   . ASP A 1 35  ? 33.952  8.369   14.668  1.00 16.85 ? 82  ASP A C   1 
ATOM   211  O  O   . ASP A 1 35  ? 33.892  8.221   15.875  1.00 17.42 ? 82  ASP A O   1 
ATOM   212  C  CB  . ASP A 1 35  ? 32.327  10.015  13.672  1.00 17.20 ? 82  ASP A CB  1 
ATOM   213  C  CG  . ASP A 1 35  ? 31.282  10.263  12.587  1.00 18.56 ? 82  ASP A CG  1 
ATOM   214  O  OD1 . ASP A 1 35  ? 31.181  9.393   11.703  1.00 19.90 ? 82  ASP A OD1 1 
ATOM   215  O  OD2 . ASP A 1 35  ? 30.600  11.328  12.633  1.00 23.03 ? 82  ASP A OD2 1 
ATOM   216  N  N   . VAL A 1 36  ? 35.085  8.374   13.969  1.00 17.74 ? 83  VAL A N   1 
ATOM   217  C  CA  . VAL A 1 36  ? 36.376  8.175   14.611  1.00 19.23 ? 83  VAL A CA  1 
ATOM   218  C  C   . VAL A 1 36  ? 36.947  9.542   14.960  1.00 21.16 ? 83  VAL A C   1 
ATOM   219  O  O   . VAL A 1 36  ? 36.883  10.462  14.166  1.00 24.60 ? 83  VAL A O   1 
ATOM   220  C  CB  . VAL A 1 36  ? 37.315  7.372   13.698  1.00 21.77 ? 83  VAL A CB  1 
ATOM   221  C  CG1 . VAL A 1 36  ? 38.712  7.252   14.310  1.00 23.57 ? 83  VAL A CG1 1 
ATOM   222  C  CG2 . VAL A 1 36  ? 36.746  6.005   13.360  1.00 22.17 ? 83  VAL A CG2 1 
ATOM   223  N  N   . THR A 1 37  ? 37.469  9.664   16.178  1.00 20.46 ? 84  THR A N   1 
ATOM   224  C  CA  . THR A 1 37  ? 38.029  10.924  16.658  1.00 23.82 ? 84  THR A CA  1 
ATOM   225  C  C   . THR A 1 37  ? 39.522  10.835  16.958  1.00 27.22 ? 84  THR A C   1 
ATOM   226  O  O   . THR A 1 37  ? 40.066  11.806  17.470  1.00 35.17 ? 84  THR A O   1 
ATOM   227  C  CB  . THR A 1 37  ? 37.273  11.394  17.889  1.00 25.72 ? 84  THR A CB  1 
ATOM   228  O  OG1 . THR A 1 37  ? 37.372  10.431  18.931  1.00 27.17 ? 84  THR A OG1 1 
ATOM   229  C  CG2 . THR A 1 37  ? 35.830  11.722  17.551  1.00 27.16 ? 84  THR A CG2 1 
ATOM   230  N  N   . THR A 1 38  ? 40.177  9.725   16.652  1.00 23.00 ? 85  THR A N   1 
ATOM   231  C  CA  . THR A 1 38  ? 41.625  9.632   16.811  1.00 23.81 ? 85  THR A CA  1 
ATOM   232  C  C   . THR A 1 38  ? 42.265  9.612   15.431  1.00 26.59 ? 85  THR A C   1 
ATOM   233  O  O   . THR A 1 38  ? 41.663  9.112   14.477  1.00 24.89 ? 85  THR A O   1 
ATOM   234  C  CB  . THR A 1 38  ? 42.025  8.391   17.618  1.00 24.88 ? 85  THR A CB  1 
ATOM   235  O  OG1 . THR A 1 38  ? 43.451  8.411   17.691  1.00 25.14 ? 85  THR A OG1 1 
ATOM   236  C  CG2 . THR A 1 38  ? 41.644  7.059   16.996  1.00 25.91 ? 85  THR A CG2 1 
ATOM   237  N  N   . GLU A 1 39  ? 43.483  10.185  15.316  1.00 26.09 ? 86  GLU A N   1 
ATOM   238  C  CA  . GLU A 1 39  ? 44.261  10.119  14.096  1.00 27.73 ? 86  GLU A CA  1 
ATOM   239  C  C   . GLU A 1 39  ? 45.389  9.105   14.234  1.00 26.12 ? 86  GLU A C   1 
ATOM   240  O  O   . GLU A 1 39  ? 46.156  8.900   13.287  1.00 32.47 ? 86  GLU A O   1 
ATOM   241  C  CB  . GLU A 1 39  ? 44.793  11.505  13.712  1.00 29.98 ? 86  GLU A CB  1 
ATOM   242  C  CG  . GLU A 1 39  ? 43.764  12.337  12.948  1.00 35.66 ? 86  GLU A CG  1 
ATOM   243  C  CD  . GLU A 1 39  ? 44.138  13.793  12.747  1.00 45.05 ? 86  GLU A CD  1 
ATOM   244  O  OE1 . GLU A 1 39  ? 43.405  14.461  11.984  1.00 51.64 ? 86  GLU A OE1 1 
ATOM   245  O  OE2 . GLU A 1 39  ? 45.123  14.262  13.366  1.00 50.32 ? 86  GLU A OE2 1 
ATOM   246  N  N   . ASP A 1 40  ? 45.422  8.401   15.372  1.00 22.52 ? 87  ASP A N   1 
ATOM   247  C  CA  . ASP A 1 40  ? 46.491  7.464   15.641  1.00 22.58 ? 87  ASP A CA  1 
ATOM   248  C  C   . ASP A 1 40  ? 46.048  6.058   15.224  1.00 22.09 ? 87  ASP A C   1 
ATOM   249  O  O   . ASP A 1 40  ? 45.216  5.424   15.876  1.00 22.39 ? 87  ASP A O   1 
ATOM   250  C  CB  . ASP A 1 40  ? 46.918  7.617   17.086  1.00 22.84 ? 87  ASP A CB  1 
ATOM   251  C  CG  . ASP A 1 40  ? 47.975  6.653   17.604  1.00 25.07 ? 87  ASP A CG  1 
ATOM   252  O  OD1 . ASP A 1 40  ? 48.283  5.671   16.927  1.00 28.34 ? 87  ASP A OD1 1 
ATOM   253  O  OD2 . ASP A 1 40  ? 48.513  6.950   18.680  1.00 29.23 ? 87  ASP A OD2 1 
ATOM   254  N  N   . ARG A 1 41  ? 46.649  5.552   14.158  1.00 23.05 ? 88  ARG A N   1 
ATOM   255  C  CA  A ARG A 1 41  ? 46.345  4.232   13.618  0.50 24.28 ? 88  ARG A CA  1 
ATOM   256  C  CA  B ARG A 1 41  ? 46.316  4.241   13.627  0.50 23.45 ? 88  ARG A CA  1 
ATOM   257  C  C   . ARG A 1 41  ? 46.535  3.157   14.682  1.00 23.22 ? 88  ARG A C   1 
ATOM   258  O  O   . ARG A 1 41  ? 45.759  2.206   14.788  1.00 22.44 ? 88  ARG A O   1 
ATOM   259  C  CB  A ARG A 1 41  ? 47.265  3.878   12.442  0.50 26.50 ? 88  ARG A CB  1 
ATOM   260  C  CB  B ARG A 1 41  ? 47.142  4.040   12.353  0.50 24.39 ? 88  ARG A CB  1 
ATOM   261  C  CG  A ARG A 1 41  ? 46.934  2.589   11.708  0.50 28.64 ? 88  ARG A CG  1 
ATOM   262  C  CG  B ARG A 1 41  ? 46.838  2.766   11.591  0.50 24.07 ? 88  ARG A CG  1 
ATOM   263  C  CD  A ARG A 1 41  ? 48.064  2.175   10.786  0.50 31.57 ? 88  ARG A CD  1 
ATOM   264  C  CD  B ARG A 1 41  ? 47.619  2.689   10.306  0.50 25.08 ? 88  ARG A CD  1 
ATOM   265  N  NE  A ARG A 1 41  ? 47.611  1.206   9.785   0.50 34.51 ? 88  ARG A NE  1 
ATOM   266  N  NE  B ARG A 1 41  ? 47.639  1.280   9.910   0.50 26.37 ? 88  ARG A NE  1 
ATOM   267  C  CZ  A ARG A 1 41  ? 47.896  -0.082  9.817   0.50 36.45 ? 88  ARG A CZ  1 
ATOM   268  C  CZ  B ARG A 1 41  ? 47.360  0.878   8.690   0.50 26.43 ? 88  ARG A CZ  1 
ATOM   269  N  NH1 A ARG A 1 41  ? 48.396  -0.633  10.911  0.50 36.61 ? 88  ARG A NH1 1 
ATOM   270  N  NH1 B ARG A 1 41  ? 47.478  -0.393  8.391   0.50 25.80 ? 88  ARG A NH1 1 
ATOM   271  N  NH2 A ARG A 1 41  ? 47.636  -0.820  8.759   0.50 38.83 ? 88  ARG A NH2 1 
ATOM   272  N  NH2 B ARG A 1 41  ? 47.013  1.755   7.771   0.50 26.63 ? 88  ARG A NH2 1 
ATOM   273  N  N   . ALA A 1 42  ? 47.631  3.240   15.449  1.00 21.67 ? 89  ALA A N   1 
ATOM   274  C  CA  . ALA A 1 42  ? 47.906  2.210   16.441  1.00 21.61 ? 89  ALA A CA  1 
ATOM   275  C  C   . ALA A 1 42  ? 46.816  2.196   17.504  1.00 20.21 ? 89  ALA A C   1 
ATOM   276  O  O   . ALA A 1 42  ? 46.424  1.129   17.985  1.00 21.49 ? 89  ALA A O   1 
ATOM   277  C  CB  . ALA A 1 42  ? 49.255  2.402   17.108  1.00 21.57 ? 89  ALA A CB  1 
ATOM   278  N  N   . ALA A 1 43  ? 46.357  3.370   17.899  1.00 20.65 ? 90  ALA A N   1 
ATOM   279  C  CA  . ALA A 1 43  ? 45.306  3.464   18.902  1.00 21.97 ? 90  ALA A CA  1 
ATOM   280  C  C   . ALA A 1 43  ? 44.005  2.878   18.358  1.00 23.78 ? 90  ALA A C   1 
ATOM   281  O  O   . ALA A 1 43  ? 43.241  2.279   19.104  1.00 21.75 ? 90  ALA A O   1 
ATOM   282  C  CB  . ALA A 1 43  ? 45.125  4.890   19.343  1.00 24.90 ? 90  ALA A CB  1 
ATOM   283  N  N   . PHE A 1 44  ? 43.731  3.096   17.073  1.00 20.94 ? 91  PHE A N   1 
ATOM   284  C  CA  . PHE A 1 44  ? 42.526  2.551   16.463  1.00 20.89 ? 91  PHE A CA  1 
ATOM   285  C  C   . PHE A 1 44  ? 42.609  1.029   16.393  1.00 19.34 ? 91  PHE A C   1 
ATOM   286  O  O   . PHE A 1 44  ? 41.621  0.351   16.688  1.00 19.42 ? 91  PHE A O   1 
ATOM   287  C  CB  . PHE A 1 44  ? 42.270  3.218   15.118  1.00 20.82 ? 91  PHE A CB  1 
ATOM   288  C  CG  . PHE A 1 44  ? 40.905  2.832   14.578  1.00 20.77 ? 91  PHE A CG  1 
ATOM   289  C  CD1 . PHE A 1 44  ? 39.764  3.333   15.167  1.00 24.19 ? 91  PHE A CD1 1 
ATOM   290  C  CD2 . PHE A 1 44  ? 40.784  1.983   13.501  1.00 20.37 ? 91  PHE A CD2 1 
ATOM   291  C  CE1 . PHE A 1 44  ? 38.517  3.004   14.664  1.00 24.16 ? 91  PHE A CE1 1 
ATOM   292  C  CE2 . PHE A 1 44  ? 39.530  1.652   13.013  1.00 21.94 ? 91  PHE A CE2 1 
ATOM   293  C  CZ  . PHE A 1 44  ? 38.409  2.160   13.595  1.00 23.02 ? 91  PHE A CZ  1 
ATOM   294  N  N   . VAL A 1 45  ? 43.758  0.463   16.009  1.00 18.61 ? 92  VAL A N   1 
ATOM   295  C  CA  . VAL A 1 45  ? 43.944  -0.976  15.984  1.00 19.08 ? 92  VAL A CA  1 
ATOM   296  C  C   . VAL A 1 45  ? 43.724  -1.554  17.384  1.00 19.96 ? 92  VAL A C   1 
ATOM   297  O  O   . VAL A 1 45  ? 43.101  -2.604  17.554  1.00 19.77 ? 92  VAL A O   1 
ATOM   298  C  CB  . VAL A 1 45  ? 45.314  -1.346  15.389  1.00 22.51 ? 92  VAL A CB  1 
ATOM   299  C  CG1 . VAL A 1 45  ? 45.679  -2.803  15.634  1.00 22.99 ? 92  VAL A CG1 1 
ATOM   300  C  CG2 . VAL A 1 45  ? 45.319  -1.042  13.904  1.00 24.58 ? 92  VAL A CG2 1 
ATOM   301  N  N   . ALA A 1 46  ? 44.260  -0.866  18.397  1.00 19.42 ? 93  ALA A N   1 
ATOM   302  C  CA  . ALA A 1 46  ? 44.112  -1.337  19.755  1.00 19.35 ? 93  ALA A CA  1 
ATOM   303  C  C   . ALA A 1 46  ? 42.630  -1.389  20.111  1.00 18.73 ? 93  ALA A C   1 
ATOM   304  O  O   . ALA A 1 46  ? 42.226  -2.325  20.794  1.00 20.51 ? 93  ALA A O   1 
ATOM   305  C  CB  . ALA A 1 46  ? 44.932  -0.501  20.732  1.00 21.35 ? 93  ALA A CB  1 
ATOM   306  N  N   . LEU A 1 47  ? 41.847  -0.388  19.692  1.00 18.96 ? 94  LEU A N   1 
ATOM   307  C  CA  . LEU A 1 47  ? 40.420  -0.382  19.939  1.00 18.52 ? 94  LEU A CA  1 
ATOM   308  C  C   . LEU A 1 47  ? 39.744  -1.554  19.238  1.00 17.05 ? 94  LEU A C   1 
ATOM   309  O  O   . LEU A 1 47  ? 38.925  -2.238  19.851  1.00 17.70 ? 94  LEU A O   1 
ATOM   310  C  CB  . LEU A 1 47  ? 39.813  0.934   19.494  1.00 20.37 ? 94  LEU A CB  1 
ATOM   311  C  CG  . LEU A 1 47  ? 38.287  0.962   19.613  1.00 22.76 ? 94  LEU A CG  1 
ATOM   312  C  CD1 . LEU A 1 47  ? 37.908  0.919   21.064  1.00 23.56 ? 94  LEU A CD1 1 
ATOM   313  C  CD2 . LEU A 1 47  ? 37.724  2.163   18.911  1.00 25.70 ? 94  LEU A CD2 1 
ATOM   314  N  N   . LEU A 1 48  ? 40.079  -1.832  17.984  1.00 16.17 ? 95  LEU A N   1 
ATOM   315  C  CA  . LEU A 1 48  ? 39.447  -2.951  17.300  1.00 16.81 ? 95  LEU A CA  1 
ATOM   316  C  C   . LEU A 1 48  ? 39.719  -4.246  18.051  1.00 17.63 ? 95  LEU A C   1 
ATOM   317  O  O   . LEU A 1 48  ? 38.859  -5.117  18.123  1.00 16.52 ? 95  LEU A O   1 
ATOM   318  C  CB  . LEU A 1 48  ? 39.932  -3.033  15.855  1.00 18.19 ? 95  LEU A CB  1 
ATOM   319  C  CG  . LEU A 1 48  ? 39.461  -1.906  14.932  1.00 20.07 ? 95  LEU A CG  1 
ATOM   320  C  CD1 . LEU A 1 48  ? 40.150  -2.007  13.612  1.00 21.69 ? 95  LEU A CD1 1 
ATOM   321  C  CD2 . LEU A 1 48  ? 37.929  -1.902  14.825  1.00 22.11 ? 95  LEU A CD2 1 
ATOM   322  N  N   . LYS A 1 49  ? 40.924  -4.399  18.595  1.00 15.86 ? 96  LYS A N   1 
ATOM   323  C  CA  . LYS A 1 49  ? 41.230  -5.617  19.335  1.00 16.36 ? 96  LYS A CA  1 
ATOM   324  C  C   . LYS A 1 49  ? 40.436  -5.700  20.630  1.00 16.54 ? 96  LYS A C   1 
ATOM   325  O  O   . LYS A 1 49  ? 39.944  -6.773  20.990  1.00 17.78 ? 96  LYS A O   1 
ATOM   326  C  CB  . LYS A 1 49  ? 42.726  -5.728  19.612  1.00 18.70 ? 96  LYS A CB  1 
ATOM   327  C  CG  . LYS A 1 49  ? 43.509  -5.935  18.352  1.00 19.46 ? 96  LYS A CG  1 
ATOM   328  C  CD  . LYS A 1 49  ? 45.015  -5.981  18.604  1.00 22.81 ? 96  LYS A CD  1 
ATOM   329  C  CE  . LYS A 1 49  ? 45.827  -6.160  17.357  1.00 25.16 ? 96  LYS A CE  1 
ATOM   330  N  NZ  . LYS A 1 49  ? 47.253  -6.003  17.702  1.00 30.26 ? 96  LYS A NZ  1 
ATOM   331  N  N   . GLU A 1 50  ? 40.324  -4.594  21.345  1.00 15.86 ? 97  GLU A N   1 
ATOM   332  C  CA  . GLU A 1 50  ? 39.602  -4.547  22.591  1.00 17.36 ? 97  GLU A CA  1 
ATOM   333  C  C   . GLU A 1 50  ? 38.114  -4.804  22.341  1.00 16.99 ? 97  GLU A C   1 
ATOM   334  O  O   . GLU A 1 50  ? 37.437  -5.509  23.100  1.00 16.42 ? 97  GLU A O   1 
ATOM   335  C  CB  . GLU A 1 50  ? 39.792  -3.218  23.308  1.00 20.18 ? 97  GLU A CB  1 
ATOM   336  C  CG  . GLU A 1 50  ? 39.382  -3.272  24.772  1.00 27.97 ? 97  GLU A CG  1 
ATOM   337  C  CD  . GLU A 1 50  ? 39.831  -2.040  25.539  1.00 33.99 ? 97  GLU A CD  1 
ATOM   338  O  OE1 . GLU A 1 50  ? 40.589  -1.198  24.975  1.00 36.45 ? 97  GLU A OE1 1 
ATOM   339  O  OE2 . GLU A 1 50  ? 39.391  -1.950  26.703  1.00 42.19 ? 97  GLU A OE2 1 
ATOM   340  N  N   . TRP A 1 51  ? 37.592  -4.217  21.260  1.00 16.60 ? 98  TRP A N   1 
ATOM   341  C  CA  . TRP A 1 51  ? 36.204  -4.437  20.888  1.00 15.50 ? 98  TRP A CA  1 
ATOM   342  C  C   . TRP A 1 51  ? 35.942  -5.900  20.554  1.00 15.10 ? 98  TRP A C   1 
ATOM   343  O  O   . TRP A 1 51  ? 34.899  -6.445  20.898  1.00 14.32 ? 98  TRP A O   1 
ATOM   344  C  CB  . TRP A 1 51  ? 35.824  -3.552  19.698  1.00 14.24 ? 98  TRP A CB  1 
ATOM   345  C  CG  . TRP A 1 51  ? 35.259  -2.219  20.075  1.00 14.69 ? 98  TRP A CG  1 
ATOM   346  C  CD1 . TRP A 1 51  ? 35.196  -1.655  21.304  1.00 15.89 ? 98  TRP A CD1 1 
ATOM   347  C  CD2 . TRP A 1 51  ? 34.577  -1.311  19.183  1.00 16.03 ? 98  TRP A CD2 1 
ATOM   348  N  NE1 . TRP A 1 51  ? 34.567  -0.445  21.239  1.00 17.03 ? 98  TRP A NE1 1 
ATOM   349  C  CE2 . TRP A 1 51  ? 34.151  -0.226  19.957  1.00 16.73 ? 98  TRP A CE2 1 
ATOM   350  C  CE3 . TRP A 1 51  ? 34.260  -1.348  17.836  1.00 19.06 ? 98  TRP A CE3 1 
ATOM   351  C  CZ2 . TRP A 1 51  ? 33.437  0.842   19.414  1.00 19.34 ? 98  TRP A CZ2 1 
ATOM   352  C  CZ3 . TRP A 1 51  ? 33.542  -0.304  17.300  1.00 20.79 ? 98  TRP A CZ3 1 
ATOM   353  C  CH2 . TRP A 1 51  ? 33.150  0.778   18.078  1.00 19.58 ? 98  TRP A CH2 1 
ATOM   354  N  N   . THR A 1 52  ? 36.872  -6.534  19.833  1.00 14.27 ? 99  THR A N   1 
ATOM   355  C  CA  . THR A 1 52  ? 36.728  -7.934  19.485  1.00 14.62 ? 99  THR A CA  1 
ATOM   356  C  C   . THR A 1 52  ? 36.675  -8.798  20.749  1.00 14.16 ? 99  THR A C   1 
ATOM   357  O  O   . THR A 1 52  ? 35.854  -9.701  20.860  1.00 14.26 ? 99  THR A O   1 
ATOM   358  C  CB  . THR A 1 52  ? 37.834  -8.418  18.551  1.00 14.23 ? 99  THR A CB  1 
ATOM   359  O  OG1 . THR A 1 52  ? 37.857  -7.576  17.407  1.00 15.39 ? 99  THR A OG1 1 
ATOM   360  C  CG2 . THR A 1 52  ? 37.536  -9.820  18.092  1.00 15.50 ? 99  THR A CG2 1 
ATOM   361  N  N   . ALA A 1 53  ? 37.564  -8.530  21.700  1.00 14.59 ? 100 ALA A N   1 
ATOM   362  C  CA  . ALA A 1 53  ? 37.576  -9.272  22.938  1.00 15.09 ? 100 ALA A CA  1 
ATOM   363  C  C   . ALA A 1 53  ? 36.246  -9.106  23.646  1.00 14.03 ? 100 ALA A C   1 
ATOM   364  O  O   . ALA A 1 53  ? 35.691  -10.044 24.178  1.00 14.88 ? 100 ALA A O   1 
ATOM   365  C  CB  . ALA A 1 53  ? 38.728  -8.819  23.802  1.00 15.88 ? 100 ALA A CB  1 
ATOM   366  N  N   . ALA A 1 54  ? 35.736  -7.871  23.694  1.00 14.39 ? 101 ALA A N   1 
ATOM   367  C  CA  . ALA A 1 54  ? 34.462  -7.617  24.326  1.00 14.22 ? 101 ALA A CA  1 
ATOM   368  C  C   . ALA A 1 54  ? 33.328  -8.362  23.632  1.00 13.00 ? 101 ALA A C   1 
ATOM   369  O  O   . ALA A 1 54  ? 32.491  -8.940  24.280  1.00 13.64 ? 101 ALA A O   1 
ATOM   370  C  CB  . ALA A 1 54  ? 34.233  -6.147  24.351  1.00 14.68 ? 101 ALA A CB  1 
ATOM   371  N  N   . ALA A 1 55  ? 33.355  -8.358  22.309  1.00 13.37 ? 102 ALA A N   1 
ATOM   372  C  CA  . ALA A 1 55  ? 32.347  -9.039  21.527  1.00 13.27 ? 102 ALA A CA  1 
ATOM   373  C  C   . ALA A 1 55  ? 32.310  -10.534 21.817  1.00 14.36 ? 102 ALA A C   1 
ATOM   374  O  O   . ALA A 1 55  ? 31.243  -11.118 21.862  1.00 14.17 ? 102 ALA A O   1 
ATOM   375  C  CB  . ALA A 1 55  ? 32.565  -8.784  20.054  1.00 14.52 ? 102 ALA A CB  1 
ATOM   376  N  N   . ARG A 1 56  ? 33.479  -11.182 21.964  1.00 13.78 ? 103 ARG A N   1 
ATOM   377  C  CA  . ARG A 1 56  ? 33.497  -12.587 22.313  1.00 14.12 ? 103 ARG A CA  1 
ATOM   378  C  C   . ARG A 1 56  ? 32.816  -12.853 23.636  1.00 15.15 ? 103 ARG A C   1 
ATOM   379  O  O   . ARG A 1 56  ? 32.111  -13.838 23.763  1.00 17.30 ? 103 ARG A O   1 
ATOM   380  C  CB  . ARG A 1 56  ? 34.918  -13.136 22.477  1.00 15.82 ? 103 ARG A CB  1 
ATOM   381  C  CG  . ARG A 1 56  ? 35.620  -13.238 21.143  1.00 15.46 ? 103 ARG A CG  1 
ATOM   382  C  CD  . ARG A 1 56  ? 36.962  -13.920 21.383  1.00 16.92 ? 103 ARG A CD  1 
ATOM   383  N  NE  . ARG A 1 56  ? 37.644  -13.944 20.108  1.00 15.32 ? 103 ARG A NE  1 
ATOM   384  C  CZ  . ARG A 1 56  ? 38.563  -13.093 19.720  1.00 16.00 ? 103 ARG A CZ  1 
ATOM   385  N  NH1 . ARG A 1 56  ? 39.049  -12.170 20.491  1.00 17.93 ? 103 ARG A NH1 1 
ATOM   386  N  NH2 . ARG A 1 56  ? 38.988  -13.239 18.481  1.00 16.59 ? 103 ARG A NH2 1 
ATOM   387  N  N   . ARG A 1 57  ? 32.996  -11.970 24.607  1.00 13.52 ? 104 ARG A N   1 
ATOM   388  C  CA  A ARG A 1 57  ? 32.323  -12.126 25.876  0.50 14.56 ? 104 ARG A CA  1 
ATOM   389  C  CA  B ARG A 1 57  ? 32.326  -12.112 25.884  0.50 15.18 ? 104 ARG A CA  1 
ATOM   390  C  C   . ARG A 1 57  ? 30.830  -11.873 25.708  1.00 13.93 ? 104 ARG A C   1 
ATOM   391  O  O   . ARG A 1 57  ? 30.018  -12.671 26.112  1.00 14.49 ? 104 ARG A O   1 
ATOM   392  C  CB  A ARG A 1 57  ? 32.902  -11.193 26.940  0.50 14.09 ? 104 ARG A CB  1 
ATOM   393  C  CB  B ARG A 1 57  ? 32.789  -11.130 26.966  0.50 15.58 ? 104 ARG A CB  1 
ATOM   394  C  CG  A ARG A 1 57  ? 34.394  -11.405 27.174  0.50 15.41 ? 104 ARG A CG  1 
ATOM   395  C  CG  B ARG A 1 57  ? 34.252  -11.173 27.397  0.50 18.22 ? 104 ARG A CG  1 
ATOM   396  C  CD  A ARG A 1 57  ? 34.651  -12.658 27.958  0.50 14.98 ? 104 ARG A CD  1 
ATOM   397  C  CD  B ARG A 1 57  ? 34.558  -12.148 28.515  0.50 18.90 ? 104 ARG A CD  1 
ATOM   398  N  NE  A ARG A 1 57  ? 34.190  -12.524 29.341  0.50 15.68 ? 104 ARG A NE  1 
ATOM   399  N  NE  B ARG A 1 57  ? 34.555  -13.562 28.134  0.50 20.63 ? 104 ARG A NE  1 
ATOM   400  C  CZ  A ARG A 1 57  ? 34.244  -13.480 30.247  0.50 17.80 ? 104 ARG A CZ  1 
ATOM   401  C  CZ  B ARG A 1 57  ? 34.739  -14.533 29.029  0.50 20.93 ? 104 ARG A CZ  1 
ATOM   402  N  NH1 A ARG A 1 57  ? 34.546  -14.716 29.881  0.50 19.06 ? 104 ARG A NH1 1 
ATOM   403  N  NH1 B ARG A 1 57  ? 34.555  -14.252 30.318  0.50 19.88 ? 104 ARG A NH1 1 
ATOM   404  N  NH2 A ARG A 1 57  ? 33.909  -13.161 31.475  0.50 18.54 ? 104 ARG A NH2 1 
ATOM   405  N  NH2 B ARG A 1 57  ? 35.033  -15.756 28.602  0.50 23.63 ? 104 ARG A NH2 1 
ATOM   406  N  N   . LEU A 1 58  ? 30.463  -10.763 25.049  1.00 13.52 ? 105 LEU A N   1 
ATOM   407  C  CA  . LEU A 1 58  ? 29.074  -10.361 25.000  1.00 12.49 ? 105 LEU A CA  1 
ATOM   408  C  C   . LEU A 1 58  ? 28.212  -11.382 24.287  1.00 12.14 ? 105 LEU A C   1 
ATOM   409  O  O   . LEU A 1 58  ? 27.113  -11.698 24.708  1.00 12.61 ? 105 LEU A O   1 
ATOM   410  C  CB  . LEU A 1 58  ? 28.962  -9.015  24.297  1.00 13.50 ? 105 LEU A CB  1 
ATOM   411  C  CG  . LEU A 1 58  ? 29.566  -7.821  25.021  1.00 13.57 ? 105 LEU A CG  1 
ATOM   412  C  CD1 . LEU A 1 58  ? 29.785  -6.657  24.047  1.00 15.62 ? 105 LEU A CD1 1 
ATOM   413  C  CD2 . LEU A 1 58  ? 28.654  -7.427  26.122  1.00 16.16 ? 105 LEU A CD2 1 
ATOM   414  N  N   . THR A 1 59  ? 28.749  -11.936 23.213  1.00 12.08 ? 106 THR A N   1 
ATOM   415  C  CA  . THR A 1 59  ? 27.973  -12.866 22.422  1.00 12.84 ? 106 THR A CA  1 
ATOM   416  C  C   . THR A 1 59  ? 27.829  -14.229 23.083  1.00 12.98 ? 106 THR A C   1 
ATOM   417  O  O   . THR A 1 59  ? 26.933  -15.005 22.739  1.00 15.37 ? 106 THR A O   1 
ATOM   418  C  CB  . THR A 1 59  ? 28.522  -13.053 21.002  1.00 13.16 ? 106 THR A CB  1 
ATOM   419  O  OG1 . THR A 1 59  ? 29.890  -13.478 21.081  1.00 15.40 ? 106 THR A OG1 1 
ATOM   420  C  CG2 . THR A 1 59  ? 28.445  -11.794 20.172  1.00 14.32 ? 106 THR A CG2 1 
ATOM   421  N  N   . ALA A 1 60  ? 28.632  -14.501 24.119  1.00 14.18 ? 107 ALA A N   1 
ATOM   422  C  CA  . ALA A 1 60  ? 28.476  -15.722 24.886  1.00 15.57 ? 107 ALA A CA  1 
ATOM   423  C  C   . ALA A 1 60  ? 27.722  -15.467 26.179  1.00 16.96 ? 107 ALA A C   1 
ATOM   424  O  O   . ALA A 1 60  ? 27.559  -16.402 26.977  1.00 19.06 ? 107 ALA A O   1 
ATOM   425  C  CB  . ALA A 1 60  ? 29.851  -16.277 25.164  1.00 17.39 ? 107 ALA A CB  1 
ATOM   426  N  N   . GLY A 1 61  ? 27.235  -14.256 26.408  1.00 14.88 ? 108 GLY A N   1 
ATOM   427  C  CA  . GLY A 1 61  ? 26.479  -13.937 27.605  1.00 15.05 ? 108 GLY A CA  1 
ATOM   428  C  C   . GLY A 1 61  ? 27.369  -13.643 28.792  1.00 14.31 ? 108 GLY A C   1 
ATOM   429  O  O   . GLY A 1 61  ? 26.840  -13.687 29.903  1.00 20.07 ? 108 GLY A O   1 
ATOM   430  N  N   . HIS A 1 62  ? 28.640  -13.365 28.594  1.00 14.88 ? 109 HIS A N   1 
ATOM   431  C  CA  . HIS A 1 62  ? 29.510  -13.009 29.703  1.00 15.22 ? 109 HIS A CA  1 
ATOM   432  C  C   . HIS A 1 62  ? 29.733  -11.508 29.750  1.00 15.62 ? 109 HIS A C   1 
ATOM   433  O  O   . HIS A 1 62  ? 29.619  -10.801 28.735  1.00 15.38 ? 109 HIS A O   1 
ATOM   434  C  CB  . HIS A 1 62  ? 30.867  -13.682 29.531  1.00 15.77 ? 109 HIS A CB  1 
ATOM   435  C  CG  . HIS A 1 62  ? 30.768  -15.157 29.398  1.00 18.16 ? 109 HIS A CG  1 
ATOM   436  N  ND1 . HIS A 1 62  ? 29.947  -15.960 30.154  1.00 23.50 ? 109 HIS A ND1 1 
ATOM   437  C  CD2 . HIS A 1 62  ? 31.323  -15.925 28.469  1.00 19.25 ? 109 HIS A CD2 1 
ATOM   438  C  CE1 . HIS A 1 62  ? 30.078  -17.220 29.712  1.00 23.51 ? 109 HIS A CE1 1 
ATOM   439  N  NE2 . HIS A 1 62  ? 30.896  -17.208 28.681  1.00 23.24 ? 109 HIS A NE2 1 
ATOM   440  N  N   . ALA A 1 63  ? 30.042  -11.012 30.935  1.00 16.44 ? 110 ALA A N   1 
ATOM   441  C  CA  . ALA A 1 63  ? 30.345  -9.611  31.121  1.00 14.98 ? 110 ALA A CA  1 
ATOM   442  C  C   . ALA A 1 63  ? 31.693  -9.277  30.503  1.00 16.62 ? 110 ALA A C   1 
ATOM   443  O  O   . ALA A 1 63  ? 32.572  -10.129 30.416  1.00 17.96 ? 110 ALA A O   1 
ATOM   444  C  CB  . ALA A 1 63  ? 30.311  -9.282  32.607  1.00 18.41 ? 110 ALA A CB  1 
ATOM   445  N  N   . VAL A 1 64  ? 31.887  -8.034  30.105  1.00 15.72 ? 111 VAL A N   1 
ATOM   446  C  CA  . VAL A 1 64  ? 33.141  -7.598  29.524  1.00 16.92 ? 111 VAL A CA  1 
ATOM   447  C  C   . VAL A 1 64  ? 34.175  -7.423  30.625  1.00 17.49 ? 111 VAL A C   1 
ATOM   448  O  O   . VAL A 1 64  ? 33.864  -7.184  31.788  1.00 17.04 ? 111 VAL A O   1 
ATOM   449  C  CB  . VAL A 1 64  ? 33.016  -6.326  28.673  1.00 20.49 ? 111 VAL A CB  1 
ATOM   450  C  CG1 . VAL A 1 64  ? 32.010  -6.561  27.541  1.00 21.33 ? 111 VAL A CG1 1 
ATOM   451  C  CG2 . VAL A 1 64  ? 32.603  -5.145  29.492  1.00 24.42 ? 111 VAL A CG2 1 
ATOM   452  N  N   . GLY A 1 65  ? 35.443  -7.553  30.225  1.00 18.95 ? 112 GLY A N   1 
ATOM   453  C  CA  . GLY A 1 65  ? 36.561  -7.252  31.082  1.00 19.28 ? 112 GLY A CA  1 
ATOM   454  C  C   . GLY A 1 65  ? 36.517  -8.124  32.329  1.00 19.09 ? 112 GLY A C   1 
ATOM   455  O  O   . GLY A 1 65  ? 36.240  -9.330  32.267  1.00 20.56 ? 112 GLY A O   1 
ATOM   456  N  N   . GLU A 1 66  ? 36.763  -7.486  33.473  1.00 20.38 ? 113 GLU A N   1 
ATOM   457  C  CA  . GLU A 1 66  ? 36.742  -8.233  34.722  1.00 22.93 ? 113 GLU A CA  1 
ATOM   458  C  C   . GLU A 1 66  ? 35.354  -8.316  35.358  1.00 24.71 ? 113 GLU A C   1 
ATOM   459  O  O   . GLU A 1 66  ? 35.228  -8.759  36.494  1.00 28.62 ? 113 GLU A O   1 
ATOM   460  C  CB  . GLU A 1 66  ? 37.759  -7.604  35.673  1.00 29.52 ? 113 GLU A CB  1 
ATOM   461  C  CG  . GLU A 1 66  ? 39.165  -8.164  35.476  1.00 38.42 ? 113 GLU A CG  1 
ATOM   462  C  CD  . GLU A 1 66  ? 40.197  -7.285  36.154  1.00 44.90 ? 113 GLU A CD  1 
ATOM   463  O  OE1 . GLU A 1 66  ? 39.891  -6.710  37.225  1.00 53.00 ? 113 GLU A OE1 1 
ATOM   464  O  OE2 . GLU A 1 66  ? 41.299  -7.163  35.590  1.00 53.64 ? 113 GLU A OE2 1 
ATOM   465  N  N   . GLY A 1 67  ? 34.296  -7.917  34.651  1.00 20.48 ? 114 GLY A N   1 
ATOM   466  C  CA  . GLY A 1 67  ? 32.954  -8.170  35.124  1.00 19.35 ? 114 GLY A CA  1 
ATOM   467  C  C   . GLY A 1 67  ? 32.223  -6.893  35.552  1.00 17.29 ? 114 GLY A C   1 
ATOM   468  O  O   . GLY A 1 67  ? 32.747  -5.793  35.447  1.00 17.63 ? 114 GLY A O   1 
ATOM   469  N  N   . ALA A 1 68  ? 31.029  -7.128  36.090  1.00 18.26 ? 115 ALA A N   1 
ATOM   470  C  CA  . ALA A 1 68  ? 30.084  -6.084  36.451  1.00 18.46 ? 115 ALA A CA  1 
ATOM   471  C  C   . ALA A 1 68  ? 30.162  -5.712  37.941  1.00 19.66 ? 115 ALA A C   1 
ATOM   472  O  O   . ALA A 1 68  ? 29.579  -4.705  38.354  1.00 20.56 ? 115 ALA A O   1 
ATOM   473  C  CB  . ALA A 1 68  ? 28.714  -6.549  36.044  1.00 19.96 ? 115 ALA A CB  1 
ATOM   474  N  N   . TYR A 1 69  ? 30.832  -6.516  38.769  1.00 20.48 ? 116 TYR A N   1 
ATOM   475  C  CA  . TYR A 1 69  ? 30.919  -6.243  40.191  1.00 23.05 ? 116 TYR A CA  1 
ATOM   476  C  C   . TYR A 1 69  ? 32.010  -7.156  40.735  1.00 25.58 ? 116 TYR A C   1 
ATOM   477  O  O   . TYR A 1 69  ? 32.585  -7.914  39.992  1.00 26.62 ? 116 TYR A O   1 
ATOM   478  C  CB  . TYR A 1 69  ? 29.563  -6.474  40.849  1.00 24.89 ? 116 TYR A CB  1 
ATOM   479  C  CG  . TYR A 1 69  ? 29.088  -7.917  40.790  1.00 25.45 ? 116 TYR A CG  1 
ATOM   480  C  CD1 . TYR A 1 69  ? 28.368  -8.415  39.708  1.00 27.22 ? 116 TYR A CD1 1 
ATOM   481  C  CD2 . TYR A 1 69  ? 29.364  -8.794  41.838  1.00 25.82 ? 116 TYR A CD2 1 
ATOM   482  C  CE1 . TYR A 1 69  ? 27.939  -9.733  39.683  1.00 30.63 ? 116 TYR A CE1 1 
ATOM   483  C  CE2 . TYR A 1 69  ? 28.941  -10.111 41.823  1.00 29.49 ? 116 TYR A CE2 1 
ATOM   484  C  CZ  . TYR A 1 69  ? 28.228  -10.581 40.739  1.00 31.45 ? 116 TYR A CZ  1 
ATOM   485  O  OH  . TYR A 1 69  ? 27.801  -11.880 40.708  1.00 40.27 ? 116 TYR A OH  1 
ATOM   486  N  N   . GLY A 1 70  ? 32.325  -7.008  42.016  1.00 30.99 ? 117 GLY A N   1 
ATOM   487  C  CA  . GLY A 1 70  ? 33.367  -7.811  42.651  1.00 32.57 ? 117 GLY A CA  1 
ATOM   488  C  C   . GLY A 1 70  ? 34.788  -7.298  42.405  1.00 35.89 ? 117 GLY A C   1 
ATOM   489  O  O   . GLY A 1 70  ? 35.759  -7.970  42.775  1.00 38.46 ? 117 GLY A O   1 
ATOM   490  N  N   . GLY A 1 71  ? 34.928  -6.125  41.778  1.00 30.95 ? 118 GLY A N   1 
ATOM   491  C  CA  . GLY A 1 71  ? 36.223  -5.496  41.584  1.00 31.59 ? 118 GLY A CA  1 
ATOM   492  C  C   . GLY A 1 71  ? 36.534  -4.519  42.714  1.00 29.71 ? 118 GLY A C   1 
ATOM   493  O  O   . GLY A 1 71  ? 35.843  -4.511  43.731  1.00 30.37 ? 118 GLY A O   1 
ATOM   494  N  N   . LEU A 1 72  ? 37.568  -3.707  42.486  1.00 29.05 ? 119 LEU A N   1 
ATOM   495  C  CA  . LEU A 1 72  ? 37.962  -2.645  43.391  1.00 31.23 ? 119 LEU A CA  1 
ATOM   496  C  C   . LEU A 1 72  ? 36.757  -1.744  43.610  1.00 28.78 ? 119 LEU A C   1 
ATOM   497  O  O   . LEU A 1 72  ? 36.213  -1.207  42.643  1.00 26.40 ? 119 LEU A O   1 
ATOM   498  C  CB  . LEU A 1 72  ? 39.129  -1.840  42.818  1.00 35.26 ? 119 LEU A CB  1 
ATOM   499  C  CG  . LEU A 1 72  ? 40.450  -2.590  42.626  1.00 43.13 ? 119 LEU A CG  1 
ATOM   500  C  CD1 . LEU A 1 72  ? 41.498  -1.658  42.018  1.00 44.39 ? 119 LEU A CD1 1 
ATOM   501  C  CD2 . LEU A 1 72  ? 40.925  -3.184  43.937  1.00 44.50 ? 119 LEU A CD2 1 
ATOM   502  N  N   . PRO A 1 73  ? 36.305  -1.528  44.862  1.00 25.83 ? 120 PRO A N   1 
ATOM   503  C  CA  . PRO A 1 73  ? 35.220  -0.571  45.113  1.00 25.89 ? 120 PRO A CA  1 
ATOM   504  C  C   . PRO A 1 73  ? 35.417  0.810   44.489  1.00 27.30 ? 120 PRO A C   1 
ATOM   505  O  O   . PRO A 1 73  ? 34.463  1.469   44.079  1.00 21.73 ? 120 PRO A O   1 
ATOM   506  C  CB  . PRO A 1 73  ? 35.098  -0.487  46.657  1.00 26.93 ? 120 PRO A CB  1 
ATOM   507  C  CG  . PRO A 1 73  ? 36.132  -1.453  47.221  1.00 28.16 ? 120 PRO A CG  1 
ATOM   508  C  CD  . PRO A 1 73  ? 36.758  -2.220  46.090  1.00 27.20 ? 120 PRO A CD  1 
ATOM   509  N  N   . GLU A 1 74  ? 36.663  1.290   44.408  1.00 22.89 ? 121 GLU A N   1 
ATOM   510  C  CA  . GLU A 1 74  ? 36.930  2.656   44.016  1.00 23.60 ? 121 GLU A CA  1 
ATOM   511  C  C   . GLU A 1 74  ? 37.034  2.789   42.502  1.00 22.36 ? 121 GLU A C   1 
ATOM   512  O  O   . GLU A 1 74  ? 37.260  3.889   42.030  1.00 25.27 ? 121 GLU A O   1 
ATOM   513  C  CB  . GLU A 1 74  ? 38.176  3.219   44.715  1.00 28.59 ? 121 GLU A CB  1 
ATOM   514  C  CG  . GLU A 1 74  ? 39.483  2.507   44.379  1.00 36.00 ? 121 GLU A CG  1 
ATOM   515  C  CD  . GLU A 1 74  ? 39.861  1.320   45.248  1.00 42.41 ? 121 GLU A CD  1 
ATOM   516  O  OE1 . GLU A 1 74  ? 38.999  0.696   45.925  1.00 40.03 ? 121 GLU A OE1 1 
ATOM   517  O  OE2 . GLU A 1 74  ? 41.087  1.037   45.244  1.00 51.68 ? 121 GLU A OE2 1 
ATOM   518  N  N   . ALA A 1 75  ? 36.866  1.686   41.758  1.00 23.22 ? 122 ALA A N   1 
ATOM   519  C  CA  . ALA A 1 75  ? 36.916  1.763   40.305  1.00 22.64 ? 122 ALA A CA  1 
ATOM   520  C  C   . ALA A 1 75  ? 35.536  1.551   39.697  1.00 20.68 ? 122 ALA A C   1 
ATOM   521  O  O   . ALA A 1 75  ? 34.702  0.849   40.247  1.00 20.47 ? 122 ALA A O   1 
ATOM   522  C  CB  . ALA A 1 75  ? 37.866  0.747   39.727  1.00 26.26 ? 122 ALA A CB  1 
ATOM   523  N  N   . PRO A 1 76  ? 35.261  2.199   38.548  1.00 20.53 ? 123 PRO A N   1 
ATOM   524  C  CA  . PRO A 1 76  ? 34.036  1.913   37.813  1.00 19.69 ? 123 PRO A CA  1 
ATOM   525  C  C   . PRO A 1 76  ? 34.101  0.464   37.381  1.00 20.00 ? 123 PRO A C   1 
ATOM   526  O  O   . PRO A 1 76  ? 35.164  -0.017  37.017  1.00 20.85 ? 123 PRO A O   1 
ATOM   527  C  CB  . PRO A 1 76  ? 34.081  2.838   36.599  1.00 22.86 ? 123 PRO A CB  1 
ATOM   528  C  CG  . PRO A 1 76  ? 35.178  3.855   36.874  1.00 26.08 ? 123 PRO A CG  1 
ATOM   529  C  CD  . PRO A 1 76  ? 36.087  3.218   37.902  1.00 22.10 ? 123 PRO A CD  1 
ATOM   530  N  N   . PRO A 1 77  ? 32.982  -0.264  37.395  1.00 17.23 ? 124 PRO A N   1 
ATOM   531  C  CA  . PRO A 1 77  ? 32.959  -1.637  36.907  1.00 18.19 ? 124 PRO A CA  1 
ATOM   532  C  C   . PRO A 1 77  ? 33.323  -1.672  35.424  1.00 18.21 ? 124 PRO A C   1 
ATOM   533  O  O   . PRO A 1 77  ? 32.996  -0.774  34.653  1.00 17.61 ? 124 PRO A O   1 
ATOM   534  C  CB  . PRO A 1 77  ? 31.543  -2.121  37.155  1.00 20.53 ? 124 PRO A CB  1 
ATOM   535  C  CG  . PRO A 1 77  ? 30.729  -0.876  37.405  1.00 24.57 ? 124 PRO A CG  1 
ATOM   536  C  CD  . PRO A 1 77  ? 31.675  0.204   37.881  1.00 21.09 ? 124 PRO A CD  1 
ATOM   537  N  N   . ASP A 1 78  ? 33.947  -2.756  34.983  1.00 18.61 ? 125 ASP A N   1 
ATOM   538  C  CA  . ASP A 1 78  ? 34.315  -2.893  33.590  1.00 18.61 ? 125 ASP A CA  1 
ATOM   539  C  C   . ASP A 1 78  ? 33.088  -3.124  32.713  1.00 16.42 ? 125 ASP A C   1 
ATOM   540  O  O   . ASP A 1 78  ? 33.111  -2.729  31.549  1.00 17.80 ? 125 ASP A O   1 
ATOM   541  C  CB  . ASP A 1 78  ? 35.262  -4.065  33.386  1.00 20.31 ? 125 ASP A CB  1 
ATOM   542  C  CG  . ASP A 1 78  ? 36.731  -3.798  33.648  1.00 25.79 ? 125 ASP A CG  1 
ATOM   543  O  OD1 . ASP A 1 78  ? 37.067  -2.649  33.924  1.00 25.37 ? 125 ASP A OD1 1 
ATOM   544  O  OD2 . ASP A 1 78  ? 37.502  -4.760  33.530  1.00 27.09 ? 125 ASP A OD2 1 
ATOM   545  N  N   . ASP A 1 79  ? 32.054  -3.759  33.251  1.00 15.24 ? 126 ASP A N   1 
ATOM   546  C  CA  . ASP A 1 79  ? 30.831  -4.019  32.530  1.00 14.01 ? 126 ASP A CA  1 
ATOM   547  C  C   . ASP A 1 79  ? 29.733  -3.238  33.249  1.00 15.21 ? 126 ASP A C   1 
ATOM   548  O  O   . ASP A 1 79  ? 29.717  -3.247  34.463  1.00 15.03 ? 126 ASP A O   1 
ATOM   549  C  CB  . ASP A 1 79  ? 30.505  -5.509  32.497  1.00 14.50 ? 126 ASP A CB  1 
ATOM   550  C  CG  . ASP A 1 79  ? 29.323  -5.859  31.621  1.00 14.78 ? 126 ASP A CG  1 
ATOM   551  O  OD1 . ASP A 1 79  ? 28.201  -5.468  31.942  1.00 15.22 ? 126 ASP A OD1 1 
ATOM   552  O  OD2 . ASP A 1 79  ? 29.532  -6.438  30.552  1.00 16.14 ? 126 ASP A OD2 1 
ATOM   553  N  N   . THR A 1 80  ? 28.811  -2.610  32.525  1.00 14.41 ? 127 THR A N   1 
ATOM   554  C  CA  . THR A 1 80  ? 27.801  -1.737  33.116  1.00 14.23 ? 127 THR A CA  1 
ATOM   555  C  C   . THR A 1 80  ? 26.704  -2.495  33.829  1.00 14.62 ? 127 THR A C   1 
ATOM   556  O  O   . THR A 1 80  ? 25.930  -1.878  34.581  1.00 15.41 ? 127 THR A O   1 
ATOM   557  C  CB  . THR A 1 80  ? 27.222  -0.771  32.080  1.00 13.94 ? 127 THR A CB  1 
ATOM   558  O  OG1 . THR A 1 80  ? 26.653  -1.512  31.000  1.00 14.53 ? 127 THR A OG1 1 
ATOM   559  C  CG2 . THR A 1 80  ? 28.317  0.105   31.520  1.00 15.46 ? 127 THR A CG2 1 
ATOM   560  N  N   . GLY A 1 81  ? 26.598  -3.818  33.647  1.00 13.72 ? 128 GLY A N   1 
ATOM   561  C  CA  . GLY A 1 81  ? 25.862  -4.661  34.561  1.00 15.27 ? 128 GLY A CA  1 
ATOM   562  C  C   . GLY A 1 81  ? 24.411  -4.958  34.214  1.00 13.75 ? 128 GLY A C   1 
ATOM   563  O  O   . GLY A 1 81  ? 23.797  -5.820  34.833  1.00 15.92 ? 128 GLY A O   1 
ATOM   564  N  N   . GLU A 1 82  ? 23.823  -4.269  33.225  1.00 14.68 ? 129 GLU A N   1 
ATOM   565  C  CA  . GLU A 1 82  ? 22.393  -4.416  33.001  1.00 13.16 ? 129 GLU A CA  1 
ATOM   566  C  C   . GLU A 1 82  ? 22.014  -5.701  32.263  1.00 14.90 ? 129 GLU A C   1 
ATOM   567  O  O   . GLU A 1 82  ? 20.825  -5.992  32.136  1.00 17.13 ? 129 GLU A O   1 
ATOM   568  C  CB  . GLU A 1 82  ? 21.784  -3.165  32.380  1.00 15.35 ? 129 GLU A CB  1 
ATOM   569  C  CG  . GLU A 1 82  ? 22.070  -2.985  30.902  1.00 14.52 ? 129 GLU A CG  1 
ATOM   570  C  CD  . GLU A 1 82  ? 23.378  -2.307  30.560  1.00 14.07 ? 129 GLU A CD  1 
ATOM   571  O  OE1 . GLU A 1 82  ? 24.221  -2.243  31.449  1.00 14.85 ? 129 GLU A OE1 1 
ATOM   572  O  OE2 . GLU A 1 82  ? 23.450  -1.767  29.457  1.00 14.87 ? 129 GLU A OE2 1 
ATOM   573  N  N   . ALA A 1 83  ? 23.003  -6.487  31.819  1.00 13.88 ? 130 ALA A N   1 
ATOM   574  C  CA  . ALA A 1 83  ? 22.709  -7.792  31.222  1.00 14.18 ? 130 ALA A CA  1 
ATOM   575  C  C   . ALA A 1 83  ? 23.028  -8.941  32.172  1.00 15.42 ? 130 ALA A C   1 
ATOM   576  O  O   . ALA A 1 83  ? 22.989  -10.108 31.767  1.00 16.26 ? 130 ALA A O   1 
ATOM   577  C  CB  . ALA A 1 83  ? 23.419  -7.945  29.889  1.00 14.48 ? 130 ALA A CB  1 
ATOM   578  N  N   . LEU A 1 84  ? 23.348  -8.644  33.417  1.00 14.95 ? 131 LEU A N   1 
ATOM   579  C  CA  . LEU A 1 84  ? 23.649  -9.744  34.317  1.00 17.17 ? 131 LEU A CA  1 
ATOM   580  C  C   . LEU A 1 84  ? 22.434  -10.631 34.462  1.00 17.08 ? 131 LEU A C   1 
ATOM   581  O  O   . LEU A 1 84  ? 21.296  -10.174 34.547  1.00 19.74 ? 131 LEU A O   1 
ATOM   582  C  CB  . LEU A 1 84  ? 24.033  -9.184  35.674  1.00 17.79 ? 131 LEU A CB  1 
ATOM   583  C  CG  . LEU A 1 84  ? 25.420  -8.601  35.795  1.00 21.57 ? 131 LEU A CG  1 
ATOM   584  C  CD1 . LEU A 1 84  ? 25.440  -7.951  37.150  1.00 22.26 ? 131 LEU A CD1 1 
ATOM   585  C  CD2 . LEU A 1 84  ? 26.454  -9.723  35.635  1.00 23.20 ? 131 LEU A CD2 1 
ATOM   586  N  N   . GLY A 1 85  ? 22.685  -11.944 34.409  1.00 19.71 ? 132 GLY A N   1 
ATOM   587  C  CA  . GLY A 1 85  ? 21.603  -12.881 34.618  1.00 20.80 ? 132 GLY A CA  1 
ATOM   588  C  C   . GLY A 1 85  ? 20.804  -13.148 33.354  1.00 21.35 ? 132 GLY A C   1 
ATOM   589  O  O   . GLY A 1 85  ? 19.813  -13.874 33.396  1.00 24.20 ? 132 GLY A O   1 
ATOM   590  N  N   . LEU A 1 86  ? 21.230  -12.578 32.220  1.00 18.46 ? 133 LEU A N   1 
ATOM   591  C  CA  . LEU A 1 86  ? 20.499  -12.801 30.981  1.00 18.29 ? 133 LEU A CA  1 
ATOM   592  C  C   . LEU A 1 86  ? 21.252  -13.791 30.114  1.00 17.47 ? 133 LEU A C   1 
ATOM   593  O  O   . LEU A 1 86  ? 22.466  -13.804 30.083  1.00 21.08 ? 133 LEU A O   1 
ATOM   594  C  CB  . LEU A 1 86  ? 20.248  -11.501 30.220  1.00 16.75 ? 133 LEU A CB  1 
ATOM   595  C  CG  . LEU A 1 86  ? 19.535  -10.404 31.017  1.00 18.33 ? 133 LEU A CG  1 
ATOM   596  C  CD1 . LEU A 1 86  ? 19.281  -9.245  30.095  1.00 17.80 ? 133 LEU A CD1 1 
ATOM   597  C  CD2 . LEU A 1 86  ? 18.242  -10.900 31.620  1.00 19.89 ? 133 LEU A CD2 1 
ATOM   598  N  N   . LYS A 1 87  ? 20.508  -14.508 29.303  1.00 17.98 ? 134 LYS A N   1 
ATOM   599  C  CA  . LYS A 1 87  ? 21.104  -15.392 28.339  1.00 16.92 ? 134 LYS A CA  1 
ATOM   600  C  C   . LYS A 1 87  ? 21.656  -14.624 27.147  1.00 16.97 ? 134 LYS A C   1 
ATOM   601  O  O   . LYS A 1 87  ? 21.301  -13.477 26.898  1.00 16.57 ? 134 LYS A O   1 
ATOM   602  C  CB  . LYS A 1 87  ? 20.025  -16.365 27.878  1.00 18.97 ? 134 LYS A CB  1 
ATOM   603  C  CG  . LYS A 1 87  ? 19.562  -17.276 28.989  1.00 24.14 ? 134 LYS A CG  1 
ATOM   604  C  CD  . LYS A 1 87  ? 20.544  -18.377 29.348  1.00 33.56 ? 134 LYS A CD  1 
ATOM   605  C  CE  . LYS A 1 87  ? 20.216  -19.671 28.679  1.00 41.65 ? 134 LYS A CE  1 
ATOM   606  N  NZ  . LYS A 1 87  ? 21.007  -20.736 29.302  1.00 45.18 ? 134 LYS A NZ  1 
ATOM   607  N  N   . PRO A 1 88  ? 22.531  -15.269 26.346  1.00 15.46 ? 135 PRO A N   1 
ATOM   608  C  CA  . PRO A 1 88  ? 23.055  -14.638 25.135  1.00 15.96 ? 135 PRO A CA  1 
ATOM   609  C  C   . PRO A 1 88  ? 21.983  -14.108 24.200  1.00 14.35 ? 135 PRO A C   1 
ATOM   610  O  O   . PRO A 1 88  ? 22.199  -13.102 23.501  1.00 15.41 ? 135 PRO A O   1 
ATOM   611  C  CB  . PRO A 1 88  ? 23.890  -15.765 24.511  1.00 17.96 ? 135 PRO A CB  1 
ATOM   612  C  CG  . PRO A 1 88  ? 24.217  -16.737 25.615  1.00 18.91 ? 135 PRO A CG  1 
ATOM   613  C  CD  . PRO A 1 88  ? 23.054  -16.641 26.557  1.00 17.30 ? 135 PRO A CD  1 
ATOM   614  N  N   . SER A 1 89  ? 20.850  -14.766 24.123  1.00 13.54 ? 136 SER A N   1 
ATOM   615  C  CA  . SER A 1 89  ? 19.697  -14.265 23.415  1.00 13.55 ? 136 SER A CA  1 
ATOM   616  C  C   . SER A 1 89  ? 19.993  -14.064 21.935  1.00 14.23 ? 136 SER A C   1 
ATOM   617  O  O   . SER A 1 89  ? 19.495  -13.118 21.299  1.00 14.72 ? 136 SER A O   1 
ATOM   618  C  CB  . SER A 1 89  ? 19.202  -13.004 24.040  1.00 16.19 ? 136 SER A CB  1 
ATOM   619  O  OG  . SER A 1 89  ? 18.995  -13.215 25.437  1.00 19.13 ? 136 SER A OG  1 
ATOM   620  N  N   . ARG A 1 90  ? 20.780  -14.959 21.366  1.00 12.65 ? 137 ARG A N   1 
ATOM   621  C  CA  . ARG A 1 90  ? 21.188  -14.964 19.975  1.00 12.99 ? 137 ARG A CA  1 
ATOM   622  C  C   . ARG A 1 90  ? 21.854  -13.653 19.588  1.00 12.28 ? 137 ARG A C   1 
ATOM   623  O  O   . ARG A 1 90  ? 21.759  -13.264 18.431  1.00 13.65 ? 137 ARG A O   1 
ATOM   624  C  CB  . ARG A 1 90  ? 20.032  -15.319 19.055  1.00 13.28 ? 137 ARG A CB  1 
ATOM   625  C  CG  . ARG A 1 90  ? 19.462  -16.684 19.344  1.00 14.71 ? 137 ARG A CG  1 
ATOM   626  C  CD  . ARG A 1 90  ? 18.570  -17.191 18.234  1.00 17.87 ? 137 ARG A CD  1 
ATOM   627  N  NE  . ARG A 1 90  ? 17.433  -16.302 17.978  1.00 17.19 ? 137 ARG A NE  1 
ATOM   628  C  CZ  . ARG A 1 90  ? 16.657  -16.310 16.912  1.00 19.03 ? 137 ARG A CZ  1 
ATOM   629  N  NH1 . ARG A 1 90  ? 15.663  -15.442 16.806  1.00 18.63 ? 137 ARG A NH1 1 
ATOM   630  N  NH2 . ARG A 1 90  ? 16.872  -17.186 15.942  1.00 20.39 ? 137 ARG A NH2 1 
ATOM   631  N  N   . LEU A 1 91  ? 22.534  -12.975 20.480  1.00 11.11 ? 138 LEU A N   1 
ATOM   632  C  CA  . LEU A 1 91  ? 23.202  -11.722 20.161  1.00 11.46 ? 138 LEU A CA  1 
ATOM   633  C  C   . LEU A 1 91  ? 24.211  -11.962 19.050  1.00 11.30 ? 138 LEU A C   1 
ATOM   634  O  O   . LEU A 1 91  ? 25.078  -12.840 19.165  1.00 12.39 ? 138 LEU A O   1 
ATOM   635  C  CB  . LEU A 1 91  ? 23.902  -11.149 21.373  1.00 11.64 ? 138 LEU A CB  1 
ATOM   636  C  CG  . LEU A 1 91  ? 24.701  -9.880  21.153  1.00 12.13 ? 138 LEU A CG  1 
ATOM   637  C  CD1 . LEU A 1 91  ? 23.823  -8.687  20.747  1.00 13.10 ? 138 LEU A CD1 1 
ATOM   638  C  CD2 . LEU A 1 91  ? 25.535  -9.557  22.368  1.00 14.28 ? 138 LEU A CD2 1 
ATOM   639  N  N   . THR A 1 92  ? 24.168  -11.152 18.000  1.00 11.15 ? 139 THR A N   1 
ATOM   640  C  CA  . THR A 1 92  ? 25.264  -11.024 17.055  1.00 10.91 ? 139 THR A CA  1 
ATOM   641  C  C   . THR A 1 92  ? 25.691  -9.573  17.033  1.00 10.81 ? 139 THR A C   1 
ATOM   642  O  O   . THR A 1 92  ? 24.878  -8.677  17.208  1.00 11.81 ? 139 THR A O   1 
ATOM   643  C  CB  . THR A 1 92  ? 24.872  -11.500 15.666  1.00 11.55 ? 139 THR A CB  1 
ATOM   644  O  OG1 . THR A 1 92  ? 23.714  -10.789 15.184  1.00 12.15 ? 139 THR A OG1 1 
ATOM   645  C  CG2 . THR A 1 92  ? 24.564  -12.973 15.647  1.00 11.68 ? 139 THR A CG2 1 
ATOM   646  N  N   . LEU A 1 93  ? 26.974  -9.365  16.751  1.00 11.08 ? 140 LEU A N   1 
ATOM   647  C  CA  . LEU A 1 93  ? 27.556  -8.046  16.626  1.00 11.73 ? 140 LEU A CA  1 
ATOM   648  C  C   . LEU A 1 93  ? 28.302  -8.036  15.316  1.00 12.80 ? 140 LEU A C   1 
ATOM   649  O  O   . LEU A 1 93  ? 29.206  -8.831  15.147  1.00 14.31 ? 140 LEU A O   1 
ATOM   650  C  CB  . LEU A 1 93  ? 28.505  -7.815  17.774  1.00 13.06 ? 140 LEU A CB  1 
ATOM   651  C  CG  . LEU A 1 93  ? 27.844  -7.631  19.134  1.00 13.36 ? 140 LEU A CG  1 
ATOM   652  C  CD1 . LEU A 1 93  ? 28.892  -7.590  20.197  1.00 14.39 ? 140 LEU A CD1 1 
ATOM   653  C  CD2 . LEU A 1 93  ? 26.987  -6.382  19.180  1.00 15.67 ? 140 LEU A CD2 1 
ATOM   654  N  N   . THR A 1 94  ? 27.906  -7.163  14.391  1.00 11.99 ? 141 THR A N   1 
ATOM   655  C  CA  . THR A 1 94  ? 28.438  -7.105  13.036  1.00 11.80 ? 141 THR A CA  1 
ATOM   656  C  C   . THR A 1 94  ? 29.005  -5.718  12.853  1.00 12.73 ? 141 THR A C   1 
ATOM   657  O  O   . THR A 1 94  ? 28.275  -4.732  13.027  1.00 13.62 ? 141 THR A O   1 
ATOM   658  C  CB  . THR A 1 94  ? 27.309  -7.379  12.053  1.00 12.33 ? 141 THR A CB  1 
ATOM   659  O  OG1 . THR A 1 94  ? 26.598  -8.564  12.412  1.00 13.43 ? 141 THR A OG1 1 
ATOM   660  C  CG2 . THR A 1 94  ? 27.865  -7.568  10.656  1.00 14.57 ? 141 THR A CG2 1 
ATOM   661  N  N   . ILE A 1 95  ? 30.283  -5.617  12.502  1.00 11.96 ? 142 ILE A N   1 
ATOM   662  C  CA  . ILE A 1 95  ? 30.944  -4.330  12.305  1.00 13.13 ? 142 ILE A CA  1 
ATOM   663  C  C   . ILE A 1 95  ? 31.056  -4.041  10.818  1.00 12.87 ? 142 ILE A C   1 
ATOM   664  O  O   . ILE A 1 95  ? 31.224  -4.917  10.027  1.00 13.45 ? 142 ILE A O   1 
ATOM   665  C  CB  . ILE A 1 95  ? 32.328  -4.314  12.998  1.00 14.09 ? 142 ILE A CB  1 
ATOM   666  C  CG1 . ILE A 1 95  ? 32.900  -2.899  13.073  1.00 15.32 ? 142 ILE A CG1 1 
ATOM   667  C  CG2 . ILE A 1 95  ? 33.325  -5.277  12.377  1.00 14.67 ? 142 ILE A CG2 1 
ATOM   668  C  CD1 . ILE A 1 95  ? 34.086  -2.759  14.003  1.00 15.94 ? 142 ILE A CD1 1 
ATOM   669  N  N   . GLY A 1 96  ? 30.982  -2.755  10.498  1.00 13.28 ? 143 GLY A N   1 
ATOM   670  C  CA  . GLY A 1 96  ? 31.219  -2.280  9.151   1.00 13.11 ? 143 GLY A CA  1 
ATOM   671  C  C   . GLY A 1 96  ? 31.979  -0.979  9.158   1.00 13.40 ? 143 GLY A C   1 
ATOM   672  O  O   . GLY A 1 96  ? 31.983  -0.256  10.115  1.00 14.60 ? 143 GLY A O   1 
ATOM   673  N  N   . PHE A 1 97  ? 32.620  -0.747  8.029   1.00 13.18 ? 144 PHE A N   1 
ATOM   674  C  CA  . PHE A 1 97  ? 33.455  0.439   7.841   1.00 14.31 ? 144 PHE A CA  1 
ATOM   675  C  C   . PHE A 1 97  ? 32.840  1.302   6.739   1.00 14.54 ? 144 PHE A C   1 
ATOM   676  O  O   . PHE A 1 97  ? 32.610  0.835   5.629   1.00 15.65 ? 144 PHE A O   1 
ATOM   677  C  CB  . PHE A 1 97  ? 34.853  0.018   7.430   1.00 15.51 ? 144 PHE A CB  1 
ATOM   678  C  CG  . PHE A 1 97  ? 35.577  -0.862  8.418   1.00 16.83 ? 144 PHE A CG  1 
ATOM   679  C  CD1 . PHE A 1 97  ? 35.456  -0.637  9.769   1.00 19.48 ? 144 PHE A CD1 1 
ATOM   680  C  CD2 . PHE A 1 97  ? 36.385  -1.867  7.975   1.00 19.10 ? 144 PHE A CD2 1 
ATOM   681  C  CE1 . PHE A 1 97  ? 36.126  -1.459  10.679  1.00 19.72 ? 144 PHE A CE1 1 
ATOM   682  C  CE2 . PHE A 1 97  ? 37.057  -2.668  8.881   1.00 21.35 ? 144 PHE A CE2 1 
ATOM   683  C  CZ  . PHE A 1 97  ? 36.928  -2.452  10.218  1.00 21.95 ? 144 PHE A CZ  1 
ATOM   684  N  N   . GLY A 1 98  ? 32.632  2.581   7.035   1.00 14.61 ? 145 GLY A N   1 
ATOM   685  C  CA  . GLY A 1 98  ? 32.047  3.469   6.040   1.00 15.55 ? 145 GLY A CA  1 
ATOM   686  C  C   . GLY A 1 98  ? 33.098  4.065   5.108   1.00 16.19 ? 145 GLY A C   1 
ATOM   687  O  O   . GLY A 1 98  ? 34.295  4.056   5.413   1.00 16.85 ? 145 GLY A O   1 
ATOM   688  N  N   . PRO A 1 99  ? 32.665  4.641   3.973   1.00 16.66 ? 146 PRO A N   1 
ATOM   689  C  CA  . PRO A 1 99  ? 33.601  5.304   3.053   1.00 17.99 ? 146 PRO A CA  1 
ATOM   690  C  C   . PRO A 1 99  ? 34.517  6.338   3.698   1.00 18.94 ? 146 PRO A C   1 
ATOM   691  O  O   . PRO A 1 99  ? 35.687  6.417   3.332   1.00 20.09 ? 146 PRO A O   1 
ATOM   692  C  CB  . PRO A 1 99  ? 32.659  5.955   2.019   1.00 20.11 ? 146 PRO A CB  1 
ATOM   693  C  CG  . PRO A 1 99  ? 31.338  5.239   2.095   1.00 21.68 ? 146 PRO A CG  1 
ATOM   694  C  CD  . PRO A 1 99  ? 31.278  4.592   3.483   1.00 19.33 ? 146 PRO A CD  1 
ATOM   695  N  N   . SER A 1 100 ? 33.980  7.108   4.622   1.00 17.97 ? 147 SER A N   1 
ATOM   696  C  CA  . SER A 1 100 ? 34.714  8.179   5.276   1.00 19.38 ? 147 SER A CA  1 
ATOM   697  C  C   . SER A 1 100 ? 35.891  7.654   6.092   1.00 21.91 ? 147 SER A C   1 
ATOM   698  O  O   . SER A 1 100 ? 36.832  8.410   6.350   1.00 22.14 ? 147 SER A O   1 
ATOM   699  C  CB  . SER A 1 100 ? 33.788  9.041   6.081   1.00 20.02 ? 147 SER A CB  1 
ATOM   700  O  OG  . SER A 1 100 ? 33.002  8.288   7.009   1.00 20.94 ? 147 SER A OG  1 
ATOM   701  N  N   . LEU A 1 101 ? 35.853  6.395   6.526   1.00 18.84 ? 148 LEU A N   1 
ATOM   702  C  CA  . LEU A 1 101 ? 36.954  5.834   7.294   1.00 19.10 ? 148 LEU A CA  1 
ATOM   703  C  C   . LEU A 1 101 ? 38.232  5.870   6.462   1.00 21.52 ? 148 LEU A C   1 
ATOM   704  O  O   . LEU A 1 101 ? 39.327  5.979   7.022   1.00 21.15 ? 148 LEU A O   1 
ATOM   705  C  CB  . LEU A 1 101 ? 36.674  4.402   7.754   1.00 20.80 ? 148 LEU A CB  1 
ATOM   706  C  CG  . LEU A 1 101 ? 37.731  3.797   8.687   1.00 21.81 ? 148 LEU A CG  1 
ATOM   707  C  CD1 . LEU A 1 101 ? 37.654  4.461   10.021  1.00 26.00 ? 148 LEU A CD1 1 
ATOM   708  C  CD2 . LEU A 1 101 ? 37.526  2.285   8.809   1.00 23.54 ? 148 LEU A CD2 1 
ATOM   709  N  N   . PHE A 1 102 ? 38.104  5.705   5.153   1.00 21.73 ? 149 PHE A N   1 
ATOM   710  C  CA  . PHE A 1 102 ? 39.279  5.476   4.323   1.00 23.45 ? 149 PHE A CA  1 
ATOM   711  C  C   . PHE A 1 102 ? 40.035  6.791   4.070   1.00 26.87 ? 149 PHE A C   1 
ATOM   712  O  O   . PHE A 1 102 ? 41.094  6.746   3.449   1.00 29.94 ? 149 PHE A O   1 
ATOM   713  C  CB  . PHE A 1 102 ? 38.885  4.721   3.046   1.00 23.22 ? 149 PHE A CB  1 
ATOM   714  C  CG  . PHE A 1 102 ? 38.344  3.324   3.311   1.00 21.42 ? 149 PHE A CG  1 
ATOM   715  C  CD1 . PHE A 1 102 ? 36.999  3.122   3.624   1.00 22.26 ? 149 PHE A CD1 1 
ATOM   716  C  CD2 . PHE A 1 102 ? 39.186  2.227   3.339   1.00 21.33 ? 149 PHE A CD2 1 
ATOM   717  C  CE1 . PHE A 1 102 ? 36.543  1.844   3.922   1.00 22.91 ? 149 PHE A CE1 1 
ATOM   718  C  CE2 . PHE A 1 102 ? 38.730  0.969   3.650   1.00 23.76 ? 149 PHE A CE2 1 
ATOM   719  C  CZ  . PHE A 1 102 ? 37.414  0.783   3.960   1.00 23.66 ? 149 PHE A CZ  1 
ATOM   720  N  N   . THR A 1 103 ? 39.557  7.927   4.604   1.00 27.80 ? 150 THR A N   1 
ATOM   721  C  CA  . THR A 1 103 ? 40.334  9.171   4.567   1.00 29.80 ? 150 THR A CA  1 
ATOM   722  C  C   . THR A 1 103 ? 41.334  9.236   5.722   1.00 32.52 ? 150 THR A C   1 
ATOM   723  O  O   . THR A 1 103 ? 42.086  10.208  5.802   1.00 31.81 ? 150 THR A O   1 
ATOM   724  C  CB  . THR A 1 103 ? 39.421  10.396  4.595   1.00 30.27 ? 150 THR A CB  1 
ATOM   725  O  OG1 . THR A 1 103 ? 38.725  10.490  5.830   1.00 32.15 ? 150 THR A OG1 1 
ATOM   726  C  CG2 . THR A 1 103 ? 38.390  10.393  3.488   1.00 32.77 ? 150 THR A CG2 1 
ATOM   727  N  N   . ARG A 1 104 ? 41.362  8.218   6.592   1.00 29.83 ? 151 ARG A N   1 
ATOM   728  C  CA  . ARG A 1 104 ? 42.202  8.200   7.777   1.00 28.82 ? 151 ARG A CA  1 
ATOM   729  C  C   . ARG A 1 104 ? 43.175  7.025   7.692   1.00 25.54 ? 151 ARG A C   1 
ATOM   730  O  O   . ARG A 1 104 ? 42.980  6.086   6.925   1.00 24.76 ? 151 ARG A O   1 
ATOM   731  C  CB  . ARG A 1 104 ? 41.332  8.052   9.030   1.00 32.89 ? 151 ARG A CB  1 
ATOM   732  C  CG  . ARG A 1 104 ? 40.249  9.109   9.184   1.00 39.27 ? 151 ARG A CG  1 
ATOM   733  C  CD  . ARG A 1 104 ? 39.566  9.025   10.551  1.00 42.65 ? 151 ARG A CD  1 
ATOM   734  N  NE  . ARG A 1 104 ? 38.835  10.270  10.814  1.00 47.08 ? 151 ARG A NE  1 
ATOM   735  C  CZ  . ARG A 1 104 ? 39.140  11.149  11.757  1.00 44.66 ? 151 ARG A CZ  1 
ATOM   736  N  NH1 . ARG A 1 104 ? 40.017  10.854  12.700  1.00 41.65 ? 151 ARG A NH1 1 
ATOM   737  N  NH2 . ARG A 1 104 ? 38.538  12.322  11.777  1.00 51.16 ? 151 ARG A NH2 1 
ATOM   738  N  N   . PHE A 1 105 ? 44.254  7.112   8.480   1.00 25.69 ? 152 PHE A N   1 
ATOM   739  C  CA  . PHE A 1 105 ? 45.135  5.991   8.760   1.00 26.69 ? 152 PHE A CA  1 
ATOM   740  C  C   . PHE A 1 105 ? 45.845  5.457   7.513   1.00 26.00 ? 152 PHE A C   1 
ATOM   741  O  O   . PHE A 1 105 ? 46.280  4.310   7.527   1.00 30.59 ? 152 PHE A O   1 
ATOM   742  C  CB  . PHE A 1 105 ? 44.381  4.850   9.467   1.00 26.34 ? 152 PHE A CB  1 
ATOM   743  C  CG  . PHE A 1 105 ? 43.531  5.249   10.664  1.00 25.27 ? 152 PHE A CG  1 
ATOM   744  C  CD1 . PHE A 1 105 ? 44.033  6.108   11.632  1.00 27.78 ? 152 PHE A CD1 1 
ATOM   745  C  CD2 . PHE A 1 105 ? 42.216  4.809   10.799  1.00 26.90 ? 152 PHE A CD2 1 
ATOM   746  C  CE1 . PHE A 1 105 ? 43.272  6.458   12.734  1.00 26.39 ? 152 PHE A CE1 1 
ATOM   747  C  CE2 . PHE A 1 105 ? 41.447  5.197   11.892  1.00 26.78 ? 152 PHE A CE2 1 
ATOM   748  C  CZ  . PHE A 1 105 ? 41.975  6.009   12.860  1.00 26.64 ? 152 PHE A CZ  1 
ATOM   749  N  N   . GLY A 1 106 ? 45.954  6.277   6.464   1.00 27.93 ? 153 GLY A N   1 
ATOM   750  C  CA  . GLY A 1 106 ? 46.621  5.902   5.223   1.00 30.51 ? 153 GLY A CA  1 
ATOM   751  C  C   . GLY A 1 106 ? 45.871  4.815   4.458   1.00 29.36 ? 153 GLY A C   1 
ATOM   752  O  O   . GLY A 1 106 ? 46.476  3.999   3.755   1.00 30.72 ? 153 GLY A O   1 
ATOM   753  N  N   . LEU A 1 107 ? 44.534  4.820   4.589   1.00 29.43 ? 154 LEU A N   1 
ATOM   754  C  CA  . LEU A 1 107 ? 43.702  3.757   4.044   1.00 26.85 ? 154 LEU A CA  1 
ATOM   755  C  C   . LEU A 1 107 ? 43.131  4.087   2.670   1.00 26.16 ? 154 LEU A C   1 
ATOM   756  O  O   . LEU A 1 107 ? 42.429  3.258   2.109   1.00 26.29 ? 154 LEU A O   1 
ATOM   757  C  CB  . LEU A 1 107 ? 42.557  3.511   5.022   1.00 24.99 ? 154 LEU A CB  1 
ATOM   758  C  CG  . LEU A 1 107 ? 42.986  2.867   6.332   1.00 25.28 ? 154 LEU A CG  1 
ATOM   759  C  CD1 . LEU A 1 107 ? 41.699  2.793   7.149   1.00 25.22 ? 154 LEU A CD1 1 
ATOM   760  C  CD2 . LEU A 1 107 ? 43.642  1.507   6.178   1.00 25.38 ? 154 LEU A CD2 1 
ATOM   761  N  N   . ALA A 1 108 ? 43.429  5.269   2.113   1.00 28.23 ? 155 ALA A N   1 
ATOM   762  C  CA  . ALA A 1 108 ? 42.702  5.744   0.937   1.00 29.78 ? 155 ALA A CA  1 
ATOM   763  C  C   . ALA A 1 108 ? 42.724  4.718   -0.202  1.00 28.98 ? 155 ALA A C   1 
ATOM   764  O  O   . ALA A 1 108 ? 41.700  4.462   -0.831  1.00 29.48 ? 155 ALA A O   1 
ATOM   765  C  CB  . ALA A 1 108 ? 43.235  7.099   0.495   1.00 30.86 ? 155 ALA A CB  1 
ATOM   766  N  N   . ASP A 1 109 ? 43.863  4.067   -0.441  1.00 28.56 ? 156 ASP A N   1 
ATOM   767  C  CA  . ASP A 1 109 ? 44.002  3.158   -1.565  1.00 30.05 ? 156 ASP A CA  1 
ATOM   768  C  C   . ASP A 1 109 ? 43.352  1.793   -1.321  1.00 28.93 ? 156 ASP A C   1 
ATOM   769  O  O   . ASP A 1 109 ? 43.324  0.958   -2.211  1.00 28.30 ? 156 ASP A O   1 
ATOM   770  C  CB  . ASP A 1 109 ? 45.467  2.888   -1.860  1.00 35.26 ? 156 ASP A CB  1 
ATOM   771  C  CG  . ASP A 1 109 ? 46.235  4.034   -2.498  1.00 41.66 ? 156 ASP A CG  1 
ATOM   772  O  OD1 . ASP A 1 109 ? 45.593  4.974   -3.017  1.00 41.40 ? 156 ASP A OD1 1 
ATOM   773  O  OD2 . ASP A 1 109 ? 47.476  3.967   -2.458  1.00 47.99 ? 156 ASP A OD2 1 
ATOM   774  N  N   . LEU A 1 110 ? 42.828  1.559   -0.110  1.00 24.68 ? 157 LEU A N   1 
ATOM   775  C  CA  . LEU A 1 110 ? 42.240  0.270   0.221   1.00 24.42 ? 157 LEU A CA  1 
ATOM   776  C  C   . LEU A 1 110 ? 40.711  0.347   0.205   1.00 22.60 ? 157 LEU A C   1 
ATOM   777  O  O   . LEU A 1 110 ? 40.071  -0.670  0.500   1.00 22.52 ? 157 LEU A O   1 
ATOM   778  C  CB  . LEU A 1 110 ? 42.787  -0.159  1.581   1.00 26.72 ? 157 LEU A CB  1 
ATOM   779  C  CG  . LEU A 1 110 ? 44.258  -0.579  1.573   1.00 30.58 ? 157 LEU A CG  1 
ATOM   780  C  CD1 . LEU A 1 110 ? 44.853  -0.477  2.965   1.00 34.68 ? 157 LEU A CD1 1 
ATOM   781  C  CD2 . LEU A 1 110 ? 44.366  -1.984  1.079   1.00 30.55 ? 157 LEU A CD2 1 
ATOM   782  N  N   . ARG A 1 111 ? 40.132  1.508   -0.128  1.00 22.33 ? 158 ARG A N   1 
ATOM   783  C  CA  . ARG A 1 111 ? 38.682  1.616   -0.211  1.00 23.67 ? 158 ARG A CA  1 
ATOM   784  C  C   . ARG A 1 111 ? 38.196  0.709   -1.332  1.00 23.34 ? 158 ARG A C   1 
ATOM   785  O  O   . ARG A 1 111 ? 38.660  0.835   -2.465  1.00 23.57 ? 158 ARG A O   1 
ATOM   786  C  CB  . ARG A 1 111 ? 38.236  3.053   -0.473  1.00 23.85 ? 158 ARG A CB  1 
ATOM   787  C  CG  . ARG A 1 111 ? 36.718  3.167   -0.564  1.00 24.88 ? 158 ARG A CG  1 
ATOM   788  C  CD  . ARG A 1 111 ? 36.235  4.535   -0.914  1.00 28.53 ? 158 ARG A CD  1 
ATOM   789  N  NE  . ARG A 1 111 ? 34.783  4.475   -1.134  1.00 26.11 ? 158 ARG A NE  1 
ATOM   790  C  CZ  . ARG A 1 111 ? 34.018  5.530   -1.300  1.00 25.71 ? 158 ARG A CZ  1 
ATOM   791  N  NH1 . ARG A 1 111 ? 34.482  6.716   -0.979  1.00 28.60 ? 158 ARG A NH1 1 
ATOM   792  N  NH2 . ARG A 1 111 ? 32.770  5.341   -1.706  1.00 25.97 ? 158 ARG A NH2 1 
ATOM   793  N  N   . PRO A 1 112 ? 37.279  -0.255  -1.063  1.00 22.71 ? 159 PRO A N   1 
ATOM   794  C  CA  . PRO A 1 112 ? 36.776  -1.134  -2.117  1.00 20.80 ? 159 PRO A CA  1 
ATOM   795  C  C   . PRO A 1 112 ? 35.945  -0.373  -3.137  1.00 21.51 ? 159 PRO A C   1 
ATOM   796  O  O   . PRO A 1 112 ? 35.123  0.453   -2.775  1.00 21.26 ? 159 PRO A O   1 
ATOM   797  C  CB  . PRO A 1 112 ? 35.877  -2.102  -1.331  1.00 21.83 ? 159 PRO A CB  1 
ATOM   798  C  CG  . PRO A 1 112 ? 36.369  -1.989  0.075   1.00 22.96 ? 159 PRO A CG  1 
ATOM   799  C  CD  . PRO A 1 112 ? 36.714  -0.554  0.271   1.00 21.06 ? 159 PRO A CD  1 
ATOM   800  N  N   . GLU A 1 113 ? 36.108  -0.729  -4.409  1.00 22.87 ? 160 GLU A N   1 
ATOM   801  C  CA  . GLU A 1 113 ? 35.285  -0.157  -5.456  1.00 24.76 ? 160 GLU A CA  1 
ATOM   802  C  C   . GLU A 1 113 ? 33.817  -0.519  -5.226  1.00 23.64 ? 160 GLU A C   1 
ATOM   803  O  O   . GLU A 1 113 ? 32.920  0.265   -5.554  1.00 23.77 ? 160 GLU A O   1 
ATOM   804  C  CB  . GLU A 1 113 ? 35.743  -0.633  -6.839  1.00 30.52 ? 160 GLU A CB  1 
ATOM   805  C  CG  . GLU A 1 113 ? 36.970  0.115   -7.354  1.00 39.97 ? 160 GLU A CG  1 
ATOM   806  C  CD  . GLU A 1 113 ? 36.786  1.609   -7.598  1.00 43.46 ? 160 GLU A CD  1 
ATOM   807  O  OE1 . GLU A 1 113 ? 37.480  2.405   -6.922  1.00 52.71 ? 160 GLU A OE1 1 
ATOM   808  O  OE2 . GLU A 1 113 ? 35.967  1.993   -8.460  1.00 45.83 ? 160 GLU A OE2 1 
ATOM   809  N  N   . ALA A 1 114 ? 33.573  -1.695  -4.618  1.00 20.93 ? 161 ALA A N   1 
ATOM   810  C  CA  . ALA A 1 114 ? 32.213  -2.153  -4.346  1.00 21.42 ? 161 ALA A CA  1 
ATOM   811  C  C   . ALA A 1 114 ? 31.534  -1.320  -3.247  1.00 20.10 ? 161 ALA A C   1 
ATOM   812  O  O   . ALA A 1 114 ? 30.302  -1.370  -3.115  1.00 20.76 ? 161 ALA A O   1 
ATOM   813  C  CB  . ALA A 1 114 ? 32.195  -3.614  -4.008  1.00 20.91 ? 161 ALA A CB  1 
ATOM   814  N  N   . LEU A 1 115 ? 32.295  -0.542  -2.481  1.00 19.63 ? 162 LEU A N   1 
ATOM   815  C  CA  . LEU A 1 115 ? 31.754  0.368   -1.496  1.00 19.77 ? 162 LEU A CA  1 
ATOM   816  C  C   . LEU A 1 115 ? 31.484  1.686   -2.209  1.00 19.64 ? 162 LEU A C   1 
ATOM   817  O  O   . LEU A 1 115 ? 32.222  2.656   -2.086  1.00 21.76 ? 162 LEU A O   1 
ATOM   818  C  CB  . LEU A 1 115 ? 32.715  0.514   -0.315  1.00 18.91 ? 162 LEU A CB  1 
ATOM   819  C  CG  . LEU A 1 115 ? 32.197  1.397   0.814   1.00 18.67 ? 162 LEU A CG  1 
ATOM   820  C  CD1 . LEU A 1 115 ? 30.958  0.840   1.460   1.00 19.73 ? 162 LEU A CD1 1 
ATOM   821  C  CD2 . LEU A 1 115 ? 33.262  1.559   1.870   1.00 18.05 ? 162 LEU A CD2 1 
ATOM   822  N  N   . ALA A 1 116 ? 30.367  1.710   -2.926  1.00 20.59 ? 163 ALA A N   1 
ATOM   823  C  CA  . ALA A 1 116 ? 30.052  2.805   -3.823  1.00 21.50 ? 163 ALA A CA  1 
ATOM   824  C  C   . ALA A 1 116 ? 29.231  3.816   -3.051  1.00 22.65 ? 163 ALA A C   1 
ATOM   825  O  O   . ALA A 1 116 ? 28.400  3.445   -2.232  1.00 23.84 ? 163 ALA A O   1 
ATOM   826  C  CB  . ALA A 1 116 ? 29.297  2.281   -5.019  1.00 21.78 ? 163 ALA A CB  1 
ATOM   827  N  N   . ASP A 1 117 ? 29.441  5.106   -3.288  1.00 22.90 ? 164 ASP A N   1 
ATOM   828  C  CA  . ASP A 1 117 ? 28.504  6.074   -2.761  1.00 24.10 ? 164 ASP A CA  1 
ATOM   829  C  C   . ASP A 1 117 ? 27.208  5.956   -3.553  1.00 24.00 ? 164 ASP A C   1 
ATOM   830  O  O   . ASP A 1 117 ? 27.206  5.647   -4.736  1.00 26.96 ? 164 ASP A O   1 
ATOM   831  C  CB  . ASP A 1 117 ? 29.007  7.498   -2.895  1.00 28.18 ? 164 ASP A CB  1 
ATOM   832  C  CG  . ASP A 1 117 ? 30.329  7.756   -2.190  1.00 33.38 ? 164 ASP A CG  1 
ATOM   833  O  OD1 . ASP A 1 117 ? 30.400  7.488   -0.981  1.00 32.83 ? 164 ASP A OD1 1 
ATOM   834  O  OD2 . ASP A 1 117 ? 31.257  8.242   -2.863  1.00 41.52 ? 164 ASP A OD2 1 
ATOM   835  N  N   . LEU A 1 118 ? 26.090  6.167   -2.873  1.00 22.06 ? 165 LEU A N   1 
ATOM   836  C  CA  . LEU A 1 118 ? 24.817  6.000   -3.531  1.00 20.11 ? 165 LEU A CA  1 
ATOM   837  C  C   . LEU A 1 118 ? 24.544  7.267   -4.315  1.00 21.19 ? 165 LEU A C   1 
ATOM   838  O  O   . LEU A 1 118 ? 24.816  8.347   -3.802  1.00 24.61 ? 165 LEU A O   1 
ATOM   839  C  CB  . LEU A 1 118 ? 23.730  5.773   -2.493  1.00 20.60 ? 165 LEU A CB  1 
ATOM   840  C  CG  . LEU A 1 118 ? 23.871  4.489   -1.683  1.00 19.84 ? 165 LEU A CG  1 
ATOM   841  C  CD1 . LEU A 1 118 ? 22.739  4.415   -0.653  1.00 20.82 ? 165 LEU A CD1 1 
ATOM   842  C  CD2 . LEU A 1 118 ? 23.916  3.280   -2.564  1.00 19.99 ? 165 LEU A CD2 1 
ATOM   843  N  N   . PRO A 1 119 ? 23.876  7.150   -5.474  1.00 23.75 ? 166 PRO A N   1 
ATOM   844  C  CA  . PRO A 1 119 ? 23.378  8.349   -6.143  1.00 25.52 ? 166 PRO A CA  1 
ATOM   845  C  C   . PRO A 1 119 ? 22.202  8.921   -5.363  1.00 25.55 ? 166 PRO A C   1 
ATOM   846  O  O   . PRO A 1 119 ? 21.651  8.273   -4.475  1.00 23.19 ? 166 PRO A O   1 
ATOM   847  C  CB  . PRO A 1 119 ? 23.002  7.830   -7.528  1.00 27.49 ? 166 PRO A CB  1 
ATOM   848  C  CG  . PRO A 1 119 ? 22.607  6.394   -7.303  1.00 27.85 ? 166 PRO A CG  1 
ATOM   849  C  CD  . PRO A 1 119 ? 23.456  5.904   -6.128  1.00 24.58 ? 166 PRO A CD  1 
ATOM   850  N  N   . LYS A 1 120 ? 21.785  10.130  -5.725  1.00 26.35 ? 167 LYS A N   1 
ATOM   851  C  CA  . LYS A 1 120 ? 20.551  10.703  -5.245  1.00 26.60 ? 167 LYS A CA  1 
ATOM   852  C  C   . LYS A 1 120 ? 19.429  9.965   -5.952  1.00 23.86 ? 167 LYS A C   1 
ATOM   853  O  O   . LYS A 1 120 ? 19.554  9.605   -7.118  1.00 26.55 ? 167 LYS A O   1 
ATOM   854  C  CB  . LYS A 1 120 ? 20.564  12.199  -5.589  1.00 32.51 ? 167 LYS A CB  1 
ATOM   855  C  CG  . LYS A 1 120 ? 21.712  12.982  -4.931  1.00 41.38 ? 167 LYS A CG  1 
ATOM   856  C  CD  . LYS A 1 120 ? 22.929  13.379  -5.776  1.00 48.99 ? 167 LYS A CD  1 
ATOM   857  C  CE  . LYS A 1 120 ? 23.946  12.316  -6.145  1.00 49.96 ? 167 LYS A CE  1 
ATOM   858  N  NZ  . LYS A 1 120 ? 23.718  11.705  -7.467  1.00 47.78 ? 167 LYS A NZ  1 
ATOM   859  N  N   . PHE A 1 121 ? 18.400  9.616   -5.196  1.00 19.81 ? 168 PHE A N   1 
ATOM   860  C  CA  . PHE A 1 121 ? 17.222  8.987   -5.748  1.00 21.38 ? 168 PHE A CA  1 
ATOM   861  C  C   . PHE A 1 121 ? 16.069  9.962   -5.636  1.00 21.45 ? 168 PHE A C   1 
ATOM   862  O  O   . PHE A 1 121 ? 16.007  10.761  -4.716  1.00 21.08 ? 168 PHE A O   1 
ATOM   863  C  CB  . PHE A 1 121 ? 16.879  7.712   -4.974  1.00 20.14 ? 168 PHE A CB  1 
ATOM   864  C  CG  . PHE A 1 121 ? 17.950  6.664   -5.134  1.00 19.27 ? 168 PHE A CG  1 
ATOM   865  C  CD1 . PHE A 1 121 ? 18.110  5.943   -6.318  1.00 19.56 ? 168 PHE A CD1 1 
ATOM   866  C  CD2 . PHE A 1 121 ? 18.785  6.364   -4.076  1.00 18.79 ? 168 PHE A CD2 1 
ATOM   867  C  CE1 . PHE A 1 121 ? 19.118  5.025   -6.438  1.00 21.10 ? 168 PHE A CE1 1 
ATOM   868  C  CE2 . PHE A 1 121 ? 19.741  5.389   -4.205  1.00 21.09 ? 168 PHE A CE2 1 
ATOM   869  C  CZ  . PHE A 1 121 ? 19.903  4.737   -5.363  1.00 20.45 ? 168 PHE A CZ  1 
ATOM   870  N  N   . PRO A 1 122 ? 15.128  9.949   -6.609  1.00 21.99 ? 169 PRO A N   1 
ATOM   871  C  CA  . PRO A 1 122 ? 13.967  10.838  -6.553  1.00 26.53 ? 169 PRO A CA  1 
ATOM   872  C  C   . PRO A 1 122 ? 13.229  10.630  -5.240  1.00 24.60 ? 169 PRO A C   1 
ATOM   873  O  O   . PRO A 1 122 ? 13.038  9.502   -4.770  1.00 26.82 ? 169 PRO A O   1 
ATOM   874  C  CB  . PRO A 1 122 ? 13.094  10.486  -7.774  1.00 25.96 ? 169 PRO A CB  1 
ATOM   875  C  CG  . PRO A 1 122 ? 13.845  9.413   -8.518  1.00 27.85 ? 169 PRO A CG  1 
ATOM   876  C  CD  . PRO A 1 122 ? 15.149  9.095   -7.801  1.00 25.22 ? 169 PRO A CD  1 
ATOM   877  N  N   . GLY A 1 123 ? 12.837  11.725  -4.611  1.00 22.86 ? 170 GLY A N   1 
ATOM   878  C  CA  . GLY A 1 123 ? 12.040  11.654  -3.411  1.00 24.06 ? 170 GLY A CA  1 
ATOM   879  C  C   . GLY A 1 123 ? 12.894  11.609  -2.145  1.00 21.81 ? 170 GLY A C   1 
ATOM   880  O  O   . GLY A 1 123 ? 12.323  11.761  -1.083  1.00 24.83 ? 170 GLY A O   1 
ATOM   881  N  N   . ASP A 1 124 ? 14.222  11.429  -2.265  1.00 21.70 ? 171 ASP A N   1 
ATOM   882  C  CA  . ASP A 1 124 ? 15.103  11.396  -1.088  1.00 21.38 ? 171 ASP A CA  1 
ATOM   883  C  C   . ASP A 1 124 ? 14.877  12.668  -0.270  1.00 20.90 ? 171 ASP A C   1 
ATOM   884  O  O   . ASP A 1 124 ? 14.783  13.766  -0.850  1.00 23.66 ? 171 ASP A O   1 
ATOM   885  C  CB  . ASP A 1 124 ? 16.593  11.428  -1.447  1.00 24.73 ? 171 ASP A CB  1 
ATOM   886  C  CG  . ASP A 1 124 ? 17.326  10.149  -1.849  1.00 26.98 ? 171 ASP A CG  1 
ATOM   887  O  OD1 . ASP A 1 124 ? 16.733  9.084   -1.652  1.00 23.44 ? 171 ASP A OD1 1 
ATOM   888  O  OD2 . ASP A 1 124 ? 18.497  10.255  -2.367  1.00 28.76 ? 171 ASP A OD2 1 
ATOM   889  N  N   . ASN A 1 125 ? 14.943  12.567  1.056   1.00 18.67 ? 172 ASN A N   1 
ATOM   890  C  CA  . ASN A 1 125 ? 14.944  13.707  1.958   1.00 19.59 ? 172 ASN A CA  1 
ATOM   891  C  C   . ASN A 1 125 ? 15.842  13.336  3.141   1.00 16.59 ? 172 ASN A C   1 
ATOM   892  O  O   . ASN A 1 125 ? 15.336  13.140  4.228   1.00 18.76 ? 172 ASN A O   1 
ATOM   893  C  CB  . ASN A 1 125 ? 13.508  14.058  2.304   1.00 23.76 ? 172 ASN A CB  1 
ATOM   894  C  CG  . ASN A 1 125 ? 13.367  15.264  3.201   1.00 31.69 ? 172 ASN A CG  1 
ATOM   895  O  OD1 . ASN A 1 125 ? 14.216  16.160  3.206   1.00 32.36 ? 172 ASN A OD1 1 
ATOM   896  N  ND2 . ASN A 1 125 ? 12.339  15.259  4.032   1.00 38.97 ? 172 ASN A ND2 1 
ATOM   897  N  N   . LEU A 1 126 ? 17.132  13.207  2.838   1.00 19.30 ? 173 LEU A N   1 
ATOM   898  C  CA  . LEU A 1 126 ? 18.097  12.593  3.745   1.00 18.34 ? 173 LEU A CA  1 
ATOM   899  C  C   . LEU A 1 126 ? 18.502  13.600  4.810   1.00 21.31 ? 173 LEU A C   1 
ATOM   900  O  O   . LEU A 1 126 ? 19.022  14.672  4.493   1.00 23.84 ? 173 LEU A O   1 
ATOM   901  C  CB  . LEU A 1 126 ? 19.319  12.026  3.025   1.00 20.13 ? 173 LEU A CB  1 
ATOM   902  C  CG  . LEU A 1 126 ? 19.023  11.052  1.882   1.00 20.22 ? 173 LEU A CG  1 
ATOM   903  C  CD1 . LEU A 1 126 ? 20.281  10.572  1.258   1.00 22.29 ? 173 LEU A CD1 1 
ATOM   904  C  CD2 . LEU A 1 126 ? 18.211  9.849   2.371   1.00 20.43 ? 173 LEU A CD2 1 
ATOM   905  N  N   . ASP A 1 127 ? 18.360  13.213  6.071   1.00 19.58 ? 174 ASP A N   1 
ATOM   906  C  CA  . ASP A 1 127 ? 18.915  13.962  7.187   1.00 20.00 ? 174 ASP A CA  1 
ATOM   907  C  C   . ASP A 1 127 ? 20.403  13.645  7.315   1.00 23.77 ? 174 ASP A C   1 
ATOM   908  O  O   . ASP A 1 127 ? 20.780  12.510  7.584   1.00 19.28 ? 174 ASP A O   1 
ATOM   909  C  CB  . ASP A 1 127 ? 18.165  13.618  8.454   1.00 23.01 ? 174 ASP A CB  1 
ATOM   910  C  CG  . ASP A 1 127 ? 18.607  14.371  9.700   1.00 28.07 ? 174 ASP A CG  1 
ATOM   911  O  OD1 . ASP A 1 127 ? 19.618  15.075  9.593   1.00 31.23 ? 174 ASP A OD1 1 
ATOM   912  O  OD2 . ASP A 1 127 ? 17.953  14.176  10.744  1.00 32.33 ? 174 ASP A OD2 1 
ATOM   913  N  N   . ARG A 1 128 ? 21.272  14.636  7.116   1.00 21.33 ? 175 ARG A N   1 
ATOM   914  C  CA  . ARG A 1 128 ? 22.705  14.409  7.128   1.00 24.13 ? 175 ARG A CA  1 
ATOM   915  C  C   . ARG A 1 128 ? 23.175  13.978  8.510   1.00 22.75 ? 175 ARG A C   1 
ATOM   916  O  O   . ARG A 1 128 ? 24.156  13.235  8.602   1.00 25.11 ? 175 ARG A O   1 
ATOM   917  C  CB  . ARG A 1 128 ? 23.429  15.702  6.720   1.00 30.02 ? 175 ARG A CB  1 
ATOM   918  C  CG  . ARG A 1 128 ? 23.149  16.069  5.269   1.00 39.12 ? 175 ARG A CG  1 
ATOM   919  C  CD  . ARG A 1 128 ? 23.943  17.285  4.798   1.00 48.90 ? 175 ARG A CD  1 
ATOM   920  N  NE  . ARG A 1 128 ? 25.380  16.992  4.851   1.00 53.70 ? 175 ARG A NE  1 
ATOM   921  C  CZ  . ARG A 1 128 ? 26.211  17.311  5.847   1.00 58.13 ? 175 ARG A CZ  1 
ATOM   922  N  NH1 . ARG A 1 128 ? 25.793  18.020  6.884   1.00 57.78 ? 175 ARG A NH1 1 
ATOM   923  N  NH2 . ARG A 1 128 ? 27.467  16.904  5.808   1.00 59.59 ? 175 ARG A NH2 1 
ATOM   924  N  N   . ALA A 1 129 ? 22.465  14.380  9.560   1.00 24.23 ? 176 ALA A N   1 
ATOM   925  C  CA  . ALA A 1 129 ? 22.901  14.059  10.912  1.00 27.14 ? 176 ALA A CA  1 
ATOM   926  C  C   . ALA A 1 129 ? 22.694  12.576  11.179  1.00 26.98 ? 176 ALA A C   1 
ATOM   927  O  O   . ALA A 1 129 ? 23.351  12.014  12.057  1.00 33.97 ? 176 ALA A O   1 
ATOM   928  C  CB  . ALA A 1 129 ? 22.156  14.877  11.933  1.00 29.93 ? 176 ALA A CB  1 
ATOM   929  N  N   . ARG A 1 130 ? 21.728  11.967  10.493  1.00 23.89 ? 177 ARG A N   1 
ATOM   930  C  CA  . ARG A 1 130 ? 21.368  10.578  10.743  1.00 26.56 ? 177 ARG A CA  1 
ATOM   931  C  C   . ARG A 1 130 ? 21.684  9.749   9.506   1.00 20.80 ? 177 ARG A C   1 
ATOM   932  O  O   . ARG A 1 130 ? 21.043  8.747   9.208   1.00 22.93 ? 177 ARG A O   1 
ATOM   933  C  CB  . ARG A 1 130 ? 19.908  10.471  11.175  1.00 31.26 ? 177 ARG A CB  1 
ATOM   934  C  CG  . ARG A 1 130 ? 19.679  11.364  12.386  1.00 37.60 ? 177 ARG A CG  1 
ATOM   935  C  CD  . ARG A 1 130 ? 18.387  11.038  13.084  1.00 41.90 ? 177 ARG A CD  1 
ATOM   936  N  NE  . ARG A 1 130 ? 18.397  9.640   13.520  1.00 47.42 ? 177 ARG A NE  1 
ATOM   937  C  CZ  . ARG A 1 130 ? 17.367  9.028   14.074  1.00 44.61 ? 177 ARG A CZ  1 
ATOM   938  N  NH1 . ARG A 1 130 ? 16.270  9.707   14.349  1.00 46.88 ? 177 ARG A NH1 1 
ATOM   939  N  NH2 . ARG A 1 130 ? 17.463  7.748   14.391  1.00 42.05 ? 177 ARG A NH2 1 
ATOM   940  N  N   . SER A 1 131 ? 22.735  10.153  8.813   1.00 17.37 ? 178 SER A N   1 
ATOM   941  C  CA  . SER A 1 131 ? 23.260  9.500   7.636   1.00 17.81 ? 178 SER A CA  1 
ATOM   942  C  C   . SER A 1 131 ? 24.767  9.359   7.810   1.00 17.30 ? 178 SER A C   1 
ATOM   943  O  O   . SER A 1 131 ? 25.392  10.025  8.652   1.00 18.76 ? 178 SER A O   1 
ATOM   944  C  CB  . SER A 1 131 ? 22.925  10.263  6.378   1.00 18.64 ? 178 SER A CB  1 
ATOM   945  O  OG  . SER A 1 131 ? 21.502  10.332  6.211   1.00 19.43 ? 178 SER A OG  1 
ATOM   946  N  N   . GLY A 1 132 ? 25.353  8.455   7.052   1.00 16.67 ? 179 GLY A N   1 
ATOM   947  C  CA  . GLY A 1 132 ? 26.780  8.238   7.044   1.00 17.24 ? 179 GLY A CA  1 
ATOM   948  C  C   . GLY A 1 132 ? 27.293  7.635   8.338   1.00 17.24 ? 179 GLY A C   1 
ATOM   949  O  O   . GLY A 1 132 ? 26.569  6.955   9.045   1.00 18.25 ? 179 GLY A O   1 
ATOM   950  N  N   . GLY A 1 133 ? 28.579  7.874   8.575   1.00 17.80 ? 180 GLY A N   1 
ATOM   951  C  CA  . GLY A 1 133 ? 29.299  7.273   9.681   1.00 16.36 ? 180 GLY A CA  1 
ATOM   952  C  C   . GLY A 1 133 ? 30.574  6.593   9.234   1.00 16.06 ? 180 GLY A C   1 
ATOM   953  O  O   . GLY A 1 133 ? 30.608  5.878   8.270   1.00 17.53 ? 180 GLY A O   1 
ATOM   954  N  N   . ASP A 1 134 ? 31.631  6.738   10.042  1.00 15.52 ? 181 ASP A N   1 
ATOM   955  C  CA  . ASP A 1 134 ? 32.877  6.074   9.751   1.00 15.85 ? 181 ASP A CA  1 
ATOM   956  C  C   . ASP A 1 134 ? 32.773  4.557   9.919   1.00 13.33 ? 181 ASP A C   1 
ATOM   957  O  O   . ASP A 1 134 ? 33.504  3.818   9.273   1.00 15.56 ? 181 ASP A O   1 
ATOM   958  C  CB  . ASP A 1 134 ? 33.958  6.648   10.665  1.00 15.80 ? 181 ASP A CB  1 
ATOM   959  C  CG  . ASP A 1 134 ? 34.403  8.066   10.350  1.00 18.06 ? 181 ASP A CG  1 
ATOM   960  O  OD1 . ASP A 1 134 ? 34.250  8.482   9.179   1.00 21.58 ? 181 ASP A OD1 1 
ATOM   961  O  OD2 . ASP A 1 134 ? 34.813  8.751   11.297  1.00 20.27 ? 181 ASP A OD2 1 
ATOM   962  N  N   . LEU A 1 135 ? 31.954  4.129   10.879  1.00 14.63 ? 182 LEU A N   1 
ATOM   963  C  CA  . LEU A 1 135 ? 31.822  2.702   11.114  1.00 16.72 ? 182 LEU A CA  1 
ATOM   964  C  C   . LEU A 1 135 ? 30.471  2.451   11.745  1.00 15.07 ? 182 LEU A C   1 
ATOM   965  O  O   . LEU A 1 135 ? 29.770  3.341   12.184  1.00 15.83 ? 182 LEU A O   1 
ATOM   966  C  CB  . LEU A 1 135 ? 32.980  2.155   11.923  1.00 25.51 ? 182 LEU A CB  1 
ATOM   967  C  CG  . LEU A 1 135 ? 33.036  2.600   13.365  1.00 26.09 ? 182 LEU A CG  1 
ATOM   968  C  CD1 . LEU A 1 135 ? 32.549  1.519   14.312  1.00 30.44 ? 182 LEU A CD1 1 
ATOM   969  C  CD2 . LEU A 1 135 ? 34.455  3.017   13.677  1.00 33.59 ? 182 LEU A CD2 1 
ATOM   970  N  N   . CYS A 1 136 ? 30.077  1.183   11.714  1.00 13.41 ? 183 CYS A N   1 
ATOM   971  C  CA  . CYS A 1 136 ? 28.824  0.786   12.330  1.00 14.43 ? 183 CYS A CA  1 
ATOM   972  C  C   . CYS A 1 136 ? 29.010  -0.474  13.147  1.00 12.98 ? 183 CYS A C   1 
ATOM   973  O  O   . CYS A 1 136 ? 29.890  -1.282  12.861  1.00 13.61 ? 183 CYS A O   1 
ATOM   974  C  CB  . CYS A 1 136 ? 27.694  0.558   11.324  1.00 16.50 ? 183 CYS A CB  1 
ATOM   975  S  SG  . CYS A 1 136 ? 27.913  -0.843  10.220  1.00 16.85 ? 183 CYS A SG  1 
ATOM   976  N  N   . VAL A 1 137 ? 28.100  -0.614  14.105  1.00 13.54 ? 184 VAL A N   1 
ATOM   977  C  CA  . VAL A 1 137 ? 27.919  -1.889  14.767  1.00 12.75 ? 184 VAL A CA  1 
ATOM   978  C  C   . VAL A 1 137 ? 26.430  -2.196  14.733  1.00 12.77 ? 184 VAL A C   1 
ATOM   979  O  O   . VAL A 1 137 ? 25.606  -1.419  15.214  1.00 13.49 ? 184 VAL A O   1 
ATOM   980  C  CB  . VAL A 1 137 ? 28.513  -1.911  16.177  1.00 13.31 ? 184 VAL A CB  1 
ATOM   981  C  CG1 . VAL A 1 137 ? 28.191  -3.244  16.841  1.00 16.69 ? 184 VAL A CG1 1 
ATOM   982  C  CG2 . VAL A 1 137 ? 30.012  -1.626  16.187  1.00 16.17 ? 184 VAL A CG2 1 
ATOM   983  N  N   . GLN A 1 138 ? 26.093  -3.320  14.116  1.00 11.48 ? 185 GLN A N   1 
ATOM   984  C  CA  . GLN A 1 138 ? 24.742  -3.840  14.145  1.00 11.54 ? 185 GLN A CA  1 
ATOM   985  C  C   . GLN A 1 138 ? 24.653  -4.828  15.276  1.00 12.04 ? 185 GLN A C   1 
ATOM   986  O  O   . GLN A 1 138 ? 25.305  -5.877  15.220  1.00 12.20 ? 185 GLN A O   1 
ATOM   987  C  CB  . GLN A 1 138 ? 24.479  -4.561  12.823  1.00 11.72 ? 185 GLN A CB  1 
ATOM   988  C  CG  . GLN A 1 138 ? 23.104  -5.207  12.766  1.00 11.75 ? 185 GLN A CG  1 
ATOM   989  C  CD  . GLN A 1 138 ? 22.975  -6.087  11.557  1.00 12.65 ? 185 GLN A CD  1 
ATOM   990  O  OE1 . GLN A 1 138 ? 22.578  -5.637  10.470  1.00 14.74 ? 185 GLN A OE1 1 
ATOM   991  N  NE2 . GLN A 1 138 ? 23.317  -7.365  11.663  1.00 12.10 ? 185 GLN A NE2 1 
ATOM   992  N  N   . ALA A 1 139 ? 23.859  -4.557  16.282  1.00 11.40 ? 186 ALA A N   1 
ATOM   993  C  CA  . ALA A 1 139 ? 23.610  -5.506  17.358  1.00 12.24 ? 186 ALA A CA  1 
ATOM   994  C  C   . ALA A 1 139 ? 22.211  -6.052  17.228  1.00 11.65 ? 186 ALA A C   1 
ATOM   995  O  O   . ALA A 1 139 ? 21.232  -5.282  17.226  1.00 14.25 ? 186 ALA A O   1 
ATOM   996  C  CB  . ALA A 1 139 ? 23.786  -4.842  18.696  1.00 12.48 ? 186 ALA A CB  1 
ATOM   997  N  N   . CYS A 1 140 ? 22.076  -7.343  17.029  1.00 10.90 ? 187 CYS A N   1 
ATOM   998  C  CA  . CYS A 1 140 ? 20.807  -7.991  16.921  1.00 11.75 ? 187 CYS A CA  1 
ATOM   999  C  C   . CYS A 1 140 ? 20.696  -9.008  18.033  1.00 12.41 ? 187 CYS A C   1 
ATOM   1000 O  O   . CYS A 1 140 ? 21.667  -9.722  18.278  1.00 12.98 ? 187 CYS A O   1 
ATOM   1001 C  CB  . CYS A 1 140 ? 20.643  -8.711  15.595  1.00 11.62 ? 187 CYS A CB  1 
ATOM   1002 S  SG  . CYS A 1 140 ? 20.607  -7.601  14.160  1.00 13.46 ? 187 CYS A SG  1 
ATOM   1003 N  N   . ALA A 1 141 ? 19.531  -9.117  18.648  1.00 11.52 ? 188 ALA A N   1 
ATOM   1004 C  CA  . ALA A 1 141 ? 19.334  -10.090 19.709  1.00 11.21 ? 188 ALA A CA  1 
ATOM   1005 C  C   . ALA A 1 141 ? 17.855  -10.268 19.903  1.00 12.63 ? 188 ALA A C   1 
ATOM   1006 O  O   . ALA A 1 141 ? 17.057  -9.436  19.474  1.00 13.55 ? 188 ALA A O   1 
ATOM   1007 C  CB  . ALA A 1 141 ? 19.961  -9.661  21.010  1.00 12.48 ? 188 ALA A CB  1 
ATOM   1008 N  N   . ASP A 1 142 ? 17.467  -11.289 20.651  1.00 12.58 ? 189 ASP A N   1 
ATOM   1009 C  CA  . ASP A 1 142 ? 16.061  -11.431 20.939  1.00 13.60 ? 189 ASP A CA  1 
ATOM   1010 C  C   . ASP A 1 142 ? 15.613  -10.590 22.132  1.00 13.12 ? 189 ASP A C   1 
ATOM   1011 O  O   . ASP A 1 142 ? 14.401  -10.464 22.347  1.00 19.50 ? 189 ASP A O   1 
ATOM   1012 C  CB  . ASP A 1 142 ? 15.723  -12.882 21.126  1.00 15.21 ? 189 ASP A CB  1 
ATOM   1013 C  CG  . ASP A 1 142 ? 15.842  -13.700 19.867  1.00 16.14 ? 189 ASP A CG  1 
ATOM   1014 O  OD1 . ASP A 1 142 ? 15.582  -13.194 18.743  1.00 15.60 ? 189 ASP A OD1 1 
ATOM   1015 O  OD2 . ASP A 1 142 ? 16.208  -14.879 19.996  1.00 19.68 ? 189 ASP A OD2 1 
ATOM   1016 N  N   . ASP A 1 143 ? 16.548  -10.073 22.899  1.00 12.74 ? 190 ASP A N   1 
ATOM   1017 C  CA  . ASP A 1 143 ? 16.288  -9.321  24.096  1.00 13.25 ? 190 ASP A CA  1 
ATOM   1018 C  C   . ASP A 1 143 ? 16.839  -7.935  23.848  1.00 13.85 ? 190 ASP A C   1 
ATOM   1019 O  O   . ASP A 1 143 ? 18.047  -7.756  23.677  1.00 14.26 ? 190 ASP A O   1 
ATOM   1020 C  CB  . ASP A 1 143 ? 16.924  -10.063 25.263  1.00 14.28 ? 190 ASP A CB  1 
ATOM   1021 C  CG  . ASP A 1 143 ? 16.691  -9.407  26.613  1.00 16.15 ? 190 ASP A CG  1 
ATOM   1022 O  OD1 . ASP A 1 143 ? 16.606  -8.143  26.651  1.00 16.47 ? 190 ASP A OD1 1 
ATOM   1023 O  OD2 . ASP A 1 143 ? 16.652  -10.146 27.615  1.00 15.77 ? 190 ASP A OD2 1 
ATOM   1024 N  N   . PRO A 1 144 ? 16.003  -6.889  23.930  1.00 14.15 ? 191 PRO A N   1 
ATOM   1025 C  CA  . PRO A 1 144 ? 16.485  -5.538  23.696  1.00 14.63 ? 191 PRO A CA  1 
ATOM   1026 C  C   . PRO A 1 144 ? 17.515  -5.092  24.707  1.00 14.58 ? 191 PRO A C   1 
ATOM   1027 O  O   . PRO A 1 144 ? 18.383  -4.289  24.391  1.00 15.17 ? 191 PRO A O   1 
ATOM   1028 C  CB  . PRO A 1 144 ? 15.207  -4.685  23.730  1.00 16.62 ? 191 PRO A CB  1 
ATOM   1029 C  CG  . PRO A 1 144 ? 14.297  -5.461  24.626  1.00 16.84 ? 191 PRO A CG  1 
ATOM   1030 C  CD  . PRO A 1 144 ? 14.576  -6.924  24.316  1.00 14.96 ? 191 PRO A CD  1 
ATOM   1031 N  N   . GLN A 1 145 ? 17.447  -5.562  25.964  1.00 12.62 ? 192 GLN A N   1 
ATOM   1032 C  CA  . GLN A 1 145 ? 18.392  -5.126  26.963  1.00 13.25 ? 192 GLN A CA  1 
ATOM   1033 C  C   . GLN A 1 145 ? 19.785  -5.650  26.628  1.00 12.10 ? 192 GLN A C   1 
ATOM   1034 O  O   . GLN A 1 145 ? 20.784  -5.012  26.915  1.00 14.12 ? 192 GLN A O   1 
ATOM   1035 C  CB  . GLN A 1 145 ? 17.850  -5.546  28.320  1.00 14.55 ? 192 GLN A CB  1 
ATOM   1036 C  CG  . GLN A 1 145 ? 18.624  -4.921  29.453  1.00 16.49 ? 192 GLN A CG  1 
ATOM   1037 C  CD  . GLN A 1 145 ? 17.727  -4.638  30.619  1.00 16.90 ? 192 GLN A CD  1 
ATOM   1038 O  OE1 . GLN A 1 145 ? 16.535  -4.366  30.446  1.00 20.82 ? 192 GLN A OE1 1 
ATOM   1039 N  NE2 . GLN A 1 145 ? 18.271  -4.782  31.796  1.00 16.28 ? 192 GLN A NE2 1 
ATOM   1040 N  N   . VAL A 1 146 ? 19.844  -6.865  26.104  1.00 13.57 ? 193 VAL A N   1 
ATOM   1041 C  CA  . VAL A 1 146 ? 21.090  -7.481  25.683  1.00 12.96 ? 193 VAL A CA  1 
ATOM   1042 C  C   . VAL A 1 146 ? 21.690  -6.663  24.536  1.00 12.75 ? 193 VAL A C   1 
ATOM   1043 O  O   . VAL A 1 146 ? 22.874  -6.390  24.550  1.00 12.82 ? 193 VAL A O   1 
ATOM   1044 C  CB  . VAL A 1 146 ? 20.882  -8.945  25.289  1.00 13.60 ? 193 VAL A CB  1 
ATOM   1045 C  CG1 . VAL A 1 146 ? 22.108  -9.554  24.621  1.00 14.88 ? 193 VAL A CG1 1 
ATOM   1046 C  CG2 . VAL A 1 146 ? 20.512  -9.767  26.524  1.00 14.42 ? 193 VAL A CG2 1 
ATOM   1047 N  N   . ALA A 1 147 ? 20.877  -6.225  23.580  1.00 12.92 ? 194 ALA A N   1 
ATOM   1048 C  CA  . ALA A 1 147 ? 21.370  -5.426  22.481  1.00 12.90 ? 194 ALA A CA  1 
ATOM   1049 C  C   . ALA A 1 147 ? 21.868  -4.053  22.932  1.00 13.12 ? 194 ALA A C   1 
ATOM   1050 O  O   . ALA A 1 147 ? 22.972  -3.645  22.554  1.00 14.47 ? 194 ALA A O   1 
ATOM   1051 C  CB  . ALA A 1 147 ? 20.309  -5.297  21.414  1.00 13.92 ? 194 ALA A CB  1 
ATOM   1052 N  N   . VAL A 1 148 ? 21.105  -3.344  23.777  1.00 13.64 ? 195 VAL A N   1 
ATOM   1053 C  CA  . VAL A 1 148 ? 21.535  -2.042  24.279  1.00 15.24 ? 195 VAL A CA  1 
ATOM   1054 C  C   . VAL A 1 148 ? 22.819  -2.169  25.090  1.00 13.48 ? 195 VAL A C   1 
ATOM   1055 O  O   . VAL A 1 148 ? 23.723  -1.374  24.937  1.00 14.32 ? 195 VAL A O   1 
ATOM   1056 C  CB  . VAL A 1 148 ? 20.431  -1.329  25.091  1.00 19.93 ? 195 VAL A CB  1 
ATOM   1057 C  CG1 . VAL A 1 148 ? 20.936  -0.008  25.656  1.00 21.05 ? 195 VAL A CG1 1 
ATOM   1058 C  CG2 . VAL A 1 148 ? 19.190  -1.119  24.249  1.00 25.69 ? 195 VAL A CG2 1 
ATOM   1059 N  N   . HIS A 1 149 ? 22.913  -3.190  25.960  1.00 12.77 ? 196 HIS A N   1 
ATOM   1060 C  CA  . HIS A 1 149 ? 24.086  -3.381  26.768  1.00 13.23 ? 196 HIS A CA  1 
ATOM   1061 C  C   . HIS A 1 149 ? 25.301  -3.507  25.880  1.00 12.16 ? 196 HIS A C   1 
ATOM   1062 O  O   . HIS A 1 149 ? 26.365  -2.983  26.197  1.00 12.88 ? 196 HIS A O   1 
ATOM   1063 C  CB  . HIS A 1 149 ? 23.886  -4.645  27.602  1.00 13.86 ? 196 HIS A CB  1 
ATOM   1064 C  CG  . HIS A 1 149 ? 25.075  -5.056  28.376  1.00 13.01 ? 196 HIS A CG  1 
ATOM   1065 N  ND1 . HIS A 1 149 ? 25.870  -6.099  27.922  1.00 13.77 ? 196 HIS A ND1 1 
ATOM   1066 C  CD2 . HIS A 1 149 ? 25.590  -4.614  29.528  1.00 13.34 ? 196 HIS A CD2 1 
ATOM   1067 C  CE1 . HIS A 1 149 ? 26.828  -6.285  28.826  1.00 14.44 ? 196 HIS A CE1 1 
ATOM   1068 N  NE2 . HIS A 1 149 ? 26.681  -5.408  29.801  1.00 13.92 ? 196 HIS A NE2 1 
ATOM   1069 N  N   . ALA A 1 150 ? 25.168  -4.266  24.793  1.00 12.73 ? 197 ALA A N   1 
ATOM   1070 C  CA  . ALA A 1 150 ? 26.317  -4.484  23.915  1.00 13.03 ? 197 ALA A CA  1 
ATOM   1071 C  C   . ALA A 1 150 ? 26.796  -3.142  23.339  1.00 12.18 ? 197 ALA A C   1 
ATOM   1072 O  O   . ALA A 1 150 ? 27.953  -2.794  23.369  1.00 14.07 ? 197 ALA A O   1 
ATOM   1073 C  CB  . ALA A 1 150 ? 25.980  -5.455  22.839  1.00 12.90 ? 197 ALA A CB  1 
ATOM   1074 N  N   . ILE A 1 151 ? 25.882  -2.367  22.770  1.00 12.77 ? 198 ILE A N   1 
ATOM   1075 C  CA  . ILE A 1 151 ? 26.261  -1.094  22.165  1.00 12.73 ? 198 ILE A CA  1 
ATOM   1076 C  C   . ILE A 1 151 ? 26.803  -0.082  23.186  1.00 12.52 ? 198 ILE A C   1 
ATOM   1077 O  O   . ILE A 1 151 ? 27.833  0.561   22.964  1.00 14.23 ? 198 ILE A O   1 
ATOM   1078 C  CB  . ILE A 1 151 ? 25.050  -0.520  21.400  1.00 13.95 ? 198 ILE A CB  1 
ATOM   1079 C  CG1 . ILE A 1 151 ? 24.625  -1.364  20.212  1.00 15.98 ? 198 ILE A CG1 1 
ATOM   1080 C  CG2 . ILE A 1 151 ? 25.347  0.919   20.975  1.00 16.20 ? 198 ILE A CG2 1 
ATOM   1081 C  CD1 . ILE A 1 151 ? 25.644  -1.431  19.112  1.00 17.85 ? 198 ILE A CD1 1 
ATOM   1082 N  N   . ARG A 1 152 ? 26.187  -0.041  24.359  1.00 13.33 ? 199 ARG A N   1 
ATOM   1083 C  CA  . ARG A 1 152 ? 26.664  0.836   25.417  1.00 13.51 ? 199 ARG A CA  1 
ATOM   1084 C  C   . ARG A 1 152 ? 28.090  0.540   25.834  1.00 13.60 ? 199 ARG A C   1 
ATOM   1085 O  O   . ARG A 1 152 ? 28.925  1.418   26.057  1.00 15.12 ? 199 ARG A O   1 
ATOM   1086 C  CB  . ARG A 1 152 ? 25.672  0.702   26.548  1.00 14.25 ? 199 ARG A CB  1 
ATOM   1087 C  CG  . ARG A 1 152 ? 26.132  1.445   27.788  1.00 14.36 ? 199 ARG A CG  1 
ATOM   1088 C  CD  . ARG A 1 152 ? 25.156  1.138   28.815  1.00 16.13 ? 199 ARG A CD  1 
ATOM   1089 N  NE  . ARG A 1 152 ? 25.349  1.701   30.144  1.00 13.65 ? 199 ARG A NE  1 
ATOM   1090 C  CZ  . ARG A 1 152 ? 24.414  1.565   31.001  1.00 13.33 ? 199 ARG A CZ  1 
ATOM   1091 N  NH1 . ARG A 1 152 ? 23.314  0.899   30.695  1.00 13.94 ? 199 ARG A NH1 1 
ATOM   1092 N  NH2 . ARG A 1 152 ? 24.555  2.134   32.187  1.00 14.68 ? 199 ARG A NH2 1 
ATOM   1093 N  N   . ASN A 1 153 ? 28.383  -0.766  25.989  1.00 13.85 ? 200 ASN A N   1 
ATOM   1094 C  CA  . ASN A 1 153 ? 29.687  -1.147  26.468  1.00 14.21 ? 200 ASN A CA  1 
ATOM   1095 C  C   . ASN A 1 153 ? 30.733  -0.956  25.396  1.00 14.28 ? 200 ASN A C   1 
ATOM   1096 O  O   . ASN A 1 153 ? 31.841  -0.538  25.700  1.00 16.13 ? 200 ASN A O   1 
ATOM   1097 C  CB  . ASN A 1 153 ? 29.687  -2.545  27.058  1.00 14.32 ? 200 ASN A CB  1 
ATOM   1098 C  CG  . ASN A 1 153 ? 29.128  -2.505  28.459  1.00 15.99 ? 200 ASN A CG  1 
ATOM   1099 O  OD1 . ASN A 1 153 ? 29.875  -2.385  29.425  1.00 16.42 ? 200 ASN A OD1 1 
ATOM   1100 N  ND2 . ASN A 1 153 ? 27.826  -2.500  28.601  1.00 14.87 ? 200 ASN A ND2 1 
ATOM   1101 N  N   . LEU A 1 154 ? 30.404  -1.208  24.120  1.00 13.85 ? 201 LEU A N   1 
ATOM   1102 C  CA  . LEU A 1 154 ? 31.355  -0.902  23.070  1.00 13.10 ? 201 LEU A CA  1 
ATOM   1103 C  C   . LEU A 1 154 ? 31.632  0.602   23.028  1.00 13.77 ? 201 LEU A C   1 
ATOM   1104 O  O   . LEU A 1 154 ? 32.793  1.019   22.943  1.00 15.43 ? 201 LEU A O   1 
ATOM   1105 C  CB  . LEU A 1 154 ? 30.836  -1.458  21.746  1.00 14.68 ? 201 LEU A CB  1 
ATOM   1106 C  CG  . LEU A 1 154 ? 30.832  -2.989  21.613  1.00 16.57 ? 201 LEU A CG  1 
ATOM   1107 C  CD1 . LEU A 1 154 ? 30.217  -3.366  20.278  1.00 19.57 ? 201 LEU A CD1 1 
ATOM   1108 C  CD2 . LEU A 1 154 ? 32.170  -3.637  21.760  1.00 18.80 ? 201 LEU A CD2 1 
ATOM   1109 N  N   . ALA A 1 155 ? 30.598  1.425   23.118  1.00 15.50 ? 202 ALA A N   1 
ATOM   1110 C  CA  . ALA A 1 155 ? 30.812  2.872   23.071  1.00 15.72 ? 202 ALA A CA  1 
ATOM   1111 C  C   . ALA A 1 155 ? 31.688  3.315   24.235  1.00 16.92 ? 202 ALA A C   1 
ATOM   1112 O  O   . ALA A 1 155 ? 32.556  4.147   24.059  1.00 18.34 ? 202 ALA A O   1 
ATOM   1113 C  CB  . ALA A 1 155 ? 29.501  3.615   23.078  1.00 16.15 ? 202 ALA A CB  1 
ATOM   1114 N  N   . ARG A 1 156 ? 31.460  2.757   25.420  1.00 16.44 ? 203 ARG A N   1 
ATOM   1115 C  CA  . ARG A 1 156 ? 32.241  3.132   26.582  1.00 16.90 ? 203 ARG A CA  1 
ATOM   1116 C  C   . ARG A 1 156 ? 33.704  2.759   26.415  1.00 18.05 ? 203 ARG A C   1 
ATOM   1117 O  O   . ARG A 1 156 ? 34.579  3.574   26.690  1.00 19.39 ? 203 ARG A O   1 
ATOM   1118 C  CB  . ARG A 1 156 ? 31.589  2.442   27.772  1.00 17.55 ? 203 ARG A CB  1 
ATOM   1119 C  CG  . ARG A 1 156 ? 32.306  2.749   29.076  1.00 19.72 ? 203 ARG A CG  1 
ATOM   1120 C  CD  . ARG A 1 156 ? 31.447  2.219   30.170  1.00 20.09 ? 203 ARG A CD  1 
ATOM   1121 N  NE  . ARG A 1 156 ? 32.148  2.494   31.424  1.00 22.00 ? 203 ARG A NE  1 
ATOM   1122 C  CZ  . ARG A 1 156 ? 32.736  1.583   32.168  1.00 24.74 ? 203 ARG A CZ  1 
ATOM   1123 N  NH1 . ARG A 1 156 ? 32.555  0.301   31.925  1.00 23.73 ? 203 ARG A NH1 1 
ATOM   1124 N  NH2 . ARG A 1 156 ? 33.436  1.976   33.225  1.00 28.05 ? 203 ARG A NH2 1 
ATOM   1125 N  N   . ILE A 1 157 ? 33.991  1.544   25.936  1.00 17.44 ? 204 ILE A N   1 
ATOM   1126 C  CA  . ILE A 1 157 ? 35.352  1.108   25.668  1.00 19.33 ? 204 ILE A CA  1 
ATOM   1127 C  C   . ILE A 1 157 ? 36.017  2.050   24.675  1.00 18.66 ? 204 ILE A C   1 
ATOM   1128 O  O   . ILE A 1 157 ? 37.214  2.276   24.746  1.00 21.59 ? 204 ILE A O   1 
ATOM   1129 C  CB  . ILE A 1 157 ? 35.368  -0.342  25.158  1.00 19.40 ? 204 ILE A CB  1 
ATOM   1130 C  CG1 . ILE A 1 157 ? 35.019  -1.281  26.287  1.00 20.79 ? 204 ILE A CG1 1 
ATOM   1131 C  CG2 . ILE A 1 157 ? 36.714  -0.702  24.522  1.00 21.93 ? 204 ILE A CG2 1 
ATOM   1132 C  CD1 . ILE A 1 157 ? 34.603  -2.654  25.805  1.00 22.12 ? 204 ILE A CD1 1 
ATOM   1133 N  N   . GLY A 1 158 ? 35.237  2.558   23.722  1.00 18.50 ? 205 GLY A N   1 
ATOM   1134 C  CA  . GLY A 1 158 ? 35.743  3.391   22.646  1.00 19.80 ? 205 GLY A CA  1 
ATOM   1135 C  C   . GLY A 1 158 ? 35.886  4.870   23.008  1.00 19.36 ? 205 GLY A C   1 
ATOM   1136 O  O   . GLY A 1 158 ? 36.283  5.660   22.154  1.00 19.41 ? 205 GLY A O   1 
ATOM   1137 N  N   . PHE A 1 159 ? 35.522  5.250   24.229  1.00 20.16 ? 206 PHE A N   1 
ATOM   1138 C  CA  . PHE A 1 159 ? 35.513  6.653   24.618  1.00 24.48 ? 206 PHE A CA  1 
ATOM   1139 C  C   . PHE A 1 159 ? 36.884  7.271   24.336  1.00 23.11 ? 206 PHE A C   1 
ATOM   1140 O  O   . PHE A 1 159 ? 37.919  6.683   24.635  1.00 23.50 ? 206 PHE A O   1 
ATOM   1141 C  CB  . PHE A 1 159 ? 35.105  6.807   26.085  1.00 26.53 ? 206 PHE A CB  1 
ATOM   1142 C  CG  . PHE A 1 159 ? 35.201  8.256   26.540  1.00 34.00 ? 206 PHE A CG  1 
ATOM   1143 C  CD1 . PHE A 1 159 ? 34.161  9.150   26.304  1.00 41.56 ? 206 PHE A CD1 1 
ATOM   1144 C  CD2 . PHE A 1 159 ? 36.359  8.725   27.154  1.00 42.60 ? 206 PHE A CD2 1 
ATOM   1145 C  CE1 . PHE A 1 159 ? 34.272  10.479  26.698  1.00 45.78 ? 206 PHE A CE1 1 
ATOM   1146 C  CE2 . PHE A 1 159 ? 36.469  10.056  27.540  1.00 45.62 ? 206 PHE A CE2 1 
ATOM   1147 C  CZ  . PHE A 1 159 ? 35.424  10.927  27.315  1.00 46.42 ? 206 PHE A CZ  1 
ATOM   1148 N  N   . GLY A 1 160 ? 36.859  8.453   23.700  1.00 24.94 ? 207 GLY A N   1 
ATOM   1149 C  CA  . GLY A 1 160 ? 38.070  9.166   23.332  1.00 27.41 ? 207 GLY A CA  1 
ATOM   1150 C  C   . GLY A 1 160 ? 38.587  8.769   21.947  1.00 27.89 ? 207 GLY A C   1 
ATOM   1151 O  O   . GLY A 1 160 ? 39.421  9.489   21.403  1.00 30.90 ? 207 GLY A O   1 
ATOM   1152 N  N   . LYS A 1 161 ? 38.129  7.634   21.366  1.00 21.75 ? 208 LYS A N   1 
ATOM   1153 C  CA  . LYS A 1 161 ? 38.610  7.213   20.061  1.00 20.03 ? 208 LYS A CA  1 
ATOM   1154 C  C   . LYS A 1 161 ? 37.491  7.219   19.021  1.00 18.78 ? 208 LYS A C   1 
ATOM   1155 O  O   . LYS A 1 161 ? 37.770  7.412   17.850  1.00 20.04 ? 208 LYS A O   1 
ATOM   1156 C  CB  . LYS A 1 161 ? 39.260  5.826   20.118  1.00 21.37 ? 208 LYS A CB  1 
ATOM   1157 C  CG  . LYS A 1 161 ? 40.466  5.713   21.066  1.00 27.00 ? 208 LYS A CG  1 
ATOM   1158 C  CD  . LYS A 1 161 ? 41.001  4.292   21.075  1.00 28.58 ? 208 LYS A CD  1 
ATOM   1159 C  CE  . LYS A 1 161 ? 42.217  4.074   21.934  1.00 31.59 ? 208 LYS A CE  1 
ATOM   1160 N  NZ  . LYS A 1 161 ? 42.732  2.693   21.835  1.00 31.43 ? 208 LYS A NZ  1 
ATOM   1161 N  N   . VAL A 1 162 ? 36.249  7.013   19.472  1.00 18.80 ? 209 VAL A N   1 
ATOM   1162 C  CA  . VAL A 1 162 ? 35.086  6.997   18.590  1.00 17.71 ? 209 VAL A CA  1 
ATOM   1163 C  C   . VAL A 1 162 ? 33.973  7.674   19.349  1.00 17.84 ? 209 VAL A C   1 
ATOM   1164 O  O   . VAL A 1 162 ? 33.996  7.742   20.578  1.00 19.57 ? 209 VAL A O   1 
ATOM   1165 C  CB  . VAL A 1 162 ? 34.636  5.604   18.120  1.00 19.34 ? 209 VAL A CB  1 
ATOM   1166 C  CG1 . VAL A 1 162 ? 35.677  4.941   17.264  1.00 21.65 ? 209 VAL A CG1 1 
ATOM   1167 C  CG2 . VAL A 1 162 ? 34.226  4.714   19.267  1.00 20.50 ? 209 VAL A CG2 1 
ATOM   1168 N  N   . VAL A 1 163 ? 33.014  8.238   18.605  1.00 19.55 ? 210 VAL A N   1 
ATOM   1169 C  CA  . VAL A 1 163 ? 31.815  8.798   19.181  1.00 18.99 ? 210 VAL A CA  1 
ATOM   1170 C  C   . VAL A 1 163 ? 30.624  8.255   18.405  1.00 20.37 ? 210 VAL A C   1 
ATOM   1171 O  O   . VAL A 1 163 ? 30.745  7.998   17.224  1.00 19.22 ? 210 VAL A O   1 
ATOM   1172 C  CB  . VAL A 1 163 ? 31.830  10.346  19.112  1.00 22.36 ? 210 VAL A CB  1 
ATOM   1173 C  CG1 . VAL A 1 163 ? 32.936  10.954  19.963  1.00 28.38 ? 210 VAL A CG1 1 
ATOM   1174 C  CG2 . VAL A 1 163 ? 31.924  10.871  17.692  1.00 23.66 ? 210 VAL A CG2 1 
ATOM   1175 N  N   . VAL A 1 164 ? 29.477  8.155   19.053  1.00 20.06 ? 211 VAL A N   1 
ATOM   1176 C  CA  . VAL A 1 164 ? 28.272  7.757   18.350  1.00 20.05 ? 211 VAL A CA  1 
ATOM   1177 C  C   . VAL A 1 164 ? 27.768  8.937   17.536  1.00 20.16 ? 211 VAL A C   1 
ATOM   1178 O  O   . VAL A 1 164 ? 27.495  10.013  18.050  1.00 23.78 ? 211 VAL A O   1 
ATOM   1179 C  CB  . VAL A 1 164 ? 27.191  7.222   19.292  1.00 19.37 ? 211 VAL A CB  1 
ATOM   1180 C  CG1 . VAL A 1 164 ? 25.954  6.843   18.490  1.00 21.96 ? 211 VAL A CG1 1 
ATOM   1181 C  CG2 . VAL A 1 164 ? 27.681  6.022   20.106  1.00 23.20 ? 211 VAL A CG2 1 
ATOM   1182 N  N   . ARG A 1 165 ? 27.604  8.723   16.238  1.00 16.22 ? 212 ARG A N   1 
ATOM   1183 C  CA  . ARG A 1 165 ? 27.049  9.707   15.326  1.00 17.96 ? 212 ARG A CA  1 
ATOM   1184 C  C   . ARG A 1 165 ? 25.529  9.647   15.319  1.00 17.76 ? 212 ARG A C   1 
ATOM   1185 O  O   . ARG A 1 165 ? 24.846  10.643  15.493  1.00 19.18 ? 212 ARG A O   1 
ATOM   1186 C  CB  . ARG A 1 165 ? 27.686  9.455   13.971  1.00 18.25 ? 212 ARG A CB  1 
ATOM   1187 C  CG  . ARG A 1 165 ? 27.187  10.458  12.944  1.00 18.50 ? 212 ARG A CG  1 
ATOM   1188 C  CD  . ARG A 1 165 ? 27.666  10.053  11.579  1.00 19.40 ? 212 ARG A CD  1 
ATOM   1189 N  NE  . ARG A 1 165 ? 27.215  10.992  10.555  1.00 21.28 ? 212 ARG A NE  1 
ATOM   1190 C  CZ  . ARG A 1 165 ? 27.689  12.214  10.363  1.00 26.20 ? 212 ARG A CZ  1 
ATOM   1191 N  NH1 . ARG A 1 165 ? 28.828  12.564  10.934  1.00 27.05 ? 212 ARG A NH1 1 
ATOM   1192 N  NH2 . ARG A 1 165 ? 27.094  13.033  9.502   1.00 27.42 ? 212 ARG A NH2 1 
ATOM   1193 N  N   . TRP A 1 166 ? 24.984  8.451   15.134  1.00 16.82 ? 213 TRP A N   1 
ATOM   1194 C  CA  . TRP A 1 166 ? 23.549  8.242   15.175  1.00 15.77 ? 213 TRP A CA  1 
ATOM   1195 C  C   . TRP A 1 166 ? 23.250  6.793   15.500  1.00 16.34 ? 213 TRP A C   1 
ATOM   1196 O  O   . TRP A 1 166 ? 24.102  5.929   15.366  1.00 15.69 ? 213 TRP A O   1 
ATOM   1197 C  CB  . TRP A 1 166 ? 22.855  8.661   13.870  1.00 15.64 ? 213 TRP A CB  1 
ATOM   1198 C  CG  . TRP A 1 166 ? 23.300  7.966   12.616  1.00 15.06 ? 213 TRP A CG  1 
ATOM   1199 C  CD1 . TRP A 1 166 ? 24.245  8.377   11.737  1.00 15.35 ? 213 TRP A CD1 1 
ATOM   1200 C  CD2 . TRP A 1 166 ? 22.817  6.710   12.093  1.00 16.40 ? 213 TRP A CD2 1 
ATOM   1201 N  NE1 . TRP A 1 166 ? 24.390  7.493   10.715  1.00 16.06 ? 213 TRP A NE1 1 
ATOM   1202 C  CE2 . TRP A 1 166 ? 23.513  6.454   10.902  1.00 17.11 ? 213 TRP A CE2 1 
ATOM   1203 C  CE3 . TRP A 1 166 ? 21.865  5.780   12.527  1.00 17.29 ? 213 TRP A CE3 1 
ATOM   1204 C  CZ2 . TRP A 1 166 ? 23.300  5.305   10.149  1.00 16.92 ? 213 TRP A CZ2 1 
ATOM   1205 C  CZ3 . TRP A 1 166 ? 21.668  4.641   11.784  1.00 18.83 ? 213 TRP A CZ3 1 
ATOM   1206 C  CH2 . TRP A 1 166 ? 22.355  4.423   10.599  1.00 17.91 ? 213 TRP A CH2 1 
ATOM   1207 N  N   . SER A 1 167 ? 22.069  6.545   16.035  1.00 14.69 ? 214 SER A N   1 
ATOM   1208 C  CA  . SER A 1 167 ? 21.657  5.180   16.290  1.00 15.06 ? 214 SER A CA  1 
ATOM   1209 C  C   . SER A 1 167 ? 20.204  4.992   15.891  1.00 16.84 ? 214 SER A C   1 
ATOM   1210 O  O   . SER A 1 167 ? 19.460  5.959   15.670  1.00 17.90 ? 214 SER A O   1 
ATOM   1211 C  CB  . SER A 1 167 ? 21.923  4.770   17.679  1.00 20.60 ? 214 SER A CB  1 
ATOM   1212 O  OG  . SER A 1 167 ? 21.123  5.479   18.574  1.00 23.36 ? 214 SER A OG  1 
ATOM   1213 N  N   . GLN A 1 168 ? 19.825  3.726   15.745  1.00 14.71 ? 215 GLN A N   1 
ATOM   1214 C  CA  . GLN A 1 168 ? 18.455  3.365   15.428  1.00 15.26 ? 215 GLN A CA  1 
ATOM   1215 C  C   . GLN A 1 168 ? 18.128  2.068   16.145  1.00 13.90 ? 215 GLN A C   1 
ATOM   1216 O  O   . GLN A 1 168 ? 18.846  1.061   16.010  1.00 15.83 ? 215 GLN A O   1 
ATOM   1217 C  CB  . GLN A 1 168 ? 18.307  3.148   13.924  1.00 16.96 ? 215 GLN A CB  1 
ATOM   1218 C  CG  . GLN A 1 168 ? 16.873  2.806   13.509  1.00 17.27 ? 215 GLN A CG  1 
ATOM   1219 C  CD  . GLN A 1 168 ? 15.868  3.917   13.748  1.00 18.01 ? 215 GLN A CD  1 
ATOM   1220 O  OE1 . GLN A 1 168 ? 16.042  5.018   13.197  1.00 21.63 ? 215 GLN A OE1 1 
ATOM   1221 N  NE2 . GLN A 1 168 ? 14.912  3.756   14.643  1.00 18.89 ? 215 GLN A NE2 1 
ATOM   1222 N  N   . LEU A 1 169 ? 17.065  2.063   16.886  1.00 13.24 ? 216 LEU A N   1 
ATOM   1223 C  CA  . LEU A 1 169 ? 16.504  0.866   17.463  1.00 15.13 ? 216 LEU A CA  1 
ATOM   1224 C  C   . LEU A 1 169 ? 15.375  0.350   16.601  1.00 14.64 ? 216 LEU A C   1 
ATOM   1225 O  O   . LEU A 1 169 ? 14.585  1.130   16.054  1.00 15.05 ? 216 LEU A O   1 
ATOM   1226 C  CB  . LEU A 1 169 ? 16.052  1.059   18.894  1.00 17.57 ? 216 LEU A CB  1 
ATOM   1227 C  CG  . LEU A 1 169 ? 17.225  1.170   19.877  1.00 20.34 ? 216 LEU A CG  1 
ATOM   1228 C  CD1 . LEU A 1 169 ? 17.711  2.610   19.962  1.00 21.92 ? 216 LEU A CD1 1 
ATOM   1229 C  CD2 . LEU A 1 169 ? 16.877  0.641   21.231  1.00 24.34 ? 216 LEU A CD2 1 
ATOM   1230 N  N   . GLY A 1 170 ? 15.319  -0.956  16.479  1.00 12.28 ? 217 GLY A N   1 
ATOM   1231 C  CA  . GLY A 1 170 ? 14.267  -1.618  15.758  1.00 11.91 ? 217 GLY A CA  1 
ATOM   1232 C  C   . GLY A 1 170 ? 13.498  -2.531  16.689  1.00 12.74 ? 217 GLY A C   1 
ATOM   1233 O  O   . GLY A 1 170 ? 14.093  -3.396  17.345  1.00 13.94 ? 217 GLY A O   1 
ATOM   1234 N  N   . PHE A 1 171 ? 12.191  -2.321  16.874  1.00 11.81 ? 218 PHE A N   1 
ATOM   1235 C  CA  . PHE A 1 171 ? 11.447  -3.028  17.897  1.00 11.92 ? 218 PHE A CA  1 
ATOM   1236 C  C   . PHE A 1 171 ? 11.040  -4.408  17.438  1.00 12.80 ? 218 PHE A C   1 
ATOM   1237 O  O   . PHE A 1 171 ? 10.755  -5.259  18.300  1.00 15.17 ? 218 PHE A O   1 
ATOM   1238 C  CB  . PHE A 1 171 ? 10.233  -2.249  18.403  1.00 12.61 ? 218 PHE A CB  1 
ATOM   1239 C  CG  . PHE A 1 171 ? 9.126   -2.100  17.394  1.00 12.31 ? 218 PHE A CG  1 
ATOM   1240 C  CD1 . PHE A 1 171 ? 8.256   -3.133  17.167  1.00 14.23 ? 218 PHE A CD1 1 
ATOM   1241 C  CD2 . PHE A 1 171 ? 8.956   -0.925  16.709  1.00 13.67 ? 218 PHE A CD2 1 
ATOM   1242 C  CE1 . PHE A 1 171 ? 7.221   -2.991  16.238  1.00 15.05 ? 218 PHE A CE1 1 
ATOM   1243 C  CE2 . PHE A 1 171 ? 7.918   -0.781  15.812  1.00 13.87 ? 218 PHE A CE2 1 
ATOM   1244 C  CZ  . PHE A 1 171 ? 7.063   -1.801  15.573  1.00 14.67 ? 218 PHE A CZ  1 
ATOM   1245 N  N   . GLY A 1 172 ? 11.012  -4.664  16.143  1.00 11.69 ? 219 GLY A N   1 
ATOM   1246 C  CA  . GLY A 1 172 ? 10.551  -5.909  15.590  1.00 13.49 ? 219 GLY A CA  1 
ATOM   1247 C  C   . GLY A 1 172 ? 11.112  -6.073  14.194  1.00 13.54 ? 219 GLY A C   1 
ATOM   1248 O  O   . GLY A 1 172 ? 11.316  -5.106  13.484  1.00 13.40 ? 219 GLY A O   1 
ATOM   1249 N  N   . LYS A 1 173 ? 11.342  -7.313  13.823  1.00 13.17 ? 220 LYS A N   1 
ATOM   1250 C  CA  . LYS A 1 173 ? 11.962  -7.606  12.549  1.00 12.70 ? 220 LYS A CA  1 
ATOM   1251 C  C   . LYS A 1 173 ? 10.931  -7.507  11.426  1.00 12.16 ? 220 LYS A C   1 
ATOM   1252 O  O   . LYS A 1 173 ? 9.726   -7.785  11.584  1.00 13.34 ? 220 LYS A O   1 
ATOM   1253 C  CB  . LYS A 1 173 ? 12.576  -9.009  12.554  1.00 13.63 ? 220 LYS A CB  1 
ATOM   1254 C  CG  . LYS A 1 173 ? 11.612  -10.134 12.720  1.00 15.43 ? 220 LYS A CG  1 
ATOM   1255 C  CD  . LYS A 1 173 ? 12.298  -11.477 12.997  1.00 16.95 ? 220 LYS A CD  1 
ATOM   1256 C  CE  . LYS A 1 173 ? 11.321  -12.542 13.334  1.00 19.26 ? 220 LYS A CE  1 
ATOM   1257 N  NZ  . LYS A 1 173 ? 12.060  -13.809 13.292  1.00 24.12 ? 220 LYS A NZ  1 
ATOM   1258 N  N   . THR A 1 174 ? 11.415  -7.213  10.241  1.00 11.28 ? 221 THR A N   1 
ATOM   1259 C  CA  . THR A 1 174 ? 10.580  -7.212  9.064   1.00 12.23 ? 221 THR A CA  1 
ATOM   1260 C  C   . THR A 1 174 ? 11.336  -7.906  7.951   1.00 12.19 ? 221 THR A C   1 
ATOM   1261 O  O   . THR A 1 174 ? 11.329  -7.459  6.807   1.00 13.44 ? 221 THR A O   1 
ATOM   1262 C  CB  . THR A 1 174 ? 10.200  -5.777  8.690   1.00 14.65 ? 221 THR A CB  1 
ATOM   1263 O  OG1 . THR A 1 174 ? 9.086   -5.896  7.821   1.00 22.50 ? 221 THR A OG1 1 
ATOM   1264 C  CG2 . THR A 1 174 ? 11.390  -4.974  8.263   1.00 12.53 ? 221 THR A CG2 1 
ATOM   1265 N  N   . SER A 1 175 ? 11.985  -9.008  8.304   1.00 11.29 ? 222 SER A N   1 
ATOM   1266 C  CA  . SER A 1 175 ? 12.848  -9.716  7.374   1.00 10.87 ? 222 SER A CA  1 
ATOM   1267 C  C   . SER A 1 175 ? 12.933  -11.153 7.813   1.00 10.77 ? 222 SER A C   1 
ATOM   1268 O  O   . SER A 1 175 ? 12.631  -11.489 8.949   1.00 11.47 ? 222 SER A O   1 
ATOM   1269 C  CB  . SER A 1 175 ? 14.165  -9.035  7.307   1.00 11.22 ? 222 SER A CB  1 
ATOM   1270 O  OG  . SER A 1 175 ? 14.759  -8.876  8.578   1.00 12.35 ? 222 SER A OG  1 
ATOM   1271 N  N   . SER A 1 176 ? 13.407  -11.986 6.903   1.00 11.22 ? 223 SER A N   1 
ATOM   1272 C  CA  . SER A 1 176 ? 13.532  -13.427 7.156   1.00 12.14 ? 223 SER A CA  1 
ATOM   1273 C  C   . SER A 1 176 ? 14.700  -14.007 6.385   1.00 11.80 ? 223 SER A C   1 
ATOM   1274 O  O   . SER A 1 176 ? 14.790  -13.792 5.177   1.00 12.94 ? 223 SER A O   1 
ATOM   1275 C  CB  . SER A 1 176 ? 12.299  -14.135 6.762   1.00 12.68 ? 223 SER A CB  1 
ATOM   1276 O  OG  . SER A 1 176 ? 12.500  -15.552 6.947   1.00 14.33 ? 223 SER A OG  1 
ATOM   1277 N  N   . THR A 1 177 ? 15.533  -14.803 7.067   1.00 11.90 ? 224 THR A N   1 
ATOM   1278 C  CA  . THR A 1 177 ? 16.540  -15.649 6.423   1.00 12.06 ? 224 THR A CA  1 
ATOM   1279 C  C   . THR A 1 177 ? 16.178  -17.109 6.693   1.00 13.93 ? 224 THR A C   1 
ATOM   1280 O  O   . THR A 1 177 ? 17.038  -17.961 6.516   1.00 14.70 ? 224 THR A O   1 
ATOM   1281 C  CB  . THR A 1 177 ? 17.944  -15.308 6.920   1.00 12.59 ? 224 THR A CB  1 
ATOM   1282 O  OG1 . THR A 1 177 ? 17.940  -15.450 8.329   1.00 13.86 ? 224 THR A OG1 1 
ATOM   1283 C  CG2 . THR A 1 177 ? 18.332  -13.898 6.531   1.00 13.21 ? 224 THR A CG2 1 
ATOM   1284 N  N   . THR A 1 178 ? 14.946  -17.382 7.112   1.00 13.04 ? 225 THR A N   1 
ATOM   1285 C  CA  . THR A 1 178 ? 14.511  -18.722 7.522   1.00 13.81 ? 225 THR A CA  1 
ATOM   1286 C  C   . THR A 1 178 ? 13.113  -18.928 6.936   1.00 15.59 ? 225 THR A C   1 
ATOM   1287 O  O   . THR A 1 178 ? 12.120  -18.695 7.601   1.00 16.08 ? 225 THR A O   1 
ATOM   1288 C  CB  . THR A 1 178 ? 14.523  -18.899 9.035   1.00 15.01 ? 225 THR A CB  1 
ATOM   1289 O  OG1 . THR A 1 178 ? 13.679  -17.873 9.562   1.00 15.42 ? 225 THR A OG1 1 
ATOM   1290 C  CG2 . THR A 1 178 ? 15.934  -18.823 9.594   1.00 17.66 ? 225 THR A CG2 1 
ATOM   1291 N  N   . PRO A 1 179 ? 13.024  -19.445 5.703   1.00 16.87 ? 226 PRO A N   1 
ATOM   1292 C  CA  . PRO A 1 179 ? 11.743  -19.641 5.019   1.00 18.67 ? 226 PRO A CA  1 
ATOM   1293 C  C   . PRO A 1 179 ? 10.880  -20.730 5.650   1.00 20.33 ? 226 PRO A C   1 
ATOM   1294 O  O   . PRO A 1 179 ? 9.670   -20.736 5.398   1.00 23.83 ? 226 PRO A O   1 
ATOM   1295 C  CB  . PRO A 1 179 ? 12.142  -19.936 3.564   1.00 21.01 ? 226 PRO A CB  1 
ATOM   1296 C  CG  . PRO A 1 179 ? 13.560  -20.398 3.643   1.00 21.49 ? 226 PRO A CG  1 
ATOM   1297 C  CD  . PRO A 1 179 ? 14.181  -19.697 4.825   1.00 18.35 ? 226 PRO A CD  1 
ATOM   1298 N  N   . ASP A 1 180 ? 11.447  -21.532 6.548   1.00 20.31 ? 227 ASP A N   1 
ATOM   1299 C  CA  . ASP A 1 180 ? 10.710  -22.562 7.268   1.00 24.05 ? 227 ASP A CA  1 
ATOM   1300 C  C   . ASP A 1 180 ? 9.903   -21.986 8.437   1.00 24.82 ? 227 ASP A C   1 
ATOM   1301 O  O   . ASP A 1 180 ? 9.094   -22.690 9.047   1.00 26.49 ? 227 ASP A O   1 
ATOM   1302 C  CB  . ASP A 1 180 ? 11.665  -23.645 7.744   1.00 24.88 ? 227 ASP A CB  1 
ATOM   1303 C  CG  . ASP A 1 180 ? 12.772  -23.114 8.644   1.00 31.79 ? 227 ASP A CG  1 
ATOM   1304 O  OD1 . ASP A 1 180 ? 13.515  -22.207 8.171   1.00 34.05 ? 227 ASP A OD1 1 
ATOM   1305 O  OD2 . ASP A 1 180 ? 12.894  -23.595 9.797   1.00 41.29 ? 227 ASP A OD2 1 
ATOM   1306 N  N   . LYS A 1 181 ? 10.112  -20.709 8.789   1.00 19.26 ? 228 LYS A N   1 
ATOM   1307 C  CA  . LYS A 1 181 ? 9.436   -20.065 9.890   1.00 19.55 ? 228 LYS A CA  1 
ATOM   1308 C  C   . LYS A 1 181 ? 8.534   -18.973 9.316   1.00 17.32 ? 228 LYS A C   1 
ATOM   1309 O  O   . LYS A 1 181 ? 8.657   -18.596 8.147   1.00 16.57 ? 228 LYS A O   1 
ATOM   1310 C  CB  . LYS A 1 181 ? 10.496  -19.432 10.790  1.00 22.85 ? 228 LYS A CB  1 
ATOM   1311 C  CG  . LYS A 1 181 ? 10.026  -18.846 12.101  1.00 36.11 ? 228 LYS A CG  1 
ATOM   1312 C  CD  . LYS A 1 181 ? 9.603   -19.869 13.154  1.00 42.80 ? 228 LYS A CD  1 
ATOM   1313 C  CE  . LYS A 1 181 ? 8.295   -19.512 13.798  1.00 45.82 ? 228 LYS A CE  1 
ATOM   1314 N  NZ  . LYS A 1 181 ? 7.178   -19.749 12.878  1.00 41.14 ? 228 LYS A NZ  1 
ATOM   1315 N  N   . GLN A 1 182 ? 7.599   -18.523 10.137  1.00 16.97 ? 229 GLN A N   1 
ATOM   1316 C  CA  . GLN A 1 182 ? 6.607   -17.534 9.741   1.00 16.51 ? 229 GLN A CA  1 
ATOM   1317 C  C   . GLN A 1 182 ? 7.298   -16.246 9.326   1.00 13.62 ? 229 GLN A C   1 
ATOM   1318 O  O   . GLN A 1 182 ? 8.214   -15.748 9.974   1.00 15.38 ? 229 GLN A O   1 
ATOM   1319 C  CB  . GLN A 1 182 ? 5.713   -17.233 10.934  1.00 21.84 ? 229 GLN A CB  1 
ATOM   1320 C  CG  . GLN A 1 182 ? 4.561   -16.284 10.634  1.00 27.50 ? 229 GLN A CG  1 
ATOM   1321 C  CD  . GLN A 1 182 ? 3.555   -16.164 11.764  1.00 36.32 ? 229 GLN A CD  1 
ATOM   1322 O  OE1 . GLN A 1 182 ? 3.377   -15.098 12.371  1.00 43.26 ? 229 GLN A OE1 1 
ATOM   1323 N  NE2 . GLN A 1 182 ? 2.895   -17.273 12.064  1.00 42.40 ? 229 GLN A NE2 1 
ATOM   1324 N  N   . THR A 1 183 ? 6.837   -15.706 8.214   1.00 12.35 ? 230 THR A N   1 
ATOM   1325 C  CA  . THR A 1 183 ? 7.336   -14.440 7.715   1.00 11.67 ? 230 THR A CA  1 
ATOM   1326 C  C   . THR A 1 183 ? 6.717   -13.296 8.506   1.00 11.59 ? 230 THR A C   1 
ATOM   1327 O  O   . THR A 1 183 ? 5.507   -13.260 8.659   1.00 13.90 ? 230 THR A O   1 
ATOM   1328 C  CB  . THR A 1 183 ? 6.989   -14.307 6.254   1.00 12.96 ? 230 THR A CB  1 
ATOM   1329 O  OG1 . THR A 1 183 ? 7.484   -15.476 5.602   1.00 13.94 ? 230 THR A OG1 1 
ATOM   1330 C  CG2 . THR A 1 183 ? 7.646   -13.092 5.651   1.00 14.14 ? 230 THR A CG2 1 
ATOM   1331 N  N   . PRO A 1 184 ? 7.528   -12.388 9.057   1.00 11.42 ? 231 PRO A N   1 
ATOM   1332 C  CA  . PRO A 1 184 ? 6.971   -11.291 9.829   1.00 10.94 ? 231 PRO A CA  1 
ATOM   1333 C  C   . PRO A 1 184 ? 6.331   -10.245 8.958   1.00 11.46 ? 231 PRO A C   1 
ATOM   1334 O  O   . PRO A 1 184 ? 6.582   -10.172 7.757   1.00 13.43 ? 231 PRO A O   1 
ATOM   1335 C  CB  . PRO A 1 184 ? 8.189   -10.735 10.531  1.00 12.56 ? 231 PRO A CB  1 
ATOM   1336 C  CG  . PRO A 1 184 ? 9.313   -10.970 9.568   1.00 13.65 ? 231 PRO A CG  1 
ATOM   1337 C  CD  . PRO A 1 184 ? 8.981   -12.308 8.955   1.00 11.60 ? 231 PRO A CD  1 
ATOM   1338 N  N   . ARG A 1 185 ? 5.492   -9.419  9.543   1.00 10.45 ? 232 ARG A N   1 
ATOM   1339 C  CA  . ARG A 1 185 ? 4.827   -8.306  8.897   1.00 10.15 ? 232 ARG A CA  1 
ATOM   1340 C  C   . ARG A 1 185 ? 5.431   -6.979  9.275   1.00 10.89 ? 232 ARG A C   1 
ATOM   1341 O  O   . ARG A 1 185 ? 5.808   -6.734  10.408  1.00 12.04 ? 232 ARG A O   1 
ATOM   1342 C  CB  . ARG A 1 185 ? 3.337   -8.312  9.220   1.00 11.56 ? 232 ARG A CB  1 
ATOM   1343 C  CG  . ARG A 1 185 ? 2.653   -9.544  8.656   1.00 12.46 ? 232 ARG A CG  1 
ATOM   1344 C  CD  . ARG A 1 185 ? 1.182   -9.541  8.949   1.00 13.70 ? 232 ARG A CD  1 
ATOM   1345 N  NE  . ARG A 1 185 ? 0.589   -10.798 8.495   1.00 13.85 ? 232 ARG A NE  1 
ATOM   1346 C  CZ  . ARG A 1 185 ? -0.101  -10.979 7.401   1.00 13.68 ? 232 ARG A CZ  1 
ATOM   1347 N  NH1 . ARG A 1 185 ? -0.288  -10.004 6.557   1.00 14.65 ? 232 ARG A NH1 1 
ATOM   1348 N  NH2 . ARG A 1 185 ? -0.586  -12.176 7.130   1.00 15.19 ? 232 ARG A NH2 1 
ATOM   1349 N  N   . ASN A 1 186 ? 5.464   -6.089  8.302   1.00 10.36 ? 233 ASN A N   1 
ATOM   1350 C  CA  . ASN A 1 186 ? 5.839   -4.696  8.516   1.00 10.61 ? 233 ASN A CA  1 
ATOM   1351 C  C   . ASN A 1 186 ? 4.610   -3.910  8.992   1.00 10.91 ? 233 ASN A C   1 
ATOM   1352 O  O   . ASN A 1 186 ? 3.525   -4.469  9.095   1.00 10.75 ? 233 ASN A O   1 
ATOM   1353 C  CB  . ASN A 1 186 ? 6.517   -4.114  7.277   1.00 11.94 ? 233 ASN A CB  1 
ATOM   1354 C  CG  . ASN A 1 186 ? 5.620   -4.165  6.072   1.00 11.68 ? 233 ASN A CG  1 
ATOM   1355 O  OD1 . ASN A 1 186 ? 4.417   -3.885  6.141   1.00 12.52 ? 233 ASN A OD1 1 
ATOM   1356 N  ND2 . ASN A 1 186 ? 6.171   -4.562  4.927   1.00 12.67 ? 233 ASN A ND2 1 
ATOM   1357 N  N   . LEU A 1 187 ? 4.790   -2.608  9.261   1.00 10.95 ? 234 LEU A N   1 
ATOM   1358 C  CA  . LEU A 1 187 ? 3.716   -1.789  9.810   1.00 11.21 ? 234 LEU A CA  1 
ATOM   1359 C  C   . LEU A 1 187 ? 2.695   -1.390  8.763   1.00 11.41 ? 234 LEU A C   1 
ATOM   1360 O  O   . LEU A 1 187 ? 1.662   -0.849  9.135   1.00 13.56 ? 234 LEU A O   1 
ATOM   1361 C  CB  . LEU A 1 187 ? 4.272   -0.558  10.517  1.00 11.59 ? 234 LEU A CB  1 
ATOM   1362 C  CG  . LEU A 1 187 ? 5.017   -0.889  11.808  1.00 13.61 ? 234 LEU A CG  1 
ATOM   1363 C  CD1 . LEU A 1 187 ? 5.662   0.362   12.341  1.00 15.35 ? 234 LEU A CD1 1 
ATOM   1364 C  CD2 . LEU A 1 187 ? 4.083   -1.515  12.789  1.00 16.72 ? 234 LEU A CD2 1 
ATOM   1365 N  N   . LEU A 1 188 ? 2.877   -1.728  7.509   1.00 10.34 ? 235 LEU A N   1 
ATOM   1366 C  CA  . LEU A 1 188 ? 1.816   -1.617  6.519   1.00 10.98 ? 235 LEU A CA  1 
ATOM   1367 C  C   . LEU A 1 188 ? 0.907   -2.839  6.553   1.00 11.88 ? 235 LEU A C   1 
ATOM   1368 O  O   . LEU A 1 188 ? -0.082  -2.895  5.826   1.00 13.77 ? 235 LEU A O   1 
ATOM   1369 C  CB  . LEU A 1 188 ? 2.385   -1.386  5.139   1.00 11.56 ? 235 LEU A CB  1 
ATOM   1370 C  CG  . LEU A 1 188 ? 3.242   -0.156  4.991   1.00 13.08 ? 235 LEU A CG  1 
ATOM   1371 C  CD1 . LEU A 1 188 ? 3.601   0.043   3.521   1.00 15.12 ? 235 LEU A CD1 1 
ATOM   1372 C  CD2 . LEU A 1 188 ? 2.578   1.091   5.536   1.00 14.44 ? 235 LEU A CD2 1 
ATOM   1373 N  N   . GLY A 1 189 ? 1.249   -3.873  7.317   1.00 11.08 ? 236 GLY A N   1 
ATOM   1374 C  CA  . GLY A 1 189 ? 0.459   -5.044  7.494   1.00 10.79 ? 236 GLY A CA  1 
ATOM   1375 C  C   . GLY A 1 189 ? 0.745   -6.173  6.527   1.00 11.57 ? 236 GLY A C   1 
ATOM   1376 O  O   . GLY A 1 189 ? -0.002  -7.128  6.557   1.00 13.22 ? 236 GLY A O   1 
ATOM   1377 N  N   . PHE A 1 190 ? 1.775   -6.068  5.712   1.00 10.44 ? 237 PHE A N   1 
ATOM   1378 C  CA  . PHE A 1 190 ? 2.117   -7.117  4.753   1.00 10.52 ? 237 PHE A CA  1 
ATOM   1379 C  C   . PHE A 1 190 ? 3.308   -7.884  5.271   1.00 10.55 ? 237 PHE A C   1 
ATOM   1380 O  O   . PHE A 1 190 ? 4.224   -7.344  5.869   1.00 11.53 ? 237 PHE A O   1 
ATOM   1381 C  CB  . PHE A 1 190 ? 2.493   -6.472  3.424   1.00 10.81 ? 237 PHE A CB  1 
ATOM   1382 C  CG  . PHE A 1 190 ? 1.290   -6.120  2.589   1.00 11.55 ? 237 PHE A CG  1 
ATOM   1383 C  CD1 . PHE A 1 190 ? 0.500   -5.010  2.853   1.00 11.94 ? 237 PHE A CD1 1 
ATOM   1384 C  CD2 . PHE A 1 190 ? 0.903   -6.927  1.526   1.00 12.74 ? 237 PHE A CD2 1 
ATOM   1385 C  CE1 . PHE A 1 190 ? -0.614  -4.742  2.088   1.00 12.86 ? 237 PHE A CE1 1 
ATOM   1386 C  CE2 . PHE A 1 190 ? -0.218  -6.639  0.767   1.00 13.46 ? 237 PHE A CE2 1 
ATOM   1387 C  CZ  . PHE A 1 190 ? -0.974  -5.568  1.050   1.00 13.45 ? 237 PHE A CZ  1 
ATOM   1388 N  N   . LYS A 1 191 ? 3.306   -9.178  4.959   1.00 10.29 ? 238 LYS A N   1 
ATOM   1389 C  CA  . LYS A 1 191 ? 4.460   -10.037 5.167   1.00 10.05 ? 238 LYS A CA  1 
ATOM   1390 C  C   . LYS A 1 191 ? 5.636   -9.476  4.390   1.00 10.21 ? 238 LYS A C   1 
ATOM   1391 O  O   . LYS A 1 191 ? 5.471   -9.073  3.233   1.00 11.78 ? 238 LYS A O   1 
ATOM   1392 C  CB  . LYS A 1 191 ? 4.197   -11.466 4.682   1.00 11.10 ? 238 LYS A CB  1 
ATOM   1393 C  CG  . LYS A 1 191 ? 3.142   -12.185 5.481   1.00 12.29 ? 238 LYS A CG  1 
ATOM   1394 C  CD  . LYS A 1 191 ? 2.886   -13.583 4.893   1.00 12.70 ? 238 LYS A CD  1 
ATOM   1395 C  CE  . LYS A 1 191 ? 1.905   -14.363 5.705   1.00 14.77 ? 238 LYS A CE  1 
ATOM   1396 N  NZ  . LYS A 1 191 ? 1.579   -15.652 5.056   1.00 15.25 ? 238 LYS A NZ  1 
ATOM   1397 N  N   . ASP A 1 192 ? 6.813   -9.480  4.983   1.00 10.73 ? 239 ASP A N   1 
ATOM   1398 C  CA  . ASP A 1 192 ? 8.004   -8.874  4.414   1.00 10.70 ? 239 ASP A CA  1 
ATOM   1399 C  C   . ASP A 1 192 ? 9.134   -9.852  4.686   1.00 10.99 ? 239 ASP A C   1 
ATOM   1400 O  O   . ASP A 1 192 ? 9.512   -10.050 5.831   1.00 11.88 ? 239 ASP A O   1 
ATOM   1401 C  CB  . ASP A 1 192 ? 8.237   -7.492  5.017   1.00 11.12 ? 239 ASP A CB  1 
ATOM   1402 C  CG  . ASP A 1 192 ? 9.089   -6.535  4.228   1.00 13.42 ? 239 ASP A CG  1 
ATOM   1403 O  OD1 . ASP A 1 192 ? 9.786   -6.920  3.301   1.00 12.05 ? 239 ASP A OD1 1 
ATOM   1404 O  OD2 . ASP A 1 192 ? 8.938   -5.336  4.517   1.00 13.71 ? 239 ASP A OD2 1 
ATOM   1405 N  N   . GLY A 1 193 ? 9.663   -10.445 3.609   1.00 11.71 ? 240 GLY A N   1 
ATOM   1406 C  CA  . GLY A 1 193 ? 10.755  -11.387 3.702   1.00 12.17 ? 240 GLY A CA  1 
ATOM   1407 C  C   . GLY A 1 193 ? 10.499  -12.702 2.983   1.00 12.12 ? 240 GLY A C   1 
ATOM   1408 O  O   . GLY A 1 193 ? 11.382  -13.549 3.016   1.00 14.40 ? 240 GLY A O   1 
ATOM   1409 N  N   . THR A 1 194 ? 9.374   -12.882 2.310   1.00 10.74 ? 241 THR A N   1 
ATOM   1410 C  CA  . THR A 1 194 ? 9.070   -14.154 1.680   1.00 11.16 ? 241 THR A CA  1 
ATOM   1411 C  C   . THR A 1 194 ? 10.167  -14.558 0.706   1.00 12.17 ? 241 THR A C   1 
ATOM   1412 O  O   . THR A 1 194 ? 10.663  -15.692 0.768   1.00 13.04 ? 241 THR A O   1 
ATOM   1413 C  CB  . THR A 1 194 ? 7.728   -14.033 0.968   1.00 11.99 ? 241 THR A CB  1 
ATOM   1414 O  OG1 . THR A 1 194 ? 6.760   -13.649 1.930   1.00 12.57 ? 241 THR A OG1 1 
ATOM   1415 C  CG2 . THR A 1 194 ? 7.343   -15.315 0.265   1.00 12.49 ? 241 THR A CG2 1 
ATOM   1416 N  N   . ARG A 1 195 ? 10.514  -13.697 -0.254  1.00 11.75 ? 242 ARG A N   1 
ATOM   1417 C  CA  . ARG A 1 195 ? 11.495  -14.031 -1.263  1.00 11.79 ? 242 ARG A CA  1 
ATOM   1418 C  C   . ARG A 1 195 ? 12.782  -13.288 -0.980  1.00 12.33 ? 242 ARG A C   1 
ATOM   1419 O  O   . ARG A 1 195 ? 13.044  -12.234 -1.529  1.00 13.83 ? 242 ARG A O   1 
ATOM   1420 C  CB  . ARG A 1 195 ? 10.967  -13.753 -2.663  1.00 13.12 ? 242 ARG A CB  1 
ATOM   1421 C  CG  . ARG A 1 195 ? 10.121  -14.899 -3.220  1.00 13.50 ? 242 ARG A CG  1 
ATOM   1422 C  CD  . ARG A 1 195 ? 9.526   -14.664 -4.585  1.00 13.79 ? 242 ARG A CD  1 
ATOM   1423 N  NE  . ARG A 1 195 ? 10.501  -14.076 -5.494  1.00 14.09 ? 242 ARG A NE  1 
ATOM   1424 C  CZ  . ARG A 1 195 ? 11.585  -14.657 -5.947  1.00 15.06 ? 242 ARG A CZ  1 
ATOM   1425 N  NH1 . ARG A 1 195 ? 12.525  -13.903 -6.418  1.00 15.69 ? 242 ARG A NH1 1 
ATOM   1426 N  NH2 . ARG A 1 195 ? 11.722  -15.976 -5.900  1.00 17.80 ? 242 ARG A NH2 1 
ATOM   1427 N  N   . ASN A 1 196 ? 13.546  -13.842 -0.043  1.00 13.19 ? 243 ASN A N   1 
ATOM   1428 C  CA  . ASN A 1 196 ? 14.821  -13.320 0.386   1.00 13.42 ? 243 ASN A CA  1 
ATOM   1429 C  C   . ASN A 1 196 ? 15.892  -14.333 -0.005  1.00 16.59 ? 243 ASN A C   1 
ATOM   1430 O  O   . ASN A 1 196 ? 15.837  -14.904 -1.110  1.00 22.48 ? 243 ASN A O   1 
ATOM   1431 C  CB  . ASN A 1 196 ? 14.696  -12.881 1.836   1.00 12.56 ? 243 ASN A CB  1 
ATOM   1432 C  CG  . ASN A 1 196 ? 15.803  -11.960 2.244   1.00 12.68 ? 243 ASN A CG  1 
ATOM   1433 O  OD1 . ASN A 1 196 ? 16.241  -11.104 1.476   1.00 13.53 ? 243 ASN A OD1 1 
ATOM   1434 N  ND2 . ASN A 1 196 ? 16.272  -12.069 3.454   1.00 12.67 ? 243 ASN A ND2 1 
ATOM   1435 N  N   . ILE A 1 197 ? 16.996  -14.334 0.665   1.00 15.64 ? 244 ILE A N   1 
ATOM   1436 C  CA  . ILE A 1 197 ? 18.003  -15.388 0.595   1.00 15.82 ? 244 ILE A CA  1 
ATOM   1437 C  C   . ILE A 1 197 ? 18.023  -16.057 1.946   1.00 16.90 ? 244 ILE A C   1 
ATOM   1438 O  O   . ILE A 1 197 ? 18.004  -15.350 2.969   1.00 18.53 ? 244 ILE A O   1 
ATOM   1439 C  CB  . ILE A 1 197 ? 19.366  -14.820 0.198   1.00 17.11 ? 244 ILE A CB  1 
ATOM   1440 C  CG1 . ILE A 1 197 ? 19.318  -14.154 -1.150  1.00 17.63 ? 244 ILE A CG1 1 
ATOM   1441 C  CG2 . ILE A 1 197 ? 20.413  -15.933 0.233   1.00 19.67 ? 244 ILE A CG2 1 
ATOM   1442 C  CD1 . ILE A 1 197 ? 20.600  -13.441 -1.551  1.00 19.34 ? 244 ILE A CD1 1 
ATOM   1443 N  N   . ALA A 1 198 ? 17.921  -17.382 1.974   1.00 17.12 ? 245 ALA A N   1 
ATOM   1444 C  CA  . ALA A 1 198 ? 17.939  -18.142 3.203   1.00 17.64 ? 245 ALA A CA  1 
ATOM   1445 C  C   . ALA A 1 198 ? 19.372  -18.425 3.622   1.00 18.26 ? 245 ALA A C   1 
ATOM   1446 O  O   . ALA A 1 198 ? 20.248  -18.558 2.783   1.00 19.01 ? 245 ALA A O   1 
ATOM   1447 C  CB  . ALA A 1 198 ? 17.173  -19.413 3.032   1.00 18.35 ? 245 ALA A CB  1 
ATOM   1448 N  N   . GLY A 1 199 ? 19.597  -18.522 4.923   1.00 18.11 ? 246 GLY A N   1 
ATOM   1449 C  CA  . GLY A 1 199 ? 20.913  -18.820 5.474   1.00 19.35 ? 246 GLY A CA  1 
ATOM   1450 C  C   . GLY A 1 199 ? 21.435  -20.195 5.051   1.00 23.11 ? 246 GLY A C   1 
ATOM   1451 O  O   . GLY A 1 199 ? 22.637  -20.437 5.092   1.00 26.41 ? 246 GLY A O   1 
ATOM   1452 N  N   . THR A 1 200 ? 20.550  -21.076 4.592   1.00 21.19 ? 247 THR A N   1 
ATOM   1453 C  CA  . THR A 1 200 ? 20.955  -22.413 4.169   1.00 25.49 ? 247 THR A CA  1 
ATOM   1454 C  C   . THR A 1 200 ? 21.377  -22.383 2.706   1.00 25.19 ? 247 THR A C   1 
ATOM   1455 O  O   . THR A 1 200 ? 21.900  -23.393 2.241   1.00 27.37 ? 247 THR A O   1 
ATOM   1456 C  CB  . THR A 1 200 ? 19.827  -23.433 4.379   1.00 26.25 ? 247 THR A CB  1 
ATOM   1457 O  OG1 . THR A 1 200 ? 18.614  -22.873 3.881   1.00 29.51 ? 247 THR A OG1 1 
ATOM   1458 C  CG2 . THR A 1 200 ? 19.651  -23.820 5.838   1.00 32.49 ? 247 THR A CG2 1 
ATOM   1459 N  N   . GLU A 1 201 ? 21.084  -21.300 1.961   1.00 21.30 ? 248 GLU A N   1 
ATOM   1460 C  CA  . GLU A 1 201 ? 21.301  -21.277 0.521   1.00 19.70 ? 248 GLU A CA  1 
ATOM   1461 C  C   . GLU A 1 201 ? 22.729  -20.840 0.238   1.00 20.82 ? 248 GLU A C   1 
ATOM   1462 O  O   . GLU A 1 201 ? 22.972  -19.722 -0.195  1.00 21.20 ? 248 GLU A O   1 
ATOM   1463 C  CB  . GLU A 1 201 ? 20.260  -20.378 -0.150  1.00 19.97 ? 248 GLU A CB  1 
ATOM   1464 C  CG  . GLU A 1 201 ? 18.852  -20.957 -0.092  1.00 20.63 ? 248 GLU A CG  1 
ATOM   1465 C  CD  . GLU A 1 201 ? 17.730  -20.084 -0.609  1.00 23.94 ? 248 GLU A CD  1 
ATOM   1466 O  OE1 . GLU A 1 201 ? 17.802  -18.868 -0.479  1.00 20.10 ? 248 GLU A OE1 1 
ATOM   1467 O  OE2 . GLU A 1 201 ? 16.745  -20.639 -1.143  1.00 32.23 ? 248 GLU A OE2 1 
ATOM   1468 N  N   . LYS A 1 202 ? 23.691  -21.747 0.458   1.00 20.36 ? 249 LYS A N   1 
ATOM   1469 C  CA  . LYS A 1 202 ? 25.094  -21.397 0.428   1.00 25.16 ? 249 LYS A CA  1 
ATOM   1470 C  C   . LYS A 1 202 ? 25.459  -20.906 -0.970  1.00 21.21 ? 249 LYS A C   1 
ATOM   1471 O  O   . LYS A 1 202 ? 26.202  -19.945 -1.104  1.00 21.66 ? 249 LYS A O   1 
ATOM   1472 C  CB  . LYS A 1 202 ? 25.952  -22.553 0.975   1.00 31.22 ? 249 LYS A CB  1 
ATOM   1473 C  CG  . LYS A 1 202 ? 26.093  -22.566 2.516   1.00 41.24 ? 249 LYS A CG  1 
ATOM   1474 C  CD  . LYS A 1 202 ? 26.352  -21.176 3.107   1.00 48.18 ? 249 LYS A CD  1 
ATOM   1475 C  CE  . LYS A 1 202 ? 27.138  -21.057 4.391   1.00 54.17 ? 249 LYS A CE  1 
ATOM   1476 N  NZ  . LYS A 1 202 ? 27.554  -19.659 4.612   1.00 57.11 ? 249 LYS A NZ  1 
ATOM   1477 N  N   . ASP A 1 203 ? 24.898  -21.503 -2.019  1.00 22.27 ? 250 ASP A N   1 
ATOM   1478 C  CA  . ASP A 1 203 ? 25.270  -21.095 -3.363  1.00 23.81 ? 250 ASP A CA  1 
ATOM   1479 C  C   . ASP A 1 203 ? 24.805  -19.669 -3.647  1.00 20.11 ? 250 ASP A C   1 
ATOM   1480 O  O   . ASP A 1 203 ? 25.525  -18.872 -4.217  1.00 21.30 ? 250 ASP A O   1 
ATOM   1481 C  CB  . ASP A 1 203 ? 24.799  -22.092 -4.414  1.00 30.19 ? 250 ASP A CB  1 
ATOM   1482 C  CG  . ASP A 1 203 ? 25.593  -23.393 -4.479  1.00 40.09 ? 250 ASP A CG  1 
ATOM   1483 O  OD1 . ASP A 1 203 ? 26.433  -23.634 -3.575  1.00 44.79 ? 250 ASP A OD1 1 
ATOM   1484 O  OD2 . ASP A 1 203 ? 25.385  -24.153 -5.447  1.00 49.04 ? 250 ASP A OD2 1 
ATOM   1485 N  N   . ARG A 1 204 ? 23.586  -19.322 -3.211  1.00 18.96 ? 251 ARG A N   1 
ATOM   1486 C  CA  . ARG A 1 204 ? 23.066  -17.982 -3.428  1.00 18.33 ? 251 ARG A CA  1 
ATOM   1487 C  C   . ARG A 1 204 ? 23.790  -16.927 -2.580  1.00 15.74 ? 251 ARG A C   1 
ATOM   1488 O  O   . ARG A 1 204 ? 23.991  -15.803 -3.027  1.00 16.68 ? 251 ARG A O   1 
ATOM   1489 C  CB  . ARG A 1 204 ? 21.551  -17.941 -3.139  1.00 19.06 ? 251 ARG A CB  1 
ATOM   1490 C  CG  . ARG A 1 204 ? 20.725  -18.936 -3.956  1.00 21.64 ? 251 ARG A CG  1 
ATOM   1491 C  CD  . ARG A 1 204 ? 19.231  -18.832 -3.692  1.00 23.78 ? 251 ARG A CD  1 
ATOM   1492 N  NE  . ARG A 1 204 ? 18.653  -17.621 -4.274  1.00 24.56 ? 251 ARG A NE  1 
ATOM   1493 C  CZ  . ARG A 1 204 ? 17.676  -16.841 -3.815  1.00 22.00 ? 251 ARG A CZ  1 
ATOM   1494 N  NH1 . ARG A 1 204 ? 17.123  -17.021 -2.623  1.00 21.94 ? 251 ARG A NH1 1 
ATOM   1495 N  NH2 . ARG A 1 204 ? 17.255  -15.855 -4.570  1.00 23.52 ? 251 ARG A NH2 1 
ATOM   1496 N  N   . LEU A 1 205 ? 24.205  -17.325 -1.387  1.00 15.77 ? 252 LEU A N   1 
ATOM   1497 C  CA  . LEU A 1 205 ? 25.009  -16.456 -0.558  1.00 16.25 ? 252 LEU A CA  1 
ATOM   1498 C  C   . LEU A 1 205 ? 26.328  -16.155 -1.243  1.00 16.28 ? 252 LEU A C   1 
ATOM   1499 O  O   . LEU A 1 205 ? 26.753  -15.016 -1.306  1.00 16.11 ? 252 LEU A O   1 
ATOM   1500 C  CB  . LEU A 1 205 ? 25.220  -17.018 0.840   1.00 17.08 ? 252 LEU A CB  1 
ATOM   1501 C  CG  . LEU A 1 205 ? 23.954  -17.074 1.699   1.00 17.19 ? 252 LEU A CG  1 
ATOM   1502 C  CD1 . LEU A 1 205 ? 24.159  -17.997 2.889   1.00 19.17 ? 252 LEU A CD1 1 
ATOM   1503 C  CD2 . LEU A 1 205 ? 23.505  -15.672 2.100   1.00 18.08 ? 252 LEU A CD2 1 
ATOM   1504 N  N   . ASP A 1 206 ? 26.992  -17.207 -1.753  1.00 17.21 ? 253 ASP A N   1 
ATOM   1505 C  CA  . ASP A 1 206 ? 28.248  -16.989 -2.461  1.00 19.38 ? 253 ASP A CA  1 
ATOM   1506 C  C   . ASP A 1 206 ? 28.053  -16.121 -3.705  1.00 19.50 ? 253 ASP A C   1 
ATOM   1507 O  O   . ASP A 1 206 ? 28.903  -15.295 -4.010  1.00 21.79 ? 253 ASP A O   1 
ATOM   1508 C  CB  . ASP A 1 206 ? 28.910  -18.327 -2.781  1.00 20.31 ? 253 ASP A CB  1 
ATOM   1509 C  CG  . ASP A 1 206 ? 29.547  -19.031 -1.590  1.00 24.72 ? 253 ASP A CG  1 
ATOM   1510 O  OD1 . ASP A 1 206 ? 29.821  -18.386 -0.573  1.00 28.25 ? 253 ASP A OD1 1 
ATOM   1511 O  OD2 . ASP A 1 206 ? 29.737  -20.256 -1.664  1.00 31.32 ? 253 ASP A OD2 1 
ATOM   1512 N  N   . ARG A 1 207 ? 26.951  -16.283 -4.434  1.00 17.23 ? 254 ARG A N   1 
ATOM   1513 C  CA  . ARG A 1 207 ? 26.733  -15.533 -5.648  1.00 18.55 ? 254 ARG A CA  1 
ATOM   1514 C  C   . ARG A 1 207 ? 26.399  -14.071 -5.364  1.00 16.92 ? 254 ARG A C   1 
ATOM   1515 O  O   . ARG A 1 207 ? 26.847  -13.168 -6.063  1.00 18.25 ? 254 ARG A O   1 
ATOM   1516 C  CB  . ARG A 1 207 ? 25.633  -16.249 -6.432  1.00 22.46 ? 254 ARG A CB  1 
ATOM   1517 C  CG  . ARG A 1 207 ? 25.326  -15.570 -7.757  1.00 30.01 ? 254 ARG A CG  1 
ATOM   1518 C  CD  . ARG A 1 207 ? 24.454  -16.465 -8.638  1.00 37.07 ? 254 ARG A CD  1 
ATOM   1519 N  NE  . ARG A 1 207 ? 24.174  -15.796 -9.916  1.00 47.48 ? 254 ARG A NE  1 
ATOM   1520 C  CZ  . ARG A 1 207 ? 23.213  -16.123 -10.787 1.00 52.58 ? 254 ARG A CZ  1 
ATOM   1521 N  NH1 . ARG A 1 207 ? 22.391  -17.133 -10.544 1.00 56.56 ? 254 ARG A NH1 1 
ATOM   1522 N  NH2 . ARG A 1 207 ? 23.076  -15.434 -11.904 1.00 54.74 ? 254 ARG A NH2 1 
ATOM   1523 N  N   . PHE A 1 208 ? 25.538  -13.810 -4.349  1.00 16.16 ? 255 PHE A N   1 
ATOM   1524 C  CA  . PHE A 1 208 ? 24.917  -12.505 -4.211  1.00 15.10 ? 255 PHE A CA  1 
ATOM   1525 C  C   . PHE A 1 208 ? 25.304  -11.710 -2.961  1.00 14.71 ? 255 PHE A C   1 
ATOM   1526 O  O   . PHE A 1 208 ? 24.998  -10.528 -2.904  1.00 15.97 ? 255 PHE A O   1 
ATOM   1527 C  CB  . PHE A 1 208 ? 23.416  -12.712 -4.150  1.00 16.02 ? 255 PHE A CB  1 
ATOM   1528 C  CG  . PHE A 1 208 ? 22.841  -13.256 -5.443  1.00 18.02 ? 255 PHE A CG  1 
ATOM   1529 C  CD1 . PHE A 1 208 ? 22.958  -12.521 -6.605  1.00 18.30 ? 255 PHE A CD1 1 
ATOM   1530 C  CD2 . PHE A 1 208 ? 22.170  -14.461 -5.474  1.00 19.77 ? 255 PHE A CD2 1 
ATOM   1531 C  CE1 . PHE A 1 208 ? 22.394  -13.023 -7.785  1.00 20.54 ? 255 PHE A CE1 1 
ATOM   1532 C  CE2 . PHE A 1 208 ? 21.622  -14.947 -6.658  1.00 22.36 ? 255 PHE A CE2 1 
ATOM   1533 C  CZ  . PHE A 1 208 ? 21.742  -14.222 -7.784  1.00 21.96 ? 255 PHE A CZ  1 
ATOM   1534 N  N   . VAL A 1 209 ? 25.937  -12.352 -1.976  1.00 13.84 ? 256 VAL A N   1 
ATOM   1535 C  CA  . VAL A 1 209 ? 26.151  -11.699 -0.690  1.00 14.50 ? 256 VAL A CA  1 
ATOM   1536 C  C   . VAL A 1 209 ? 27.621  -11.549 -0.344  1.00 13.99 ? 256 VAL A C   1 
ATOM   1537 O  O   . VAL A 1 209 ? 28.023  -10.476 0.071   1.00 15.60 ? 256 VAL A O   1 
ATOM   1538 C  CB  . VAL A 1 209 ? 25.344  -12.439 0.389   1.00 14.85 ? 256 VAL A CB  1 
ATOM   1539 C  CG1 . VAL A 1 209 ? 25.643  -11.904 1.770   1.00 16.31 ? 256 VAL A CG1 1 
ATOM   1540 C  CG2 . VAL A 1 209 ? 23.862  -12.357 0.025   1.00 15.69 ? 256 VAL A CG2 1 
ATOM   1541 N  N   . TRP A 1 210 ? 28.429  -12.628 -0.424  1.00 14.97 ? 257 TRP A N   1 
ATOM   1542 C  CA  . TRP A 1 210 ? 29.805  -12.563 0.043   1.00 14.80 ? 257 TRP A CA  1 
ATOM   1543 C  C   . TRP A 1 210 ? 30.722  -12.018 -1.046  1.00 17.42 ? 257 TRP A C   1 
ATOM   1544 O  O   . TRP A 1 210 ? 30.658  -12.474 -2.173  1.00 19.34 ? 257 TRP A O   1 
ATOM   1545 C  CB  . TRP A 1 210 ? 30.260  -13.952 0.496   1.00 16.22 ? 257 TRP A CB  1 
ATOM   1546 C  CG  . TRP A 1 210 ? 29.400  -14.595 1.541   1.00 15.69 ? 257 TRP A CG  1 
ATOM   1547 C  CD1 . TRP A 1 210 ? 28.918  -15.855 1.491   1.00 17.27 ? 257 TRP A CD1 1 
ATOM   1548 C  CD2 . TRP A 1 210 ? 28.987  -14.040 2.799   1.00 15.83 ? 257 TRP A CD2 1 
ATOM   1549 N  NE1 . TRP A 1 210 ? 28.190  -16.126 2.614   1.00 18.74 ? 257 TRP A NE1 1 
ATOM   1550 C  CE2 . TRP A 1 210 ? 28.222  -15.040 3.431   1.00 16.00 ? 257 TRP A CE2 1 
ATOM   1551 C  CE3 . TRP A 1 210 ? 29.192  -12.838 3.440   1.00 16.68 ? 257 TRP A CE3 1 
ATOM   1552 C  CZ2 . TRP A 1 210 ? 27.673  -14.850 4.691   1.00 18.10 ? 257 TRP A CZ2 1 
ATOM   1553 C  CZ3 . TRP A 1 210 ? 28.675  -12.677 4.703   1.00 17.28 ? 257 TRP A CZ3 1 
ATOM   1554 C  CH2 . TRP A 1 210 ? 27.899  -13.646 5.289   1.00 17.36 ? 257 TRP A CH2 1 
ATOM   1555 N  N   . ALA A 1 211 ? 31.620  -11.118 -0.683  1.00 16.78 ? 258 ALA A N   1 
ATOM   1556 C  CA  . ALA A 1 211 ? 32.714  -10.705 -1.556  1.00 18.80 ? 258 ALA A CA  1 
ATOM   1557 C  C   . ALA A 1 211 ? 33.731  -11.837 -1.762  1.00 19.71 ? 258 ALA A C   1 
ATOM   1558 O  O   . ALA A 1 211 ? 34.063  -12.598 -0.854  1.00 19.91 ? 258 ALA A O   1 
ATOM   1559 C  CB  . ALA A 1 211 ? 33.336  -9.463  -0.968  1.00 19.26 ? 258 ALA A CB  1 
ATOM   1560 N  N   . ALA A 1 212 ? 34.170  -11.977 -3.027  1.00 21.82 ? 259 ALA A N   1 
ATOM   1561 C  CA  . ALA A 1 212 ? 35.126  -13.000 -3.418  1.00 24.60 ? 259 ALA A CA  1 
ATOM   1562 C  C   . ALA A 1 212 ? 36.460  -12.321 -3.706  1.00 23.70 ? 259 ALA A C   1 
ATOM   1563 O  O   . ALA A 1 212 ? 36.490  -11.141 -3.998  1.00 23.71 ? 259 ALA A O   1 
ATOM   1564 C  CB  . ALA A 1 212 ? 34.616  -13.725 -4.628  1.00 26.51 ? 259 ALA A CB  1 
ATOM   1565 N  N   . GLU A 1 213 ? 37.568  -13.079 -3.622  1.00 26.82 ? 260 GLU A N   1 
ATOM   1566 C  CA  . GLU A 1 213 ? 38.878  -12.482 -3.823  1.00 30.08 ? 260 GLU A CA  1 
ATOM   1567 C  C   . GLU A 1 213 ? 38.976  -11.838 -5.207  1.00 26.97 ? 260 GLU A C   1 
ATOM   1568 O  O   . GLU A 1 213 ? 39.474  -10.717 -5.339  1.00 28.00 ? 260 GLU A O   1 
ATOM   1569 C  CB  . GLU A 1 213 ? 40.010  -13.494 -3.663  1.00 33.50 ? 260 GLU A CB  1 
ATOM   1570 C  CG  . GLU A 1 213 ? 41.365  -12.862 -3.973  1.00 38.24 ? 260 GLU A CG  1 
ATOM   1571 C  CD  . GLU A 1 213 ? 42.549  -13.525 -3.304  1.00 45.50 ? 260 GLU A CD  1 
ATOM   1572 O  OE1 . GLU A 1 213 ? 42.498  -14.762 -3.145  1.00 48.84 ? 260 GLU A OE1 1 
ATOM   1573 O  OE2 . GLU A 1 213 ? 43.511  -12.803 -2.956  1.00 50.50 ? 260 GLU A OE2 1 
ATOM   1574 N  N   . LYS A 1 214 ? 38.405  -12.516 -6.195  1.00 31.40 ? 261 LYS A N   1 
ATOM   1575 C  CA  . LYS A 1 214 ? 38.497  -12.064 -7.573  1.00 33.07 ? 261 LYS A CA  1 
ATOM   1576 C  C   . LYS A 1 214 ? 37.713  -10.773 -7.796  1.00 29.00 ? 261 LYS A C   1 
ATOM   1577 O  O   . LYS A 1 214 ? 37.844  -10.164 -8.846  1.00 26.26 ? 261 LYS A O   1 
ATOM   1578 C  CB  . LYS A 1 214 ? 38.030  -13.140 -8.558  1.00 38.57 ? 261 LYS A CB  1 
ATOM   1579 C  CG  . LYS A 1 214 ? 36.545  -13.481 -8.524  1.00 45.82 ? 261 LYS A CG  1 
ATOM   1580 C  CD  . LYS A 1 214 ? 36.219  -14.914 -8.940  1.00 55.25 ? 261 LYS A CD  1 
ATOM   1581 C  CE  . LYS A 1 214 ? 36.049  -15.108 -10.418 1.00 60.87 ? 261 LYS A CE  1 
ATOM   1582 N  NZ  . LYS A 1 214 ? 34.831  -14.458 -10.917 1.00 64.84 ? 261 LYS A NZ  1 
ATOM   1583 N  N   . ASP A 1 215 ? 36.887  -10.317 -6.826  1.00 24.23 ? 262 ASP A N   1 
ATOM   1584 C  CA  . ASP A 1 215 ? 36.132  -9.096  -7.044  1.00 23.10 ? 262 ASP A CA  1 
ATOM   1585 C  C   . ASP A 1 215 ? 37.020  -7.854  -7.009  1.00 23.09 ? 262 ASP A C   1 
ATOM   1586 O  O   . ASP A 1 215 ? 36.586  -6.779  -7.407  1.00 29.27 ? 262 ASP A O   1 
ATOM   1587 C  CB  . ASP A 1 215 ? 34.991  -8.944  -6.040  1.00 21.83 ? 262 ASP A CB  1 
ATOM   1588 C  CG  . ASP A 1 215 ? 33.938  -10.043 -6.132  1.00 23.75 ? 262 ASP A CG  1 
ATOM   1589 O  OD1 . ASP A 1 215 ? 33.916  -10.798 -7.129  1.00 23.36 ? 262 ASP A OD1 1 
ATOM   1590 O  OD2 . ASP A 1 215 ? 33.141  -10.220 -5.167  1.00 19.96 ? 262 ASP A OD2 1 
ATOM   1591 N  N   . GLY A 1 216 ? 38.255  -7.983  -6.521  1.00 24.52 ? 263 GLY A N   1 
ATOM   1592 C  CA  . GLY A 1 216 ? 39.220  -6.916  -6.717  1.00 24.32 ? 263 GLY A CA  1 
ATOM   1593 C  C   . GLY A 1 216 ? 39.752  -6.327  -5.421  1.00 25.79 ? 263 GLY A C   1 
ATOM   1594 O  O   . GLY A 1 216 ? 40.612  -5.454  -5.482  1.00 27.98 ? 263 GLY A O   1 
ATOM   1595 N  N   . THR A 1 217 ? 39.214  -6.736  -4.259  1.00 24.58 ? 264 THR A N   1 
ATOM   1596 C  CA  . THR A 1 217 ? 39.663  -6.172  -2.998  1.00 23.55 ? 264 THR A CA  1 
ATOM   1597 C  C   . THR A 1 217 ? 39.952  -7.318  -2.035  1.00 25.50 ? 264 THR A C   1 
ATOM   1598 O  O   . THR A 1 217 ? 39.051  -7.794  -1.331  1.00 22.08 ? 264 THR A O   1 
ATOM   1599 C  CB  . THR A 1 217 ? 38.620  -5.215  -2.414  1.00 25.20 ? 264 THR A CB  1 
ATOM   1600 O  OG1 . THR A 1 217 ? 38.298  -4.169  -3.337  1.00 26.82 ? 264 THR A OG1 1 
ATOM   1601 C  CG2 . THR A 1 217 ? 39.121  -4.540  -1.156  1.00 25.91 ? 264 THR A CG2 1 
ATOM   1602 N  N   . PRO A 1 218 ? 41.193  -7.851  -1.979  1.00 22.56 ? 265 PRO A N   1 
ATOM   1603 C  CA  . PRO A 1 218 ? 41.450  -9.078  -1.245  1.00 23.22 ? 265 PRO A CA  1 
ATOM   1604 C  C   . PRO A 1 218 ? 41.083  -9.013  0.234   1.00 21.00 ? 265 PRO A C   1 
ATOM   1605 O  O   . PRO A 1 218 ? 40.630  -10.021 0.739   1.00 22.25 ? 265 PRO A O   1 
ATOM   1606 C  CB  . PRO A 1 218 ? 42.964  -9.315  -1.501  1.00 27.80 ? 265 PRO A CB  1 
ATOM   1607 C  CG  . PRO A 1 218 ? 43.152  -8.731  -2.885  1.00 30.61 ? 265 PRO A CG  1 
ATOM   1608 C  CD  . PRO A 1 218 ? 42.351  -7.440  -2.810  1.00 27.19 ? 265 PRO A CD  1 
ATOM   1609 N  N   . TRP A 1 219 ? 41.246  -7.855  0.876   1.00 20.24 ? 266 TRP A N   1 
ATOM   1610 C  CA  . TRP A 1 219 ? 40.998  -7.789  2.311   1.00 19.65 ? 266 TRP A CA  1 
ATOM   1611 C  C   . TRP A 1 219 ? 39.521  -8.006  2.601   1.00 20.09 ? 266 TRP A C   1 
ATOM   1612 O  O   . TRP A 1 219 ? 39.162  -8.337  3.717   1.00 20.47 ? 266 TRP A O   1 
ATOM   1613 C  CB  . TRP A 1 219 ? 41.462  -6.494  2.983   1.00 19.11 ? 266 TRP A CB  1 
ATOM   1614 C  CG  . TRP A 1 219 ? 40.732  -5.230  2.640   1.00 20.77 ? 266 TRP A CG  1 
ATOM   1615 C  CD1 . TRP A 1 219 ? 41.070  -4.304  1.696   1.00 19.90 ? 266 TRP A CD1 1 
ATOM   1616 C  CD2 . TRP A 1 219 ? 39.584  -4.691  3.319   1.00 20.07 ? 266 TRP A CD2 1 
ATOM   1617 N  NE1 . TRP A 1 219 ? 40.183  -3.264  1.719   1.00 21.84 ? 266 TRP A NE1 1 
ATOM   1618 C  CE2 . TRP A 1 219 ? 39.256  -3.464  2.712   1.00 20.26 ? 266 TRP A CE2 1 
ATOM   1619 C  CE3 . TRP A 1 219 ? 38.802  -5.127  4.393   1.00 20.99 ? 266 TRP A CE3 1 
ATOM   1620 C  CZ2 . TRP A 1 219 ? 38.197  -2.680  3.123   1.00 21.25 ? 266 TRP A CZ2 1 
ATOM   1621 C  CZ3 . TRP A 1 219 ? 37.756  -4.335  4.806   1.00 20.32 ? 266 TRP A CZ3 1 
ATOM   1622 C  CH2 . TRP A 1 219 ? 37.444  -3.137  4.182   1.00 21.85 ? 266 TRP A CH2 1 
ATOM   1623 N  N   . MET A 1 220 ? 38.652  -7.792  1.610   1.00 17.46 ? 267 MET A N   1 
ATOM   1624 C  CA  . MET A 1 220 ? 37.225  -7.944  1.828   1.00 17.12 ? 267 MET A CA  1 
ATOM   1625 C  C   . MET A 1 220 ? 36.714  -9.343  1.537   1.00 18.00 ? 267 MET A C   1 
ATOM   1626 O  O   . MET A 1 220 ? 35.526  -9.553  1.662   1.00 17.38 ? 267 MET A O   1 
ATOM   1627 C  CB  . MET A 1 220 ? 36.466  -6.961  0.942   1.00 17.73 ? 267 MET A CB  1 
ATOM   1628 C  CG  . MET A 1 220 ? 36.226  -5.643  1.622   1.00 16.73 ? 267 MET A CG  1 
ATOM   1629 S  SD  . MET A 1 220 ? 35.161  -5.759  3.082   1.00 18.53 ? 267 MET A SD  1 
ATOM   1630 C  CE  . MET A 1 220 ? 33.612  -6.166  2.274   1.00 19.15 ? 267 MET A CE  1 
ATOM   1631 N  N   . THR A 1 221 ? 37.552  -10.296 1.125   1.00 19.20 ? 268 THR A N   1 
ATOM   1632 C  CA  . THR A 1 221 ? 37.120  -11.644 0.822   1.00 18.57 ? 268 THR A CA  1 
ATOM   1633 C  C   . THR A 1 221 ? 36.402  -12.245 2.021   1.00 18.09 ? 268 THR A C   1 
ATOM   1634 O  O   . THR A 1 221 ? 36.969  -12.361 3.093   1.00 20.51 ? 268 THR A O   1 
ATOM   1635 C  CB  . THR A 1 221 ? 38.278  -12.575 0.447   1.00 20.56 ? 268 THR A CB  1 
ATOM   1636 O  OG1 . THR A 1 221 ? 38.895  -11.979 -0.697  1.00 23.14 ? 268 THR A OG1 1 
ATOM   1637 C  CG2 . THR A 1 221 ? 37.791  -13.974 0.099   1.00 21.48 ? 268 THR A CG2 1 
ATOM   1638 N  N   . GLY A 1 222 ? 35.162  -12.651 1.804   1.00 17.47 ? 269 GLY A N   1 
ATOM   1639 C  CA  . GLY A 1 222 ? 34.351  -13.228 2.865   1.00 16.49 ? 269 GLY A CA  1 
ATOM   1640 C  C   . GLY A 1 222 ? 33.506  -12.180 3.592   1.00 15.47 ? 269 GLY A C   1 
ATOM   1641 O  O   . GLY A 1 222 ? 32.723  -12.526 4.456   1.00 15.96 ? 269 GLY A O   1 
ATOM   1642 N  N   . GLY A 1 223 ? 33.691  -10.910 3.278   1.00 14.17 ? 270 GLY A N   1 
ATOM   1643 C  CA  . GLY A 1 223 ? 32.865  -9.837  3.811   1.00 14.16 ? 270 GLY A CA  1 
ATOM   1644 C  C   . GLY A 1 223 ? 31.667  -9.587  2.898   1.00 14.29 ? 270 GLY A C   1 
ATOM   1645 O  O   . GLY A 1 223 ? 31.349  -10.356 2.018   1.00 16.13 ? 270 GLY A O   1 
ATOM   1646 N  N   . SER A 1 224 ? 30.949  -8.508  3.181   1.00 13.68 ? 271 SER A N   1 
ATOM   1647 C  CA  . SER A 1 224 ? 29.775  -8.123  2.411   1.00 13.91 ? 271 SER A CA  1 
ATOM   1648 C  C   . SER A 1 224 ? 29.670  -6.615  2.455   1.00 13.55 ? 271 SER A C   1 
ATOM   1649 O  O   . SER A 1 224 ? 30.458  -5.960  3.125   1.00 15.32 ? 271 SER A O   1 
ATOM   1650 C  CB  . SER A 1 224 ? 28.555  -8.775  2.981   1.00 13.77 ? 271 SER A CB  1 
ATOM   1651 O  OG  . SER A 1 224 ? 27.437  -8.645  2.120   1.00 14.56 ? 271 SER A OG  1 
ATOM   1652 N  N   . TYR A 1 225 ? 28.689  -6.064  1.754   1.00 13.09 ? 272 TYR A N   1 
ATOM   1653 C  CA  . TYR A 1 225 ? 28.476  -4.639  1.743   1.00 12.77 ? 272 TYR A CA  1 
ATOM   1654 C  C   . TYR A 1 225 ? 27.049  -4.373  2.192   1.00 13.46 ? 272 TYR A C   1 
ATOM   1655 O  O   . TYR A 1 225 ? 26.123  -5.090  1.797   1.00 13.76 ? 272 TYR A O   1 
ATOM   1656 C  CB  . TYR A 1 225 ? 28.671  -4.001  0.365   1.00 13.87 ? 272 TYR A CB  1 
ATOM   1657 C  CG  . TYR A 1 225 ? 30.110  -4.173  -0.072  1.00 13.39 ? 272 TYR A CG  1 
ATOM   1658 C  CD1 . TYR A 1 225 ? 30.511  -5.319  -0.733  1.00 15.15 ? 272 TYR A CD1 1 
ATOM   1659 C  CD2 . TYR A 1 225 ? 31.069  -3.224  0.259   1.00 14.73 ? 272 TYR A CD2 1 
ATOM   1660 C  CE1 . TYR A 1 225 ? 31.841  -5.537  -1.060  1.00 15.14 ? 272 TYR A CE1 1 
ATOM   1661 C  CE2 . TYR A 1 225 ? 32.395  -3.449  -0.056  1.00 15.10 ? 272 TYR A CE2 1 
ATOM   1662 C  CZ  . TYR A 1 225 ? 32.773  -4.577  -0.730  1.00 15.39 ? 272 TYR A CZ  1 
ATOM   1663 O  OH  . TYR A 1 225 ? 34.089  -4.803  -1.059  1.00 18.29 ? 272 TYR A OH  1 
ATOM   1664 N  N   . LEU A 1 226 ? 26.897  -3.364  3.021   1.00 12.86 ? 273 LEU A N   1 
ATOM   1665 C  CA  . LEU A 1 226 ? 25.631  -3.069  3.681   1.00 12.65 ? 273 LEU A CA  1 
ATOM   1666 C  C   . LEU A 1 226 ? 25.153  -1.689  3.240   1.00 13.47 ? 273 LEU A C   1 
ATOM   1667 O  O   . LEU A 1 226 ? 25.894  -0.720  3.261   1.00 14.31 ? 273 LEU A O   1 
ATOM   1668 C  CB  . LEU A 1 226 ? 25.878  -3.046  5.188   1.00 13.71 ? 273 LEU A CB  1 
ATOM   1669 C  CG  . LEU A 1 226 ? 24.722  -2.591  6.066   1.00 14.69 ? 273 LEU A CG  1 
ATOM   1670 C  CD1 . LEU A 1 226 ? 23.530  -3.511  5.874   1.00 15.66 ? 273 LEU A CD1 1 
ATOM   1671 C  CD2 . LEU A 1 226 ? 25.129  -2.533  7.531   1.00 16.56 ? 273 LEU A CD2 1 
ATOM   1672 N  N   . VAL A 1 227 ? 23.876  -1.638  2.868   1.00 12.19 ? 274 VAL A N   1 
ATOM   1673 C  CA  . VAL A 1 227 ? 23.154  -0.383  2.725   1.00 12.64 ? 274 VAL A CA  1 
ATOM   1674 C  C   . VAL A 1 227 ? 22.100  -0.281  3.796   1.00 12.15 ? 274 VAL A C   1 
ATOM   1675 O  O   . VAL A 1 227 ? 21.299  -1.207  3.968   1.00 13.36 ? 274 VAL A O   1 
ATOM   1676 C  CB  . VAL A 1 227 ? 22.466  -0.347  1.354   1.00 15.29 ? 274 VAL A CB  1 
ATOM   1677 C  CG1 . VAL A 1 227 ? 21.600  0.876   1.204   1.00 16.53 ? 274 VAL A CG1 1 
ATOM   1678 C  CG2 . VAL A 1 227 ? 23.463  -0.452  0.219   1.00 16.32 ? 274 VAL A CG2 1 
ATOM   1679 N  N   . ALA A 1 228 ? 22.066  0.855   4.442   1.00 12.01 ? 275 ALA A N   1 
ATOM   1680 C  CA  . ALA A 1 228 ? 21.068  1.173   5.442   1.00 12.24 ? 275 ALA A CA  1 
ATOM   1681 C  C   . ALA A 1 228 ? 20.224  2.327   4.956   1.00 13.30 ? 275 ALA A C   1 
ATOM   1682 O  O   . ALA A 1 228 ? 20.786  3.340   4.563   1.00 14.61 ? 275 ALA A O   1 
ATOM   1683 C  CB  . ALA A 1 228 ? 21.701  1.505   6.782   1.00 13.32 ? 275 ALA A CB  1 
ATOM   1684 N  N   . ARG A 1 229 ? 18.911  2.179   4.981   1.00 12.62 ? 276 ARG A N   1 
ATOM   1685 C  CA  . ARG A 1 229 ? 18.034  3.287   4.626   1.00 12.72 ? 276 ARG A CA  1 
ATOM   1686 C  C   . ARG A 1 229 ? 16.972  3.408   5.690   1.00 12.10 ? 276 ARG A C   1 
ATOM   1687 O  O   . ARG A 1 229 ? 16.235  2.460   5.991   1.00 13.18 ? 276 ARG A O   1 
ATOM   1688 C  CB  . ARG A 1 229 ? 17.352  3.105   3.272   1.00 13.12 ? 276 ARG A CB  1 
ATOM   1689 C  CG  . ARG A 1 229 ? 18.322  2.928   2.113   1.00 13.87 ? 276 ARG A CG  1 
ATOM   1690 C  CD  . ARG A 1 229 ? 19.069  4.150   1.686   1.00 15.29 ? 276 ARG A CD  1 
ATOM   1691 N  NE  . ARG A 1 229 ? 18.113  4.976   0.947   1.00 14.98 ? 276 ARG A NE  1 
ATOM   1692 C  CZ  . ARG A 1 229 ? 18.449  5.971   0.132   1.00 15.91 ? 276 ARG A CZ  1 
ATOM   1693 N  NH1 . ARG A 1 229 ? 19.667  6.388   0.045   1.00 16.75 ? 276 ARG A NH1 1 
ATOM   1694 N  NH2 . ARG A 1 229 ? 17.508  6.562   -0.584  1.00 17.58 ? 276 ARG A NH2 1 
ATOM   1695 N  N   . ARG A 1 230 ? 16.850  4.591   6.285   1.00 12.01 ? 277 ARG A N   1 
ATOM   1696 C  CA  A ARG A 1 230 ? 15.782  4.866   7.213   0.50 11.88 ? 277 ARG A CA  1 
ATOM   1697 C  CA  B ARG A 1 230 ? 15.782  4.862   7.218   0.50 12.57 ? 277 ARG A CA  1 
ATOM   1698 C  C   . ARG A 1 230 ? 14.600  5.386   6.420   1.00 12.95 ? 277 ARG A C   1 
ATOM   1699 O  O   . ARG A 1 230 ? 14.755  6.389   5.720   1.00 13.43 ? 277 ARG A O   1 
ATOM   1700 C  CB  A ARG A 1 230 ? 16.211  5.937   8.213   0.50 13.25 ? 277 ARG A CB  1 
ATOM   1701 C  CB  B ARG A 1 230 ? 16.307  5.842   8.269   0.50 15.23 ? 277 ARG A CB  1 
ATOM   1702 C  CG  A ARG A 1 230 ? 15.264  6.072   9.384   0.50 14.64 ? 277 ARG A CG  1 
ATOM   1703 C  CG  B ARG A 1 230 ? 15.363  6.257   9.383   0.50 18.07 ? 277 ARG A CG  1 
ATOM   1704 C  CD  A ARG A 1 230 ? 15.691  7.238   10.286  0.50 15.82 ? 277 ARG A CD  1 
ATOM   1705 C  CD  B ARG A 1 230 ? 16.141  6.808   10.617  0.50 20.67 ? 277 ARG A CD  1 
ATOM   1706 N  NE  A ARG A 1 230 ? 15.038  7.227   11.608  0.50 19.22 ? 277 ARG A NE  1 
ATOM   1707 N  NE  B ARG A 1 230 ? 17.497  7.185   10.225  0.50 24.90 ? 277 ARG A NE  1 
ATOM   1708 C  CZ  A ARG A 1 230 ? 14.185  8.152   11.962  0.50 21.28 ? 277 ARG A CZ  1 
ATOM   1709 C  CZ  B ARG A 1 230 ? 18.627  6.698   10.722  0.50 25.83 ? 277 ARG A CZ  1 
ATOM   1710 N  NH1 A ARG A 1 230 ? 13.942  9.143   11.126  0.50 22.03 ? 277 ARG A NH1 1 
ATOM   1711 N  NH1 B ARG A 1 230 ? 19.660  6.501   9.920   0.50 27.26 ? 277 ARG A NH1 1 
ATOM   1712 N  NH2 A ARG A 1 230 ? 13.567  8.121   13.127  0.50 23.61 ? 277 ARG A NH2 1 
ATOM   1713 N  NH2 B ARG A 1 230 ? 18.643  6.254   11.957  0.50 27.04 ? 277 ARG A NH2 1 
ATOM   1714 N  N   . ILE A 1 231 ? 13.464  4.682   6.475   1.00 11.82 ? 278 ILE A N   1 
ATOM   1715 C  CA  . ILE A 1 231 ? 12.315  4.970   5.625   1.00 11.11 ? 278 ILE A CA  1 
ATOM   1716 C  C   . ILE A 1 231 ? 11.129  5.283   6.499   1.00 12.53 ? 278 ILE A C   1 
ATOM   1717 O  O   . ILE A 1 231 ? 10.646  4.444   7.256   1.00 13.97 ? 278 ILE A O   1 
ATOM   1718 C  CB  . ILE A 1 231 ? 12.042  3.795   4.688   1.00 12.08 ? 278 ILE A CB  1 
ATOM   1719 C  CG1 . ILE A 1 231 ? 13.264  3.424   3.899   1.00 13.32 ? 278 ILE A CG1 1 
ATOM   1720 C  CG2 . ILE A 1 231 ? 10.868  4.146   3.773   1.00 13.35 ? 278 ILE A CG2 1 
ATOM   1721 C  CD1 . ILE A 1 231 ? 13.104  2.188   3.041   1.00 14.60 ? 278 ILE A CD1 1 
ATOM   1722 N  N   . ARG A 1 232 ? 10.616  6.515   6.380   1.00 12.74 ? 279 ARG A N   1 
ATOM   1723 C  CA  . ARG A 1 232 ? 9.420   6.880   7.083   1.00 13.40 ? 279 ARG A CA  1 
ATOM   1724 C  C   . ARG A 1 232 ? 8.232   6.395   6.270   1.00 13.19 ? 279 ARG A C   1 
ATOM   1725 O  O   . ARG A 1 232 ? 8.250   6.416   5.048   1.00 15.16 ? 279 ARG A O   1 
ATOM   1726 C  CB  . ARG A 1 232 ? 9.372   8.414   7.111   1.00 17.21 ? 279 ARG A CB  1 
ATOM   1727 C  CG  . ARG A 1 232 ? 8.016   8.938   7.541   1.00 24.60 ? 279 ARG A CG  1 
ATOM   1728 C  CD  . ARG A 1 232 ? 8.056   10.457  7.658   1.00 32.47 ? 279 ARG A CD  1 
ATOM   1729 N  NE  . ARG A 1 232 ? 9.044   10.852  8.658   1.00 40.37 ? 279 ARG A NE  1 
ATOM   1730 C  CZ  . ARG A 1 232 ? 8.938   10.609  9.943   1.00 45.66 ? 279 ARG A CZ  1 
ATOM   1731 N  NH1 . ARG A 1 232 ? 7.813   10.100  10.435  1.00 49.39 ? 279 ARG A NH1 1 
ATOM   1732 N  NH2 . ARG A 1 232 ? 9.957   10.912  10.730  1.00 52.58 ? 279 ARG A NH2 1 
ATOM   1733 N  N   . MET A 1 233 ? 7.201   5.933   6.958   1.00 13.01 ? 280 MET A N   1 
ATOM   1734 C  CA  . MET A 1 233 ? 5.961   5.489   6.334   1.00 13.42 ? 280 MET A CA  1 
ATOM   1735 C  C   . MET A 1 233 ? 4.872   6.504   6.617   1.00 13.14 ? 280 MET A C   1 
ATOM   1736 O  O   . MET A 1 233 ? 4.682   6.931   7.738   1.00 14.80 ? 280 MET A O   1 
ATOM   1737 C  CB  . MET A 1 233 ? 5.529   4.142   6.918   1.00 14.69 ? 280 MET A CB  1 
ATOM   1738 C  CG  . MET A 1 233 ? 6.416   2.990   6.511   1.00 16.20 ? 280 MET A CG  1 
ATOM   1739 S  SD  . MET A 1 233 ? 6.014   1.525   7.522   1.00 20.03 ? 280 MET A SD  1 
ATOM   1740 C  CE  . MET A 1 233 ? 6.690   0.167   6.563   1.00 21.03 ? 280 MET A CE  1 
ATOM   1741 N  N   . HIS A 1 234 ? 4.123   6.842   5.573   1.00 12.82 ? 281 HIS A N   1 
ATOM   1742 C  CA  . HIS A 1 234 ? 2.978   7.747   5.677   1.00 12.78 ? 281 HIS A CA  1 
ATOM   1743 C  C   . HIS A 1 234 ? 1.740   6.966   6.086   1.00 12.53 ? 281 HIS A C   1 
ATOM   1744 O  O   . HIS A 1 234 ? 0.912   6.643   5.230   1.00 13.86 ? 281 HIS A O   1 
ATOM   1745 C  CB  . HIS A 1 234 ? 2.781   8.493   4.363   1.00 14.38 ? 281 HIS A CB  1 
ATOM   1746 C  CG  . HIS A 1 234 ? 3.947   9.291   3.906   1.00 14.25 ? 281 HIS A CG  1 
ATOM   1747 N  ND1 . HIS A 1 234 ? 4.747   10.009  4.760   1.00 16.95 ? 281 HIS A ND1 1 
ATOM   1748 C  CD2 . HIS A 1 234 ? 4.461   9.444   2.656   1.00 15.80 ? 281 HIS A CD2 1 
ATOM   1749 C  CE1 . HIS A 1 234 ? 5.702   10.602  4.011   1.00 17.19 ? 281 HIS A CE1 1 
ATOM   1750 N  NE2 . HIS A 1 234 ? 5.545   10.250  2.756   1.00 18.29 ? 281 HIS A NE2 1 
ATOM   1751 N  N   . ILE A 1 235 ? 1.649   6.584   7.348   1.00 12.04 ? 282 ILE A N   1 
ATOM   1752 C  CA  . ILE A 1 235 ? 0.604   5.665   7.747   1.00 13.51 ? 282 ILE A CA  1 
ATOM   1753 C  C   . ILE A 1 235 ? -0.774  6.301   7.678   1.00 12.58 ? 282 ILE A C   1 
ATOM   1754 O  O   . ILE A 1 235 ? -1.721  5.593   7.389   1.00 13.04 ? 282 ILE A O   1 
ATOM   1755 C  CB  . ILE A 1 235 ? 0.811   4.981   9.092   1.00 17.61 ? 282 ILE A CB  1 
ATOM   1756 C  CG1 . ILE A 1 235 ? 0.984   5.924   10.181  1.00 19.49 ? 282 ILE A CG1 1 
ATOM   1757 C  CG2 . ILE A 1 235 ? 1.961   3.950   8.987   1.00 20.41 ? 282 ILE A CG2 1 
ATOM   1758 C  CD1 . ILE A 1 235 ? 0.965   5.221   11.527  1.00 22.88 ? 282 ILE A CD1 1 
ATOM   1759 N  N   . GLU A 1 236 ? -0.915  7.615   7.864   1.00 11.67 ? 283 GLU A N   1 
ATOM   1760 C  CA  . GLU A 1 236 ? -2.232  8.216   7.724   1.00 11.07 ? 283 GLU A CA  1 
ATOM   1761 C  C   . GLU A 1 236 ? -2.739  7.999   6.301   1.00 11.58 ? 283 GLU A C   1 
ATOM   1762 O  O   . GLU A 1 236 ? -3.879  7.594   6.089   1.00 12.61 ? 283 GLU A O   1 
ATOM   1763 C  CB  . GLU A 1 236 ? -2.184  9.726   7.956   1.00 11.39 ? 283 GLU A CB  1 
ATOM   1764 C  CG  . GLU A 1 236 ? -3.564  10.373  7.839   1.00 11.75 ? 283 GLU A CG  1 
ATOM   1765 C  CD  . GLU A 1 236 ? -3.610  11.866  8.041   1.00 12.14 ? 283 GLU A CD  1 
ATOM   1766 O  OE1 . GLU A 1 236 ? -2.642  12.473  8.509   1.00 13.38 ? 283 GLU A OE1 1 
ATOM   1767 O  OE2 . GLU A 1 236 ? -4.664  12.393  7.631   1.00 14.19 ? 283 GLU A OE2 1 
ATOM   1768 N  N   . THR A 1 237 ? -1.860  8.228   5.338   1.00 12.50 ? 284 THR A N   1 
ATOM   1769 C  CA  . THR A 1 237 ? -2.177  8.109   3.919   1.00 12.72 ? 284 THR A CA  1 
ATOM   1770 C  C   . THR A 1 237 ? -2.486  6.642   3.582   1.00 12.24 ? 284 THR A C   1 
ATOM   1771 O  O   . THR A 1 237 ? -3.455  6.329   2.905   1.00 13.50 ? 284 THR A O   1 
ATOM   1772 C  CB  . THR A 1 237 ? -0.977  8.616   3.129   1.00 13.53 ? 284 THR A CB  1 
ATOM   1773 O  OG1 . THR A 1 237 ? -0.484  9.824   3.739   1.00 16.19 ? 284 THR A OG1 1 
ATOM   1774 C  CG2 . THR A 1 237 ? -1.300  8.762   1.667   1.00 15.94 ? 284 THR A CG2 1 
ATOM   1775 N  N   . TRP A 1 238 ? -1.660  5.725   4.081   1.00 11.57 ? 285 TRP A N   1 
ATOM   1776 C  CA  . TRP A 1 238 ? -1.818  4.294   3.834   1.00 10.98 ? 285 TRP A CA  1 
ATOM   1777 C  C   . TRP A 1 238 ? -3.111  3.785   4.436   1.00 11.96 ? 285 TRP A C   1 
ATOM   1778 O  O   . TRP A 1 238 ? -3.828  2.996   3.799   1.00 12.59 ? 285 TRP A O   1 
ATOM   1779 C  CB  . TRP A 1 238 ? -0.644  3.566   4.441   1.00 11.47 ? 285 TRP A CB  1 
ATOM   1780 C  CG  . TRP A 1 238 ? -0.730  2.075   4.282   1.00 11.08 ? 285 TRP A CG  1 
ATOM   1781 C  CD1 . TRP A 1 238 ? -0.987  1.187   5.260   1.00 10.52 ? 285 TRP A CD1 1 
ATOM   1782 C  CD2 . TRP A 1 238 ? -0.454  1.313   3.102   1.00 11.71 ? 285 TRP A CD2 1 
ATOM   1783 N  NE1 . TRP A 1 238 ? -0.894  -0.087  4.767   1.00 12.00 ? 285 TRP A NE1 1 
ATOM   1784 C  CE2 . TRP A 1 238 ? -0.567  -0.051  3.465   1.00 11.26 ? 285 TRP A CE2 1 
ATOM   1785 C  CE3 . TRP A 1 238 ? -0.108  1.650   1.794   1.00 13.03 ? 285 TRP A CE3 1 
ATOM   1786 C  CZ2 . TRP A 1 238 ? -0.333  -1.070  2.544   1.00 12.50 ? 285 TRP A CZ2 1 
ATOM   1787 C  CZ3 . TRP A 1 238 ? 0.106   0.623   0.897   1.00 13.35 ? 285 TRP A CZ3 1 
ATOM   1788 C  CH2 . TRP A 1 238 ? -0.008  -0.694  1.280   1.00 13.64 ? 285 TRP A CH2 1 
ATOM   1789 N  N   . ASP A 1 239 ? -3.466  4.213   5.634   1.00 12.00 ? 286 ASP A N   1 
ATOM   1790 C  CA  . ASP A 1 239 ? -4.553  3.600   6.359   1.00 13.33 ? 286 ASP A CA  1 
ATOM   1791 C  C   . ASP A 1 239 ? -5.898  4.002   5.785   1.00 15.67 ? 286 ASP A C   1 
ATOM   1792 O  O   . ASP A 1 239 ? -6.879  3.287   6.040   1.00 17.30 ? 286 ASP A O   1 
ATOM   1793 C  CB  . ASP A 1 239 ? -4.466  3.890   7.843   1.00 14.00 ? 286 ASP A CB  1 
ATOM   1794 C  CG  . ASP A 1 239 ? -3.398  3.111   8.585   1.00 13.57 ? 286 ASP A CG  1 
ATOM   1795 O  OD1 . ASP A 1 239 ? -2.842  2.168   7.992   1.00 13.92 ? 286 ASP A OD1 1 
ATOM   1796 O  OD2 . ASP A 1 239 ? -3.169  3.417   9.761   1.00 13.92 ? 286 ASP A OD2 1 
ATOM   1797 N  N   . ARG A 1 240 ? -5.937  5.057   4.980   1.00 13.64 ? 287 ARG A N   1 
ATOM   1798 C  CA  . ARG A 1 240 ? -7.187  5.426   4.320   1.00 15.23 ? 287 ARG A CA  1 
ATOM   1799 C  C   . ARG A 1 240 ? -7.288  4.824   2.932   1.00 16.39 ? 287 ARG A C   1 
ATOM   1800 O  O   . ARG A 1 240 ? -8.321  4.989   2.272   1.00 17.60 ? 287 ARG A O   1 
ATOM   1801 C  CB  . ARG A 1 240 ? -7.426  6.925   4.283   1.00 16.65 ? 287 ARG A CB  1 
ATOM   1802 C  CG  . ARG A 1 240 ? -6.478  7.720   3.435   1.00 16.19 ? 287 ARG A CG  1 
ATOM   1803 C  CD  . ARG A 1 240 ? -7.021  9.151   3.377   1.00 16.53 ? 287 ARG A CD  1 
ATOM   1804 N  NE  . ARG A 1 240 ? -6.147  9.970   2.556   1.00 16.42 ? 287 ARG A NE  1 
ATOM   1805 C  CZ  . ARG A 1 240 ? -5.070  10.619  2.959   1.00 14.74 ? 287 ARG A CZ  1 
ATOM   1806 N  NH1 . ARG A 1 240 ? -4.207  11.068  2.081   1.00 16.84 ? 287 ARG A NH1 1 
ATOM   1807 N  NH2 . ARG A 1 240 ? -4.792  10.726  4.254   1.00 14.91 ? 287 ARG A NH2 1 
ATOM   1808 N  N   . ALA A 1 241 ? -6.264  4.120   2.452   1.00 13.83 ? 288 ALA A N   1 
ATOM   1809 C  CA  . ALA A 1 241 ? -6.329  3.428   1.174   1.00 14.01 ? 288 ALA A CA  1 
ATOM   1810 C  C   . ALA A 1 241 ? -7.217  2.193   1.281   1.00 15.53 ? 288 ALA A C   1 
ATOM   1811 O  O   . ALA A 1 241 ? -7.267  1.505   2.303   1.00 16.62 ? 288 ALA A O   1 
ATOM   1812 C  CB  . ALA A 1 241 ? -4.948  3.067   0.704   1.00 15.72 ? 288 ALA A CB  1 
ATOM   1813 N  N   . SER A 1 242 ? -7.920  1.858   0.195   1.00 14.35 ? 289 SER A N   1 
ATOM   1814 C  CA  . SER A 1 242 ? -8.669  0.617   0.160   1.00 14.72 ? 289 SER A CA  1 
ATOM   1815 C  C   . SER A 1 242 ? -7.785  -0.621  0.185   1.00 13.53 ? 289 SER A C   1 
ATOM   1816 O  O   . SER A 1 242 ? -6.597  -0.569  -0.168  1.00 13.86 ? 289 SER A O   1 
ATOM   1817 C  CB  . SER A 1 242 ? -9.533  0.564   -1.067  1.00 16.06 ? 289 SER A CB  1 
ATOM   1818 O  OG  . SER A 1 242 ? -8.756  0.478   -2.224  1.00 17.43 ? 289 SER A OG  1 
ATOM   1819 N  N   . LEU A 1 243 ? -8.408  -1.738  0.548   1.00 13.74 ? 290 LEU A N   1 
ATOM   1820 C  CA  . LEU A 1 243 ? -7.703  -3.005  0.534   1.00 14.34 ? 290 LEU A CA  1 
ATOM   1821 C  C   . LEU A 1 243 ? -7.141  -3.275  -0.856  1.00 14.57 ? 290 LEU A C   1 
ATOM   1822 O  O   . LEU A 1 243 ? -6.004  -3.678  -1.015  1.00 13.98 ? 290 LEU A O   1 
ATOM   1823 C  CB  . LEU A 1 243 ? -8.621  -4.126  0.993   1.00 16.80 ? 290 LEU A CB  1 
ATOM   1824 C  CG  . LEU A 1 243 ? -7.996  -5.523  1.007   1.00 17.64 ? 290 LEU A CG  1 
ATOM   1825 C  CD1 . LEU A 1 243 ? -6.837  -5.683  1.955   1.00 18.84 ? 290 LEU A CD1 1 
ATOM   1826 C  CD2 . LEU A 1 243 ? -9.081  -6.550  1.297   1.00 19.80 ? 290 LEU A CD2 1 
ATOM   1827 N  N   . GLN A 1 244 ? -7.966  -3.062  -1.887  1.00 14.65 ? 291 GLN A N   1 
ATOM   1828 C  CA  . GLN A 1 244 ? -7.476  -3.336  -3.220  1.00 15.76 ? 291 GLN A CA  1 
ATOM   1829 C  C   . GLN A 1 244 ? -6.296  -2.466  -3.597  1.00 13.87 ? 291 GLN A C   1 
ATOM   1830 O  O   . GLN A 1 244 ? -5.363  -2.941  -4.211  1.00 14.61 ? 291 GLN A O   1 
ATOM   1831 C  CB  . GLN A 1 244 ? -8.564  -3.049  -4.259  1.00 18.25 ? 291 GLN A CB  1 
ATOM   1832 C  CG  . GLN A 1 244 ? -8.199  -3.576  -5.643  1.00 22.76 ? 291 GLN A CG  1 
ATOM   1833 C  CD  . GLN A 1 244 ? -7.921  -5.066  -5.653  1.00 27.68 ? 291 GLN A CD  1 
ATOM   1834 O  OE1 . GLN A 1 244 ? -8.780  -5.896  -5.322  1.00 35.26 ? 291 GLN A OE1 1 
ATOM   1835 N  NE2 . GLN A 1 244 ? -6.699  -5.441  -6.015  1.00 31.17 ? 291 GLN A NE2 1 
ATOM   1836 N  N   . GLU A 1 245 ? -6.317  -1.184  -3.207  1.00 13.75 ? 292 GLU A N   1 
ATOM   1837 C  CA  A GLU A 1 245 ? -5.198  -0.311  -3.492  0.50 13.59 ? 292 GLU A CA  1 
ATOM   1838 C  CA  B GLU A 1 245 ? -5.210  -0.289  -3.467  0.50 13.23 ? 292 GLU A CA  1 
ATOM   1839 C  C   . GLU A 1 245 ? -3.933  -0.827  -2.807  1.00 13.03 ? 292 GLU A C   1 
ATOM   1840 O  O   . GLU A 1 245 ? -2.879  -0.851  -3.414  1.00 13.58 ? 292 GLU A O   1 
ATOM   1841 C  CB  A GLU A 1 245 ? -5.411  1.141   -3.080  0.50 15.80 ? 292 GLU A CB  1 
ATOM   1842 C  CB  B GLU A 1 245 ? -5.571  1.126   -3.008  0.50 15.03 ? 292 GLU A CB  1 
ATOM   1843 C  CG  A GLU A 1 245 ? -4.269  2.057   -3.510  0.50 19.37 ? 292 GLU A CG  1 
ATOM   1844 C  CG  B GLU A 1 245 ? -6.609  1.838   -3.887  0.50 17.42 ? 292 GLU A CG  1 
ATOM   1845 C  CD  A GLU A 1 245 ? -4.540  3.554   -3.407  0.50 21.63 ? 292 GLU A CD  1 
ATOM   1846 C  CD  B GLU A 1 245 ? -7.181  3.147   -3.362  0.50 21.25 ? 292 GLU A CD  1 
ATOM   1847 O  OE1 A GLU A 1 245 ? -5.677  3.949   -3.064  0.50 25.78 ? 292 GLU A OE1 1 
ATOM   1848 O  OE1 B GLU A 1 245 ? -7.596  3.303   -2.206  0.50 20.16 ? 292 GLU A OE1 1 
ATOM   1849 O  OE2 A GLU A 1 245 ? -3.592  4.333   -3.653  0.50 23.15 ? 292 GLU A OE2 1 
ATOM   1850 O  OE2 B GLU A 1 245 ? -7.295  4.056   -4.200  0.50 27.81 ? 292 GLU A OE2 1 
ATOM   1851 N  N   . GLN A 1 246 ? -4.058  -1.223  -1.539  1.00 11.66 ? 293 GLN A N   1 
ATOM   1852 C  CA  . GLN A 1 246 ? -2.892  -1.715  -0.823  1.00 12.43 ? 293 GLN A CA  1 
ATOM   1853 C  C   . GLN A 1 246 ? -2.323  -2.940  -1.515  1.00 12.01 ? 293 GLN A C   1 
ATOM   1854 O  O   . GLN A 1 246 ? -1.107  -3.095  -1.655  1.00 12.67 ? 293 GLN A O   1 
ATOM   1855 C  CB  . GLN A 1 246 ? -3.289  -2.036  0.594   1.00 11.63 ? 293 GLN A CB  1 
ATOM   1856 C  CG  . GLN A 1 246 ? -3.640  -0.799  1.418   1.00 11.71 ? 293 GLN A CG  1 
ATOM   1857 C  CD  . GLN A 1 246 ? -3.801  -1.113  2.875   1.00 13.16 ? 293 GLN A CD  1 
ATOM   1858 O  OE1 . GLN A 1 246 ? -3.614  -2.242  3.330   1.00 13.86 ? 293 GLN A OE1 1 
ATOM   1859 N  NE2 . GLN A 1 246 ? -4.061  -0.099  3.663   1.00 14.48 ? 293 GLN A NE2 1 
ATOM   1860 N  N   . GLU A 1 247 ? -3.200  -3.891  -1.898  1.00 12.09 ? 294 GLU A N   1 
ATOM   1861 C  CA  . GLU A 1 247 ? -2.731  -5.122  -2.510  1.00 12.50 ? 294 GLU A CA  1 
ATOM   1862 C  C   . GLU A 1 247 ? -2.165  -4.840  -3.882  1.00 12.94 ? 294 GLU A C   1 
ATOM   1863 O  O   . GLU A 1 247 ? -1.167  -5.443  -4.285  1.00 13.91 ? 294 GLU A O   1 
ATOM   1864 C  CB  . GLU A 1 247 ? -3.828  -6.160  -2.622  1.00 13.07 ? 294 GLU A CB  1 
ATOM   1865 C  CG  . GLU A 1 247 ? -4.323  -6.609  -1.267  1.00 13.62 ? 294 GLU A CG  1 
ATOM   1866 C  CD  . GLU A 1 247 ? -5.318  -7.731  -1.189  1.00 14.75 ? 294 GLU A CD  1 
ATOM   1867 O  OE1 . GLU A 1 247 ? -5.961  -7.930  -2.258  1.00 18.60 ? 294 GLU A OE1 1 
ATOM   1868 O  OE2 . GLU A 1 247 ? -5.438  -8.402  -0.174  1.00 14.75 ? 294 GLU A OE2 1 
ATOM   1869 N  N   . ASP A 1 248 ? -2.732  -3.873  -4.581  1.00 13.20 ? 295 ASP A N   1 
ATOM   1870 C  CA  . ASP A 1 248 ? -2.189  -3.537  -5.886  1.00 13.36 ? 295 ASP A CA  1 
ATOM   1871 C  C   . ASP A 1 248 ? -0.806  -2.913  -5.799  1.00 14.25 ? 295 ASP A C   1 
ATOM   1872 O  O   . ASP A 1 248 ? 0.021   -3.031  -6.693  1.00 15.15 ? 295 ASP A O   1 
ATOM   1873 C  CB  . ASP A 1 248 ? -3.087  -2.540  -6.602  1.00 15.66 ? 295 ASP A CB  1 
ATOM   1874 C  CG  . ASP A 1 248 ? -4.316  -3.114  -7.295  1.00 18.23 ? 295 ASP A CG  1 
ATOM   1875 O  OD1 . ASP A 1 248 ? -4.418  -4.320  -7.345  1.00 19.58 ? 295 ASP A OD1 1 
ATOM   1876 O  OD2 . ASP A 1 248 ? -5.231  -2.282  -7.575  1.00 23.49 ? 295 ASP A OD2 1 
ATOM   1877 N  N   . VAL A 1 249 ? -0.537  -2.150  -4.723  1.00 13.17 ? 296 VAL A N   1 
ATOM   1878 C  CA  . VAL A 1 249 ? 0.751   -1.539  -4.503  1.00 13.06 ? 296 VAL A CA  1 
ATOM   1879 C  C   . VAL A 1 249 ? 1.834   -2.596  -4.493  1.00 12.23 ? 296 VAL A C   1 
ATOM   1880 O  O   . VAL A 1 249 ? 2.923   -2.361  -5.001  1.00 13.11 ? 296 VAL A O   1 
ATOM   1881 C  CB  . VAL A 1 249 ? 0.764   -0.709  -3.212  1.00 13.77 ? 296 VAL A CB  1 
ATOM   1882 C  CG1 . VAL A 1 249 ? 2.171   -0.433  -2.697  1.00 15.09 ? 296 VAL A CG1 1 
ATOM   1883 C  CG2 . VAL A 1 249 ? 0.015   0.586   -3.435  1.00 15.04 ? 296 VAL A CG2 1 
ATOM   1884 N  N   . PHE A 1 250 ? 1.563   -3.729  -3.848  1.00 11.62 ? 297 PHE A N   1 
ATOM   1885 C  CA  . PHE A 1 250 ? 2.580   -4.753  -3.678  1.00 12.72 ? 297 PHE A CA  1 
ATOM   1886 C  C   . PHE A 1 250 ? 2.582   -5.820  -4.763  1.00 12.29 ? 297 PHE A C   1 
ATOM   1887 O  O   . PHE A 1 250 ? 3.653   -6.304  -5.141  1.00 15.05 ? 297 PHE A O   1 
ATOM   1888 C  CB  . PHE A 1 250 ? 2.451   -5.389  -2.296  1.00 12.24 ? 297 PHE A CB  1 
ATOM   1889 C  CG  . PHE A 1 250 ? 3.017   -4.467  -1.242  1.00 11.81 ? 297 PHE A CG  1 
ATOM   1890 C  CD1 . PHE A 1 250 ? 4.364   -4.158  -1.237  1.00 11.66 ? 297 PHE A CD1 1 
ATOM   1891 C  CD2 . PHE A 1 250 ? 2.194   -3.899  -0.283  1.00 14.80 ? 297 PHE A CD2 1 
ATOM   1892 C  CE1 . PHE A 1 250 ? 4.869   -3.254  -0.320  1.00 12.35 ? 297 PHE A CE1 1 
ATOM   1893 C  CE2 . PHE A 1 250 ? 2.733   -3.006  0.647   1.00 14.12 ? 297 PHE A CE2 1 
ATOM   1894 C  CZ  . PHE A 1 250 ? 4.062   -2.688  0.598   1.00 13.87 ? 297 PHE A CZ  1 
ATOM   1895 N  N   . GLY A 1 251 ? 1.413   -6.247  -5.197  1.00 12.23 ? 298 GLY A N   1 
ATOM   1896 C  CA  . GLY A 1 251 ? 1.262   -7.396  -6.066  1.00 12.84 ? 298 GLY A CA  1 
ATOM   1897 C  C   . GLY A 1 251 ? 1.077   -8.711  -5.339  1.00 14.38 ? 298 GLY A C   1 
ATOM   1898 O  O   . GLY A 1 251 ? 1.170   -9.787  -5.946  1.00 14.63 ? 298 GLY A O   1 
ATOM   1899 N  N   . ARG A 1 252 ? 0.834   -8.650  -4.024  1.00 12.20 ? 299 ARG A N   1 
ATOM   1900 C  CA  . ARG A 1 252 ? 0.534   -9.791  -3.183  1.00 12.00 ? 299 ARG A CA  1 
ATOM   1901 C  C   . ARG A 1 252 ? -0.716  -9.452  -2.392  1.00 12.82 ? 299 ARG A C   1 
ATOM   1902 O  O   . ARG A 1 252 ? -0.969  -8.282  -2.149  1.00 13.11 ? 299 ARG A O   1 
ATOM   1903 C  CB  . ARG A 1 252 ? 1.673   -10.148 -2.230  1.00 12.03 ? 299 ARG A CB  1 
ATOM   1904 C  CG  . ARG A 1 252 ? 2.858   -10.724 -2.967  1.00 12.07 ? 299 ARG A CG  1 
ATOM   1905 C  CD  . ARG A 1 252 ? 4.026   -11.000 -2.012  1.00 12.22 ? 299 ARG A CD  1 
ATOM   1906 N  NE  . ARG A 1 252 ? 5.168   -11.673 -2.621  1.00 12.23 ? 299 ARG A NE  1 
ATOM   1907 C  CZ  . ARG A 1 252 ? 5.339   -12.982 -2.661  1.00 12.71 ? 299 ARG A CZ  1 
ATOM   1908 N  NH1 . ARG A 1 252 ? 4.418   -13.845 -2.238  1.00 13.88 ? 299 ARG A NH1 1 
ATOM   1909 N  NH2 . ARG A 1 252 ? 6.458   -13.430 -3.169  1.00 14.73 ? 299 ARG A NH2 1 
ATOM   1910 N  N   . ASP A 1 253 ? -1.494  -10.430 -1.994  1.00 12.51 ? 300 ASP A N   1 
ATOM   1911 C  CA  . ASP A 1 253 ? -2.652  -10.197 -1.158  1.00 12.82 ? 300 ASP A CA  1 
ATOM   1912 C  C   . ASP A 1 253 ? -2.176  -9.995  0.268   1.00 13.01 ? 300 ASP A C   1 
ATOM   1913 O  O   . ASP A 1 253 ? -1.096  -10.408 0.679   1.00 13.71 ? 300 ASP A O   1 
ATOM   1914 C  CB  . ASP A 1 253 ? -3.706  -11.290 -1.256  1.00 13.56 ? 300 ASP A CB  1 
ATOM   1915 C  CG  . ASP A 1 253 ? -3.307  -12.550 -0.518  1.00 16.92 ? 300 ASP A CG  1 
ATOM   1916 O  OD1 . ASP A 1 253 ? -2.407  -13.226 -0.954  1.00 22.45 ? 300 ASP A OD1 1 
ATOM   1917 O  OD2 . ASP A 1 253 ? -3.772  -12.756 0.623   1.00 21.38 ? 300 ASP A OD2 1 
ATOM   1918 N  N   . LYS A 1 254 ? -3.057  -9.384  1.069   1.00 13.33 ? 301 LYS A N   1 
ATOM   1919 C  CA  . LYS A 1 254 ? -2.608  -8.941  2.382   1.00 13.44 ? 301 LYS A CA  1 
ATOM   1920 C  C   . LYS A 1 254 ? -2.660  -10.082 3.374   1.00 13.68 ? 301 LYS A C   1 
ATOM   1921 O  O   . LYS A 1 254 ? -1.716  -10.216 4.156   1.00 15.22 ? 301 LYS A O   1 
ATOM   1922 C  CB  . LYS A 1 254 ? -3.399  -7.709  2.794   1.00 13.66 ? 301 LYS A CB  1 
ATOM   1923 C  CG  . LYS A 1 254 ? -2.802  -7.031  4.004   1.00 13.53 ? 301 LYS A CG  1 
ATOM   1924 C  CD  . LYS A 1 254 ? -3.401  -5.660  4.277   1.00 12.92 ? 301 LYS A CD  1 
ATOM   1925 C  CE  . LYS A 1 254 ? -2.602  -4.957  5.306   1.00 12.81 ? 301 LYS A CE  1 
ATOM   1926 N  NZ  . LYS A 1 254 ? -3.166  -3.659  5.591   1.00 12.83 ? 301 LYS A NZ  1 
ATOM   1927 N  N   . GLY A 1 255 ? -3.677  -10.909 3.315   1.00 12.94 ? 302 GLY A N   1 
ATOM   1928 C  CA  . GLY A 1 255 ? -3.924  -11.954 4.303   1.00 14.38 ? 302 GLY A CA  1 
ATOM   1929 C  C   . GLY A 1 255 ? -2.894  -13.070 4.245   1.00 14.87 ? 302 GLY A C   1 
ATOM   1930 O  O   . GLY A 1 255 ? -2.214  -13.384 5.212   1.00 18.46 ? 302 GLY A O   1 
ATOM   1931 N  N   . GLU A 1 256 ? -2.781  -13.681 3.077   1.00 14.07 ? 303 GLU A N   1 
ATOM   1932 C  CA  . GLU A 1 256 ? -1.877  -14.801 2.884   1.00 14.35 ? 303 GLU A CA  1 
ATOM   1933 C  C   . GLU A 1 256 ? -0.509  -14.329 2.420   1.00 12.76 ? 303 GLU A C   1 
ATOM   1934 O  O   . GLU A 1 256 ? 0.498   -14.986 2.694   1.00 13.85 ? 303 GLU A O   1 
ATOM   1935 C  CB  . GLU A 1 256 ? -2.494  -15.739 1.845   1.00 15.46 ? 303 GLU A CB  1 
ATOM   1936 C  CG  . GLU A 1 256 ? -1.608  -16.918 1.438   1.00 16.45 ? 303 GLU A CG  1 
ATOM   1937 C  CD  . GLU A 1 256 ? -1.180  -17.886 2.498   1.00 20.93 ? 303 GLU A CD  1 
ATOM   1938 O  OE1 . GLU A 1 256 ? -1.917  -17.962 3.533   1.00 22.83 ? 303 GLU A OE1 1 
ATOM   1939 O  OE2 . GLU A 1 256 ? -0.166  -18.625 2.303   1.00 18.84 ? 303 GLU A OE2 1 
ATOM   1940 N  N   . GLY A 1 257 ? -0.457  -13.180 1.743   1.00 12.68 ? 304 GLY A N   1 
ATOM   1941 C  CA  . GLY A 1 257 ? 0.773   -12.740 1.121   1.00 12.12 ? 304 GLY A CA  1 
ATOM   1942 C  C   . GLY A 1 257 ? 1.156   -13.573 -0.105  1.00 11.90 ? 304 GLY A C   1 
ATOM   1943 O  O   . GLY A 1 257 ? 2.322   -13.644 -0.451  1.00 12.50 ? 304 GLY A O   1 
ATOM   1944 N  N   . ALA A 1 258 ? 0.155   -14.138 -0.769  1.00 12.67 ? 305 ALA A N   1 
ATOM   1945 C  CA  . ALA A 1 258 ? 0.414   -14.862 -2.007  1.00 12.62 ? 305 ALA A CA  1 
ATOM   1946 C  C   . ALA A 1 258 ? 0.548   -13.876 -3.128  1.00 12.60 ? 305 ALA A C   1 
ATOM   1947 O  O   . ALA A 1 258 ? -0.063  -12.817 -3.123  1.00 13.31 ? 305 ALA A O   1 
ATOM   1948 C  CB  . ALA A 1 258 ? -0.754  -15.785 -2.291  1.00 13.97 ? 305 ALA A CB  1 
ATOM   1949 N  N   . PRO A 1 259 ? 1.312   -14.200 -4.178  1.00 12.84 ? 306 PRO A N   1 
ATOM   1950 C  CA  . PRO A 1 259 ? 1.274   -13.388 -5.369  1.00 12.72 ? 306 PRO A CA  1 
ATOM   1951 C  C   . PRO A 1 259 ? -0.142  -13.318 -5.912  1.00 13.58 ? 306 PRO A C   1 
ATOM   1952 O  O   . PRO A 1 259 ? -0.899  -14.280 -5.775  1.00 14.54 ? 306 PRO A O   1 
ATOM   1953 C  CB  . PRO A 1 259 ? 2.226   -14.115 -6.323  1.00 14.79 ? 306 PRO A CB  1 
ATOM   1954 C  CG  . PRO A 1 259 ? 2.998   -15.074 -5.489  1.00 16.02 ? 306 PRO A CG  1 
ATOM   1955 C  CD  . PRO A 1 259 ? 2.078   -15.423 -4.335  1.00 13.65 ? 306 PRO A CD  1 
ATOM   1956 N  N   . VAL A 1 260 ? -0.478  -12.193 -6.511  1.00 13.61 ? 307 VAL A N   1 
ATOM   1957 C  CA  . VAL A 1 260 ? -1.814  -11.993 -7.045  1.00 14.58 ? 307 VAL A CA  1 
ATOM   1958 C  C   . VAL A 1 260 ? -2.193  -13.177 -7.934  1.00 15.06 ? 307 VAL A C   1 
ATOM   1959 O  O   . VAL A 1 260 ? -1.416  -13.659 -8.741  1.00 16.54 ? 307 VAL A O   1 
ATOM   1960 C  CB  . VAL A 1 260 ? -1.937  -10.640 -7.756  1.00 19.29 ? 307 VAL A CB  1 
ATOM   1961 C  CG1 . VAL A 1 260 ? -1.030  -10.563 -8.958  1.00 21.00 ? 307 VAL A CG1 1 
ATOM   1962 C  CG2 . VAL A 1 260 ? -3.380  -10.317 -8.150  1.00 21.30 ? 307 VAL A CG2 1 
ATOM   1963 N  N   . GLY A 1 261 ? -3.375  -13.690 -7.672  1.00 15.44 ? 308 GLY A N   1 
ATOM   1964 C  CA  . GLY A 1 261 ? -3.933  -14.771 -8.462  1.00 17.51 ? 308 GLY A CA  1 
ATOM   1965 C  C   . GLY A 1 261 ? -3.667  -16.130 -7.837  1.00 17.95 ? 308 GLY A C   1 
ATOM   1966 O  O   . GLY A 1 261 ? -4.402  -17.082 -8.123  1.00 21.47 ? 308 GLY A O   1 
ATOM   1967 N  N   . LYS A 1 262 ? -2.663  -16.255 -6.983  1.00 15.32 ? 309 LYS A N   1 
ATOM   1968 C  CA  . LYS A 1 262 ? -2.259  -17.526 -6.432  1.00 14.54 ? 309 LYS A CA  1 
ATOM   1969 C  C   . LYS A 1 262 ? -2.726  -17.693 -5.001  1.00 15.59 ? 309 LYS A C   1 
ATOM   1970 O  O   . LYS A 1 262 ? -3.221  -16.742 -4.384  1.00 19.09 ? 309 LYS A O   1 
ATOM   1971 C  CB  . LYS A 1 262 ? -0.750  -17.697 -6.607  1.00 15.32 ? 309 LYS A CB  1 
ATOM   1972 C  CG  . LYS A 1 262 ? -0.287  -17.706 -8.039  1.00 15.65 ? 309 LYS A CG  1 
ATOM   1973 C  CD  . LYS A 1 262 ? 1.085   -18.309 -8.191  1.00 15.12 ? 309 LYS A CD  1 
ATOM   1974 C  CE  . LYS A 1 262 ? 1.482   -18.544 -9.588  1.00 15.16 ? 309 LYS A CE  1 
ATOM   1975 N  NZ  . LYS A 1 262 ? 2.788   -19.145 -9.675  1.00 13.24 ? 309 LYS A NZ  1 
ATOM   1976 N  N   . ALA A 1 263 ? -2.570  -18.902 -4.480  1.00 15.90 ? 310 ALA A N   1 
ATOM   1977 C  CA  . ALA A 1 263 ? -3.190  -19.303 -3.237  1.00 16.53 ? 310 ALA A CA  1 
ATOM   1978 C  C   . ALA A 1 263 ? -2.268  -19.147 -2.039  1.00 14.77 ? 310 ALA A C   1 
ATOM   1979 O  O   . ALA A 1 263 ? -2.755  -19.036 -0.929  1.00 17.70 ? 310 ALA A O   1 
ATOM   1980 C  CB  . ALA A 1 263 ? -3.699  -20.739 -3.363  1.00 20.20 ? 310 ALA A CB  1 
ATOM   1981 N  N   . LYS A 1 264 ? -0.953  -19.352 -2.210  1.00 13.92 ? 311 LYS A N   1 
ATOM   1982 C  CA  . LYS A 1 264 ? -0.094  -19.510 -1.069  1.00 14.51 ? 311 LYS A CA  1 
ATOM   1983 C  C   . LYS A 1 264 ? 1.081   -18.549 -1.144  1.00 12.90 ? 311 LYS A C   1 
ATOM   1984 O  O   . LYS A 1 264 ? 1.566   -18.252 -2.205  1.00 13.25 ? 311 LYS A O   1 
ATOM   1985 C  CB  . LYS A 1 264 ? 0.476   -20.933 -1.010  1.00 17.20 ? 311 LYS A CB  1 
ATOM   1986 C  CG  . LYS A 1 264 ? -0.626  -22.001 -0.821  1.00 20.82 ? 311 LYS A CG  1 
ATOM   1987 C  CD  . LYS A 1 264 ? -1.299  -21.968 0.534   1.00 24.17 ? 311 LYS A CD  1 
ATOM   1988 C  CE  . LYS A 1 264 ? -2.540  -22.810 0.543   1.00 28.31 ? 311 LYS A CE  1 
ATOM   1989 N  NZ  . LYS A 1 264 ? -3.255  -22.633 1.796   1.00 32.22 ? 311 LYS A NZ  1 
ATOM   1990 N  N   . GLU A 1 265 ? 1.523   -18.149 0.035   1.00 13.60 ? 312 GLU A N   1 
ATOM   1991 C  CA  . GLU A 1 265 ? 2.623   -17.213 0.203   1.00 11.72 ? 312 GLU A CA  1 
ATOM   1992 C  C   . GLU A 1 265 ? 3.804   -17.558 -0.699  1.00 12.80 ? 312 GLU A C   1 
ATOM   1993 O  O   . GLU A 1 265 ? 4.361   -16.683 -1.318  1.00 13.97 ? 312 GLU A O   1 
ATOM   1994 C  CB  . GLU A 1 265 ? 3.036   -17.184 1.655   1.00 12.01 ? 312 GLU A CB  1 
ATOM   1995 C  CG  . GLU A 1 265 ? 4.132   -16.167 1.901   1.00 12.94 ? 312 GLU A CG  1 
ATOM   1996 C  CD  . GLU A 1 265 ? 4.746   -16.161 3.268   1.00 12.31 ? 312 GLU A CD  1 
ATOM   1997 O  OE1 . GLU A 1 265 ? 4.151   -16.786 4.187   1.00 14.20 ? 312 GLU A OE1 1 
ATOM   1998 O  OE2 . GLU A 1 265 ? 5.856   -15.638 3.454   1.00 13.21 ? 312 GLU A OE2 1 
ATOM   1999 N  N   . ARG A 1 266 ? 4.227   -18.811 -0.658  1.00 12.37 ? 313 ARG A N   1 
ATOM   2000 C  CA  . ARG A 1 266 ? 5.481   -19.180 -1.284  1.00 13.43 ? 313 ARG A CA  1 
ATOM   2001 C  C   . ARG A 1 266 ? 5.293   -19.678 -2.707  1.00 13.37 ? 313 ARG A C   1 
ATOM   2002 O  O   . ARG A 1 266 ? 6.270   -20.121 -3.311  1.00 15.18 ? 313 ARG A O   1 
ATOM   2003 C  CB  . ARG A 1 266 ? 6.268   -20.198 -0.448  1.00 13.88 ? 313 ARG A CB  1 
ATOM   2004 C  CG  . ARG A 1 266 ? 6.692   -19.503 0.839   1.00 15.32 ? 313 ARG A CG  1 
ATOM   2005 C  CD  . ARG A 1 266 ? 7.646   -20.322 1.648   1.00 20.10 ? 313 ARG A CD  1 
ATOM   2006 N  NE  . ARG A 1 266 ? 8.166   -19.497 2.748   1.00 21.65 ? 313 ARG A NE  1 
ATOM   2007 C  CZ  . ARG A 1 266 ? 9.031   -18.469 2.649   1.00 20.35 ? 313 ARG A CZ  1 
ATOM   2008 N  NH1 . ARG A 1 266 ? 9.703   -18.232 1.551   1.00 21.41 ? 313 ARG A NH1 1 
ATOM   2009 N  NH2 . ARG A 1 266 ? 9.272   -17.716 3.704   1.00 22.53 ? 313 ARG A NH2 1 
ATOM   2010 N  N   . ASP A 1 267 ? 4.078   -19.603 -3.264  1.00 12.00 ? 314 ASP A N   1 
ATOM   2011 C  CA  . ASP A 1 267 ? 3.935   -19.815 -4.689  1.00 13.01 ? 314 ASP A CA  1 
ATOM   2012 C  C   . ASP A 1 267 ? 4.750   -18.763 -5.417  1.00 12.99 ? 314 ASP A C   1 
ATOM   2013 O  O   . ASP A 1 267 ? 4.863   -17.623 -4.934  1.00 13.77 ? 314 ASP A O   1 
ATOM   2014 C  CB  . ASP A 1 267 ? 2.491   -19.843 -5.115  1.00 13.63 ? 314 ASP A CB  1 
ATOM   2015 C  CG  . ASP A 1 267 ? 1.662   -21.003 -4.585  1.00 15.21 ? 314 ASP A CG  1 
ATOM   2016 O  OD1 . ASP A 1 267 ? 2.275   -22.074 -4.208  1.00 15.51 ? 314 ASP A OD1 1 
ATOM   2017 O  OD2 . ASP A 1 267 ? 0.401   -20.802 -4.532  1.00 16.78 ? 314 ASP A OD2 1 
ATOM   2018 N  N   . GLU A 1 268 ? 5.231   -19.069 -6.608  1.00 13.09 ? 315 GLU A N   1 
ATOM   2019 C  CA  . GLU A 1 268 ? 6.132   -18.157 -7.273  1.00 14.34 ? 315 GLU A CA  1 
ATOM   2020 C  C   . GLU A 1 268 ? 5.354   -17.025 -7.903  1.00 14.65 ? 315 GLU A C   1 
ATOM   2021 O  O   . GLU A 1 268 ? 4.288   -17.205 -8.488  1.00 15.15 ? 315 GLU A O   1 
ATOM   2022 C  CB  . GLU A 1 268 ? 6.964   -18.867 -8.334  1.00 18.51 ? 315 GLU A CB  1 
ATOM   2023 C  CG  . GLU A 1 268 ? 8.158   -19.605 -7.735  1.00 23.54 ? 315 GLU A CG  1 
ATOM   2024 C  CD  . GLU A 1 268 ? 9.083   -18.903 -6.753  1.00 23.76 ? 315 GLU A CD  1 
ATOM   2025 O  OE1 . GLU A 1 268 ? 9.549   -19.584 -5.808  1.00 29.64 ? 315 GLU A OE1 1 
ATOM   2026 O  OE2 . GLU A 1 268 ? 9.331   -17.675 -6.822  1.00 25.95 ? 315 GLU A OE2 1 
ATOM   2027 N  N   . PRO A 1 269 ? 5.832   -15.776 -7.831  1.00 13.81 ? 316 PRO A N   1 
ATOM   2028 C  CA  . PRO A 1 269 ? 5.109   -14.727 -8.512  1.00 13.99 ? 316 PRO A CA  1 
ATOM   2029 C  C   . PRO A 1 269 ? 5.026   -14.944 -10.005 1.00 15.32 ? 316 PRO A C   1 
ATOM   2030 O  O   . PRO A 1 269 ? 5.988   -15.359 -10.616 1.00 17.14 ? 316 PRO A O   1 
ATOM   2031 C  CB  . PRO A 1 269 ? 5.890   -13.445 -8.179  1.00 16.64 ? 316 PRO A CB  1 
ATOM   2032 C  CG  . PRO A 1 269 ? 6.957   -13.852 -7.237  1.00 19.80 ? 316 PRO A CG  1 
ATOM   2033 C  CD  . PRO A 1 269 ? 7.031   -15.354 -7.100  1.00 16.38 ? 316 PRO A CD  1 
ATOM   2034 N  N   . PHE A 1 270 ? 3.869   -14.601 -10.549 1.00 15.09 ? 317 PHE A N   1 
ATOM   2035 C  CA  . PHE A 1 270 ? 3.658   -14.430 -11.975 1.00 14.23 ? 317 PHE A CA  1 
ATOM   2036 C  C   . PHE A 1 270 ? 3.547   -12.938 -12.235 1.00 13.48 ? 317 PHE A C   1 
ATOM   2037 O  O   . PHE A 1 270 ? 2.512   -12.323 -12.000 1.00 15.02 ? 317 PHE A O   1 
ATOM   2038 C  CB  . PHE A 1 270 ? 2.463   -15.270 -12.414 1.00 15.96 ? 317 PHE A CB  1 
ATOM   2039 C  CG  . PHE A 1 270 ? 2.229   -15.241 -13.903 1.00 17.07 ? 317 PHE A CG  1 
ATOM   2040 C  CD1 . PHE A 1 270 ? 2.961   -16.057 -14.757 1.00 20.01 ? 317 PHE A CD1 1 
ATOM   2041 C  CD2 . PHE A 1 270 ? 1.180   -14.499 -14.425 1.00 19.13 ? 317 PHE A CD2 1 
ATOM   2042 C  CE1 . PHE A 1 270 ? 2.680   -16.060 -16.118 1.00 22.20 ? 317 PHE A CE1 1 
ATOM   2043 C  CE2 . PHE A 1 270 ? 0.916   -14.514 -15.780 1.00 19.99 ? 317 PHE A CE2 1 
ATOM   2044 C  CZ  . PHE A 1 270 ? 1.659   -15.299 -16.611 1.00 21.80 ? 317 PHE A CZ  1 
ATOM   2045 N  N   . LEU A 1 271 ? 4.650   -12.353 -12.685 1.00 15.14 ? 318 LEU A N   1 
ATOM   2046 C  CA  . LEU A 1 271 ? 4.780   -10.898 -12.622 1.00 15.09 ? 318 LEU A CA  1 
ATOM   2047 C  C   . LEU A 1 271 ? 3.797   -10.172 -13.540 1.00 16.17 ? 318 LEU A C   1 
ATOM   2048 O  O   . LEU A 1 271 ? 3.391   -9.043  -13.271 1.00 16.70 ? 318 LEU A O   1 
ATOM   2049 C  CB  . LEU A 1 271 ? 6.209   -10.474 -12.916 1.00 17.82 ? 318 LEU A CB  1 
ATOM   2050 C  CG  . LEU A 1 271 ? 7.291   -10.945 -11.930 1.00 19.61 ? 318 LEU A CG  1 
ATOM   2051 C  CD1 . LEU A 1 271 ? 8.640   -10.347 -12.335 1.00 22.97 ? 318 LEU A CD1 1 
ATOM   2052 C  CD2 . LEU A 1 271 ? 7.016   -10.621 -10.470 1.00 20.55 ? 318 LEU A CD2 1 
ATOM   2053 N  N   . LYS A 1 272 ? 3.409   -10.820 -14.639 1.00 17.22 ? 319 LYS A N   1 
ATOM   2054 C  CA  . LYS A 1 272 ? 2.592   -10.145 -15.636 1.00 19.47 ? 319 LYS A CA  1 
ATOM   2055 C  C   . LYS A 1 272 ? 1.182   -9.929  -15.125 1.00 18.85 ? 319 LYS A C   1 
ATOM   2056 O  O   . LYS A 1 272 ? 0.461   -9.082  -15.666 1.00 20.68 ? 319 LYS A O   1 
ATOM   2057 C  CB  . LYS A 1 272 ? 2.560   -10.922 -16.956 1.00 28.31 ? 319 LYS A CB  1 
ATOM   2058 C  CG  . LYS A 1 272 ? 3.847   -10.818 -17.751 1.00 32.08 ? 319 LYS A CG  1 
ATOM   2059 C  CD  . LYS A 1 272 ? 3.809   -11.625 -19.047 1.00 40.26 ? 319 LYS A CD  1 
ATOM   2060 C  CE  . LYS A 1 272 ? 5.156   -11.734 -19.686 1.00 47.95 ? 319 LYS A CE  1 
ATOM   2061 N  NZ  . LYS A 1 272 ? 5.757   -10.412 -19.890 1.00 50.40 ? 319 LYS A NZ  1 
ATOM   2062 N  N   . ALA A 1 273 ? 0.775   -10.617 -14.056 1.00 17.21 ? 320 ALA A N   1 
ATOM   2063 C  CA  . ALA A 1 273 ? -0.525  -10.407 -13.446 1.00 16.55 ? 320 ALA A CA  1 
ATOM   2064 C  C   . ALA A 1 273 ? -0.533  -9.197  -12.502 1.00 15.43 ? 320 ALA A C   1 
ATOM   2065 O  O   . ALA A 1 273 ? -1.596  -8.772  -12.088 1.00 19.15 ? 320 ALA A O   1 
ATOM   2066 C  CB  . ALA A 1 273 ? -0.981  -11.636 -12.699 1.00 18.19 ? 320 ALA A CB  1 
ATOM   2067 N  N   . MET A 1 274 ? 0.636   -8.684  -12.143 1.00 15.24 ? 321 MET A N   1 
ATOM   2068 C  CA  . MET A 1 274 ? 0.722   -7.553  -11.240 1.00 16.04 ? 321 MET A CA  1 
ATOM   2069 C  C   . MET A 1 274 ? 0.646   -6.271  -12.027 1.00 16.98 ? 321 MET A C   1 
ATOM   2070 O  O   . MET A 1 274 ? 0.990   -6.222  -13.214 1.00 19.08 ? 321 MET A O   1 
ATOM   2071 C  CB  . MET A 1 274 ? 2.035   -7.609  -10.475 1.00 15.00 ? 321 MET A CB  1 
ATOM   2072 C  CG  . MET A 1 274 ? 2.195   -8.829  -9.650  1.00 15.02 ? 321 MET A CG  1 
ATOM   2073 S  SD  . MET A 1 274 ? 3.800   -8.857  -8.860  1.00 16.32 ? 321 MET A SD  1 
ATOM   2074 C  CE  . MET A 1 274 ? 3.679   -10.472 -8.090  1.00 15.86 ? 321 MET A CE  1 
ATOM   2075 N  N   . LYS A 1 275 ? 0.266   -5.190  -11.366 1.00 16.40 ? 322 LYS A N   1 
ATOM   2076 C  CA  . LYS A 1 275 ? 0.318   -3.878  -11.972 1.00 17.02 ? 322 LYS A CA  1 
ATOM   2077 C  C   . LYS A 1 275 ? 1.755   -3.547  -12.340 1.00 17.14 ? 322 LYS A C   1 
ATOM   2078 O  O   . LYS A 1 275 ? 2.727   -3.985  -11.711 1.00 16.96 ? 322 LYS A O   1 
ATOM   2079 C  CB  . LYS A 1 275 ? -0.201  -2.785  -11.048 1.00 19.42 ? 322 LYS A CB  1 
ATOM   2080 C  CG  . LYS A 1 275 ? -1.603  -2.969  -10.585 1.00 25.06 ? 322 LYS A CG  1 
ATOM   2081 C  CD  . LYS A 1 275 ? -2.638  -2.685  -11.647 1.00 31.33 ? 322 LYS A CD  1 
ATOM   2082 C  CE  . LYS A 1 275 ? -4.003  -2.726  -11.018 1.00 36.46 ? 322 LYS A CE  1 
ATOM   2083 N  NZ  . LYS A 1 275 ? -5.085  -2.521  -11.983 1.00 46.40 ? 322 LYS A NZ  1 
ATOM   2084 N  N   . PRO A 1 276 ? 1.995   -2.722  -13.379 1.00 17.39 ? 323 PRO A N   1 
ATOM   2085 C  CA  . PRO A 1 276 ? 3.352   -2.462  -13.811 1.00 16.64 ? 323 PRO A CA  1 
ATOM   2086 C  C   . PRO A 1 276 ? 4.202   -1.706  -12.802 1.00 16.62 ? 323 PRO A C   1 
ATOM   2087 O  O   . PRO A 1 276 ? 5.422   -1.721  -12.939 1.00 20.49 ? 323 PRO A O   1 
ATOM   2088 C  CB  . PRO A 1 276 ? 3.176   -1.654  -15.128 1.00 21.49 ? 323 PRO A CB  1 
ATOM   2089 C  CG  . PRO A 1 276 ? 1.735   -1.241  -15.129 1.00 25.14 ? 323 PRO A CG  1 
ATOM   2090 C  CD  . PRO A 1 276 ? 0.943   -2.200  -14.287 1.00 20.19 ? 323 PRO A CD  1 
ATOM   2091 N  N   . ASP A 1 277 ? 3.539   -1.032  -11.867 1.00 15.42 ? 324 ASP A N   1 
ATOM   2092 C  CA  . ASP A 1 277 ? 4.229   -0.269  -10.841 1.00 15.64 ? 324 ASP A CA  1 
ATOM   2093 C  C   . ASP A 1 277 ? 4.190   -0.983  -9.501  1.00 14.58 ? 324 ASP A C   1 
ATOM   2094 O  O   . ASP A 1 277 ? 4.487   -0.356  -8.480  1.00 15.31 ? 324 ASP A O   1 
ATOM   2095 C  CB  . ASP A 1 277 ? 3.670   1.140   -10.697 1.00 18.74 ? 324 ASP A CB  1 
ATOM   2096 C  CG  . ASP A 1 277 ? 2.163   1.285   -10.485 1.00 21.89 ? 324 ASP A CG  1 
ATOM   2097 O  OD1 . ASP A 1 277 ? 1.429   0.256   -10.462 1.00 20.22 ? 324 ASP A OD1 1 
ATOM   2098 O  OD2 . ASP A 1 277 ? 1.708   2.444   -10.256 1.00 25.01 ? 324 ASP A OD2 1 
ATOM   2099 N  N   . ALA A 1 278 ? 3.802   -2.229  -9.473  1.00 13.81 ? 325 ALA A N   1 
ATOM   2100 C  CA  . ALA A 1 278 ? 3.752   -2.964  -8.212  1.00 13.36 ? 325 ALA A CA  1 
ATOM   2101 C  C   . ALA A 1 278 ? 5.172   -3.132  -7.702  1.00 12.02 ? 325 ALA A C   1 
ATOM   2102 O  O   . ALA A 1 278 ? 6.086   -3.484  -8.426  1.00 12.87 ? 325 ALA A O   1 
ATOM   2103 C  CB  . ALA A 1 278 ? 3.094   -4.294  -8.408  1.00 13.58 ? 325 ALA A CB  1 
ATOM   2104 N  N   . HIS A 1 279 ? 5.295   -3.009  -6.377  1.00 11.70 ? 326 HIS A N   1 
ATOM   2105 C  CA  . HIS A 1 279 ? 6.592   -3.119  -5.724  1.00 12.26 ? 326 HIS A CA  1 
ATOM   2106 C  C   . HIS A 1 279 ? 7.296   -4.441  -6.025  1.00 11.95 ? 326 HIS A C   1 
ATOM   2107 O  O   . HIS A 1 279 ? 8.465   -4.438  -6.355  1.00 12.72 ? 326 HIS A O   1 
ATOM   2108 C  CB  . HIS A 1 279 ? 6.395   -2.915  -4.221  1.00 11.23 ? 326 HIS A CB  1 
ATOM   2109 C  CG  . HIS A 1 279 ? 7.649   -3.004  -3.445  1.00 11.40 ? 326 HIS A CG  1 
ATOM   2110 N  ND1 . HIS A 1 279 ? 8.563   -1.998  -3.427  1.00 11.84 ? 326 HIS A ND1 1 
ATOM   2111 C  CD2 . HIS A 1 279 ? 8.145   -3.973  -2.612  1.00 10.67 ? 326 HIS A CD2 1 
ATOM   2112 C  CE1 . HIS A 1 279 ? 9.564   -2.346  -2.605  1.00 11.66 ? 326 HIS A CE1 1 
ATOM   2113 N  NE2 . HIS A 1 279 ? 9.337   -3.531  -2.091  1.00 11.31 ? 326 HIS A NE2 1 
ATOM   2114 N  N   . VAL A 1 280 ? 6.593   -5.576  -5.895  1.00 11.81 ? 327 VAL A N   1 
ATOM   2115 C  CA  . VAL A 1 280 ? 7.225   -6.870  -6.123  1.00 12.25 ? 327 VAL A CA  1 
ATOM   2116 C  C   . VAL A 1 280 ? 7.691   -6.996  -7.568  1.00 12.86 ? 327 VAL A C   1 
ATOM   2117 O  O   . VAL A 1 280 ? 8.780   -7.511  -7.831  1.00 14.41 ? 327 VAL A O   1 
ATOM   2118 C  CB  . VAL A 1 280 ? 6.322   -8.027  -5.698  1.00 12.99 ? 327 VAL A CB  1 
ATOM   2119 C  CG1 . VAL A 1 280 ? 6.891   -9.342  -6.189  1.00 13.98 ? 327 VAL A CG1 1 
ATOM   2120 C  CG2 . VAL A 1 280 ? 6.163   -8.013  -4.183  1.00 14.28 ? 327 VAL A CG2 1 
ATOM   2121 N  N   . ARG A 1 281 ? 6.851   -6.515  -8.470  1.00 13.00 ? 328 ARG A N   1 
ATOM   2122 C  CA  . ARG A 1 281 ? 7.227   -6.607  -9.871  1.00 13.78 ? 328 ARG A CA  1 
ATOM   2123 C  C   . ARG A 1 281 ? 8.494   -5.807  -10.146 1.00 14.67 ? 328 ARG A C   1 
ATOM   2124 O  O   . ARG A 1 281 ? 9.400   -6.316  -10.832 1.00 16.86 ? 328 ARG A O   1 
ATOM   2125 C  CB  . ARG A 1 281 ? 6.036   -6.134  -10.710 1.00 14.37 ? 328 ARG A CB  1 
ATOM   2126 C  CG  . ARG A 1 281 ? 6.316   -6.273  -12.206 1.00 16.96 ? 328 ARG A CG  1 
ATOM   2127 C  CD  . ARG A 1 281 ? 5.057   -6.147  -12.978 1.00 19.25 ? 328 ARG A CD  1 
ATOM   2128 N  NE  . ARG A 1 281 ? 5.339   -6.035  -14.417 1.00 23.61 ? 328 ARG A NE  1 
ATOM   2129 C  CZ  . ARG A 1 281 ? 4.378   -6.079  -15.332 1.00 24.53 ? 328 ARG A CZ  1 
ATOM   2130 N  NH1 . ARG A 1 281 ? 3.119   -6.126  -14.999 1.00 22.22 ? 328 ARG A NH1 1 
ATOM   2131 N  NH2 . ARG A 1 281 ? 4.693   -6.053  -16.618 1.00 29.02 ? 328 ARG A NH2 1 
ATOM   2132 N  N   . LEU A 1 282 ? 8.604   -4.606  -9.606  1.00 12.64 ? 329 LEU A N   1 
ATOM   2133 C  CA  . LEU A 1 282 ? 9.755   -3.771  -9.882  1.00 12.97 ? 329 LEU A CA  1 
ATOM   2134 C  C   . LEU A 1 282 ? 11.005  -4.250  -9.168  1.00 13.24 ? 329 LEU A C   1 
ATOM   2135 O  O   . LEU A 1 282 ? 12.108  -4.015  -9.626  1.00 14.58 ? 329 LEU A O   1 
ATOM   2136 C  CB  . LEU A 1 282 ? 9.446   -2.334  -9.516  1.00 14.23 ? 329 LEU A CB  1 
ATOM   2137 C  CG  . LEU A 1 282 ? 8.385   -1.650  -10.373 1.00 14.99 ? 329 LEU A CG  1 
ATOM   2138 C  CD1 . LEU A 1 282 ? 8.055   -0.315  -9.817  1.00 17.16 ? 329 LEU A CD1 1 
ATOM   2139 C  CD2 . LEU A 1 282 ? 8.818   -1.496  -11.814 1.00 18.22 ? 329 LEU A CD2 1 
ATOM   2140 N  N   . ALA A 1 283 ? 10.843  -4.889  -7.997  1.00 12.14 ? 330 ALA A N   1 
ATOM   2141 C  CA  . ALA A 1 283 ? 11.992  -5.245  -7.180  1.00 12.85 ? 330 ALA A CA  1 
ATOM   2142 C  C   . ALA A 1 283 ? 12.500  -6.633  -7.477  1.00 12.42 ? 330 ALA A C   1 
ATOM   2143 O  O   . ALA A 1 283 ? 13.577  -7.004  -7.028  1.00 13.72 ? 330 ALA A O   1 
ATOM   2144 C  CB  . ALA A 1 283 ? 11.566  -5.203  -5.718  1.00 13.31 ? 330 ALA A CB  1 
ATOM   2145 N  N   . HIS A 1 284 ? 11.725  -7.456  -8.192  1.00 12.61 ? 331 HIS A N   1 
ATOM   2146 C  CA  . HIS A 1 284 ? 12.054  -8.865  -8.398  1.00 13.72 ? 331 HIS A CA  1 
ATOM   2147 C  C   . HIS A 1 284 ? 13.345  -8.983  -9.183  1.00 13.70 ? 331 HIS A C   1 
ATOM   2148 O  O   . HIS A 1 284 ? 13.564  -8.167  -10.087 1.00 14.80 ? 331 HIS A O   1 
ATOM   2149 C  CB  . HIS A 1 284 ? 10.939  -9.542  -9.201  1.00 14.43 ? 331 HIS A CB  1 
ATOM   2150 C  CG  . HIS A 1 284 ? 10.959  -11.006 -9.224  1.00 14.11 ? 331 HIS A CG  1 
ATOM   2151 N  ND1 . HIS A 1 284 ? 11.791  -11.712 -10.070 1.00 16.72 ? 331 HIS A ND1 1 
ATOM   2152 C  CD2 . HIS A 1 284 ? 10.235  -11.914 -8.570  1.00 14.89 ? 331 HIS A CD2 1 
ATOM   2153 C  CE1 . HIS A 1 284 ? 11.571  -13.003 -9.910  1.00 15.55 ? 331 HIS A CE1 1 
ATOM   2154 N  NE2 . HIS A 1 284 ? 10.618  -13.179 -9.014  1.00 16.60 ? 331 HIS A NE2 1 
ATOM   2155 N  N   . PRO A 1 285 ? 14.214  -9.972  -8.891  1.00 13.89 ? 332 PRO A N   1 
ATOM   2156 C  CA  . PRO A 1 285 ? 15.446  -10.165 -9.662  1.00 15.66 ? 332 PRO A CA  1 
ATOM   2157 C  C   . PRO A 1 285 ? 15.232  -10.215 -11.170 1.00 16.86 ? 332 PRO A C   1 
ATOM   2158 O  O   . PRO A 1 285 ? 16.054  -9.640  -11.898 1.00 17.53 ? 332 PRO A O   1 
ATOM   2159 C  CB  . PRO A 1 285 ? 15.972  -11.498 -9.126  1.00 16.67 ? 332 PRO A CB  1 
ATOM   2160 C  CG  . PRO A 1 285 ? 15.495  -11.543 -7.720  1.00 17.41 ? 332 PRO A CG  1 
ATOM   2161 C  CD  . PRO A 1 285 ? 14.132  -10.931 -7.786  1.00 14.65 ? 332 PRO A CD  1 
ATOM   2162 N  N   . ASP A 1 286 ? 14.150  -10.823 -11.629 1.00 16.94 ? 333 ASP A N   1 
ATOM   2163 C  CA  . ASP A 1 286 ? 13.918  -10.964 -13.058 1.00 17.95 ? 333 ASP A CA  1 
ATOM   2164 C  C   . ASP A 1 286 ? 13.687  -9.610  -13.706 1.00 20.97 ? 333 ASP A C   1 
ATOM   2165 O  O   . ASP A 1 286 ? 13.802  -9.535  -14.943 1.00 23.00 ? 333 ASP A O   1 
ATOM   2166 C  CB  . ASP A 1 286 ? 12.709  -11.839 -13.355 1.00 20.61 ? 333 ASP A CB  1 
ATOM   2167 C  CG  . ASP A 1 286 ? 12.868  -13.323 -13.112 1.00 25.36 ? 333 ASP A CG  1 
ATOM   2168 O  OD1 . ASP A 1 286 ? 13.950  -13.721 -12.726 1.00 28.10 ? 333 ASP A OD1 1 
ATOM   2169 O  OD2 . ASP A 1 286 ? 11.865  -14.031 -13.257 1.00 28.85 ? 333 ASP A OD2 1 
ATOM   2170 N  N   . SER A 1 287 ? 13.282  -8.574  -12.950 1.00 15.91 ? 334 SER A N   1 
ATOM   2171 C  CA  . SER A 1 287 ? 13.090  -7.227  -13.456 1.00 16.34 ? 334 SER A CA  1 
ATOM   2172 C  C   . SER A 1 287 ? 14.382  -6.426  -13.396 1.00 17.86 ? 334 SER A C   1 
ATOM   2173 O  O   . SER A 1 287 ? 14.399  -5.286  -13.857 1.00 19.32 ? 334 SER A O   1 
ATOM   2174 C  CB  . SER A 1 287 ? 11.987  -6.506  -12.747 1.00 17.51 ? 334 SER A CB  1 
ATOM   2175 O  OG  . SER A 1 287 ? 10.797  -7.253  -12.864 1.00 19.90 ? 334 SER A OG  1 
ATOM   2176 N  N   . ASN A 1 288 ? 15.460  -7.002  -12.842 1.00 16.40 ? 335 ASN A N   1 
ATOM   2177 C  CA  . ASN A 1 288 ? 16.656  -6.242  -12.526 1.00 16.53 ? 335 ASN A CA  1 
ATOM   2178 C  C   . ASN A 1 288 ? 17.919  -6.971  -12.948 1.00 16.51 ? 335 ASN A C   1 
ATOM   2179 O  O   . ASN A 1 288 ? 18.968  -6.887  -12.310 1.00 18.50 ? 335 ASN A O   1 
ATOM   2180 C  CB  . ASN A 1 288 ? 16.753  -5.921  -11.047 1.00 15.71 ? 335 ASN A CB  1 
ATOM   2181 C  CG  . ASN A 1 288 ? 15.708  -4.935  -10.623 1.00 16.30 ? 335 ASN A CG  1 
ATOM   2182 O  OD1 . ASN A 1 288 ? 15.808  -3.726  -10.858 1.00 20.33 ? 335 ASN A OD1 1 
ATOM   2183 N  ND2 . ASN A 1 288 ? 14.645  -5.417  -10.002 1.00 15.88 ? 335 ASN A ND2 1 
ATOM   2184 N  N   . GLY A 1 289 ? 17.815  -7.697  -14.058 1.00 18.49 ? 336 GLY A N   1 
ATOM   2185 C  CA  . GLY A 1 289 ? 18.952  -8.402  -14.601 1.00 20.52 ? 336 GLY A CA  1 
ATOM   2186 C  C   . GLY A 1 289 ? 19.515  -9.439  -13.643 1.00 19.28 ? 336 GLY A C   1 
ATOM   2187 O  O   . GLY A 1 289 ? 20.708  -9.749  -13.700 1.00 22.35 ? 336 GLY A O   1 
ATOM   2188 N  N   . GLY A 1 290 ? 18.667  -9.993  -12.759 1.00 17.64 ? 337 GLY A N   1 
ATOM   2189 C  CA  . GLY A 1 290 ? 19.127  -10.992 -11.812 1.00 17.35 ? 337 GLY A CA  1 
ATOM   2190 C  C   . GLY A 1 290 ? 19.548  -10.445 -10.441 1.00 16.19 ? 337 GLY A C   1 
ATOM   2191 O  O   . GLY A 1 290 ? 19.877  -11.254 -9.585  1.00 19.41 ? 337 GLY A O   1 
ATOM   2192 N  N   . ALA A 1 291 ? 19.590  -9.133  -10.258 1.00 17.25 ? 338 ALA A N   1 
ATOM   2193 C  CA  . ALA A 1 291 ? 20.062  -8.516  -9.019  1.00 17.89 ? 338 ALA A CA  1 
ATOM   2194 C  C   . ALA A 1 291 ? 19.207  -9.002  -7.845  1.00 16.13 ? 338 ALA A C   1 
ATOM   2195 O  O   . ALA A 1 291 ? 17.983  -8.910  -7.885  1.00 16.75 ? 338 ALA A O   1 
ATOM   2196 C  CB  . ALA A 1 291 ? 20.004  -7.038  -9.109  1.00 18.65 ? 338 ALA A CB  1 
ATOM   2197 N  N   . THR A 1 292 ? 19.902  -9.558  -6.861  1.00 15.51 ? 339 THR A N   1 
ATOM   2198 C  CA  . THR A 1 292 ? 19.260  -10.197 -5.716  1.00 15.71 ? 339 THR A CA  1 
ATOM   2199 C  C   . THR A 1 292 ? 19.945  -9.648  -4.470  1.00 15.96 ? 339 THR A C   1 
ATOM   2200 O  O   . THR A 1 292 ? 21.167  -9.428  -4.471  1.00 19.38 ? 339 THR A O   1 
ATOM   2201 C  CB  . THR A 1 292 ? 19.383  -11.708 -5.792  1.00 17.31 ? 339 THR A CB  1 
ATOM   2202 O  OG1 . THR A 1 292 ? 18.868  -12.121 -7.059  1.00 18.67 ? 339 THR A OG1 1 
ATOM   2203 C  CG2 . THR A 1 292 ? 18.576  -12.408 -4.718  1.00 18.03 ? 339 THR A CG2 1 
ATOM   2204 N  N   . LEU A 1 293 ? 19.161  -9.385  -3.407  1.00 13.93 ? 340 LEU A N   1 
ATOM   2205 C  CA  . LEU A 1 293 ? 19.658  -8.795  -2.162  1.00 15.47 ? 340 LEU A CA  1 
ATOM   2206 C  C   . LEU A 1 293 ? 19.334  -9.682  -0.981  1.00 13.63 ? 340 LEU A C   1 
ATOM   2207 O  O   . LEU A 1 293 ? 18.406  -10.459 -1.059  1.00 14.96 ? 340 LEU A O   1 
ATOM   2208 C  CB  . LEU A 1 293 ? 18.840  -7.530  -1.869  1.00 18.91 ? 340 LEU A CB  1 
ATOM   2209 C  CG  . LEU A 1 293 ? 18.782  -6.455  -2.938  1.00 20.85 ? 340 LEU A CG  1 
ATOM   2210 C  CD1 . LEU A 1 293 ? 17.876  -5.291  -2.565  1.00 23.80 ? 340 LEU A CD1 1 
ATOM   2211 C  CD2 . LEU A 1 293 ? 20.181  -5.936  -3.143  1.00 26.69 ? 340 LEU A CD2 1 
ATOM   2212 N  N   . LEU A 1 294 ? 20.088  -9.571  0.098   1.00 11.74 ? 341 LEU A N   1 
ATOM   2213 C  CA  . LEU A 1 294 ? 19.650  -10.135 1.352   1.00 11.93 ? 341 LEU A CA  1 
ATOM   2214 C  C   . LEU A 1 294 ? 19.152  -8.983  2.220   1.00 11.95 ? 341 LEU A C   1 
ATOM   2215 O  O   . LEU A 1 294 ? 19.912  -8.153  2.682   1.00 12.99 ? 341 LEU A O   1 
ATOM   2216 C  CB  . LEU A 1 294 ? 20.784  -10.905 2.018   1.00 12.65 ? 341 LEU A CB  1 
ATOM   2217 C  CG  . LEU A 1 294 ? 20.404  -11.721 3.260   1.00 13.01 ? 341 LEU A CG  1 
ATOM   2218 C  CD1 . LEU A 1 294 ? 21.450  -12.786 3.537   1.00 16.26 ? 341 LEU A CD1 1 
ATOM   2219 C  CD2 . LEU A 1 294 ? 20.149  -10.889 4.498   1.00 15.41 ? 341 LEU A CD2 1 
ATOM   2220 N  N   . ARG A 1 295 ? 17.858  -8.955  2.405   1.00 11.07 ? 342 ARG A N   1 
ATOM   2221 C  CA  . ARG A 1 295 ? 17.177  -7.937  3.186   1.00 9.94  ? 342 ARG A CA  1 
ATOM   2222 C  C   . ARG A 1 295 ? 17.110  -8.370  4.639   1.00 10.79 ? 342 ARG A C   1 
ATOM   2223 O  O   . ARG A 1 295 ? 16.778  -9.518  4.923   1.00 12.71 ? 342 ARG A O   1 
ATOM   2224 C  CB  . ARG A 1 295 ? 15.765  -7.728  2.651   1.00 10.81 ? 342 ARG A CB  1 
ATOM   2225 C  CG  . ARG A 1 295 ? 15.716  -7.093  1.276   1.00 11.62 ? 342 ARG A CG  1 
ATOM   2226 C  CD  . ARG A 1 295 ? 14.355  -6.999  0.725   1.00 12.13 ? 342 ARG A CD  1 
ATOM   2227 N  NE  . ARG A 1 295 ? 13.879  -8.318  0.357   1.00 11.81 ? 342 ARG A NE  1 
ATOM   2228 C  CZ  . ARG A 1 295 ? 12.672  -8.778  0.526   1.00 11.43 ? 342 ARG A CZ  1 
ATOM   2229 N  NH1 . ARG A 1 295 ? 11.749  -8.106  1.153   1.00 12.01 ? 342 ARG A NH1 1 
ATOM   2230 N  NH2 . ARG A 1 295 ? 12.387  -10.007 0.129   1.00 13.29 ? 342 ARG A NH2 1 
ATOM   2231 N  N   . ARG A 1 296 ? 17.367  -7.452  5.554   1.00 10.86 ? 343 ARG A N   1 
ATOM   2232 C  CA  . ARG A 1 296 ? 17.489  -7.828  6.957   1.00 10.83 ? 343 ARG A CA  1 
ATOM   2233 C  C   . ARG A 1 296 ? 17.024  -6.705  7.860   1.00 11.33 ? 343 ARG A C   1 
ATOM   2234 O  O   . ARG A 1 296 ? 17.594  -6.475  8.905   1.00 12.53 ? 343 ARG A O   1 
ATOM   2235 C  CB  . ARG A 1 296 ? 18.921  -8.272  7.269   1.00 11.03 ? 343 ARG A CB  1 
ATOM   2236 C  CG  . ARG A 1 296 ? 18.924  -9.405  8.290   1.00 11.12 ? 343 ARG A CG  1 
ATOM   2237 C  CD  . ARG A 1 296 ? 20.345  -9.849  8.615   1.00 11.55 ? 343 ARG A CD  1 
ATOM   2238 N  NE  . ARG A 1 296 ? 20.417  -11.000 9.523   1.00 11.25 ? 343 ARG A NE  1 
ATOM   2239 C  CZ  . ARG A 1 296 ? 20.358  -10.940 10.838  1.00 12.34 ? 343 ARG A CZ  1 
ATOM   2240 N  NH1 . ARG A 1 296 ? 20.133  -9.803  11.448  1.00 12.21 ? 343 ARG A NH1 1 
ATOM   2241 N  NH2 . ARG A 1 296 ? 20.428  -12.073 11.542  1.00 12.34 ? 343 ARG A NH2 1 
ATOM   2242 N  N   . GLY A 1 297 ? 15.958  -6.016  7.474   1.00 10.56 ? 344 GLY A N   1 
ATOM   2243 C  CA  . GLY A 1 297 ? 15.530  -4.817  8.185   1.00 11.07 ? 344 GLY A CA  1 
ATOM   2244 C  C   . GLY A 1 297 ? 14.545  -5.086  9.292   1.00 10.04 ? 344 GLY A C   1 
ATOM   2245 O  O   . GLY A 1 297 ? 14.099  -6.199  9.553   1.00 10.57 ? 344 GLY A O   1 
ATOM   2246 N  N   . TYR A 1 298 ? 14.230  -3.972  9.970   1.00 10.09 ? 345 TYR A N   1 
ATOM   2247 C  CA  . TYR A 1 298 ? 13.419  -3.904  11.187  1.00 9.82  ? 345 TYR A CA  1 
ATOM   2248 C  C   . TYR A 1 298 ? 12.492  -2.714  11.135  1.00 10.45 ? 345 TYR A C   1 
ATOM   2249 O  O   . TYR A 1 298 ? 12.799  -1.703  10.507  1.00 12.78 ? 345 TYR A O   1 
ATOM   2250 C  CB  . TYR A 1 298 ? 14.321  -3.742  12.404  1.00 10.50 ? 345 TYR A CB  1 
ATOM   2251 C  CG  . TYR A 1 298 ? 15.099  -5.008  12.744  1.00 11.12 ? 345 TYR A CG  1 
ATOM   2252 C  CD1 . TYR A 1 298 ? 16.214  -5.421  12.034  1.00 12.11 ? 345 TYR A CD1 1 
ATOM   2253 C  CD2 . TYR A 1 298 ? 14.714  -5.774  13.812  1.00 11.42 ? 345 TYR A CD2 1 
ATOM   2254 C  CE1 . TYR A 1 298 ? 16.890  -6.584  12.361  1.00 11.61 ? 345 TYR A CE1 1 
ATOM   2255 C  CE2 . TYR A 1 298 ? 15.361  -6.948  14.160  1.00 11.14 ? 345 TYR A CE2 1 
ATOM   2256 C  CZ  . TYR A 1 298 ? 16.460  -7.336  13.433  1.00 11.28 ? 345 TYR A CZ  1 
ATOM   2257 O  OH  . TYR A 1 298 ? 17.125  -8.521  13.721  1.00 13.08 ? 345 TYR A OH  1 
ATOM   2258 N  N   . SER A 1 299 ? 11.407  -2.795  11.879  1.00 11.24 ? 346 SER A N   1 
ATOM   2259 C  CA  . SER A 1 299 ? 10.452  -1.690  12.053  1.00 10.72 ? 346 SER A CA  1 
ATOM   2260 C  C   . SER A 1 299 ? 10.915  -0.793  13.173  1.00 11.66 ? 346 SER A C   1 
ATOM   2261 O  O   . SER A 1 299 ? 11.558  -1.230  14.134  1.00 11.79 ? 346 SER A O   1 
ATOM   2262 C  CB  . SER A 1 299 ? 9.095   -2.185  12.417  1.00 11.73 ? 346 SER A CB  1 
ATOM   2263 O  OG  . SER A 1 299 ? 8.534   -2.892  11.334  1.00 13.73 ? 346 SER A OG  1 
ATOM   2264 N  N   . PHE A 1 300 ? 10.500  0.482   13.099  1.00 11.73 ? 347 PHE A N   1 
ATOM   2265 C  CA  . PHE A 1 300 ? 10.720  1.404   14.186  1.00 12.19 ? 347 PHE A CA  1 
ATOM   2266 C  C   . PHE A 1 300 ? 9.510   2.304   14.363  1.00 12.66 ? 347 PHE A C   1 
ATOM   2267 O  O   . PHE A 1 300 ? 8.698   2.509   13.458  1.00 12.41 ? 347 PHE A O   1 
ATOM   2268 C  CB  . PHE A 1 300 ? 11.987  2.241   14.044  1.00 13.17 ? 347 PHE A CB  1 
ATOM   2269 C  CG  . PHE A 1 300 ? 11.956  3.213   12.901  1.00 14.49 ? 347 PHE A CG  1 
ATOM   2270 C  CD1 . PHE A 1 300 ? 11.437  4.498   13.098  1.00 16.59 ? 347 PHE A CD1 1 
ATOM   2271 C  CD2 . PHE A 1 300 ? 12.537  2.939   11.674  1.00 15.40 ? 347 PHE A CD2 1 
ATOM   2272 C  CE1 . PHE A 1 300 ? 11.376  5.426   12.036  1.00 19.53 ? 347 PHE A CE1 1 
ATOM   2273 C  CE2 . PHE A 1 300 ? 12.524  3.859   10.660  1.00 18.49 ? 347 PHE A CE2 1 
ATOM   2274 C  CZ  . PHE A 1 300 ? 11.932  5.098   10.821  1.00 19.89 ? 347 PHE A CZ  1 
ATOM   2275 N  N   . THR A 1 301 ? 9.377   2.847   15.568  1.00 13.94 ? 348 THR A N   1 
ATOM   2276 C  CA  . THR A 1 301 ? 8.501   3.975   15.871  1.00 14.89 ? 348 THR A CA  1 
ATOM   2277 C  C   . THR A 1 301 ? 9.240   4.825   16.876  1.00 17.50 ? 348 THR A C   1 
ATOM   2278 O  O   . THR A 1 301 ? 9.653   4.338   17.924  1.00 21.71 ? 348 THR A O   1 
ATOM   2279 C  CB  . THR A 1 301 ? 7.124   3.555   16.330  1.00 18.29 ? 348 THR A CB  1 
ATOM   2280 O  OG1 . THR A 1 301 ? 6.508   4.812   16.631  1.00 20.08 ? 348 THR A OG1 1 
ATOM   2281 C  CG2 . THR A 1 301 ? 7.091   2.649   17.536  1.00 19.91 ? 348 THR A CG2 1 
ATOM   2282 N  N   . ASP A 1 302 ? 9.384   6.086   16.534  1.00 17.10 ? 349 ASP A N   1 
ATOM   2283 C  CA  . ASP A 1 302 ? 10.154  6.991   17.365  1.00 21.35 ? 349 ASP A CA  1 
ATOM   2284 C  C   . ASP A 1 302 ? 9.208   8.109   17.768  1.00 24.68 ? 349 ASP A C   1 
ATOM   2285 O  O   . ASP A 1 302 ? 9.315   9.242   17.307  1.00 35.71 ? 349 ASP A O   1 
ATOM   2286 C  CB  . ASP A 1 302 ? 11.405  7.506   16.649  1.00 29.64 ? 349 ASP A CB  1 
ATOM   2287 C  CG  . ASP A 1 302 ? 12.509  6.499   16.332  1.00 33.08 ? 349 ASP A CG  1 
ATOM   2288 O  OD1 . ASP A 1 302 ? 12.484  5.346   16.845  1.00 36.22 ? 349 ASP A OD1 1 
ATOM   2289 O  OD2 . ASP A 1 302 ? 13.385  6.847   15.521  1.00 48.55 ? 349 ASP A OD2 1 
ATOM   2290 N  N   . GLY A 1 303 ? 8.161   7.728   18.456  1.00 18.53 ? 350 GLY A N   1 
ATOM   2291 C  CA  . GLY A 1 303 ? 7.303   8.655   19.158  1.00 18.68 ? 350 GLY A CA  1 
ATOM   2292 C  C   . GLY A 1 303 ? 6.139   9.094   18.289  1.00 16.99 ? 350 GLY A C   1 
ATOM   2293 O  O   . GLY A 1 303 ? 5.579   8.329   17.523  1.00 20.26 ? 350 GLY A O   1 
ATOM   2294 N  N   . THR A 1 304 ? 5.740   10.336  18.487  1.00 18.03 ? 351 THR A N   1 
ATOM   2295 C  CA  . THR A 1 304 ? 4.802   11.009  17.606  1.00 16.84 ? 351 THR A CA  1 
ATOM   2296 C  C   . THR A 1 304 ? 5.541   11.969  16.687  1.00 21.52 ? 351 THR A C   1 
ATOM   2297 O  O   . THR A 1 304 ? 6.704   12.329  16.867  1.00 22.70 ? 351 THR A O   1 
ATOM   2298 C  CB  . THR A 1 304 ? 3.744   11.719  18.432  1.00 20.88 ? 351 THR A CB  1 
ATOM   2299 O  OG1 . THR A 1 304 ? 4.406   12.735  19.185  1.00 28.02 ? 351 THR A OG1 1 
ATOM   2300 C  CG2 . THR A 1 304 ? 2.959   10.787  19.317  1.00 21.68 ? 351 THR A CG2 1 
ATOM   2301 N  N   . ASP A 1 305 ? 4.824   12.437  15.670  1.00 18.43 ? 352 ASP A N   1 
ATOM   2302 C  CA  . ASP A 1 305 ? 5.394   13.327  14.676  1.00 19.11 ? 352 ASP A CA  1 
ATOM   2303 C  C   . ASP A 1 305 ? 5.104   14.779  15.001  1.00 18.49 ? 352 ASP A C   1 
ATOM   2304 O  O   . ASP A 1 305 ? 5.413   15.668  14.196  1.00 22.69 ? 352 ASP A O   1 
ATOM   2305 C  CB  . ASP A 1 305 ? 4.844   12.981  13.309  1.00 19.70 ? 352 ASP A CB  1 
ATOM   2306 C  CG  . ASP A 1 305 ? 3.341   13.082  13.144  1.00 18.48 ? 352 ASP A CG  1 
ATOM   2307 O  OD1 . ASP A 1 305 ? 2.608   13.519  14.097  1.00 16.44 ? 352 ASP A OD1 1 
ATOM   2308 O  OD2 . ASP A 1 305 ? 2.935   12.613  12.064  1.00 20.80 ? 352 ASP A OD2 1 
ATOM   2309 N  N   . GLY A 1 306 ? 4.473   15.060  16.122  1.00 16.00 ? 353 GLY A N   1 
ATOM   2310 C  CA  . GLY A 1 306 ? 4.113   16.397  16.555  1.00 17.86 ? 353 GLY A CA  1 
ATOM   2311 C  C   . GLY A 1 306 ? 2.862   16.959  15.875  1.00 17.86 ? 353 GLY A C   1 
ATOM   2312 O  O   . GLY A 1 306 ? 2.418   18.073  16.162  1.00 21.90 ? 353 GLY A O   1 
ATOM   2313 N  N   . LEU A 1 307 ? 2.239   16.137  15.033  1.00 16.64 ? 354 LEU A N   1 
ATOM   2314 C  CA  . LEU A 1 307 ? 1.046   16.493  14.269  1.00 17.50 ? 354 LEU A CA  1 
ATOM   2315 C  C   . LEU A 1 307 ? -0.088  15.550  14.635  1.00 15.82 ? 354 LEU A C   1 
ATOM   2316 O  O   . LEU A 1 307 ? -1.011  15.356  13.868  1.00 16.93 ? 354 LEU A O   1 
ATOM   2317 C  CB  . LEU A 1 307 ? 1.355   16.419  12.775  1.00 18.86 ? 354 LEU A CB  1 
ATOM   2318 C  CG  . LEU A 1 307 ? 2.460   17.376  12.320  1.00 22.05 ? 354 LEU A CG  1 
ATOM   2319 C  CD1 . LEU A 1 307 ? 2.964   16.929  10.977  1.00 26.08 ? 354 LEU A CD1 1 
ATOM   2320 C  CD2 . LEU A 1 307 ? 2.014   18.828  12.273  1.00 25.84 ? 354 LEU A CD2 1 
ATOM   2321 N  N   . GLY A 1 308 ? -0.014  14.908  15.803  1.00 13.47 ? 355 GLY A N   1 
ATOM   2322 C  CA  . GLY A 1 308 ? -1.156  14.168  16.276  1.00 12.36 ? 355 GLY A CA  1 
ATOM   2323 C  C   . GLY A 1 308 ? -1.096  12.709  15.880  1.00 12.35 ? 355 GLY A C   1 
ATOM   2324 O  O   . GLY A 1 308 ? -2.069  12.008  16.118  1.00 13.00 ? 355 GLY A O   1 
ATOM   2325 N  N   . ARG A 1 309 ? 0.012   12.240  15.326  1.00 11.97 ? 356 ARG A N   1 
ATOM   2326 C  CA  . ARG A 1 309 ? 0.070   10.886  14.797  1.00 12.18 ? 356 ARG A CA  1 
ATOM   2327 C  C   . ARG A 1 309 ? 1.275   10.132  15.329  1.00 13.05 ? 356 ARG A C   1 
ATOM   2328 O  O   . ARG A 1 309 ? 2.296   10.710  15.662  1.00 14.64 ? 356 ARG A O   1 
ATOM   2329 C  CB  . ARG A 1 309 ? 0.241   10.899  13.277  1.00 13.59 ? 356 ARG A CB  1 
ATOM   2330 C  CG  . ARG A 1 309 ? -0.879  11.693  12.620  1.00 14.16 ? 356 ARG A CG  1 
ATOM   2331 C  CD  . ARG A 1 309 ? -0.736  11.799  11.130  1.00 15.20 ? 356 ARG A CD  1 
ATOM   2332 N  NE  . ARG A 1 309 ? 0.507   12.517  10.817  1.00 15.08 ? 356 ARG A NE  1 
ATOM   2333 C  CZ  . ARG A 1 309 ? 0.917   12.660  9.584   1.00 15.09 ? 356 ARG A CZ  1 
ATOM   2334 N  NH1 . ARG A 1 309 ? 0.110   12.404  8.576   1.00 15.03 ? 356 ARG A NH1 1 
ATOM   2335 N  NH2 . ARG A 1 309 ? 2.119   13.120  9.393   1.00 16.54 ? 356 ARG A NH2 1 
ATOM   2336 N  N   . LEU A 1 310 ? 1.200   8.793   15.289  1.00 13.95 ? 357 LEU A N   1 
ATOM   2337 C  CA  . LEU A 1 310 ? 2.378   7.992   15.526  1.00 15.08 ? 357 LEU A CA  1 
ATOM   2338 C  C   . LEU A 1 310 ? 3.377   8.153   14.411  1.00 15.78 ? 357 LEU A C   1 
ATOM   2339 O  O   . LEU A 1 310 ? 2.944   8.218   13.283  1.00 19.15 ? 357 LEU A O   1 
ATOM   2340 C  CB  . LEU A 1 310 ? 1.990   6.520   15.561  1.00 17.72 ? 357 LEU A CB  1 
ATOM   2341 C  CG  . LEU A 1 310 ? 1.198   6.080   16.772  1.00 20.02 ? 357 LEU A CG  1 
ATOM   2342 C  CD1 . LEU A 1 310 ? 0.947   4.589   16.602  1.00 22.53 ? 357 LEU A CD1 1 
ATOM   2343 C  CD2 . LEU A 1 310 ? 1.939   6.322   18.052  1.00 21.85 ? 357 LEU A CD2 1 
ATOM   2344 N  N   . ASP A 1 311 ? 4.647   8.172   14.752  1.00 16.27 ? 358 ASP A N   1 
ATOM   2345 C  CA  . ASP A 1 311 ? 5.725   8.059   13.805  1.00 18.66 ? 358 ASP A CA  1 
ATOM   2346 C  C   . ASP A 1 311 ? 5.862   6.561   13.531  1.00 21.89 ? 358 ASP A C   1 
ATOM   2347 O  O   . ASP A 1 311 ? 5.637   5.672   14.373  1.00 24.25 ? 358 ASP A O   1 
ATOM   2348 C  CB  . ASP A 1 311 ? 6.964   8.655   14.440  1.00 25.25 ? 358 ASP A CB  1 
ATOM   2349 C  CG  . ASP A 1 311 ? 8.219   8.324   13.659  1.00 31.65 ? 358 ASP A CG  1 
ATOM   2350 O  OD1 . ASP A 1 311 ? 8.438   9.037   12.666  1.00 32.86 ? 358 ASP A OD1 1 
ATOM   2351 O  OD2 . ASP A 1 311 ? 8.882   7.309   14.006  1.00 30.23 ? 358 ASP A OD2 1 
ATOM   2352 N  N   . ALA A 1 312 ? 6.137   6.216   12.300  1.00 16.38 ? 359 ALA A N   1 
ATOM   2353 C  CA  . ALA A 1 312 ? 6.327   4.802   11.973  1.00 17.82 ? 359 ALA A CA  1 
ATOM   2354 C  C   . ALA A 1 312 ? 7.295   4.753   10.819  1.00 14.95 ? 359 ALA A C   1 
ATOM   2355 O  O   . ALA A 1 312 ? 7.216   5.539   9.892   1.00 15.45 ? 359 ALA A O   1 
ATOM   2356 C  CB  . ALA A 1 312 ? 5.031   4.130   11.595  1.00 23.72 ? 359 ALA A CB  1 
ATOM   2357 N  N   . GLY A 1 313 ? 8.118   3.721   10.792  1.00 12.57 ? 360 GLY A N   1 
ATOM   2358 C  CA  . GLY A 1 313 ? 8.966   3.509   9.659   1.00 14.75 ? 360 GLY A CA  1 
ATOM   2359 C  C   . GLY A 1 313 ? 9.587   2.121   9.648   1.00 12.03 ? 360 GLY A C   1 
ATOM   2360 O  O   . GLY A 1 313 ? 9.221   1.211   10.397  1.00 12.82 ? 360 GLY A O   1 
ATOM   2361 N  N   . LEU A 1 314 ? 10.457  2.014   8.676   1.00 12.35 ? 361 LEU A N   1 
ATOM   2362 C  CA  . LEU A 1 314 ? 11.190  0.779   8.457   1.00 11.45 ? 361 LEU A CA  1 
ATOM   2363 C  C   . LEU A 1 314 ? 12.631  1.155   8.277   1.00 11.05 ? 361 LEU A C   1 
ATOM   2364 O  O   . LEU A 1 314 ? 12.958  2.030   7.488   1.00 12.54 ? 361 LEU A O   1 
ATOM   2365 C  CB  . LEU A 1 314 ? 10.560  0.076   7.252   1.00 13.07 ? 361 LEU A CB  1 
ATOM   2366 C  CG  . LEU A 1 314 ? 10.911  -1.395  7.070   1.00 14.91 ? 361 LEU A CG  1 
ATOM   2367 C  CD1 . LEU A 1 314 ? 9.863   -2.179  6.339   1.00 14.71 ? 361 LEU A CD1 1 
ATOM   2368 C  CD2 . LEU A 1 314 ? 12.196  -1.554  6.343   1.00 16.06 ? 361 LEU A CD2 1 
ATOM   2369 N  N   . PHE A 1 315 ? 13.515  0.485   9.036   1.00 10.21 ? 362 PHE A N   1 
ATOM   2370 C  CA  . PHE A 1 315 ? 14.937  0.645   8.933   1.00 10.92 ? 362 PHE A CA  1 
ATOM   2371 C  C   . PHE A 1 315 ? 15.402  -0.489  8.036   1.00 10.54 ? 362 PHE A C   1 
ATOM   2372 O  O   . PHE A 1 315 ? 15.530  -1.639  8.442   1.00 11.87 ? 362 PHE A O   1 
ATOM   2373 C  CB  . PHE A 1 315 ? 15.575  0.639   10.323  1.00 11.45 ? 362 PHE A CB  1 
ATOM   2374 C  CG  . PHE A 1 315 ? 17.052  0.965   10.250  1.00 13.45 ? 362 PHE A CG  1 
ATOM   2375 C  CD1 . PHE A 1 315 ? 17.491  2.217   9.858   1.00 15.71 ? 362 PHE A CD1 1 
ATOM   2376 C  CD2 . PHE A 1 315 ? 17.999  0.046   10.655  1.00 14.46 ? 362 PHE A CD2 1 
ATOM   2377 C  CE1 . PHE A 1 315 ? 18.853  2.528   9.845   1.00 16.79 ? 362 PHE A CE1 1 
ATOM   2378 C  CE2 . PHE A 1 315 ? 19.341  0.403   10.707  1.00 15.53 ? 362 PHE A CE2 1 
ATOM   2379 C  CZ  . PHE A 1 315 ? 19.762  1.619   10.263  1.00 15.08 ? 362 PHE A CZ  1 
ATOM   2380 N  N   . PHE A 1 316 ? 15.563  -0.172  6.777   1.00 10.93 ? 363 PHE A N   1 
ATOM   2381 C  CA  . PHE A 1 316 ? 15.872  -1.118  5.731   1.00 10.78 ? 363 PHE A CA  1 
ATOM   2382 C  C   . PHE A 1 316 ? 17.362  -1.394  5.723   1.00 11.40 ? 363 PHE A C   1 
ATOM   2383 O  O   . PHE A 1 316 ? 18.165  -0.487  5.680   1.00 12.87 ? 363 PHE A O   1 
ATOM   2384 C  CB  . PHE A 1 316 ? 15.418  -0.488  4.407   1.00 11.93 ? 363 PHE A CB  1 
ATOM   2385 C  CG  . PHE A 1 316 ? 15.635  -1.399  3.222   1.00 12.67 ? 363 PHE A CG  1 
ATOM   2386 C  CD1 . PHE A 1 316 ? 14.669  -2.325  2.880   1.00 13.73 ? 363 PHE A CD1 1 
ATOM   2387 C  CD2 . PHE A 1 316 ? 16.787  -1.340  2.495   1.00 14.21 ? 363 PHE A CD2 1 
ATOM   2388 C  CE1 . PHE A 1 316 ? 14.876  -3.180  1.797   1.00 15.61 ? 363 PHE A CE1 1 
ATOM   2389 C  CE2 . PHE A 1 316 ? 16.952  -2.169  1.408   1.00 16.25 ? 363 PHE A CE2 1 
ATOM   2390 C  CZ  . PHE A 1 316 ? 16.020  -3.105  1.102   1.00 16.51 ? 363 PHE A CZ  1 
ATOM   2391 N  N   . LEU A 1 317 ? 17.747  -2.664  5.799   1.00 10.99 ? 364 LEU A N   1 
ATOM   2392 C  CA  . LEU A 1 317 ? 19.130  -3.108  5.717   1.00 12.35 ? 364 LEU A CA  1 
ATOM   2393 C  C   . LEU A 1 317 ? 19.235  -4.117  4.597   1.00 12.80 ? 364 LEU A C   1 
ATOM   2394 O  O   . LEU A 1 317 ? 18.444  -5.063  4.524   1.00 14.53 ? 364 LEU A O   1 
ATOM   2395 C  CB  . LEU A 1 317 ? 19.544  -3.747  7.033   1.00 12.83 ? 364 LEU A CB  1 
ATOM   2396 C  CG  . LEU A 1 317 ? 19.610  -2.805  8.220   1.00 13.09 ? 364 LEU A CG  1 
ATOM   2397 C  CD1 . LEU A 1 317 ? 19.780  -3.567  9.521   1.00 14.00 ? 364 LEU A CD1 1 
ATOM   2398 C  CD2 . LEU A 1 317 ? 20.748  -1.819  8.055   1.00 15.40 ? 364 LEU A CD2 1 
ATOM   2399 N  N   . ALA A 1 318 ? 20.207  -3.929  3.727   1.00 11.79 ? 365 ALA A N   1 
ATOM   2400 C  CA  . ALA A 1 318 ? 20.431  -4.920  2.697   1.00 13.00 ? 365 ALA A CA  1 
ATOM   2401 C  C   . ALA A 1 318 ? 21.911  -5.223  2.582   1.00 12.66 ? 365 ALA A C   1 
ATOM   2402 O  O   . ALA A 1 318 ? 22.722  -4.303  2.581   1.00 12.97 ? 365 ALA A O   1 
ATOM   2403 C  CB  . ALA A 1 318 ? 19.950  -4.432  1.376   1.00 16.22 ? 365 ALA A CB  1 
ATOM   2404 N  N   . TYR A 1 319 ? 22.196  -6.512  2.497   1.00 11.94 ? 366 TYR A N   1 
ATOM   2405 C  CA  . TYR A 1 319 ? 23.543  -7.007  2.318   1.00 12.09 ? 366 TYR A CA  1 
ATOM   2406 C  C   . TYR A 1 319 ? 23.666  -7.532  0.894   1.00 12.89 ? 366 TYR A C   1 
ATOM   2407 O  O   . TYR A 1 319 ? 22.733  -8.118  0.339   1.00 13.79 ? 366 TYR A O   1 
ATOM   2408 C  CB  . TYR A 1 319 ? 23.840  -8.116  3.316   1.00 13.16 ? 366 TYR A CB  1 
ATOM   2409 C  CG  . TYR A 1 319 ? 23.985  -7.653  4.742   1.00 12.99 ? 366 TYR A CG  1 
ATOM   2410 C  CD1 . TYR A 1 319 ? 25.208  -7.246  5.223   1.00 13.32 ? 366 TYR A CD1 1 
ATOM   2411 C  CD2 . TYR A 1 319 ? 22.901  -7.591  5.589   1.00 13.50 ? 366 TYR A CD2 1 
ATOM   2412 C  CE1 . TYR A 1 319 ? 25.383  -6.795  6.507   1.00 14.36 ? 366 TYR A CE1 1 
ATOM   2413 C  CE2 . TYR A 1 319 ? 23.047  -7.113  6.874   1.00 13.63 ? 366 TYR A CE2 1 
ATOM   2414 C  CZ  . TYR A 1 319 ? 24.297  -6.753  7.339   1.00 14.86 ? 366 TYR A CZ  1 
ATOM   2415 O  OH  . TYR A 1 319 ? 24.487  -6.300  8.601   1.00 17.07 ? 366 TYR A OH  1 
ATOM   2416 N  N   . GLN A 1 320 ? 24.853  -7.322  0.321   1.00 12.29 ? 367 GLN A N   1 
ATOM   2417 C  CA  . GLN A 1 320 ? 25.103  -7.716  -1.054  1.00 13.12 ? 367 GLN A CA  1 
ATOM   2418 C  C   . GLN A 1 320 ? 26.594  -7.779  -1.305  1.00 12.94 ? 367 GLN A C   1 
ATOM   2419 O  O   . GLN A 1 320 ? 27.371  -7.164  -0.631  1.00 13.26 ? 367 GLN A O   1 
ATOM   2420 C  CB  . GLN A 1 320 ? 24.457  -6.733  -2.015  1.00 13.68 ? 367 GLN A CB  1 
ATOM   2421 C  CG  . GLN A 1 320 ? 24.972  -5.306  -1.935  1.00 13.93 ? 367 GLN A CG  1 
ATOM   2422 C  CD  . GLN A 1 320 ? 23.973  -4.358  -1.322  1.00 15.58 ? 367 GLN A CD  1 
ATOM   2423 O  OE1 . GLN A 1 320 ? 23.051  -3.923  -2.010  1.00 21.07 ? 367 GLN A OE1 1 
ATOM   2424 N  NE2 . GLN A 1 320 ? 24.053  -4.067  -0.038  1.00 15.08 ? 367 GLN A NE2 1 
ATOM   2425 N  N   . ARG A 1 321 ? 26.942  -8.496  -2.370  1.00 13.29 ? 368 ARG A N   1 
ATOM   2426 C  CA  . ARG A 1 321 ? 28.328  -8.678  -2.782  1.00 14.50 ? 368 ARG A CA  1 
ATOM   2427 C  C   . ARG A 1 321 ? 28.925  -7.422  -3.397  1.00 15.43 ? 368 ARG A C   1 
ATOM   2428 O  O   . ARG A 1 321 ? 30.120  -7.232  -3.282  1.00 16.08 ? 368 ARG A O   1 
ATOM   2429 C  CB  . ARG A 1 321 ? 28.317  -9.856  -3.753  1.00 15.44 ? 368 ARG A CB  1 
ATOM   2430 C  CG  . ARG A 1 321 ? 29.640  -10.117 -4.445  1.00 16.34 ? 368 ARG A CG  1 
ATOM   2431 C  CD  . ARG A 1 321 ? 29.548  -11.490 -5.087  1.00 16.83 ? 368 ARG A CD  1 
ATOM   2432 N  NE  . ARG A 1 321 ? 30.799  -11.746 -5.812  1.00 20.17 ? 368 ARG A NE  1 
ATOM   2433 C  CZ  . ARG A 1 321 ? 30.920  -12.754 -6.652  1.00 23.57 ? 368 ARG A CZ  1 
ATOM   2434 N  NH1 . ARG A 1 321 ? 29.909  -13.549 -6.903  1.00 26.19 ? 368 ARG A NH1 1 
ATOM   2435 N  NH2 . ARG A 1 321 ? 32.079  -12.976 -7.249  1.00 27.70 ? 368 ARG A NH2 1 
ATOM   2436 N  N   . ASP A 1 322 ? 28.107  -6.533  -3.930  1.00 14.44 ? 369 ASP A N   1 
ATOM   2437 C  CA  . ASP A 1 322 ? 28.574  -5.294  -4.524  1.00 16.16 ? 369 ASP A CA  1 
ATOM   2438 C  C   . ASP A 1 322 ? 27.405  -4.316  -4.531  1.00 14.97 ? 369 ASP A C   1 
ATOM   2439 O  O   . ASP A 1 322 ? 26.361  -4.614  -5.081  1.00 15.76 ? 369 ASP A O   1 
ATOM   2440 C  CB  . ASP A 1 322 ? 29.109  -5.555  -5.920  1.00 16.81 ? 369 ASP A CB  1 
ATOM   2441 C  CG  . ASP A 1 322 ? 29.827  -4.379  -6.549  1.00 18.25 ? 369 ASP A CG  1 
ATOM   2442 O  OD1 . ASP A 1 322 ? 29.458  -3.234  -6.331  1.00 17.99 ? 369 ASP A OD1 1 
ATOM   2443 O  OD2 . ASP A 1 322 ? 30.788  -4.674  -7.323  1.00 22.31 ? 369 ASP A OD2 1 
ATOM   2444 N  N   . ILE A 1 323 ? 27.566  -3.145  -3.948  1.00 14.49 ? 370 ILE A N   1 
ATOM   2445 C  CA  . ILE A 1 323 ? 26.466  -2.189  -3.910  1.00 15.78 ? 370 ILE A CA  1 
ATOM   2446 C  C   . ILE A 1 323 ? 26.022  -1.809  -5.325  1.00 17.32 ? 370 ILE A C   1 
ATOM   2447 O  O   . ILE A 1 323 ? 24.840  -1.523  -5.573  1.00 16.98 ? 370 ILE A O   1 
ATOM   2448 C  CB  . ILE A 1 323 ? 26.857  -0.966  -3.089  1.00 16.15 ? 370 ILE A CB  1 
ATOM   2449 C  CG1 . ILE A 1 323 ? 26.970  -1.359  -1.616  1.00 18.70 ? 370 ILE A CG1 1 
ATOM   2450 C  CG2 . ILE A 1 323 ? 25.842  0.173   -3.260  1.00 19.10 ? 370 ILE A CG2 1 
ATOM   2451 C  CD1 . ILE A 1 323 ? 27.648  -0.320  -0.766  1.00 19.33 ? 370 ILE A CD1 1 
ATOM   2452 N  N   . ARG A 1 324 ? 26.987  -1.794  -6.242  1.00 16.81 ? 371 ARG A N   1 
ATOM   2453 C  CA  . ARG A 1 324 ? 26.698  -1.340  -7.586  1.00 18.68 ? 371 ARG A CA  1 
ATOM   2454 C  C   . ARG A 1 324 ? 25.816  -2.335  -8.312  1.00 17.99 ? 371 ARG A C   1 
ATOM   2455 O  O   . ARG A 1 324 ? 25.120  -1.905  -9.254  1.00 20.06 ? 371 ARG A O   1 
ATOM   2456 C  CB  . ARG A 1 324 ? 28.012  -1.177  -8.347  1.00 18.32 ? 371 ARG A CB  1 
ATOM   2457 C  CG  . ARG A 1 324 ? 28.855  -0.077  -7.725  1.00 20.91 ? 371 ARG A CG  1 
ATOM   2458 C  CD  . ARG A 1 324 ? 30.226  -0.071  -8.370  1.00 21.45 ? 371 ARG A CD  1 
ATOM   2459 N  NE  . ARG A 1 324 ? 30.924  -1.337  -8.154  1.00 22.90 ? 371 ARG A NE  1 
ATOM   2460 C  CZ  . ARG A 1 324 ? 32.108  -1.700  -8.649  1.00 26.40 ? 371 ARG A CZ  1 
ATOM   2461 N  NH1 . ARG A 1 324 ? 32.743  -0.920  -9.527  1.00 28.10 ? 371 ARG A NH1 1 
ATOM   2462 N  NH2 . ARG A 1 324 ? 32.656  -2.841  -8.294  1.00 26.61 ? 371 ARG A NH2 1 
ATOM   2463 N  N   . THR A 1 325 ? 25.803  -3.618  -7.929  1.00 17.49 ? 372 THR A N   1 
ATOM   2464 C  CA  . THR A 1 325 ? 25.024  -4.646  -8.610  1.00 18.39 ? 372 THR A CA  1 
ATOM   2465 C  C   . THR A 1 325 ? 23.868  -5.173  -7.758  1.00 18.79 ? 372 THR A C   1 
ATOM   2466 O  O   . THR A 1 325 ? 23.217  -6.153  -8.112  1.00 21.29 ? 372 THR A O   1 
ATOM   2467 C  CB  . THR A 1 325 ? 25.907  -5.799  -9.077  1.00 21.44 ? 372 THR A CB  1 
ATOM   2468 O  OG1 . THR A 1 325 ? 26.562  -6.378  -7.957  1.00 21.60 ? 372 THR A OG1 1 
ATOM   2469 C  CG2 . THR A 1 325 ? 26.982  -5.339  -10.051 1.00 24.05 ? 372 THR A CG2 1 
ATOM   2470 N  N   . GLY A 1 326 ? 23.683  -4.592  -6.580  1.00 17.30 ? 373 GLY A N   1 
ATOM   2471 C  CA  . GLY A 1 326 ? 22.657  -5.055  -5.658  1.00 15.83 ? 373 GLY A CA  1 
ATOM   2472 C  C   . GLY A 1 326 ? 21.650  -3.941  -5.450  1.00 14.87 ? 373 GLY A C   1 
ATOM   2473 O  O   . GLY A 1 326 ? 20.733  -3.736  -6.239  1.00 17.00 ? 373 GLY A O   1 
ATOM   2474 N  N   . PHE A 1 327 ? 21.839  -3.150  -4.411  1.00 14.76 ? 374 PHE A N   1 
ATOM   2475 C  CA  . PHE A 1 327 ? 20.864  -2.140  -4.054  1.00 14.54 ? 374 PHE A CA  1 
ATOM   2476 C  C   . PHE A 1 327 ? 20.658  -1.108  -5.163  1.00 16.39 ? 374 PHE A C   1 
ATOM   2477 O  O   . PHE A 1 327 ? 19.531  -0.687  -5.376  1.00 16.36 ? 374 PHE A O   1 
ATOM   2478 C  CB  . PHE A 1 327 ? 21.341  -1.461  -2.768  1.00 15.62 ? 374 PHE A CB  1 
ATOM   2479 C  CG  . PHE A 1 327 ? 20.443  -0.336  -2.293  1.00 15.54 ? 374 PHE A CG  1 
ATOM   2480 C  CD1 . PHE A 1 327 ? 19.275  -0.632  -1.618  1.00 15.68 ? 374 PHE A CD1 1 
ATOM   2481 C  CD2 . PHE A 1 327 ? 20.665  0.997   -2.616  1.00 16.12 ? 374 PHE A CD2 1 
ATOM   2482 C  CE1 . PHE A 1 327 ? 18.412  0.365   -1.219  1.00 16.00 ? 374 PHE A CE1 1 
ATOM   2483 C  CE2 . PHE A 1 327 ? 19.802  1.985   -2.182  1.00 16.27 ? 374 PHE A CE2 1 
ATOM   2484 C  CZ  . PHE A 1 327 ? 18.665  1.664   -1.543  1.00 16.53 ? 374 PHE A CZ  1 
ATOM   2485 N  N   . VAL A 1 328 ? 21.727  -0.611  -5.776  1.00 16.47 ? 375 VAL A N   1 
ATOM   2486 C  CA  . VAL A 1 328 ? 21.583  0.514   -6.685  1.00 17.30 ? 375 VAL A CA  1 
ATOM   2487 C  C   . VAL A 1 328 ? 20.670  0.174   -7.855  1.00 15.89 ? 375 VAL A C   1 
ATOM   2488 O  O   . VAL A 1 328 ? 19.711  0.915   -8.058  1.00 16.01 ? 375 VAL A O   1 
ATOM   2489 C  CB  . VAL A 1 328 ? 22.934  1.033   -7.184  1.00 18.09 ? 375 VAL A CB  1 
ATOM   2490 C  CG1 . VAL A 1 328 ? 22.779  2.042   -8.306  1.00 19.97 ? 375 VAL A CG1 1 
ATOM   2491 C  CG2 . VAL A 1 328 ? 23.691  1.654   -6.030  1.00 19.57 ? 375 VAL A CG2 1 
ATOM   2492 N  N   . PRO A 1 329 ? 20.877  -0.907  -8.614  1.00 16.31 ? 376 PRO A N   1 
ATOM   2493 C  CA  . PRO A 1 329 ? 19.938  -1.191  -9.696  1.00 17.43 ? 376 PRO A CA  1 
ATOM   2494 C  C   . PRO A 1 329 ? 18.508  -1.363  -9.208  1.00 16.48 ? 376 PRO A C   1 
ATOM   2495 O  O   . PRO A 1 329 ? 17.585  -0.897  -9.877  1.00 16.73 ? 376 PRO A O   1 
ATOM   2496 C  CB  . PRO A 1 329 ? 20.473  -2.421  -10.420 1.00 18.54 ? 376 PRO A CB  1 
ATOM   2497 C  CG  . PRO A 1 329 ? 21.536  -2.967  -9.506  1.00 21.17 ? 376 PRO A CG  1 
ATOM   2498 C  CD  . PRO A 1 329 ? 22.004  -1.841  -8.602  1.00 16.91 ? 376 PRO A CD  1 
ATOM   2499 N  N   . VAL A 1 330 ? 18.291  -2.062  -8.071  1.00 15.72 ? 377 VAL A N   1 
ATOM   2500 C  CA  . VAL A 1 330 ? 16.938  -2.339  -7.636  1.00 15.14 ? 377 VAL A CA  1 
ATOM   2501 C  C   . VAL A 1 330 ? 16.279  -1.030  -7.210  1.00 14.38 ? 377 VAL A C   1 
ATOM   2502 O  O   . VAL A 1 330 ? 15.173  -0.740  -7.629  1.00 14.44 ? 377 VAL A O   1 
ATOM   2503 C  CB  . VAL A 1 330 ? 16.953  -3.404  -6.525  1.00 15.70 ? 377 VAL A CB  1 
ATOM   2504 C  CG1 . VAL A 1 330 ? 15.557  -3.579  -5.960  1.00 16.10 ? 377 VAL A CG1 1 
ATOM   2505 C  CG2 . VAL A 1 330 ? 17.499  -4.729  -7.041  1.00 16.89 ? 377 VAL A CG2 1 
ATOM   2506 N  N   . GLN A 1 331 ? 16.952  -0.195  -6.411  1.00 14.70 ? 378 GLN A N   1 
ATOM   2507 C  CA  . GLN A 1 331 ? 16.368  1.081   -6.009  1.00 13.67 ? 378 GLN A CA  1 
ATOM   2508 C  C   . GLN A 1 331 ? 16.096  1.994   -7.202  1.00 14.95 ? 378 GLN A C   1 
ATOM   2509 O  O   . GLN A 1 331 ? 15.103  2.720   -7.221  1.00 14.89 ? 378 GLN A O   1 
ATOM   2510 C  CB  . GLN A 1 331 ? 17.256  1.769   -4.981  1.00 14.42 ? 378 GLN A CB  1 
ATOM   2511 C  CG  . GLN A 1 331 ? 16.729  3.095   -4.460  1.00 16.61 ? 378 GLN A CG  1 
ATOM   2512 C  CD  . GLN A 1 331 ? 15.395  3.038   -3.776  1.00 19.98 ? 378 GLN A CD  1 
ATOM   2513 O  OE1 . GLN A 1 331 ? 15.041  2.055   -3.142  1.00 20.17 ? 378 GLN A OE1 1 
ATOM   2514 N  NE2 . GLN A 1 331 ? 14.622  4.091   -3.902  1.00 23.18 ? 378 GLN A NE2 1 
ATOM   2515 N  N   . ARG A 1 332 ? 16.995  1.998   -8.179  1.00 15.71 ? 379 ARG A N   1 
ATOM   2516 C  CA  . ARG A 1 332 ? 16.763  2.795   -9.389  1.00 16.50 ? 379 ARG A CA  1 
ATOM   2517 C  C   . ARG A 1 332 ? 15.481  2.344   -10.077 1.00 15.64 ? 379 ARG A C   1 
ATOM   2518 O  O   . ARG A 1 332 ? 14.680  3.159   -10.528 1.00 17.21 ? 379 ARG A O   1 
ATOM   2519 C  CB  . ARG A 1 332 ? 17.934  2.647   -10.355 1.00 18.81 ? 379 ARG A CB  1 
ATOM   2520 C  CG  . ARG A 1 332 ? 19.143  3.529   -10.074 1.00 24.25 ? 379 ARG A CG  1 
ATOM   2521 C  CD  . ARG A 1 332 ? 20.054  3.637   -11.300 1.00 33.05 ? 379 ARG A CD  1 
ATOM   2522 N  NE  . ARG A 1 332 ? 21.247  4.476   -11.114 1.00 40.29 ? 379 ARG A NE  1 
ATOM   2523 C  CZ  . ARG A 1 332 ? 21.295  5.770   -10.781 1.00 51.28 ? 379 ARG A CZ  1 
ATOM   2524 N  NH1 . ARG A 1 332 ? 20.205  6.445   -10.452 1.00 52.52 ? 379 ARG A NH1 1 
ATOM   2525 N  NH2 . ARG A 1 332 ? 22.458  6.398   -10.767 1.00 55.82 ? 379 ARG A NH2 1 
ATOM   2526 N  N   . ASN A 1 333 ? 15.224  1.044   -10.086 1.00 14.58 ? 380 ASN A N   1 
ATOM   2527 C  CA  . ASN A 1 333 ? 14.039  0.517   -10.713 1.00 15.13 ? 380 ASN A CA  1 
ATOM   2528 C  C   . ASN A 1 333 ? 12.781  0.788   -9.901  1.00 15.58 ? 380 ASN A C   1 
ATOM   2529 O  O   . ASN A 1 333 ? 11.676  0.656   -10.433 1.00 17.88 ? 380 ASN A O   1 
ATOM   2530 C  CB  . ASN A 1 333 ? 14.093  -0.983  -10.885 1.00 16.06 ? 380 ASN A CB  1 
ATOM   2531 C  CG  . ASN A 1 333 ? 13.392  -1.410  -12.142 1.00 19.10 ? 380 ASN A CG  1 
ATOM   2532 O  OD1 . ASN A 1 333 ? 13.588  -0.774  -13.199 1.00 20.52 ? 380 ASN A OD1 1 
ATOM   2533 N  ND2 . ASN A 1 333 ? 12.595  -2.463  -12.070 1.00 16.85 ? 380 ASN A ND2 1 
ATOM   2534 N  N   . LEU A 1 334 ? 12.908  1.215   -8.636  1.00 14.66 ? 381 LEU A N   1 
ATOM   2535 C  CA  . LEU A 1 334 ? 11.767  1.587   -7.829  1.00 15.69 ? 381 LEU A CA  1 
ATOM   2536 C  C   . LEU A 1 334 ? 11.377  3.048   -8.021  1.00 15.79 ? 381 LEU A C   1 
ATOM   2537 O  O   . LEU A 1 334 ? 10.499  3.559   -7.331  1.00 16.72 ? 381 LEU A O   1 
ATOM   2538 C  CB  . LEU A 1 334 ? 12.018  1.272   -6.357  1.00 15.85 ? 381 LEU A CB  1 
ATOM   2539 C  CG  . LEU A 1 334 ? 12.309  -0.192  -6.036  1.00 15.38 ? 381 LEU A CG  1 
ATOM   2540 C  CD1 . LEU A 1 334 ? 12.456  -0.396  -4.522  1.00 17.00 ? 381 LEU A CD1 1 
ATOM   2541 C  CD2 . LEU A 1 334 ? 11.243  -1.104  -6.525  1.00 16.81 ? 381 LEU A CD2 1 
ATOM   2542 N  N   . ALA A 1 335 ? 11.966  3.728   -9.016  1.00 17.16 ? 382 ALA A N   1 
ATOM   2543 C  CA  . ALA A 1 335 ? 11.604  5.117   -9.231  1.00 18.20 ? 382 ALA A CA  1 
ATOM   2544 C  C   . ALA A 1 335 ? 10.111  5.298   -9.505  1.00 16.81 ? 382 ALA A C   1 
ATOM   2545 O  O   . ALA A 1 335 ? 9.567   6.315   -9.129  1.00 19.56 ? 382 ALA A O   1 
ATOM   2546 C  CB  . ALA A 1 335 ? 12.368  5.678   -10.408 1.00 19.08 ? 382 ALA A CB  1 
ATOM   2547 N  N   . THR A 1 336 ? 9.446   4.299   -10.108 1.00 15.59 ? 383 THR A N   1 
ATOM   2548 C  CA  . THR A 1 336 ? 8.033   4.377   -10.439 1.00 17.94 ? 383 THR A CA  1 
ATOM   2549 C  C   . THR A 1 336 ? 7.159   3.544   -9.516  1.00 16.75 ? 383 THR A C   1 
ATOM   2550 O  O   . THR A 1 336 ? 5.979   3.359   -9.780  1.00 18.28 ? 383 THR A O   1 
ATOM   2551 C  CB  . THR A 1 336 ? 7.762   3.925   -11.879 1.00 19.89 ? 383 THR A CB  1 
ATOM   2552 O  OG1 . THR A 1 336 ? 8.202   2.601   -12.122 1.00 22.00 ? 383 THR A OG1 1 
ATOM   2553 C  CG2 . THR A 1 336 ? 8.475   4.782   -12.912 1.00 21.87 ? 383 THR A CG2 1 
ATOM   2554 N  N   . ASP A 1 337 ? 7.752   3.016   -8.441  1.00 14.72 ? 384 ASP A N   1 
ATOM   2555 C  CA  . ASP A 1 337 ? 7.020   2.147   -7.528  1.00 13.79 ? 384 ASP A CA  1 
ATOM   2556 C  C   . ASP A 1 337 ? 5.783   2.841   -6.986  1.00 12.58 ? 384 ASP A C   1 
ATOM   2557 O  O   . ASP A 1 337 ? 5.845   3.943   -6.436  1.00 14.52 ? 384 ASP A O   1 
ATOM   2558 C  CB  . ASP A 1 337 ? 7.990   1.784   -6.406  1.00 13.57 ? 384 ASP A CB  1 
ATOM   2559 C  CG  . ASP A 1 337 ? 7.565   0.693   -5.444  1.00 13.60 ? 384 ASP A CG  1 
ATOM   2560 O  OD1 . ASP A 1 337 ? 6.426   0.227   -5.528  1.00 13.32 ? 384 ASP A OD1 1 
ATOM   2561 O  OD2 . ASP A 1 337 ? 8.463   0.330   -4.684  1.00 15.16 ? 384 ASP A OD2 1 
ATOM   2562 N  N   . ALA A 1 338 ? 4.662   2.133   -7.006  1.00 13.03 ? 385 ALA A N   1 
ATOM   2563 C  CA  . ALA A 1 338 ? 3.447   2.615   -6.385  1.00 13.08 ? 385 ALA A CA  1 
ATOM   2564 C  C   . ALA A 1 338 ? 3.617   2.837   -4.880  1.00 13.85 ? 385 ALA A C   1 
ATOM   2565 O  O   . ALA A 1 338 ? 2.956   3.668   -4.305  1.00 15.31 ? 385 ALA A O   1 
ATOM   2566 C  CB  . ALA A 1 338 ? 2.320   1.650   -6.604  1.00 15.25 ? 385 ALA A CB  1 
ATOM   2567 N  N   . LEU A 1 339 ? 4.568   2.113   -4.258  1.00 13.11 ? 386 LEU A N   1 
ATOM   2568 C  CA  . LEU A 1 339 ? 4.841   2.286   -2.840  1.00 12.17 ? 386 LEU A CA  1 
ATOM   2569 C  C   . LEU A 1 339 ? 5.394   3.675   -2.524  1.00 12.76 ? 386 LEU A C   1 
ATOM   2570 O  O   . LEU A 1 339 ? 5.231   4.144   -1.414  1.00 12.77 ? 386 LEU A O   1 
ATOM   2571 C  CB  . LEU A 1 339 ? 5.832   1.195   -2.414  1.00 12.31 ? 386 LEU A CB  1 
ATOM   2572 C  CG  . LEU A 1 339 ? 6.173   1.164   -0.918  1.00 13.78 ? 386 LEU A CG  1 
ATOM   2573 C  CD1 . LEU A 1 339 ? 4.977   0.924   -0.043  1.00 15.11 ? 386 LEU A CD1 1 
ATOM   2574 C  CD2 . LEU A 1 339 ? 7.249   0.137   -0.659  1.00 14.28 ? 386 LEU A CD2 1 
ATOM   2575 N  N   . ASN A 1 340 ? 5.975   4.366   -3.506  1.00 12.67 ? 387 ASN A N   1 
ATOM   2576 C  CA  . ASN A 1 340 ? 6.574   5.664   -3.205  1.00 13.06 ? 387 ASN A CA  1 
ATOM   2577 C  C   . ASN A 1 340 ? 5.567   6.684   -2.689  1.00 14.41 ? 387 ASN A C   1 
ATOM   2578 O  O   . ASN A 1 340 ? 5.976   7.616   -1.996  1.00 15.72 ? 387 ASN A O   1 
ATOM   2579 C  CB  . ASN A 1 340 ? 7.265   6.206   -4.442  1.00 15.20 ? 387 ASN A CB  1 
ATOM   2580 C  CG  . ASN A 1 340 ? 8.495   5.449   -4.826  1.00 16.87 ? 387 ASN A CG  1 
ATOM   2581 O  OD1 . ASN A 1 340 ? 9.090   4.774   -3.988  1.00 19.20 ? 387 ASN A OD1 1 
ATOM   2582 N  ND2 . ASN A 1 340 ? 8.909   5.559   -6.078  1.00 18.29 ? 387 ASN A ND2 1 
ATOM   2583 N  N   . GLU A 1 341 ? 4.295   6.540   -2.988  1.00 13.64 ? 388 GLU A N   1 
ATOM   2584 C  CA  . GLU A 1 341 ? 3.312   7.448   -2.458  1.00 16.03 ? 388 GLU A CA  1 
ATOM   2585 C  C   . GLU A 1 341 ? 3.237   7.408   -0.940  1.00 15.83 ? 388 GLU A C   1 
ATOM   2586 O  O   . GLU A 1 341 ? 2.706   8.333   -0.316  1.00 18.59 ? 388 GLU A O   1 
ATOM   2587 C  CB  . GLU A 1 341 ? 1.937   7.070   -3.022  1.00 19.50 ? 388 GLU A CB  1 
ATOM   2588 C  CG  . GLU A 1 341 ? 0.886   8.152   -2.818  1.00 30.28 ? 388 GLU A CG  1 
ATOM   2589 C  CD  . GLU A 1 341 ? 1.204   9.332   -3.734  1.00 31.44 ? 388 GLU A CD  1 
ATOM   2590 O  OE1 . GLU A 1 341 ? 1.593   10.404  -3.255  1.00 45.70 ? 388 GLU A OE1 1 
ATOM   2591 O  OE2 . GLU A 1 341 ? 1.116   9.144   -4.960  1.00 49.10 ? 388 GLU A OE2 1 
ATOM   2592 N  N   . PHE A 1 342 ? 3.702   6.307   -0.321  1.00 13.32 ? 389 PHE A N   1 
ATOM   2593 C  CA  . PHE A 1 342 ? 3.455   6.044   1.072   1.00 14.04 ? 389 PHE A CA  1 
ATOM   2594 C  C   . PHE A 1 342 ? 4.734   6.033   1.889   1.00 12.93 ? 389 PHE A C   1 
ATOM   2595 O  O   . PHE A 1 342 ? 4.636   5.763   3.092   1.00 14.20 ? 389 PHE A O   1 
ATOM   2596 C  CB  . PHE A 1 342 ? 2.760   4.694   1.231   1.00 13.71 ? 389 PHE A CB  1 
ATOM   2597 C  CG  . PHE A 1 342 ? 1.475   4.631   0.449   1.00 13.90 ? 389 PHE A CG  1 
ATOM   2598 C  CD1 . PHE A 1 342 ? 0.352   5.271   0.934   1.00 13.81 ? 389 PHE A CD1 1 
ATOM   2599 C  CD2 . PHE A 1 342 ? 1.397   3.959   -0.756  1.00 14.39 ? 389 PHE A CD2 1 
ATOM   2600 C  CE1 . PHE A 1 342 ? -0.831  5.221   0.244   1.00 15.77 ? 389 PHE A CE1 1 
ATOM   2601 C  CE2 . PHE A 1 342 ? 0.210   3.908   -1.429  1.00 15.33 ? 389 PHE A CE2 1 
ATOM   2602 C  CZ  . PHE A 1 342 ? -0.879  4.573   -0.954  1.00 15.81 ? 389 PHE A CZ  1 
ATOM   2603 N  N   . ILE A 1 343 ? 5.884   6.348   1.314   1.00 12.79 ? 390 ILE A N   1 
ATOM   2604 C  CA  . ILE A 1 343 ? 7.162   6.247   2.025   1.00 13.54 ? 390 ILE A CA  1 
ATOM   2605 C  C   . ILE A 1 343 ? 8.041   7.426   1.677   1.00 14.30 ? 390 ILE A C   1 
ATOM   2606 O  O   . ILE A 1 343 ? 7.818   8.107   0.687   1.00 15.49 ? 390 ILE A O   1 
ATOM   2607 C  CB  . ILE A 1 343 ? 7.910   4.938   1.761   1.00 13.96 ? 390 ILE A CB  1 
ATOM   2608 C  CG1 . ILE A 1 343 ? 8.327   4.814   0.308   1.00 14.63 ? 390 ILE A CG1 1 
ATOM   2609 C  CG2 . ILE A 1 343 ? 7.099   3.742   2.217   1.00 15.71 ? 390 ILE A CG2 1 
ATOM   2610 C  CD1 . ILE A 1 343 ? 9.344   3.705   0.063   1.00 17.19 ? 390 ILE A CD1 1 
ATOM   2611 N  N   . GLN A 1 344 ? 9.049   7.686   2.508   1.00 13.46 ? 391 GLN A N   1 
ATOM   2612 C  CA  . GLN A 1 344 ? 10.089  8.642   2.190   1.00 14.48 ? 391 GLN A CA  1 
ATOM   2613 C  C   . GLN A 1 344 ? 11.390  8.160   2.816   1.00 13.50 ? 391 GLN A C   1 
ATOM   2614 O  O   . GLN A 1 344 ? 11.418  7.892   4.002   1.00 14.81 ? 391 GLN A O   1 
ATOM   2615 C  CB  . GLN A 1 344 ? 9.709   10.038  2.677   1.00 17.91 ? 391 GLN A CB  1 
ATOM   2616 C  CG  . GLN A 1 344 ? 10.716  11.082  2.227   1.00 20.34 ? 391 GLN A CG  1 
ATOM   2617 C  CD  . GLN A 1 344 ? 10.290  12.475  2.608   1.00 24.66 ? 391 GLN A CD  1 
ATOM   2618 O  OE1 . GLN A 1 344 ? 10.126  12.763  3.784   1.00 28.60 ? 391 GLN A OE1 1 
ATOM   2619 N  NE2 . GLN A 1 344 ? 10.120  13.316  1.607   1.00 32.69 ? 391 GLN A NE2 1 
ATOM   2620 N  N   . HIS A 1 345 ? 12.439  8.099   2.024   1.00 13.64 ? 392 HIS A N   1 
ATOM   2621 C  CA  . HIS A 1 345 ? 13.737  7.777   2.598   1.00 13.88 ? 392 HIS A CA  1 
ATOM   2622 C  C   . HIS A 1 345 ? 14.303  9.021   3.253   1.00 14.15 ? 392 HIS A C   1 
ATOM   2623 O  O   . HIS A 1 345 ? 14.450  10.063  2.585   1.00 15.43 ? 392 HIS A O   1 
ATOM   2624 C  CB  . HIS A 1 345 ? 14.668  7.295   1.510   1.00 14.13 ? 392 HIS A CB  1 
ATOM   2625 C  CG  . HIS A 1 345 ? 14.295  5.993   0.901   1.00 13.42 ? 392 HIS A CG  1 
ATOM   2626 N  ND1 . HIS A 1 345 ? 15.194  4.959   0.772   1.00 14.84 ? 392 HIS A ND1 1 
ATOM   2627 C  CD2 . HIS A 1 345 ? 13.153  5.578   0.285   1.00 14.45 ? 392 HIS A CD2 1 
ATOM   2628 C  CE1 . HIS A 1 345 ? 14.604  3.957   0.141   1.00 15.35 ? 392 HIS A CE1 1 
ATOM   2629 N  NE2 . HIS A 1 345 ? 13.363  4.318   -0.186  1.00 14.47 ? 392 HIS A NE2 1 
ATOM   2630 N  N   . VAL A 1 346 ? 14.667  8.922   4.522   1.00 13.10 ? 393 VAL A N   1 
ATOM   2631 C  CA  . VAL A 1 346 ? 15.123  10.064  5.284   1.00 13.59 ? 393 VAL A CA  1 
ATOM   2632 C  C   . VAL A 1 346 ? 16.475  9.845   5.965   1.00 15.19 ? 393 VAL A C   1 
ATOM   2633 O  O   . VAL A 1 346 ? 16.955  10.743  6.643   1.00 16.16 ? 393 VAL A O   1 
ATOM   2634 C  CB  . VAL A 1 346 ? 14.091  10.461  6.331   1.00 15.51 ? 393 VAL A CB  1 
ATOM   2635 C  CG1 . VAL A 1 346 ? 12.830  10.987  5.646   1.00 17.55 ? 393 VAL A CG1 1 
ATOM   2636 C  CG2 . VAL A 1 346 ? 13.785  9.334   7.289   1.00 17.02 ? 393 VAL A CG2 1 
ATOM   2637 N  N   . GLY A 1 347 ? 17.167  8.735   5.729   1.00 14.21 ? 394 GLY A N   1 
ATOM   2638 C  CA  . GLY A 1 347 ? 18.523  8.528   6.230   1.00 14.57 ? 394 GLY A CA  1 
ATOM   2639 C  C   . GLY A 1 347 ? 19.191  7.456   5.410   1.00 14.58 ? 394 GLY A C   1 
ATOM   2640 O  O   . GLY A 1 347 ? 18.479  6.616   4.872   1.00 14.96 ? 394 GLY A O   1 
ATOM   2641 N  N   . SER A 1 348 ? 20.497  7.518   5.245   1.00 14.20 ? 395 SER A N   1 
ATOM   2642 C  CA  . SER A 1 348 ? 21.202  6.612   4.373   1.00 13.44 ? 395 SER A CA  1 
ATOM   2643 C  C   . SER A 1 348 ? 22.612  6.418   4.869   1.00 14.23 ? 395 SER A C   1 
ATOM   2644 O  O   . SER A 1 348 ? 23.218  7.388   5.306   1.00 15.15 ? 395 SER A O   1 
ATOM   2645 C  CB  . SER A 1 348 ? 21.227  7.169   3.006   1.00 15.02 ? 395 SER A CB  1 
ATOM   2646 O  OG  . SER A 1 348 ? 21.741  6.245   2.081   1.00 16.81 ? 395 SER A OG  1 
ATOM   2647 N  N   . ALA A 1 349 ? 23.131  5.202   4.734   1.00 14.16 ? 396 ALA A N   1 
ATOM   2648 C  CA  . ALA A 1 349 ? 24.541  4.957   4.965   1.00 13.96 ? 396 ALA A CA  1 
ATOM   2649 C  C   . ALA A 1 349 ? 24.957  3.691   4.276   1.00 14.60 ? 396 ALA A C   1 
ATOM   2650 O  O   . ALA A 1 349 ? 24.154  2.769   4.101   1.00 16.28 ? 396 ALA A O   1 
ATOM   2651 C  CB  . ALA A 1 349 ? 24.792  4.831   6.457   1.00 15.91 ? 396 ALA A CB  1 
ATOM   2652 N  N   . VAL A 1 350 ? 26.216  3.619   3.874   1.00 13.85 ? 397 VAL A N   1 
ATOM   2653 C  CA  . VAL A 1 350 ? 26.765  2.398   3.324   1.00 14.20 ? 397 VAL A CA  1 
ATOM   2654 C  C   . VAL A 1 350 ? 28.002  1.980   4.105   1.00 13.31 ? 397 VAL A C   1 
ATOM   2655 O  O   . VAL A 1 350 ? 28.734  2.843   4.618   1.00 13.53 ? 397 VAL A O   1 
ATOM   2656 C  CB  . VAL A 1 350 ? 27.111  2.532   1.842   1.00 16.18 ? 397 VAL A CB  1 
ATOM   2657 C  CG1 . VAL A 1 350 ? 25.866  2.874   1.033   1.00 17.25 ? 397 VAL A CG1 1 
ATOM   2658 C  CG2 . VAL A 1 350 ? 28.191  3.577   1.607   1.00 17.25 ? 397 VAL A CG2 1 
ATOM   2659 N  N   . PHE A 1 351 ? 28.241  0.670   4.148   1.00 12.82 ? 398 PHE A N   1 
ATOM   2660 C  CA  . PHE A 1 351 ? 29.373  0.155   4.899   1.00 13.99 ? 398 PHE A CA  1 
ATOM   2661 C  C   . PHE A 1 351 ? 29.930  -1.087  4.223   1.00 13.83 ? 398 PHE A C   1 
ATOM   2662 O  O   . PHE A 1 351 ? 29.181  -1.911  3.704   1.00 14.98 ? 398 PHE A O   1 
ATOM   2663 C  CB  . PHE A 1 351 ? 28.992  -0.191  6.344   1.00 13.33 ? 398 PHE A CB  1 
ATOM   2664 C  CG  . PHE A 1 351 ? 28.379  0.927   7.157   1.00 13.61 ? 398 PHE A CG  1 
ATOM   2665 C  CD1 . PHE A 1 351 ? 29.198  1.824   7.819   1.00 13.29 ? 398 PHE A CD1 1 
ATOM   2666 C  CD2 . PHE A 1 351 ? 27.013  1.115   7.212   1.00 15.03 ? 398 PHE A CD2 1 
ATOM   2667 C  CE1 . PHE A 1 351 ? 28.642  2.845   8.544   1.00 15.11 ? 398 PHE A CE1 1 
ATOM   2668 C  CE2 . PHE A 1 351 ? 26.474  2.134   7.945   1.00 15.72 ? 398 PHE A CE2 1 
ATOM   2669 C  CZ  . PHE A 1 351 ? 27.279  3.010   8.568   1.00 15.45 ? 398 PHE A CZ  1 
ATOM   2670 N  N   . ALA A 1 352 ? 31.249  -1.254  4.332   1.00 14.27 ? 399 ALA A N   1 
ATOM   2671 C  CA  . ALA A 1 352 ? 31.946  -2.482  4.032   1.00 14.29 ? 399 ALA A CA  1 
ATOM   2672 C  C   . ALA A 1 352 ? 32.038  -3.299  5.299   1.00 13.29 ? 399 ALA A C   1 
ATOM   2673 O  O   . ALA A 1 352 ? 32.603  -2.835  6.285   1.00 15.10 ? 399 ALA A O   1 
ATOM   2674 C  CB  . ALA A 1 352 ? 33.334  -2.156  3.534   1.00 15.08 ? 399 ALA A CB  1 
ATOM   2675 N  N   . VAL A 1 353 ? 31.474  -4.476  5.240   1.00 13.71 ? 400 VAL A N   1 
ATOM   2676 C  CA  . VAL A 1 353 ? 31.419  -5.383  6.367   1.00 13.52 ? 400 VAL A CA  1 
ATOM   2677 C  C   . VAL A 1 353 ? 32.528  -6.391  6.189   1.00 13.36 ? 400 VAL A C   1 
ATOM   2678 O  O   . VAL A 1 353 ? 32.467  -7.206  5.274   1.00 14.78 ? 400 VAL A O   1 
ATOM   2679 C  CB  . VAL A 1 353 ? 30.024  -6.012  6.420   1.00 15.41 ? 400 VAL A CB  1 
ATOM   2680 C  CG1 . VAL A 1 353 ? 29.935  -7.106  7.463   1.00 17.76 ? 400 VAL A CG1 1 
ATOM   2681 C  CG2 . VAL A 1 353 ? 28.985  -4.929  6.680   1.00 18.76 ? 400 VAL A CG2 1 
ATOM   2682 N  N   . PRO A 1 354 ? 33.582  -6.330  7.032   1.00 14.15 ? 401 PRO A N   1 
ATOM   2683 C  CA  . PRO A 1 354 ? 34.709  -7.200  6.735   1.00 14.91 ? 401 PRO A CA  1 
ATOM   2684 C  C   . PRO A 1 354 ? 34.419  -8.664  6.945   1.00 15.63 ? 401 PRO A C   1 
ATOM   2685 O  O   . PRO A 1 354 ? 33.367  -9.059  7.469   1.00 14.09 ? 401 PRO A O   1 
ATOM   2686 C  CB  . PRO A 1 354 ? 35.779  -6.682  7.679   1.00 16.30 ? 401 PRO A CB  1 
ATOM   2687 C  CG  . PRO A 1 354 ? 35.038  -5.969  8.766   1.00 16.81 ? 401 PRO A CG  1 
ATOM   2688 C  CD  . PRO A 1 354 ? 33.829  -5.333  8.068   1.00 14.52 ? 401 PRO A CD  1 
ATOM   2689 N  N   . PRO A 1 355 ? 35.360  -9.528  6.558   1.00 14.84 ? 402 PRO A N   1 
ATOM   2690 C  CA  . PRO A 1 355 ? 35.244  -10.943 6.838   1.00 15.27 ? 402 PRO A CA  1 
ATOM   2691 C  C   . PRO A 1 355 ? 35.173  -11.230 8.320   1.00 14.59 ? 402 PRO A C   1 
ATOM   2692 O  O   . PRO A 1 355 ? 35.392  -10.376 9.161   1.00 15.02 ? 402 PRO A O   1 
ATOM   2693 C  CB  . PRO A 1 355 ? 36.465  -11.618 6.195   1.00 17.95 ? 402 PRO A CB  1 
ATOM   2694 C  CG  . PRO A 1 355 ? 37.345  -10.476 5.832   1.00 18.55 ? 402 PRO A CG  1 
ATOM   2695 C  CD  . PRO A 1 355 ? 36.576  -9.171  5.806   1.00 17.50 ? 402 PRO A CD  1 
ATOM   2696 N  N   . GLY A 1 356 ? 34.882  -12.479 8.559   1.00 14.21 ? 403 GLY A N   1 
ATOM   2697 C  CA  . GLY A 1 356 ? 34.701  -12.945 9.924   1.00 14.46 ? 403 GLY A CA  1 
ATOM   2698 C  C   . GLY A 1 356 ? 35.996  -13.003 10.714  1.00 15.96 ? 403 GLY A C   1 
ATOM   2699 O  O   . GLY A 1 356 ? 37.100  -12.935 10.162  1.00 16.93 ? 403 GLY A O   1 
ATOM   2700 N  N   . VAL A 1 357 ? 35.811  -13.096 12.019  1.00 14.42 ? 404 VAL A N   1 
ATOM   2701 C  CA  . VAL A 1 357 ? 36.907  -13.277 12.961  1.00 14.76 ? 404 VAL A CA  1 
ATOM   2702 C  C   . VAL A 1 357 ? 37.155  -14.778 13.032  1.00 14.71 ? 404 VAL A C   1 
ATOM   2703 O  O   . VAL A 1 357 ? 36.297  -15.548 13.417  1.00 15.37 ? 404 VAL A O   1 
ATOM   2704 C  CB  . VAL A 1 357 ? 36.507  -12.702 14.318  1.00 16.23 ? 404 VAL A CB  1 
ATOM   2705 C  CG1 . VAL A 1 357 ? 37.613  -12.893 15.345  1.00 18.19 ? 404 VAL A CG1 1 
ATOM   2706 C  CG2 . VAL A 1 357 ? 36.117  -11.230 14.214  1.00 18.31 ? 404 VAL A CG2 1 
ATOM   2707 N  N   . ARG A 1 358 ? 38.339  -15.203 12.552  1.00 17.38 ? 405 ARG A N   1 
ATOM   2708 C  CA  . ARG A 1 358 ? 38.547  -16.607 12.250  1.00 19.36 ? 405 ARG A CA  1 
ATOM   2709 C  C   . ARG A 1 358 ? 38.661  -17.462 13.511  1.00 17.05 ? 405 ARG A C   1 
ATOM   2710 O  O   . ARG A 1 358 ? 38.161  -18.600 13.538  1.00 20.05 ? 405 ARG A O   1 
ATOM   2711 C  CB  . ARG A 1 358 ? 39.844  -16.772 11.441  1.00 22.56 ? 405 ARG A CB  1 
ATOM   2712 C  CG  . ARG A 1 358 ? 39.854  -16.016 10.112  1.00 31.14 ? 405 ARG A CG  1 
ATOM   2713 C  CD  . ARG A 1 358 ? 38.648  -16.270 9.197   1.00 40.20 ? 405 ARG A CD  1 
ATOM   2714 N  NE  . ARG A 1 358 ? 38.416  -17.692 8.904   1.00 47.60 ? 405 ARG A NE  1 
ATOM   2715 C  CZ  . ARG A 1 358 ? 38.371  -18.275 7.702   1.00 51.22 ? 405 ARG A CZ  1 
ATOM   2716 N  NH1 . ARG A 1 358 ? 38.564  -17.580 6.593   1.00 50.92 ? 405 ARG A NH1 1 
ATOM   2717 N  NH2 . ARG A 1 358 ? 38.132  -19.574 7.613   1.00 55.22 ? 405 ARG A NH2 1 
ATOM   2718 N  N   . ASP A 1 359 ? 39.304  -16.910 14.533  1.00 16.36 ? 406 ASP A N   1 
ATOM   2719 C  CA  . ASP A 1 359 ? 39.559  -17.653 15.752  1.00 17.71 ? 406 ASP A CA  1 
ATOM   2720 C  C   . ASP A 1 359 ? 39.854  -16.654 16.841  1.00 15.86 ? 406 ASP A C   1 
ATOM   2721 O  O   . ASP A 1 359 ? 39.799  -15.450 16.638  1.00 15.45 ? 406 ASP A O   1 
ATOM   2722 C  CB  . ASP A 1 359 ? 40.672  -18.650 15.523  1.00 21.47 ? 406 ASP A CB  1 
ATOM   2723 C  CG  . ASP A 1 359 ? 41.978  -18.038 15.051  1.00 22.91 ? 406 ASP A CG  1 
ATOM   2724 O  OD1 . ASP A 1 359 ? 42.341  -16.926 15.484  1.00 21.43 ? 406 ASP A OD1 1 
ATOM   2725 O  OD2 . ASP A 1 359 ? 42.630  -18.728 14.232  1.00 33.55 ? 406 ASP A OD2 1 
ATOM   2726 N  N   . ALA A 1 360 ? 40.247  -17.168 18.014  1.00 17.00 ? 407 ALA A N   1 
ATOM   2727 C  CA  . ALA A 1 360 ? 40.440  -16.385 19.212  1.00 18.03 ? 407 ALA A CA  1 
ATOM   2728 C  C   . ALA A 1 360 ? 41.612  -15.413 19.142  1.00 17.98 ? 407 ALA A C   1 
ATOM   2729 O  O   . ALA A 1 360 ? 41.703  -14.508 19.958  1.00 21.27 ? 407 ALA A O   1 
ATOM   2730 C  CB  . ALA A 1 360 ? 40.632  -17.315 20.381  1.00 19.24 ? 407 ALA A CB  1 
ATOM   2731 N  N   . ASP A 1 361 ? 42.513  -15.602 18.180  1.00 19.01 ? 408 ASP A N   1 
ATOM   2732 C  CA  . ASP A 1 361 ? 43.636  -14.701 17.986  1.00 21.35 ? 408 ASP A CA  1 
ATOM   2733 C  C   . ASP A 1 361 ? 43.347  -13.594 16.972  1.00 20.83 ? 408 ASP A C   1 
ATOM   2734 O  O   . ASP A 1 361 ? 44.114  -12.649 16.837  1.00 23.37 ? 408 ASP A O   1 
ATOM   2735 C  CB  . ASP A 1 361 ? 44.830  -15.482 17.459  1.00 27.14 ? 408 ASP A CB  1 
ATOM   2736 C  CG  . ASP A 1 361 ? 45.905  -15.740 18.492  1.00 38.11 ? 408 ASP A CG  1 
ATOM   2737 O  OD1 . ASP A 1 361 ? 46.475  -14.737 18.993  1.00 41.21 ? 408 ASP A OD1 1 
ATOM   2738 O  OD2 . ASP A 1 361 ? 46.142  -16.931 18.763  1.00 42.32 ? 408 ASP A OD2 1 
ATOM   2739 N  N   . ASP A 1 362 ? 42.246  -13.716 16.248  1.00 18.84 ? 409 ASP A N   1 
ATOM   2740 C  CA  . ASP A 1 362 ? 41.932  -12.748 15.201  1.00 16.87 ? 409 ASP A CA  1 
ATOM   2741 C  C   . ASP A 1 362 ? 41.142  -11.599 15.804  1.00 17.79 ? 409 ASP A C   1 
ATOM   2742 O  O   . ASP A 1 362 ? 40.839  -11.574 16.985  1.00 18.50 ? 409 ASP A O   1 
ATOM   2743 C  CB  . ASP A 1 362 ? 41.166  -13.441 14.098  1.00 17.13 ? 409 ASP A CB  1 
ATOM   2744 C  CG  . ASP A 1 362 ? 41.119  -12.755 12.742  1.00 16.48 ? 409 ASP A CG  1 
ATOM   2745 O  OD1 . ASP A 1 362 ? 41.892  -11.802 12.594  1.00 19.44 ? 409 ASP A OD1 1 
ATOM   2746 O  OD2 . ASP A 1 362 ? 40.343  -13.212 11.893  1.00 17.77 ? 409 ASP A OD2 1 
ATOM   2747 N  N   . TRP A 1 363 ? 40.865  -10.592 14.975  1.00 16.59 ? 410 TRP A N   1 
ATOM   2748 C  CA  . TRP A 1 363 ? 40.268  -9.358  15.426  1.00 16.00 ? 410 TRP A CA  1 
ATOM   2749 C  C   . TRP A 1 363 ? 39.588  -8.674  14.256  1.00 16.39 ? 410 TRP A C   1 
ATOM   2750 O  O   . TRP A 1 363 ? 40.011  -8.813  13.108  1.00 16.81 ? 410 TRP A O   1 
ATOM   2751 C  CB  . TRP A 1 363 ? 41.261  -8.431  16.155  1.00 17.47 ? 410 TRP A CB  1 
ATOM   2752 C  CG  . TRP A 1 363 ? 42.611  -8.280  15.502  1.00 17.59 ? 410 TRP A CG  1 
ATOM   2753 C  CD1 . TRP A 1 363 ? 43.649  -9.170  15.551  1.00 20.07 ? 410 TRP A CD1 1 
ATOM   2754 C  CD2 . TRP A 1 363 ? 43.080  -7.169  14.732  1.00 18.73 ? 410 TRP A CD2 1 
ATOM   2755 N  NE1 . TRP A 1 363 ? 44.728  -8.680  14.872  1.00 21.79 ? 410 TRP A NE1 1 
ATOM   2756 C  CE2 . TRP A 1 363 ? 44.407  -7.457  14.353  1.00 20.77 ? 410 TRP A CE2 1 
ATOM   2757 C  CE3 . TRP A 1 363 ? 42.502  -5.971  14.318  1.00 19.26 ? 410 TRP A CE3 1 
ATOM   2758 C  CZ2 . TRP A 1 363 ? 45.157  -6.575  13.592  1.00 22.40 ? 410 TRP A CZ2 1 
ATOM   2759 C  CZ3 . TRP A 1 363 ? 43.243  -5.100  13.550  1.00 18.30 ? 410 TRP A CZ3 1 
ATOM   2760 C  CH2 . TRP A 1 363 ? 44.543  -5.420  13.175  1.00 21.66 ? 410 TRP A CH2 1 
ATOM   2761 N  N   . TRP A 1 364 ? 38.530  -7.948  14.606  1.00 15.56 ? 411 TRP A N   1 
ATOM   2762 C  CA  . TRP A 1 364 ? 37.770  -7.176  13.639  1.00 16.13 ? 411 TRP A CA  1 
ATOM   2763 C  C   . TRP A 1 364 ? 38.687  -6.264  12.856  1.00 16.93 ? 411 TRP A C   1 
ATOM   2764 O  O   . TRP A 1 364 ? 39.410  -5.471  13.418  1.00 18.06 ? 411 TRP A O   1 
ATOM   2765 C  CB  . TRP A 1 364 ? 36.749  -6.313  14.376  1.00 15.04 ? 411 TRP A CB  1 
ATOM   2766 C  CG  . TRP A 1 364 ? 35.465  -6.998  14.706  1.00 14.24 ? 411 TRP A CG  1 
ATOM   2767 C  CD1 . TRP A 1 364 ? 34.906  -8.068  14.099  1.00 15.24 ? 411 TRP A CD1 1 
ATOM   2768 C  CD2 . TRP A 1 364 ? 34.520  -6.509  15.666  1.00 14.61 ? 411 TRP A CD2 1 
ATOM   2769 N  NE1 . TRP A 1 364 ? 33.665  -8.328  14.649  1.00 15.40 ? 411 TRP A NE1 1 
ATOM   2770 C  CE2 . TRP A 1 364 ? 33.404  -7.369  15.585  1.00 15.57 ? 411 TRP A CE2 1 
ATOM   2771 C  CE3 . TRP A 1 364 ? 34.483  -5.428  16.538  1.00 16.92 ? 411 TRP A CE3 1 
ATOM   2772 C  CZ2 . TRP A 1 364 ? 32.280  -7.185  16.381  1.00 15.92 ? 411 TRP A CZ2 1 
ATOM   2773 C  CZ3 . TRP A 1 364 ? 33.351  -5.241  17.312  1.00 18.52 ? 411 TRP A CZ3 1 
ATOM   2774 C  CH2 . TRP A 1 364 ? 32.260  -6.094  17.194  1.00 17.10 ? 411 TRP A CH2 1 
ATOM   2775 N  N   . GLY A 1 365 ? 38.609  -6.364  11.544  1.00 16.09 ? 412 GLY A N   1 
ATOM   2776 C  CA  . GLY A 1 365 ? 39.385  -5.491  10.681  1.00 17.02 ? 412 GLY A CA  1 
ATOM   2777 C  C   . GLY A 1 365 ? 40.817  -5.958  10.460  1.00 17.47 ? 412 GLY A C   1 
ATOM   2778 O  O   . GLY A 1 365 ? 41.568  -5.210  9.812   1.00 18.27 ? 412 GLY A O   1 
ATOM   2779 N  N   . SER A 1 366 ? 41.221  -7.155  10.913  1.00 16.08 ? 413 SER A N   1 
ATOM   2780 C  CA  . SER A 1 366 ? 42.629  -7.542  10.814  1.00 17.51 ? 413 SER A CA  1 
ATOM   2781 C  C   . SER A 1 366 ? 43.076  -7.621  9.361   1.00 19.50 ? 413 SER A C   1 
ATOM   2782 O  O   . SER A 1 366 ? 44.272  -7.460  9.102   1.00 19.88 ? 413 SER A O   1 
ATOM   2783 C  CB  . SER A 1 366 ? 42.827  -8.868  11.494  1.00 17.01 ? 413 SER A CB  1 
ATOM   2784 O  OG  . SER A 1 366 ? 42.124  -9.897  10.824  1.00 17.50 ? 413 SER A OG  1 
ATOM   2785 N  N   . THR A 1 367 ? 42.198  -7.981  8.422   1.00 18.54 ? 414 THR A N   1 
ATOM   2786 C  CA  . THR A 1 367 ? 42.641  -8.114  7.041   1.00 18.18 ? 414 THR A CA  1 
ATOM   2787 C  C   . THR A 1 367 ? 42.906  -6.730  6.447   1.00 19.94 ? 414 THR A C   1 
ATOM   2788 O  O   . THR A 1 367 ? 43.696  -6.617  5.511   1.00 22.38 ? 414 THR A O   1 
ATOM   2789 C  CB  . THR A 1 367 ? 41.643  -8.901  6.184   1.00 19.29 ? 414 THR A CB  1 
ATOM   2790 O  OG1 . THR A 1 367 ? 40.412  -8.179  6.143   1.00 20.47 ? 414 THR A OG1 1 
ATOM   2791 C  CG2 . THR A 1 367 ? 41.429  -10.301 6.704   1.00 20.37 ? 414 THR A CG2 1 
ATOM   2792 N  N   . LEU A 1 368 ? 42.259  -5.688  6.946   1.00 17.76 ? 415 LEU A N   1 
ATOM   2793 C  CA  . LEU A 1 368 ? 42.423  -4.331  6.441   1.00 19.83 ? 415 LEU A CA  1 
ATOM   2794 C  C   . LEU A 1 368 ? 43.699  -3.735  7.025   1.00 22.13 ? 415 LEU A C   1 
ATOM   2795 O  O   . LEU A 1 368 ? 44.497  -3.120  6.298   1.00 26.04 ? 415 LEU A O   1 
ATOM   2796 C  CB  . LEU A 1 368 ? 41.205  -3.474  6.787   1.00 19.99 ? 415 LEU A CB  1 
ATOM   2797 C  CG  . LEU A 1 368 ? 41.294  -1.984  6.444   1.00 22.54 ? 415 LEU A CG  1 
ATOM   2798 C  CD1 . LEU A 1 368 ? 41.560  -1.756  4.988   1.00 23.53 ? 415 LEU A CD1 1 
ATOM   2799 C  CD2 . LEU A 1 368 ? 40.022  -1.295  6.845   1.00 24.61 ? 415 LEU A CD2 1 
ATOM   2800 N  N   . PHE A 1 369 ? 43.873  -3.901  8.342   1.00 24.19 ? 416 PHE A N   1 
ATOM   2801 C  CA  . PHE A 1 369 ? 44.951  -3.287  9.103   1.00 26.73 ? 416 PHE A CA  1 
ATOM   2802 C  C   . PHE A 1 369 ? 46.065  -4.329  9.221   1.00 29.09 ? 416 PHE A C   1 
ATOM   2803 O  O   . PHE A 1 369 ? 47.176  -3.754  9.200   1.00 38.62 ? 416 PHE A O   1 
ATOM   2804 C  CB  . PHE A 1 369 ? 44.429  -2.809  10.462  1.00 26.18 ? 416 PHE A CB  1 
ATOM   2805 C  CG  . PHE A 1 369 ? 43.484  -1.616  10.424  1.00 25.86 ? 416 PHE A CG  1 
ATOM   2806 C  CD1 . PHE A 1 369 ? 43.969  -0.316  10.384  1.00 25.94 ? 416 PHE A CD1 1 
ATOM   2807 C  CD2 . PHE A 1 369 ? 42.102  -1.788  10.427  1.00 26.04 ? 416 PHE A CD2 1 
ATOM   2808 C  CE1 . PHE A 1 369 ? 43.099  0.768   10.366  1.00 28.43 ? 416 PHE A CE1 1 
ATOM   2809 C  CE2 . PHE A 1 369 ? 41.245  -0.703  10.396  1.00 26.70 ? 416 PHE A CE2 1 
ATOM   2810 C  CZ  . PHE A 1 369 ? 41.749  0.580   10.374  1.00 28.54 ? 416 PHE A CZ  1 
ATOM   2811 N  N   . SER B 1 9   ? -1.008  -16.938 28.074  1.00 31.18 ? 56  SER B N   1 
ATOM   2812 C  CA  . SER B 1 9   ? -1.439  -16.667 26.671  1.00 30.16 ? 56  SER B CA  1 
ATOM   2813 C  C   . SER B 1 9   ? -2.250  -15.368 26.610  1.00 23.86 ? 56  SER B C   1 
ATOM   2814 O  O   . SER B 1 9   ? -1.896  -14.475 25.896  1.00 20.74 ? 56  SER B O   1 
ATOM   2815 C  CB  . SER B 1 9   ? -2.196  -17.827 26.091  1.00 41.20 ? 56  SER B CB  1 
ATOM   2816 O  OG  . SER B 1 9   ? -2.662  -17.519 24.788  1.00 44.36 ? 56  SER B OG  1 
ATOM   2817 N  N   . ALA B 1 10  ? -3.303  -15.231 27.400  1.00 20.87 ? 57  ALA B N   1 
ATOM   2818 C  CA  . ALA B 1 10  ? -4.126  -14.025 27.353  1.00 18.38 ? 57  ALA B CA  1 
ATOM   2819 C  C   . ALA B 1 10  ? -4.497  -13.681 28.774  1.00 17.36 ? 57  ALA B C   1 
ATOM   2820 O  O   . ALA B 1 10  ? -4.383  -14.502 29.672  1.00 20.08 ? 57  ALA B O   1 
ATOM   2821 C  CB  . ALA B 1 10  ? -5.348  -14.192 26.542  1.00 18.77 ? 57  ALA B CB  1 
ATOM   2822 N  N   . VAL B 1 11  ? -4.900  -12.423 28.939  1.00 13.26 ? 58  VAL B N   1 
ATOM   2823 C  CA  . VAL B 1 11  ? -5.326  -11.946 30.227  1.00 13.13 ? 58  VAL B CA  1 
ATOM   2824 C  C   . VAL B 1 11  ? -6.767  -11.529 30.057  1.00 13.02 ? 58  VAL B C   1 
ATOM   2825 O  O   . VAL B 1 11  ? -7.115  -10.829 29.113  1.00 13.15 ? 58  VAL B O   1 
ATOM   2826 C  CB  . VAL B 1 11  ? -4.460  -10.766 30.659  1.00 13.79 ? 58  VAL B CB  1 
ATOM   2827 C  CG1 . VAL B 1 11  ? -4.973  -10.172 31.954  1.00 15.23 ? 58  VAL B CG1 1 
ATOM   2828 C  CG2 . VAL B 1 11  ? -3.031  -11.238 30.801  1.00 15.92 ? 58  VAL B CG2 1 
ATOM   2829 N  N   . PRO B 1 12  ? -7.700  -11.924 30.931  1.00 13.34 ? 59  PRO B N   1 
ATOM   2830 C  CA  . PRO B 1 12  ? -9.083  -11.500 30.774  1.00 14.12 ? 59  PRO B CA  1 
ATOM   2831 C  C   . PRO B 1 12  ? -9.212  -9.973  30.757  1.00 12.99 ? 59  PRO B C   1 
ATOM   2832 O  O   . PRO B 1 12  ? -8.661  -9.288  31.594  1.00 14.63 ? 59  PRO B O   1 
ATOM   2833 C  CB  . PRO B 1 12  ? -9.763  -12.130 32.041  1.00 15.47 ? 59  PRO B CB  1 
ATOM   2834 C  CG  . PRO B 1 12  ? -8.859  -13.150 32.510  1.00 17.91 ? 59  PRO B CG  1 
ATOM   2835 C  CD  . PRO B 1 12  ? -7.478  -12.809 32.087  1.00 14.99 ? 59  PRO B CD  1 
ATOM   2836 N  N   . PHE B 1 13  ? -10.043 -9.505  29.864  1.00 13.01 ? 60  PHE B N   1 
ATOM   2837 C  CA  . PHE B 1 13  ? -10.305 -8.091  29.701  1.00 13.21 ? 60  PHE B CA  1 
ATOM   2838 C  C   . PHE B 1 13  ? -11.308 -7.578  30.729  1.00 13.05 ? 60  PHE B C   1 
ATOM   2839 O  O   . PHE B 1 13  ? -11.149 -6.475  31.244  1.00 12.58 ? 60  PHE B O   1 
ATOM   2840 C  CB  . PHE B 1 13  ? -10.809 -7.808  28.293  1.00 13.55 ? 60  PHE B CB  1 
ATOM   2841 C  CG  . PHE B 1 13  ? -11.124 -6.363  27.996  1.00 13.69 ? 60  PHE B CG  1 
ATOM   2842 C  CD1 . PHE B 1 13  ? -10.124 -5.425  27.906  1.00 15.17 ? 60  PHE B CD1 1 
ATOM   2843 C  CD2 . PHE B 1 13  ? -12.437 -5.935  27.911  1.00 14.80 ? 60  PHE B CD2 1 
ATOM   2844 C  CE1 . PHE B 1 13  ? -10.419 -4.109  27.701  1.00 15.63 ? 60  PHE B CE1 1 
ATOM   2845 C  CE2 . PHE B 1 13  ? -12.715 -4.616  27.615  1.00 17.03 ? 60  PHE B CE2 1 
ATOM   2846 C  CZ  . PHE B 1 13  ? -11.701 -3.708  27.551  1.00 16.72 ? 60  PHE B CZ  1 
ATOM   2847 N  N   . HIS B 1 14  ? -12.333 -8.372  31.040  1.00 13.94 ? 61  HIS B N   1 
ATOM   2848 C  CA  . HIS B 1 14  ? -13.401 -7.935  31.919  1.00 14.76 ? 61  HIS B CA  1 
ATOM   2849 C  C   . HIS B 1 14  ? -13.020 -8.191  33.354  1.00 15.63 ? 61  HIS B C   1 
ATOM   2850 O  O   . HIS B 1 14  ? -12.292 -9.133  33.690  1.00 19.75 ? 61  HIS B O   1 
ATOM   2851 C  CB  . HIS B 1 14  ? -14.711 -8.676  31.592  1.00 16.17 ? 61  HIS B CB  1 
ATOM   2852 C  CG  . HIS B 1 14  ? -15.137 -8.436  30.192  1.00 18.16 ? 61  HIS B CG  1 
ATOM   2853 N  ND1 . HIS B 1 14  ? -15.034 -9.353  29.169  1.00 24.59 ? 61  HIS B ND1 1 
ATOM   2854 C  CD2 . HIS B 1 14  ? -15.584 -7.320  29.605  1.00 17.69 ? 61  HIS B CD2 1 
ATOM   2855 C  CE1 . HIS B 1 14  ? -15.504 -8.816  28.046  1.00 25.76 ? 61  HIS B CE1 1 
ATOM   2856 N  NE2 . HIS B 1 14  ? -15.880 -7.579  28.293  1.00 20.15 ? 61  HIS B NE2 1 
ATOM   2857 N  N   . GLY B 1 15  ? -13.511 -7.350  34.232  1.00 15.49 ? 62  GLY B N   1 
ATOM   2858 C  CA  . GLY B 1 15  ? -13.324 -7.535  35.650  1.00 16.83 ? 62  GLY B CA  1 
ATOM   2859 C  C   . GLY B 1 15  ? -13.812 -6.326  36.414  1.00 15.35 ? 62  GLY B C   1 
ATOM   2860 O  O   . GLY B 1 15  ? -14.204 -5.326  35.857  1.00 16.08 ? 62  GLY B O   1 
ATOM   2861 N  N   . ALA B 1 16  ? -13.734 -6.422  37.728  1.00 15.20 ? 63  ALA B N   1 
ATOM   2862 C  CA  . ALA B 1 16  ? -14.057 -5.303  38.574  1.00 15.14 ? 63  ALA B CA  1 
ATOM   2863 C  C   . ALA B 1 16  ? -13.025 -4.187  38.407  1.00 14.04 ? 63  ALA B C   1 
ATOM   2864 O  O   . ALA B 1 16  ? -13.335 -3.015  38.550  1.00 14.71 ? 63  ALA B O   1 
ATOM   2865 C  CB  . ALA B 1 16  ? -14.097 -5.745  40.035  1.00 18.22 ? 63  ALA B CB  1 
ATOM   2866 N  N   . HIS B 1 17  ? -11.799 -4.585  38.078  1.00 13.06 ? 64  HIS B N   1 
ATOM   2867 C  CA  . HIS B 1 17  ? -10.703 -3.655  37.843  1.00 11.59 ? 64  HIS B CA  1 
ATOM   2868 C  C   . HIS B 1 17  ? -10.262 -3.823  36.415  1.00 12.23 ? 64  HIS B C   1 
ATOM   2869 O  O   . HIS B 1 17  ? -10.414 -4.895  35.858  1.00 13.34 ? 64  HIS B O   1 
ATOM   2870 C  CB  . HIS B 1 17  ? -9.504  -3.940  38.749  1.00 12.55 ? 64  HIS B CB  1 
ATOM   2871 C  CG  . HIS B 1 17  ? -9.889  -4.025  40.185  1.00 13.84 ? 64  HIS B CG  1 
ATOM   2872 N  ND1 . HIS B 1 17  ? -10.315 -2.961  40.928  1.00 14.05 ? 64  HIS B ND1 1 
ATOM   2873 C  CD2 . HIS B 1 17  ? -9.826  -5.092  41.007  1.00 16.02 ? 64  HIS B CD2 1 
ATOM   2874 C  CE1 . HIS B 1 17  ? -10.554 -3.395  42.169  1.00 15.44 ? 64  HIS B CE1 1 
ATOM   2875 N  NE2 . HIS B 1 17  ? -10.267 -4.672  42.228  1.00 16.98 ? 64  HIS B NE2 1 
ATOM   2876 N  N   . GLN B 1 18  ? -9.726  -2.762  35.844  1.00 10.69 ? 65  GLN B N   1 
ATOM   2877 C  CA  . GLN B 1 18  ? -9.022  -2.878  34.584  1.00 10.86 ? 65  GLN B CA  1 
ATOM   2878 C  C   . GLN B 1 18  ? -7.817  -3.786  34.764  1.00 10.97 ? 65  GLN B C   1 
ATOM   2879 O  O   . GLN B 1 18  ? -7.138  -3.715  35.770  1.00 12.03 ? 65  GLN B O   1 
ATOM   2880 C  CB  . GLN B 1 18  ? -8.588  -1.522  34.081  1.00 10.97 ? 65  GLN B CB  1 
ATOM   2881 C  CG  . GLN B 1 18  ? -9.755  -0.684  33.589  1.00 10.50 ? 65  GLN B CG  1 
ATOM   2882 C  CD  . GLN B 1 18  ? -9.212  0.497   32.850  1.00 10.32 ? 65  GLN B CD  1 
ATOM   2883 O  OE1 . GLN B 1 18  ? -8.750  0.345   31.728  1.00 11.40 ? 65  GLN B OE1 1 
ATOM   2884 N  NE2 . GLN B 1 18  ? -9.307  1.694   33.411  1.00 11.11 ? 65  GLN B NE2 1 
ATOM   2885 N  N   . ALA B 1 19  ? -7.553  -4.615  33.765  1.00 11.03 ? 66  ALA B N   1 
ATOM   2886 C  CA  . ALA B 1 19  ? -6.323  -5.387  33.726  1.00 11.00 ? 66  ALA B CA  1 
ATOM   2887 C  C   . ALA B 1 19  ? -5.177  -4.433  33.443  1.00 11.48 ? 66  ALA B C   1 
ATOM   2888 O  O   . ALA B 1 19  ? -5.398  -3.297  33.023  1.00 13.31 ? 66  ALA B O   1 
ATOM   2889 C  CB  . ALA B 1 19  ? -6.399  -6.505  32.708  1.00 11.44 ? 66  ALA B CB  1 
ATOM   2890 N  N   . GLY B 1 20  ? -3.946  -4.901  33.633  1.00 11.04 ? 67  GLY B N   1 
ATOM   2891 C  CA  . GLY B 1 20  ? -2.750  -4.126  33.397  1.00 11.51 ? 67  GLY B CA  1 
ATOM   2892 C  C   . GLY B 1 20  ? -2.215  -3.378  34.602  1.00 11.15 ? 67  GLY B C   1 
ATOM   2893 O  O   . GLY B 1 20  ? -1.331  -2.567  34.431  1.00 12.10 ? 67  GLY B O   1 
ATOM   2894 N  N   . ILE B 1 21  ? -2.795  -3.613  35.783  1.00 11.45 ? 68  ILE B N   1 
ATOM   2895 C  CA  . ILE B 1 21  ? -2.377  -2.921  36.998  1.00 11.93 ? 68  ILE B CA  1 
ATOM   2896 C  C   . ILE B 1 21  ? -1.822  -3.975  37.941  1.00 12.63 ? 68  ILE B C   1 
ATOM   2897 O  O   . ILE B 1 21  ? -0.624  -4.003  38.184  1.00 15.42 ? 68  ILE B O   1 
ATOM   2898 C  CB  . ILE B 1 21  ? -3.502  -2.114  37.595  1.00 12.32 ? 68  ILE B CB  1 
ATOM   2899 C  CG1 . ILE B 1 21  ? -4.005  -1.086  36.570  1.00 14.70 ? 68  ILE B CG1 1 
ATOM   2900 C  CG2 . ILE B 1 21  ? -3.008  -1.447  38.868  1.00 13.70 ? 68  ILE B CG2 1 
ATOM   2901 C  CD1 . ILE B 1 21  ? -5.358  -0.459  36.903  1.00 16.28 ? 68  ILE B CD1 1 
ATOM   2902 N  N   . ALA B 1 22  ? -2.683  -4.890  38.364  1.00 12.23 ? 69  ALA B N   1 
ATOM   2903 C  CA  . ALA B 1 22  ? -2.342  -5.986  39.260  1.00 13.77 ? 69  ALA B CA  1 
ATOM   2904 C  C   . ALA B 1 22  ? -2.132  -7.283  38.529  1.00 15.36 ? 69  ALA B C   1 
ATOM   2905 O  O   . ALA B 1 22  ? -1.830  -8.285  39.164  1.00 18.94 ? 69  ALA B O   1 
ATOM   2906 C  CB  . ALA B 1 22  ? -3.437  -6.193  40.277  1.00 16.22 ? 69  ALA B CB  1 
ATOM   2907 N  N   . THR B 1 23  ? -2.272  -7.328  37.222  1.00 12.66 ? 70  THR B N   1 
ATOM   2908 C  CA  . THR B 1 23  ? -2.093  -8.560  36.470  1.00 13.15 ? 70  THR B CA  1 
ATOM   2909 C  C   . THR B 1 23  ? -0.617  -8.677  36.144  1.00 14.77 ? 70  THR B C   1 
ATOM   2910 O  O   . THR B 1 23  ? 0.164   -7.737  36.274  1.00 14.42 ? 70  THR B O   1 
ATOM   2911 C  CB  . THR B 1 23  ? -3.034  -8.584  35.273  1.00 14.41 ? 70  THR B CB  1 
ATOM   2912 O  OG1 . THR B 1 23  ? -2.832  -7.393  34.510  1.00 14.25 ? 70  THR B OG1 1 
ATOM   2913 C  CG2 . THR B 1 23  ? -4.506  -8.630  35.672  1.00 15.31 ? 70  THR B CG2 1 
ATOM   2914 N  N   . PRO B 1 24  ? -0.168  -9.901  35.788  1.00 15.22 ? 71  PRO B N   1 
ATOM   2915 C  CA  . PRO B 1 24  ? 1.266   -10.092 35.619  1.00 15.40 ? 71  PRO B CA  1 
ATOM   2916 C  C   . PRO B 1 24  ? 1.928   -9.129  34.640  1.00 14.54 ? 71  PRO B C   1 
ATOM   2917 O  O   . PRO B 1 24  ? 1.367   -8.773  33.610  1.00 14.39 ? 71  PRO B O   1 
ATOM   2918 C  CB  . PRO B 1 24  ? 1.326   -11.561 35.113  1.00 17.24 ? 71  PRO B CB  1 
ATOM   2919 C  CG  . PRO B 1 24  ? 0.093   -12.219 35.720  1.00 19.07 ? 71  PRO B CG  1 
ATOM   2920 C  CD  . PRO B 1 24  ? -0.968  -11.141 35.658  1.00 17.85 ? 71  PRO B CD  1 
ATOM   2921 N  N   . VAL B 1 25  ? 3.128   -8.686  34.973  1.00 14.32 ? 72  VAL B N   1 
ATOM   2922 C  CA  . VAL B 1 25  ? 3.835   -7.678  34.245  1.00 14.75 ? 72  VAL B CA  1 
ATOM   2923 C  C   . VAL B 1 25  ? 4.368   -8.284  32.959  1.00 13.98 ? 72  VAL B C   1 
ATOM   2924 O  O   . VAL B 1 25  ? 5.163   -9.235  32.958  1.00 16.30 ? 72  VAL B O   1 
ATOM   2925 C  CB  . VAL B 1 25  ? 4.948   -6.994  35.045  1.00 17.85 ? 72  VAL B CB  1 
ATOM   2926 C  CG1 . VAL B 1 25  ? 5.693   -5.964  34.225  1.00 21.13 ? 72  VAL B CG1 1 
ATOM   2927 C  CG2 . VAL B 1 25  ? 4.380   -6.277  36.275  1.00 19.30 ? 72  VAL B CG2 1 
ATOM   2928 N  N   . GLN B 1 26  ? 3.954   -7.713  31.837  1.00 11.71 ? 73  GLN B N   1 
ATOM   2929 C  CA  . GLN B 1 26  ? 4.352   -8.193  30.539  1.00 11.31 ? 73  GLN B CA  1 
ATOM   2930 C  C   . GLN B 1 26  ? 5.654   -7.559  30.096  1.00 10.46 ? 73  GLN B C   1 
ATOM   2931 O  O   . GLN B 1 26  ? 6.127   -6.570  30.625  1.00 12.57 ? 73  GLN B O   1 
ATOM   2932 C  CB  . GLN B 1 26  ? 3.247   -7.936  29.523  1.00 10.88 ? 73  GLN B CB  1 
ATOM   2933 C  CG  . GLN B 1 26  ? 1.868   -8.372  29.986  1.00 10.39 ? 73  GLN B CG  1 
ATOM   2934 C  CD  . GLN B 1 26  ? 1.043   -7.264  30.555  1.00 9.76  ? 73  GLN B CD  1 
ATOM   2935 O  OE1 . GLN B 1 26  ? 1.509   -6.458  31.365  1.00 10.38 ? 73  GLN B OE1 1 
ATOM   2936 N  NE2 . GLN B 1 26  ? -0.192  -7.213  30.107  1.00 11.03 ? 73  GLN B NE2 1 
ATOM   2937 N  N   . ASP B 1 27  ? 6.240   -8.148  29.083  1.00 11.07 ? 74  ASP B N   1 
ATOM   2938 C  CA  . ASP B 1 27  ? 7.610   -7.819  28.688  1.00 11.87 ? 74  ASP B CA  1 
ATOM   2939 C  C   . ASP B 1 27  ? 7.750   -6.434  28.051  1.00 11.25 ? 74  ASP B C   1 
ATOM   2940 O  O   . ASP B 1 27  ? 8.841   -5.891  28.092  1.00 11.61 ? 74  ASP B O   1 
ATOM   2941 C  CB  . ASP B 1 27  ? 8.151   -8.882  27.736  1.00 13.25 ? 74  ASP B CB  1 
ATOM   2942 C  CG  . ASP B 1 27  ? 8.272   -10.287 28.305  1.00 15.42 ? 74  ASP B CG  1 
ATOM   2943 O  OD1 . ASP B 1 27  ? 8.019   -10.474 29.477  1.00 18.38 ? 74  ASP B OD1 1 
ATOM   2944 O  OD2 . ASP B 1 27  ? 8.691   -11.166 27.535  1.00 17.37 ? 74  ASP B OD2 1 
ATOM   2945 N  N   . ARG B 1 28  ? 6.701   -5.893  27.434  1.00 11.00 ? 75  ARG B N   1 
ATOM   2946 C  CA  . ARG B 1 28  ? 6.805   -4.711  26.617  1.00 10.87 ? 75  ARG B CA  1 
ATOM   2947 C  C   . ARG B 1 28  ? 5.654   -3.762  26.873  1.00 10.38 ? 75  ARG B C   1 
ATOM   2948 O  O   . ARG B 1 28  ? 4.589   -4.144  27.357  1.00 11.21 ? 75  ARG B O   1 
ATOM   2949 C  CB  . ARG B 1 28  ? 6.791   -5.059  25.120  1.00 12.49 ? 75  ARG B CB  1 
ATOM   2950 C  CG  . ARG B 1 28  ? 7.735   -6.182  24.725  1.00 14.53 ? 75  ARG B CG  1 
ATOM   2951 C  CD  . ARG B 1 28  ? 9.180   -5.777  24.783  1.00 15.65 ? 75  ARG B CD  1 
ATOM   2952 N  NE  . ARG B 1 28  ? 10.035  -6.924  24.448  1.00 20.99 ? 75  ARG B NE  1 
ATOM   2953 C  CZ  . ARG B 1 28  ? 10.896  -7.521  25.228  1.00 18.24 ? 75  ARG B CZ  1 
ATOM   2954 N  NH1 . ARG B 1 28  ? 11.130  -7.101  26.442  1.00 19.70 ? 75  ARG B NH1 1 
ATOM   2955 N  NH2 . ARG B 1 28  ? 11.595  -8.519  24.723  1.00 23.09 ? 75  ARG B NH2 1 
ATOM   2956 N  N   . LEU B 1 29  ? 5.913   -2.475  26.588  1.00 10.40 ? 76  LEU B N   1 
ATOM   2957 C  CA  . LEU B 1 29  ? 4.958   -1.392  26.792  1.00 10.03 ? 76  LEU B CA  1 
ATOM   2958 C  C   . LEU B 1 29  ? 4.909   -0.502  25.577  1.00 9.93  ? 76  LEU B C   1 
ATOM   2959 O  O   . LEU B 1 29  ? 5.947   -0.140  25.011  1.00 10.71 ? 76  LEU B O   1 
ATOM   2960 C  CB  . LEU B 1 29  ? 5.448   -0.533  27.942  1.00 11.05 ? 76  LEU B CB  1 
ATOM   2961 C  CG  . LEU B 1 29  ? 4.698   0.781   28.162  1.00 11.20 ? 76  LEU B CG  1 
ATOM   2962 C  CD1 . LEU B 1 29  ? 3.328   0.573   28.755  1.00 14.16 ? 76  LEU B CD1 1 
ATOM   2963 C  CD2 . LEU B 1 29  ? 5.566   1.709   29.025  1.00 14.03 ? 76  LEU B CD2 1 
ATOM   2964 N  N   . HIS B 1 30  ? 3.686   -0.084  25.221  1.00 9.57  ? 77  HIS B N   1 
ATOM   2965 C  CA  . HIS B 1 30  ? 3.476   1.062   24.372  1.00 9.56  ? 77  HIS B CA  1 
ATOM   2966 C  C   . HIS B 1 30  ? 2.470   1.912   25.088  1.00 10.33 ? 77  HIS B C   1 
ATOM   2967 O  O   . HIS B 1 30  ? 1.318   1.521   25.236  1.00 10.88 ? 77  HIS B O   1 
ATOM   2968 C  CB  . HIS B 1 30  ? 3.045   0.655   22.953  1.00 10.72 ? 77  HIS B CB  1 
ATOM   2969 C  CG  . HIS B 1 30  ? 3.083   1.785   21.994  1.00 10.91 ? 77  HIS B CG  1 
ATOM   2970 N  ND1 . HIS B 1 30  ? 2.579   1.702   20.731  1.00 14.05 ? 77  HIS B ND1 1 
ATOM   2971 C  CD2 . HIS B 1 30  ? 3.489   3.028   22.138  1.00 15.73 ? 77  HIS B CD2 1 
ATOM   2972 C  CE1 . HIS B 1 30  ? 2.783   2.834   20.108  1.00 14.71 ? 77  HIS B CE1 1 
ATOM   2973 N  NE2 . HIS B 1 30  ? 3.341   3.674   20.907  1.00 17.17 ? 77  HIS B NE2 1 
ATOM   2974 N  N   . PHE B 1 31  ? 2.914   3.087   25.548  1.00 10.20 ? 78  PHE B N   1 
ATOM   2975 C  CA  . PHE B 1 31  ? 2.060   4.014   26.287  1.00 9.97  ? 78  PHE B CA  1 
ATOM   2976 C  C   . PHE B 1 31  ? 1.764   5.215   25.429  1.00 10.66 ? 78  PHE B C   1 
ATOM   2977 O  O   . PHE B 1 31  ? 2.682   5.761   24.871  1.00 12.60 ? 78  PHE B O   1 
ATOM   2978 C  CB  . PHE B 1 31  ? 2.789   4.456   27.559  1.00 11.48 ? 78  PHE B CB  1 
ATOM   2979 C  CG  . PHE B 1 31  ? 1.894   5.157   28.560  1.00 11.49 ? 78  PHE B CG  1 
ATOM   2980 C  CD1 . PHE B 1 31  ? 1.589   6.502   28.427  1.00 12.13 ? 78  PHE B CD1 1 
ATOM   2981 C  CD2 . PHE B 1 31  ? 1.383   4.461   29.626  1.00 12.85 ? 78  PHE B CD2 1 
ATOM   2982 C  CE1 . PHE B 1 31  ? 0.760   7.115   29.369  1.00 13.00 ? 78  PHE B CE1 1 
ATOM   2983 C  CE2 . PHE B 1 31  ? 0.563   5.099   30.553  1.00 14.76 ? 78  PHE B CE2 1 
ATOM   2984 C  CZ  . PHE B 1 31  ? 0.261   6.395   30.383  1.00 13.92 ? 78  PHE B CZ  1 
ATOM   2985 N  N   . ALA B 1 32  ? 0.513   5.568   25.242  1.00 10.62 ? 79  ALA B N   1 
ATOM   2986 C  CA  . ALA B 1 32  ? 0.160   6.726   24.452  1.00 10.80 ? 79  ALA B CA  1 
ATOM   2987 C  C   . ALA B 1 32  ? -0.752  7.641   25.233  1.00 10.53 ? 79  ALA B C   1 
ATOM   2988 O  O   . ALA B 1 32  ? -1.699  7.191   25.870  1.00 11.62 ? 79  ALA B O   1 
ATOM   2989 C  CB  . ALA B 1 32  ? -0.534  6.326   23.184  1.00 14.46 ? 79  ALA B CB  1 
ATOM   2990 N  N   . ALA B 1 33  ? -0.472  8.934   25.166  1.00 9.81  ? 80  ALA B N   1 
ATOM   2991 C  CA  . ALA B 1 33  ? -1.357  9.972   25.664  1.00 10.13 ? 80  ALA B CA  1 
ATOM   2992 C  C   . ALA B 1 33  ? -2.064  10.583  24.467  1.00 10.76 ? 80  ALA B C   1 
ATOM   2993 O  O   . ALA B 1 33  ? -1.439  10.836  23.433  1.00 11.83 ? 80  ALA B O   1 
ATOM   2994 C  CB  . ALA B 1 33  ? -0.550  11.022  26.392  1.00 11.52 ? 80  ALA B CB  1 
ATOM   2995 N  N   . PHE B 1 34  ? -3.347  10.871  24.610  1.00 10.70 ? 81  PHE B N   1 
ATOM   2996 C  CA  . PHE B 1 34  ? -4.187  11.437  23.566  1.00 10.64 ? 81  PHE B CA  1 
ATOM   2997 C  C   . PHE B 1 34  ? -4.801  12.730  24.069  1.00 10.84 ? 81  PHE B C   1 
ATOM   2998 O  O   . PHE B 1 34  ? -5.112  12.859  25.250  1.00 12.24 ? 81  PHE B O   1 
ATOM   2999 C  CB  . PHE B 1 34  ? -5.332  10.485  23.231  1.00 11.21 ? 81  PHE B CB  1 
ATOM   3000 C  CG  . PHE B 1 34  ? -4.961  9.150   22.616  1.00 12.29 ? 81  PHE B CG  1 
ATOM   3001 C  CD1 . PHE B 1 34  ? -4.544  8.084   23.399  1.00 13.68 ? 81  PHE B CD1 1 
ATOM   3002 C  CD2 . PHE B 1 34  ? -5.008  8.992   21.256  1.00 13.96 ? 81  PHE B CD2 1 
ATOM   3003 C  CE1 . PHE B 1 34  ? -4.251  6.856   22.803  1.00 17.17 ? 81  PHE B CE1 1 
ATOM   3004 C  CE2 . PHE B 1 34  ? -4.742  7.764   20.681  1.00 15.31 ? 81  PHE B CE2 1 
ATOM   3005 C  CZ  . PHE B 1 34  ? -4.281  6.745   21.461  1.00 15.72 ? 81  PHE B CZ  1 
ATOM   3006 N  N   . ASP B 1 35  ? -4.981  13.657  23.133  1.00 11.03 ? 82  ASP B N   1 
ATOM   3007 C  CA  . ASP B 1 35  ? -5.784  14.850  23.351  1.00 12.11 ? 82  ASP B CA  1 
ATOM   3008 C  C   . ASP B 1 35  ? -7.085  14.725  22.589  1.00 12.69 ? 82  ASP B C   1 
ATOM   3009 O  O   . ASP B 1 35  ? -7.144  14.167  21.496  1.00 13.14 ? 82  ASP B O   1 
ATOM   3010 C  CB  . ASP B 1 35  ? -5.021  16.095  22.950  1.00 12.51 ? 82  ASP B CB  1 
ATOM   3011 C  CG  . ASP B 1 35  ? -3.956  16.481  23.949  1.00 13.96 ? 82  ASP B CG  1 
ATOM   3012 O  OD1 . ASP B 1 35  ? -4.040  16.060  25.120  1.00 14.97 ? 82  ASP B OD1 1 
ATOM   3013 O  OD2 . ASP B 1 35  ? -3.065  17.195  23.505  1.00 16.05 ? 82  ASP B OD2 1 
ATOM   3014 N  N   . VAL B 1 36  ? -8.163  15.185  23.217  1.00 13.18 ? 83  VAL B N   1 
ATOM   3015 C  CA  . VAL B 1 36  ? -9.493  15.142  22.625  1.00 13.45 ? 83  VAL B CA  1 
ATOM   3016 C  C   . VAL B 1 36  ? -9.756  16.392  21.815  1.00 15.35 ? 83  VAL B C   1 
ATOM   3017 O  O   . VAL B 1 36  ? -9.455  17.492  22.266  1.00 18.39 ? 83  VAL B O   1 
ATOM   3018 C  CB  . VAL B 1 36  ? -10.529 15.005  23.744  1.00 15.67 ? 83  VAL B CB  1 
ATOM   3019 C  CG1 . VAL B 1 36  ? -11.960 15.044  23.223  1.00 18.42 ? 83  VAL B CG1 1 
ATOM   3020 C  CG2 . VAL B 1 36  ? -10.249 13.759  24.554  1.00 17.80 ? 83  VAL B CG2 1 
ATOM   3021 N  N   . THR B 1 37  ? -10.276 16.219  20.609  1.00 14.97 ? 84  THR B N   1 
ATOM   3022 C  CA  . THR B 1 37  ? -10.509 17.343  19.723  1.00 17.13 ? 84  THR B CA  1 
ATOM   3023 C  C   . THR B 1 37  ? -11.987 17.684  19.625  1.00 20.07 ? 84  THR B C   1 
ATOM   3024 O  O   . THR B 1 37  ? -12.290 18.838  19.321  1.00 29.31 ? 84  THR B O   1 
ATOM   3025 C  CB  . THR B 1 37  ? -9.837  17.113  18.374  1.00 18.13 ? 84  THR B CB  1 
ATOM   3026 O  OG1 . THR B 1 37  ? -10.331 15.925  17.774  1.00 20.90 ? 84  THR B OG1 1 
ATOM   3027 C  CG2 . THR B 1 37  ? -8.352  16.905  18.583  1.00 19.20 ? 84  THR B CG2 1 
ATOM   3028 N  N   . THR B 1 38  ? -12.893 16.821  20.038  1.00 16.55 ? 85  THR B N   1 
ATOM   3029 C  CA  . THR B 1 38  ? -14.312 17.117  19.916  1.00 16.73 ? 85  THR B CA  1 
ATOM   3030 C  C   . THR B 1 38  ? -14.789 17.780  21.207  1.00 17.73 ? 85  THR B C   1 
ATOM   3031 O  O   . THR B 1 38  ? -14.315 17.453  22.300  1.00 17.80 ? 85  THR B O   1 
ATOM   3032 C  CB  . THR B 1 38  ? -15.050 15.815  19.609  1.00 19.32 ? 85  THR B CB  1 
ATOM   3033 O  OG1 . THR B 1 38  ? -16.421 16.188  19.478  1.00 19.10 ? 85  THR B OG1 1 
ATOM   3034 C  CG2 . THR B 1 38  ? -14.912 14.768  20.692  1.00 19.65 ? 85  THR B CG2 1 
ATOM   3035 N  N   . GLU B 1 39  ? -15.793 18.661  21.067  1.00 17.03 ? 86  GLU B N   1 
ATOM   3036 C  CA  . GLU B 1 39  ? -16.499 19.221  22.207  1.00 16.57 ? 86  GLU B CA  1 
ATOM   3037 C  C   . GLU B 1 39  ? -17.799 18.486  22.534  1.00 17.11 ? 86  GLU B C   1 
ATOM   3038 O  O   . GLU B 1 39  ? -18.454 18.783  23.542  1.00 19.50 ? 86  GLU B O   1 
ATOM   3039 C  CB  . GLU B 1 39  ? -16.940 20.662  21.921  1.00 19.42 ? 86  GLU B CB  1 
ATOM   3040 C  CG  . GLU B 1 39  ? -15.770 21.583  21.668  1.00 22.29 ? 86  GLU B CG  1 
ATOM   3041 C  CD  . GLU B 1 39  ? -16.204 23.019  21.363  1.00 22.21 ? 86  GLU B CD  1 
ATOM   3042 O  OE1 . GLU B 1 39  ? -17.419 23.300  21.280  1.00 25.31 ? 86  GLU B OE1 1 
ATOM   3043 O  OE2 . GLU B 1 39  ? -15.266 23.809  21.205  1.00 26.91 ? 86  GLU B OE2 1 
ATOM   3044 N  N   . ASP B 1 40  ? -18.143 17.486  21.706  1.00 17.21 ? 87  ASP B N   1 
ATOM   3045 C  CA  . ASP B 1 40  ? -19.444 16.828  21.705  1.00 18.14 ? 87  ASP B CA  1 
ATOM   3046 C  C   . ASP B 1 40  ? -19.387 15.597  22.612  1.00 16.62 ? 87  ASP B C   1 
ATOM   3047 O  O   . ASP B 1 40  ? -18.713 14.601  22.269  1.00 17.37 ? 87  ASP B O   1 
ATOM   3048 C  CB  . ASP B 1 40  ? -19.807 16.488  20.270  1.00 20.68 ? 87  ASP B CB  1 
ATOM   3049 C  CG  . ASP B 1 40  ? -21.100 15.719  20.010  1.00 24.39 ? 87  ASP B CG  1 
ATOM   3050 O  OD1 . ASP B 1 40  ? -21.736 15.284  20.956  1.00 26.63 ? 87  ASP B OD1 1 
ATOM   3051 O  OD2 . ASP B 1 40  ? -21.461 15.580  18.824  1.00 33.39 ? 87  ASP B OD2 1 
ATOM   3052 N  N   . ARG B 1 41  ? -20.034 15.647  23.755  1.00 16.70 ? 88  ARG B N   1 
ATOM   3053 C  CA  . ARG B 1 41  ? -20.016 14.566  24.709  1.00 17.70 ? 88  ARG B CA  1 
ATOM   3054 C  C   . ARG B 1 41  ? -20.535 13.288  24.064  1.00 18.14 ? 88  ARG B C   1 
ATOM   3055 O  O   . ARG B 1 41  ? -20.041 12.200  24.333  1.00 16.92 ? 88  ARG B O   1 
ATOM   3056 C  CB  . ARG B 1 41  ? -20.868 14.982  25.904  1.00 20.18 ? 88  ARG B CB  1 
ATOM   3057 C  CG  . ARG B 1 41  ? -20.952 13.943  26.998  1.00 21.50 ? 88  ARG B CG  1 
ATOM   3058 C  CD  . ARG B 1 41  ? -21.845 14.481  28.116  1.00 26.45 ? 88  ARG B CD  1 
ATOM   3059 N  NE  . ARG B 1 41  ? -21.988 13.509  29.195  1.00 30.68 ? 88  ARG B NE  1 
ATOM   3060 C  CZ  . ARG B 1 41  ? -21.762 13.684  30.483  1.00 31.00 ? 88  ARG B CZ  1 
ATOM   3061 N  NH1 . ARG B 1 41  ? -21.308 14.833  30.979  1.00 32.53 ? 88  ARG B NH1 1 
ATOM   3062 N  NH2 . ARG B 1 41  ? -22.031 12.671  31.288  1.00 35.58 ? 88  ARG B NH2 1 
ATOM   3063 N  N   . ALA B 1 42  ? -21.610 13.361  23.281  1.00 17.57 ? 89  ALA B N   1 
ATOM   3064 C  CA  . ALA B 1 42  ? -22.195 12.162  22.717  1.00 17.98 ? 89  ALA B CA  1 
ATOM   3065 C  C   . ALA B 1 42  ? -21.179 11.508  21.791  1.00 15.90 ? 89  ALA B C   1 
ATOM   3066 O  O   . ALA B 1 42  ? -21.085 10.273  21.782  1.00 17.95 ? 89  ALA B O   1 
ATOM   3067 C  CB  . ALA B 1 42  ? -23.471 12.484  21.979  1.00 19.54 ? 89  ALA B CB  1 
ATOM   3068 N  N   . ALA B 1 43  ? -20.449 12.292  21.012  1.00 16.09 ? 90  ALA B N   1 
ATOM   3069 C  CA  . ALA B 1 43  ? -19.464 11.760  20.105  1.00 16.41 ? 90  ALA B CA  1 
ATOM   3070 C  C   . ALA B 1 43  ? -18.334 11.100  20.884  1.00 16.74 ? 90  ALA B C   1 
ATOM   3071 O  O   . ALA B 1 43  ? -17.817 10.082  20.452  1.00 15.68 ? 90  ALA B O   1 
ATOM   3072 C  CB  . ALA B 1 43  ? -18.906 12.836  19.207  1.00 19.14 ? 90  ALA B CB  1 
ATOM   3073 N  N   . PHE B 1 44  ? -17.952 11.656  22.016  1.00 15.15 ? 91  PHE B N   1 
ATOM   3074 C  CA  . PHE B 1 44  ? -16.891 11.064  22.804  1.00 14.26 ? 91  PHE B CA  1 
ATOM   3075 C  C   . PHE B 1 44  ? -17.376 9.752   23.408  1.00 14.35 ? 91  PHE B C   1 
ATOM   3076 O  O   . PHE B 1 44  ? -16.620 8.767   23.432  1.00 14.54 ? 91  PHE B O   1 
ATOM   3077 C  CB  . PHE B 1 44  ? -16.439 12.088  23.853  1.00 15.00 ? 91  PHE B CB  1 
ATOM   3078 C  CG  . PHE B 1 44  ? -15.192 11.617  24.579  1.00 15.28 ? 91  PHE B CG  1 
ATOM   3079 C  CD1 . PHE B 1 44  ? -13.995 11.501  23.902  1.00 17.97 ? 91  PHE B CD1 1 
ATOM   3080 C  CD2 . PHE B 1 44  ? -15.276 11.193  25.885  1.00 16.14 ? 91  PHE B CD2 1 
ATOM   3081 C  CE1 . PHE B 1 44  ? -12.908 10.986  24.562  1.00 19.80 ? 91  PHE B CE1 1 
ATOM   3082 C  CE2 . PHE B 1 44  ? -14.153 10.733  26.549  1.00 17.36 ? 91  PHE B CE2 1 
ATOM   3083 C  CZ  . PHE B 1 44  ? -12.991 10.605  25.846  1.00 18.46 ? 91  PHE B CZ  1 
ATOM   3084 N  N   . VAL B 1 45  ? -18.578 9.710   23.954  1.00 14.68 ? 92  VAL B N   1 
ATOM   3085 C  CA  . VAL B 1 45  ? -19.114 8.456   24.466  1.00 13.91 ? 92  VAL B CA  1 
ATOM   3086 C  C   . VAL B 1 45  ? -19.173 7.377   23.389  1.00 13.68 ? 92  VAL B C   1 
ATOM   3087 O  O   . VAL B 1 45  ? -18.845 6.207   23.629  1.00 14.25 ? 92  VAL B O   1 
ATOM   3088 C  CB  . VAL B 1 45  ? -20.493 8.688   25.119  1.00 15.82 ? 92  VAL B CB  1 
ATOM   3089 C  CG1 . VAL B 1 45  ? -21.224 7.388   25.397  1.00 18.34 ? 92  VAL B CG1 1 
ATOM   3090 C  CG2 . VAL B 1 45  ? -20.289 9.507   26.386  1.00 17.25 ? 92  VAL B CG2 1 
ATOM   3091 N  N   . ALA B 1 46  ? -19.553 7.765   22.164  1.00 14.31 ? 93  ALA B N   1 
ATOM   3092 C  CA  . ALA B 1 46  ? -19.622 6.800   21.102  1.00 14.32 ? 93  ALA B CA  1 
ATOM   3093 C  C   . ALA B 1 46  ? -18.239 6.235   20.842  1.00 14.34 ? 93  ALA B C   1 
ATOM   3094 O  O   . ALA B 1 46  ? -18.093 5.028   20.563  1.00 15.28 ? 93  ALA B O   1 
ATOM   3095 C  CB  . ALA B 1 46  ? -20.223 7.452   19.876  1.00 15.00 ? 93  ALA B CB  1 
ATOM   3096 N  N   . LEU B 1 47  ? -17.221 7.078   20.912  1.00 14.37 ? 94  LEU B N   1 
ATOM   3097 C  CA  . LEU B 1 47  ? -15.838 6.654   20.772  1.00 13.78 ? 94  LEU B CA  1 
ATOM   3098 C  C   . LEU B 1 47  ? -15.474 5.654   21.854  1.00 12.87 ? 94  LEU B C   1 
ATOM   3099 O  O   . LEU B 1 47  ? -14.822 4.625   21.583  1.00 13.00 ? 94  LEU B O   1 
ATOM   3100 C  CB  . LEU B 1 47  ? -14.873 7.824   20.743  1.00 14.77 ? 94  LEU B CB  1 
ATOM   3101 C  CG  . LEU B 1 47  ? -13.402 7.431   20.651  1.00 17.01 ? 94  LEU B CG  1 
ATOM   3102 C  CD1 . LEU B 1 47  ? -13.079 6.733   19.362  1.00 19.85 ? 94  LEU B CD1 1 
ATOM   3103 C  CD2 . LEU B 1 47  ? -12.534 8.679   20.823  1.00 19.91 ? 94  LEU B CD2 1 
ATOM   3104 N  N   . LEU B 1 48  ? -15.740 5.973   23.100  1.00 12.25 ? 95  LEU B N   1 
ATOM   3105 C  CA  . LEU B 1 48  ? -15.415 5.063   24.188  1.00 12.80 ? 95  LEU B CA  1 
ATOM   3106 C  C   . LEU B 1 48  ? -16.045 3.698   23.959  1.00 13.11 ? 95  LEU B C   1 
ATOM   3107 O  O   . LEU B 1 48  ? -15.386 2.673   24.236  1.00 12.75 ? 95  LEU B O   1 
ATOM   3108 C  CB  . LEU B 1 48  ? -15.849 5.616   25.523  1.00 13.29 ? 95  LEU B CB  1 
ATOM   3109 C  CG  . LEU B 1 48  ? -15.016 6.808   25.986  1.00 14.70 ? 95  LEU B CG  1 
ATOM   3110 C  CD1 . LEU B 1 48  ? -15.683 7.417   27.181  1.00 17.31 ? 95  LEU B CD1 1 
ATOM   3111 C  CD2 . LEU B 1 48  ? -13.606 6.426   26.241  1.00 17.63 ? 95  LEU B CD2 1 
ATOM   3112 N  N   . LYS B 1 49  ? -17.288 3.631   23.481  1.00 12.73 ? 96  LYS B N   1 
ATOM   3113 C  CA  . LYS B 1 49  ? -17.896 2.344   23.184  1.00 12.61 ? 96  LYS B CA  1 
ATOM   3114 C  C   . LYS B 1 49  ? -17.170 1.614   22.061  1.00 12.76 ? 96  LYS B C   1 
ATOM   3115 O  O   . LYS B 1 49  ? -16.952 0.404   22.168  1.00 13.93 ? 96  LYS B O   1 
ATOM   3116 C  CB  . LYS B 1 49  ? -19.382 2.585   22.876  1.00 13.84 ? 96  LYS B CB  1 
ATOM   3117 C  CG  . LYS B 1 49  ? -20.134 2.979   24.065  1.00 15.79 ? 96  LYS B CG  1 
ATOM   3118 C  CD  . LYS B 1 49  ? -21.573 3.380   23.731  1.00 18.34 ? 96  LYS B CD  1 
ATOM   3119 C  CE  . LYS B 1 49  ? -22.395 3.706   24.936  1.00 20.06 ? 96  LYS B CE  1 
ATOM   3120 N  NZ  . LYS B 1 49  ? -23.739 4.147   24.557  1.00 22.82 ? 96  LYS B NZ  1 
ATOM   3121 N  N   . GLU B 1 50  ? -16.820 2.291   20.989  1.00 12.98 ? 97  GLU B N   1 
ATOM   3122 C  CA  . GLU B 1 50  ? -16.119 1.685   19.877  1.00 12.94 ? 97  GLU B CA  1 
ATOM   3123 C  C   . GLU B 1 50  ? -14.735 1.231   20.297  1.00 12.94 ? 97  GLU B C   1 
ATOM   3124 O  O   . GLU B 1 50  ? -14.302 0.153   19.904  1.00 12.73 ? 97  GLU B O   1 
ATOM   3125 C  CB  . GLU B 1 50  ? -15.982 2.693   18.754  1.00 16.86 ? 97  GLU B CB  1 
ATOM   3126 C  CG  . GLU B 1 50  ? -17.232 3.027   17.959  1.00 23.73 ? 97  GLU B CG  1 
ATOM   3127 C  CD  . GLU B 1 50  ? -16.844 3.805   16.701  1.00 30.21 ? 97  GLU B CD  1 
ATOM   3128 O  OE1 . GLU B 1 50  ? -17.484 4.851   16.455  1.00 40.71 ? 97  GLU B OE1 1 
ATOM   3129 O  OE2 . GLU B 1 50  ? -15.928 3.337   15.965  1.00 35.39 ? 97  GLU B OE2 1 
ATOM   3130 N  N   . TRP B 1 51  ? -14.044 2.015   21.100  1.00 12.17 ? 98  TRP B N   1 
ATOM   3131 C  CA  . TRP B 1 51  ? -12.767 1.589   21.621  1.00 12.32 ? 98  TRP B CA  1 
ATOM   3132 C  C   . TRP B 1 51  ? -12.899 0.375   22.520  1.00 12.43 ? 98  TRP B C   1 
ATOM   3133 O  O   . TRP B 1 51  ? -12.024 -0.502  22.462  1.00 12.28 ? 98  TRP B O   1 
ATOM   3134 C  CB  . TRP B 1 51  ? -12.121 2.737   22.406  1.00 12.10 ? 98  TRP B CB  1 
ATOM   3135 C  CG  . TRP B 1 51  ? -11.278 3.659   21.590  1.00 11.91 ? 98  TRP B CG  1 
ATOM   3136 C  CD1 . TRP B 1 51  ? -11.086 3.664   20.250  1.00 12.18 ? 98  TRP B CD1 1 
ATOM   3137 C  CD2 . TRP B 1 51  ? -10.338 4.618   22.121  1.00 12.79 ? 98  TRP B CD2 1 
ATOM   3138 N  NE1 . TRP B 1 51  ? -10.171 4.632   19.899  1.00 12.74 ? 98  TRP B NE1 1 
ATOM   3139 C  CE2 . TRP B 1 51  ? -9.658  5.187   21.029  1.00 12.44 ? 98  TRP B CE2 1 
ATOM   3140 C  CE3 . TRP B 1 51  ? -10.014 5.015   23.411  1.00 14.90 ? 98  TRP B CE3 1 
ATOM   3141 C  CZ2 . TRP B 1 51  ? -8.686  6.152   21.202  1.00 15.46 ? 98  TRP B CZ2 1 
ATOM   3142 C  CZ3 . TRP B 1 51  ? -8.994  5.929   23.575  1.00 17.92 ? 98  TRP B CZ3 1 
ATOM   3143 C  CH2 . TRP B 1 51  ? -8.353  6.509   22.474  1.00 17.70 ? 98  TRP B CH2 1 
ATOM   3144 N  N   . THR B 1 52  ? -13.937 0.289   23.347  1.00 11.15 ? 99  THR B N   1 
ATOM   3145 C  CA  . THR B 1 52  ? -14.080 -0.872  24.203  1.00 11.95 ? 99  THR B CA  1 
ATOM   3146 C  C   . THR B 1 52  ? -14.285 -2.103  23.334  1.00 12.63 ? 99  THR B C   1 
ATOM   3147 O  O   . THR B 1 52  ? -13.708 -3.155  23.622  1.00 13.03 ? 99  THR B O   1 
ATOM   3148 C  CB  . THR B 1 52  ? -15.232 -0.696  25.167  1.00 12.19 ? 99  THR B CB  1 
ATOM   3149 O  OG1 . THR B 1 52  ? -15.076 0.511   25.910  1.00 13.26 ? 99  THR B OG1 1 
ATOM   3150 C  CG2 . THR B 1 52  ? -15.232 -1.901  26.082  1.00 14.28 ? 99  THR B CG2 1 
ATOM   3151 N  N   . ALA B 1 53  ? -15.114 -2.013  22.301  1.00 12.16 ? 100 ALA B N   1 
ATOM   3152 C  CA  . ALA B 1 53  ? -15.357 -3.139  21.403  1.00 13.42 ? 100 ALA B CA  1 
ATOM   3153 C  C   . ALA B 1 53  ? -14.050 -3.579  20.771  1.00 11.85 ? 100 ALA B C   1 
ATOM   3154 O  O   . ALA B 1 53  ? -13.748 -4.779  20.695  1.00 13.20 ? 100 ALA B O   1 
ATOM   3155 C  CB  . ALA B 1 53  ? -16.396 -2.767  20.390  1.00 13.97 ? 100 ALA B CB  1 
ATOM   3156 N  N   . ALA B 1 54  ? -13.248 -2.619  20.327  1.00 11.61 ? 101 ALA B N   1 
ATOM   3157 C  CA  . ALA B 1 54  ? -11.957 -2.952  19.742  1.00 11.44 ? 101 ALA B CA  1 
ATOM   3158 C  C   . ALA B 1 54  ? -11.031 -3.610  20.751  1.00 11.54 ? 101 ALA B C   1 
ATOM   3159 O  O   . ALA B 1 54  ? -10.332 -4.582  20.433  1.00 11.89 ? 101 ALA B O   1 
ATOM   3160 C  CB  . ALA B 1 54  ? -11.324 -1.685  19.172  1.00 13.57 ? 101 ALA B CB  1 
ATOM   3161 N  N   . ALA B 1 55  ? -11.001 -3.116  21.995  1.00 11.71 ? 102 ALA B N   1 
ATOM   3162 C  CA  . ALA B 1 55  ? -10.140 -3.660  23.019  1.00 11.53 ? 102 ALA B CA  1 
ATOM   3163 C  C   . ALA B 1 55  ? -10.505 -5.099  23.297  1.00 11.86 ? 102 ALA B C   1 
ATOM   3164 O  O   . ALA B 1 55  ? -9.614  -5.912  23.531  1.00 12.32 ? 102 ALA B O   1 
ATOM   3165 C  CB  . ALA B 1 55  ? -10.170 -2.780  24.264  1.00 13.06 ? 102 ALA B CB  1 
ATOM   3166 N  N   . ARG B 1 56  ? -11.784 -5.440  23.281  1.00 11.96 ? 103 ARG B N   1 
ATOM   3167 C  CA  . ARG B 1 56  ? -12.193 -6.815  23.514  1.00 13.17 ? 103 ARG B CA  1 
ATOM   3168 C  C   . ARG B 1 56  ? -11.599 -7.711  22.461  1.00 13.82 ? 103 ARG B C   1 
ATOM   3169 O  O   . ARG B 1 56  ? -11.203 -8.844  22.782  1.00 15.92 ? 103 ARG B O   1 
ATOM   3170 C  CB  . ARG B 1 56  ? -13.718 -6.944  23.476  1.00 16.17 ? 103 ARG B CB  1 
ATOM   3171 C  CG  . ARG B 1 56  ? -14.422 -6.381  24.676  1.00 16.73 ? 103 ARG B CG  1 
ATOM   3172 C  CD  . ARG B 1 56  ? -15.837 -6.879  24.582  1.00 18.29 ? 103 ARG B CD  1 
ATOM   3173 N  NE  . ARG B 1 56  ? -16.453 -6.331  25.771  1.00 18.04 ? 103 ARG B NE  1 
ATOM   3174 C  CZ  . ARG B 1 56  ? -17.087 -5.216  25.804  1.00 18.42 ? 103 ARG B CZ  1 
ATOM   3175 N  NH1 . ARG B 1 56  ? -17.370 -4.579  24.691  1.00 21.46 ? 103 ARG B NH1 1 
ATOM   3176 N  NH2 . ARG B 1 56  ? -17.516 -4.753  26.958  1.00 19.69 ? 103 ARG B NH2 1 
ATOM   3177 N  N   . ARG B 1 57  ? -11.608 -7.280  21.206  1.00 12.26 ? 104 ARG B N   1 
ATOM   3178 C  CA  . ARG B 1 57  ? -11.051 -8.079  20.140  1.00 13.30 ? 104 ARG B CA  1 
ATOM   3179 C  C   . ARG B 1 57  ? -9.541  -8.154  20.303  1.00 12.86 ? 104 ARG B C   1 
ATOM   3180 O  O   . ARG B 1 57  ? -8.948  -9.225  20.263  1.00 13.31 ? 104 ARG B O   1 
ATOM   3181 C  CB  . ARG B 1 57  ? -11.378 -7.419  18.803  1.00 15.26 ? 104 ARG B CB  1 
ATOM   3182 C  CG  . ARG B 1 57  ? -12.843 -7.518  18.433  1.00 20.09 ? 104 ARG B CG  1 
ATOM   3183 C  CD  . ARG B 1 57  ? -13.184 -8.891  17.944  1.00 26.15 ? 104 ARG B CD  1 
ATOM   3184 N  NE  . ARG B 1 57  ? -14.496 -8.887  17.294  1.00 32.34 ? 104 ARG B NE  1 
ATOM   3185 C  CZ  . ARG B 1 57  ? -14.788 -8.267  16.149  1.00 38.84 ? 104 ARG B CZ  1 
ATOM   3186 N  NH1 . ARG B 1 57  ? -13.827 -7.807  15.368  1.00 35.43 ? 104 ARG B NH1 1 
ATOM   3187 N  NH2 . ARG B 1 57  ? -16.045 -8.129  15.766  1.00 39.43 ? 104 ARG B NH2 1 
ATOM   3188 N  N   . LEU B 1 58  ? -8.887  -6.995  20.502  1.00 11.61 ? 105 LEU B N   1 
ATOM   3189 C  CA  . LEU B 1 58  ? -7.431  -6.941  20.516  1.00 11.87 ? 105 LEU B CA  1 
ATOM   3190 C  C   . LEU B 1 58  ? -6.863  -7.832  21.599  1.00 11.19 ? 105 LEU B C   1 
ATOM   3191 O  O   . LEU B 1 58  ? -5.887  -8.531  21.370  1.00 10.76 ? 105 LEU B O   1 
ATOM   3192 C  CB  . LEU B 1 58  ? -6.964  -5.497  20.698  1.00 11.89 ? 105 LEU B CB  1 
ATOM   3193 C  CG  . LEU B 1 58  ? -7.224  -4.565  19.512  1.00 11.83 ? 105 LEU B CG  1 
ATOM   3194 C  CD1 . LEU B 1 58  ? -7.143  -3.115  19.947  1.00 12.62 ? 105 LEU B CD1 1 
ATOM   3195 C  CD2 . LEU B 1 58  ? -6.313  -4.869  18.361  1.00 15.05 ? 105 LEU B CD2 1 
ATOM   3196 N  N   . THR B 1 59  ? -7.445  -7.771  22.793  1.00 11.44 ? 106 THR B N   1 
ATOM   3197 C  CA  . THR B 1 59  ? -6.903  -8.535  23.909  1.00 11.53 ? 106 THR B CA  1 
ATOM   3198 C  C   . THR B 1 59  ? -7.127  -10.034 23.776  1.00 12.91 ? 106 THR B C   1 
ATOM   3199 O  O   . THR B 1 59  ? -6.445  -10.786 24.479  1.00 15.25 ? 106 THR B O   1 
ATOM   3200 C  CB  . THR B 1 59  ? -7.445  -8.006  25.243  1.00 12.10 ? 106 THR B CB  1 
ATOM   3201 O  OG1 . THR B 1 59  ? -8.858  -8.089  25.243  1.00 13.80 ? 106 THR B OG1 1 
ATOM   3202 C  CG2 . THR B 1 59  ? -7.014  -6.586  25.544  1.00 12.95 ? 106 THR B CG2 1 
ATOM   3203 N  N   . ALA B 1 60  ? -7.994  -10.454 22.861  1.00 13.42 ? 107 ALA B N   1 
ATOM   3204 C  CA  . ALA B 1 60  ? -8.235  -11.865 22.586  1.00 13.93 ? 107 ALA B CA  1 
ATOM   3205 C  C   . ALA B 1 60  ? -7.439  -12.290 21.360  1.00 16.70 ? 107 ALA B C   1 
ATOM   3206 O  O   . ALA B 1 60  ? -7.492  -13.436 20.910  1.00 18.16 ? 107 ALA B O   1 
ATOM   3207 C  CB  . ALA B 1 60  ? -9.695  -12.090 22.402  1.00 16.78 ? 107 ALA B CB  1 
ATOM   3208 N  N   . GLY B 1 61  ? -6.635  -11.438 20.770  1.00 13.87 ? 108 GLY B N   1 
ATOM   3209 C  CA  . GLY B 1 61  ? -5.805  -11.804 19.630  1.00 15.22 ? 108 GLY B CA  1 
ATOM   3210 C  C   . GLY B 1 61  ? -6.562  -11.711 18.312  1.00 16.17 ? 108 GLY B C   1 
ATOM   3211 O  O   . GLY B 1 61  ? -6.071  -12.201 17.282  1.00 18.45 ? 108 GLY B O   1 
ATOM   3212 N  N   . HIS B 1 62  ? -7.714  -11.059 18.283  1.00 14.77 ? 109 HIS B N   1 
ATOM   3213 C  CA  . HIS B 1 62  ? -8.517  -10.923 17.076  1.00 15.40 ? 109 HIS B CA  1 
ATOM   3214 C  C   . HIS B 1 62  ? -8.374  -9.526  16.499  1.00 14.16 ? 109 HIS B C   1 
ATOM   3215 O  O   . HIS B 1 62  ? -8.070  -8.559  17.214  1.00 15.08 ? 109 HIS B O   1 
ATOM   3216 C  CB  . HIS B 1 62  ? -9.998  -11.178 17.354  1.00 19.29 ? 109 HIS B CB  1 
ATOM   3217 C  CG  . HIS B 1 62  ? -10.246 -12.482 18.026  1.00 26.84 ? 109 HIS B CG  1 
ATOM   3218 N  ND1 . HIS B 1 62  ? -9.615  -13.639 17.628  1.00 33.28 ? 109 HIS B ND1 1 
ATOM   3219 C  CD2 . HIS B 1 62  ? -11.044 -12.825 19.052  1.00 31.16 ? 109 HIS B CD2 1 
ATOM   3220 C  CE1 . HIS B 1 62  ? -9.997  -14.638 18.427  1.00 33.10 ? 109 HIS B CE1 1 
ATOM   3221 N  NE2 . HIS B 1 62  ? -10.860 -14.168 19.287  1.00 31.71 ? 109 HIS B NE2 1 
ATOM   3222 N  N   . ALA B 1 63  ? -8.569  -9.396  15.196  1.00 15.74 ? 110 ALA B N   1 
ATOM   3223 C  CA  . ALA B 1 63  ? -8.559  -8.123  14.539  1.00 15.33 ? 110 ALA B CA  1 
ATOM   3224 C  C   . ALA B 1 63  ? -9.789  -7.321  14.894  1.00 15.75 ? 110 ALA B C   1 
ATOM   3225 O  O   . ALA B 1 63  ? -10.835 -7.900  15.214  1.00 17.55 ? 110 ALA B O   1 
ATOM   3226 C  CB  . ALA B 1 63  ? -8.541  -8.397  13.046  1.00 17.71 ? 110 ALA B CB  1 
ATOM   3227 N  N   . VAL B 1 64  ? -9.667  -6.009  14.789  1.00 13.13 ? 111 VAL B N   1 
ATOM   3228 C  CA  . VAL B 1 64  ? -10.783 -5.116  15.058  1.00 14.57 ? 111 VAL B CA  1 
ATOM   3229 C  C   . VAL B 1 64  ? -11.785 -5.159  13.916  1.00 16.60 ? 111 VAL B C   1 
ATOM   3230 O  O   . VAL B 1 64  ? -11.466 -5.437  12.749  1.00 15.79 ? 111 VAL B O   1 
ATOM   3231 C  CB  . VAL B 1 64  ? -10.335 -3.697  15.401  1.00 17.65 ? 111 VAL B CB  1 
ATOM   3232 C  CG1 . VAL B 1 64  ? -9.354  -3.718  16.554  1.00 17.66 ? 111 VAL B CG1 1 
ATOM   3233 C  CG2 . VAL B 1 64  ? -9.739  -2.940  14.252  1.00 18.50 ? 111 VAL B CG2 1 
ATOM   3234 N  N   . GLY B 1 65  ? -13.039 -4.843  14.280  1.00 17.85 ? 112 GLY B N   1 
ATOM   3235 C  CA  . GLY B 1 65  ? -14.073 -4.661  13.271  1.00 18.90 ? 112 GLY B CA  1 
ATOM   3236 C  C   . GLY B 1 65  ? -14.293 -5.929  12.451  1.00 20.64 ? 112 GLY B C   1 
ATOM   3237 O  O   . GLY B 1 65  ? -14.293 -7.028  12.984  1.00 21.86 ? 112 GLY B O   1 
ATOM   3238 N  N   . GLU B 1 66  ? -14.413 -5.760  11.136  1.00 22.40 ? 113 GLU B N   1 
ATOM   3239 C  CA  . GLU B 1 66  ? -14.657 -6.900  10.263  1.00 25.99 ? 113 GLU B CA  1 
ATOM   3240 C  C   . GLU B 1 66  ? -13.347 -7.549  9.825   1.00 25.50 ? 113 GLU B C   1 
ATOM   3241 O  O   . GLU B 1 66  ? -13.348 -8.481  9.026   1.00 28.86 ? 113 GLU B O   1 
ATOM   3242 C  CB  . GLU B 1 66  ? -15.461 -6.478  9.035   1.00 33.79 ? 113 GLU B CB  1 
ATOM   3243 C  CG  . GLU B 1 66  ? -16.869 -5.984  9.362   1.00 42.12 ? 113 GLU B CG  1 
ATOM   3244 C  CD  . GLU B 1 66  ? -17.704 -5.743  8.115   1.00 52.04 ? 113 GLU B CD  1 
ATOM   3245 O  OE1 . GLU B 1 66  ? -18.109 -4.581  7.885   1.00 58.09 ? 113 GLU B OE1 1 
ATOM   3246 O  OE2 . GLU B 1 66  ? -17.927 -6.723  7.365   1.00 59.05 ? 113 GLU B OE2 1 
ATOM   3247 N  N   . GLY B 1 67  ? -12.201 -7.068  10.318  1.00 19.67 ? 114 GLY B N   1 
ATOM   3248 C  CA  . GLY B 1 67  ? -10.955 -7.770  10.099  1.00 19.02 ? 114 GLY B CA  1 
ATOM   3249 C  C   . GLY B 1 67  ? -9.957  -6.941  9.297   1.00 15.54 ? 114 GLY B C   1 
ATOM   3250 O  O   . GLY B 1 67  ? -10.177 -5.803  8.955   1.00 16.06 ? 114 GLY B O   1 
ATOM   3251 N  N   . ALA B 1 68  ? -8.852  -7.598  8.983   1.00 14.97 ? 115 ALA B N   1 
ATOM   3252 C  CA  . ALA B 1 68  ? -7.725  -7.014  8.298   1.00 14.94 ? 115 ALA B CA  1 
ATOM   3253 C  C   . ALA B 1 68  ? -7.734  -7.285  6.790   1.00 15.81 ? 115 ALA B C   1 
ATOM   3254 O  O   . ALA B 1 68  ? -6.955  -6.714  6.062   1.00 16.11 ? 115 ALA B O   1 
ATOM   3255 C  CB  . ALA B 1 68  ? -6.473  -7.531  8.948   1.00 15.72 ? 115 ALA B CB  1 
ATOM   3256 N  N   . TYR B 1 69  ? -8.575  -8.225  6.341   1.00 17.03 ? 116 TYR B N   1 
ATOM   3257 C  CA  . TYR B 1 69  ? -8.663  -8.575  4.932   1.00 20.71 ? 116 TYR B CA  1 
ATOM   3258 C  C   . TYR B 1 69  ? -9.994  -9.297  4.756   1.00 20.20 ? 116 TYR B C   1 
ATOM   3259 O  O   . TYR B 1 69  ? -10.675 -9.589  5.712   1.00 22.60 ? 116 TYR B O   1 
ATOM   3260 C  CB  . TYR B 1 69  ? -7.442  -9.393  4.500   1.00 20.71 ? 116 TYR B CB  1 
ATOM   3261 C  CG  . TYR B 1 69  ? -7.377  -10.760 5.135   1.00 18.83 ? 116 TYR B CG  1 
ATOM   3262 C  CD1 . TYR B 1 69  ? -6.804  -10.942 6.376   1.00 20.99 ? 116 TYR B CD1 1 
ATOM   3263 C  CD2 . TYR B 1 69  ? -7.851  -11.887 4.475   1.00 23.09 ? 116 TYR B CD2 1 
ATOM   3264 C  CE1 . TYR B 1 69  ? -6.749  -12.181 6.976   1.00 24.34 ? 116 TYR B CE1 1 
ATOM   3265 C  CE2 . TYR B 1 69  ? -7.819  -13.130 5.075   1.00 25.96 ? 116 TYR B CE2 1 
ATOM   3266 C  CZ  . TYR B 1 69  ? -7.255  -13.284 6.322   1.00 27.32 ? 116 TYR B CZ  1 
ATOM   3267 O  OH  . TYR B 1 69  ? -7.213  -14.507 6.931   1.00 34.73 ? 116 TYR B OH  1 
ATOM   3268 N  N   . GLY B 1 70  ? -10.357 -9.500  3.483   1.00 26.49 ? 117 GLY B N   1 
ATOM   3269 C  CA  . GLY B 1 70  ? -11.516 -10.302 3.122   1.00 28.95 ? 117 GLY B CA  1 
ATOM   3270 C  C   . GLY B 1 70  ? -12.793 -9.471  3.058   1.00 29.23 ? 117 GLY B C   1 
ATOM   3271 O  O   . GLY B 1 70  ? -13.850 -9.986  2.700   1.00 32.94 ? 117 GLY B O   1 
ATOM   3272 N  N   . GLY B 1 71  ? -12.718 -8.174  3.369   1.00 28.95 ? 118 GLY B N   1 
ATOM   3273 C  CA  . GLY B 1 71  ? -13.884 -7.330  3.224   1.00 28.38 ? 118 GLY B CA  1 
ATOM   3274 C  C   . GLY B 1 71  ? -13.998 -6.817  1.793   1.00 27.87 ? 118 GLY B C   1 
ATOM   3275 O  O   . GLY B 1 71  ? -13.375 -7.330  0.874   1.00 28.80 ? 118 GLY B O   1 
ATOM   3276 N  N   . LEU B 1 72  ? -14.810 -5.777  1.643   1.00 25.50 ? 119 LEU B N   1 
ATOM   3277 C  CA  . LEU B 1 72  ? -15.029 -5.164  0.350   1.00 26.81 ? 119 LEU B CA  1 
ATOM   3278 C  C   . LEU B 1 72  ? -13.687 -4.668  -0.174  1.00 24.35 ? 119 LEU B C   1 
ATOM   3279 O  O   . LEU B 1 72  ? -13.009 -3.884  0.481   1.00 23.76 ? 119 LEU B O   1 
ATOM   3280 C  CB  . LEU B 1 72  ? -16.006 -3.996  0.466   1.00 34.96 ? 119 LEU B CB  1 
ATOM   3281 C  CG  . LEU B 1 72  ? -17.446 -4.329  0.878   1.00 42.71 ? 119 LEU B CG  1 
ATOM   3282 C  CD1 . LEU B 1 72  ? -18.192 -3.014  1.035   1.00 43.60 ? 119 LEU B CD1 1 
ATOM   3283 C  CD2 . LEU B 1 72  ? -18.153 -5.248  -0.122  1.00 44.12 ? 119 LEU B CD2 1 
ATOM   3284 N  N   . PRO B 1 73  ? -13.267 -4.998  -1.400  1.00 21.90 ? 120 PRO B N   1 
ATOM   3285 C  CA  . PRO B 1 73  ? -11.994 -4.484  -1.901  1.00 23.35 ? 120 PRO B CA  1 
ATOM   3286 C  C   . PRO B 1 73  ? -11.896 -2.964  -1.916  1.00 21.96 ? 120 PRO B C   1 
ATOM   3287 O  O   . PRO B 1 73  ? -10.802 -2.411  -1.807  1.00 20.37 ? 120 PRO B O   1 
ATOM   3288 C  CB  . PRO B 1 73  ? -11.870 -5.090  -3.314  1.00 27.13 ? 120 PRO B CB  1 
ATOM   3289 C  CG  . PRO B 1 73  ? -13.269 -5.582  -3.626  1.00 29.44 ? 120 PRO B CG  1 
ATOM   3290 C  CD  . PRO B 1 73  ? -13.917 -5.955  -2.314  1.00 26.45 ? 120 PRO B CD  1 
ATOM   3291 N  N   . GLU B 1 74  ? -13.019 -2.256  -2.076  1.00 19.38 ? 121 GLU B N   1 
ATOM   3292 C  CA  . GLU B 1 74  ? -12.976 -0.820  -2.273  1.00 21.07 ? 121 GLU B CA  1 
ATOM   3293 C  C   . GLU B 1 74  ? -12.991 -0.059  -0.939  1.00 19.70 ? 121 GLU B C   1 
ATOM   3294 O  O   . GLU B 1 74  ? -12.937 1.171   -0.928  1.00 22.55 ? 121 GLU B O   1 
ATOM   3295 C  CB  . GLU B 1 74  ? -14.123 -0.342  -3.177  1.00 27.80 ? 121 GLU B CB  1 
ATOM   3296 C  CG  . GLU B 1 74  ? -15.520 -0.695  -2.684  1.00 34.60 ? 121 GLU B CG  1 
ATOM   3297 C  CD  . GLU B 1 74  ? -16.068 -2.050  -3.118  1.00 37.44 ? 121 GLU B CD  1 
ATOM   3298 O  OE1 . GLU B 1 74  ? -15.367 -2.903  -3.733  1.00 37.51 ? 121 GLU B OE1 1 
ATOM   3299 O  OE2 . GLU B 1 74  ? -17.280 -2.215  -2.826  1.00 50.10 ? 121 GLU B OE2 1 
ATOM   3300 N  N   . ALA B 1 75  ? -13.016 -0.788  0.178   1.00 18.39 ? 122 ALA B N   1 
ATOM   3301 C  CA  . ALA B 1 75  ? -13.001 -0.154  1.476   1.00 18.77 ? 122 ALA B CA  1 
ATOM   3302 C  C   . ALA B 1 75  ? -11.648 -0.356  2.149   1.00 16.91 ? 122 ALA B C   1 
ATOM   3303 O  O   . ALA B 1 75  ? -10.987 -1.378  1.976   1.00 16.44 ? 122 ALA B O   1 
ATOM   3304 C  CB  . ALA B 1 75  ? -14.044 -0.752  2.352   1.00 21.30 ? 122 ALA B CB  1 
ATOM   3305 N  N   . PRO B 1 76  ? -11.203 0.629   2.935   1.00 15.78 ? 123 PRO B N   1 
ATOM   3306 C  CA  . PRO B 1 76  ? -10.030 0.421   3.774   1.00 16.53 ? 123 PRO B CA  1 
ATOM   3307 C  C   . PRO B 1 76  ? -10.355 -0.717  4.721   1.00 16.50 ? 123 PRO B C   1 
ATOM   3308 O  O   . PRO B 1 76  ? -11.471 -0.830  5.239   1.00 17.90 ? 123 PRO B O   1 
ATOM   3309 C  CB  . PRO B 1 76  ? -9.809  1.755   4.481   1.00 18.50 ? 123 PRO B CB  1 
ATOM   3310 C  CG  . PRO B 1 76  ? -10.710 2.749   3.765   1.00 22.25 ? 123 PRO B CG  1 
ATOM   3311 C  CD  . PRO B 1 76  ? -11.772 1.983   3.075   1.00 19.79 ? 123 PRO B CD  1 
ATOM   3312 N  N   . PRO B 1 77  ? -9.369  -1.572  5.050   1.00 16.15 ? 124 PRO B N   1 
ATOM   3313 C  CA  . PRO B 1 77  ? -9.610  -2.586  6.054   1.00 16.14 ? 124 PRO B CA  1 
ATOM   3314 C  C   . PRO B 1 77  ? -9.852  -1.987  7.435   1.00 16.00 ? 124 PRO B C   1 
ATOM   3315 O  O   . PRO B 1 77  ? -9.276  -0.952  7.759   1.00 16.25 ? 124 PRO B O   1 
ATOM   3316 C  CB  . PRO B 1 77  ? -8.367  -3.450  6.055   1.00 17.89 ? 124 PRO B CB  1 
ATOM   3317 C  CG  . PRO B 1 77  ? -7.315  -2.614  5.372   1.00 20.08 ? 124 PRO B CG  1 
ATOM   3318 C  CD  . PRO B 1 77  ? -8.035  -1.645  4.429   1.00 17.28 ? 124 PRO B CD  1 
ATOM   3319 N  N   . ASP B 1 78  ? -10.652 -2.660  8.229   1.00 14.53 ? 125 ASP B N   1 
ATOM   3320 C  CA  . ASP B 1 78  ? -10.996 -2.201  9.563   1.00 14.85 ? 125 ASP B CA  1 
ATOM   3321 C  C   . ASP B 1 78  ? -9.801  -2.314  10.503  1.00 15.17 ? 125 ASP B C   1 
ATOM   3322 O  O   . ASP B 1 78  ? -9.641  -1.470  11.378  1.00 17.56 ? 125 ASP B O   1 
ATOM   3323 C  CB  . ASP B 1 78  ? -12.186 -2.960  10.121  1.00 18.17 ? 125 ASP B CB  1 
ATOM   3324 C  CG  . ASP B 1 78  ? -13.568 -2.483  9.690   1.00 20.80 ? 125 ASP B CG  1 
ATOM   3325 O  OD1 . ASP B 1 78  ? -13.650 -1.450  8.998   1.00 26.39 ? 125 ASP B OD1 1 
ATOM   3326 O  OD2 . ASP B 1 78  ? -14.492 -3.202  10.084  1.00 26.70 ? 125 ASP B OD2 1 
ATOM   3327 N  N   . ASP B 1 79  ? -8.949  -3.321  10.315  1.00 12.32 ? 126 ASP B N   1 
ATOM   3328 C  CA  . ASP B 1 79  ? -7.785  -3.513  11.119  1.00 12.50 ? 126 ASP B CA  1 
ATOM   3329 C  C   . ASP B 1 79  ? -6.593  -3.377  10.198  1.00 11.40 ? 126 ASP B C   1 
ATOM   3330 O  O   . ASP B 1 79  ? -6.655  -3.877  9.085   1.00 13.07 ? 126 ASP B O   1 
ATOM   3331 C  CB  . ASP B 1 79  ? -7.804  -4.895  11.732  1.00 13.00 ? 126 ASP B CB  1 
ATOM   3332 C  CG  . ASP B 1 79  ? -6.708  -5.174  12.728  1.00 12.37 ? 126 ASP B CG  1 
ATOM   3333 O  OD1 . ASP B 1 79  ? -5.537  -5.210  12.306  1.00 12.08 ? 126 ASP B OD1 1 
ATOM   3334 O  OD2 . ASP B 1 79  ? -7.006  -5.277  13.903  1.00 14.23 ? 126 ASP B OD2 1 
ATOM   3335 N  N   . THR B 1 80  ? -5.510  -2.728  10.615  1.00 10.58 ? 127 THR B N   1 
ATOM   3336 C  CA  . THR B 1 80  ? -4.389  -2.404  9.758   1.00 11.12 ? 127 THR B CA  1 
ATOM   3337 C  C   . THR B 1 80  ? -3.500  -3.613  9.490   1.00 10.50 ? 127 THR B C   1 
ATOM   3338 O  O   . THR B 1 80  ? -2.641  -3.517  8.620   1.00 11.92 ? 127 THR B O   1 
ATOM   3339 C  CB  . THR B 1 80  ? -3.621  -1.230  10.355  1.00 11.07 ? 127 THR B CB  1 
ATOM   3340 O  OG1 . THR B 1 80  ? -3.125  -1.563  11.642  1.00 11.87 ? 127 THR B OG1 1 
ATOM   3341 C  CG2 . THR B 1 80  ? -4.496  0.008   10.388  1.00 11.75 ? 127 THR B CG2 1 
ATOM   3342 N  N   . GLY B 1 81  ? -3.656  -4.715  10.224  1.00 10.44 ? 128 GLY B N   1 
ATOM   3343 C  CA  . GLY B 1 81  ? -3.146  -6.013  9.760   1.00 11.30 ? 128 GLY B CA  1 
ATOM   3344 C  C   . GLY B 1 81  ? -1.793  -6.453  10.285  1.00 12.15 ? 128 GLY B C   1 
ATOM   3345 O  O   . GLY B 1 81  ? -1.408  -7.603  10.102  1.00 12.97 ? 128 GLY B O   1 
ATOM   3346 N  N   . GLU B 1 82  ? -1.054  -5.606  10.995  1.00 11.18 ? 129 GLU B N   1 
ATOM   3347 C  CA  . GLU B 1 82  ? 0.320   -5.933  11.353  1.00 11.54 ? 129 GLU B CA  1 
ATOM   3348 C  C   . GLU B 1 82  ? 0.404   -6.921  12.502  1.00 11.96 ? 129 GLU B C   1 
ATOM   3349 O  O   . GLU B 1 82  ? 1.525   -7.353  12.814  1.00 14.47 ? 129 GLU B O   1 
ATOM   3350 C  CB  . GLU B 1 82  ? 1.189   -4.699  11.566  1.00 12.07 ? 129 GLU B CB  1 
ATOM   3351 C  CG  . GLU B 1 82  ? 0.905   -3.889  12.808  1.00 12.16 ? 129 GLU B CG  1 
ATOM   3352 C  CD  . GLU B 1 82  ? -0.159  -2.815  12.667  1.00 11.43 ? 129 GLU B CD  1 
ATOM   3353 O  OE1 . GLU B 1 82  ? -1.014  -2.930  11.766  1.00 12.34 ? 129 GLU B OE1 1 
ATOM   3354 O  OE2 . GLU B 1 82  ? -0.150  -1.857  13.473  1.00 13.03 ? 129 GLU B OE2 1 
ATOM   3355 N  N   . ALA B 1 83  ? -0.706  -7.279  13.135  1.00 11.40 ? 130 ALA B N   1 
ATOM   3356 C  CA  . ALA B 1 83  ? -0.674  -8.307  14.173  1.00 11.77 ? 130 ALA B CA  1 
ATOM   3357 C  C   . ALA B 1 83  ? -1.242  -9.644  13.694  1.00 12.94 ? 130 ALA B C   1 
ATOM   3358 O  O   . ALA B 1 83  ? -1.338  -10.583 14.472  1.00 14.42 ? 130 ALA B O   1 
ATOM   3359 C  CB  . ALA B 1 83  ? -1.364  -7.834  15.435  1.00 13.86 ? 130 ALA B CB  1 
ATOM   3360 N  N   . LEU B 1 84  ? -1.569  -9.750  12.426  1.00 12.54 ? 131 LEU B N   1 
ATOM   3361 C  CA  . LEU B 1 84  ? -2.019  -11.043 11.926  1.00 14.22 ? 131 LEU B CA  1 
ATOM   3362 C  C   . LEU B 1 84  ? -0.914  -12.067 12.097  1.00 15.55 ? 131 LEU B C   1 
ATOM   3363 O  O   . LEU B 1 84  ? 0.258   -11.824 11.832  1.00 17.15 ? 131 LEU B O   1 
ATOM   3364 C  CB  . LEU B 1 84  ? -2.346  -10.964 10.459  1.00 14.83 ? 131 LEU B CB  1 
ATOM   3365 C  CG  . LEU B 1 84  ? -3.564  -10.158 10.074  1.00 16.48 ? 131 LEU B CG  1 
ATOM   3366 C  CD1 . LEU B 1 84  ? -3.557  -10.067 8.531   1.00 18.53 ? 131 LEU B CD1 1 
ATOM   3367 C  CD2 . LEU B 1 84  ? -4.819  -10.855 10.637  1.00 19.96 ? 131 LEU B CD2 1 
ATOM   3368 N  N   . GLY B 1 85  ? -1.335  -13.211 12.613  1.00 17.20 ? 132 GLY B N   1 
ATOM   3369 C  CA  . GLY B 1 85  ? -0.412  -14.295 12.831  1.00 17.99 ? 132 GLY B CA  1 
ATOM   3370 C  C   . GLY B 1 85  ? 0.264   -14.276 14.184  1.00 18.58 ? 132 GLY B C   1 
ATOM   3371 O  O   . GLY B 1 85  ? 1.031   -15.182 14.488  1.00 20.95 ? 132 GLY B O   1 
ATOM   3372 N  N   . LEU B 1 86  ? 0.039   -13.230 14.982  1.00 15.14 ? 133 LEU B N   1 
ATOM   3373 C  CA  . LEU B 1 86  ? 0.617   -13.155 16.302  1.00 15.41 ? 133 LEU B CA  1 
ATOM   3374 C  C   . LEU B 1 86  ? -0.397  -13.651 17.310  1.00 17.27 ? 133 LEU B C   1 
ATOM   3375 O  O   . LEU B 1 86  ? -1.587  -13.695 17.101  1.00 22.14 ? 133 LEU B O   1 
ATOM   3376 C  CB  . LEU B 1 86  ? 1.054   -11.724 16.600  1.00 16.10 ? 133 LEU B CB  1 
ATOM   3377 C  CG  . LEU B 1 86  ? 2.023   -11.108 15.593  1.00 15.92 ? 133 LEU B CG  1 
ATOM   3378 C  CD1 . LEU B 1 86  ? 2.410   -9.706  16.009  1.00 17.11 ? 133 LEU B CD1 1 
ATOM   3379 C  CD2 . LEU B 1 86  ? 3.266   -11.959 15.453  1.00 19.73 ? 133 LEU B CD2 1 
ATOM   3380 N  N   . LYS B 1 87  ? 0.118   -13.931 18.482  1.00 18.19 ? 134 LYS B N   1 
ATOM   3381 C  CA  . LYS B 1 87  ? -0.674  -14.419 19.590  1.00 18.35 ? 134 LYS B CA  1 
ATOM   3382 C  C   . LYS B 1 87  ? -1.197  -13.246 20.405  1.00 15.06 ? 134 LYS B C   1 
ATOM   3383 O  O   . LYS B 1 87  ? -0.677  -12.133 20.299  1.00 15.25 ? 134 LYS B O   1 
ATOM   3384 C  CB  . LYS B 1 87  ? 0.250   -15.268 20.468  1.00 21.52 ? 134 LYS B CB  1 
ATOM   3385 C  CG  . LYS B 1 87  ? 0.850   -16.502 19.773  1.00 28.29 ? 134 LYS B CG  1 
ATOM   3386 C  CD  . LYS B 1 87  ? -0.193  -17.519 19.352  1.00 35.54 ? 134 LYS B CD  1 
ATOM   3387 C  CE  . LYS B 1 87  ? 0.397   -18.893 19.197  1.00 41.87 ? 134 LYS B CE  1 
ATOM   3388 N  NZ  . LYS B 1 87  ? 1.368   -19.010 18.099  1.00 47.25 ? 134 LYS B NZ  1 
ATOM   3389 N  N   . PRO B 1 88  ? -2.171  -13.450 21.313  1.00 13.76 ? 135 PRO B N   1 
ATOM   3390 C  CA  . PRO B 1 88  ? -2.605  -12.366 22.187  1.00 13.91 ? 135 PRO B CA  1 
ATOM   3391 C  C   . PRO B 1 88  ? -1.464  -11.768 22.977  1.00 12.82 ? 135 PRO B C   1 
ATOM   3392 O  O   . PRO B 1 88  ? -1.537  -10.577 23.333  1.00 13.49 ? 135 PRO B O   1 
ATOM   3393 C  CB  . PRO B 1 88  ? -3.671  -13.012 23.102  1.00 15.55 ? 135 PRO B CB  1 
ATOM   3394 C  CG  . PRO B 1 88  ? -4.136  -14.197 22.345  1.00 17.94 ? 135 PRO B CG  1 
ATOM   3395 C  CD  . PRO B 1 88  ? -2.925  -14.685 21.565  1.00 15.31 ? 135 PRO B CD  1 
ATOM   3396 N  N   . SER B 1 89  ? -0.506  -12.568 23.405  1.00 11.96 ? 136 SER B N   1 
ATOM   3397 C  CA  A SER B 1 89  ? 0.712   -12.044 23.955  0.50 11.79 ? 136 SER B CA  1 
ATOM   3398 C  CA  B SER B 1 89  ? 0.732   -12.123 24.008  0.50 12.36 ? 136 SER B CA  1 
ATOM   3399 C  C   . SER B 1 89  ? 0.469   -11.375 25.312  1.00 11.38 ? 136 SER B C   1 
ATOM   3400 O  O   . SER B 1 89  ? 1.136   -10.408 25.673  1.00 11.59 ? 136 SER B O   1 
ATOM   3401 C  CB  A SER B 1 89  ? 1.301   -11.067 22.972  0.50 12.94 ? 136 SER B CB  1 
ATOM   3402 C  CB  B SER B 1 89  ? 1.553   -11.289 23.061  0.50 14.51 ? 136 SER B CB  1 
ATOM   3403 O  OG  A SER B 1 89  ? 2.694   -11.006 23.202  0.50 13.12 ? 136 SER B OG  1 
ATOM   3404 O  OG  B SER B 1 89  ? 1.877   -12.035 21.901  0.50 15.61 ? 136 SER B OG  1 
ATOM   3405 N  N   . ARG B 1 90  ? -0.547  -11.808 26.034  1.00 10.43 ? 137 ARG B N   1 
ATOM   3406 C  CA  . ARG B 1 90  ? -0.904  -11.223 27.318  1.00 10.99 ? 137 ARG B CA  1 
ATOM   3407 C  C   . ARG B 1 90  ? -1.255  -9.744  27.188  1.00 10.64 ? 137 ARG B C   1 
ATOM   3408 O  O   . ARG B 1 90  ? -1.093  -9.029  28.157  1.00 11.24 ? 137 ARG B O   1 
ATOM   3409 C  CB  . ARG B 1 90  ? 0.130   -11.499 28.406  1.00 10.55 ? 137 ARG B CB  1 
ATOM   3410 C  CG  . ARG B 1 90  ? 0.304   -13.003 28.653  1.00 11.44 ? 137 ARG B CG  1 
ATOM   3411 C  CD  . ARG B 1 90  ? 1.075   -13.233 29.888  1.00 12.96 ? 137 ARG B CD  1 
ATOM   3412 N  NE  . ARG B 1 90  ? 2.440   -12.703 29.845  1.00 12.18 ? 137 ARG B NE  1 
ATOM   3413 C  CZ  . ARG B 1 90  ? 3.278   -12.524 30.834  1.00 12.12 ? 137 ARG B CZ  1 
ATOM   3414 N  NH1 . ARG B 1 90  ? 4.476   -11.999 30.704  1.00 14.34 ? 137 ARG B NH1 1 
ATOM   3415 N  NH2 . ARG B 1 90  ? 2.899   -12.924 32.035  1.00 15.00 ? 137 ARG B NH2 1 
ATOM   3416 N  N   . LEU B 1 91  ? -1.763  -9.284  26.046  1.00 9.53  ? 138 LEU B N   1 
ATOM   3417 C  CA  . LEU B 1 91  ? -2.065  -7.880  25.864  1.00 9.37  ? 138 LEU B CA  1 
ATOM   3418 C  C   . LEU B 1 91  ? -3.077  -7.454  26.897  1.00 9.61  ? 138 LEU B C   1 
ATOM   3419 O  O   . LEU B 1 91  ? -4.138  -8.049  27.054  1.00 10.72 ? 138 LEU B O   1 
ATOM   3420 C  CB  . LEU B 1 91  ? -2.619  -7.640  24.488  1.00 10.01 ? 138 LEU B CB  1 
ATOM   3421 C  CG  . LEU B 1 91  ? -3.032  -6.180  24.231  1.00 10.32 ? 138 LEU B CG  1 
ATOM   3422 C  CD1 . LEU B 1 91  ? -1.873  -5.214  24.207  1.00 12.04 ? 138 LEU B CD1 1 
ATOM   3423 C  CD2 . LEU B 1 91  ? -3.798  -6.096  22.923  1.00 12.17 ? 138 LEU B CD2 1 
ATOM   3424 N  N   . THR B 1 92  ? -2.795  -6.333  27.558  1.00 9.14  ? 139 THR B N   1 
ATOM   3425 C  CA  . THR B 1 92  ? -3.774  -5.591  28.315  1.00 9.47  ? 139 THR B CA  1 
ATOM   3426 C  C   . THR B 1 92  ? -3.790  -4.157  27.804  1.00 8.79  ? 139 THR B C   1 
ATOM   3427 O  O   . THR B 1 92  ? -2.763  -3.619  27.366  1.00 9.31  ? 139 THR B O   1 
ATOM   3428 C  CB  . THR B 1 92  ? -3.454  -5.618  29.806  1.00 8.99  ? 139 THR B CB  1 
ATOM   3429 O  OG1 . THR B 1 92  ? -2.164  -5.104  30.092  1.00 9.84  ? 139 THR B OG1 1 
ATOM   3430 C  CG2 . THR B 1 92  ? -3.553  -7.010  30.395  1.00 9.76  ? 139 THR B CG2 1 
ATOM   3431 N  N   . LEU B 1 93  ? -4.952  -3.543  27.885  1.00 9.09  ? 140 LEU B N   1 
ATOM   3432 C  CA  . LEU B 1 93  ? -5.206  -2.158  27.474  1.00 9.17  ? 140 LEU B CA  1 
ATOM   3433 C  C   . LEU B 1 93  ? -5.897  -1.476  28.622  1.00 9.89  ? 140 LEU B C   1 
ATOM   3434 O  O   . LEU B 1 93  ? -6.960  -1.906  29.040  1.00 11.88 ? 140 LEU B O   1 
ATOM   3435 C  CB  . LEU B 1 93  ? -6.109  -2.126  26.253  1.00 9.97  ? 140 LEU B CB  1 
ATOM   3436 C  CG  . LEU B 1 93  ? -5.446  -2.690  24.997  1.00 10.78 ? 140 LEU B CG  1 
ATOM   3437 C  CD1 . LEU B 1 93  ? -6.461  -2.843  23.871  1.00 12.64 ? 140 LEU B CD1 1 
ATOM   3438 C  CD2 . LEU B 1 93  ? -4.307  -1.797  24.542  1.00 12.15 ? 140 LEU B CD2 1 
ATOM   3439 N  N   . THR B 1 94  ? -5.235  -0.468  29.174  1.00 9.90  ? 141 THR B N   1 
ATOM   3440 C  CA  . THR B 1 94  ? -5.719  0.220   30.360  1.00 9.50  ? 141 THR B CA  1 
ATOM   3441 C  C   . THR B 1 94  ? -5.899  1.692   30.001  1.00 10.17 ? 141 THR B C   1 
ATOM   3442 O  O   . THR B 1 94  ? -4.947  2.335   29.556  1.00 11.23 ? 141 THR B O   1 
ATOM   3443 C  CB  . THR B 1 94  ? -4.700  0.099   31.461  1.00 10.30 ? 141 THR B CB  1 
ATOM   3444 O  OG1 . THR B 1 94  ? -4.314  -1.270  31.596  1.00 11.73 ? 141 THR B OG1 1 
ATOM   3445 C  CG2 . THR B 1 94  ? -5.184  0.621   32.794  1.00 12.12 ? 141 THR B CG2 1 
ATOM   3446 N  N   . ILE B 1 95  ? -7.101  2.214   30.171  1.00 9.69  ? 142 ILE B N   1 
ATOM   3447 C  CA  . ILE B 1 95  ? -7.403  3.606   29.858  1.00 9.91  ? 142 ILE B CA  1 
ATOM   3448 C  C   . ILE B 1 95  ? -7.364  4.457   31.110  1.00 9.60  ? 142 ILE B C   1 
ATOM   3449 O  O   . ILE B 1 95  ? -7.731  4.016   32.168  1.00 10.38 ? 142 ILE B O   1 
ATOM   3450 C  CB  . ILE B 1 95  ? -8.745  3.704   29.125  1.00 10.66 ? 142 ILE B CB  1 
ATOM   3451 C  CG1 . ILE B 1 95  ? -8.901  5.089   28.468  1.00 12.71 ? 142 ILE B CG1 1 
ATOM   3452 C  CG2 . ILE B 1 95  ? -9.908  3.337   30.031  1.00 12.37 ? 142 ILE B CG2 1 
ATOM   3453 C  CD1 . ILE B 1 95  ? -10.023 5.194   27.444  1.00 15.16 ? 142 ILE B CD1 1 
ATOM   3454 N  N   . GLY B 1 96  ? -6.963  5.716   30.939  1.00 9.75  ? 143 GLY B N   1 
ATOM   3455 C  CA  . GLY B 1 96  ? -7.039  6.701   32.004  1.00 10.44 ? 143 GLY B CA  1 
ATOM   3456 C  C   . GLY B 1 96  ? -7.412  8.068   31.479  1.00 10.44 ? 143 GLY B C   1 
ATOM   3457 O  O   . GLY B 1 96  ? -7.229  8.351   30.317  1.00 10.68 ? 143 GLY B O   1 
ATOM   3458 N  N   . PHE B 1 97  ? -7.927  8.880   32.398  1.00 10.12 ? 144 PHE B N   1 
ATOM   3459 C  CA  . PHE B 1 97  ? -8.414  10.211  32.100  1.00 10.75 ? 144 PHE B CA  1 
ATOM   3460 C  C   . PHE B 1 97  ? -7.573  11.244  32.810  1.00 9.49  ? 144 PHE B C   1 
ATOM   3461 O  O   . PHE B 1 97  ? -7.422  11.183  34.027  1.00 11.15 ? 144 PHE B O   1 
ATOM   3462 C  CB  . PHE B 1 97  ? -9.874  10.316  32.538  1.00 12.70 ? 144 PHE B CB  1 
ATOM   3463 C  CG  . PHE B 1 97  ? -10.849 9.340   31.902  1.00 13.41 ? 144 PHE B CG  1 
ATOM   3464 C  CD1 . PHE B 1 97  ? -10.735 8.935   30.585  1.00 15.41 ? 144 PHE B CD1 1 
ATOM   3465 C  CD2 . PHE B 1 97  ? -11.874 8.787   32.652  1.00 15.93 ? 144 PHE B CD2 1 
ATOM   3466 C  CE1 . PHE B 1 97  ? -11.644 8.057   30.006  1.00 17.03 ? 144 PHE B CE1 1 
ATOM   3467 C  CE2 . PHE B 1 97  ? -12.759 7.898   32.072  1.00 17.86 ? 144 PHE B CE2 1 
ATOM   3468 C  CZ  . PHE B 1 97  ? -12.643 7.549   30.757  1.00 17.05 ? 144 PHE B CZ  1 
ATOM   3469 N  N   . GLY B 1 98  ? -7.049  12.212  32.065  1.00 10.50 ? 145 GLY B N   1 
ATOM   3470 C  CA  . GLY B 1 98  ? -6.233  13.252  32.651  1.00 10.81 ? 145 GLY B CA  1 
ATOM   3471 C  C   . GLY B 1 98  ? -7.079  14.391  33.204  1.00 11.84 ? 145 GLY B C   1 
ATOM   3472 O  O   . GLY B 1 98  ? -8.239  14.570  32.828  1.00 11.97 ? 145 GLY B O   1 
ATOM   3473 N  N   . PRO B 1 99  ? -6.463  15.226  34.065  1.00 12.18 ? 146 PRO B N   1 
ATOM   3474 C  CA  . PRO B 1 99  ? -7.194  16.372  34.631  1.00 12.92 ? 146 PRO B CA  1 
ATOM   3475 C  C   . PRO B 1 99  ? -7.823  17.239  33.561  1.00 13.70 ? 146 PRO B C   1 
ATOM   3476 O  O   . PRO B 1 99  ? -8.897  17.806  33.774  1.00 14.25 ? 146 PRO B O   1 
ATOM   3477 C  CB  . PRO B 1 99  ? -6.133  17.164  35.366  1.00 15.68 ? 146 PRO B CB  1 
ATOM   3478 C  CG  . PRO B 1 99  ? -5.021  16.229  35.611  1.00 15.95 ? 146 PRO B CG  1 
ATOM   3479 C  CD  . PRO B 1 99  ? -5.130  15.070  34.636  1.00 12.67 ? 146 PRO B CD  1 
ATOM   3480 N  N   . SER B 1 100 ? -7.155  17.408  32.436  1.00 11.78 ? 147 SER B N   1 
ATOM   3481 C  CA  . SER B 1 100 ? -7.637  18.313  31.415  1.00 13.49 ? 147 SER B CA  1 
ATOM   3482 C  C   . SER B 1 100 ? -8.932  17.803  30.789  1.00 14.05 ? 147 SER B C   1 
ATOM   3483 O  O   . SER B 1 100 ? -9.691  18.571  30.206  1.00 15.08 ? 147 SER B O   1 
ATOM   3484 C  CB  . SER B 1 100 ? -6.570  18.584  30.389  1.00 14.01 ? 147 SER B CB  1 
ATOM   3485 O  OG  . SER B 1 100 ? -6.051  17.343  29.889  1.00 15.06 ? 147 SER B OG  1 
ATOM   3486 N  N   . LEU B 1 101 ? -9.221  16.487  30.827  1.00 12.17 ? 148 LEU B N   1 
ATOM   3487 C  CA  . LEU B 1 101 ? -10.457 16.009  30.259  1.00 12.30 ? 148 LEU B CA  1 
ATOM   3488 C  C   . LEU B 1 101 ? -11.651 16.646  30.951  1.00 13.21 ? 148 LEU B C   1 
ATOM   3489 O  O   . LEU B 1 101 ? -12.702 16.812  30.358  1.00 13.71 ? 148 LEU B O   1 
ATOM   3490 C  CB  . LEU B 1 101 ? -10.500 14.492  30.381  1.00 13.29 ? 148 LEU B CB  1 
ATOM   3491 C  CG  . LEU B 1 101 ? -11.687 13.845  29.683  1.00 15.52 ? 148 LEU B CG  1 
ATOM   3492 C  CD1 . LEU B 1 101 ? -11.538 13.931  28.218  1.00 19.35 ? 148 LEU B CD1 1 
ATOM   3493 C  CD2 . LEU B 1 101 ? -11.831 12.428  30.117  1.00 19.69 ? 148 LEU B CD2 1 
ATOM   3494 N  N   . PHE B 1 102 ? -11.486 16.919  32.244  1.00 13.34 ? 149 PHE B N   1 
ATOM   3495 C  CA  . PHE B 1 102 ? -12.587 17.387  33.072  1.00 15.35 ? 149 PHE B CA  1 
ATOM   3496 C  C   . PHE B 1 102 ? -12.968 18.833  32.794  1.00 16.94 ? 149 PHE B C   1 
ATOM   3497 O  O   . PHE B 1 102 ? -14.010 19.241  33.294  1.00 20.69 ? 149 PHE B O   1 
ATOM   3498 C  CB  . PHE B 1 102 ? -12.273 17.134  34.545  1.00 14.56 ? 149 PHE B CB  1 
ATOM   3499 C  CG  . PHE B 1 102 ? -12.181 15.647  34.833  1.00 14.51 ? 149 PHE B CG  1 
ATOM   3500 C  CD1 . PHE B 1 102 ? -13.288 14.899  35.173  1.00 15.07 ? 149 PHE B CD1 1 
ATOM   3501 C  CD2 . PHE B 1 102 ? -10.969 14.987  34.757  1.00 14.96 ? 149 PHE B CD2 1 
ATOM   3502 C  CE1 . PHE B 1 102 ? -13.199 13.535  35.369  1.00 15.26 ? 149 PHE B CE1 1 
ATOM   3503 C  CE2 . PHE B 1 102 ? -10.885 13.615  34.946  1.00 15.61 ? 149 PHE B CE2 1 
ATOM   3504 C  CZ  . PHE B 1 102 ? -11.998 12.902  35.252  1.00 15.11 ? 149 PHE B CZ  1 
ATOM   3505 N  N   . THR B 1 103 ? -12.222 19.547  31.985  1.00 15.06 ? 150 THR B N   1 
ATOM   3506 C  CA  . THR B 1 103 ? -12.639 20.863  31.523  1.00 16.78 ? 150 THR B CA  1 
ATOM   3507 C  C   . THR B 1 103 ? -13.593 20.759  30.331  1.00 18.10 ? 150 THR B C   1 
ATOM   3508 O  O   . THR B 1 103 ? -14.100 21.777  29.832  1.00 20.76 ? 150 THR B O   1 
ATOM   3509 C  CB  . THR B 1 103 ? -11.408 21.687  31.159  1.00 18.69 ? 150 THR B CB  1 
ATOM   3510 O  OG1 . THR B 1 103 ? -10.807 21.208  29.971  1.00 20.88 ? 150 THR B OG1 1 
ATOM   3511 C  CG2 . THR B 1 103 ? -10.391 21.766  32.280  1.00 21.16 ? 150 THR B CG2 1 
ATOM   3512 N  N   . ARG B 1 104 ? -13.856 19.553  29.812  1.00 16.36 ? 151 ARG B N   1 
ATOM   3513 C  CA  . ARG B 1 104 ? -14.754 19.305  28.706  1.00 17.15 ? 151 ARG B CA  1 
ATOM   3514 C  C   . ARG B 1 104 ? -15.992 18.583  29.186  1.00 16.32 ? 151 ARG B C   1 
ATOM   3515 O  O   . ARG B 1 104 ? -16.024 17.985  30.254  1.00 15.81 ? 151 ARG B O   1 
ATOM   3516 C  CB  . ARG B 1 104 ? -14.182 18.370  27.627  1.00 19.26 ? 151 ARG B CB  1 
ATOM   3517 C  CG  . ARG B 1 104 ? -12.942 18.990  27.021  1.00 23.75 ? 151 ARG B CG  1 
ATOM   3518 C  CD  . ARG B 1 104 ? -12.514 18.193  25.789  1.00 26.21 ? 151 ARG B CD  1 
ATOM   3519 N  NE  . ARG B 1 104 ? -11.379 18.910  25.214  1.00 27.75 ? 151 ARG B NE  1 
ATOM   3520 C  CZ  . ARG B 1 104 ? -11.422 19.658  24.137  1.00 27.00 ? 151 ARG B CZ  1 
ATOM   3521 N  NH1 . ARG B 1 104 ? -12.458 19.573  23.312  1.00 26.95 ? 151 ARG B NH1 1 
ATOM   3522 N  NH2 . ARG B 1 104 ? -10.415 20.470  23.869  1.00 28.51 ? 151 ARG B NH2 1 
ATOM   3523 N  N   . PHE B 1 105 ? -17.038 18.649  28.376  1.00 16.68 ? 152 PHE B N   1 
ATOM   3524 C  CA  . PHE B 1 105 ? -18.202 17.794  28.497  1.00 17.86 ? 152 PHE B CA  1 
ATOM   3525 C  C   . PHE B 1 105 ? -18.988 18.030  29.790  1.00 17.85 ? 152 PHE B C   1 
ATOM   3526 O  O   . PHE B 1 105 ? -19.753 17.169  30.202  1.00 20.86 ? 152 PHE B O   1 
ATOM   3527 C  CB  . PHE B 1 105 ? -17.787 16.321  28.400  1.00 17.43 ? 152 PHE B CB  1 
ATOM   3528 C  CG  . PHE B 1 105 ? -16.938 15.966  27.199  1.00 16.79 ? 152 PHE B CG  1 
ATOM   3529 C  CD1 . PHE B 1 105 ? -17.231 16.420  25.932  1.00 17.74 ? 152 PHE B CD1 1 
ATOM   3530 C  CD2 . PHE B 1 105 ? -15.807 15.179  27.363  1.00 18.24 ? 152 PHE B CD2 1 
ATOM   3531 C  CE1 . PHE B 1 105 ? -16.414 16.109  24.857  1.00 17.32 ? 152 PHE B CE1 1 
ATOM   3532 C  CE2 . PHE B 1 105 ? -15.013 14.841  26.286  1.00 17.97 ? 152 PHE B CE2 1 
ATOM   3533 C  CZ  . PHE B 1 105 ? -15.338 15.260  25.041  1.00 18.90 ? 152 PHE B CZ  1 
ATOM   3534 N  N   . GLY B 1 106 ? -18.756 19.166  30.442  1.00 19.64 ? 153 GLY B N   1 
ATOM   3535 C  CA  . GLY B 1 106 ? -19.450 19.528  31.664  1.00 19.97 ? 153 GLY B CA  1 
ATOM   3536 C  C   . GLY B 1 106 ? -18.972 18.743  32.876  1.00 21.79 ? 153 GLY B C   1 
ATOM   3537 O  O   . GLY B 1 106 ? -19.698 18.578  33.841  1.00 22.52 ? 153 GLY B O   1 
ATOM   3538 N  N   . LEU B 1 107 ? -17.742 18.226  32.819  1.00 17.66 ? 154 LEU B N   1 
ATOM   3539 C  CA  . LEU B 1 107 ? -17.296 17.278  33.820  1.00 17.20 ? 154 LEU B CA  1 
ATOM   3540 C  C   . LEU B 1 107 ? -16.558 17.942  34.983  1.00 14.50 ? 154 LEU B C   1 
ATOM   3541 O  O   . LEU B 1 107 ? -16.016 17.234  35.815  1.00 15.05 ? 154 LEU B O   1 
ATOM   3542 C  CB  . LEU B 1 107 ? -16.346 16.244  33.212  1.00 17.98 ? 154 LEU B CB  1 
ATOM   3543 C  CG  . LEU B 1 107 ? -16.903 15.285  32.172  1.00 19.72 ? 154 LEU B CG  1 
ATOM   3544 C  CD1 . LEU B 1 107 ? -15.728 14.543  31.547  1.00 19.83 ? 154 LEU B CD1 1 
ATOM   3545 C  CD2 . LEU B 1 107 ? -17.852 14.313  32.795  1.00 22.24 ? 154 LEU B CD2 1 
ATOM   3546 N  N   . ALA B 1 108 ? -16.490 19.286  35.101  1.00 14.93 ? 155 ALA B N   1 
ATOM   3547 C  CA  . ALA B 1 108 ? -15.531 19.859  36.033  1.00 16.07 ? 155 ALA B CA  1 
ATOM   3548 C  C   . ALA B 1 108 ? -15.770 19.444  37.476  1.00 15.84 ? 155 ALA B C   1 
ATOM   3549 O  O   . ALA B 1 108 ? -14.829 19.212  38.246  1.00 19.83 ? 155 ALA B O   1 
ATOM   3550 C  CB  . ALA B 1 108 ? -15.544 21.364  35.920  1.00 18.83 ? 155 ALA B CB  1 
ATOM   3551 N  N   . ASP B 1 109 ? -17.038 19.268  37.867  1.00 14.43 ? 156 ASP B N   1 
ATOM   3552 C  CA  . ASP B 1 109 ? -17.366 18.874  39.211  1.00 14.66 ? 156 ASP B CA  1 
ATOM   3553 C  C   . ASP B 1 109 ? -17.251 17.374  39.499  1.00 15.47 ? 156 ASP B C   1 
ATOM   3554 O  O   . ASP B 1 109 ? -17.507 16.929  40.611  1.00 18.24 ? 156 ASP B O   1 
ATOM   3555 C  CB  . ASP B 1 109 ? -18.762 19.361  39.590  1.00 15.55 ? 156 ASP B CB  1 
ATOM   3556 C  CG  . ASP B 1 109 ? -19.885 18.907  38.695  1.00 17.72 ? 156 ASP B CG  1 
ATOM   3557 O  OD1 . ASP B 1 109 ? -19.611 18.296  37.647  1.00 20.54 ? 156 ASP B OD1 1 
ATOM   3558 O  OD2 . ASP B 1 109 ? -21.067 19.212  38.981  1.00 20.52 ? 156 ASP B OD2 1 
ATOM   3559 N  N   . LEU B 1 110 ? -16.786 16.585  38.519  1.00 14.20 ? 157 LEU B N   1 
ATOM   3560 C  CA  . LEU B 1 110 ? -16.606 15.153  38.687  1.00 13.96 ? 157 LEU B CA  1 
ATOM   3561 C  C   . LEU B 1 110 ? -15.116 14.818  38.697  1.00 14.60 ? 157 LEU B C   1 
ATOM   3562 O  O   . LEU B 1 110 ? -14.767 13.633  38.807  1.00 14.99 ? 157 LEU B O   1 
ATOM   3563 C  CB  . LEU B 1 110 ? -17.339 14.430  37.563  1.00 15.78 ? 157 LEU B CB  1 
ATOM   3564 C  CG  . LEU B 1 110 ? -18.862 14.453  37.708  1.00 19.07 ? 157 LEU B CG  1 
ATOM   3565 C  CD1 . LEU B 1 110 ? -19.563 13.848  36.518  1.00 21.23 ? 157 LEU B CD1 1 
ATOM   3566 C  CD2 . LEU B 1 110 ? -19.326 13.736  38.945  1.00 23.75 ? 157 LEU B CD2 1 
ATOM   3567 N  N   . ARG B 1 111 ? -14.216 15.795  38.593  1.00 13.24 ? 158 ARG B N   1 
ATOM   3568 C  CA  . ARG B 1 111 ? -12.798 15.535  38.729  1.00 14.05 ? 158 ARG B CA  1 
ATOM   3569 C  C   . ARG B 1 111 ? -12.533 15.041  40.138  1.00 14.72 ? 158 ARG B C   1 
ATOM   3570 O  O   . ARG B 1 111 ? -12.910 15.651  41.130  1.00 15.27 ? 158 ARG B O   1 
ATOM   3571 C  CB  . ARG B 1 111 ? -11.977 16.777  38.455  1.00 14.17 ? 158 ARG B CB  1 
ATOM   3572 C  CG  . ARG B 1 111 ? -10.495 16.480  38.613  1.00 15.96 ? 158 ARG B CG  1 
ATOM   3573 C  CD  . ARG B 1 111 ? -9.677  17.676  38.352  1.00 16.80 ? 158 ARG B CD  1 
ATOM   3574 N  NE  . ARG B 1 111 ? -8.288  17.387  38.732  1.00 15.98 ? 158 ARG B NE  1 
ATOM   3575 C  CZ  . ARG B 1 111 ? -7.373  18.317  38.559  1.00 15.98 ? 158 ARG B CZ  1 
ATOM   3576 N  NH1 . ARG B 1 111 ? -7.654  19.379  37.869  1.00 16.71 ? 158 ARG B NH1 1 
ATOM   3577 N  NH2 . ARG B 1 111 ? -6.188  18.133  39.079  1.00 16.80 ? 158 ARG B NH2 1 
ATOM   3578 N  N   . PRO B 1 112 ? -11.898 13.869  40.341  1.00 13.51 ? 159 PRO B N   1 
ATOM   3579 C  CA  . PRO B 1 112 ? -11.659 13.393  41.688  1.00 14.98 ? 159 PRO B CA  1 
ATOM   3580 C  C   . PRO B 1 112 ? -10.652 14.270  42.413  1.00 15.26 ? 159 PRO B C   1 
ATOM   3581 O  O   . PRO B 1 112 ? -9.692  14.712  41.808  1.00 14.55 ? 159 PRO B O   1 
ATOM   3582 C  CB  . PRO B 1 112 ? -11.055 11.980  41.469  1.00 14.87 ? 159 PRO B CB  1 
ATOM   3583 C  CG  . PRO B 1 112 ? -11.451 11.609  40.100  1.00 15.58 ? 159 PRO B CG  1 
ATOM   3584 C  CD  . PRO B 1 112 ? -11.520 12.881  39.304  1.00 13.80 ? 159 PRO B CD  1 
ATOM   3585 N  N   . GLU B 1 113 ? -10.878 14.513  43.692  1.00 17.52 ? 160 GLU B N   1 
ATOM   3586 C  CA  . GLU B 1 113 ? -9.891  15.242  44.459  1.00 18.97 ? 160 GLU B CA  1 
ATOM   3587 C  C   . GLU B 1 113 ? -8.551  14.502  44.493  1.00 16.33 ? 160 GLU B C   1 
ATOM   3588 O  O   . GLU B 1 113 ? -7.508  15.121  44.570  1.00 17.14 ? 160 GLU B O   1 
ATOM   3589 C  CB  . GLU B 1 113 ? -10.430 15.479  45.875  1.00 24.01 ? 160 GLU B CB  1 
ATOM   3590 C  CG  . GLU B 1 113 ? -11.523 16.550  45.916  1.00 29.27 ? 160 GLU B CG  1 
ATOM   3591 C  CD  . GLU B 1 113 ? -11.823 17.133  47.297  1.00 37.18 ? 160 GLU B CD  1 
ATOM   3592 O  OE1 . GLU B 1 113 ? -12.226 16.367  48.188  1.00 41.89 ? 160 GLU B OE1 1 
ATOM   3593 O  OE2 . GLU B 1 113 ? -11.630 18.349  47.492  1.00 42.55 ? 160 GLU B OE2 1 
ATOM   3594 N  N   . ALA B 1 114 ? -8.559  13.160  44.416  1.00 13.99 ? 161 ALA B N   1 
ATOM   3595 C  CA  . ALA B 1 114 ? -7.347  12.370  44.413  1.00 14.71 ? 161 ALA B CA  1 
ATOM   3596 C  C   . ALA B 1 114 ? -6.567  12.506  43.114  1.00 14.41 ? 161 ALA B C   1 
ATOM   3597 O  O   . ALA B 1 114 ? -5.412  12.109  43.093  1.00 15.02 ? 161 ALA B O   1 
ATOM   3598 C  CB  . ALA B 1 114 ? -7.701  10.925  44.673  1.00 15.66 ? 161 ALA B CB  1 
ATOM   3599 N  N   . LEU B 1 115 ? -7.173  13.056  42.084  1.00 13.19 ? 162 LEU B N   1 
ATOM   3600 C  CA  . LEU B 1 115 ? -6.475  13.345  40.853  1.00 13.48 ? 162 LEU B CA  1 
ATOM   3601 C  C   . LEU B 1 115 ? -5.848  14.726  40.965  1.00 13.99 ? 162 LEU B C   1 
ATOM   3602 O  O   . LEU B 1 115 ? -6.346  15.695  40.411  1.00 14.91 ? 162 LEU B O   1 
ATOM   3603 C  CB  . LEU B 1 115 ? -7.401  13.236  39.646  1.00 14.61 ? 162 LEU B CB  1 
ATOM   3604 C  CG  . LEU B 1 115 ? -6.699  13.399  38.287  1.00 14.09 ? 162 LEU B CG  1 
ATOM   3605 C  CD1 . LEU B 1 115 ? -5.651  12.324  38.010  1.00 14.89 ? 162 LEU B CD1 1 
ATOM   3606 C  CD2 . LEU B 1 115 ? -7.751  13.392  37.238  1.00 14.22 ? 162 LEU B CD2 1 
ATOM   3607 N  N   . ALA B 1 116 ? -4.780  14.788  41.761  1.00 14.53 ? 163 ALA B N   1 
ATOM   3608 C  CA  . ALA B 1 116 ? -4.143  16.063  42.067  1.00 15.86 ? 163 ALA B CA  1 
ATOM   3609 C  C   . ALA B 1 116 ? -3.130  16.424  41.006  1.00 16.68 ? 163 ALA B C   1 
ATOM   3610 O  O   . ALA B 1 116 ? -2.441  15.584  40.464  1.00 20.35 ? 163 ALA B O   1 
ATOM   3611 C  CB  . ALA B 1 116 ? -3.468  15.928  43.409  1.00 17.79 ? 163 ALA B CB  1 
ATOM   3612 N  N   . ASP B 1 117 ? -3.024  17.714  40.726  1.00 17.46 ? 164 ASP B N   1 
ATOM   3613 C  CA  . ASP B 1 117 ? -1.914  18.253  39.964  1.00 18.61 ? 164 ASP B CA  1 
ATOM   3614 C  C   . ASP B 1 117 ? -0.652  18.078  40.786  1.00 17.88 ? 164 ASP B C   1 
ATOM   3615 O  O   . ASP B 1 117 ? -0.651  18.282  41.995  1.00 20.51 ? 164 ASP B O   1 
ATOM   3616 C  CB  . ASP B 1 117 ? -2.140  19.733  39.719  1.00 20.61 ? 164 ASP B CB  1 
ATOM   3617 C  CG  . ASP B 1 117 ? -3.367  20.084  38.885  1.00 24.11 ? 164 ASP B CG  1 
ATOM   3618 O  OD1 . ASP B 1 117 ? -3.597  19.372  37.929  1.00 24.28 ? 164 ASP B OD1 1 
ATOM   3619 O  OD2 . ASP B 1 117 ? -3.961  21.135  39.144  1.00 34.62 ? 164 ASP B OD2 1 
ATOM   3620 N  N   . LEU B 1 118 ? 0.410   17.671  40.112  1.00 16.15 ? 165 LEU B N   1 
ATOM   3621 C  CA  . LEU B 1 118 ? 1.685   17.506  40.786  1.00 16.42 ? 165 LEU B CA  1 
ATOM   3622 C  C   . LEU B 1 118 ? 2.296   18.870  41.018  1.00 17.50 ? 165 LEU B C   1 
ATOM   3623 O  O   . LEU B 1 118 ? 2.240   19.712  40.118  1.00 19.72 ? 165 LEU B O   1 
ATOM   3624 C  CB  . LEU B 1 118 ? 2.646   16.653  39.977  1.00 15.53 ? 165 LEU B CB  1 
ATOM   3625 C  CG  . LEU B 1 118 ? 2.203   15.223  39.703  1.00 15.26 ? 165 LEU B CG  1 
ATOM   3626 C  CD1 . LEU B 1 118 ? 3.170   14.492  38.862  1.00 17.59 ? 165 LEU B CD1 1 
ATOM   3627 C  CD2 . LEU B 1 118 ? 1.986   14.490  40.989  1.00 16.52 ? 165 LEU B CD2 1 
ATOM   3628 N  N   . PRO B 1 119 ? 2.994   19.024  42.147  1.00 18.50 ? 166 PRO B N   1 
ATOM   3629 C  CA  . PRO B 1 119 ? 3.796   20.218  42.316  1.00 20.32 ? 166 PRO B CA  1 
ATOM   3630 C  C   . PRO B 1 119 ? 5.019   20.143  41.427  1.00 19.81 ? 166 PRO B C   1 
ATOM   3631 O  O   . PRO B 1 119 ? 5.368   19.089  40.891  1.00 16.99 ? 166 PRO B O   1 
ATOM   3632 C  CB  . PRO B 1 119 ? 4.135   20.235  43.776  1.00 23.27 ? 166 PRO B CB  1 
ATOM   3633 C  CG  . PRO B 1 119 ? 4.089   18.838  44.185  1.00 23.08 ? 166 PRO B CG  1 
ATOM   3634 C  CD  . PRO B 1 119 ? 3.071   18.113  43.280  1.00 19.24 ? 166 PRO B CD  1 
ATOM   3635 N  N   . LYS B 1 120 ? 5.684   21.276  41.304  1.00 20.36 ? 167 LYS B N   1 
ATOM   3636 C  CA  . LYS B 1 120 ? 6.988   21.349  40.690  1.00 21.37 ? 167 LYS B CA  1 
ATOM   3637 C  C   . LYS B 1 120 ? 7.952   20.729  41.690  1.00 20.11 ? 167 LYS B C   1 
ATOM   3638 O  O   . LYS B 1 120 ? 7.909   21.040  42.885  1.00 24.52 ? 167 LYS B O   1 
ATOM   3639 C  CB  . LYS B 1 120 ? 7.278   22.840  40.509  1.00 25.85 ? 167 LYS B CB  1 
ATOM   3640 C  CG  . LYS B 1 120 ? 8.537   23.192  39.751  1.00 38.10 ? 167 LYS B CG  1 
ATOM   3641 C  CD  . LYS B 1 120 ? 8.655   24.687  39.456  1.00 44.21 ? 167 LYS B CD  1 
ATOM   3642 C  CE  . LYS B 1 120 ? 8.883   25.502  40.696  1.00 49.49 ? 167 LYS B CE  1 
ATOM   3643 N  NZ  . LYS B 1 120 ? 8.972   26.936  40.393  1.00 53.09 ? 167 LYS B NZ  1 
ATOM   3644 N  N   . PHE B 1 121 ? 8.778   19.809  41.232  1.00 16.10 ? 168 PHE B N   1 
ATOM   3645 C  CA  . PHE B 1 121 ? 9.770   19.204  42.102  1.00 15.12 ? 168 PHE B CA  1 
ATOM   3646 C  C   . PHE B 1 121 ? 11.142  19.731  41.724  1.00 15.71 ? 168 PHE B C   1 
ATOM   3647 O  O   . PHE B 1 121 ? 11.437  20.028  40.569  1.00 16.40 ? 168 PHE B O   1 
ATOM   3648 C  CB  . PHE B 1 121 ? 9.781   17.675  41.976  1.00 14.34 ? 168 PHE B CB  1 
ATOM   3649 C  CG  . PHE B 1 121 ? 8.494   17.064  42.493  1.00 14.78 ? 168 PHE B CG  1 
ATOM   3650 C  CD1 . PHE B 1 121 ? 8.265   16.899  43.848  1.00 15.85 ? 168 PHE B CD1 1 
ATOM   3651 C  CD2 . PHE B 1 121 ? 7.549   16.553  41.631  1.00 14.63 ? 168 PHE B CD2 1 
ATOM   3652 C  CE1 . PHE B 1 121 ? 7.101   16.338  44.323  1.00 17.21 ? 168 PHE B CE1 1 
ATOM   3653 C  CE2 . PHE B 1 121 ? 6.387   16.014  42.147  1.00 16.36 ? 168 PHE B CE2 1 
ATOM   3654 C  CZ  . PHE B 1 121 ? 6.189   15.893  43.453  1.00 17.76 ? 168 PHE B CZ  1 
ATOM   3655 N  N   . PRO B 1 122 ? 12.068  19.846  42.707  1.00 16.26 ? 169 PRO B N   1 
ATOM   3656 C  CA  . PRO B 1 122 ? 13.422  20.308  42.402  1.00 16.30 ? 169 PRO B CA  1 
ATOM   3657 C  C   . PRO B 1 122 ? 14.048  19.466  41.310  1.00 16.13 ? 169 PRO B C   1 
ATOM   3658 O  O   . PRO B 1 122 ? 13.992  18.236  41.315  1.00 17.03 ? 169 PRO B O   1 
ATOM   3659 C  CB  . PRO B 1 122 ? 14.176  20.160  43.702  1.00 18.56 ? 169 PRO B CB  1 
ATOM   3660 C  CG  . PRO B 1 122 ? 13.111  20.204  44.742  1.00 19.14 ? 169 PRO B CG  1 
ATOM   3661 C  CD  . PRO B 1 122 ? 11.847  19.620  44.136  1.00 16.84 ? 169 PRO B CD  1 
ATOM   3662 N  N   . GLY B 1 123 ? 14.655  20.134  40.348  1.00 15.79 ? 170 GLY B N   1 
ATOM   3663 C  CA  . GLY B 1 123 ? 15.362  19.470  39.270  1.00 16.95 ? 170 GLY B CA  1 
ATOM   3664 C  C   . GLY B 1 123 ? 14.450  19.050  38.100  1.00 15.36 ? 170 GLY B C   1 
ATOM   3665 O  O   . GLY B 1 123 ? 14.994  18.547  37.133  1.00 18.53 ? 170 GLY B O   1 
ATOM   3666 N  N   . ASP B 1 124 ? 13.135  19.293  38.198  1.00 15.87 ? 171 ASP B N   1 
ATOM   3667 C  CA  . ASP B 1 124 ? 12.237  18.985  37.083  1.00 18.09 ? 171 ASP B CA  1 
ATOM   3668 C  C   . ASP B 1 124 ? 12.741  19.716  35.844  1.00 17.53 ? 171 ASP B C   1 
ATOM   3669 O  O   . ASP B 1 124 ? 13.111  20.891  35.895  1.00 17.84 ? 171 ASP B O   1 
ATOM   3670 C  CB  . ASP B 1 124 ? 10.839  19.538  37.311  1.00 19.30 ? 171 ASP B CB  1 
ATOM   3671 C  CG  . ASP B 1 124 ? 9.833   18.698  38.090  1.00 20.86 ? 171 ASP B CG  1 
ATOM   3672 O  OD1 . ASP B 1 124 ? 10.182  17.558  38.381  1.00 19.34 ? 171 ASP B OD1 1 
ATOM   3673 O  OD2 . ASP B 1 124 ? 8.758   19.294  38.431  1.00 23.60 ? 171 ASP B OD2 1 
ATOM   3674 N  N   . ASN B 1 125 ? 12.684  19.075  34.698  1.00 15.72 ? 172 ASN B N   1 
ATOM   3675 C  CA  . ASN B 1 125 ? 12.931  19.693  33.422  1.00 15.80 ? 172 ASN B CA  1 
ATOM   3676 C  C   . ASN B 1 125 ? 11.918  19.148  32.424  1.00 15.14 ? 172 ASN B C   1 
ATOM   3677 O  O   . ASN B 1 125 ? 12.283  18.467  31.498  1.00 15.87 ? 172 ASN B O   1 
ATOM   3678 C  CB  . ASN B 1 125 ? 14.342  19.435  32.918  1.00 20.26 ? 172 ASN B CB  1 
ATOM   3679 C  CG  . ASN B 1 125 ? 14.693  20.237  31.696  1.00 25.09 ? 172 ASN B CG  1 
ATOM   3680 O  OD1 . ASN B 1 125 ? 14.049  21.238  31.383  1.00 27.66 ? 172 ASN B OD1 1 
ATOM   3681 N  ND2 . ASN B 1 125 ? 15.663  19.733  30.949  1.00 31.00 ? 172 ASN B ND2 1 
ATOM   3682 N  N   . LEU B 1 126 ? 10.672  19.489  32.623  1.00 14.69 ? 173 LEU B N   1 
ATOM   3683 C  CA  . LEU B 1 126 ? 9.602   18.786  31.917  1.00 15.49 ? 173 LEU B CA  1 
ATOM   3684 C  C   . LEU B 1 126 ? 9.410   19.373  30.535  1.00 16.89 ? 173 LEU B C   1 
ATOM   3685 O  O   . LEU B 1 126 ? 9.298   20.589  30.392  1.00 20.15 ? 173 LEU B O   1 
ATOM   3686 C  CB  . LEU B 1 126 ? 8.299   18.880  32.683  1.00 16.70 ? 173 LEU B CB  1 
ATOM   3687 C  CG  . LEU B 1 126 ? 8.323   18.343  34.113  1.00 16.71 ? 173 LEU B CG  1 
ATOM   3688 C  CD1 . LEU B 1 126 ? 6.950   18.483  34.768  1.00 17.89 ? 173 LEU B CD1 1 
ATOM   3689 C  CD2 . LEU B 1 126 ? 8.803   16.891  34.132  1.00 17.15 ? 173 LEU B CD2 1 
ATOM   3690 N  N   . ASP B 1 127 ? 9.338   18.498  29.568  1.00 14.97 ? 174 ASP B N   1 
ATOM   3691 C  CA  . ASP B 1 127 ? 9.054   18.871  28.184  1.00 16.52 ? 174 ASP B CA  1 
ATOM   3692 C  C   . ASP B 1 127 ? 7.541   18.881  28.099  1.00 17.15 ? 174 ASP B C   1 
ATOM   3693 O  O   . ASP B 1 127 ? 6.905   17.828  28.232  1.00 16.04 ? 174 ASP B O   1 
ATOM   3694 C  CB  . ASP B 1 127 ? 9.672   17.846  27.257  1.00 18.08 ? 174 ASP B CB  1 
ATOM   3695 C  CG  . ASP B 1 127 ? 9.418   18.051  25.766  1.00 21.82 ? 174 ASP B CG  1 
ATOM   3696 O  OD1 . ASP B 1 127 ? 8.571   18.899  25.452  1.00 23.29 ? 174 ASP B OD1 1 
ATOM   3697 O  OD2 . ASP B 1 127 ? 10.061  17.324  24.978  1.00 27.80 ? 174 ASP B OD2 1 
ATOM   3698 N  N   . ARG B 1 128 ? 6.952   20.032  27.797  1.00 18.70 ? 175 ARG B N   1 
ATOM   3699 C  CA  . ARG B 1 128 ? 5.507   20.158  27.763  1.00 20.31 ? 175 ARG B CA  1 
ATOM   3700 C  C   . ARG B 1 128 ? 4.889   19.279  26.685  1.00 19.48 ? 175 ARG B C   1 
ATOM   3701 O  O   . ARG B 1 128 ? 3.758   18.850  26.894  1.00 19.40 ? 175 ARG B O   1 
ATOM   3702 C  CB  . ARG B 1 128 ? 5.148   21.611  27.477  1.00 27.43 ? 175 ARG B CB  1 
ATOM   3703 C  CG  . ARG B 1 128 ? 5.578   22.574  28.571  1.00 37.78 ? 175 ARG B CG  1 
ATOM   3704 C  CD  . ARG B 1 128 ? 5.519   24.037  28.111  1.00 47.58 ? 175 ARG B CD  1 
ATOM   3705 N  NE  . ARG B 1 128 ? 4.318   24.297  27.306  1.00 55.87 ? 175 ARG B NE  1 
ATOM   3706 C  CZ  . ARG B 1 128 ? 3.058   24.220  27.736  1.00 59.00 ? 175 ARG B CZ  1 
ATOM   3707 N  NH1 . ARG B 1 128 ? 2.798   24.057  29.023  1.00 58.42 ? 175 ARG B NH1 1 
ATOM   3708 N  NH2 . ARG B 1 128 ? 2.059   24.326  26.874  1.00 60.09 ? 175 ARG B NH2 1 
ATOM   3709 N  N   . ALA B 1 129 ? 5.625   19.005  25.610  1.00 18.53 ? 176 ALA B N   1 
ATOM   3710 C  CA  . ALA B 1 129 ? 5.128   18.194  24.506  1.00 20.63 ? 176 ALA B CA  1 
ATOM   3711 C  C   . ALA B 1 129 ? 5.049   16.715  24.884  1.00 22.43 ? 176 ALA B C   1 
ATOM   3712 O  O   . ALA B 1 129 ? 4.312   15.974  24.222  1.00 25.98 ? 176 ALA B O   1 
ATOM   3713 C  CB  . ALA B 1 129 ? 5.986   18.390  23.275  1.00 24.21 ? 176 ALA B CB  1 
ATOM   3714 N  N   . ARG B 1 130 ? 5.810   16.296  25.894  1.00 17.73 ? 177 ARG B N   1 
ATOM   3715 C  CA  . ARG B 1 130 ? 5.814   14.918  26.344  1.00 18.04 ? 177 ARG B CA  1 
ATOM   3716 C  C   . ARG B 1 130 ? 5.239   14.818  27.739  1.00 15.92 ? 177 ARG B C   1 
ATOM   3717 O  O   . ARG B 1 130 ? 5.585   13.915  28.503  1.00 18.85 ? 177 ARG B O   1 
ATOM   3718 C  CB  . ARG B 1 130 ? 7.225   14.332  26.252  1.00 23.29 ? 177 ARG B CB  1 
ATOM   3719 C  CG  . ARG B 1 130 ? 7.551   14.249  24.765  1.00 29.57 ? 177 ARG B CG  1 
ATOM   3720 C  CD  . ARG B 1 130 ? 8.992   13.973  24.467  1.00 37.71 ? 177 ARG B CD  1 
ATOM   3721 N  NE  . ARG B 1 130 ? 9.257   12.553  24.241  1.00 44.15 ? 177 ARG B NE  1 
ATOM   3722 C  CZ  . ARG B 1 130 ? 10.450  12.061  23.945  1.00 45.40 ? 177 ARG B CZ  1 
ATOM   3723 N  NH1 . ARG B 1 130 ? 11.528  12.811  24.083  1.00 48.26 ? 177 ARG B NH1 1 
ATOM   3724 N  NH2 . ARG B 1 130 ? 10.560  10.804  23.565  1.00 45.01 ? 177 ARG B NH2 1 
ATOM   3725 N  N   . SER B 1 131 ? 4.359   15.765  28.060  1.00 13.81 ? 178 SER B N   1 
ATOM   3726 C  CA  . SER B 1 131 ? 3.714   15.825  29.342  1.00 13.20 ? 178 SER B CA  1 
ATOM   3727 C  C   . SER B 1 131 ? 2.221   15.989  29.137  1.00 14.08 ? 178 SER B C   1 
ATOM   3728 O  O   . SER B 1 131 ? 1.783   16.409  28.073  1.00 16.03 ? 178 SER B O   1 
ATOM   3729 C  CB  . SER B 1 131 ? 4.278   16.937  30.173  1.00 13.55 ? 178 SER B CB  1 
ATOM   3730 O  OG  . SER B 1 131 ? 5.647   16.700  30.481  1.00 14.12 ? 178 SER B OG  1 
ATOM   3731 N  N   . GLY B 1 132 ? 1.462   15.677  30.151  1.00 13.12 ? 179 GLY B N   1 
ATOM   3732 C  CA  . GLY B 1 132 ? 0.023   15.870  30.095  1.00 13.23 ? 179 GLY B CA  1 
ATOM   3733 C  C   . GLY B 1 132 ? -0.673  14.925  29.142  1.00 12.62 ? 179 GLY B C   1 
ATOM   3734 O  O   . GLY B 1 132 ? -0.188  13.866  28.803  1.00 14.34 ? 179 GLY B O   1 
ATOM   3735 N  N   . GLY B 1 133 ? -1.873  15.318  28.790  1.00 12.40 ? 180 GLY B N   1 
ATOM   3736 C  CA  . GLY B 1 133 ? -2.739  14.577  27.901  1.00 11.88 ? 180 GLY B CA  1 
ATOM   3737 C  C   . GLY B 1 133 ? -4.107  14.414  28.524  1.00 10.82 ? 180 GLY B C   1 
ATOM   3738 O  O   . GLY B 1 133 ? -4.259  14.175  29.710  1.00 11.83 ? 180 GLY B O   1 
ATOM   3739 N  N   . ASP B 1 134 ? -5.132  14.500  27.702  1.00 10.23 ? 181 ASP B N   1 
ATOM   3740 C  CA  . ASP B 1 134 ? -6.483  14.291  28.156  1.00 11.03 ? 181 ASP B CA  1 
ATOM   3741 C  C   . ASP B 1 134 ? -6.785  12.846  28.532  1.00 11.42 ? 181 ASP B C   1 
ATOM   3742 O  O   . ASP B 1 134 ? -7.633  12.617  29.386  1.00 11.59 ? 181 ASP B O   1 
ATOM   3743 C  CB  . ASP B 1 134 ? -7.477  14.720  27.090  1.00 11.89 ? 181 ASP B CB  1 
ATOM   3744 C  CG  . ASP B 1 134 ? -7.525  16.195  26.766  1.00 13.14 ? 181 ASP B CG  1 
ATOM   3745 O  OD1 . ASP B 1 134 ? -7.263  16.987  27.694  1.00 15.45 ? 181 ASP B OD1 1 
ATOM   3746 O  OD2 . ASP B 1 134 ? -7.797  16.563  25.633  1.00 13.91 ? 181 ASP B OD2 1 
ATOM   3747 N  N   . LEU B 1 135 ? -6.174  11.889  27.844  1.00 11.03 ? 182 LEU B N   1 
ATOM   3748 C  CA  . LEU B 1 135 ? -6.453  10.477  28.054  1.00 12.83 ? 182 LEU B CA  1 
ATOM   3749 C  C   . LEU B 1 135 ? -5.167  9.739   27.883  1.00 11.09 ? 182 LEU B C   1 
ATOM   3750 O  O   . LEU B 1 135 ? -4.299  10.215  27.193  1.00 11.83 ? 182 LEU B O   1 
ATOM   3751 C  CB  . LEU B 1 135 ? -7.366  9.850   26.977  1.00 20.73 ? 182 LEU B CB  1 
ATOM   3752 C  CG  . LEU B 1 135 ? -8.640  10.513  26.479  1.00 27.35 ? 182 LEU B CG  1 
ATOM   3753 C  CD1 . LEU B 1 135 ? -9.177  9.846   25.233  1.00 28.29 ? 182 LEU B CD1 1 
ATOM   3754 C  CD2 . LEU B 1 135 ? -9.625  10.360  27.608  1.00 29.91 ? 182 LEU B CD2 1 
ATOM   3755 N  N   . CYS B 1 136 ? -5.077  8.536   28.434  1.00 10.37 ? 183 CYS B N   1 
ATOM   3756 C  CA  . CYS B 1 136 ? -3.975  7.641   28.099  1.00 10.82 ? 183 CYS B CA  1 
ATOM   3757 C  C   . CYS B 1 136 ? -4.529  6.252   27.782  1.00 9.35  ? 183 CYS B C   1 
ATOM   3758 O  O   . CYS B 1 136 ? -5.565  5.831   28.281  1.00 10.11 ? 183 CYS B O   1 
ATOM   3759 C  CB  . CYS B 1 136 ? -2.921  7.514   29.193  1.00 12.91 ? 183 CYS B CB  1 
ATOM   3760 S  SG  . CYS B 1 136 ? -3.494  6.731   30.713  1.00 14.02 ? 183 CYS B SG  1 
ATOM   3761 N  N   . VAL B 1 137 ? -3.730  5.523   27.019  1.00 9.84  ? 184 VAL B N   1 
ATOM   3762 C  CA  . VAL B 1 137 ? -3.892  4.063   26.898  1.00 9.64  ? 184 VAL B CA  1 
ATOM   3763 C  C   . VAL B 1 137 ? -2.525  3.451   27.144  1.00 9.82  ? 184 VAL B C   1 
ATOM   3764 O  O   . VAL B 1 137 ? -1.552  3.724   26.440  1.00 10.59 ? 184 VAL B O   1 
ATOM   3765 C  CB  . VAL B 1 137 ? -4.479  3.610   25.571  1.00 10.34 ? 184 VAL B CB  1 
ATOM   3766 C  CG1 . VAL B 1 137 ? -4.551  2.101   25.516  1.00 12.90 ? 184 VAL B CG1 1 
ATOM   3767 C  CG2 . VAL B 1 137 ? -5.813  4.270   25.335  1.00 12.46 ? 184 VAL B CG2 1 
ATOM   3768 N  N   . GLN B 1 138 ? -2.474  2.596   28.171  1.00 9.80  ? 185 GLN B N   1 
ATOM   3769 C  CA  . GLN B 1 138 ? -1.313  1.772   28.448  1.00 9.48  ? 185 GLN B CA  1 
ATOM   3770 C  C   . GLN B 1 138 ? -1.516  0.428   27.781  1.00 9.23  ? 185 GLN B C   1 
ATOM   3771 O  O   . GLN B 1 138 ? -2.419  -0.305  28.166  1.00 10.20 ? 185 GLN B O   1 
ATOM   3772 C  CB  . GLN B 1 138 ? -1.158  1.587   29.939  1.00 9.34  ? 185 GLN B CB  1 
ATOM   3773 C  CG  . GLN B 1 138 ? -0.004  0.682   30.366  1.00 9.99  ? 185 GLN B CG  1 
ATOM   3774 C  CD  . GLN B 1 138 ? -0.081  0.315   31.819  1.00 11.02 ? 185 GLN B CD  1 
ATOM   3775 O  OE1 . GLN B 1 138 ? 0.393   1.072   32.658  1.00 12.89 ? 185 GLN B OE1 1 
ATOM   3776 N  NE2 . GLN B 1 138 ? -0.749  -0.785  32.124  1.00 11.39 ? 185 GLN B NE2 1 
ATOM   3777 N  N   . ALA B 1 139 ? -0.688  0.101   26.808  1.00 8.48  ? 186 ALA B N   1 
ATOM   3778 C  CA  . ALA B 1 139 ? -0.741  -1.180  26.114  1.00 9.29  ? 186 ALA B CA  1 
ATOM   3779 C  C   . ALA B 1 139 ? 0.461   -1.985  26.545  1.00 9.41  ? 186 ALA B C   1 
ATOM   3780 O  O   . ALA B 1 139 ? 1.596   -1.591  26.310  1.00 11.92 ? 186 ALA B O   1 
ATOM   3781 C  CB  . ALA B 1 139 ? -0.767  -1.014  24.605  1.00 9.74  ? 186 ALA B CB  1 
ATOM   3782 N  N   . CYS B 1 140 ? 0.269   -3.087  27.226  1.00 9.23  ? 187 CYS B N   1 
ATOM   3783 C  CA  . CYS B 1 140 ? 1.349   -3.956  27.656  1.00 10.04 ? 187 CYS B CA  1 
ATOM   3784 C  C   . CYS B 1 140 ? 1.166   -5.328  27.048  1.00 9.76  ? 187 CYS B C   1 
ATOM   3785 O  O   . CYS B 1 140 ? 0.041   -5.836  26.998  1.00 10.57 ? 187 CYS B O   1 
ATOM   3786 C  CB  . CYS B 1 140 ? 1.383   -4.143  29.175  1.00 9.73  ? 187 CYS B CB  1 
ATOM   3787 S  SG  . CYS B 1 140 ? 1.710   -2.627  30.075  1.00 12.01 ? 187 CYS B SG  1 
ATOM   3788 N  N   . ALA B 1 141 ? 2.243   -5.917  26.537  1.00 10.19 ? 188 ALA B N   1 
ATOM   3789 C  CA  . ALA B 1 141 ? 2.167   -7.228  25.907  1.00 9.72  ? 188 ALA B CA  1 
ATOM   3790 C  C   . ALA B 1 141 ? 3.553   -7.810  25.924  1.00 11.01 ? 188 ALA B C   1 
ATOM   3791 O  O   . ALA B 1 141 ? 4.512   -7.095  26.125  1.00 11.36 ? 188 ALA B O   1 
ATOM   3792 C  CB  . ALA B 1 141 ? 1.642   -7.149  24.494  1.00 10.64 ? 188 ALA B CB  1 
ATOM   3793 N  N   . ASP B 1 142 ? 3.687   -9.108  25.614  1.00 10.73 ? 189 ASP B N   1 
ATOM   3794 C  CA  . ASP B 1 142 ? 5.014   -9.693  25.519  1.00 10.73 ? 189 ASP B CA  1 
ATOM   3795 C  C   . ASP B 1 142 ? 5.683   -9.430  24.184  1.00 12.03 ? 189 ASP B C   1 
ATOM   3796 O  O   . ASP B 1 142 ? 6.905   -9.501  24.096  1.00 16.19 ? 189 ASP B O   1 
ATOM   3797 C  CB  . ASP B 1 142 ? 4.959   -11.177 25.836  1.00 10.92 ? 189 ASP B CB  1 
ATOM   3798 C  CG  . ASP B 1 142 ? 4.534   -11.429 27.266  1.00 12.78 ? 189 ASP B CG  1 
ATOM   3799 O  OD1 . ASP B 1 142 ? 4.892   -10.638 28.148  1.00 12.60 ? 189 ASP B OD1 1 
ATOM   3800 O  OD2 . ASP B 1 142 ? 3.848   -12.463 27.448  1.00 15.38 ? 189 ASP B OD2 1 
ATOM   3801 N  N   . ASP B 1 143 ? 4.909   -9.067  23.191  1.00 11.67 ? 190 ASP B N   1 
ATOM   3802 C  CA  . ASP B 1 143 ? 5.371   -8.840  21.834  1.00 11.94 ? 190 ASP B CA  1 
ATOM   3803 C  C   . ASP B 1 143 ? 5.116   -7.372  21.570  1.00 11.45 ? 190 ASP B C   1 
ATOM   3804 O  O   . ASP B 1 143 ? 3.975   -6.919  21.598  1.00 11.83 ? 190 ASP B O   1 
ATOM   3805 C  CB  . ASP B 1 143 ? 4.598   -9.721  20.871  1.00 13.81 ? 190 ASP B CB  1 
ATOM   3806 C  CG  . ASP B 1 143 ? 5.016   -9.609  19.427  1.00 16.03 ? 190 ASP B CG  1 
ATOM   3807 O  OD1 . ASP B 1 143 ? 5.440   -8.519  19.045  1.00 16.88 ? 190 ASP B OD1 1 
ATOM   3808 O  OD2 . ASP B 1 143 ? 4.753   -10.563 18.672  1.00 18.14 ? 190 ASP B OD2 1 
ATOM   3809 N  N   . PRO B 1 144 ? 6.149   -6.571  21.290  1.00 10.98 ? 191 PRO B N   1 
ATOM   3810 C  CA  . PRO B 1 144 ? 5.921   -5.156  21.083  1.00 11.29 ? 191 PRO B CA  1 
ATOM   3811 C  C   . PRO B 1 144 ? 5.043   -4.842  19.879  1.00 11.38 ? 191 PRO B C   1 
ATOM   3812 O  O   . PRO B 1 144 ? 4.385   -3.813  19.860  1.00 12.79 ? 191 PRO B O   1 
ATOM   3813 C  CB  . PRO B 1 144 ? 7.326   -4.588  20.875  1.00 12.02 ? 191 PRO B CB  1 
ATOM   3814 C  CG  . PRO B 1 144 ? 8.130   -5.731  20.404  1.00 13.81 ? 191 PRO B CG  1 
ATOM   3815 C  CD  . PRO B 1 144 ? 7.546   -6.969  20.989  1.00 11.71 ? 191 PRO B CD  1 
ATOM   3816 N  N   . GLN B 1 145 ? 5.060   -5.679  18.847  1.00 11.20 ? 192 GLN B N   1 
ATOM   3817 C  CA  . GLN B 1 145 ? 4.200   -5.417  17.712  1.00 11.13 ? 192 GLN B CA  1 
ATOM   3818 C  C   . GLN B 1 145 ? 2.736   -5.558  18.066  1.00 10.23 ? 192 GLN B C   1 
ATOM   3819 O  O   . GLN B 1 145 ? 1.893   -4.879  17.476  1.00 11.28 ? 192 GLN B O   1 
ATOM   3820 C  CB  . GLN B 1 145 ? 4.577   -6.358  16.580  1.00 13.01 ? 192 GLN B CB  1 
ATOM   3821 C  CG  . GLN B 1 145 ? 3.919   -5.934  15.268  1.00 14.67 ? 192 GLN B CG  1 
ATOM   3822 C  CD  . GLN B 1 145 ? 4.861   -6.153  14.108  1.00 15.62 ? 192 GLN B CD  1 
ATOM   3823 O  OE1 . GLN B 1 145 ? 6.084   -5.934  14.166  1.00 17.98 ? 192 GLN B OE1 1 
ATOM   3824 N  NE2 . GLN B 1 145 ? 4.293   -6.593  13.008  1.00 15.76 ? 192 GLN B NE2 1 
ATOM   3825 N  N   . VAL B 1 146 ? 2.378   -6.440  18.980  1.00 10.25 ? 193 VAL B N   1 
ATOM   3826 C  CA  . VAL B 1 146 ? 1.016   -6.533  19.435  1.00 9.87  ? 193 VAL B CA  1 
ATOM   3827 C  C   . VAL B 1 146 ? 0.609   -5.225  20.128  1.00 9.90  ? 193 VAL B C   1 
ATOM   3828 O  O   . VAL B 1 146 ? -0.495  -4.741  19.945  1.00 10.15 ? 193 VAL B O   1 
ATOM   3829 C  CB  . VAL B 1 146 ? 0.875   -7.788  20.304  1.00 10.73 ? 193 VAL B CB  1 
ATOM   3830 C  CG1 . VAL B 1 146 ? -0.456  -7.816  21.008  1.00 11.46 ? 193 VAL B CG1 1 
ATOM   3831 C  CG2 . VAL B 1 146 ? 1.057   -9.051  19.469  1.00 11.77 ? 193 VAL B CG2 1 
ATOM   3832 N  N   . ALA B 1 147 ? 1.482   -4.680  20.955  1.00 10.36 ? 194 ALA B N   1 
ATOM   3833 C  CA  . ALA B 1 147 ? 1.177   -3.427  21.645  1.00 10.23 ? 194 ALA B CA  1 
ATOM   3834 C  C   . ALA B 1 147 ? 1.069   -2.268  20.672  1.00 10.18 ? 194 ALA B C   1 
ATOM   3835 O  O   . ALA B 1 147 ? 0.134   -1.473  20.779  1.00 11.31 ? 194 ALA B O   1 
ATOM   3836 C  CB  . ALA B 1 147 ? 2.225   -3.183  22.680  1.00 11.16 ? 194 ALA B CB  1 
ATOM   3837 N  N   . VAL B 1 148 ? 2.031   -2.151  19.768  1.00 10.10 ? 195 VAL B N   1 
ATOM   3838 C  CA  . VAL B 1 148 ? 2.009   -1.061  18.805  1.00 10.47 ? 195 VAL B CA  1 
ATOM   3839 C  C   . VAL B 1 148 ? 0.751   -1.148  17.937  1.00 10.96 ? 195 VAL B C   1 
ATOM   3840 O  O   . VAL B 1 148 ? 0.073   -0.171  17.662  1.00 10.82 ? 195 VAL B O   1 
ATOM   3841 C  CB  . VAL B 1 148 ? 3.304   -1.055  17.988  1.00 12.35 ? 195 VAL B CB  1 
ATOM   3842 C  CG1 . VAL B 1 148 ? 3.239   -0.068  16.854  1.00 14.16 ? 195 VAL B CG1 1 
ATOM   3843 C  CG2 . VAL B 1 148 ? 4.527   -0.748  18.824  1.00 14.11 ? 195 VAL B CG2 1 
ATOM   3844 N  N   . HIS B 1 149 ? 0.407   -2.355  17.490  1.00 10.84 ? 196 HIS B N   1 
ATOM   3845 C  CA  . HIS B 1 149 ? -0.803  -2.553  16.713  1.00 10.01 ? 196 HIS B CA  1 
ATOM   3846 C  C   . HIS B 1 149 ? -2.041  -2.063  17.421  1.00 9.48  ? 196 HIS B C   1 
ATOM   3847 O  O   . HIS B 1 149 ? -2.899  -1.429  16.827  1.00 9.90  ? 196 HIS B O   1 
ATOM   3848 C  CB  . HIS B 1 149 ? -0.935  -4.027  16.333  1.00 9.65  ? 196 HIS B CB  1 
ATOM   3849 C  CG  . HIS B 1 149 ? -2.231  -4.377  15.683  1.00 10.32 ? 196 HIS B CG  1 
ATOM   3850 N  ND1 . HIS B 1 149 ? -3.258  -4.942  16.417  1.00 11.08 ? 196 HIS B ND1 1 
ATOM   3851 C  CD2 . HIS B 1 149 ? -2.706  -4.285  14.441  1.00 10.99 ? 196 HIS B CD2 1 
ATOM   3852 C  CE1 . HIS B 1 149 ? -4.290  -5.188  15.640  1.00 10.85 ? 196 HIS B CE1 1 
ATOM   3853 N  NE2 . HIS B 1 149 ? -3.982  -4.791  14.438  1.00 11.60 ? 196 HIS B NE2 1 
ATOM   3854 N  N   . ALA B 1 150 ? -2.117  -2.356  18.713  1.00 9.73  ? 197 ALA B N   1 
ATOM   3855 C  CA  . ALA B 1 150 ? -3.236  -1.878  19.498  1.00 9.94  ? 197 ALA B CA  1 
ATOM   3856 C  C   . ALA B 1 150 ? -3.335  -0.364  19.486  1.00 9.81  ? 197 ALA B C   1 
ATOM   3857 O  O   . ALA B 1 150 ? -4.385  0.202   19.239  1.00 11.35 ? 197 ALA B O   1 
ATOM   3858 C  CB  . ALA B 1 150 ? -3.200  -2.426  20.893  1.00 9.76  ? 197 ALA B CB  1 
ATOM   3859 N  N   . ILE B 1 151 ? -2.244  0.316   19.801  1.00 9.92  ? 198 ILE B N   1 
ATOM   3860 C  CA  . ILE B 1 151 ? -2.266  1.771   19.857  1.00 10.48 ? 198 ILE B CA  1 
ATOM   3861 C  C   . ILE B 1 151 ? -2.573  2.354   18.486  1.00 10.37 ? 198 ILE B C   1 
ATOM   3862 O  O   . ILE B 1 151 ? -3.365  3.276   18.351  1.00 10.98 ? 198 ILE B O   1 
ATOM   3863 C  CB  . ILE B 1 151 ? -0.962  2.312   20.437  1.00 11.73 ? 198 ILE B CB  1 
ATOM   3864 C  CG1 . ILE B 1 151 ? -0.766  1.838   21.860  1.00 13.65 ? 198 ILE B CG1 1 
ATOM   3865 C  CG2 . ILE B 1 151 ? -0.897  3.825   20.338  1.00 12.49 ? 198 ILE B CG2 1 
ATOM   3866 C  CD1 . ILE B 1 151 ? -1.829  2.278   22.819  1.00 15.36 ? 198 ILE B CD1 1 
ATOM   3867 N  N   . ARG B 1 152 ? -1.948  1.815   17.439  1.00 9.97  ? 199 ARG B N   1 
ATOM   3868 C  CA  . ARG B 1 152 ? -2.123  2.352   16.104  1.00 10.86 ? 199 ARG B CA  1 
ATOM   3869 C  C   . ARG B 1 152 ? -3.579  2.226   15.701  1.00 10.48 ? 199 ARG B C   1 
ATOM   3870 O  O   . ARG B 1 152 ? -4.137  3.117   15.075  1.00 11.52 ? 199 ARG B O   1 
ATOM   3871 C  CB  . ARG B 1 152 ? -1.193  1.605   15.169  1.00 12.72 ? 199 ARG B CB  1 
ATOM   3872 C  CG  . ARG B 1 152 ? -1.036  2.149   13.752  1.00 13.45 ? 199 ARG B CG  1 
ATOM   3873 C  CD  . ARG B 1 152 ? -1.987  1.459   12.847  1.00 13.65 ? 199 ARG B CD  1 
ATOM   3874 N  NE  . ARG B 1 152 ? -1.606  1.714   11.445  1.00 12.95 ? 199 ARG B NE  1 
ATOM   3875 C  CZ  . ARG B 1 152 ? -0.696  1.043   10.760  1.00 12.20 ? 199 ARG B CZ  1 
ATOM   3876 N  NH1 . ARG B 1 152 ? 0.115   0.165   11.334  1.00 13.15 ? 199 ARG B NH1 1 
ATOM   3877 N  NH2 . ARG B 1 152 ? -0.576  1.206   9.452   1.00 12.23 ? 199 ARG B NH2 1 
ATOM   3878 N  N   . ASN B 1 153 ? -4.236  1.107   16.023  1.00 10.19 ? 200 ASN B N   1 
ATOM   3879 C  CA  . ASN B 1 153 ? -5.613  0.914   15.624  1.00 10.69 ? 200 ASN B CA  1 
ATOM   3880 C  C   . ASN B 1 153 ? -6.576  1.702   16.482  1.00 10.79 ? 200 ASN B C   1 
ATOM   3881 O  O   . ASN B 1 153 ? -7.546  2.257   15.960  1.00 11.44 ? 200 ASN B O   1 
ATOM   3882 C  CB  . ASN B 1 153 ? -5.994  -0.563  15.575  1.00 10.12 ? 200 ASN B CB  1 
ATOM   3883 C  CG  . ASN B 1 153 ? -5.491  -1.210  14.317  1.00 10.90 ? 200 ASN B CG  1 
ATOM   3884 O  OD1 . ASN B 1 153 ? -6.232  -1.295  13.328  1.00 13.23 ? 200 ASN B OD1 1 
ATOM   3885 N  ND2 . ASN B 1 153 ? -4.233  -1.516  14.235  1.00 11.62 ? 200 ASN B ND2 1 
ATOM   3886 N  N   . LEU B 1 154 ? -6.340  1.843   17.772  1.00 10.49 ? 201 LEU B N   1 
ATOM   3887 C  CA  . LEU B 1 154 ? -7.175  2.748   18.556  1.00 10.44 ? 201 LEU B CA  1 
ATOM   3888 C  C   . LEU B 1 154 ? -7.058  4.185   18.051  1.00 10.07 ? 201 LEU B C   1 
ATOM   3889 O  O   . LEU B 1 154 ? -8.064  4.894   17.943  1.00 11.42 ? 201 LEU B O   1 
ATOM   3890 C  CB  . LEU B 1 154 ? -6.784  2.639   20.026  1.00 11.49 ? 201 LEU B CB  1 
ATOM   3891 C  CG  . LEU B 1 154 ? -7.130  1.320   20.708  1.00 14.01 ? 201 LEU B CG  1 
ATOM   3892 C  CD1 . LEU B 1 154 ? -6.521  1.291   22.094  1.00 16.79 ? 201 LEU B CD1 1 
ATOM   3893 C  CD2 . LEU B 1 154 ? -8.594  1.043   20.780  1.00 17.31 ? 201 LEU B CD2 1 
ATOM   3894 N  N   . ALA B 1 155 ? -5.837  4.616   17.736  1.00 10.47 ? 202 ALA B N   1 
ATOM   3895 C  CA  . ALA B 1 155 ? -5.661  5.972   17.229  1.00 10.93 ? 202 ALA B CA  1 
ATOM   3896 C  C   . ALA B 1 155 ? -6.413  6.160   15.925  1.00 12.08 ? 202 ALA B C   1 
ATOM   3897 O  O   . ALA B 1 155 ? -7.052  7.197   15.696  1.00 13.57 ? 202 ALA B O   1 
ATOM   3898 C  CB  . ALA B 1 155 ? -4.204  6.243   17.034  1.00 11.89 ? 202 ALA B CB  1 
ATOM   3899 N  N   . ARG B 1 156 ? -6.405  5.167   15.053  1.00 11.93 ? 203 ARG B N   1 
ATOM   3900 C  CA  . ARG B 1 156 ? -7.083  5.259   13.778  1.00 11.89 ? 203 ARG B CA  1 
ATOM   3901 C  C   . ARG B 1 156 ? -8.582  5.316   13.997  1.00 12.97 ? 203 ARG B C   1 
ATOM   3902 O  O   . ARG B 1 156 ? -9.306  6.105   13.357  1.00 14.29 ? 203 ARG B O   1 
ATOM   3903 C  CB  . ARG B 1 156 ? -6.677  4.075   12.908  1.00 12.55 ? 203 ARG B CB  1 
ATOM   3904 C  CG  . ARG B 1 156 ? -7.424  4.035   11.584  1.00 13.63 ? 203 ARG B CG  1 
ATOM   3905 C  CD  . ARG B 1 156 ? -6.786  3.079   10.666  1.00 15.57 ? 203 ARG B CD  1 
ATOM   3906 N  NE  . ARG B 1 156 ? -7.559  3.058   9.415   1.00 17.61 ? 203 ARG B NE  1 
ATOM   3907 C  CZ  . ARG B 1 156 ? -8.308  2.035   9.048   1.00 19.04 ? 203 ARG B CZ  1 
ATOM   3908 N  NH1 . ARG B 1 156 ? -8.455  0.945   9.783   1.00 21.13 ? 203 ARG B NH1 1 
ATOM   3909 N  NH2 . ARG B 1 156 ? -8.888  2.117   7.851   1.00 22.78 ? 203 ARG B NH2 1 
ATOM   3910 N  N   . ILE B 1 157 ? -9.115  4.471   14.849  1.00 12.59 ? 204 ILE B N   1 
ATOM   3911 C  CA  . ILE B 1 157 ? -10.557 4.473   15.112  1.00 12.16 ? 204 ILE B CA  1 
ATOM   3912 C  C   . ILE B 1 157 ? -10.975 5.841   15.634  1.00 14.11 ? 204 ILE B C   1 
ATOM   3913 O  O   . ILE B 1 157 ? -12.075 6.344   15.350  1.00 16.30 ? 204 ILE B O   1 
ATOM   3914 C  CB  . ILE B 1 157 ? -10.928 3.351   16.100  1.00 13.93 ? 204 ILE B CB  1 
ATOM   3915 C  CG1 . ILE B 1 157 ? -10.777 1.991   15.455  1.00 14.62 ? 204 ILE B CG1 1 
ATOM   3916 C  CG2 . ILE B 1 157 ? -12.325 3.562   16.725  1.00 15.57 ? 204 ILE B CG2 1 
ATOM   3917 C  CD1 . ILE B 1 157 ? -10.682 0.856   16.467  1.00 16.86 ? 204 ILE B CD1 1 
ATOM   3918 N  N   . GLY B 1 158 ? -10.123 6.452   16.425  1.00 12.50 ? 205 GLY B N   1 
ATOM   3919 C  CA  . GLY B 1 158 ? -10.428 7.741   17.035  1.00 13.14 ? 205 GLY B CA  1 
ATOM   3920 C  C   . GLY B 1 158 ? -10.131 8.953   16.165  1.00 14.36 ? 205 GLY B C   1 
ATOM   3921 O  O   . GLY B 1 158 ? -10.348 10.062  16.636  1.00 15.18 ? 205 GLY B O   1 
ATOM   3922 N  N   . PHE B 1 159 ? -9.655  8.765   14.952  1.00 15.65 ? 206 PHE B N   1 
ATOM   3923 C  CA  . PHE B 1 159 ? -9.182  9.902   14.170  1.00 19.73 ? 206 PHE B CA  1 
ATOM   3924 C  C   . PHE B 1 159 ? -10.389 10.793  13.894  1.00 17.54 ? 206 PHE B C   1 
ATOM   3925 O  O   . PHE B 1 159 ? -11.501 10.340  13.662  1.00 20.71 ? 206 PHE B O   1 
ATOM   3926 C  CB  . PHE B 1 159 ? -8.426  9.446   12.918  1.00 23.96 ? 206 PHE B CB  1 
ATOM   3927 C  CG  . PHE B 1 159 ? -7.406  10.450  12.374  1.00 27.05 ? 206 PHE B CG  1 
ATOM   3928 C  CD1 . PHE B 1 159 ? -6.524  11.138  13.219  1.00 32.05 ? 206 PHE B CD1 1 
ATOM   3929 C  CD2 . PHE B 1 159 ? -7.386  10.752  11.028  1.00 28.61 ? 206 PHE B CD2 1 
ATOM   3930 C  CE1 . PHE B 1 159 ? -5.628  12.086  12.716  1.00 32.56 ? 206 PHE B CE1 1 
ATOM   3931 C  CE2 . PHE B 1 159 ? -6.467  11.665  10.519  1.00 27.64 ? 206 PHE B CE2 1 
ATOM   3932 C  CZ  . PHE B 1 159 ? -5.616  12.352  11.360  1.00 32.30 ? 206 PHE B CZ  1 
ATOM   3933 N  N   . GLY B 1 160 ? -10.174 12.100  14.155  1.00 17.90 ? 207 GLY B N   1 
ATOM   3934 C  CA  . GLY B 1 160 ? -11.210 13.114  14.058  1.00 18.26 ? 207 GLY B CA  1 
ATOM   3935 C  C   . GLY B 1 160 ? -11.769 13.523  15.413  1.00 20.64 ? 207 GLY B C   1 
ATOM   3936 O  O   . GLY B 1 160 ? -12.289 14.626  15.541  1.00 22.42 ? 207 GLY B O   1 
ATOM   3937 N  N   . LYS B 1 161 ? -11.608 12.673  16.429  1.00 15.36 ? 208 LYS B N   1 
ATOM   3938 C  CA  . LYS B 1 161 ? -12.077 12.889  17.780  1.00 14.76 ? 208 LYS B CA  1 
ATOM   3939 C  C   . LYS B 1 161 ? -10.931 13.004  18.783  1.00 13.74 ? 208 LYS B C   1 
ATOM   3940 O  O   . LYS B 1 161 ? -11.106 13.645  19.819  1.00 14.99 ? 208 LYS B O   1 
ATOM   3941 C  CB  . LYS B 1 161 ? -13.018 11.786  18.247  1.00 15.44 ? 208 LYS B CB  1 
ATOM   3942 C  CG  . LYS B 1 161 ? -14.306 11.673  17.404  1.00 18.67 ? 208 LYS B CG  1 
ATOM   3943 C  CD  . LYS B 1 161 ? -15.293 10.649  17.965  1.00 22.59 ? 208 LYS B CD  1 
ATOM   3944 C  CE  . LYS B 1 161 ? -16.547 10.547  17.141  1.00 23.53 ? 208 LYS B CE  1 
ATOM   3945 N  NZ  . LYS B 1 161 ? -17.463 9.526   17.664  1.00 23.03 ? 208 LYS B NZ  1 
ATOM   3946 N  N   . VAL B 1 162 ? -9.807  12.331  18.526  1.00 12.71 ? 209 VAL B N   1 
ATOM   3947 C  CA  . VAL B 1 162 ? -8.627  12.367  19.380  1.00 12.12 ? 209 VAL B CA  1 
ATOM   3948 C  C   . VAL B 1 162 ? -7.403  12.398  18.497  1.00 12.07 ? 209 VAL B C   1 
ATOM   3949 O  O   . VAL B 1 162 ? -7.428  11.927  17.357  1.00 13.90 ? 209 VAL B O   1 
ATOM   3950 C  CB  . VAL B 1 162 ? -8.485  11.171  20.339  1.00 14.20 ? 209 VAL B CB  1 
ATOM   3951 C  CG1 . VAL B 1 162 ? -9.633  11.149  21.339  1.00 16.07 ? 209 VAL B CG1 1 
ATOM   3952 C  CG2 . VAL B 1 162 ? -8.356  9.841   19.606  1.00 14.81 ? 209 VAL B CG2 1 
ATOM   3953 N  N   . VAL B 1 163 ? -6.327  12.929  19.051  1.00 12.12 ? 210 VAL B N   1 
ATOM   3954 C  CA  . VAL B 1 163 ? -5.025  12.894  18.402  1.00 13.20 ? 210 VAL B CA  1 
ATOM   3955 C  C   . VAL B 1 163 ? -4.049  12.302  19.409  1.00 12.85 ? 210 VAL B C   1 
ATOM   3956 O  O   . VAL B 1 163 ? -4.294  12.370  20.608  1.00 12.36 ? 210 VAL B O   1 
ATOM   3957 C  CB  . VAL B 1 163 ? -4.531  14.272  17.936  1.00 14.38 ? 210 VAL B CB  1 
ATOM   3958 C  CG1 . VAL B 1 163 ? -5.375  14.762  16.759  1.00 17.15 ? 210 VAL B CG1 1 
ATOM   3959 C  CG2 . VAL B 1 163 ? -4.557  15.288  19.059  1.00 15.34 ? 210 VAL B CG2 1 
ATOM   3960 N  N   . VAL B 1 164 ? -2.953  11.757  18.933  1.00 11.91 ? 211 VAL B N   1 
ATOM   3961 C  CA  . VAL B 1 164 ? -1.896  11.271  19.804  1.00 11.86 ? 211 VAL B CA  1 
ATOM   3962 C  C   . VAL B 1 164 ? -1.024  12.437  20.177  1.00 13.16 ? 211 VAL B C   1 
ATOM   3963 O  O   . VAL B 1 164 ? -0.437  13.067  19.315  1.00 15.99 ? 211 VAL B O   1 
ATOM   3964 C  CB  . VAL B 1 164 ? -1.071  10.172  19.126  1.00 14.41 ? 211 VAL B CB  1 
ATOM   3965 C  CG1 . VAL B 1 164 ? -0.082  9.558   20.128  1.00 17.04 ? 211 VAL B CG1 1 
ATOM   3966 C  CG2 . VAL B 1 164 ? -1.926  9.080   18.517  1.00 15.13 ? 211 VAL B CG2 1 
ATOM   3967 N  N   . ARG B 1 165 ? -0.892  12.687  21.467  1.00 11.56 ? 212 ARG B N   1 
ATOM   3968 C  CA  . ARG B 1 165 ? -0.091  13.784  21.953  1.00 11.42 ? 212 ARG B CA  1 
ATOM   3969 C  C   . ARG B 1 165 ? 1.356   13.370  22.126  1.00 11.62 ? 212 ARG B C   1 
ATOM   3970 O  O   . ARG B 1 165 ? 2.294   14.058  21.680  1.00 13.90 ? 212 ARG B O   1 
ATOM   3971 C  CB  . ARG B 1 165 ? -0.637  14.254  23.296  1.00 11.68 ? 212 ARG B CB  1 
ATOM   3972 C  CG  . ARG B 1 165 ? 0.070   15.460  23.894  1.00 13.18 ? 212 ARG B CG  1 
ATOM   3973 C  CD  . ARG B 1 165 ? -0.466  15.801  25.249  1.00 14.48 ? 212 ARG B CD  1 
ATOM   3974 N  NE  . ARG B 1 165 ? 0.219   16.948  25.837  1.00 16.09 ? 212 ARG B NE  1 
ATOM   3975 C  CZ  . ARG B 1 165 ? 0.102   18.193  25.447  1.00 19.65 ? 212 ARG B CZ  1 
ATOM   3976 N  NH1 . ARG B 1 165 ? -0.868  18.578  24.649  1.00 21.02 ? 212 ARG B NH1 1 
ATOM   3977 N  NH2 . ARG B 1 165 ? 0.949   19.097  25.893  1.00 23.03 ? 212 ARG B NH2 1 
ATOM   3978 N  N   . TRP B 1 166 ? 1.599   12.224  22.795  1.00 11.10 ? 213 TRP B N   1 
ATOM   3979 C  CA  . TRP B 1 166 ? 2.937   11.688  22.951  1.00 11.47 ? 213 TRP B CA  1 
ATOM   3980 C  C   . TRP B 1 166 ? 2.850   10.188  23.141  1.00 10.67 ? 213 TRP B C   1 
ATOM   3981 O  O   . TRP B 1 166 ? 1.786   9.674   23.478  1.00 11.95 ? 213 TRP B O   1 
ATOM   3982 C  CB  . TRP B 1 166 ? 3.746   12.386  24.062  1.00 11.49 ? 213 TRP B CB  1 
ATOM   3983 C  CG  . TRP B 1 166 ? 3.132   12.367  25.421  1.00 11.65 ? 213 TRP B CG  1 
ATOM   3984 C  CD1 . TRP B 1 166 ? 2.421   13.341  26.026  1.00 11.44 ? 213 TRP B CD1 1 
ATOM   3985 C  CD2 . TRP B 1 166 ? 3.274   11.333  26.405  1.00 11.66 ? 213 TRP B CD2 1 
ATOM   3986 N  NE1 . TRP B 1 166 ? 2.079   12.986  27.297  1.00 11.40 ? 213 TRP B NE1 1 
ATOM   3987 C  CE2 . TRP B 1 166 ? 2.614   11.752  27.567  1.00 11.83 ? 213 TRP B CE2 1 
ATOM   3988 C  CE3 . TRP B 1 166 ? 3.907   10.097  26.408  1.00 14.18 ? 213 TRP B CE3 1 
ATOM   3989 C  CZ2 . TRP B 1 166 ? 2.556   10.952  28.687  1.00 13.21 ? 213 TRP B CZ2 1 
ATOM   3990 C  CZ3 . TRP B 1 166 ? 3.829   9.300   27.530  1.00 15.52 ? 213 TRP B CZ3 1 
ATOM   3991 C  CH2 . TRP B 1 166 ? 3.204   9.759   28.677  1.00 15.16 ? 213 TRP B CH2 1 
ATOM   3992 N  N   . SER B 1 167 ? 3.941   9.489   22.841  1.00 12.16 ? 214 SER B N   1 
ATOM   3993 C  CA  . SER B 1 167 ? 3.983   8.037   22.802  1.00 13.49 ? 214 SER B CA  1 
ATOM   3994 C  C   . SER B 1 167 ? 5.313   7.590   23.364  1.00 14.63 ? 214 SER B C   1 
ATOM   3995 O  O   . SER B 1 167 ? 6.328   8.237   23.109  1.00 17.33 ? 214 SER B O   1 
ATOM   3996 C  CB  . SER B 1 167 ? 3.886   7.624   21.299  1.00 16.69 ? 214 SER B CB  1 
ATOM   3997 O  OG  . SER B 1 167 ? 4.088   6.248   21.041  1.00 23.96 ? 214 SER B OG  1 
ATOM   3998 N  N   . GLN B 1 168 ? 5.340   6.488   24.093  1.00 11.07 ? 215 GLN B N   1 
ATOM   3999 C  CA  . GLN B 1 168 ? 6.583   5.951   24.630  1.00 11.43 ? 215 GLN B CA  1 
ATOM   4000 C  C   . GLN B 1 168 ? 6.564   4.436   24.527  1.00 10.88 ? 215 GLN B C   1 
ATOM   4001 O  O   . GLN B 1 168 ? 5.652   3.771   25.014  1.00 12.10 ? 215 GLN B O   1 
ATOM   4002 C  CB  . GLN B 1 168 ? 6.705   6.337   26.094  1.00 12.95 ? 215 GLN B CB  1 
ATOM   4003 C  CG  . GLN B 1 168 ? 8.002   5.871   26.749  1.00 14.20 ? 215 GLN B CG  1 
ATOM   4004 C  CD  . GLN B 1 168 ? 9.204   6.587   26.213  1.00 16.37 ? 215 GLN B CD  1 
ATOM   4005 O  OE1 . GLN B 1 168 ? 9.265   7.811   26.308  1.00 17.46 ? 215 GLN B OE1 1 
ATOM   4006 N  NE2 . GLN B 1 168 ? 10.099  5.893   25.545  1.00 15.97 ? 215 GLN B NE2 1 
ATOM   4007 N  N   . LEU B 1 169 ? 7.597   3.866   23.927  1.00 11.54 ? 216 LEU B N   1 
ATOM   4008 C  CA  . LEU B 1 169 ? 7.817   2.418   23.961  1.00 12.21 ? 216 LEU B CA  1 
ATOM   4009 C  C   . LEU B 1 169 ? 8.716   2.083   25.137  1.00 11.71 ? 216 LEU B C   1 
ATOM   4010 O  O   . LEU B 1 169 ? 9.683   2.807   25.424  1.00 13.95 ? 216 LEU B O   1 
ATOM   4011 C  CB  . LEU B 1 169 ? 8.547   2.013   22.679  1.00 16.11 ? 216 LEU B CB  1 
ATOM   4012 C  CG  . LEU B 1 169 ? 8.000   0.875   21.820  1.00 27.88 ? 216 LEU B CG  1 
ATOM   4013 C  CD1 . LEU B 1 169 ? 6.545   1.126   21.543  1.00 29.67 ? 216 LEU B CD1 1 
ATOM   4014 C  CD2 . LEU B 1 169 ? 8.839   0.876   20.528  1.00 25.58 ? 216 LEU B CD2 1 
ATOM   4015 N  N   . GLY B 1 170 ? 8.516   0.971   25.759  1.00 11.83 ? 217 GLY B N   1 
ATOM   4016 C  CA  . GLY B 1 170 ? 9.354   0.492   26.816  1.00 12.11 ? 217 GLY B CA  1 
ATOM   4017 C  C   . GLY B 1 170 ? 9.502   -1.030  26.803  1.00 12.90 ? 217 GLY B C   1 
ATOM   4018 O  O   . GLY B 1 170 ? 8.785   -1.775  26.170  1.00 12.61 ? 217 GLY B O   1 
ATOM   4019 N  N   . PHE B 1 171 ? 10.478  -1.522  27.606  1.00 12.81 ? 218 PHE B N   1 
ATOM   4020 C  CA  . PHE B 1 171 ? 10.764  -2.955  27.774  1.00 13.49 ? 218 PHE B CA  1 
ATOM   4021 C  C   . PHE B 1 171 ? 11.162  -3.268  29.225  1.00 13.20 ? 218 PHE B C   1 
ATOM   4022 O  O   . PHE B 1 171 ? 11.693  -2.409  29.953  1.00 13.39 ? 218 PHE B O   1 
ATOM   4023 C  CB  . PHE B 1 171 ? 11.810  -3.373  26.737  1.00 14.17 ? 218 PHE B CB  1 
ATOM   4024 C  CG  . PHE B 1 171 ? 13.140  -2.657  26.834  1.00 14.51 ? 218 PHE B CG  1 
ATOM   4025 C  CD1 . PHE B 1 171 ? 14.114  -3.113  27.714  1.00 15.26 ? 218 PHE B CD1 1 
ATOM   4026 C  CD2 . PHE B 1 171 ? 13.413  -1.590  25.981  1.00 17.36 ? 218 PHE B CD2 1 
ATOM   4027 C  CE1 . PHE B 1 171 ? 15.352  -2.457  27.772  1.00 17.25 ? 218 PHE B CE1 1 
ATOM   4028 C  CE2 . PHE B 1 171 ? 14.621  -0.913  26.081  1.00 19.07 ? 218 PHE B CE2 1 
ATOM   4029 C  CZ  . PHE B 1 171 ? 15.586  -1.344  26.987  1.00 18.65 ? 218 PHE B CZ  1 
ATOM   4030 N  N   . GLY B 1 172 ? 10.806  -4.471  29.663  1.00 15.93 ? 219 GLY B N   1 
ATOM   4031 C  CA  . GLY B 1 172 ? 11.274  -5.020  30.909  1.00 15.83 ? 219 GLY B CA  1 
ATOM   4032 C  C   . GLY B 1 172 ? 12.125  -6.245  30.587  1.00 17.81 ? 219 GLY B C   1 
ATOM   4033 O  O   . GLY B 1 172 ? 13.172  -6.183  29.940  1.00 20.78 ? 219 GLY B O   1 
ATOM   4034 N  N   . LYS B 1 173 ? 11.671  -7.386  31.075  1.00 17.82 ? 220 LYS B N   1 
ATOM   4035 C  CA  . LYS B 1 173 ? 12.393  -8.627  30.852  1.00 18.66 ? 220 LYS B CA  1 
ATOM   4036 C  C   . LYS B 1 173 ? 11.883  -9.233  29.549  1.00 16.56 ? 220 LYS B C   1 
ATOM   4037 O  O   . LYS B 1 173 ? 10.862  -8.821  29.003  1.00 18.95 ? 220 LYS B O   1 
ATOM   4038 C  CB  . LYS B 1 173 ? 12.279  -9.613  32.011  1.00 24.79 ? 220 LYS B CB  1 
ATOM   4039 C  CG  . LYS B 1 173 ? 10.885  -9.955  32.389  1.00 28.74 ? 220 LYS B CG  1 
ATOM   4040 C  CD  . LYS B 1 173 ? 10.852  -11.143 33.339  1.00 34.25 ? 220 LYS B CD  1 
ATOM   4041 C  CE  . LYS B 1 173 ? 11.490  -10.767 34.625  1.00 37.15 ? 220 LYS B CE  1 
ATOM   4042 N  NZ  . LYS B 1 173 ? 11.200  -11.783 35.637  1.00 35.76 ? 220 LYS B NZ  1 
ATOM   4043 N  N   . THR B 1 174 ? 12.588  -10.217 29.048  1.00 16.56 ? 221 THR B N   1 
ATOM   4044 C  CA  . THR B 1 174 ? 12.155  -11.043 27.942  1.00 16.27 ? 221 THR B CA  1 
ATOM   4045 C  C   . THR B 1 174 ? 11.850  -12.405 28.562  1.00 17.71 ? 221 THR B C   1 
ATOM   4046 O  O   . THR B 1 174 ? 12.752  -13.152 28.962  1.00 18.90 ? 221 THR B O   1 
ATOM   4047 C  CB  . THR B 1 174 ? 13.251  -11.087 26.883  1.00 16.45 ? 221 THR B CB  1 
ATOM   4048 O  OG1 . THR B 1 174 ? 13.434  -9.753  26.406  1.00 17.54 ? 221 THR B OG1 1 
ATOM   4049 C  CG2 . THR B 1 174 ? 12.888  -11.967 25.706  1.00 16.89 ? 221 THR B CG2 1 
ATOM   4050 N  N   . SER B 1 175 ? 10.570  -12.772 28.629  1.00 18.79 ? 222 SER B N   1 
ATOM   4051 C  CA  . SER B 1 175 ? 10.118  -13.914 29.422  1.00 21.28 ? 222 SER B CA  1 
ATOM   4052 C  C   . SER B 1 175 ? 10.501  -15.253 28.797  1.00 24.49 ? 222 SER B C   1 
ATOM   4053 O  O   . SER B 1 175 ? 10.595  -16.243 29.521  1.00 28.29 ? 222 SER B O   1 
ATOM   4054 C  CB  . SER B 1 175 ? 8.647   -13.853 29.628  1.00 22.88 ? 222 SER B CB  1 
ATOM   4055 O  OG  . SER B 1 175 ? 8.404   -12.879 30.609  1.00 24.86 ? 222 SER B OG  1 
ATOM   4056 N  N   . SER B 1 176 ? 10.711  -15.290 27.482  1.00 24.61 ? 223 SER B N   1 
ATOM   4057 C  CA  . SER B 1 176 ? 11.092  -16.527 26.814  1.00 28.81 ? 223 SER B CA  1 
ATOM   4058 C  C   . SER B 1 176 ? 12.399  -17.075 27.388  1.00 31.52 ? 223 SER B C   1 
ATOM   4059 O  O   . SER B 1 176 ? 12.565  -18.292 27.484  1.00 34.46 ? 223 SER B O   1 
ATOM   4060 C  CB  . SER B 1 176 ? 11.183  -16.337 25.327  1.00 29.70 ? 223 SER B CB  1 
ATOM   4061 O  OG  . SER B 1 176 ? 12.112  -15.316 24.985  1.00 33.09 ? 223 SER B OG  1 
ATOM   4062 N  N   . THR B 1 177 ? 13.321  -16.180 27.773  1.00 28.19 ? 224 THR B N   1 
ATOM   4063 C  CA  . THR B 1 177 ? 14.674  -16.584 28.151  1.00 29.24 ? 224 THR B CA  1 
ATOM   4064 C  C   . THR B 1 177 ? 14.983  -16.264 29.614  1.00 29.11 ? 224 THR B C   1 
ATOM   4065 O  O   . THR B 1 177 ? 16.036  -16.652 30.105  1.00 32.88 ? 224 THR B O   1 
ATOM   4066 C  CB  . THR B 1 177 ? 15.680  -15.869 27.249  1.00 31.90 ? 224 THR B CB  1 
ATOM   4067 O  OG1 . THR B 1 177 ? 15.333  -14.492 27.358  1.00 36.12 ? 224 THR B OG1 1 
ATOM   4068 C  CG2 . THR B 1 177 ? 15.597  -16.311 25.802  1.00 37.05 ? 224 THR B CG2 1 
ATOM   4069 N  N   . THR B 1 178 ? 14.111  -15.515 30.303  1.00 24.77 ? 225 THR B N   1 
ATOM   4070 C  CA  . THR B 1 178 ? 14.384  -15.007 31.641  1.00 24.75 ? 225 THR B CA  1 
ATOM   4071 C  C   . THR B 1 178 ? 13.297  -15.553 32.560  1.00 27.09 ? 225 THR B C   1 
ATOM   4072 O  O   . THR B 1 178 ? 12.112  -15.319 32.310  1.00 30.85 ? 225 THR B O   1 
ATOM   4073 C  CB  . THR B 1 178 ? 14.384  -13.471 31.680  1.00 22.92 ? 225 THR B CB  1 
ATOM   4074 O  OG1 . THR B 1 178 ? 15.118  -12.947 30.578  1.00 26.44 ? 225 THR B OG1 1 
ATOM   4075 C  CG2 . THR B 1 178 ? 14.944  -12.867 32.957  1.00 22.44 ? 225 THR B CG2 1 
ATOM   4076 N  N   . PRO B 1 179 ? 13.648  -16.204 33.689  1.00 31.42 ? 226 PRO B N   1 
ATOM   4077 C  CA  . PRO B 1 179 ? 12.633  -16.737 34.604  1.00 31.30 ? 226 PRO B CA  1 
ATOM   4078 C  C   . PRO B 1 179 ? 11.711  -15.674 35.189  1.00 36.98 ? 226 PRO B C   1 
ATOM   4079 O  O   . PRO B 1 179 ? 12.139  -14.563 35.500  1.00 29.66 ? 226 PRO B O   1 
ATOM   4080 C  CB  . PRO B 1 179 ? 13.427  -17.454 35.718  1.00 34.40 ? 226 PRO B CB  1 
ATOM   4081 C  CG  . PRO B 1 179 ? 14.844  -17.523 35.205  1.00 32.15 ? 226 PRO B CG  1 
ATOM   4082 C  CD  . PRO B 1 179 ? 15.021  -16.409 34.175  1.00 32.25 ? 226 PRO B CD  1 
ATOM   4083 N  N   . ASP B 1 180 ? 10.453  -16.062 35.423  1.00 36.85 ? 227 ASP B N   1 
ATOM   4084 C  CA  . ASP B 1 180 ? 9.433   -15.107 35.830  1.00 42.85 ? 227 ASP B CA  1 
ATOM   4085 C  C   . ASP B 1 180 ? 9.788   -14.496 37.187  1.00 42.27 ? 227 ASP B C   1 
ATOM   4086 O  O   . ASP B 1 180 ? 9.466   -13.337 37.449  1.00 44.03 ? 227 ASP B O   1 
ATOM   4087 C  CB  . ASP B 1 180 ? 8.049   -15.741 35.813  1.00 49.79 ? 227 ASP B CB  1 
ATOM   4088 C  CG  . ASP B 1 180 ? 6.900   -14.746 35.870  1.00 56.16 ? 227 ASP B CG  1 
ATOM   4089 O  OD1 . ASP B 1 180 ? 6.638   -14.214 36.968  1.00 57.43 ? 227 ASP B OD1 1 
ATOM   4090 O  OD2 . ASP B 1 180 ? 6.306   -14.481 34.804  1.00 66.41 ? 227 ASP B OD2 1 
ATOM   4091 N  N   . LYS B 1 181 ? 10.467  -15.266 38.041  1.00 36.93 ? 228 LYS B N   1 
ATOM   4092 C  CA  . LYS B 1 181 ? 10.669  -14.825 39.411  1.00 41.19 ? 228 LYS B CA  1 
ATOM   4093 C  C   . LYS B 1 181 ? 11.778  -13.773 39.482  1.00 37.97 ? 228 LYS B C   1 
ATOM   4094 O  O   . LYS B 1 181 ? 11.675  -12.884 40.326  1.00 44.50 ? 228 LYS B O   1 
ATOM   4095 C  CB  . LYS B 1 181 ? 10.904  -15.986 40.390  1.00 47.78 ? 228 LYS B CB  1 
ATOM   4096 C  CG  . LYS B 1 181 ? 9.635   -16.429 41.126  1.00 50.57 ? 228 LYS B CG  1 
ATOM   4097 C  CD  . LYS B 1 181 ? 9.002   -15.325 41.974  1.00 57.33 ? 228 LYS B CD  1 
ATOM   4098 C  CE  . LYS B 1 181 ? 7.834   -15.768 42.798  1.00 57.52 ? 228 LYS B CE  1 
ATOM   4099 N  NZ  . LYS B 1 181 ? 6.678   -16.109 41.963  1.00 57.83 ? 228 LYS B NZ  1 
ATOM   4100 N  N   . GLN B 1 182 ? 12.782  -13.878 38.586  1.00 29.81 ? 229 GLN B N   1 
ATOM   4101 C  CA  . GLN B 1 182 ? 13.984  -13.052 38.590  1.00 27.46 ? 229 GLN B CA  1 
ATOM   4102 C  C   . GLN B 1 182 ? 13.618  -11.572 38.466  1.00 23.44 ? 229 GLN B C   1 
ATOM   4103 O  O   . GLN B 1 182 ? 12.829  -11.173 37.612  1.00 23.30 ? 229 GLN B O   1 
ATOM   4104 C  CB  . GLN B 1 182 ? 14.856  -13.496 37.410  1.00 28.04 ? 229 GLN B CB  1 
ATOM   4105 C  CG  . GLN B 1 182 ? 16.262  -12.899 37.388  1.00 28.73 ? 229 GLN B CG  1 
ATOM   4106 C  CD  . GLN B 1 182 ? 17.134  -13.579 36.350  1.00 32.04 ? 229 GLN B CD  1 
ATOM   4107 O  OE1 . GLN B 1 182 ? 17.282  -14.806 36.352  1.00 36.84 ? 229 GLN B OE1 1 
ATOM   4108 N  NE2 . GLN B 1 182 ? 17.688  -12.813 35.422  1.00 28.29 ? 229 GLN B NE2 1 
ATOM   4109 N  N   . THR B 1 183 ? 14.156  -10.759 39.388  1.00 21.81 ? 230 THR B N   1 
ATOM   4110 C  CA  . THR B 1 183 ? 13.891  -9.337  39.366  1.00 19.91 ? 230 THR B CA  1 
ATOM   4111 C  C   . THR B 1 183 ? 14.591  -8.763  38.132  1.00 16.53 ? 230 THR B C   1 
ATOM   4112 O  O   . THR B 1 183 ? 15.774  -9.050  37.939  1.00 19.66 ? 230 THR B O   1 
ATOM   4113 C  CB  . THR B 1 183 ? 14.418  -8.684  40.640  1.00 19.41 ? 230 THR B CB  1 
ATOM   4114 O  OG1 . THR B 1 183 ? 13.830  -9.450  41.700  1.00 21.96 ? 230 THR B OG1 1 
ATOM   4115 C  CG2 . THR B 1 183 ? 13.967  -7.241  40.737  1.00 19.94 ? 230 THR B CG2 1 
ATOM   4116 N  N   . PRO B 1 184 ? 13.912  -7.955  37.315  1.00 17.66 ? 231 PRO B N   1 
ATOM   4117 C  CA  . PRO B 1 184 ? 14.562  -7.277  36.188  1.00 16.98 ? 231 PRO B CA  1 
ATOM   4118 C  C   . PRO B 1 184 ? 15.596  -6.279  36.716  1.00 17.36 ? 231 PRO B C   1 
ATOM   4119 O  O   . PRO B 1 184 ? 15.483  -5.762  37.814  1.00 18.07 ? 231 PRO B O   1 
ATOM   4120 C  CB  . PRO B 1 184 ? 13.452  -6.580  35.403  1.00 22.02 ? 231 PRO B CB  1 
ATOM   4121 C  CG  . PRO B 1 184 ? 12.277  -6.510  36.365  1.00 24.88 ? 231 PRO B CG  1 
ATOM   4122 C  CD  . PRO B 1 184 ? 12.498  -7.595  37.400  1.00 19.99 ? 231 PRO B CD  1 
ATOM   4123 N  N   . ARG B 1 185 ? 16.623  -5.987  35.920  1.00 15.94 ? 232 ARG B N   1 
ATOM   4124 C  CA  . ARG B 1 185 ? 17.523  -4.886  36.222  1.00 14.77 ? 232 ARG B CA  1 
ATOM   4125 C  C   . ARG B 1 185 ? 17.116  -3.707  35.353  1.00 14.39 ? 232 ARG B C   1 
ATOM   4126 O  O   . ARG B 1 185 ? 16.741  -3.817  34.187  1.00 14.23 ? 232 ARG B O   1 
ATOM   4127 C  CB  . ARG B 1 185 ? 18.980  -5.261  35.947  1.00 15.23 ? 232 ARG B CB  1 
ATOM   4128 C  CG  . ARG B 1 185 ? 19.498  -6.310  36.905  1.00 17.23 ? 232 ARG B CG  1 
ATOM   4129 C  CD  . ARG B 1 185 ? 20.928  -6.700  36.667  1.00 17.65 ? 232 ARG B CD  1 
ATOM   4130 N  NE  . ARG B 1 185 ? 21.284  -7.773  37.601  1.00 17.81 ? 232 ARG B NE  1 
ATOM   4131 C  CZ  . ARG B 1 185 ? 21.964  -7.642  38.694  1.00 17.67 ? 232 ARG B CZ  1 
ATOM   4132 N  NH1 . ARG B 1 185 ? 22.343  -6.470  39.136  1.00 18.81 ? 232 ARG B NH1 1 
ATOM   4133 N  NH2 . ARG B 1 185 ? 22.243  -8.694  39.426  1.00 21.01 ? 232 ARG B NH2 1 
ATOM   4134 N  N   . ASN B 1 186 ? 17.268  -2.523  35.906  1.00 13.14 ? 233 ASN B N   1 
ATOM   4135 C  CA  . ASN B 1 186 ? 17.124  -1.306  35.149  1.00 13.05 ? 233 ASN B CA  1 
ATOM   4136 C  C   . ASN B 1 186 ? 18.434  -1.002  34.428  1.00 12.51 ? 233 ASN B C   1 
ATOM   4137 O  O   . ASN B 1 186 ? 19.401  -1.761  34.538  1.00 13.02 ? 233 ASN B O   1 
ATOM   4138 C  CB  . ASN B 1 186 ? 16.680  -0.165  36.055  1.00 13.87 ? 233 ASN B CB  1 
ATOM   4139 C  CG  . ASN B 1 186 ? 17.663  0.131   37.147  1.00 16.13 ? 233 ASN B CG  1 
ATOM   4140 O  OD1 . ASN B 1 186 ? 18.869  0.091   36.969  1.00 14.49 ? 233 ASN B OD1 1 
ATOM   4141 N  ND2 . ASN B 1 186 ? 17.152  0.415   38.332  1.00 16.78 ? 233 ASN B ND2 1 
ATOM   4142 N  N   . LEU B 1 187 ? 18.478  0.089   33.688  1.00 12.25 ? 234 LEU B N   1 
ATOM   4143 C  CA  . LEU B 1 187 ? 19.613  0.391   32.841  1.00 12.02 ? 234 LEU B CA  1 
ATOM   4144 C  C   . LEU B 1 187 ? 20.780  0.952   33.636  1.00 13.08 ? 234 LEU B C   1 
ATOM   4145 O  O   . LEU B 1 187 ? 21.837  1.178   33.063  1.00 14.63 ? 234 LEU B O   1 
ATOM   4146 C  CB  . LEU B 1 187 ? 19.234  1.283   31.674  1.00 13.31 ? 234 LEU B CB  1 
ATOM   4147 C  CG  . LEU B 1 187 ? 18.270  0.627   30.678  1.00 15.05 ? 234 LEU B CG  1 
ATOM   4148 C  CD1 . LEU B 1 187 ? 17.844  1.636   29.648  1.00 17.59 ? 234 LEU B CD1 1 
ATOM   4149 C  CD2 . LEU B 1 187 ? 18.871  -0.640  30.054  1.00 19.48 ? 234 LEU B CD2 1 
ATOM   4150 N  N   . LEU B 1 188 ? 20.637  1.152   34.927  1.00 12.20 ? 235 LEU B N   1 
ATOM   4151 C  CA  . LEU B 1 188 ? 21.810  1.444   35.740  1.00 11.94 ? 235 LEU B CA  1 
ATOM   4152 C  C   . LEU B 1 188 ? 22.434  0.160   36.218  1.00 12.92 ? 235 LEU B C   1 
ATOM   4153 O  O   . LEU B 1 188 ? 23.462  0.194   36.899  1.00 15.15 ? 235 LEU B O   1 
ATOM   4154 C  CB  . LEU B 1 188 ? 21.384  2.316   36.902  1.00 13.15 ? 235 LEU B CB  1 
ATOM   4155 C  CG  . LEU B 1 188 ? 20.822  3.684   36.533  1.00 14.12 ? 235 LEU B CG  1 
ATOM   4156 C  CD1 . LEU B 1 188 ? 20.513  4.462   37.789  1.00 17.30 ? 235 LEU B CD1 1 
ATOM   4157 C  CD2 . LEU B 1 188 ? 21.717  4.513   35.634  1.00 16.24 ? 235 LEU B CD2 1 
ATOM   4158 N  N   . GLY B 1 189 ? 21.841  -0.993  35.923  1.00 11.99 ? 236 GLY B N   1 
ATOM   4159 C  CA  . GLY B 1 189 ? 22.431  -2.287  36.243  1.00 12.33 ? 236 GLY B CA  1 
ATOM   4160 C  C   . GLY B 1 189 ? 22.015  -2.818  37.595  1.00 14.33 ? 236 GLY B C   1 
ATOM   4161 O  O   . GLY B 1 189 ? 22.561  -3.807  38.041  1.00 15.04 ? 236 GLY B O   1 
ATOM   4162 N  N   . PHE B 1 190 ? 21.070  -2.155  38.250  1.00 12.48 ? 237 PHE B N   1 
ATOM   4163 C  CA  . PHE B 1 190 ? 20.554  -2.573  39.553  1.00 12.35 ? 237 PHE B CA  1 
ATOM   4164 C  C   . PHE B 1 190 ? 19.234  -3.302  39.374  1.00 13.29 ? 237 PHE B C   1 
ATOM   4165 O  O   . PHE B 1 190 ? 18.396  -2.901  38.586  1.00 14.44 ? 237 PHE B O   1 
ATOM   4166 C  CB  . PHE B 1 190 ? 20.406  -1.427  40.534  1.00 12.68 ? 237 PHE B CB  1 
ATOM   4167 C  CG  . PHE B 1 190 ? 21.727  -1.046  41.150  1.00 12.52 ? 237 PHE B CG  1 
ATOM   4168 C  CD1 . PHE B 1 190 ? 22.720  -0.382  40.453  1.00 14.03 ? 237 PHE B CD1 1 
ATOM   4169 C  CD2 . PHE B 1 190 ? 21.963  -1.360  42.482  1.00 14.54 ? 237 PHE B CD2 1 
ATOM   4170 C  CE1 . PHE B 1 190 ? 23.932  -0.071  41.060  1.00 14.26 ? 237 PHE B CE1 1 
ATOM   4171 C  CE2 . PHE B 1 190 ? 23.162  -1.022  43.080  1.00 15.05 ? 237 PHE B CE2 1 
ATOM   4172 C  CZ  . PHE B 1 190 ? 24.149  -0.389  42.374  1.00 16.06 ? 237 PHE B CZ  1 
ATOM   4173 N  N   . LYS B 1 191 ? 19.025  -4.333  40.191  1.00 14.19 ? 238 LYS B N   1 
ATOM   4174 C  CA  . LYS B 1 191 ? 17.724  -4.967  40.285  1.00 14.59 ? 238 LYS B CA  1 
ATOM   4175 C  C   . LYS B 1 191 ? 16.699  -3.917  40.674  1.00 14.96 ? 238 LYS B C   1 
ATOM   4176 O  O   . LYS B 1 191 ? 16.937  -3.100  41.562  1.00 15.21 ? 238 LYS B O   1 
ATOM   4177 C  CB  . LYS B 1 191 ? 17.729  -6.099  41.321  1.00 15.73 ? 238 LYS B CB  1 
ATOM   4178 C  CG  . LYS B 1 191 ? 18.650  -7.240  40.929  1.00 18.23 ? 238 LYS B CG  1 
ATOM   4179 C  CD  . LYS B 1 191 ? 18.581  -8.338  41.987  1.00 17.57 ? 238 LYS B CD  1 
ATOM   4180 C  CE  . LYS B 1 191 ? 19.445  -9.510  41.639  1.00 21.18 ? 238 LYS B CE  1 
ATOM   4181 N  NZ  . LYS B 1 191 ? 19.392  -10.525 42.703  1.00 21.58 ? 238 LYS B NZ  1 
ATOM   4182 N  N   . ASP B 1 192 ? 15.503  -3.992  40.086  1.00 15.01 ? 239 ASP B N   1 
ATOM   4183 C  CA  . ASP B 1 192 ? 14.501  -2.957  40.198  1.00 14.76 ? 239 ASP B CA  1 
ATOM   4184 C  C   . ASP B 1 192 ? 13.169  -3.655  40.333  1.00 16.03 ? 239 ASP B C   1 
ATOM   4185 O  O   . ASP B 1 192 ? 12.708  -4.334  39.401  1.00 17.32 ? 239 ASP B O   1 
ATOM   4186 C  CB  . ASP B 1 192 ? 14.592  -1.935  39.070  1.00 15.84 ? 239 ASP B CB  1 
ATOM   4187 C  CG  . ASP B 1 192 ? 13.884  -0.622  39.306  1.00 18.22 ? 239 ASP B CG  1 
ATOM   4188 O  OD1 . ASP B 1 192 ? 12.934  -0.596  40.106  1.00 21.50 ? 239 ASP B OD1 1 
ATOM   4189 O  OD2 . ASP B 1 192 ? 14.380  0.373   38.820  1.00 18.54 ? 239 ASP B OD2 1 
ATOM   4190 N  N   . GLY B 1 193 ? 12.591  -3.560  41.526  1.00 14.73 ? 240 GLY B N   1 
ATOM   4191 C  CA  . GLY B 1 193 ? 11.267  -4.117  41.789  1.00 14.56 ? 240 GLY B CA  1 
ATOM   4192 C  C   . GLY B 1 193 ? 11.206  -5.016  43.023  1.00 14.61 ? 240 GLY B C   1 
ATOM   4193 O  O   . GLY B 1 193 ? 10.128  -5.560  43.314  1.00 18.17 ? 240 GLY B O   1 
ATOM   4194 N  N   . THR B 1 194 ? 12.323  -5.179  43.732  1.00 14.20 ? 241 THR B N   1 
ATOM   4195 C  CA  . THR B 1 194 ? 12.403  -6.099  44.845  1.00 14.20 ? 241 THR B CA  1 
ATOM   4196 C  C   . THR B 1 194 ? 11.291  -5.840  45.861  1.00 15.20 ? 241 THR B C   1 
ATOM   4197 O  O   . THR B 1 194 ? 10.595  -6.772  46.294  1.00 18.38 ? 241 THR B O   1 
ATOM   4198 C  CB  . THR B 1 194 ? 13.791  -6.000  45.475  1.00 16.14 ? 241 THR B CB  1 
ATOM   4199 O  OG1 . THR B 1 194 ? 14.751  -6.274  44.454  1.00 15.26 ? 241 THR B OG1 1 
ATOM   4200 C  CG2 . THR B 1 194 ? 13.903  -6.974  46.627  1.00 16.79 ? 241 THR B CG2 1 
ATOM   4201 N  N   . ARG B 1 195 ? 11.155  -4.612  46.337  1.00 13.20 ? 242 ARG B N   1 
ATOM   4202 C  CA  . ARG B 1 195 ? 10.179  -4.266  47.358  1.00 13.31 ? 242 ARG B CA  1 
ATOM   4203 C  C   . ARG B 1 195 ? 9.105   -3.425  46.707  1.00 14.12 ? 242 ARG B C   1 
ATOM   4204 O  O   . ARG B 1 195 ? 9.184   -2.187  46.616  1.00 15.53 ? 242 ARG B O   1 
ATOM   4205 C  CB  . ARG B 1 195 ? 10.813  -3.543  48.548  1.00 14.26 ? 242 ARG B CB  1 
ATOM   4206 C  CG  . ARG B 1 195 ? 11.440  -4.520  49.531  1.00 15.51 ? 242 ARG B CG  1 
ATOM   4207 C  CD  . ARG B 1 195 ? 12.065  -3.882  50.731  1.00 15.65 ? 242 ARG B CD  1 
ATOM   4208 N  NE  . ARG B 1 195 ? 11.258  -2.787  51.258  1.00 15.17 ? 242 ARG B NE  1 
ATOM   4209 C  CZ  . ARG B 1 195 ? 10.130  -2.888  51.878  1.00 17.12 ? 242 ARG B CZ  1 
ATOM   4210 N  NH1 . ARG B 1 195 ? 9.318   -1.855  51.899  1.00 18.13 ? 242 ARG B NH1 1 
ATOM   4211 N  NH2 . ARG B 1 195 ? 9.695   -4.037  52.361  1.00 20.26 ? 242 ARG B NH2 1 
ATOM   4212 N  N   . ASN B 1 196 ? 8.073   -4.097  46.250  1.00 13.94 ? 243 ASN B N   1 
ATOM   4213 C  CA  . ASN B 1 196 ? 6.993   -3.472  45.524  1.00 14.50 ? 243 ASN B CA  1 
ATOM   4214 C  C   . ASN B 1 196 ? 5.725   -4.158  46.006  1.00 16.73 ? 243 ASN B C   1 
ATOM   4215 O  O   . ASN B 1 196 ? 5.798   -5.260  46.555  1.00 21.04 ? 243 ASN B O   1 
ATOM   4216 C  CB  . ASN B 1 196 ? 7.189   -3.723  44.044  1.00 14.53 ? 243 ASN B CB  1 
ATOM   4217 C  CG  . ASN B 1 196 ? 6.400   -2.838  43.136  1.00 13.29 ? 243 ASN B CG  1 
ATOM   4218 O  OD1 . ASN B 1 196 ? 5.796   -1.833  43.512  1.00 13.53 ? 243 ASN B OD1 1 
ATOM   4219 N  ND2 . ASN B 1 196 ? 6.481   -3.187  41.886  1.00 17.51 ? 243 ASN B ND2 1 
ATOM   4220 N  N   . ILE B 1 197 ? 4.583   -3.609  45.687  1.00 14.78 ? 244 ILE B N   1 
ATOM   4221 C  CA  . ILE B 1 197 ? 3.325   -4.321  45.832  1.00 15.11 ? 244 ILE B CA  1 
ATOM   4222 C  C   . ILE B 1 197 ? 3.191   -5.340  44.715  1.00 16.69 ? 244 ILE B C   1 
ATOM   4223 O  O   . ILE B 1 197 ? 3.338   -4.997  43.536  1.00 18.94 ? 244 ILE B O   1 
ATOM   4224 C  CB  . ILE B 1 197 ? 2.142   -3.344  45.869  1.00 15.36 ? 244 ILE B CB  1 
ATOM   4225 C  CG1 . ILE B 1 197 ? 2.315   -2.362  46.994  1.00 14.89 ? 244 ILE B CG1 1 
ATOM   4226 C  CG2 . ILE B 1 197 ? 0.810   -4.086  45.980  1.00 18.14 ? 244 ILE B CG2 1 
ATOM   4227 C  CD1 . ILE B 1 197 ? 1.291   -1.250  46.986  1.00 16.47 ? 244 ILE B CD1 1 
ATOM   4228 N  N   . ALA B 1 198 ? 2.926   -6.592  45.058  1.00 17.47 ? 245 ALA B N   1 
ATOM   4229 C  CA  . ALA B 1 198 ? 2.722   -7.635  44.068  1.00 18.88 ? 245 ALA B CA  1 
ATOM   4230 C  C   . ALA B 1 198 ? 1.226   -7.795  43.833  1.00 17.43 ? 245 ALA B C   1 
ATOM   4231 O  O   . ALA B 1 198 ? 0.393   -7.521  44.687  1.00 17.61 ? 245 ALA B O   1 
ATOM   4232 C  CB  . ALA B 1 198 ? 3.358   -8.914  44.543  1.00 20.14 ? 245 ALA B CB  1 
ATOM   4233 N  N   . GLY B 1 199 ? 0.882   -8.258  42.623  1.00 19.93 ? 246 GLY B N   1 
ATOM   4234 C  CA  . GLY B 1 199 ? -0.500  -8.466  42.240  1.00 20.23 ? 246 GLY B CA  1 
ATOM   4235 C  C   . GLY B 1 199 ? -1.210  -9.559  43.041  1.00 19.69 ? 246 GLY B C   1 
ATOM   4236 O  O   . GLY B 1 199 ? -2.440  -9.617  43.100  1.00 21.71 ? 246 GLY B O   1 
ATOM   4237 N  N   . THR B 1 200 ? -0.428  -10.359 43.754  1.00 18.14 ? 247 THR B N   1 
ATOM   4238 C  CA  . THR B 1 200 ? -0.960  -11.385 44.628  1.00 18.73 ? 247 THR B CA  1 
ATOM   4239 C  C   . THR B 1 200 ? -1.482  -10.834 45.962  1.00 19.41 ? 247 THR B C   1 
ATOM   4240 O  O   . THR B 1 200 ? -2.200  -11.467 46.717  1.00 19.80 ? 247 THR B O   1 
ATOM   4241 C  CB  . THR B 1 200 ? 0.112   -12.443 44.866  1.00 23.18 ? 247 THR B CB  1 
ATOM   4242 O  OG1 . THR B 1 200 ? 1.258   -11.803 45.422  1.00 24.90 ? 247 THR B OG1 1 
ATOM   4243 C  CG2 . THR B 1 200 ? 0.555   -13.079 43.566  1.00 23.46 ? 247 THR B CG2 1 
ATOM   4244 N  N   . GLU B 1 201 ? -1.067  -9.615  46.345  1.00 17.33 ? 248 GLU B N   1 
ATOM   4245 C  CA  . GLU B 1 201 ? -1.297  -9.046  47.659  1.00 15.32 ? 248 GLU B CA  1 
ATOM   4246 C  C   . GLU B 1 201 ? -2.590  -8.269  47.684  1.00 15.93 ? 248 GLU B C   1 
ATOM   4247 O  O   . GLU B 1 201 ? -2.631  -7.036  47.632  1.00 15.47 ? 248 GLU B O   1 
ATOM   4248 C  CB  . GLU B 1 201 ? -0.104  -8.160  48.017  1.00 17.41 ? 248 GLU B CB  1 
ATOM   4249 C  CG  . GLU B 1 201 ? 1.190   -8.941  48.137  1.00 17.39 ? 248 GLU B CG  1 
ATOM   4250 C  CD  . GLU B 1 201 ? 2.311   -8.038  48.581  1.00 19.17 ? 248 GLU B CD  1 
ATOM   4251 O  OE1 . GLU B 1 201 ? 2.710   -7.133  47.865  1.00 19.33 ? 248 GLU B OE1 1 
ATOM   4252 O  OE2 . GLU B 1 201 ? 2.714   -8.195  49.745  1.00 28.41 ? 248 GLU B OE2 1 
ATOM   4253 N  N   . LYS B 1 202 ? -3.680  -9.021  47.708  1.00 16.57 ? 249 LYS B N   1 
ATOM   4254 C  CA  . LYS B 1 202 ? -4.982  -8.429  47.553  1.00 17.09 ? 249 LYS B CA  1 
ATOM   4255 C  C   . LYS B 1 202 ? -5.246  -7.366  48.599  1.00 16.91 ? 249 LYS B C   1 
ATOM   4256 O  O   . LYS B 1 202 ? -5.758  -6.317  48.267  1.00 16.02 ? 249 LYS B O   1 
ATOM   4257 C  CB  . LYS B 1 202 ? -6.043  -9.521  47.603  1.00 21.97 ? 249 LYS B CB  1 
ATOM   4258 C  CG  . LYS B 1 202 ? -6.153  -10.291 46.286  1.00 31.82 ? 249 LYS B CG  1 
ATOM   4259 C  CD  . LYS B 1 202 ? -7.598  -10.642 45.933  1.00 39.20 ? 249 LYS B CD  1 
ATOM   4260 C  CE  . LYS B 1 202 ? -7.828  -10.760 44.453  1.00 42.41 ? 249 LYS B CE  1 
ATOM   4261 N  NZ  . LYS B 1 202 ? -9.237  -11.054 44.162  1.00 42.73 ? 249 LYS B NZ  1 
ATOM   4262 N  N   . ASP B 1 203 ? -4.878  -7.586  49.861  1.00 17.76 ? 250 ASP B N   1 
ATOM   4263 C  CA  . ASP B 1 203 ? -5.190  -6.579  50.861  1.00 17.69 ? 250 ASP B CA  1 
ATOM   4264 C  C   . ASP B 1 203 ? -4.311  -5.333  50.668  1.00 15.70 ? 250 ASP B C   1 
ATOM   4265 O  O   . ASP B 1 203 ? -4.827  -4.227  50.832  1.00 17.04 ? 250 ASP B O   1 
ATOM   4266 C  CB  . ASP B 1 203 ? -5.007  -7.140  52.262  1.00 21.11 ? 250 ASP B CB  1 
ATOM   4267 C  CG  . ASP B 1 203 ? -5.507  -6.210  53.356  1.00 28.69 ? 250 ASP B CG  1 
ATOM   4268 O  OD1 . ASP B 1 203 ? -6.722  -5.855  53.327  1.00 35.47 ? 250 ASP B OD1 1 
ATOM   4269 O  OD2 . ASP B 1 203 ? -4.685  -5.790  54.197  1.00 35.49 ? 250 ASP B OD2 1 
ATOM   4270 N  N   . ARG B 1 204 ? -3.043  -5.481  50.311  1.00 15.39 ? 251 ARG B N   1 
ATOM   4271 C  CA  . ARG B 1 204 ? -2.225  -4.307  50.066  1.00 15.21 ? 251 ARG B CA  1 
ATOM   4272 C  C   . ARG B 1 204 ? -2.763  -3.546  48.858  1.00 14.60 ? 251 ARG B C   1 
ATOM   4273 O  O   . ARG B 1 204 ? -2.679  -2.330  48.834  1.00 14.26 ? 251 ARG B O   1 
ATOM   4274 C  CB  . ARG B 1 204 ? -0.766  -4.687  49.858  1.00 17.30 ? 251 ARG B CB  1 
ATOM   4275 C  CG  . ARG B 1 204 ? -0.119  -5.181  51.146  1.00 20.48 ? 251 ARG B CG  1 
ATOM   4276 C  CD  . ARG B 1 204 ? 1.291   -5.689  50.854  1.00 26.72 ? 251 ARG B CD  1 
ATOM   4277 N  NE  . ARG B 1 204 ? 2.146   -4.521  50.771  1.00 25.08 ? 251 ARG B NE  1 
ATOM   4278 C  CZ  . ARG B 1 204 ? 3.381   -4.315  50.346  1.00 21.49 ? 251 ARG B CZ  1 
ATOM   4279 N  NH1 . ARG B 1 204 ? 3.994   -5.007  49.420  1.00 19.62 ? 251 ARG B NH1 1 
ATOM   4280 N  NH2 . ARG B 1 204 ? 3.983   -3.242  50.834  1.00 25.48 ? 251 ARG B NH2 1 
ATOM   4281 N  N   . LEU B 1 205 ? -3.315  -4.217  47.850  1.00 13.57 ? 252 LEU B N   1 
ATOM   4282 C  CA  . LEU B 1 205 ? -3.923  -3.509  46.739  1.00 13.60 ? 252 LEU B CA  1 
ATOM   4283 C  C   . LEU B 1 205 ? -5.111  -2.699  47.207  1.00 13.49 ? 252 LEU B C   1 
ATOM   4284 O  O   . LEU B 1 205 ? -5.300  -1.545  46.812  1.00 13.51 ? 252 LEU B O   1 
ATOM   4285 C  CB  . LEU B 1 205 ? -4.328  -4.496  45.657  1.00 13.82 ? 252 LEU B CB  1 
ATOM   4286 C  CG  . LEU B 1 205 ? -3.184  -5.171  44.915  1.00 15.48 ? 252 LEU B CG  1 
ATOM   4287 C  CD1 . LEU B 1 205 ? -3.713  -6.329  44.076  1.00 18.75 ? 252 LEU B CD1 1 
ATOM   4288 C  CD2 . LEU B 1 205 ? -2.457  -4.200  44.000  1.00 16.93 ? 252 LEU B CD2 1 
ATOM   4289 N  N   . ASP B 1 206 ? -5.975  -3.285  48.035  1.00 13.74 ? 253 ASP B N   1 
ATOM   4290 C  CA  . ASP B 1 206 ? -7.091  -2.536  48.566  1.00 15.50 ? 253 ASP B CA  1 
ATOM   4291 C  C   . ASP B 1 206 ? -6.662  -1.328  49.390  1.00 15.20 ? 253 ASP B C   1 
ATOM   4292 O  O   . ASP B 1 206 ? -7.309  -0.268  49.346  1.00 19.43 ? 253 ASP B O   1 
ATOM   4293 C  CB  . ASP B 1 206 ? -7.961  -3.451  49.402  1.00 18.05 ? 253 ASP B CB  1 
ATOM   4294 C  CG  . ASP B 1 206 ? -8.856  -4.384  48.602  1.00 22.64 ? 253 ASP B CG  1 
ATOM   4295 O  OD1 . ASP B 1 206 ? -9.008  -4.183  47.396  1.00 23.72 ? 253 ASP B OD1 1 
ATOM   4296 O  OD2 . ASP B 1 206 ? -9.373  -5.330  49.207  1.00 25.35 ? 253 ASP B OD2 1 
ATOM   4297 N  N   . ARG B 1 207 ? -5.557  -1.482  50.133  1.00 14.35 ? 254 ARG B N   1 
ATOM   4298 C  CA  . ARG B 1 207 ? -5.140  -0.404  51.002  1.00 15.96 ? 254 ARG B CA  1 
ATOM   4299 C  C   . ARG B 1 207 ? -4.499  0.739   50.225  1.00 15.53 ? 254 ARG B C   1 
ATOM   4300 O  O   . ARG B 1 207 ? -4.705  1.926   50.546  1.00 16.36 ? 254 ARG B O   1 
ATOM   4301 C  CB  . ARG B 1 207 ? -4.160  -0.963  52.028  1.00 18.19 ? 254 ARG B CB  1 
ATOM   4302 C  CG  . ARG B 1 207 ? -3.734  0.054   53.074  1.00 25.83 ? 254 ARG B CG  1 
ATOM   4303 C  CD  . ARG B 1 207 ? -3.006  -0.587  54.249  1.00 32.97 ? 254 ARG B CD  1 
ATOM   4304 N  NE  . ARG B 1 207 ? -3.923  -1.304  55.148  1.00 41.59 ? 254 ARG B NE  1 
ATOM   4305 C  CZ  . ARG B 1 207 ? -3.899  -2.615  55.360  1.00 46.87 ? 254 ARG B CZ  1 
ATOM   4306 N  NH1 . ARG B 1 207 ? -4.701  -3.158  56.265  1.00 46.21 ? 254 ARG B NH1 1 
ATOM   4307 N  NH2 . ARG B 1 207 ? -3.053  -3.374  54.684  1.00 50.35 ? 254 ARG B NH2 1 
ATOM   4308 N  N   . PHE B 1 208 ? -3.654  0.402   49.238  1.00 13.72 ? 255 PHE B N   1 
ATOM   4309 C  CA  . PHE B 1 208 ? -2.719  1.344   48.640  1.00 13.25 ? 255 PHE B CA  1 
ATOM   4310 C  C   . PHE B 1 208 ? -2.955  1.630   47.168  1.00 12.48 ? 255 PHE B C   1 
ATOM   4311 O  O   . PHE B 1 208 ? -2.416  2.647   46.684  1.00 13.72 ? 255 PHE B O   1 
ATOM   4312 C  CB  . PHE B 1 208 ? -1.288  0.842   48.745  1.00 12.93 ? 255 PHE B CB  1 
ATOM   4313 C  CG  . PHE B 1 208 ? -0.823  0.747   50.180  1.00 13.56 ? 255 PHE B CG  1 
ATOM   4314 C  CD1 . PHE B 1 208 ? -0.676  1.892   50.920  1.00 15.01 ? 255 PHE B CD1 1 
ATOM   4315 C  CD2 . PHE B 1 208 ? -0.425  -0.465  50.710  1.00 15.59 ? 255 PHE B CD2 1 
ATOM   4316 C  CE1 . PHE B 1 208 ? -0.181  1.812   52.219  1.00 17.63 ? 255 PHE B CE1 1 
ATOM   4317 C  CE2 . PHE B 1 208 ? 0.092   -0.535  51.999  1.00 17.81 ? 255 PHE B CE2 1 
ATOM   4318 C  CZ  . PHE B 1 208 ? 0.187   0.614   52.739  1.00 17.68 ? 255 PHE B CZ  1 
ATOM   4319 N  N   . VAL B 1 209 ? -3.822  0.875   46.484  1.00 12.62 ? 256 VAL B N   1 
ATOM   4320 C  CA  . VAL B 1 209 ? -3.912  1.008   45.025  1.00 12.42 ? 256 VAL B CA  1 
ATOM   4321 C  C   . VAL B 1 209 ? -5.319  1.333   44.549  1.00 11.98 ? 256 VAL B C   1 
ATOM   4322 O  O   . VAL B 1 209 ? -5.482  2.234   43.734  1.00 13.45 ? 256 VAL B O   1 
ATOM   4323 C  CB  . VAL B 1 209 ? -3.352  -0.254  44.329  1.00 13.35 ? 256 VAL B CB  1 
ATOM   4324 C  CG1 . VAL B 1 209 ? -3.576  -0.205  42.820  1.00 14.53 ? 256 VAL B CG1 1 
ATOM   4325 C  CG2 . VAL B 1 209 ? -1.868  -0.412  44.609  1.00 14.67 ? 256 VAL B CG2 1 
ATOM   4326 N  N   . TRP B 1 210 ? -6.332  0.590   44.966  1.00 12.37 ? 257 TRP B N   1 
ATOM   4327 C  CA  . TRP B 1 210 ? -7.666  0.797   44.433  1.00 12.93 ? 257 TRP B CA  1 
ATOM   4328 C  C   . TRP B 1 210 ? -8.422  1.897   45.154  1.00 13.39 ? 257 TRP B C   1 
ATOM   4329 O  O   . TRP B 1 210 ? -8.424  1.940   46.378  1.00 16.12 ? 257 TRP B O   1 
ATOM   4330 C  CB  . TRP B 1 210 ? -8.507  -0.482  44.528  1.00 13.47 ? 257 TRP B CB  1 
ATOM   4331 C  CG  . TRP B 1 210 ? -7.889  -1.705  43.918  1.00 13.83 ? 257 TRP B CG  1 
ATOM   4332 C  CD1 . TRP B 1 210 ? -7.719  -2.895  44.563  1.00 15.34 ? 257 TRP B CD1 1 
ATOM   4333 C  CD2 . TRP B 1 210 ? -7.462  -1.885  42.571  1.00 13.62 ? 257 TRP B CD2 1 
ATOM   4334 N  NE1 . TRP B 1 210 ? -7.201  -3.792  43.688  1.00 16.12 ? 257 TRP B NE1 1 
ATOM   4335 C  CE2 . TRP B 1 210 ? -7.010  -3.211  42.470  1.00 15.04 ? 257 TRP B CE2 1 
ATOM   4336 C  CE3 . TRP B 1 210 ? -7.401  -1.037  41.474  1.00 14.86 ? 257 TRP B CE3 1 
ATOM   4337 C  CZ2 . TRP B 1 210 ? -6.513  -3.713  41.276  1.00 15.66 ? 257 TRP B CZ2 1 
ATOM   4338 C  CZ3 . TRP B 1 210 ? -6.921  -1.544  40.290  1.00 16.02 ? 257 TRP B CZ3 1 
ATOM   4339 C  CH2 . TRP B 1 210 ? -6.455  -2.849  40.218  1.00 15.90 ? 257 TRP B CH2 1 
ATOM   4340 N  N   . ALA B 1 211 ? -9.065  2.767   44.420  1.00 13.37 ? 258 ALA B N   1 
ATOM   4341 C  CA  . ALA B 1 211 ? -9.989  3.733   44.991  1.00 15.07 ? 258 ALA B CA  1 
ATOM   4342 C  C   . ALA B 1 211 ? -11.191 3.001   45.562  1.00 15.20 ? 258 ALA B C   1 
ATOM   4343 O  O   . ALA B 1 211 ? -11.767 2.098   44.953  1.00 16.15 ? 258 ALA B O   1 
ATOM   4344 C  CB  . ALA B 1 211 ? -10.428 4.665   43.912  1.00 16.35 ? 258 ALA B CB  1 
ATOM   4345 N  N   . ALA B 1 212 ? -11.606 3.464   46.756  1.00 17.94 ? 259 ALA B N   1 
ATOM   4346 C  CA  . ALA B 1 212 ? -12.800 2.953   47.421  1.00 20.60 ? 259 ALA B CA  1 
ATOM   4347 C  C   . ALA B 1 212 ? -13.922 3.992   47.309  1.00 20.10 ? 259 ALA B C   1 
ATOM   4348 O  O   . ALA B 1 212 ? -13.684 5.175   47.184  1.00 20.07 ? 259 ALA B O   1 
ATOM   4349 C  CB  . ALA B 1 212 ? -12.416 2.666   48.851  1.00 21.52 ? 259 ALA B CB  1 
ATOM   4350 N  N   . GLU B 1 213 ? -15.179 3.549   47.463  1.00 25.65 ? 260 GLU B N   1 
ATOM   4351 C  CA  . GLU B 1 213 ? -16.314 4.464   47.358  1.00 27.40 ? 260 GLU B CA  1 
ATOM   4352 C  C   . GLU B 1 213 ? -16.250 5.564   48.419  1.00 24.76 ? 260 GLU B C   1 
ATOM   4353 O  O   . GLU B 1 213 ? -16.529 6.738   48.146  1.00 26.90 ? 260 GLU B O   1 
ATOM   4354 C  CB  . GLU B 1 213 ? -17.604 3.662   47.515  1.00 33.47 ? 260 GLU B CB  1 
ATOM   4355 C  CG  . GLU B 1 213 ? -18.862 4.514   47.380  1.00 37.03 ? 260 GLU B CG  1 
ATOM   4356 C  CD  . GLU B 1 213 ? -20.070 3.636   47.075  1.00 46.91 ? 260 GLU B CD  1 
ATOM   4357 O  OE1 . GLU B 1 213 ? -20.224 2.561   47.709  1.00 54.60 ? 260 GLU B OE1 1 
ATOM   4358 O  OE2 . GLU B 1 213 ? -20.849 4.025   46.185  1.00 56.14 ? 260 GLU B OE2 1 
ATOM   4359 N  N   . LYS B 1 214 ? -15.799 5.198   49.617  1.00 23.24 ? 261 LYS B N   1 
ATOM   4360 C  CA  . LYS B 1 214 ? -15.801 6.164   50.704  1.00 27.80 ? 261 LYS B CA  1 
ATOM   4361 C  C   . LYS B 1 214 ? -14.687 7.192   50.536  1.00 24.03 ? 261 LYS B C   1 
ATOM   4362 O  O   . LYS B 1 214 ? -14.562 8.125   51.307  1.00 24.38 ? 261 LYS B O   1 
ATOM   4363 C  CB  . LYS B 1 214 ? -15.662 5.531   52.088  1.00 29.44 ? 261 LYS B CB  1 
ATOM   4364 C  CG  . LYS B 1 214 ? -14.339 4.846   52.321  1.00 33.83 ? 261 LYS B CG  1 
ATOM   4365 C  CD  . LYS B 1 214 ? -13.956 4.627   53.783  1.00 43.64 ? 261 LYS B CD  1 
ATOM   4366 C  CE  . LYS B 1 214 ? -12.682 3.831   53.890  1.00 49.59 ? 261 LYS B CE  1 
ATOM   4367 N  NZ  . LYS B 1 214 ? -11.999 4.057   55.168  1.00 53.01 ? 261 LYS B NZ  1 
ATOM   4368 N  N   . ASP B 1 215 ? -13.812 7.036   49.537  1.00 21.27 ? 262 ASP B N   1 
ATOM   4369 C  CA  . ASP B 1 215 ? -12.768 8.013   49.333  1.00 19.93 ? 262 ASP B CA  1 
ATOM   4370 C  C   . ASP B 1 215 ? -13.310 9.329   48.783  1.00 20.56 ? 262 ASP B C   1 
ATOM   4371 O  O   . ASP B 1 215 ? -12.591 10.311  48.841  1.00 26.26 ? 262 ASP B O   1 
ATOM   4372 C  CB  . ASP B 1 215 ? -11.725 7.459   48.370  1.00 19.11 ? 262 ASP B CB  1 
ATOM   4373 C  CG  . ASP B 1 215 ? -10.928 6.305   48.934  1.00 20.15 ? 262 ASP B CG  1 
ATOM   4374 O  OD1 . ASP B 1 215 ? -11.013 6.057   50.153  1.00 20.75 ? 262 ASP B OD1 1 
ATOM   4375 O  OD2 . ASP B 1 215 ? -10.198 5.665   48.176  1.00 17.67 ? 262 ASP B OD2 1 
ATOM   4376 N  N   . GLY B 1 216 ? -14.498 9.354   48.184  1.00 19.96 ? 263 GLY B N   1 
ATOM   4377 C  CA  . GLY B 1 216 ? -15.105 10.643  47.881  1.00 21.78 ? 263 GLY B CA  1 
ATOM   4378 C  C   . GLY B 1 216 ? -15.600 10.799  46.452  1.00 23.55 ? 263 GLY B C   1 
ATOM   4379 O  O   . GLY B 1 216 ? -16.310 11.752  46.154  1.00 24.22 ? 263 GLY B O   1 
ATOM   4380 N  N   . THR B 1 217 ? -15.202 9.888   45.555  1.00 18.65 ? 264 THR B N   1 
ATOM   4381 C  CA  . THR B 1 217 ? -15.595 9.971   44.161  1.00 18.87 ? 264 THR B CA  1 
ATOM   4382 C  C   . THR B 1 217 ? -16.197 8.633   43.749  1.00 19.48 ? 264 THR B C   1 
ATOM   4383 O  O   . THR B 1 217 ? -15.494 7.699   43.355  1.00 18.30 ? 264 THR B O   1 
ATOM   4384 C  CB  . THR B 1 217 ? -14.390 10.308  43.281  1.00 18.98 ? 264 THR B CB  1 
ATOM   4385 O  OG1 . THR B 1 217 ? -13.783 11.479  43.825  1.00 21.64 ? 264 THR B OG1 1 
ATOM   4386 C  CG2 . THR B 1 217 ? -14.813 10.546  41.839  1.00 20.44 ? 264 THR B CG2 1 
ATOM   4387 N  N   . PRO B 1 218 ? -17.519 8.448   43.836  1.00 18.48 ? 265 PRO B N   1 
ATOM   4388 C  CA  . PRO B 1 218 ? -18.095 7.147   43.590  1.00 18.50 ? 265 PRO B CA  1 
ATOM   4389 C  C   . PRO B 1 218 ? -17.806 6.555   42.217  1.00 15.87 ? 265 PRO B C   1 
ATOM   4390 O  O   . PRO B 1 218 ? -17.617 5.343   42.138  1.00 17.20 ? 265 PRO B O   1 
ATOM   4391 C  CB  . PRO B 1 218 ? -19.615 7.331   43.825  1.00 21.03 ? 265 PRO B CB  1 
ATOM   4392 C  CG  . PRO B 1 218 ? -19.669 8.522   44.749  1.00 22.67 ? 265 PRO B CG  1 
ATOM   4393 C  CD  . PRO B 1 218 ? -18.472 9.418   44.432  1.00 21.89 ? 265 PRO B CD  1 
ATOM   4394 N  N   . TRP B 1 219 ? -17.671 7.363   41.169  1.00 16.41 ? 266 TRP B N   1 
ATOM   4395 C  CA  . TRP B 1 219 ? -17.501 6.761   39.861  1.00 14.96 ? 266 TRP B CA  1 
ATOM   4396 C  C   . TRP B 1 219 ? -16.147 6.074   39.740  1.00 14.19 ? 266 TRP B C   1 
ATOM   4397 O  O   . TRP B 1 219 ? -15.947 5.258   38.845  1.00 15.18 ? 266 TRP B O   1 
ATOM   4398 C  CB  . TRP B 1 219 ? -17.721 7.780   38.745  1.00 14.54 ? 266 TRP B CB  1 
ATOM   4399 C  CG  . TRP B 1 219 ? -16.690 8.864   38.564  1.00 15.34 ? 266 TRP B CG  1 
ATOM   4400 C  CD1 . TRP B 1 219 ? -16.747 10.152  39.026  1.00 16.20 ? 266 TRP B CD1 1 
ATOM   4401 C  CD2 . TRP B 1 219 ? -15.449 8.790   37.852  1.00 14.43 ? 266 TRP B CD2 1 
ATOM   4402 N  NE1 . TRP B 1 219 ? -15.626 10.852  38.680  1.00 15.54 ? 266 TRP B NE1 1 
ATOM   4403 C  CE2 . TRP B 1 219 ? -14.819 10.064  37.904  1.00 14.87 ? 266 TRP B CE2 1 
ATOM   4404 C  CE3 . TRP B 1 219 ? -14.828 7.798   37.076  1.00 15.19 ? 266 TRP B CE3 1 
ATOM   4405 C  CZ2 . TRP B 1 219 ? -13.605 10.336  37.301  1.00 16.00 ? 266 TRP B CZ2 1 
ATOM   4406 C  CZ3 . TRP B 1 219 ? -13.632 8.078   36.474  1.00 16.49 ? 266 TRP B CZ3 1 
ATOM   4407 C  CH2 . TRP B 1 219 ? -13.012 9.320   36.604  1.00 16.81 ? 266 TRP B CH2 1 
ATOM   4408 N  N   . MET B 1 220 ? -15.192 6.430   40.604  1.00 13.42 ? 267 MET B N   1 
ATOM   4409 C  CA  . MET B 1 220 ? -13.832 5.914   40.574  1.00 12.92 ? 267 MET B CA  1 
ATOM   4410 C  C   . MET B 1 220 ? -13.683 4.639   41.396  1.00 14.10 ? 267 MET B C   1 
ATOM   4411 O  O   . MET B 1 220 ? -12.602 4.076   41.409  1.00 13.68 ? 267 MET B O   1 
ATOM   4412 C  CB  . MET B 1 220 ? -12.833 6.986   41.019  1.00 13.19 ? 267 MET B CB  1 
ATOM   4413 C  CG  . MET B 1 220 ? -12.315 7.807   39.904  1.00 13.42 ? 267 MET B CG  1 
ATOM   4414 S  SD  . MET B 1 220 ? -11.370 6.864   38.695  1.00 14.08 ? 267 MET B SD  1 
ATOM   4415 C  CE  . MET B 1 220 ? -10.030 6.350   39.750  1.00 16.03 ? 267 MET B CE  1 
ATOM   4416 N  N   . THR B 1 221 ? -14.720 4.165   42.119  1.00 14.38 ? 268 THR B N   1 
ATOM   4417 C  CA  . THR B 1 221 ? -14.587 2.961   42.934  1.00 14.63 ? 268 THR B CA  1 
ATOM   4418 C  C   . THR B 1 221 ? -14.049 1.787   42.115  1.00 14.04 ? 268 THR B C   1 
ATOM   4419 O  O   . THR B 1 221 ? -14.666 1.400   41.133  1.00 15.39 ? 268 THR B O   1 
ATOM   4420 C  CB  . THR B 1 221 ? -15.945 2.573   43.536  1.00 16.15 ? 268 THR B CB  1 
ATOM   4421 O  OG1 . THR B 1 221 ? -16.402 3.707   44.261  1.00 18.46 ? 268 THR B OG1 1 
ATOM   4422 C  CG2 . THR B 1 221 ? -15.819 1.383   44.469  1.00 18.97 ? 268 THR B CG2 1 
ATOM   4423 N  N   . GLY B 1 222 ? -12.927 1.223   42.530  1.00 13.07 ? 269 GLY B N   1 
ATOM   4424 C  CA  . GLY B 1 222 ? -12.353 0.111   41.798  1.00 13.20 ? 269 GLY B CA  1 
ATOM   4425 C  C   . GLY B 1 222 ? -11.344 0.532   40.744  1.00 12.48 ? 269 GLY B C   1 
ATOM   4426 O  O   . GLY B 1 222 ? -10.710 -0.322  40.144  1.00 13.28 ? 269 GLY B O   1 
ATOM   4427 N  N   . GLY B 1 223 ? -11.200 1.832   40.554  1.00 11.97 ? 270 GLY B N   1 
ATOM   4428 C  CA  . GLY B 1 223 ? -10.161 2.399   39.708  1.00 11.08 ? 270 GLY B CA  1 
ATOM   4429 C  C   . GLY B 1 223 ? -8.926  2.682   40.533  1.00 11.28 ? 270 GLY B C   1 
ATOM   4430 O  O   . GLY B 1 223 ? -8.782  2.279   41.678  1.00 12.06 ? 270 GLY B O   1 
ATOM   4431 N  N   . SER B 1 224 ? -7.994  3.398   39.909  1.00 10.97 ? 271 SER B N   1 
ATOM   4432 C  CA  . SER B 1 224 ? -6.751  3.751   40.557  1.00 10.33 ? 271 SER B CA  1 
ATOM   4433 C  C   . SER B 1 224 ? -6.241  5.046   39.939  1.00 10.47 ? 271 SER B C   1 
ATOM   4434 O  O   . SER B 1 224 ? -6.827  5.539   38.980  1.00 11.84 ? 271 SER B O   1 
ATOM   4435 C  CB  . SER B 1 224 ? -5.754  2.630   40.442  1.00 11.44 ? 271 SER B CB  1 
ATOM   4436 O  OG  . SER B 1 224 ? -4.578  2.871   41.203  1.00 12.09 ? 271 SER B OG  1 
ATOM   4437 N  N   . TYR B 1 225 ? -5.176  5.614   40.470  1.00 10.35 ? 272 TYR B N   1 
ATOM   4438 C  CA  . TYR B 1 225 ? -4.605  6.839   39.956  1.00 10.33 ? 272 TYR B CA  1 
ATOM   4439 C  C   . TYR B 1 225 ? -3.182  6.544   39.524  1.00 10.03 ? 272 TYR B C   1 
ATOM   4440 O  O   . TYR B 1 225 ? -2.436  5.816   40.211  1.00 11.14 ? 272 TYR B O   1 
ATOM   4441 C  CB  . TYR B 1 225 ? -4.628  7.978   40.981  1.00 10.08 ? 272 TYR B CB  1 
ATOM   4442 C  CG  . TYR B 1 225 ? -6.032  8.319   41.372  1.00 10.72 ? 272 TYR B CG  1 
ATOM   4443 C  CD1 . TYR B 1 225 ? -6.762  9.217   40.630  1.00 11.54 ? 272 TYR B CD1 1 
ATOM   4444 C  CD2 . TYR B 1 225 ? -6.647  7.645   42.405  1.00 11.60 ? 272 TYR B CD2 1 
ATOM   4445 C  CE1 . TYR B 1 225 ? -8.083  9.464   40.934  1.00 11.82 ? 272 TYR B CE1 1 
ATOM   4446 C  CE2 . TYR B 1 225 ? -7.955  7.907   42.747  1.00 12.86 ? 272 TYR B CE2 1 
ATOM   4447 C  CZ  . TYR B 1 225 ? -8.663  8.815   41.986  1.00 12.35 ? 272 TYR B CZ  1 
ATOM   4448 O  OH  . TYR B 1 225 ? -9.996  9.059   42.241  1.00 14.52 ? 272 TYR B OH  1 
ATOM   4449 N  N   . LEU B 1 226 ? -2.832  7.060   38.356  1.00 9.38  ? 273 LEU B N   1 
ATOM   4450 C  CA  . LEU B 1 226 ? -1.564  6.763   37.694  1.00 9.34  ? 273 LEU B CA  1 
ATOM   4451 C  C   . LEU B 1 226 ? -0.725  8.027   37.582  1.00 10.00 ? 273 LEU B C   1 
ATOM   4452 O  O   . LEU B 1 226 ? -1.217  9.071   37.137  1.00 11.54 ? 273 LEU B O   1 
ATOM   4453 C  CB  . LEU B 1 226 ? -1.882  6.224   36.299  1.00 11.64 ? 273 LEU B CB  1 
ATOM   4454 C  CG  . LEU B 1 226 ? -0.663  5.959   35.434  1.00 12.00 ? 273 LEU B CG  1 
ATOM   4455 C  CD1 . LEU B 1 226 ? 0.327   4.955   36.000  1.00 13.87 ? 273 LEU B CD1 1 
ATOM   4456 C  CD2 . LEU B 1 226 ? -1.199  5.508   34.074  1.00 14.19 ? 273 LEU B CD2 1 
ATOM   4457 N  N   . VAL B 1 227 ? 0.544   7.914   37.966  1.00 10.04 ? 274 VAL B N   1 
ATOM   4458 C  CA  . VAL B 1 227 ? 1.544   8.922   37.675  1.00 10.59 ? 274 VAL B CA  1 
ATOM   4459 C  C   . VAL B 1 227 ? 2.514   8.334   36.689  1.00 10.83 ? 274 VAL B C   1 
ATOM   4460 O  O   . VAL B 1 227 ? 3.033   7.238   36.944  1.00 11.75 ? 274 VAL B O   1 
ATOM   4461 C  CB  . VAL B 1 227 ? 2.254   9.380   38.949  1.00 12.08 ? 274 VAL B CB  1 
ATOM   4462 C  CG1 . VAL B 1 227 ? 3.411   10.323  38.635  1.00 14.50 ? 274 VAL B CG1 1 
ATOM   4463 C  CG2 . VAL B 1 227 ? 1.288   10.034  39.894  1.00 12.98 ? 274 VAL B CG2 1 
ATOM   4464 N  N   . ALA B 1 228 ? 2.784   9.065   35.620  1.00 10.06 ? 275 ALA B N   1 
ATOM   4465 C  CA  . ALA B 1 228 ? 3.785   8.681   34.645  1.00 10.65 ? 275 ALA B CA  1 
ATOM   4466 C  C   . ALA B 1 228 ? 4.893   9.724   34.689  1.00 10.33 ? 275 ALA B C   1 
ATOM   4467 O  O   . ALA B 1 228 ? 4.608   10.933  34.638  1.00 12.18 ? 275 ALA B O   1 
ATOM   4468 C  CB  . ALA B 1 228 ? 3.197   8.666   33.274  1.00 11.17 ? 275 ALA B CB  1 
ATOM   4469 N  N   . ARG B 1 229 ? 6.135   9.284   34.767  1.00 10.60 ? 276 ARG B N   1 
ATOM   4470 C  CA  . ARG B 1 229 ? 7.268   10.195  34.690  1.00 11.07 ? 276 ARG B CA  1 
ATOM   4471 C  C   . ARG B 1 229 ? 8.284   9.580   33.751  1.00 11.36 ? 276 ARG B C   1 
ATOM   4472 O  O   . ARG B 1 229 ? 8.716   8.450   33.917  1.00 11.70 ? 276 ARG B O   1 
ATOM   4473 C  CB  . ARG B 1 229 ? 7.955   10.399  36.034  1.00 11.74 ? 276 ARG B CB  1 
ATOM   4474 C  CG  . ARG B 1 229 ? 7.059   10.917  37.140  1.00 12.09 ? 276 ARG B CG  1 
ATOM   4475 C  CD  . ARG B 1 229 ? 6.703   12.362  36.995  1.00 12.78 ? 276 ARG B CD  1 
ATOM   4476 N  NE  . ARG B 1 229 ? 7.821   13.212  37.440  1.00 12.28 ? 276 ARG B NE  1 
ATOM   4477 C  CZ  . ARG B 1 229 ? 7.690   14.473  37.836  1.00 13.09 ? 276 ARG B CZ  1 
ATOM   4478 N  NH1 . ARG B 1 229 ? 6.596   15.153  37.729  1.00 14.27 ? 276 ARG B NH1 1 
ATOM   4479 N  NH2 . ARG B 1 229 ? 8.755   15.036  38.343  1.00 14.11 ? 276 ARG B NH2 1 
ATOM   4480 N  N   . ARG B 1 230 ? 8.636   10.331  32.730  1.00 11.37 ? 277 ARG B N   1 
ATOM   4481 C  CA  . ARG B 1 230 ? 9.718   9.945   31.861  1.00 11.32 ? 277 ARG B CA  1 
ATOM   4482 C  C   . ARG B 1 230 ? 11.013  10.437  32.485  1.00 11.62 ? 277 ARG B C   1 
ATOM   4483 O  O   . ARG B 1 230 ? 11.173  11.637  32.607  1.00 12.77 ? 277 ARG B O   1 
ATOM   4484 C  CB  . ARG B 1 230 ? 9.518   10.510  30.459  1.00 13.06 ? 277 ARG B CB  1 
ATOM   4485 C  CG  . ARG B 1 230 ? 10.545  9.968   29.484  1.00 14.71 ? 277 ARG B CG  1 
ATOM   4486 C  CD  . ARG B 1 230 ? 10.232  10.522  28.117  1.00 18.60 ? 277 ARG B CD  1 
ATOM   4487 N  NE  . ARG B 1 230 ? 11.026  9.921   27.036  1.00 20.47 ? 277 ARG B NE  1 
ATOM   4488 C  CZ  . ARG B 1 230 ? 12.231  10.305  26.674  1.00 21.60 ? 277 ARG B CZ  1 
ATOM   4489 N  NH1 . ARG B 1 230 ? 12.725  11.410  27.201  1.00 24.52 ? 277 ARG B NH1 1 
ATOM   4490 N  NH2 . ARG B 1 230 ? 12.917  9.684   25.738  1.00 23.38 ? 277 ARG B NH2 1 
ATOM   4491 N  N   . ILE B 1 231 ? 11.856  9.503   32.906  1.00 11.23 ? 278 ILE B N   1 
ATOM   4492 C  CA  . ILE B 1 231 ? 13.061  9.849   33.648  1.00 11.31 ? 278 ILE B CA  1 
ATOM   4493 C  C   . ILE B 1 231 ? 14.269  9.455   32.852  1.00 11.77 ? 278 ILE B C   1 
ATOM   4494 O  O   . ILE B 1 231 ? 14.585  8.264   32.710  1.00 13.29 ? 278 ILE B O   1 
ATOM   4495 C  CB  . ILE B 1 231 ? 13.095  9.200   35.025  1.00 11.00 ? 278 ILE B CB  1 
ATOM   4496 C  CG1 . ILE B 1 231 ? 11.801  9.435   35.775  1.00 12.57 ? 278 ILE B CG1 1 
ATOM   4497 C  CG2 . ILE B 1 231 ? 14.315  9.711   35.780  1.00 12.78 ? 278 ILE B CG2 1 
ATOM   4498 C  CD1 . ILE B 1 231 ? 11.726  8.722   37.089  1.00 13.62 ? 278 ILE B CD1 1 
ATOM   4499 N  N   . ARG B 1 232 ? 14.948  10.449  32.348  1.00 11.60 ? 279 ARG B N   1 
ATOM   4500 C  CA  . ARG B 1 232 ? 16.191  10.207  31.633  1.00 13.28 ? 279 ARG B CA  1 
ATOM   4501 C  C   . ARG B 1 232 ? 17.312  9.893   32.606  1.00 13.66 ? 279 ARG B C   1 
ATOM   4502 O  O   . ARG B 1 232 ? 17.401  10.486  33.662  1.00 14.18 ? 279 ARG B O   1 
ATOM   4503 C  CB  . ARG B 1 232 ? 16.602  11.472  30.877  1.00 16.80 ? 279 ARG B CB  1 
ATOM   4504 C  CG  . ARG B 1 232 ? 17.938  11.533  30.160  1.00 22.64 ? 279 ARG B CG  1 
ATOM   4505 C  CD  . ARG B 1 232 ? 18.051  10.473  29.121  1.00 24.81 ? 279 ARG B CD  1 
ATOM   4506 N  NE  . ARG B 1 232 ? 19.409  10.550  28.563  1.00 27.16 ? 279 ARG B NE  1 
ATOM   4507 C  CZ  . ARG B 1 232 ? 19.837  11.515  27.721  1.00 31.74 ? 279 ARG B CZ  1 
ATOM   4508 N  NH1 . ARG B 1 232 ? 19.006  12.381  27.155  1.00 31.32 ? 279 ARG B NH1 1 
ATOM   4509 N  NH2 . ARG B 1 232 ? 21.122  11.562  27.395  1.00 36.84 ? 279 ARG B NH2 1 
ATOM   4510 N  N   . MET B 1 233 ? 18.152  8.937   32.258  1.00 12.64 ? 280 MET B N   1 
ATOM   4511 C  CA  . MET B 1 233 ? 19.380  8.661   32.991  1.00 12.68 ? 280 MET B CA  1 
ATOM   4512 C  C   . MET B 1 233 ? 20.560  9.265   32.260  1.00 13.18 ? 280 MET B C   1 
ATOM   4513 O  O   . MET B 1 233 ? 20.656  9.186   31.039  1.00 14.61 ? 280 MET B O   1 
ATOM   4514 C  CB  . MET B 1 233 ? 19.609  7.152   33.074  1.00 12.78 ? 280 MET B CB  1 
ATOM   4515 C  CG  . MET B 1 233 ? 18.587  6.445   33.940  1.00 12.93 ? 280 MET B CG  1 
ATOM   4516 S  SD  . MET B 1 233 ? 18.590  4.663   33.606  1.00 14.67 ? 280 MET B SD  1 
ATOM   4517 C  CE  . MET B 1 233 ? 17.392  4.098   34.813  1.00 16.15 ? 280 MET B CE  1 
ATOM   4518 N  N   . HIS B 1 234 ? 21.491  9.799   33.061  1.00 12.18 ? 281 HIS B N   1 
ATOM   4519 C  CA  . HIS B 1 234 ? 22.746  10.262  32.492  1.00 12.94 ? 281 HIS B CA  1 
ATOM   4520 C  C   . HIS B 1 234 ? 23.706  9.095   32.466  1.00 13.11 ? 281 HIS B C   1 
ATOM   4521 O  O   . HIS B 1 234 ? 24.525  8.914   33.370  1.00 14.34 ? 281 HIS B O   1 
ATOM   4522 C  CB  . HIS B 1 234 ? 23.281  11.412  33.339  1.00 15.14 ? 281 HIS B CB  1 
ATOM   4523 C  CG  . HIS B 1 234 ? 22.347  12.558  33.419  1.00 19.10 ? 281 HIS B CG  1 
ATOM   4524 N  ND1 . HIS B 1 234 ? 21.725  13.124  32.331  1.00 22.76 ? 281 HIS B ND1 1 
ATOM   4525 C  CD2 . HIS B 1 234 ? 22.000  13.278  34.484  1.00 21.85 ? 281 HIS B CD2 1 
ATOM   4526 C  CE1 . HIS B 1 234 ? 20.955  14.144  32.769  1.00 22.22 ? 281 HIS B CE1 1 
ATOM   4527 N  NE2 . HIS B 1 234 ? 21.126  14.253  34.064  1.00 22.83 ? 281 HIS B NE2 1 
ATOM   4528 N  N   . ILE B 1 235 ? 23.532  8.252   31.461  1.00 12.98 ? 282 ILE B N   1 
ATOM   4529 C  CA  . ILE B 1 235 ? 24.166  6.946   31.406  1.00 13.87 ? 282 ILE B CA  1 
ATOM   4530 C  C   . ILE B 1 235 ? 25.679  7.080   31.475  1.00 13.05 ? 282 ILE B C   1 
ATOM   4531 O  O   . ILE B 1 235 ? 26.358  6.342   32.209  1.00 14.51 ? 282 ILE B O   1 
ATOM   4532 C  CB  . ILE B 1 235 ? 23.715  6.243   30.109  1.00 15.24 ? 282 ILE B CB  1 
ATOM   4533 C  CG1 . ILE B 1 235 ? 22.199  5.882   30.068  1.00 16.50 ? 282 ILE B CG1 1 
ATOM   4534 C  CG2 . ILE B 1 235 ? 24.566  5.023   29.806  1.00 15.82 ? 282 ILE B CG2 1 
ATOM   4535 C  CD1 . ILE B 1 235 ? 21.807  4.907   31.128  1.00 17.84 ? 282 ILE B CD1 1 
ATOM   4536 N  N   . GLU B 1 236 ? 26.226  8.004   30.686  1.00 14.35 ? 283 GLU B N   1 
ATOM   4537 C  CA  . GLU B 1 236 ? 27.680  8.028   30.508  1.00 16.11 ? 283 GLU B CA  1 
ATOM   4538 C  C   . GLU B 1 236 ? 28.324  8.598   31.762  1.00 16.84 ? 283 GLU B C   1 
ATOM   4539 O  O   . GLU B 1 236 ? 29.437  8.189   32.102  1.00 19.64 ? 283 GLU B O   1 
ATOM   4540 C  CB  . GLU B 1 236 ? 28.110  8.816   29.281  1.00 17.99 ? 283 GLU B CB  1 
ATOM   4541 C  CG  . GLU B 1 236 ? 27.547  8.277   27.960  1.00 17.19 ? 283 GLU B CG  1 
ATOM   4542 C  CD  . GLU B 1 236 ? 26.081  8.559   27.619  1.00 18.47 ? 283 GLU B CD  1 
ATOM   4543 O  OE1 . GLU B 1 236 ? 25.447  9.358   28.349  1.00 19.55 ? 283 GLU B OE1 1 
ATOM   4544 O  OE2 . GLU B 1 236 ? 25.633  7.952   26.645  1.00 19.75 ? 283 GLU B OE2 1 
ATOM   4545 N  N   . THR B 1 237 ? 27.616  9.410   32.540  1.00 16.07 ? 284 THR B N   1 
ATOM   4546 C  CA  . THR B 1 237 ? 28.125  9.921   33.794  1.00 16.60 ? 284 THR B CA  1 
ATOM   4547 C  C   . THR B 1 237 ? 28.094  8.806   34.840  1.00 15.61 ? 284 THR B C   1 
ATOM   4548 O  O   . THR B 1 237 ? 29.022  8.585   35.604  1.00 15.78 ? 284 THR B O   1 
ATOM   4549 C  CB  . THR B 1 237 ? 27.269  11.114  34.231  1.00 20.93 ? 284 THR B CB  1 
ATOM   4550 O  OG1 . THR B 1 237 ? 27.376  12.102  33.198  1.00 26.42 ? 284 THR B OG1 1 
ATOM   4551 C  CG2 . THR B 1 237 ? 27.757  11.716  35.525  1.00 24.50 ? 284 THR B CG2 1 
ATOM   4552 N  N   . TRP B 1 238 ? 26.966  8.103   34.935  1.00 14.13 ? 285 TRP B N   1 
ATOM   4553 C  CA  . TRP B 1 238 ? 26.820  6.951   35.810  1.00 12.61 ? 285 TRP B CA  1 
ATOM   4554 C  C   . TRP B 1 238 ? 27.873  5.881   35.612  1.00 12.66 ? 285 TRP B C   1 
ATOM   4555 O  O   . TRP B 1 238 ? 28.442  5.383   36.574  1.00 14.37 ? 285 TRP B O   1 
ATOM   4556 C  CB  . TRP B 1 238 ? 25.441  6.344   35.577  1.00 13.01 ? 285 TRP B CB  1 
ATOM   4557 C  CG  . TRP B 1 238 ? 25.180  5.125   36.383  1.00 12.33 ? 285 TRP B CG  1 
ATOM   4558 C  CD1 . TRP B 1 238 ? 25.204  3.862   35.884  1.00 13.11 ? 285 TRP B CD1 1 
ATOM   4559 C  CD2 . TRP B 1 238 ? 24.862  5.020   37.764  1.00 12.73 ? 285 TRP B CD2 1 
ATOM   4560 N  NE1 . TRP B 1 238 ? 24.891  2.992   36.864  1.00 13.24 ? 285 TRP B NE1 1 
ATOM   4561 C  CE2 . TRP B 1 238 ? 24.671  3.654   38.039  1.00 13.97 ? 285 TRP B CE2 1 
ATOM   4562 C  CE3 . TRP B 1 238 ? 24.694  5.947   38.777  1.00 13.29 ? 285 TRP B CE3 1 
ATOM   4563 C  CZ2 . TRP B 1 238 ? 24.307  3.208   39.296  1.00 14.73 ? 285 TRP B CZ2 1 
ATOM   4564 C  CZ3 . TRP B 1 238 ? 24.338  5.480   40.028  1.00 15.31 ? 285 TRP B CZ3 1 
ATOM   4565 C  CH2 . TRP B 1 238 ? 24.146  4.139   40.280  1.00 15.07 ? 285 TRP B CH2 1 
ATOM   4566 N  N   . ASP B 1 239 ? 28.183  5.625   34.353  1.00 12.88 ? 286 ASP B N   1 
ATOM   4567 C  CA  . ASP B 1 239 ? 29.111  4.548   34.045  1.00 14.11 ? 286 ASP B CA  1 
ATOM   4568 C  C   . ASP B 1 239 ? 30.537  4.917   34.428  1.00 16.65 ? 286 ASP B C   1 
ATOM   4569 O  O   . ASP B 1 239 ? 31.371  4.007   34.516  1.00 17.55 ? 286 ASP B O   1 
ATOM   4570 C  CB  . ASP B 1 239 ? 28.993  4.153   32.588  1.00 13.62 ? 286 ASP B CB  1 
ATOM   4571 C  CG  . ASP B 1 239 ? 27.729  3.420   32.198  1.00 12.93 ? 286 ASP B CG  1 
ATOM   4572 O  OD1 . ASP B 1 239 ? 27.077  2.902   33.115  1.00 14.54 ? 286 ASP B OD1 1 
ATOM   4573 O  OD2 . ASP B 1 239 ? 27.492  3.385   30.982  1.00 14.97 ? 286 ASP B OD2 1 
ATOM   4574 N  N   . ARG B 1 240 ? 30.800  6.182   34.706  1.00 15.61 ? 287 ARG B N   1 
ATOM   4575 C  CA  . ARG B 1 240 ? 32.122  6.604   35.190  1.00 17.58 ? 287 ARG B CA  1 
ATOM   4576 C  C   . ARG B 1 240 ? 32.188  6.596   36.710  1.00 19.12 ? 287 ARG B C   1 
ATOM   4577 O  O   . ARG B 1 240 ? 33.264  6.847   37.276  1.00 21.00 ? 287 ARG B O   1 
ATOM   4578 C  CB  . ARG B 1 240 ? 32.409  8.032   34.696  1.00 21.53 ? 287 ARG B CB  1 
ATOM   4579 C  CG  . ARG B 1 240 ? 32.767  8.127   33.225  1.00 26.00 ? 287 ARG B CG  1 
ATOM   4580 C  CD  . ARG B 1 240 ? 33.308  9.519   32.880  1.00 35.13 ? 287 ARG B CD  1 
ATOM   4581 N  NE  . ARG B 1 240 ? 32.343  10.335  32.140  1.00 46.13 ? 287 ARG B NE  1 
ATOM   4582 C  CZ  . ARG B 1 240 ? 32.160  10.341  30.816  1.00 49.30 ? 287 ARG B CZ  1 
ATOM   4583 N  NH1 . ARG B 1 240 ? 32.947  9.643   30.011  1.00 53.01 ? 287 ARG B NH1 1 
ATOM   4584 N  NH2 . ARG B 1 240 ? 31.194  11.085  30.300  1.00 48.52 ? 287 ARG B NH2 1 
ATOM   4585 N  N   . ALA B 1 241 ? 31.086  6.376   37.398  1.00 16.20 ? 288 ALA B N   1 
ATOM   4586 C  CA  . ALA B 1 241 ? 31.076  6.322   38.842  1.00 17.34 ? 288 ALA B CA  1 
ATOM   4587 C  C   . ALA B 1 241 ? 31.702  5.016   39.293  1.00 16.73 ? 288 ALA B C   1 
ATOM   4588 O  O   . ALA B 1 241 ? 31.532  3.965   38.673  1.00 18.46 ? 288 ALA B O   1 
ATOM   4589 C  CB  . ALA B 1 241 ? 29.667  6.457   39.381  1.00 19.77 ? 288 ALA B CB  1 
ATOM   4590 N  N   . SER B 1 242 ? 32.373  5.060   40.442  1.00 16.58 ? 289 SER B N   1 
ATOM   4591 C  CA  . SER B 1 242 ? 32.894  3.822   41.004  1.00 16.58 ? 289 SER B CA  1 
ATOM   4592 C  C   . SER B 1 242 ? 31.782  2.879   41.450  1.00 16.26 ? 289 SER B C   1 
ATOM   4593 O  O   . SER B 1 242 ? 30.671  3.333   41.750  1.00 15.69 ? 289 SER B O   1 
ATOM   4594 C  CB  . SER B 1 242 ? 33.829  4.107   42.153  1.00 17.54 ? 289 SER B CB  1 
ATOM   4595 O  OG  . SER B 1 242 ? 33.103  4.692   43.215  1.00 19.60 ? 289 SER B OG  1 
ATOM   4596 N  N   . LEU B 1 243 ? 32.104  1.588   41.578  1.00 15.79 ? 290 LEU B N   1 
ATOM   4597 C  CA  . LEU B 1 243 ? 31.168  0.618   42.081  1.00 16.71 ? 290 LEU B CA  1 
ATOM   4598 C  C   . LEU B 1 243 ? 30.667  1.047   43.448  1.00 16.90 ? 290 LEU B C   1 
ATOM   4599 O  O   . LEU B 1 243 ? 29.485  1.002   43.727  1.00 16.96 ? 290 LEU B O   1 
ATOM   4600 C  CB  . LEU B 1 243 ? 31.817  -0.743  42.160  1.00 17.10 ? 290 LEU B CB  1 
ATOM   4601 C  CG  . LEU B 1 243 ? 30.926  -1.841  42.739  1.00 19.97 ? 290 LEU B CG  1 
ATOM   4602 C  CD1 . LEU B 1 243 ? 29.766  -2.145  41.817  1.00 21.90 ? 290 LEU B CD1 1 
ATOM   4603 C  CD2 . LEU B 1 243 ? 31.766  -3.102  42.955  1.00 24.15 ? 290 LEU B CD2 1 
ATOM   4604 N  N   . GLN B 1 244 ? 31.556  1.516   44.325  1.00 17.44 ? 291 GLN B N   1 
ATOM   4605 C  CA  . GLN B 1 244 ? 31.113  1.938   45.640  1.00 17.80 ? 291 GLN B CA  1 
ATOM   4606 C  C   . GLN B 1 244 ? 30.137  3.104   45.555  1.00 16.85 ? 291 GLN B C   1 
ATOM   4607 O  O   . GLN B 1 244 ? 29.155  3.109   46.309  1.00 17.08 ? 291 GLN B O   1 
ATOM   4608 C  CB  . GLN B 1 244 ? 32.305  2.198   46.568  1.00 20.94 ? 291 GLN B CB  1 
ATOM   4609 C  CG  . GLN B 1 244 ? 31.880  2.426   48.016  1.00 25.17 ? 291 GLN B CG  1 
ATOM   4610 C  CD  . GLN B 1 244 ? 31.231  1.192   48.615  1.00 32.84 ? 291 GLN B CD  1 
ATOM   4611 O  OE1 . GLN B 1 244 ? 31.860  0.131   48.750  1.00 36.83 ? 291 GLN B OE1 1 
ATOM   4612 N  NE2 . GLN B 1 244 ? 29.952  1.287   48.966  1.00 34.35 ? 291 GLN B NE2 1 
ATOM   4613 N  N   . GLU B 1 245 ? 30.420  4.096   44.722  1.00 16.36 ? 292 GLU B N   1 
ATOM   4614 C  CA  . GLU B 1 245 ? 29.528  5.227   44.589  1.00 16.71 ? 292 GLU B CA  1 
ATOM   4615 C  C   . GLU B 1 245 ? 28.141  4.754   44.133  1.00 14.82 ? 292 GLU B C   1 
ATOM   4616 O  O   . GLU B 1 245 ? 27.134  5.211   44.631  1.00 15.57 ? 292 GLU B O   1 
ATOM   4617 C  CB  . GLU B 1 245 ? 30.121  6.232   43.613  1.00 19.74 ? 292 GLU B CB  1 
ATOM   4618 C  CG  . GLU B 1 245 ? 31.230  7.130   44.168  1.00 26.18 ? 292 GLU B CG  1 
ATOM   4619 C  CD  . GLU B 1 245 ? 31.819  7.966   43.033  1.00 33.31 ? 292 GLU B CD  1 
ATOM   4620 O  OE1 . GLU B 1 245 ? 32.445  7.448   42.082  1.00 33.28 ? 292 GLU B OE1 1 
ATOM   4621 O  OE2 . GLU B 1 245 ? 31.582  9.186   43.080  1.00 42.33 ? 292 GLU B OE2 1 
ATOM   4622 N  N   . GLN B 1 246 ? 28.089  3.858   43.142  1.00 13.83 ? 293 GLN B N   1 
ATOM   4623 C  CA  . GLN B 1 246 ? 26.818  3.366   42.637  1.00 14.11 ? 293 GLN B CA  1 
ATOM   4624 C  C   . GLN B 1 246 ? 26.030  2.679   43.729  1.00 14.54 ? 293 GLN B C   1 
ATOM   4625 O  O   . GLN B 1 246 ? 24.828  2.873   43.867  1.00 14.93 ? 293 GLN B O   1 
ATOM   4626 C  CB  . GLN B 1 246 ? 27.030  2.392   41.477  1.00 14.39 ? 293 GLN B CB  1 
ATOM   4627 C  CG  . GLN B 1 246 ? 27.633  3.050   40.252  1.00 14.20 ? 293 GLN B CG  1 
ATOM   4628 C  CD  . GLN B 1 246 ? 27.633  2.142   39.043  1.00 15.19 ? 293 GLN B CD  1 
ATOM   4629 O  OE1 . GLN B 1 246 ? 27.123  1.024   39.102  1.00 16.08 ? 293 GLN B OE1 1 
ATOM   4630 N  NE2 . GLN B 1 246 ? 28.188  2.597   37.929  1.00 16.73 ? 293 GLN B NE2 1 
ATOM   4631 N  N   . GLU B 1 247 ? 26.682  1.789   44.495  1.00 14.24 ? 294 GLU B N   1 
ATOM   4632 C  CA  . GLU B 1 247 ? 26.019  1.079   45.563  1.00 14.03 ? 294 GLU B CA  1 
ATOM   4633 C  C   . GLU B 1 247 ? 25.582  2.034   46.651  1.00 14.72 ? 294 GLU B C   1 
ATOM   4634 O  O   . GLU B 1 247 ? 24.514  1.848   47.229  1.00 16.05 ? 294 GLU B O   1 
ATOM   4635 C  CB  . GLU B 1 247 ? 26.918  -0.049  46.081  1.00 15.39 ? 294 GLU B CB  1 
ATOM   4636 C  CG  . GLU B 1 247 ? 27.248  -1.070  45.010  1.00 16.39 ? 294 GLU B CG  1 
ATOM   4637 C  CD  . GLU B 1 247 ? 28.029  -2.290  45.456  1.00 17.30 ? 294 GLU B CD  1 
ATOM   4638 O  OE1 . GLU B 1 247 ? 28.717  -2.191  46.501  1.00 22.65 ? 294 GLU B OE1 1 
ATOM   4639 O  OE2 . GLU B 1 247 ? 27.853  -3.340  44.825  1.00 17.05 ? 294 GLU B OE2 1 
ATOM   4640 N  N   . ASP B 1 248 ? 26.400  3.035   46.957  1.00 15.38 ? 295 ASP B N   1 
ATOM   4641 C  CA  . ASP B 1 248 ? 26.035  4.012   47.967  1.00 15.70 ? 295 ASP B CA  1 
ATOM   4642 C  C   . ASP B 1 248 ? 24.790  4.788   47.564  1.00 15.33 ? 295 ASP B C   1 
ATOM   4643 O  O   . ASP B 1 248 ? 24.013  5.162   48.422  1.00 16.22 ? 295 ASP B O   1 
ATOM   4644 C  CB  . ASP B 1 248 ? 27.191  4.935   48.261  1.00 17.38 ? 295 ASP B CB  1 
ATOM   4645 C  CG  . ASP B 1 248 ? 28.289  4.389   49.162  1.00 19.57 ? 295 ASP B CG  1 
ATOM   4646 O  OD1 . ASP B 1 248 ? 28.131  3.300   49.677  1.00 21.84 ? 295 ASP B OD1 1 
ATOM   4647 O  OD2 . ASP B 1 248 ? 29.297  5.081   49.229  1.00 24.57 ? 295 ASP B OD2 1 
ATOM   4648 N  N   . VAL B 1 249 ? 24.639  5.123   46.273  1.00 13.80 ? 296 VAL B N   1 
ATOM   4649 C  CA  . VAL B 1 249 ? 23.463  5.825   45.806  1.00 13.46 ? 296 VAL B CA  1 
ATOM   4650 C  C   . VAL B 1 249 ? 22.186  5.095   46.135  1.00 13.99 ? 296 VAL B C   1 
ATOM   4651 O  O   . VAL B 1 249 ? 21.225  5.752   46.480  1.00 15.49 ? 296 VAL B O   1 
ATOM   4652 C  CB  . VAL B 1 249 ? 23.604  6.040   44.295  1.00 14.98 ? 296 VAL B CB  1 
ATOM   4653 C  CG1 . VAL B 1 249 ? 22.257  6.384   43.681  1.00 16.92 ? 296 VAL B CG1 1 
ATOM   4654 C  CG2 . VAL B 1 249 ? 24.622  7.112   43.940  1.00 15.87 ? 296 VAL B CG2 1 
ATOM   4655 N  N   . PHE B 1 250 ? 22.186  3.761   46.052  1.00 13.32 ? 297 PHE B N   1 
ATOM   4656 C  CA  . PHE B 1 250 ? 20.967  2.999   46.242  1.00 14.17 ? 297 PHE B CA  1 
ATOM   4657 C  C   . PHE B 1 250 ? 20.799  2.465   47.650  1.00 14.43 ? 297 PHE B C   1 
ATOM   4658 O  O   . PHE B 1 250 ? 19.695  2.380   48.149  1.00 17.28 ? 297 PHE B O   1 
ATOM   4659 C  CB  . PHE B 1 250 ? 20.844  1.829   45.268  1.00 14.54 ? 297 PHE B CB  1 
ATOM   4660 C  CG  . PHE B 1 250 ? 20.435  2.339   43.910  1.00 13.48 ? 297 PHE B CG  1 
ATOM   4661 C  CD1 . PHE B 1 250 ? 19.162  2.850   43.751  1.00 13.87 ? 297 PHE B CD1 1 
ATOM   4662 C  CD2 . PHE B 1 250 ? 21.304  2.307   42.841  1.00 15.39 ? 297 PHE B CD2 1 
ATOM   4663 C  CE1 . PHE B 1 250 ? 18.782  3.379   42.553  1.00 14.85 ? 297 PHE B CE1 1 
ATOM   4664 C  CE2 . PHE B 1 250 ? 20.912  2.838   41.627  1.00 14.85 ? 297 PHE B CE2 1 
ATOM   4665 C  CZ  . PHE B 1 250 ? 19.645  3.360   41.493  1.00 16.24 ? 297 PHE B CZ  1 
ATOM   4666 N  N   . GLY B 1 251 ? 21.873  2.042   48.294  1.00 14.34 ? 298 GLY B N   1 
ATOM   4667 C  CA  . GLY B 1 251 ? 21.759  1.346   49.552  1.00 14.73 ? 298 GLY B CA  1 
ATOM   4668 C  C   . GLY B 1 251 ? 21.652  -0.175  49.415  1.00 16.35 ? 298 GLY B C   1 
ATOM   4669 O  O   . GLY B 1 251 ? 21.412  -0.878  50.407  1.00 16.69 ? 298 GLY B O   1 
ATOM   4670 N  N   . ARG B 1 252 ? 21.862  -0.699  48.209  1.00 14.91 ? 299 ARG B N   1 
ATOM   4671 C  CA  . ARG B 1 252 ? 21.914  -2.121  47.952  1.00 14.51 ? 299 ARG B CA  1 
ATOM   4672 C  C   . ARG B 1 252 ? 23.143  -2.379  47.096  1.00 15.31 ? 299 ARG B C   1 
ATOM   4673 O  O   . ARG B 1 252 ? 23.619  -1.488  46.406  1.00 15.54 ? 299 ARG B O   1 
ATOM   4674 C  CB  . ARG B 1 252 ? 20.668  -2.556  47.182  1.00 14.95 ? 299 ARG B CB  1 
ATOM   4675 C  CG  . ARG B 1 252 ? 19.381  -2.539  47.951  1.00 15.42 ? 299 ARG B CG  1 
ATOM   4676 C  CD  . ARG B 1 252 ? 18.180  -2.845  47.115  1.00 14.12 ? 299 ARG B CD  1 
ATOM   4677 N  NE  . ARG B 1 252 ? 16.948  -2.964  47.904  1.00 15.16 ? 299 ARG B NE  1 
ATOM   4678 C  CZ  . ARG B 1 252 ? 16.472  -4.056  48.458  1.00 15.37 ? 299 ARG B CZ  1 
ATOM   4679 N  NH1 . ARG B 1 252 ? 17.194  -5.167  48.484  1.00 15.02 ? 299 ARG B NH1 1 
ATOM   4680 N  NH2 . ARG B 1 252 ? 15.302  -4.009  49.020  1.00 16.56 ? 299 ARG B NH2 1 
ATOM   4681 N  N   . ASP B 1 253 ? 23.693  -3.591  47.151  1.00 15.85 ? 300 ASP B N   1 
ATOM   4682 C  CA  . ASP B 1 253 ? 24.831  -3.926  46.330  1.00 16.59 ? 300 ASP B CA  1 
ATOM   4683 C  C   . ASP B 1 253 ? 24.347  -4.233  44.912  1.00 16.25 ? 300 ASP B C   1 
ATOM   4684 O  O   . ASP B 1 253 ? 23.185  -4.548  44.671  1.00 17.58 ? 300 ASP B O   1 
ATOM   4685 C  CB  . ASP B 1 253 ? 25.660  -5.066  46.931  1.00 18.27 ? 300 ASP B CB  1 
ATOM   4686 C  CG  . ASP B 1 253 ? 25.004  -6.426  46.771  1.00 21.01 ? 300 ASP B CG  1 
ATOM   4687 O  OD1 . ASP B 1 253 ? 24.085  -6.703  47.487  1.00 26.50 ? 300 ASP B OD1 1 
ATOM   4688 O  OD2 . ASP B 1 253 ? 25.331  -7.152  45.801  1.00 29.92 ? 300 ASP B OD2 1 
ATOM   4689 N  N   . LYS B 1 254 ? 25.278  -4.182  43.973  1.00 15.30 ? 301 LYS B N   1 
ATOM   4690 C  CA  . LYS B 1 254 ? 24.905  -4.270  42.577  1.00 17.04 ? 301 LYS B CA  1 
ATOM   4691 C  C   . LYS B 1 254 ? 24.683  -5.721  42.144  1.00 18.91 ? 301 LYS B C   1 
ATOM   4692 O  O   . LYS B 1 254 ? 23.713  -6.014  41.475  1.00 20.24 ? 301 LYS B O   1 
ATOM   4693 C  CB  . LYS B 1 254 ? 25.937  -3.530  41.733  1.00 16.39 ? 301 LYS B CB  1 
ATOM   4694 C  CG  . LYS B 1 254 ? 25.474  -3.350  40.289  1.00 15.46 ? 301 LYS B CG  1 
ATOM   4695 C  CD  . LYS B 1 254 ? 26.315  -2.340  39.541  1.00 15.88 ? 301 LYS B CD  1 
ATOM   4696 C  CE  . LYS B 1 254 ? 25.565  -1.902  38.322  1.00 15.37 ? 301 LYS B CE  1 
ATOM   4697 N  NZ  . LYS B 1 254 ? 26.425  -1.066  37.519  1.00 15.49 ? 301 LYS B NZ  1 
ATOM   4698 N  N   . GLY B 1 255 ? 25.542  -6.641  42.595  1.00 19.09 ? 302 GLY B N   1 
ATOM   4699 C  CA  . GLY B 1 255 ? 25.499  -8.033  42.141  1.00 20.10 ? 302 GLY B CA  1 
ATOM   4700 C  C   . GLY B 1 255 ? 24.255  -8.773  42.614  1.00 18.82 ? 302 GLY B C   1 
ATOM   4701 O  O   . GLY B 1 255 ? 23.458  -9.265  41.832  1.00 22.27 ? 302 GLY B O   1 
ATOM   4702 N  N   . GLU B 1 256 ? 24.055  -8.780  43.918  1.00 19.61 ? 303 GLU B N   1 
ATOM   4703 C  CA  . GLU B 1 256 ? 22.960  -9.518  44.511  1.00 19.07 ? 303 GLU B CA  1 
ATOM   4704 C  C   . GLU B 1 256 ? 21.747  -8.615  44.721  1.00 18.96 ? 303 GLU B C   1 
ATOM   4705 O  O   . GLU B 1 256 ? 20.628  -9.098  44.696  1.00 19.89 ? 303 GLU B O   1 
ATOM   4706 C  CB  . GLU B 1 256 ? 23.432  -10.146 45.819  1.00 22.79 ? 303 GLU B CB  1 
ATOM   4707 C  CG  . GLU B 1 256 ? 22.333  -10.821 46.629  1.00 24.04 ? 303 GLU B CG  1 
ATOM   4708 C  CD  . GLU B 1 256 ? 21.602  -11.989 46.009  1.00 25.18 ? 303 GLU B CD  1 
ATOM   4709 O  OE1 . GLU B 1 256 ? 22.100  -12.592 45.044  1.00 29.54 ? 303 GLU B OE1 1 
ATOM   4710 O  OE2 . GLU B 1 256 ? 20.481  -12.277 46.446  1.00 24.59 ? 303 GLU B OE2 1 
ATOM   4711 N  N   . GLY B 1 257 ? 21.960  -7.307  44.902  1.00 17.58 ? 304 GLY B N   1 
ATOM   4712 C  CA  . GLY B 1 257 ? 20.837  -6.434  45.193  1.00 15.76 ? 304 GLY B CA  1 
ATOM   4713 C  C   . GLY B 1 257 ? 20.380  -6.554  46.642  1.00 16.26 ? 304 GLY B C   1 
ATOM   4714 O  O   . GLY B 1 257 ? 19.252  -6.198  46.965  1.00 17.22 ? 304 GLY B O   1 
ATOM   4715 N  N   . ALA B 1 258 ? 21.267  -7.039  47.526  1.00 16.74 ? 305 ALA B N   1 
ATOM   4716 C  CA  . ALA B 1 258 ? 20.914  -7.077  48.925  1.00 17.15 ? 305 ALA B CA  1 
ATOM   4717 C  C   . ALA B 1 258 ? 21.091  -5.706  49.564  1.00 16.84 ? 305 ALA B C   1 
ATOM   4718 O  O   . ALA B 1 258 ? 21.966  -4.937  49.179  1.00 16.63 ? 305 ALA B O   1 
ATOM   4719 C  CB  . ALA B 1 258 ? 21.751  -8.106  49.661  1.00 18.95 ? 305 ALA B CB  1 
ATOM   4720 N  N   . PRO B 1 259 ? 20.288  -5.363  50.585  1.00 17.43 ? 306 PRO B N   1 
ATOM   4721 C  CA  . PRO B 1 259 ? 20.530  -4.136  51.337  1.00 17.68 ? 306 PRO B CA  1 
ATOM   4722 C  C   . PRO B 1 259 ? 21.901  -4.178  51.981  1.00 19.20 ? 306 PRO B C   1 
ATOM   4723 O  O   . PRO B 1 259 ? 22.392  -5.279  52.272  1.00 20.35 ? 306 PRO B O   1 
ATOM   4724 C  CB  . PRO B 1 259 ? 19.429  -4.127  52.392  1.00 18.29 ? 306 PRO B CB  1 
ATOM   4725 C  CG  . PRO B 1 259 ? 18.410  -5.132  51.940  1.00 21.09 ? 306 PRO B CG  1 
ATOM   4726 C  CD  . PRO B 1 259 ? 19.180  -6.161  51.132  1.00 17.79 ? 306 PRO B CD  1 
ATOM   4727 N  N   . VAL B 1 260 ? 22.496  -3.015  52.199  1.00 20.03 ? 307 VAL B N   1 
ATOM   4728 C  CA  . VAL B 1 260 ? 23.822  -2.997  52.769  1.00 22.47 ? 307 VAL B CA  1 
ATOM   4729 C  C   . VAL B 1 260 ? 23.758  -3.735  54.113  1.00 22.20 ? 307 VAL B C   1 
ATOM   4730 O  O   . VAL B 1 260 ? 22.830  -3.595  54.914  1.00 22.88 ? 307 VAL B O   1 
ATOM   4731 C  CB  . VAL B 1 260 ? 24.301  -1.538  52.837  1.00 28.59 ? 307 VAL B CB  1 
ATOM   4732 C  CG1 . VAL B 1 260 ? 23.389  -0.702  53.710  1.00 28.75 ? 307 VAL B CG1 1 
ATOM   4733 C  CG2 . VAL B 1 260 ? 25.760  -1.443  53.266  1.00 29.72 ? 307 VAL B CG2 1 
ATOM   4734 N  N   . GLY B 1 261 ? 24.755  -4.612  54.315  1.00 25.46 ? 308 GLY B N   1 
ATOM   4735 C  CA  . GLY B 1 261 ? 24.927  -5.328  55.569  1.00 26.31 ? 308 GLY B CA  1 
ATOM   4736 C  C   . GLY B 1 261 ? 24.116  -6.613  55.622  1.00 29.34 ? 308 GLY B C   1 
ATOM   4737 O  O   . GLY B 1 261 ? 24.142  -7.317  56.630  1.00 34.18 ? 308 GLY B O   1 
ATOM   4738 N  N   . LYS B 1 262 ? 23.411  -6.933  54.524  1.00 26.91 ? 309 LYS B N   1 
ATOM   4739 C  CA  . LYS B 1 262 ? 22.607  -8.143  54.441  1.00 24.28 ? 309 LYS B CA  1 
ATOM   4740 C  C   . LYS B 1 262 ? 23.174  -9.001  53.319  1.00 25.47 ? 309 LYS B C   1 
ATOM   4741 O  O   . LYS B 1 262 ? 24.035  -8.542  52.586  1.00 29.28 ? 309 LYS B O   1 
ATOM   4742 C  CB  . LYS B 1 262 ? 21.118  -7.838  54.253  1.00 26.38 ? 309 LYS B CB  1 
ATOM   4743 C  CG  . LYS B 1 262 ? 20.448  -6.954  55.286  1.00 31.03 ? 309 LYS B CG  1 
ATOM   4744 C  CD  . LYS B 1 262 ? 20.153  -7.654  56.605  1.00 33.57 ? 309 LYS B CD  1 
ATOM   4745 C  CE  . LYS B 1 262 ? 19.400  -6.776  57.562  1.00 38.75 ? 309 LYS B CE  1 
ATOM   4746 N  NZ  . LYS B 1 262 ? 19.406  -7.334  58.915  1.00 42.93 ? 309 LYS B NZ  1 
ATOM   4747 N  N   . ALA B 1 263 ? 22.669  -10.228 53.161  1.00 26.41 ? 310 ALA B N   1 
ATOM   4748 C  CA  . ALA B 1 263 ? 23.262  -11.219 52.282  1.00 28.52 ? 310 ALA B CA  1 
ATOM   4749 C  C   . ALA B 1 263 ? 22.452  -11.415 50.997  1.00 26.36 ? 310 ALA B C   1 
ATOM   4750 O  O   . ALA B 1 263 ? 23.019  -11.770 49.957  1.00 28.96 ? 310 ALA B O   1 
ATOM   4751 C  CB  . ALA B 1 263 ? 23.383  -12.535 53.051  1.00 29.43 ? 310 ALA B CB  1 
ATOM   4752 N  N   . LYS B 1 264 ? 21.116  -11.307 51.093  1.00 24.94 ? 311 LYS B N   1 
ATOM   4753 C  CA  . LYS B 1 264 ? 20.227  -11.713 50.022  1.00 24.79 ? 311 LYS B CA  1 
ATOM   4754 C  C   . LYS B 1 264 ? 19.336  -10.558 49.553  1.00 20.22 ? 311 LYS B C   1 
ATOM   4755 O  O   . LYS B 1 264 ? 18.928  -9.718  50.341  1.00 20.44 ? 311 LYS B O   1 
ATOM   4756 C  CB  . LYS B 1 264 ? 19.319  -12.860 50.470  1.00 28.48 ? 311 LYS B CB  1 
ATOM   4757 C  CG  . LYS B 1 264 ? 20.018  -14.166 50.805  1.00 36.46 ? 311 LYS B CG  1 
ATOM   4758 C  CD  . LYS B 1 264 ? 19.042  -15.180 51.392  1.00 46.14 ? 311 LYS B CD  1 
ATOM   4759 C  CE  . LYS B 1 264 ? 17.949  -15.629 50.463  1.00 51.84 ? 311 LYS B CE  1 
ATOM   4760 N  NZ  . LYS B 1 264 ? 18.448  -16.347 49.284  1.00 54.24 ? 311 LYS B NZ  1 
ATOM   4761 N  N   . GLU B 1 265 ? 18.996  -10.600 48.262  1.00 19.32 ? 312 GLU B N   1 
ATOM   4762 C  CA  . GLU B 1 265 ? 18.159  -9.568  47.652  1.00 18.64 ? 312 GLU B CA  1 
ATOM   4763 C  C   . GLU B 1 265 ? 16.956  -9.242  48.513  1.00 18.63 ? 312 GLU B C   1 
ATOM   4764 O  O   . GLU B 1 265 ? 16.623  -8.072  48.740  1.00 19.18 ? 312 GLU B O   1 
ATOM   4765 C  CB  . GLU B 1 265 ? 17.711  -10.059 46.283  1.00 19.19 ? 312 GLU B CB  1 
ATOM   4766 C  CG  . GLU B 1 265 ? 16.825  -9.042  45.567  1.00 20.54 ? 312 GLU B CG  1 
ATOM   4767 C  CD  . GLU B 1 265 ? 16.158  -9.540  44.312  1.00 19.58 ? 312 GLU B CD  1 
ATOM   4768 O  OE1 . GLU B 1 265 ? 16.557  -10.598 43.793  1.00 20.68 ? 312 GLU B OE1 1 
ATOM   4769 O  OE2 . GLU B 1 265 ? 15.232  -8.858  43.864  1.00 19.10 ? 312 GLU B OE2 1 
ATOM   4770 N  N   . ARG B 1 266 ? 16.252  -10.294 48.941  1.00 18.65 ? 313 ARG B N   1 
ATOM   4771 C  CA  . ARG B 1 266 ? 14.964  -10.120 49.588  1.00 20.59 ? 313 ARG B CA  1 
ATOM   4772 C  C   . ARG B 1 266 ? 15.096  -9.977  51.108  1.00 19.27 ? 313 ARG B C   1 
ATOM   4773 O  O   . ARG B 1 266 ? 14.070  -9.833  51.779  1.00 21.78 ? 313 ARG B O   1 
ATOM   4774 C  CB  . ARG B 1 266 ? 13.996  -11.232 49.166  1.00 22.20 ? 313 ARG B CB  1 
ATOM   4775 C  CG  . ARG B 1 266 ? 13.502  -10.959 47.747  1.00 24.72 ? 313 ARG B CG  1 
ATOM   4776 C  CD  . ARG B 1 266 ? 12.399  -11.888 47.284  1.00 30.72 ? 313 ARG B CD  1 
ATOM   4777 N  NE  . ARG B 1 266 ? 12.109  -11.700 45.858  1.00 38.62 ? 313 ARG B NE  1 
ATOM   4778 C  CZ  . ARG B 1 266 ? 11.490  -10.644 45.331  1.00 43.35 ? 313 ARG B CZ  1 
ATOM   4779 N  NH1 . ARG B 1 266 ? 10.778  -9.825  46.090  1.00 42.84 ? 313 ARG B NH1 1 
ATOM   4780 N  NH2 . ARG B 1 266 ? 11.551  -10.433 44.026  1.00 43.88 ? 313 ARG B NH2 1 
ATOM   4781 N  N   . ASP B 1 267 ? 16.314  -9.918  51.647  1.00 19.01 ? 314 ASP B N   1 
ATOM   4782 C  CA  . ASP B 1 267 ? 16.487  -9.564  53.055  1.00 22.16 ? 314 ASP B CA  1 
ATOM   4783 C  C   . ASP B 1 267 ? 15.910  -8.174  53.298  1.00 22.36 ? 314 ASP B C   1 
ATOM   4784 O  O   . ASP B 1 267 ? 16.037  -7.304  52.443  1.00 21.61 ? 314 ASP B O   1 
ATOM   4785 C  CB  . ASP B 1 267 ? 17.949  -9.600  53.471  1.00 22.45 ? 314 ASP B CB  1 
ATOM   4786 C  CG  . ASP B 1 267 ? 18.536  -10.993 53.627  1.00 26.48 ? 314 ASP B CG  1 
ATOM   4787 O  OD1 . ASP B 1 267 ? 17.737  -11.952 53.669  1.00 32.17 ? 314 ASP B OD1 1 
ATOM   4788 O  OD2 . ASP B 1 267 ? 19.769  -11.104 53.604  1.00 27.39 ? 314 ASP B OD2 1 
ATOM   4789 N  N   . GLU B 1 268 ? 15.232  -7.964  54.424  1.00 23.87 ? 315 GLU B N   1 
ATOM   4790 C  CA  . GLU B 1 268 ? 14.602  -6.674  54.677  1.00 23.66 ? 315 GLU B CA  1 
ATOM   4791 C  C   . GLU B 1 268 ? 15.693  -5.651  54.985  1.00 22.50 ? 315 GLU B C   1 
ATOM   4792 O  O   . GLU B 1 268 ? 16.694  -5.938  55.648  1.00 23.20 ? 315 GLU B O   1 
ATOM   4793 C  CB  . GLU B 1 268 ? 13.469  -6.762  55.709  1.00 29.91 ? 315 GLU B CB  1 
ATOM   4794 C  CG  . GLU B 1 268 ? 12.204  -7.438  55.169  1.00 30.95 ? 315 GLU B CG  1 
ATOM   4795 C  CD  . GLU B 1 268 ? 11.491  -6.743  54.004  1.00 35.60 ? 315 GLU B CD  1 
ATOM   4796 O  OE1 . GLU B 1 268 ? 11.571  -5.508  53.885  1.00 34.30 ? 315 GLU B OE1 1 
ATOM   4797 O  OE2 . GLU B 1 268 ? 10.858  -7.438  53.191  1.00 39.76 ? 315 GLU B OE2 1 
ATOM   4798 N  N   . PRO B 1 269 ? 15.580  -4.432  54.428  1.00 21.28 ? 316 PRO B N   1 
ATOM   4799 C  CA  . PRO B 1 269 ? 16.611  -3.425  54.625  1.00 21.12 ? 316 PRO B CA  1 
ATOM   4800 C  C   . PRO B 1 269 ? 16.665  -2.951  56.071  1.00 21.95 ? 316 PRO B C   1 
ATOM   4801 O  O   . PRO B 1 269 ? 15.660  -2.893  56.778  1.00 23.77 ? 316 PRO B O   1 
ATOM   4802 C  CB  . PRO B 1 269 ? 16.236  -2.281  53.694  1.00 23.91 ? 316 PRO B CB  1 
ATOM   4803 C  CG  . PRO B 1 269 ? 14.865  -2.568  53.223  1.00 25.02 ? 316 PRO B CG  1 
ATOM   4804 C  CD  . PRO B 1 269 ? 14.493  -3.993  53.532  1.00 21.45 ? 316 PRO B CD  1 
ATOM   4805 N  N   . PHE B 1 270 ? 17.884  -2.651  56.497  1.00 20.96 ? 317 PHE B N   1 
ATOM   4806 C  CA  . PHE B 1 270 ? 18.129  -1.910  57.719  1.00 19.91 ? 317 PHE B CA  1 
ATOM   4807 C  C   . PHE B 1 270 ? 18.506  -0.502  57.279  1.00 16.80 ? 317 PHE B C   1 
ATOM   4808 O  O   . PHE B 1 270 ? 19.623  -0.271  56.820  1.00 18.45 ? 317 PHE B O   1 
ATOM   4809 C  CB  . PHE B 1 270 ? 19.226  -2.624  58.513  1.00 21.59 ? 317 PHE B CB  1 
ATOM   4810 C  CG  . PHE B 1 270 ? 19.663  -1.891  59.765  1.00 27.18 ? 317 PHE B CG  1 
ATOM   4811 C  CD1 . PHE B 1 270 ? 18.728  -1.236  60.569  1.00 33.28 ? 317 PHE B CD1 1 
ATOM   4812 C  CD2 . PHE B 1 270 ? 20.997  -1.835  60.128  1.00 33.24 ? 317 PHE B CD2 1 
ATOM   4813 C  CE1 . PHE B 1 270 ? 19.134  -0.569  61.717  1.00 35.19 ? 317 PHE B CE1 1 
ATOM   4814 C  CE2 . PHE B 1 270 ? 21.396  -1.165  61.282  1.00 33.93 ? 317 PHE B CE2 1 
ATOM   4815 C  CZ  . PHE B 1 270 ? 20.465  -0.527  62.064  1.00 37.25 ? 317 PHE B CZ  1 
ATOM   4816 N  N   . LEU B 1 271 ? 17.564  0.420   57.373  1.00 18.10 ? 318 LEU B N   1 
ATOM   4817 C  CA  . LEU B 1 271 ? 17.740  1.715   56.745  1.00 19.45 ? 318 LEU B CA  1 
ATOM   4818 C  C   . LEU B 1 271 ? 18.888  2.509   57.365  1.00 21.60 ? 318 LEU B C   1 
ATOM   4819 O  O   . LEU B 1 271 ? 19.527  3.294   56.661  1.00 20.88 ? 318 LEU B O   1 
ATOM   4820 C  CB  . LEU B 1 271 ? 16.440  2.505   56.829  1.00 22.13 ? 318 LEU B CB  1 
ATOM   4821 C  CG  . LEU B 1 271 ? 15.234  1.883   56.121  1.00 23.36 ? 318 LEU B CG  1 
ATOM   4822 C  CD1 . LEU B 1 271 ? 14.087  2.862   56.212  1.00 29.25 ? 318 LEU B CD1 1 
ATOM   4823 C  CD2 . LEU B 1 271 ? 15.585  1.541   54.689  1.00 24.70 ? 318 LEU B CD2 1 
ATOM   4824 N  N   . LYS B 1 272 ? 19.189  2.311   58.667  1.00 22.00 ? 319 LYS B N   1 
ATOM   4825 C  CA  . LYS B 1 272 ? 20.205  3.162   59.272  1.00 24.46 ? 319 LYS B CA  1 
ATOM   4826 C  C   . LYS B 1 272 ? 21.606  2.801   58.793  1.00 22.88 ? 319 LYS B C   1 
ATOM   4827 O  O   . LYS B 1 272 ? 22.514  3.613   58.943  1.00 24.98 ? 319 LYS B O   1 
ATOM   4828 C  CB  . LYS B 1 272 ? 20.130  3.166   60.804  1.00 30.66 ? 319 LYS B CB  1 
ATOM   4829 C  CG  . LYS B 1 272 ? 19.370  4.380   61.378  1.00 40.66 ? 319 LYS B CG  1 
ATOM   4830 C  CD  . LYS B 1 272 ? 20.228  5.526   61.930  1.00 49.86 ? 319 LYS B CD  1 
ATOM   4831 C  CE  . LYS B 1 272 ? 20.678  6.640   61.004  1.00 52.88 ? 319 LYS B CE  1 
ATOM   4832 N  NZ  . LYS B 1 272 ? 21.784  6.301   60.094  1.00 53.70 ? 319 LYS B NZ  1 
ATOM   4833 N  N   . ALA B 1 273 ? 21.775  1.654   58.135  1.00 21.23 ? 320 ALA B N   1 
ATOM   4834 C  CA  . ALA B 1 273 ? 23.067  1.250   57.617  1.00 20.75 ? 320 ALA B CA  1 
ATOM   4835 C  C   . ALA B 1 273 ? 23.340  1.930   56.283  1.00 20.36 ? 320 ALA B C   1 
ATOM   4836 O  O   . ALA B 1 273 ? 24.463  1.923   55.817  1.00 22.06 ? 320 ALA B O   1 
ATOM   4837 C  CB  . ALA B 1 273 ? 23.158  -0.244  57.465  1.00 22.32 ? 320 ALA B CB  1 
ATOM   4838 N  N   . MET B 1 274 ? 22.285  2.450   55.639  1.00 18.24 ? 321 MET B N   1 
ATOM   4839 C  CA  . MET B 1 274 ? 22.438  3.136   54.371  1.00 17.49 ? 321 MET B CA  1 
ATOM   4840 C  C   . MET B 1 274 ? 22.769  4.599   54.588  1.00 17.21 ? 321 MET B C   1 
ATOM   4841 O  O   . MET B 1 274 ? 22.449  5.166   55.624  1.00 18.60 ? 321 MET B O   1 
ATOM   4842 C  CB  . MET B 1 274 ? 21.137  3.100   53.566  1.00 18.07 ? 321 MET B CB  1 
ATOM   4843 C  CG  . MET B 1 274 ? 20.639  1.718   53.337  1.00 17.10 ? 321 MET B CG  1 
ATOM   4844 S  SD  . MET B 1 274 ? 19.045  1.723   52.497  1.00 18.40 ? 321 MET B SD  1 
ATOM   4845 C  CE  . MET B 1 274 ? 18.721  -0.040  52.425  1.00 18.55 ? 321 MET B CE  1 
ATOM   4846 N  N   . LYS B 1 275 ? 23.410  5.228   53.612  1.00 17.52 ? 322 LYS B N   1 
ATOM   4847 C  CA  . LYS B 1 275 ? 23.669  6.659   53.672  1.00 18.53 ? 322 LYS B CA  1 
ATOM   4848 C  C   . LYS B 1 275 ? 22.351  7.425   53.750  1.00 16.44 ? 322 LYS B C   1 
ATOM   4849 O  O   . LYS B 1 275 ? 21.314  6.971   53.232  1.00 16.21 ? 322 LYS B O   1 
ATOM   4850 C  CB  . LYS B 1 275 ? 24.524  7.068   52.472  1.00 23.04 ? 322 LYS B CB  1 
ATOM   4851 C  CG  . LYS B 1 275 ? 25.971  6.582   52.605  1.00 29.25 ? 322 LYS B CG  1 
ATOM   4852 C  CD  . LYS B 1 275 ? 26.943  7.192   51.603  1.00 34.75 ? 322 LYS B CD  1 
ATOM   4853 C  CE  . LYS B 1 275 ? 28.356  7.219   52.113  1.00 40.38 ? 322 LYS B CE  1 
ATOM   4854 N  NZ  . LYS B 1 275 ? 28.758  5.946   52.716  1.00 46.72 ? 322 LYS B NZ  1 
ATOM   4855 N  N   . PRO B 1 276 ? 22.300  8.573   54.433  1.00 16.94 ? 323 PRO B N   1 
ATOM   4856 C  CA  . PRO B 1 276 ? 21.041  9.266   54.659  1.00 16.72 ? 323 PRO B CA  1 
ATOM   4857 C  C   . PRO B 1 276 ? 20.272  9.637   53.400  1.00 15.06 ? 323 PRO B C   1 
ATOM   4858 O  O   . PRO B 1 276 ? 19.058  9.723   53.439  1.00 18.84 ? 323 PRO B O   1 
ATOM   4859 C  CB  . PRO B 1 276 ? 21.468  10.544  55.450  1.00 19.05 ? 323 PRO B CB  1 
ATOM   4860 C  CG  . PRO B 1 276 ? 22.719  10.131  56.131  1.00 20.52 ? 323 PRO B CG  1 
ATOM   4861 C  CD  . PRO B 1 276 ? 23.407  9.112   55.271  1.00 19.55 ? 323 PRO B CD  1 
ATOM   4862 N  N   . ASP B 1 277 ? 20.981  9.912   52.307  1.00 14.78 ? 324 ASP B N   1 
ATOM   4863 C  CA  . ASP B 1 277 ? 20.386  10.313  51.043  1.00 14.06 ? 324 ASP B CA  1 
ATOM   4864 C  C   . ASP B 1 277 ? 20.377  9.161   50.038  1.00 13.58 ? 324 ASP B C   1 
ATOM   4865 O  O   . ASP B 1 277 ? 20.157  9.384   48.844  1.00 14.61 ? 324 ASP B O   1 
ATOM   4866 C  CB  . ASP B 1 277 ? 21.004  11.604  50.565  1.00 16.51 ? 324 ASP B CB  1 
ATOM   4867 C  CG  . ASP B 1 277 ? 20.625  12.806  51.401  1.00 20.94 ? 324 ASP B CG  1 
ATOM   4868 O  OD1 . ASP B 1 277 ? 19.450  12.920  51.802  1.00 20.03 ? 324 ASP B OD1 1 
ATOM   4869 O  OD2 . ASP B 1 277 ? 21.550  13.622  51.631  1.00 26.37 ? 324 ASP B OD2 1 
ATOM   4870 N  N   . ALA B 1 278 ? 20.587  7.925   50.466  1.00 13.37 ? 325 ALA B N   1 
ATOM   4871 C  CA  . ALA B 1 278 ? 20.424  6.771   49.593  1.00 12.70 ? 325 ALA B CA  1 
ATOM   4872 C  C   . ALA B 1 278 ? 18.980  6.633   49.149  1.00 12.61 ? 325 ALA B C   1 
ATOM   4873 O  O   . ALA B 1 278 ? 18.039  6.853   49.871  1.00 13.23 ? 325 ALA B O   1 
ATOM   4874 C  CB  . ALA B 1 278 ? 20.832  5.476   50.248  1.00 14.40 ? 325 ALA B CB  1 
ATOM   4875 N  N   . HIS B 1 279 ? 18.821  6.270   47.878  1.00 11.94 ? 326 HIS B N   1 
ATOM   4876 C  CA  . HIS B 1 279 ? 17.499  6.213   47.276  1.00 11.78 ? 326 HIS B CA  1 
ATOM   4877 C  C   . HIS B 1 279 ? 16.535  5.284   48.032  1.00 12.51 ? 326 HIS B C   1 
ATOM   4878 O  O   . HIS B 1 279 ? 15.420  5.680   48.282  1.00 12.66 ? 326 HIS B O   1 
ATOM   4879 C  CB  . HIS B 1 279 ? 17.661  5.729   45.831  1.00 11.75 ? 326 HIS B CB  1 
ATOM   4880 C  CG  . HIS B 1 279 ? 16.378  5.620   45.075  1.00 11.30 ? 326 HIS B CG  1 
ATOM   4881 N  ND1 . HIS B 1 279 ? 15.711  6.714   44.640  1.00 12.42 ? 326 HIS B ND1 1 
ATOM   4882 C  CD2 . HIS B 1 279 ? 15.637  4.543   44.718  1.00 11.42 ? 326 HIS B CD2 1 
ATOM   4883 C  CE1 . HIS B 1 279 ? 14.589  6.348   44.032  1.00 11.37 ? 326 HIS B CE1 1 
ATOM   4884 N  NE2 . HIS B 1 279 ? 14.528  5.001   44.041  1.00 10.54 ? 326 HIS B NE2 1 
ATOM   4885 N  N   . VAL B 1 280 ? 16.989  4.080   48.375  1.00 11.56 ? 327 VAL B N   1 
ATOM   4886 C  CA  . VAL B 1 280 ? 16.060  3.177   49.044  1.00 12.93 ? 327 VAL B CA  1 
ATOM   4887 C  C   . VAL B 1 280 ? 15.645  3.742   50.394  1.00 13.67 ? 327 VAL B C   1 
ATOM   4888 O  O   . VAL B 1 280 ? 14.505  3.602   50.807  1.00 15.55 ? 327 VAL B O   1 
ATOM   4889 C  CB  . VAL B 1 280 ? 16.668  1.779   49.193  1.00 14.04 ? 327 VAL B CB  1 
ATOM   4890 C  CG1 . VAL B 1 280 ? 15.848  0.905   50.123  1.00 15.15 ? 327 VAL B CG1 1 
ATOM   4891 C  CG2 . VAL B 1 280 ? 16.797  1.130   47.816  1.00 15.07 ? 327 VAL B CG2 1 
ATOM   4892 N  N   . ARG B 1 281 ? 16.602  4.351   51.114  1.00 13.40 ? 328 ARG B N   1 
ATOM   4893 C  CA  . ARG B 1 281 ? 16.275  4.911   52.402  1.00 14.72 ? 328 ARG B CA  1 
ATOM   4894 C  C   . ARG B 1 281 ? 15.234  6.029   52.292  1.00 13.67 ? 328 ARG B C   1 
ATOM   4895 O  O   . ARG B 1 281 ? 14.298  6.080   53.091  1.00 16.18 ? 328 ARG B O   1 
ATOM   4896 C  CB  . ARG B 1 281 ? 17.583  5.388   53.046  1.00 14.64 ? 328 ARG B CB  1 
ATOM   4897 C  CG  . ARG B 1 281 ? 17.328  5.990   54.419  1.00 17.99 ? 328 ARG B CG  1 
ATOM   4898 C  CD  . ARG B 1 281 ? 18.636  6.108   55.206  1.00 19.61 ? 328 ARG B CD  1 
ATOM   4899 N  NE  . ARG B 1 281 ? 18.364  6.807   56.463  1.00 22.98 ? 328 ARG B NE  1 
ATOM   4900 C  CZ  . ARG B 1 281 ? 19.299  7.046   57.356  1.00 25.23 ? 328 ARG B CZ  1 
ATOM   4901 N  NH1 . ARG B 1 281 ? 20.501  6.583   57.165  1.00 22.71 ? 328 ARG B NH1 1 
ATOM   4902 N  NH2 . ARG B 1 281 ? 19.037  7.804   58.411  1.00 29.32 ? 328 ARG B NH2 1 
ATOM   4903 N  N   . LEU B 1 282 ? 15.352  6.898   51.297  1.00 13.00 ? 329 LEU B N   1 
ATOM   4904 C  CA  . LEU B 1 282 ? 14.421  7.986   51.112  1.00 12.23 ? 329 LEU B CA  1 
ATOM   4905 C  C   . LEU B 1 282 ? 13.054  7.544   50.618  1.00 13.07 ? 329 LEU B C   1 
ATOM   4906 O  O   . LEU B 1 282 ? 12.048  8.176   50.931  1.00 14.01 ? 329 LEU B O   1 
ATOM   4907 C  CB  . LEU B 1 282 ? 14.967  9.074   50.214  1.00 12.79 ? 329 LEU B CB  1 
ATOM   4908 C  CG  . LEU B 1 282 ? 16.214  9.790   50.773  1.00 13.77 ? 329 LEU B CG  1 
ATOM   4909 C  CD1 . LEU B 1 282 ? 16.794  10.677  49.720  1.00 14.40 ? 329 LEU B CD1 1 
ATOM   4910 C  CD2 . LEU B 1 282 ? 15.857  10.563  52.009  1.00 15.33 ? 329 LEU B CD2 1 
ATOM   4911 N  N   . ALA B 1 283 ? 13.029  6.461   49.831  1.00 12.68 ? 330 ALA B N   1 
ATOM   4912 C  CA  . ALA B 1 283 ? 11.807  6.022   49.169  1.00 12.85 ? 330 ALA B CA  1 
ATOM   4913 C  C   . ALA B 1 283 ? 10.994  5.038   50.003  1.00 13.15 ? 330 ALA B C   1 
ATOM   4914 O  O   . ALA B 1 283 ? 9.835   4.794   49.685  1.00 14.40 ? 330 ALA B O   1 
ATOM   4915 C  CB  . ALA B 1 283 ? 12.137  5.434   47.843  1.00 14.20 ? 330 ALA B CB  1 
ATOM   4916 N  N   . HIS B 1 284 ? 11.608  4.449   51.018  1.00 13.16 ? 331 HIS B N   1 
ATOM   4917 C  CA  . HIS B 1 284 ? 10.994  3.368   51.777  1.00 12.93 ? 331 HIS B CA  1 
ATOM   4918 C  C   . HIS B 1 284 ? 9.753   3.886   52.475  1.00 14.45 ? 331 HIS B C   1 
ATOM   4919 O  O   . HIS B 1 284 ? 9.727   5.027   52.969  1.00 13.60 ? 331 HIS B O   1 
ATOM   4920 C  CB  . HIS B 1 284 ? 12.007  2.852   52.791  1.00 14.37 ? 331 HIS B CB  1 
ATOM   4921 C  CG  . HIS B 1 284 ? 11.643  1.583   53.455  1.00 14.62 ? 331 HIS B CG  1 
ATOM   4922 N  ND1 . HIS B 1 284 ? 10.718  1.524   54.489  1.00 16.76 ? 331 HIS B ND1 1 
ATOM   4923 C  CD2 . HIS B 1 284 ? 12.075  0.324   53.213  1.00 17.05 ? 331 HIS B CD2 1 
ATOM   4924 C  CE1 . HIS B 1 284 ? 10.674  0.262   54.890  1.00 17.79 ? 331 HIS B CE1 1 
ATOM   4925 N  NE2 . HIS B 1 284 ? 11.434  -0.496  54.124  1.00 17.15 ? 331 HIS B NE2 1 
ATOM   4926 N  N   . PRO B 1 285 ? 8.688   3.086   52.594  1.00 14.31 ? 332 PRO B N   1 
ATOM   4927 C  CA  . PRO B 1 285 ? 7.505   3.518   53.306  1.00 14.26 ? 332 PRO B CA  1 
ATOM   4928 C  C   . PRO B 1 285 ? 7.765   4.065   54.710  1.00 15.68 ? 332 PRO B C   1 
ATOM   4929 O  O   . PRO B 1 285 ? 7.091   5.035   55.094  1.00 16.67 ? 332 PRO B O   1 
ATOM   4930 C  CB  . PRO B 1 285 ? 6.612   2.300   53.337  1.00 15.00 ? 332 PRO B CB  1 
ATOM   4931 C  CG  . PRO B 1 285 ? 7.023   1.482   52.141  1.00 16.91 ? 332 PRO B CG  1 
ATOM   4932 C  CD  . PRO B 1 285 ? 8.501   1.768   51.951  1.00 15.26 ? 332 PRO B CD  1 
ATOM   4933 N  N   . ASP B 1 286 ? 8.751   3.476   55.413  1.00 16.26 ? 333 ASP B N   1 
ATOM   4934 C  CA  . ASP B 1 286 ? 9.014   3.871   56.793  1.00 18.84 ? 333 ASP B CA  1 
ATOM   4935 C  C   . ASP B 1 286 ? 9.515   5.303   56.845  1.00 18.08 ? 333 ASP B C   1 
ATOM   4936 O  O   . ASP B 1 286 ? 9.453   5.945   57.901  1.00 21.49 ? 333 ASP B O   1 
ATOM   4937 C  CB  . ASP B 1 286 ? 9.993   2.939   57.489  1.00 20.87 ? 333 ASP B CB  1 
ATOM   4938 C  CG  . ASP B 1 286 ? 9.480   1.555   57.832  1.00 23.86 ? 333 ASP B CG  1 
ATOM   4939 O  OD1 . ASP B 1 286 ? 8.295   1.270   57.567  1.00 26.76 ? 333 ASP B OD1 1 
ATOM   4940 O  OD2 . ASP B 1 286 ? 10.312  0.765   58.347  1.00 30.12 ? 333 ASP B OD2 1 
ATOM   4941 N  N   . SER B 1 287 ? 10.095  5.814   55.765  1.00 16.33 ? 334 SER B N   1 
ATOM   4942 C  CA  . SER B 1 287 ? 10.577  7.182   55.690  1.00 16.03 ? 334 SER B CA  1 
ATOM   4943 C  C   . SER B 1 287 ? 9.512   8.161   55.219  1.00 15.93 ? 334 SER B C   1 
ATOM   4944 O  O   . SER B 1 287 ? 9.742   9.361   55.140  1.00 19.66 ? 334 SER B O   1 
ATOM   4945 C  CB  . SER B 1 287 ? 11.750  7.268   54.750  1.00 16.68 ? 334 SER B CB  1 
ATOM   4946 O  OG  . SER B 1 287 ? 12.844  6.489   55.188  1.00 19.77 ? 334 SER B OG  1 
ATOM   4947 N  N   . ASN B 1 288 ? 8.342   7.648   54.861  1.00 16.53 ? 335 ASN B N   1 
ATOM   4948 C  CA  . ASN B 1 288 ? 7.288   8.411   54.248  1.00 16.25 ? 335 ASN B CA  1 
ATOM   4949 C  C   . ASN B 1 288 ? 5.946   8.181   54.922  1.00 17.68 ? 335 ASN B C   1 
ATOM   4950 O  O   . ASN B 1 288 ? 4.913   8.273   54.242  1.00 18.32 ? 335 ASN B O   1 
ATOM   4951 C  CB  . ASN B 1 288 ? 7.173   8.081   52.769  1.00 16.60 ? 335 ASN B CB  1 
ATOM   4952 C  CG  . ASN B 1 288 ? 8.375   8.565   52.011  1.00 15.61 ? 335 ASN B CG  1 
ATOM   4953 O  OD1 . ASN B 1 288 ? 8.548   9.770   51.746  1.00 17.74 ? 335 ASN B OD1 1 
ATOM   4954 N  ND2 . ASN B 1 288 ? 9.261   7.640   51.701  1.00 17.06 ? 335 ASN B ND2 1 
ATOM   4955 N  N   . GLY B 1 289 ? 5.952   7.921   56.234  1.00 18.25 ? 336 GLY B N   1 
ATOM   4956 C  CA  . GLY B 1 289 ? 4.682   7.826   56.926  1.00 19.87 ? 336 GLY B CA  1 
ATOM   4957 C  C   . GLY B 1 289 ? 3.851   6.639   56.464  1.00 20.79 ? 336 GLY B C   1 
ATOM   4958 O  O   . GLY B 1 289 ? 2.628   6.607   56.656  1.00 23.26 ? 336 GLY B O   1 
ATOM   4959 N  N   . GLY B 1 290 ? 4.500   5.636   55.873  1.00 18.55 ? 337 GLY B N   1 
ATOM   4960 C  CA  . GLY B 1 290 ? 3.822   4.418   55.445  1.00 18.05 ? 337 GLY B CA  1 
ATOM   4961 C  C   . GLY B 1 290 ? 3.425   4.453   53.966  1.00 17.12 ? 337 GLY B C   1 
ATOM   4962 O  O   . GLY B 1 290 ? 2.844   3.474   53.492  1.00 18.07 ? 337 GLY B O   1 
ATOM   4963 N  N   . ALA B 1 291 ? 3.677   5.549   53.257  1.00 16.07 ? 338 ALA B N   1 
ATOM   4964 C  CA  . ALA B 1 291 ? 3.256   5.687   51.868  1.00 15.67 ? 338 ALA B CA  1 
ATOM   4965 C  C   . ALA B 1 291 ? 3.905   4.597   51.033  1.00 15.37 ? 338 ALA B C   1 
ATOM   4966 O  O   . ALA B 1 291 ? 5.107   4.411   51.100  1.00 15.62 ? 338 ALA B O   1 
ATOM   4967 C  CB  . ALA B 1 291 ? 3.618   7.027   51.351  1.00 16.35 ? 338 ALA B CB  1 
ATOM   4968 N  N   . THR B 1 292 ? 3.077   3.860   50.268  1.00 15.11 ? 339 THR B N   1 
ATOM   4969 C  CA  . THR B 1 292 ? 3.506   2.681   49.515  1.00 14.33 ? 339 THR B CA  1 
ATOM   4970 C  C   . THR B 1 292 ? 2.879   2.737   48.131  1.00 15.32 ? 339 THR B C   1 
ATOM   4971 O  O   . THR B 1 292 ? 1.721   3.118   48.029  1.00 18.93 ? 339 THR B O   1 
ATOM   4972 C  CB  . THR B 1 292 ? 3.038   1.419   50.227  1.00 16.33 ? 339 THR B CB  1 
ATOM   4973 O  OG1 . THR B 1 292 ? 3.519   1.458   51.568  1.00 17.30 ? 339 THR B OG1 1 
ATOM   4974 C  CG2 . THR B 1 292 ? 3.592   0.159   49.619  1.00 18.07 ? 339 THR B CG2 1 
ATOM   4975 N  N   . LEU B 1 293 ? 3.662   2.377   47.102  1.00 14.43 ? 340 LEU B N   1 
ATOM   4976 C  CA  . LEU B 1 293 ? 3.285   2.522   45.705  1.00 15.19 ? 340 LEU B CA  1 
ATOM   4977 C  C   . LEU B 1 293 ? 3.298   1.181   45.030  1.00 13.06 ? 340 LEU B C   1 
ATOM   4978 O  O   . LEU B 1 293 ? 4.091   0.347   45.382  1.00 14.50 ? 340 LEU B O   1 
ATOM   4979 C  CB  . LEU B 1 293 ? 4.344   3.342   44.976  1.00 16.65 ? 340 LEU B CB  1 
ATOM   4980 C  CG  . LEU B 1 293 ? 4.581   4.752   45.498  1.00 19.60 ? 340 LEU B CG  1 
ATOM   4981 C  CD1 . LEU B 1 293 ? 5.715   5.513   44.773  1.00 20.85 ? 340 LEU B CD1 1 
ATOM   4982 C  CD2 . LEU B 1 293 ? 3.339   5.587   45.445  1.00 24.06 ? 340 LEU B CD2 1 
ATOM   4983 N  N   . LEU B 1 294 ? 2.494   1.041   43.983  1.00 11.87 ? 341 LEU B N   1 
ATOM   4984 C  CA  . LEU B 1 294 ? 2.677   -0.032  43.010  1.00 11.50 ? 341 LEU B CA  1 
ATOM   4985 C  C   . LEU B 1 294 ? 3.455   0.555   41.846  1.00 11.20 ? 341 LEU B C   1 
ATOM   4986 O  O   . LEU B 1 294 ? 2.908   1.335   41.075  1.00 12.35 ? 341 LEU B O   1 
ATOM   4987 C  CB  . LEU B 1 294 ? 1.336   -0.627  42.593  1.00 12.85 ? 341 LEU B CB  1 
ATOM   4988 C  CG  . LEU B 1 294 ? 1.427   -1.834  41.660  1.00 15.74 ? 341 LEU B CG  1 
ATOM   4989 C  CD1 . LEU B 1 294 ? 0.067   -2.533  41.689  1.00 22.08 ? 341 LEU B CD1 1 
ATOM   4990 C  CD2 . LEU B 1 294 ? 1.782   -1.555  40.264  1.00 21.12 ? 341 LEU B CD2 1 
ATOM   4991 N  N   . ARG B 1 295 ? 4.711   0.172   41.710  1.00 10.95 ? 342 ARG B N   1 
ATOM   4992 C  CA  . ARG B 1 295 ? 5.531   0.546   40.571  1.00 10.66 ? 342 ARG B CA  1 
ATOM   4993 C  C   . ARG B 1 295 ? 5.344   -0.459  39.447  1.00 11.25 ? 342 ARG B C   1 
ATOM   4994 O  O   . ARG B 1 295 ? 5.334   -1.658  39.688  1.00 12.87 ? 342 ARG B O   1 
ATOM   4995 C  CB  . ARG B 1 295 ? 7.003   0.583   40.967  1.00 10.90 ? 342 ARG B CB  1 
ATOM   4996 C  CG  . ARG B 1 295 ? 7.255   1.749   41.908  1.00 12.11 ? 342 ARG B CG  1 
ATOM   4997 C  CD  . ARG B 1 295 ? 8.699   1.777   42.371  1.00 12.63 ? 342 ARG B CD  1 
ATOM   4998 N  NE  . ARG B 1 295 ? 8.953   0.685   43.313  1.00 12.54 ? 342 ARG B NE  1 
ATOM   4999 C  CZ  . ARG B 1 295 ? 10.046  -0.042  43.394  1.00 13.51 ? 342 ARG B CZ  1 
ATOM   5000 N  NH1 . ARG B 1 295 ? 11.030  0.108   42.561  1.00 13.35 ? 342 ARG B NH1 1 
ATOM   5001 N  NH2 . ARG B 1 295 ? 10.189  -0.984  44.337  1.00 14.03 ? 342 ARG B NH2 1 
ATOM   5002 N  N   . ARG B 1 296 ? 5.152   0.045   38.242  1.00 10.72 ? 343 ARG B N   1 
ATOM   5003 C  CA  . ARG B 1 296 ? 4.917   -0.818  37.087  1.00 10.69 ? 343 ARG B CA  1 
ATOM   5004 C  C   . ARG B 1 296 ? 5.544   -0.196  35.862  1.00 11.52 ? 343 ARG B C   1 
ATOM   5005 O  O   . ARG B 1 296 ? 4.986   -0.228  34.793  1.00 12.17 ? 343 ARG B O   1 
ATOM   5006 C  CB  . ARG B 1 296 ? 3.414   -1.073  36.937  1.00 11.35 ? 343 ARG B CB  1 
ATOM   5007 C  CG  . ARG B 1 296 ? 3.113   -2.423  36.306  1.00 10.95 ? 343 ARG B CG  1 
ATOM   5008 C  CD  . ARG B 1 296 ? 1.642   -2.629  36.110  1.00 11.44 ? 343 ARG B CD  1 
ATOM   5009 N  NE  . ARG B 1 296 ? 1.278   -3.980  35.680  1.00 10.87 ? 343 ARG B NE  1 
ATOM   5010 C  CZ  . ARG B 1 296 ? 1.261   -4.402  34.436  1.00 11.54 ? 343 ARG B CZ  1 
ATOM   5011 N  NH1 . ARG B 1 296 ? 1.675   -3.611  33.469  1.00 11.97 ? 343 ARG B NH1 1 
ATOM   5012 N  NH2 . ARG B 1 296 ? 0.826   -5.612  34.142  1.00 12.43 ? 343 ARG B NH2 1 
ATOM   5013 N  N   . GLY B 1 297 ? 6.753   0.340   35.995  1.00 11.75 ? 344 GLY B N   1 
ATOM   5014 C  CA  . GLY B 1 297 ? 7.467   1.019   34.957  1.00 12.24 ? 344 GLY B CA  1 
ATOM   5015 C  C   . GLY B 1 297 ? 8.286   0.094   34.076  1.00 11.46 ? 344 GLY B C   1 
ATOM   5016 O  O   . GLY B 1 297 ? 8.439   -1.100  34.321  1.00 13.25 ? 344 GLY B O   1 
ATOM   5017 N  N   . TYR B 1 298 ? 8.803   0.730   33.032  1.00 10.60 ? 345 TYR B N   1 
ATOM   5018 C  CA  . TYR B 1 298 ? 9.535   0.026   32.002  1.00 10.89 ? 345 TYR B CA  1 
ATOM   5019 C  C   . TYR B 1 298 ? 10.738  0.850   31.657  1.00 11.86 ? 345 TYR B C   1 
ATOM   5020 O  O   . TYR B 1 298 ? 10.711  2.090   31.690  1.00 12.70 ? 345 TYR B O   1 
ATOM   5021 C  CB  . TYR B 1 298 ? 8.668   -0.128  30.746  1.00 10.96 ? 345 TYR B CB  1 
ATOM   5022 C  CG  . TYR B 1 298 ? 7.623   -1.197  30.879  1.00 11.32 ? 345 TYR B CG  1 
ATOM   5023 C  CD1 . TYR B 1 298 ? 6.436   -0.994  31.568  1.00 11.09 ? 345 TYR B CD1 1 
ATOM   5024 C  CD2 . TYR B 1 298 ? 7.800   -2.448  30.290  1.00 12.31 ? 345 TYR B CD2 1 
ATOM   5025 C  CE1 . TYR B 1 298 ? 5.505   -2.004  31.683  1.00 11.12 ? 345 TYR B CE1 1 
ATOM   5026 C  CE2 . TYR B 1 298 ? 6.879   -3.459  30.417  1.00 12.39 ? 345 TYR B CE2 1 
ATOM   5027 C  CZ  . TYR B 1 298 ? 5.707   -3.234  31.110  1.00 11.78 ? 345 TYR B CZ  1 
ATOM   5028 O  OH  . TYR B 1 298 ? 4.767   -4.218  31.283  1.00 13.80 ? 345 TYR B OH  1 
ATOM   5029 N  N   . SER B 1 299 ? 11.790  0.151   31.268  1.00 12.11 ? 346 SER B N   1 
ATOM   5030 C  CA  . SER B 1 299 ? 12.942  0.850   30.742  1.00 11.52 ? 346 SER B CA  1 
ATOM   5031 C  C   . SER B 1 299 ? 12.669  1.374   29.356  1.00 13.02 ? 346 SER B C   1 
ATOM   5032 O  O   . SER B 1 299 ? 11.831  0.814   28.628  1.00 13.40 ? 346 SER B O   1 
ATOM   5033 C  CB  . SER B 1 299 ? 14.121  -0.078  30.681  1.00 13.52 ? 346 SER B CB  1 
ATOM   5034 O  OG  . SER B 1 299 ? 14.499  -0.507  31.969  1.00 16.47 ? 346 SER B OG  1 
ATOM   5035 N  N   . PHE B 1 300 ? 13.374  2.401   28.923  1.00 12.96 ? 347 PHE B N   1 
ATOM   5036 C  CA  . PHE B 1 300 ? 13.310  2.856   27.570  1.00 12.82 ? 347 PHE B CA  1 
ATOM   5037 C  C   . PHE B 1 300 ? 14.704  3.103   27.055  1.00 13.95 ? 347 PHE B C   1 
ATOM   5038 O  O   . PHE B 1 300 ? 15.630  3.422   27.812  1.00 13.43 ? 347 PHE B O   1 
ATOM   5039 C  CB  . PHE B 1 300 ? 12.386  4.056   27.366  1.00 13.67 ? 347 PHE B CB  1 
ATOM   5040 C  CG  . PHE B 1 300 ? 12.910  5.361   27.950  1.00 14.70 ? 347 PHE B CG  1 
ATOM   5041 C  CD1 . PHE B 1 300 ? 13.758  6.172   27.221  1.00 15.24 ? 347 PHE B CD1 1 
ATOM   5042 C  CD2 . PHE B 1 300 ? 12.531  5.779   29.202  1.00 15.98 ? 347 PHE B CD2 1 
ATOM   5043 C  CE1 . PHE B 1 300 ? 14.193  7.385   27.735  1.00 15.55 ? 347 PHE B CE1 1 
ATOM   5044 C  CE2 . PHE B 1 300 ? 12.976  6.989   29.703  1.00 15.67 ? 347 PHE B CE2 1 
ATOM   5045 C  CZ  . PHE B 1 300 ? 13.811  7.757   28.984  1.00 16.00 ? 347 PHE B CZ  1 
ATOM   5046 N  N   . THR B 1 301 ? 14.853  2.925   25.773  1.00 15.09 ? 348 THR B N   1 
ATOM   5047 C  CA  . THR B 1 301 ? 16.018  3.419   25.084  1.00 14.86 ? 348 THR B CA  1 
ATOM   5048 C  C   . THR B 1 301 ? 15.532  3.886   23.730  1.00 14.88 ? 348 THR B C   1 
ATOM   5049 O  O   . THR B 1 301 ? 15.036  3.045   22.969  1.00 16.96 ? 348 THR B O   1 
ATOM   5050 C  CB  . THR B 1 301 ? 17.086  2.343   24.928  1.00 16.33 ? 348 THR B CB  1 
ATOM   5051 O  OG1 . THR B 1 301 ? 17.515  1.833   26.195  1.00 18.06 ? 348 THR B OG1 1 
ATOM   5052 C  CG2 . THR B 1 301 ? 18.273  2.919   24.196  1.00 19.58 ? 348 THR B CG2 1 
ATOM   5053 N  N   . ASP B 1 302 ? 15.606  5.175   23.489  1.00 14.08 ? 349 ASP B N   1 
ATOM   5054 C  CA  . ASP B 1 302 ? 14.959  5.788   22.347  1.00 17.42 ? 349 ASP B CA  1 
ATOM   5055 C  C   . ASP B 1 302 ? 15.965  5.984   21.232  1.00 17.77 ? 349 ASP B C   1 
ATOM   5056 O  O   . ASP B 1 302 ? 15.541  6.073   20.077  1.00 22.74 ? 349 ASP B O   1 
ATOM   5057 C  CB  . ASP B 1 302 ? 14.129  6.980   22.768  1.00 18.53 ? 349 ASP B CB  1 
ATOM   5058 C  CG  . ASP B 1 302 ? 12.854  6.560   23.504  1.00 18.49 ? 349 ASP B CG  1 
ATOM   5059 O  OD1 . ASP B 1 302 ? 12.479  5.373   23.397  1.00 22.38 ? 349 ASP B OD1 1 
ATOM   5060 O  OD2 . ASP B 1 302 ? 12.249  7.409   24.168  1.00 24.53 ? 349 ASP B OD2 1 
ATOM   5061 N  N   . GLY B 1 303 ? 17.266  5.985   21.539  1.00 16.76 ? 350 GLY B N   1 
ATOM   5062 C  CA  . GLY B 1 303 ? 18.280  6.320   20.546  1.00 16.90 ? 350 GLY B CA  1 
ATOM   5063 C  C   . GLY B 1 303 ? 19.391  7.156   21.187  1.00 16.38 ? 350 GLY B C   1 
ATOM   5064 O  O   . GLY B 1 303 ? 19.735  6.922   22.339  1.00 17.38 ? 350 GLY B O   1 
ATOM   5065 N  N   . THR B 1 304 ? 19.996  8.029   20.391  1.00 17.99 ? 351 THR B N   1 
ATOM   5066 C  CA  . THR B 1 304 ? 21.092  8.854   20.889  1.00 16.99 ? 351 THR B CA  1 
ATOM   5067 C  C   . THR B 1 304 ? 20.731  10.277  20.556  1.00 19.91 ? 351 THR B C   1 
ATOM   5068 O  O   . THR B 1 304 ? 20.129  10.550  19.516  1.00 24.27 ? 351 THR B O   1 
ATOM   5069 C  CB  . THR B 1 304 ? 22.475  8.433   20.411  1.00 24.59 ? 351 THR B CB  1 
ATOM   5070 O  OG1 . THR B 1 304 ? 22.380  8.201   19.032  1.00 22.62 ? 351 THR B OG1 1 
ATOM   5071 C  CG2 . THR B 1 304 ? 22.932  7.125   21.037  1.00 24.69 ? 351 THR B CG2 1 
ATOM   5072 N  N   . ASP B 1 305 ? 21.069  11.166  21.489  1.00 21.50 ? 352 ASP B N   1 
ATOM   5073 C  CA  . ASP B 1 305 ? 20.755  12.579  21.345  1.00 27.83 ? 352 ASP B CA  1 
ATOM   5074 C  C   . ASP B 1 305 ? 21.816  13.238  20.469  1.00 27.24 ? 352 ASP B C   1 
ATOM   5075 O  O   . ASP B 1 305 ? 22.649  12.584  19.856  1.00 28.18 ? 352 ASP B O   1 
ATOM   5076 C  CB  . ASP B 1 305 ? 20.562  13.226  22.706  1.00 28.21 ? 352 ASP B CB  1 
ATOM   5077 C  CG  . ASP B 1 305 ? 21.812  13.348  23.559  1.00 26.86 ? 352 ASP B CG  1 
ATOM   5078 O  OD1 . ASP B 1 305 ? 22.919  13.225  22.991  1.00 24.68 ? 352 ASP B OD1 1 
ATOM   5079 O  OD2 . ASP B 1 305 ? 21.634  13.515  24.777  1.00 29.88 ? 352 ASP B OD2 1 
ATOM   5080 N  N   . GLY B 1 306 ? 21.747  14.569  20.371  1.00 36.60 ? 353 GLY B N   1 
ATOM   5081 C  CA  . GLY B 1 306 ? 22.569  15.311  19.431  1.00 37.36 ? 353 GLY B CA  1 
ATOM   5082 C  C   . GLY B 1 306 ? 24.039  15.318  19.831  1.00 40.88 ? 353 GLY B C   1 
ATOM   5083 O  O   . GLY B 1 306 ? 24.904  15.514  18.980  1.00 40.56 ? 353 GLY B O   1 
ATOM   5084 N  N   . LEU B 1 307 ? 24.305  15.095  21.127  1.00 39.27 ? 354 LEU B N   1 
ATOM   5085 C  CA  . LEU B 1 307 ? 25.659  15.090  21.650  1.00 39.75 ? 354 LEU B CA  1 
ATOM   5086 C  C   . LEU B 1 307 ? 26.237  13.677  21.648  1.00 37.62 ? 354 LEU B C   1 
ATOM   5087 O  O   . LEU B 1 307 ? 27.363  13.473  22.095  1.00 39.50 ? 354 LEU B O   1 
ATOM   5088 C  CB  . LEU B 1 307 ? 25.620  15.701  23.050  1.00 43.21 ? 354 LEU B CB  1 
ATOM   5089 C  CG  . LEU B 1 307 ? 24.924  17.067  23.181  1.00 49.82 ? 354 LEU B CG  1 
ATOM   5090 C  CD1 . LEU B 1 307 ? 25.331  17.744  24.477  1.00 53.48 ? 354 LEU B CD1 1 
ATOM   5091 C  CD2 . LEU B 1 307 ? 25.192  18.008  22.013  1.00 51.77 ? 354 LEU B CD2 1 
ATOM   5092 N  N   . GLY B 1 308 ? 25.461  12.701  21.148  1.00 29.94 ? 355 GLY B N   1 
ATOM   5093 C  CA  . GLY B 1 308 ? 25.927  11.334  21.012  1.00 28.34 ? 355 GLY B CA  1 
ATOM   5094 C  C   . GLY B 1 308 ? 25.712  10.531  22.291  1.00 22.48 ? 355 GLY B C   1 
ATOM   5095 O  O   . GLY B 1 308 ? 26.240  9.448   22.402  1.00 26.73 ? 355 GLY B O   1 
ATOM   5096 N  N   . ARG B 1 309 ? 24.893  11.032  23.210  1.00 21.05 ? 356 ARG B N   1 
ATOM   5097 C  CA  . ARG B 1 309 ? 24.634  10.341  24.461  1.00 20.00 ? 356 ARG B CA  1 
ATOM   5098 C  C   . ARG B 1 309 ? 23.397  9.477   24.313  1.00 18.28 ? 356 ARG B C   1 
ATOM   5099 O  O   . ARG B 1 309 ? 22.520  9.781   23.523  1.00 19.37 ? 356 ARG B O   1 
ATOM   5100 C  CB  . ARG B 1 309 ? 24.377  11.306  25.609  1.00 24.29 ? 356 ARG B CB  1 
ATOM   5101 C  CG  . ARG B 1 309 ? 25.583  12.193  25.894  1.00 30.03 ? 356 ARG B CG  1 
ATOM   5102 C  CD  . ARG B 1 309 ? 25.219  13.187  26.973  1.00 34.94 ? 356 ARG B CD  1 
ATOM   5103 N  NE  . ARG B 1 309 ? 24.338  14.207  26.392  1.00 46.46 ? 356 ARG B NE  1 
ATOM   5104 C  CZ  . ARG B 1 309 ? 24.020  15.359  26.970  1.00 52.02 ? 356 ARG B CZ  1 
ATOM   5105 N  NH1 . ARG B 1 309 ? 24.451  15.633  28.188  1.00 54.38 ? 356 ARG B NH1 1 
ATOM   5106 N  NH2 . ARG B 1 309 ? 23.273  16.234  26.322  1.00 52.29 ? 356 ARG B NH2 1 
ATOM   5107 N  N   . LEU B 1 310 ? 23.323  8.428   25.107  1.00 16.80 ? 357 LEU B N   1 
ATOM   5108 C  CA  . LEU B 1 310 ? 22.216  7.493   25.005  1.00 17.61 ? 357 LEU B CA  1 
ATOM   5109 C  C   . LEU B 1 310 ? 20.988  8.115   25.647  1.00 18.00 ? 357 LEU B C   1 
ATOM   5110 O  O   . LEU B 1 310 ? 21.007  8.483   26.821  1.00 22.20 ? 357 LEU B O   1 
ATOM   5111 C  CB  . LEU B 1 310 ? 22.660  6.216   25.731  1.00 21.74 ? 357 LEU B CB  1 
ATOM   5112 C  CG  . LEU B 1 310 ? 21.902  4.928   25.410  1.00 26.77 ? 357 LEU B CG  1 
ATOM   5113 C  CD1 . LEU B 1 310 ? 22.048  4.497   23.960  1.00 24.60 ? 357 LEU B CD1 1 
ATOM   5114 C  CD2 . LEU B 1 310 ? 22.340  3.820   26.327  1.00 27.89 ? 357 LEU B CD2 1 
ATOM   5115 N  N   . ASP B 1 311 ? 19.896  8.158   24.886  1.00 15.94 ? 358 ASP B N   1 
ATOM   5116 C  CA  . ASP B 1 311 ? 18.613  8.653   25.353  1.00 15.17 ? 358 ASP B CA  1 
ATOM   5117 C  C   . ASP B 1 311 ? 17.855  7.466   25.926  1.00 15.73 ? 358 ASP B C   1 
ATOM   5118 O  O   . ASP B 1 311 ? 17.185  6.707   25.224  1.00 16.11 ? 358 ASP B O   1 
ATOM   5119 C  CB  . ASP B 1 311 ? 17.858  9.301   24.211  1.00 18.36 ? 358 ASP B CB  1 
ATOM   5120 C  CG  . ASP B 1 311 ? 16.549  9.951   24.603  1.00 20.91 ? 358 ASP B CG  1 
ATOM   5121 O  OD1 . ASP B 1 311 ? 16.193  9.885   25.793  1.00 23.37 ? 358 ASP B OD1 1 
ATOM   5122 O  OD2 . ASP B 1 311 ? 15.899  10.490  23.687  1.00 28.28 ? 358 ASP B OD2 1 
ATOM   5123 N  N   . ALA B 1 312 ? 18.003  7.278   27.211  1.00 14.89 ? 359 ALA B N   1 
ATOM   5124 C  CA  . ALA B 1 312 ? 17.602  6.053   27.855  1.00 14.23 ? 359 ALA B CA  1 
ATOM   5125 C  C   . ALA B 1 312 ? 17.220  6.385   29.271  1.00 12.92 ? 359 ALA B C   1 
ATOM   5126 O  O   . ALA B 1 312 ? 17.694  7.405   29.820  1.00 14.43 ? 359 ALA B O   1 
ATOM   5127 C  CB  . ALA B 1 312 ? 18.669  5.021   27.812  1.00 15.63 ? 359 ALA B CB  1 
ATOM   5128 N  N   . GLY B 1 313 ? 16.426  5.541   29.857  1.00 13.12 ? 360 GLY B N   1 
ATOM   5129 C  CA  . GLY B 1 313 ? 16.038  5.762   31.234  1.00 14.04 ? 360 GLY B CA  1 
ATOM   5130 C  C   . GLY B 1 313 ? 14.938  4.832   31.660  1.00 14.02 ? 360 GLY B C   1 
ATOM   5131 O  O   . GLY B 1 313 ? 14.858  3.677   31.236  1.00 13.93 ? 360 GLY B O   1 
ATOM   5132 N  N   . LEU B 1 314 ? 14.116  5.349   32.555  1.00 12.89 ? 361 LEU B N   1 
ATOM   5133 C  CA  . LEU B 1 314 ? 13.034  4.598   33.154  1.00 12.36 ? 361 LEU B CA  1 
ATOM   5134 C  C   . LEU B 1 314 ? 11.787  5.415   32.843  1.00 12.67 ? 361 LEU B C   1 
ATOM   5135 O  O   . LEU B 1 314 ? 11.691  6.612   33.164  1.00 12.69 ? 361 LEU B O   1 
ATOM   5136 C  CB  . LEU B 1 314 ? 13.245  4.410   34.650  1.00 15.56 ? 361 LEU B CB  1 
ATOM   5137 C  CG  . LEU B 1 314 ? 12.084  3.757   35.407  1.00 17.79 ? 361 LEU B CG  1 
ATOM   5138 C  CD1 . LEU B 1 314 ? 11.847  2.323   35.044  1.00 20.32 ? 361 LEU B CD1 1 
ATOM   5139 C  CD2 . LEU B 1 314 ? 12.355  3.898   36.910  1.00 20.75 ? 361 LEU B CD2 1 
ATOM   5140 N  N   . PHE B 1 315 ? 10.797  4.781   32.219  1.00 11.00 ? 362 PHE B N   1 
ATOM   5141 C  CA  . PHE B 1 315 ? 9.455   5.322   32.109  1.00 10.03 ? 362 PHE B CA  1 
ATOM   5142 C  C   . PHE B 1 315 ? 8.715   4.813   33.333  1.00 9.86  ? 362 PHE B C   1 
ATOM   5143 O  O   . PHE B 1 315 ? 8.232   3.697   33.418  1.00 11.42 ? 362 PHE B O   1 
ATOM   5144 C  CB  . PHE B 1 315 ? 8.807   4.888   30.800  1.00 10.91 ? 362 PHE B CB  1 
ATOM   5145 C  CG  . PHE B 1 315 ? 7.467   5.557   30.571  1.00 11.84 ? 362 PHE B CG  1 
ATOM   5146 C  CD1 . PHE B 1 315 ? 7.416   6.905   30.304  1.00 14.06 ? 362 PHE B CD1 1 
ATOM   5147 C  CD2 . PHE B 1 315 ? 6.290   4.848   30.547  1.00 13.22 ? 362 PHE B CD2 1 
ATOM   5148 C  CE1 . PHE B 1 315 ? 6.202   7.526   30.052  1.00 15.24 ? 362 PHE B CE1 1 
ATOM   5149 C  CE2 . PHE B 1 315 ? 5.073   5.466   30.320  1.00 14.75 ? 362 PHE B CE2 1 
ATOM   5150 C  CZ  . PHE B 1 315 ? 5.044   6.806   30.075  1.00 14.90 ? 362 PHE B CZ  1 
ATOM   5151 N  N   . PHE B 1 316 ? 8.711   5.641   34.364  1.00 10.42 ? 363 PHE B N   1 
ATOM   5152 C  CA  . PHE B 1 316 ? 8.200   5.327   35.661  1.00 10.10 ? 363 PHE B CA  1 
ATOM   5153 C  C   . PHE B 1 316 ? 6.682   5.417   35.657  1.00 10.74 ? 363 PHE B C   1 
ATOM   5154 O  O   . PHE B 1 316 ? 6.123   6.442   35.269  1.00 12.38 ? 363 PHE B O   1 
ATOM   5155 C  CB  . PHE B 1 316 ? 8.828   6.329   36.639  1.00 11.07 ? 363 PHE B CB  1 
ATOM   5156 C  CG  . PHE B 1 316 ? 8.454   6.066   38.075  1.00 12.61 ? 363 PHE B CG  1 
ATOM   5157 C  CD1 . PHE B 1 316 ? 9.218   5.236   38.865  1.00 13.97 ? 363 PHE B CD1 1 
ATOM   5158 C  CD2 . PHE B 1 316 ? 7.333   6.682   38.590  1.00 15.02 ? 363 PHE B CD2 1 
ATOM   5159 C  CE1 . PHE B 1 316 ? 8.804   5.001   40.185  1.00 15.43 ? 363 PHE B CE1 1 
ATOM   5160 C  CE2 . PHE B 1 316 ? 6.985   6.449   39.908  1.00 15.84 ? 363 PHE B CE2 1 
ATOM   5161 C  CZ  . PHE B 1 316 ? 7.708   5.612   40.637  1.00 15.76 ? 363 PHE B CZ  1 
ATOM   5162 N  N   . LEU B 1 317 ? 6.035   4.346   36.089  1.00 10.36 ? 364 LEU B N   1 
ATOM   5163 C  CA  . LEU B 1 317 ? 4.593   4.311   36.238  1.00 10.45 ? 364 LEU B CA  1 
ATOM   5164 C  C   . LEU B 1 317 ? 4.311   3.882   37.662  1.00 11.54 ? 364 LEU B C   1 
ATOM   5165 O  O   . LEU B 1 317 ? 4.805   2.843   38.137  1.00 13.29 ? 364 LEU B O   1 
ATOM   5166 C  CB  . LEU B 1 317 ? 3.983   3.343   35.229  1.00 11.38 ? 364 LEU B CB  1 
ATOM   5167 C  CG  . LEU B 1 317 ? 4.150   3.746   33.785  1.00 11.98 ? 364 LEU B CG  1 
ATOM   5168 C  CD1 . LEU B 1 317 ? 3.745   2.599   32.835  1.00 13.45 ? 364 LEU B CD1 1 
ATOM   5169 C  CD2 . LEU B 1 317 ? 3.333   4.975   33.457  1.00 14.07 ? 364 LEU B CD2 1 
ATOM   5170 N  N   . ALA B 1 318 ? 3.499   4.639   38.370  1.00 11.06 ? 365 ALA B N   1 
ATOM   5171 C  CA  . ALA B 1 318 ? 3.064   4.262   39.686  1.00 12.46 ? 365 ALA B CA  1 
ATOM   5172 C  C   . ALA B 1 318 ? 1.566   4.358   39.772  1.00 11.16 ? 365 ALA B C   1 
ATOM   5173 O  O   . ALA B 1 318 ? 0.978   5.363   39.362  1.00 11.58 ? 365 ALA B O   1 
ATOM   5174 C  CB  . ALA B 1 318 ? 3.672   5.162   40.722  1.00 15.14 ? 365 ALA B CB  1 
ATOM   5175 N  N   . TYR B 1 319 ? 0.982   3.335   40.342  1.00 11.00 ? 366 TYR B N   1 
ATOM   5176 C  CA  . TYR B 1 319 ? -0.435  3.275   40.623  1.00 10.35 ? 366 TYR B CA  1 
ATOM   5177 C  C   . TYR B 1 319 ? -0.609  3.416   42.117  1.00 11.01 ? 366 TYR B C   1 
ATOM   5178 O  O   . TYR B 1 319 ? 0.180   2.895   42.909  1.00 12.26 ? 366 TYR B O   1 
ATOM   5179 C  CB  . TYR B 1 319 ? -1.072  1.978   40.138  1.00 10.92 ? 366 TYR B CB  1 
ATOM   5180 C  CG  . TYR B 1 319 ? -1.137  1.860   38.647  1.00 11.17 ? 366 TYR B CG  1 
ATOM   5181 C  CD1 . TYR B 1 319 ? -2.256  2.349   37.970  1.00 11.72 ? 366 TYR B CD1 1 
ATOM   5182 C  CD2 . TYR B 1 319 ? -0.131  1.281   37.893  1.00 12.63 ? 366 TYR B CD2 1 
ATOM   5183 C  CE1 . TYR B 1 319 ? -2.373  2.265   36.603  1.00 11.79 ? 366 TYR B CE1 1 
ATOM   5184 C  CE2 . TYR B 1 319 ? -0.234  1.202   36.501  1.00 13.15 ? 366 TYR B CE2 1 
ATOM   5185 C  CZ  . TYR B 1 319 ? -1.362  1.663   35.883  1.00 13.16 ? 366 TYR B CZ  1 
ATOM   5186 O  OH  . TYR B 1 319 ? -1.585  1.635   34.514  1.00 14.72 ? 366 TYR B OH  1 
ATOM   5187 N  N   . GLN B 1 320 ? -1.665  4.132   42.504  1.00 11.01 ? 367 GLN B N   1 
ATOM   5188 C  CA  . GLN B 1 320 ? -1.924  4.427   43.888  1.00 10.86 ? 367 GLN B CA  1 
ATOM   5189 C  C   . GLN B 1 320 ? -3.390  4.826   44.051  1.00 11.44 ? 367 GLN B C   1 
ATOM   5190 O  O   . GLN B 1 320 ? -4.054  5.266   43.148  1.00 11.43 ? 367 GLN B O   1 
ATOM   5191 C  CB  . GLN B 1 320 ? -1.066  5.589   44.411  1.00 12.04 ? 367 GLN B CB  1 
ATOM   5192 C  CG  . GLN B 1 320 ? -1.257  6.894   43.673  1.00 13.00 ? 367 GLN B CG  1 
ATOM   5193 C  CD  . GLN B 1 320 ? -0.098  7.222   42.761  1.00 13.07 ? 367 GLN B CD  1 
ATOM   5194 O  OE1 . GLN B 1 320 ? -0.095  6.978   41.549  1.00 15.64 ? 367 GLN B OE1 1 
ATOM   5195 N  NE2 . GLN B 1 320 ? 0.975   7.676   43.325  1.00 15.93 ? 367 GLN B NE2 1 
ATOM   5196 N  N   . ARG B 1 321 ? -3.866  4.689   45.296  1.00 11.44 ? 368 ARG B N   1 
ATOM   5197 C  CA  . ARG B 1 321 ? -5.220  5.025   45.676  1.00 11.90 ? 368 ARG B CA  1 
ATOM   5198 C  C   . ARG B 1 321 ? -5.493  6.519   45.714  1.00 12.43 ? 368 ARG B C   1 
ATOM   5199 O  O   . ARG B 1 321 ? -6.617  6.945   45.491  1.00 12.93 ? 368 ARG B O   1 
ATOM   5200 C  CB  . ARG B 1 321 ? -5.475  4.378   47.039  1.00 13.39 ? 368 ARG B CB  1 
ATOM   5201 C  CG  . ARG B 1 321 ? -6.836  4.661   47.654  1.00 14.62 ? 368 ARG B CG  1 
ATOM   5202 C  CD  . ARG B 1 321 ? -7.012  3.672   48.750  1.00 16.69 ? 368 ARG B CD  1 
ATOM   5203 N  NE  . ARG B 1 321 ? -8.247  3.980   49.466  1.00 15.92 ? 368 ARG B NE  1 
ATOM   5204 C  CZ  . ARG B 1 321 ? -8.561  3.399   50.615  1.00 20.25 ? 368 ARG B CZ  1 
ATOM   5205 N  NH1 . ARG B 1 321 ? -7.785  2.460   51.131  1.00 22.54 ? 368 ARG B NH1 1 
ATOM   5206 N  NH2 . ARG B 1 321 ? -9.681  3.767   51.215  1.00 21.01 ? 368 ARG B NH2 1 
ATOM   5207 N  N   . ASP B 1 322 ? -4.454  7.308   45.918  1.00 12.17 ? 369 ASP B N   1 
ATOM   5208 C  CA  . ASP B 1 322 ? -4.567  8.766   45.951  1.00 12.48 ? 369 ASP B CA  1 
ATOM   5209 C  C   . ASP B 1 322 ? -3.209  9.359   45.622  1.00 12.03 ? 369 ASP B C   1 
ATOM   5210 O  O   . ASP B 1 322 ? -2.261  9.024   46.319  1.00 13.48 ? 369 ASP B O   1 
ATOM   5211 C  CB  . ASP B 1 322 ? -5.062  9.204   47.321  1.00 13.60 ? 369 ASP B CB  1 
ATOM   5212 C  CG  . ASP B 1 322 ? -5.495  10.656  47.428  1.00 15.07 ? 369 ASP B CG  1 
ATOM   5213 O  OD1 . ASP B 1 322 ? -4.894  11.517  46.803  1.00 13.99 ? 369 ASP B OD1 1 
ATOM   5214 O  OD2 . ASP B 1 322 ? -6.509  10.899  48.169  1.00 18.36 ? 369 ASP B OD2 1 
ATOM   5215 N  N   . ILE B 1 323 ? -3.112  10.221  44.604  1.00 11.52 ? 370 ILE B N   1 
ATOM   5216 C  CA  . ILE B 1 323 ? -1.799  10.773  44.280  1.00 12.00 ? 370 ILE B CA  1 
ATOM   5217 C  C   . ILE B 1 323 ? -1.212  11.579  45.437  1.00 12.77 ? 370 ILE B C   1 
ATOM   5218 O  O   . ILE B 1 323 ? 0.001   11.591  45.626  1.00 14.46 ? 370 ILE B O   1 
ATOM   5219 C  CB  . ILE B 1 323 ? -1.983  11.609  43.030  1.00 14.24 ? 370 ILE B CB  1 
ATOM   5220 C  CG1 . ILE B 1 323 ? -2.297  10.639  41.879  1.00 15.77 ? 370 ILE B CG1 1 
ATOM   5221 C  CG2 . ILE B 1 323 ? -0.747  12.474  42.735  1.00 16.28 ? 370 ILE B CG2 1 
ATOM   5222 C  CD1 . ILE B 1 323 ? -2.591  11.351  40.574  1.00 16.62 ? 370 ILE B CD1 1 
ATOM   5223 N  N   . ARG B 1 324 ? -2.083  12.191  46.250  1.00 13.15 ? 371 ARG B N   1 
ATOM   5224 C  CA  . ARG B 1 324 ? -1.607  13.039  47.336  1.00 14.55 ? 371 ARG B CA  1 
ATOM   5225 C  C   . ARG B 1 324 ? -0.968  12.244  48.453  1.00 15.82 ? 371 ARG B C   1 
ATOM   5226 O  O   . ARG B 1 324 ? -0.185  12.809  49.210  1.00 17.02 ? 371 ARG B O   1 
ATOM   5227 C  CB  . ARG B 1 324 ? -2.788  13.826  47.913  1.00 15.66 ? 371 ARG B CB  1 
ATOM   5228 C  CG  . ARG B 1 324 ? -3.492  14.703  46.904  1.00 17.41 ? 371 ARG B CG  1 
ATOM   5229 C  CD  . ARG B 1 324 ? -4.797  15.268  47.382  1.00 17.71 ? 371 ARG B CD  1 
ATOM   5230 N  NE  . ARG B 1 324 ? -5.785  14.227  47.610  1.00 18.19 ? 371 ARG B NE  1 
ATOM   5231 C  CZ  . ARG B 1 324 ? -7.003  14.379  48.081  1.00 18.70 ? 371 ARG B CZ  1 
ATOM   5232 N  NH1 . ARG B 1 324 ? -7.383  15.616  48.423  1.00 23.99 ? 371 ARG B NH1 1 
ATOM   5233 N  NH2 . ARG B 1 324 ? -7.815  13.374  48.208  1.00 20.17 ? 371 ARG B NH2 1 
ATOM   5234 N  N   . THR B 1 325 ? -1.254  10.957  48.564  1.00 14.03 ? 372 THR B N   1 
ATOM   5235 C  CA  . THR B 1 325 ? -0.716  10.127  49.627  1.00 15.28 ? 372 THR B CA  1 
ATOM   5236 C  C   . THR B 1 325 ? 0.164   9.017   49.105  1.00 15.00 ? 372 THR B C   1 
ATOM   5237 O  O   . THR B 1 325 ? 0.631   8.170   49.860  1.00 17.14 ? 372 THR B O   1 
ATOM   5238 C  CB  . THR B 1 325 ? -1.816  9.521   50.487  1.00 17.64 ? 372 THR B CB  1 
ATOM   5239 O  OG1 . THR B 1 325 ? -2.607  8.680   49.659  1.00 19.18 ? 372 THR B OG1 1 
ATOM   5240 C  CG2 . THR B 1 325 ? -2.703  10.573  51.138  1.00 19.23 ? 372 THR B CG2 1 
ATOM   5241 N  N   . GLY B 1 326 ? 0.425   8.996   47.802  1.00 14.44 ? 373 GLY B N   1 
ATOM   5242 C  CA  . GLY B 1 326 ? 1.295   7.991   47.217  1.00 13.66 ? 373 GLY B CA  1 
ATOM   5243 C  C   . GLY B 1 326 ? 2.521   8.670   46.622  1.00 13.83 ? 373 GLY B C   1 
ATOM   5244 O  O   . GLY B 1 326 ? 3.509   8.947   47.279  1.00 13.89 ? 373 GLY B O   1 
ATOM   5245 N  N   . PHE B 1 327 ? 2.459   8.992   45.353  1.00 13.14 ? 374 PHE B N   1 
ATOM   5246 C  CA  . PHE B 1 327 ? 3.599   9.541   44.654  1.00 12.55 ? 374 PHE B CA  1 
ATOM   5247 C  C   . PHE B 1 327 ? 4.095   10.840  45.274  1.00 12.84 ? 374 PHE B C   1 
ATOM   5248 O  O   . PHE B 1 327 ? 5.307   11.028  45.368  1.00 13.51 ? 374 PHE B O   1 
ATOM   5249 C  CB  . PHE B 1 327 ? 3.267   9.731   43.164  1.00 12.85 ? 374 PHE B CB  1 
ATOM   5250 C  CG  . PHE B 1 327 ? 4.411   10.328  42.369  1.00 12.10 ? 374 PHE B CG  1 
ATOM   5251 C  CD1 . PHE B 1 327 ? 5.431   9.537   41.887  1.00 13.42 ? 374 PHE B CD1 1 
ATOM   5252 C  CD2 . PHE B 1 327 ? 4.505   11.693  42.163  1.00 13.67 ? 374 PHE B CD2 1 
ATOM   5253 C  CE1 . PHE B 1 327 ? 6.469   10.077  41.176  1.00 13.85 ? 374 PHE B CE1 1 
ATOM   5254 C  CE2 . PHE B 1 327 ? 5.538   12.220  41.423  1.00 13.54 ? 374 PHE B CE2 1 
ATOM   5255 C  CZ  . PHE B 1 327 ? 6.520   11.405  40.963  1.00 13.12 ? 374 PHE B CZ  1 
ATOM   5256 N  N   . VAL B 1 328 ? 3.198   11.767  45.624  1.00 13.17 ? 375 VAL B N   1 
ATOM   5257 C  CA  . VAL B 1 328 ? 3.655   13.108  45.996  1.00 13.39 ? 375 VAL B CA  1 
ATOM   5258 C  C   . VAL B 1 328 ? 4.560   13.043  47.228  1.00 13.33 ? 375 VAL B C   1 
ATOM   5259 O  O   . VAL B 1 328 ? 5.660   13.589  47.160  1.00 13.97 ? 375 VAL B O   1 
ATOM   5260 C  CB  . VAL B 1 328 ? 2.495   14.091  46.146  1.00 14.42 ? 375 VAL B CB  1 
ATOM   5261 C  CG1 . VAL B 1 328 ? 3.013   15.362  46.821  1.00 16.36 ? 375 VAL B CG1 1 
ATOM   5262 C  CG2 . VAL B 1 328 ? 1.911   14.396  44.794  1.00 16.41 ? 375 VAL B CG2 1 
ATOM   5263 N  N   . PRO B 1 329 ? 4.173   12.417  48.348  1.00 13.37 ? 376 PRO B N   1 
ATOM   5264 C  CA  . PRO B 1 329 ? 5.093   12.418  49.487  1.00 14.32 ? 376 PRO B CA  1 
ATOM   5265 C  C   . PRO B 1 329 ? 6.407   11.742  49.180  1.00 14.97 ? 376 PRO B C   1 
ATOM   5266 O  O   . PRO B 1 329 ? 7.443   12.220  49.631  1.00 15.45 ? 376 PRO B O   1 
ATOM   5267 C  CB  . PRO B 1 329 ? 4.354   11.754  50.607  1.00 16.08 ? 376 PRO B CB  1 
ATOM   5268 C  CG  . PRO B 1 329 ? 3.055   11.295  50.009  1.00 18.77 ? 376 PRO B CG  1 
ATOM   5269 C  CD  . PRO B 1 329 ? 2.825   11.937  48.657  1.00 16.06 ? 376 PRO B CD  1 
ATOM   5270 N  N   . VAL B 1 330 ? 6.395   10.631  48.445  1.00 13.41 ? 377 VAL B N   1 
ATOM   5271 C  CA  . VAL B 1 330 ? 7.606   9.891   48.214  1.00 13.29 ? 377 VAL B CA  1 
ATOM   5272 C  C   . VAL B 1 330 ? 8.522   10.706  47.329  1.00 12.54 ? 377 VAL B C   1 
ATOM   5273 O  O   . VAL B 1 330 ? 9.690   10.882  47.629  1.00 13.83 ? 377 VAL B O   1 
ATOM   5274 C  CB  . VAL B 1 330 ? 7.327   8.509   47.633  1.00 13.65 ? 377 VAL B CB  1 
ATOM   5275 C  CG1 . VAL B 1 330 ? 8.627   7.783   47.319  1.00 15.35 ? 377 VAL B CG1 1 
ATOM   5276 C  CG2 . VAL B 1 330 ? 6.471   7.683   48.570  1.00 15.82 ? 377 VAL B CG2 1 
ATOM   5277 N  N   . GLN B 1 331 ? 8.017   11.252  46.240  1.00 12.46 ? 378 GLN B N   1 
ATOM   5278 C  CA  . GLN B 1 331 ? 8.846   12.059  45.366  1.00 12.28 ? 378 GLN B CA  1 
ATOM   5279 C  C   . GLN B 1 331 ? 9.350   13.332  46.075  1.00 13.19 ? 378 GLN B C   1 
ATOM   5280 O  O   . GLN B 1 331 ? 10.499  13.720  45.903  1.00 13.69 ? 378 GLN B O   1 
ATOM   5281 C  CB  . GLN B 1 331 ? 8.094   12.408  44.083  1.00 12.39 ? 378 GLN B CB  1 
ATOM   5282 C  CG  . GLN B 1 331 ? 8.885   13.288  43.130  1.00 12.75 ? 378 GLN B CG  1 
ATOM   5283 C  CD  . GLN B 1 331 ? 10.194  12.728  42.646  1.00 15.66 ? 378 GLN B CD  1 
ATOM   5284 O  OE1 . GLN B 1 331 ? 10.337  11.547  42.379  1.00 17.83 ? 378 GLN B OE1 1 
ATOM   5285 N  NE2 . GLN B 1 331 ? 11.166  13.578  42.411  1.00 19.07 ? 378 GLN B NE2 1 
ATOM   5286 N  N   . ARG B 1 332 ? 8.506   13.931  46.921  1.00 12.62 ? 379 ARG B N   1 
ATOM   5287 C  CA  . ARG B 1 332 ? 9.000   15.049  47.739  1.00 13.16 ? 379 ARG B CA  1 
ATOM   5288 C  C   . ARG B 1 332 ? 10.216  14.636  48.566  1.00 13.50 ? 379 ARG B C   1 
ATOM   5289 O  O   . ARG B 1 332 ? 11.188  15.394  48.650  1.00 14.58 ? 379 ARG B O   1 
ATOM   5290 C  CB  . ARG B 1 332 ? 7.840   15.532  48.621  1.00 15.89 ? 379 ARG B CB  1 
ATOM   5291 C  CG  . ARG B 1 332 ? 8.254   16.677  49.527  1.00 21.22 ? 379 ARG B CG  1 
ATOM   5292 C  CD  . ARG B 1 332 ? 7.024   17.339  50.118  1.00 29.86 ? 379 ARG B CD  1 
ATOM   5293 N  NE  . ARG B 1 332 ? 6.380   18.166  49.095  1.00 35.25 ? 379 ARG B NE  1 
ATOM   5294 C  CZ  . ARG B 1 332 ? 5.087   18.204  48.772  1.00 41.23 ? 379 ARG B CZ  1 
ATOM   5295 N  NH1 . ARG B 1 332 ? 4.178   17.578  49.507  1.00 39.47 ? 379 ARG B NH1 1 
ATOM   5296 N  NH2 . ARG B 1 332 ? 4.704   18.930  47.736  1.00 46.10 ? 379 ARG B NH2 1 
ATOM   5297 N  N   . ASN B 1 333 ? 10.192  13.457  49.158  1.00 12.97 ? 380 ASN B N   1 
ATOM   5298 C  CA  . ASN B 1 333 ? 11.277  12.975  49.993  1.00 13.78 ? 380 ASN B CA  1 
ATOM   5299 C  C   . ASN B 1 333 ? 12.540  12.695  49.204  1.00 14.41 ? 380 ASN B C   1 
ATOM   5300 O  O   . ASN B 1 333 ? 13.637  12.587  49.757  1.00 15.37 ? 380 ASN B O   1 
ATOM   5301 C  CB  . ASN B 1 333 ? 10.829  11.767  50.778  1.00 15.08 ? 380 ASN B CB  1 
ATOM   5302 C  CG  . ASN B 1 333 ? 11.484  11.717  52.123  1.00 17.46 ? 380 ASN B CG  1 
ATOM   5303 O  OD1 . ASN B 1 333 ? 11.513  12.760  52.792  1.00 20.16 ? 380 ASN B OD1 1 
ATOM   5304 N  ND2 . ASN B 1 333 ? 12.013  10.579  52.488  1.00 17.57 ? 380 ASN B ND2 1 
ATOM   5305 N  N   . LEU B 1 334 ? 12.432  12.601  47.890  1.00 12.85 ? 381 LEU B N   1 
ATOM   5306 C  CA  . LEU B 1 334 ? 13.588  12.379  47.045  1.00 12.99 ? 381 LEU B CA  1 
ATOM   5307 C  C   . LEU B 1 334 ? 14.282  13.687  46.672  1.00 13.09 ? 381 LEU B C   1 
ATOM   5308 O  O   . LEU B 1 334 ? 15.209  13.691  45.865  1.00 13.45 ? 381 LEU B O   1 
ATOM   5309 C  CB  . LEU B 1 334 ? 13.188  11.602  45.794  1.00 12.70 ? 381 LEU B CB  1 
ATOM   5310 C  CG  . LEU B 1 334 ? 12.618  10.204  46.040  1.00 13.46 ? 381 LEU B CG  1 
ATOM   5311 C  CD1 . LEU B 1 334 ? 12.350  9.538   44.711  1.00 14.12 ? 381 LEU B CD1 1 
ATOM   5312 C  CD2 . LEU B 1 334 ? 13.503  9.373   46.902  1.00 15.16 ? 381 LEU B CD2 1 
ATOM   5313 N  N   . ALA B 1 335 ? 13.920  14.809  47.320  1.00 13.70 ? 382 ALA B N   1 
ATOM   5314 C  CA  . ALA B 1 335 ? 14.579  16.080  47.057  1.00 14.58 ? 382 ALA B CA  1 
ATOM   5315 C  C   . ALA B 1 335 ? 16.109  16.009  47.167  1.00 14.72 ? 382 ALA B C   1 
ATOM   5316 O  O   . ALA B 1 335 ? 16.776  16.706  46.445  1.00 16.26 ? 382 ALA B O   1 
ATOM   5317 C  CB  . ALA B 1 335 ? 14.033  17.165  47.991  1.00 16.37 ? 382 ALA B CB  1 
ATOM   5318 N  N   . THR B 1 336 ? 16.611  15.218  48.100  1.00 14.25 ? 383 THR B N   1 
ATOM   5319 C  CA  . THR B 1 336 ? 18.046  15.160  48.362  1.00 14.23 ? 383 THR B CA  1 
ATOM   5320 C  C   . THR B 1 336 ? 18.657  13.828  47.956  1.00 14.88 ? 383 THR B C   1 
ATOM   5321 O  O   . THR B 1 336 ? 19.773  13.506  48.326  1.00 15.94 ? 383 THR B O   1 
ATOM   5322 C  CB  . THR B 1 336 ? 18.330  15.438  49.841  1.00 16.79 ? 383 THR B CB  1 
ATOM   5323 O  OG1 . THR B 1 336 ? 17.652  14.475  50.610  1.00 17.26 ? 383 THR B OG1 1 
ATOM   5324 C  CG2 . THR B 1 336 ? 17.848  16.815  50.238  1.00 18.32 ? 383 THR B CG2 1 
ATOM   5325 N  N   . ASP B 1 337 ? 17.905  13.027  47.175  1.00 13.17 ? 384 ASP B N   1 
ATOM   5326 C  CA  . ASP B 1 337 ? 18.359  11.727  46.733  1.00 13.03 ? 384 ASP B CA  1 
ATOM   5327 C  C   . ASP B 1 337 ? 19.704  11.814  46.037  1.00 12.01 ? 384 ASP B C   1 
ATOM   5328 O  O   . ASP B 1 337 ? 19.870  12.592  45.112  1.00 13.19 ? 384 ASP B O   1 
ATOM   5329 C  CB  . ASP B 1 337 ? 17.272  11.151  45.861  1.00 13.16 ? 384 ASP B CB  1 
ATOM   5330 C  CG  . ASP B 1 337 ? 17.408  9.699   45.456  1.00 14.15 ? 384 ASP B CG  1 
ATOM   5331 O  OD1 . ASP B 1 337 ? 18.386  9.024   45.759  1.00 13.61 ? 384 ASP B OD1 1 
ATOM   5332 O  OD2 . ASP B 1 337 ? 16.421  9.272   44.810  1.00 14.81 ? 384 ASP B OD2 1 
ATOM   5333 N  N   . ALA B 1 338 ? 20.617  10.944  46.435  1.00 12.95 ? 385 ALA B N   1 
ATOM   5334 C  CA  . ALA B 1 338 ? 21.908  10.803  45.777  1.00 13.47 ? 385 ALA B CA  1 
ATOM   5335 C  C   . ALA B 1 338 ? 21.740  10.439  44.298  1.00 13.03 ? 385 ALA B C   1 
ATOM   5336 O  O   . ALA B 1 338 ? 22.579  10.747  43.482  1.00 14.04 ? 385 ALA B O   1 
ATOM   5337 C  CB  . ALA B 1 338 ? 22.779  9.806   46.512  1.00 15.66 ? 385 ALA B CB  1 
ATOM   5338 N  N   . LEU B 1 339 ? 20.625  9.793   43.958  1.00 12.42 ? 386 LEU B N   1 
ATOM   5339 C  CA  . LEU B 1 339 ? 20.361  9.448   42.571  1.00 12.34 ? 386 LEU B CA  1 
ATOM   5340 C  C   . LEU B 1 339 ? 20.143  10.667  41.698  1.00 12.90 ? 386 LEU B C   1 
ATOM   5341 O  O   . LEU B 1 339 ? 20.311  10.584  40.491  1.00 12.42 ? 386 LEU B O   1 
ATOM   5342 C  CB  . LEU B 1 339 ? 19.117  8.570   42.529  1.00 12.76 ? 386 LEU B CB  1 
ATOM   5343 C  CG  . LEU B 1 339 ? 18.727  7.989   41.173  1.00 13.57 ? 386 LEU B CG  1 
ATOM   5344 C  CD1 . LEU B 1 339 ? 19.822  7.146   40.574  1.00 15.42 ? 386 LEU B CD1 1 
ATOM   5345 C  CD2 . LEU B 1 339 ? 17.428  7.184   41.255  1.00 15.53 ? 386 LEU B CD2 1 
ATOM   5346 N  N   . ASN B 1 340 ? 19.804  11.828  42.270  1.00 12.38 ? 387 ASN B N   1 
ATOM   5347 C  CA  . ASN B 1 340 ? 19.449  12.975  41.447  1.00 12.64 ? 387 ASN B CA  1 
ATOM   5348 C  C   . ASN B 1 340 ? 20.577  13.475  40.553  1.00 12.85 ? 387 ASN B C   1 
ATOM   5349 O  O   . ASN B 1 340 ? 20.295  14.041  39.529  1.00 14.89 ? 387 ASN B O   1 
ATOM   5350 C  CB  . ASN B 1 340 ? 18.996  14.132  42.307  1.00 12.75 ? 387 ASN B CB  1 
ATOM   5351 C  CG  . ASN B 1 340 ? 17.645  13.884  42.914  1.00 14.34 ? 387 ASN B CG  1 
ATOM   5352 O  OD1 . ASN B 1 340 ? 16.846  13.135  42.346  1.00 17.14 ? 387 ASN B OD1 1 
ATOM   5353 N  ND2 . ASN B 1 340 ? 17.306  14.579  43.971  1.00 15.28 ? 387 ASN B ND2 1 
ATOM   5354 N  N   . GLU B 1 341 ? 21.829  13.185  40.900  1.00 13.59 ? 388 GLU B N   1 
ATOM   5355 C  CA  . GLU B 1 341 ? 22.967  13.549  40.095  1.00 15.38 ? 388 GLU B CA  1 
ATOM   5356 C  C   . GLU B 1 341 ? 22.925  12.860  38.734  1.00 14.31 ? 388 GLU B C   1 
ATOM   5357 O  O   . GLU B 1 341 ? 23.443  13.377  37.764  1.00 16.60 ? 388 GLU B O   1 
ATOM   5358 C  CB  . GLU B 1 341 ? 24.219  13.119  40.869  1.00 19.08 ? 388 GLU B CB  1 
ATOM   5359 C  CG  . GLU B 1 341 ? 25.517  13.387  40.110  1.00 22.75 ? 388 GLU B CG  1 
ATOM   5360 C  CD  . GLU B 1 341 ? 26.756  13.160  40.942  1.00 29.32 ? 388 GLU B CD  1 
ATOM   5361 O  OE1 . GLU B 1 341 ? 26.623  12.843  42.140  1.00 29.32 ? 388 GLU B OE1 1 
ATOM   5362 O  OE2 . GLU B 1 341 ? 27.858  13.247  40.353  1.00 36.86 ? 388 GLU B OE2 1 
ATOM   5363 N  N   . PHE B 1 342 ? 22.211  11.743  38.644  1.00 12.79 ? 389 PHE B N   1 
ATOM   5364 C  CA  . PHE B 1 342 ? 22.313  10.875  37.487  1.00 13.12 ? 389 PHE B CA  1 
ATOM   5365 C  C   . PHE B 1 342 ? 21.005  10.756  36.721  1.00 13.72 ? 389 PHE B C   1 
ATOM   5366 O  O   . PHE B 1 342 ? 20.969  9.966   35.763  1.00 14.94 ? 389 PHE B O   1 
ATOM   5367 C  CB  . PHE B 1 342 ? 22.733  9.477   37.927  1.00 13.92 ? 389 PHE B CB  1 
ATOM   5368 C  CG  . PHE B 1 342 ? 24.058  9.491   38.654  1.00 14.78 ? 389 PHE B CG  1 
ATOM   5369 C  CD1 . PHE B 1 342 ? 25.220  9.616   37.955  1.00 15.57 ? 389 PHE B CD1 1 
ATOM   5370 C  CD2 . PHE B 1 342 ? 24.079  9.294   40.011  1.00 15.34 ? 389 PHE B CD2 1 
ATOM   5371 C  CE1 . PHE B 1 342 ? 26.432  9.637   38.649  1.00 15.75 ? 389 PHE B CE1 1 
ATOM   5372 C  CE2 . PHE B 1 342 ? 25.287  9.304   40.686  1.00 16.46 ? 389 PHE B CE2 1 
ATOM   5373 C  CZ  . PHE B 1 342 ? 26.436  9.494   40.004  1.00 16.49 ? 389 PHE B CZ  1 
ATOM   5374 N  N   . ILE B 1 343 ? 19.962  11.444  37.141  1.00 12.68 ? 390 ILE B N   1 
ATOM   5375 C  CA  . ILE B 1 343 ? 18.650  11.353  36.475  1.00 12.64 ? 390 ILE B CA  1 
ATOM   5376 C  C   . ILE B 1 343 ? 18.076  12.726  36.249  1.00 12.65 ? 390 ILE B C   1 
ATOM   5377 O  O   . ILE B 1 343 ? 18.461  13.692  36.899  1.00 15.04 ? 390 ILE B O   1 
ATOM   5378 C  CB  . ILE B 1 343 ? 17.665  10.476  37.255  1.00 13.63 ? 390 ILE B CB  1 
ATOM   5379 C  CG1 . ILE B 1 343 ? 17.310  11.088  38.595  1.00 14.92 ? 390 ILE B CG1 1 
ATOM   5380 C  CG2 . ILE B 1 343 ? 18.166  9.050   37.395  1.00 14.75 ? 390 ILE B CG2 1 
ATOM   5381 C  CD1 . ILE B 1 343 ? 16.073  10.485  39.206  1.00 17.91 ? 390 ILE B CD1 1 
ATOM   5382 N  N   . GLN B 1 344 ? 17.120  12.816  35.361  1.00 12.44 ? 391 GLN B N   1 
ATOM   5383 C  CA  . GLN B 1 344 ? 16.341  14.026  35.200  1.00 13.06 ? 391 GLN B CA  1 
ATOM   5384 C  C   . GLN B 1 344 ? 14.942  13.637  34.747  1.00 12.09 ? 391 GLN B C   1 
ATOM   5385 O  O   . GLN B 1 344 ? 14.759  12.918  33.770  1.00 12.60 ? 391 GLN B O   1 
ATOM   5386 C  CB  . GLN B 1 344 ? 16.943  14.915  34.134  1.00 17.41 ? 391 GLN B CB  1 
ATOM   5387 C  CG  . GLN B 1 344 ? 16.412  16.340  34.193  1.00 21.16 ? 391 GLN B CG  1 
ATOM   5388 C  CD  . GLN B 1 344 ? 17.119  17.276  33.248  1.00 25.33 ? 391 GLN B CD  1 
ATOM   5389 O  OE1 . GLN B 1 344 ? 17.127  17.039  32.044  1.00 27.49 ? 391 GLN B OE1 1 
ATOM   5390 N  NE2 . GLN B 1 344 ? 17.658  18.360  33.781  1.00 31.75 ? 391 GLN B NE2 1 
ATOM   5391 N  N   . HIS B 1 345 ? 13.940  14.162  35.447  1.00 11.45 ? 392 HIS B N   1 
ATOM   5392 C  CA  . HIS B 1 345 ? 12.551  14.001  35.057  1.00 11.22 ? 392 HIS B CA  1 
ATOM   5393 C  C   . HIS B 1 345 ? 12.254  14.957  33.928  1.00 12.35 ? 392 HIS B C   1 
ATOM   5394 O  O   . HIS B 1 345 ? 12.354  16.176  34.134  1.00 13.45 ? 392 HIS B O   1 
ATOM   5395 C  CB  . HIS B 1 345 ? 11.643  14.245  36.239  1.00 12.26 ? 392 HIS B CB  1 
ATOM   5396 C  CG  . HIS B 1 345 ? 11.740  13.286  37.344  1.00 11.11 ? 392 HIS B CG  1 
ATOM   5397 N  ND1 . HIS B 1 345 ? 10.632  12.608  37.785  1.00 12.75 ? 392 HIS B ND1 1 
ATOM   5398 C  CD2 . HIS B 1 345 ? 12.769  12.882  38.102  1.00 13.26 ? 392 HIS B CD2 1 
ATOM   5399 C  CE1 . HIS B 1 345 ? 10.991  11.850  38.805  1.00 12.85 ? 392 HIS B CE1 1 
ATOM   5400 N  NE2 . HIS B 1 345 ? 12.283  12.010  39.027  1.00 12.81 ? 392 HIS B NE2 1 
ATOM   5401 N  N   . VAL B 1 346 ? 11.823  14.404  32.802  1.00 11.22 ? 393 VAL B N   1 
ATOM   5402 C  CA  . VAL B 1 346 ? 11.656  15.166  31.584  1.00 12.24 ? 393 VAL B CA  1 
ATOM   5403 C  C   . VAL B 1 346 ? 10.262  15.056  30.998  1.00 12.95 ? 393 VAL B C   1 
ATOM   5404 O  O   . VAL B 1 346 ? 9.967   15.715  30.012  1.00 14.15 ? 393 VAL B O   1 
ATOM   5405 C  CB  . VAL B 1 346 ? 12.723  14.864  30.533  1.00 12.79 ? 393 VAL B CB  1 
ATOM   5406 C  CG1 . VAL B 1 346 ? 14.115  15.285  31.042  1.00 14.75 ? 393 VAL B CG1 1 
ATOM   5407 C  CG2 . VAL B 1 346 ? 12.715  13.421  30.121  1.00 14.65 ? 393 VAL B CG2 1 
ATOM   5408 N  N   . GLY B 1 347 ? 9.375   14.277  31.598  1.00 12.69 ? 394 GLY B N   1 
ATOM   5409 C  CA  . GLY B 1 347 ? 7.992   14.258  31.166  1.00 11.46 ? 394 GLY B CA  1 
ATOM   5410 C  C   . GLY B 1 347 ? 7.153   13.829  32.341  1.00 10.82 ? 394 GLY B C   1 
ATOM   5411 O  O   . GLY B 1 347 ? 7.649   13.071  33.169  1.00 12.13 ? 394 GLY B O   1 
ATOM   5412 N  N   . SER B 1 348 ? 5.898   14.258  32.378  1.00 11.14 ? 395 SER B N   1 
ATOM   5413 C  CA  . SER B 1 348 ? 5.044   13.961  33.499  1.00 10.78 ? 395 SER B CA  1 
ATOM   5414 C  C   . SER B 1 348 ? 3.610   13.971  33.044  1.00 11.81 ? 395 SER B C   1 
ATOM   5415 O  O   . SER B 1 348 ? 3.193   14.835  32.287  1.00 12.49 ? 395 SER B O   1 
ATOM   5416 C  CB  . SER B 1 348 ? 5.275   14.998  34.536  1.00 11.88 ? 395 SER B CB  1 
ATOM   5417 O  OG  . SER B 1 348 ? 4.550   14.680  35.710  1.00 13.96 ? 395 SER B OG  1 
ATOM   5418 N  N   . ALA B 1 349 ? 2.817   13.088  33.626  1.00 10.71 ? 396 ALA B N   1 
ATOM   5419 C  CA  . ALA B 1 349 ? 1.379   13.153  33.429  1.00 11.56 ? 396 ALA B CA  1 
ATOM   5420 C  C   . ALA B 1 349 ? 0.705   12.389  34.541  1.00 11.75 ? 396 ALA B C   1 
ATOM   5421 O  O   . ALA B 1 349 ? 1.257   11.416  35.055  1.00 13.00 ? 396 ALA B O   1 
ATOM   5422 C  CB  . ALA B 1 349 ? 0.972   12.557  32.112  1.00 12.78 ? 396 ALA B CB  1 
ATOM   5423 N  N   . VAL B 1 350 ? -0.516  12.752  34.865  1.00 10.85 ? 397 VAL B N   1 
ATOM   5424 C  CA  . VAL B 1 350 ? -1.324  12.048  35.835  1.00 10.64 ? 397 VAL B CA  1 
ATOM   5425 C  C   . VAL B 1 350 ? -2.642  11.676  35.177  1.00 10.17 ? 397 VAL B C   1 
ATOM   5426 O  O   . VAL B 1 350 ? -3.193  12.403  34.367  1.00 10.72 ? 397 VAL B O   1 
ATOM   5427 C  CB  . VAL B 1 350 ? -1.539  12.807  37.154  1.00 12.54 ? 397 VAL B CB  1 
ATOM   5428 C  CG1 . VAL B 1 350 ? -0.203  13.076  37.836  1.00 14.12 ? 397 VAL B CG1 1 
ATOM   5429 C  CG2 . VAL B 1 350 ? -2.299  14.096  36.990  1.00 14.07 ? 397 VAL B CG2 1 
ATOM   5430 N  N   . PHE B 1 351 ? -3.202  10.532  35.625  1.00 10.06 ? 398 PHE B N   1 
ATOM   5431 C  CA  . PHE B 1 351 ? -4.468  10.055  35.078  1.00 10.71 ? 398 PHE B CA  1 
ATOM   5432 C  C   . PHE B 1 351 ? -5.294  9.377   36.150  1.00 10.58 ? 398 PHE B C   1 
ATOM   5433 O  O   . PHE B 1 351 ? -4.739  8.676   36.991  1.00 12.24 ? 398 PHE B O   1 
ATOM   5434 C  CB  . PHE B 1 351 ? -4.227  9.030   33.968  1.00 11.18 ? 398 PHE B CB  1 
ATOM   5435 C  CG  . PHE B 1 351 ? -3.406  9.608   32.845  1.00 10.78 ? 398 PHE B CG  1 
ATOM   5436 C  CD1 . PHE B 1 351 ? -3.974  10.342  31.840  1.00 11.69 ? 398 PHE B CD1 1 
ATOM   5437 C  CD2 . PHE B 1 351 ? -2.039  9.366   32.824  1.00 12.32 ? 398 PHE B CD2 1 
ATOM   5438 C  CE1 . PHE B 1 351 ? -3.192  10.869  30.829  1.00 12.83 ? 398 PHE B CE1 1 
ATOM   5439 C  CE2 . PHE B 1 351 ? -1.273  9.898   31.818  1.00 12.98 ? 398 PHE B CE2 1 
ATOM   5440 C  CZ  . PHE B 1 351 ? -1.856  10.615  30.831  1.00 12.57 ? 398 PHE B CZ  1 
ATOM   5441 N  N   . ALA B 1 352 ? -6.595  9.492   36.055  1.00 10.51 ? 399 ALA B N   1 
ATOM   5442 C  CA  . ALA B 1 352 ? -7.532  8.682   36.788  1.00 10.08 ? 399 ALA B CA  1 
ATOM   5443 C  C   . ALA B 1 352 ? -7.897  7.492   35.924  1.00 10.49 ? 399 ALA B C   1 
ATOM   5444 O  O   . ALA B 1 352 ? -8.388  7.666   34.830  1.00 12.00 ? 399 ALA B O   1 
ATOM   5445 C  CB  . ALA B 1 352 ? -8.798  9.473   37.080  1.00 11.89 ? 399 ALA B CB  1 
ATOM   5446 N  N   . VAL B 1 353 ? -7.644  6.314   36.432  1.00 10.15 ? 400 VAL B N   1 
ATOM   5447 C  CA  . VAL B 1 353 ? -7.845  5.055   35.731  1.00 10.34 ? 400 VAL B CA  1 
ATOM   5448 C  C   . VAL B 1 353 ? -9.139  4.454   36.229  1.00 11.03 ? 400 VAL B C   1 
ATOM   5449 O  O   . VAL B 1 353 ? -9.223  4.067   37.382  1.00 11.24 ? 400 VAL B O   1 
ATOM   5450 C  CB  . VAL B 1 353 ? -6.643  4.138   35.945  1.00 12.33 ? 400 VAL B CB  1 
ATOM   5451 C  CG1 . VAL B 1 353 ? -6.846  2.761   35.371  1.00 14.09 ? 400 VAL B CG1 1 
ATOM   5452 C  CG2 . VAL B 1 353 ? -5.372  4.780   35.377  1.00 13.94 ? 400 VAL B CG2 1 
ATOM   5453 N  N   . PRO B 1 354 ? -10.196 4.434   35.394  1.00 10.47 ? 401 PRO B N   1 
ATOM   5454 C  CA  . PRO B 1 354 ? -11.503 4.052   35.891  1.00 11.65 ? 401 PRO B CA  1 
ATOM   5455 C  C   . PRO B 1 354 ? -11.571 2.590   36.248  1.00 11.78 ? 401 PRO B C   1 
ATOM   5456 O  O   . PRO B 1 354 ? -10.681 1.770   35.971  1.00 11.32 ? 401 PRO B O   1 
ATOM   5457 C  CB  . PRO B 1 354 ? -12.440 4.400   34.787  1.00 13.19 ? 401 PRO B CB  1 
ATOM   5458 C  CG  . PRO B 1 354 ? -11.597 4.421   33.582  1.00 14.41 ? 401 PRO B CG  1 
ATOM   5459 C  CD  . PRO B 1 354 ? -10.268 4.998   34.047  1.00 11.35 ? 401 PRO B CD  1 
ATOM   5460 N  N   . PRO B 1 355 ? -12.687 2.202   36.905  1.00 12.30 ? 402 PRO B N   1 
ATOM   5461 C  CA  . PRO B 1 355 ? -12.943 0.803   37.190  1.00 12.31 ? 402 PRO B CA  1 
ATOM   5462 C  C   . PRO B 1 355 ? -13.022 -0.041  35.940  1.00 11.51 ? 402 PRO B C   1 
ATOM   5463 O  O   . PRO B 1 355 ? -13.000 0.432   34.832  1.00 12.72 ? 402 PRO B O   1 
ATOM   5464 C  CB  . PRO B 1 355 ? -14.274 0.772   37.955  1.00 15.54 ? 402 PRO B CB  1 
ATOM   5465 C  CG  . PRO B 1 355 ? -14.846 2.123   37.794  1.00 16.99 ? 402 PRO B CG  1 
ATOM   5466 C  CD  . PRO B 1 355 ? -13.758 3.098   37.391  1.00 13.73 ? 402 PRO B CD  1 
ATOM   5467 N  N   . GLY B 1 356 ? -13.065 -1.345  36.167  1.00 12.70 ? 403 GLY B N   1 
ATOM   5468 C  CA  . GLY B 1 356 ? -13.070 -2.320  35.104  1.00 13.53 ? 403 GLY B CA  1 
ATOM   5469 C  C   . GLY B 1 356 ? -14.342 -2.319  34.280  1.00 13.22 ? 403 GLY B C   1 
ATOM   5470 O  O   . GLY B 1 356 ? -15.379 -1.798  34.677  1.00 15.26 ? 403 GLY B O   1 
ATOM   5471 N  N   . VAL B 1 357 ? -14.251 -2.953  33.121  1.00 13.01 ? 404 VAL B N   1 
ATOM   5472 C  CA  . VAL B 1 357 ? -15.384 -3.236  32.271  1.00 13.73 ? 404 VAL B CA  1 
ATOM   5473 C  C   . VAL B 1 357 ? -15.980 -4.551  32.731  1.00 13.79 ? 404 VAL B C   1 
ATOM   5474 O  O   . VAL B 1 357 ? -15.349 -5.599  32.656  1.00 14.87 ? 404 VAL B O   1 
ATOM   5475 C  CB  . VAL B 1 357 ? -14.881 -3.324  30.824  1.00 14.72 ? 404 VAL B CB  1 
ATOM   5476 C  CG1 . VAL B 1 357 ? -16.023 -3.509  29.843  1.00 16.60 ? 404 VAL B CG1 1 
ATOM   5477 C  CG2 . VAL B 1 357 ? -14.071 -2.093  30.409  1.00 18.20 ? 404 VAL B CG2 1 
ATOM   5478 N  N   . ARG B 1 358 ? -17.201 -4.455  33.261  1.00 14.95 ? 405 ARG B N   1 
ATOM   5479 C  CA  . ARG B 1 358 ? -17.726 -5.551  34.054  1.00 17.88 ? 405 ARG B CA  1 
ATOM   5480 C  C   . ARG B 1 358 ? -18.097 -6.758  33.201  1.00 19.24 ? 405 ARG B C   1 
ATOM   5481 O  O   . ARG B 1 358 ? -17.957 -7.891  33.665  1.00 22.65 ? 405 ARG B O   1 
ATOM   5482 C  CB  . ARG B 1 358 ? -18.934 -5.066  34.852  1.00 21.69 ? 405 ARG B CB  1 
ATOM   5483 C  CG  . ARG B 1 358 ? -18.614 -3.916  35.789  1.00 28.48 ? 405 ARG B CG  1 
ATOM   5484 C  CD  . ARG B 1 358 ? -17.374 -4.126  36.647  1.00 35.91 ? 405 ARG B CD  1 
ATOM   5485 N  NE  . ARG B 1 358 ? -17.555 -5.326  37.472  1.00 46.96 ? 405 ARG B NE  1 
ATOM   5486 C  CZ  . ARG B 1 358 ? -17.780 -5.356  38.783  1.00 52.05 ? 405 ARG B CZ  1 
ATOM   5487 N  NH1 . ARG B 1 358 ? -17.816 -4.233  39.485  1.00 51.83 ? 405 ARG B NH1 1 
ATOM   5488 N  NH2 . ARG B 1 358 ? -17.962 -6.522  39.383  1.00 57.43 ? 405 ARG B NH2 1 
ATOM   5489 N  N   . ASP B 1 359 ? -18.630 -6.525  32.015  1.00 16.82 ? 406 ASP B N   1 
ATOM   5490 C  CA  . ASP B 1 359 ? -19.118 -7.603  31.177  1.00 18.52 ? 406 ASP B CA  1 
ATOM   5491 C  C   . ASP B 1 359 ? -19.186 -7.082  29.750  1.00 20.04 ? 406 ASP B C   1 
ATOM   5492 O  O   . ASP B 1 359 ? -18.789 -5.933  29.455  1.00 19.18 ? 406 ASP B O   1 
ATOM   5493 C  CB  . ASP B 1 359 ? -20.462 -8.092  31.699  1.00 21.23 ? 406 ASP B CB  1 
ATOM   5494 C  CG  . ASP B 1 359 ? -21.574 -7.043  31.683  1.00 25.12 ? 406 ASP B CG  1 
ATOM   5495 O  OD1 . ASP B 1 359 ? -21.538 -6.072  30.860  1.00 24.07 ? 406 ASP B OD1 1 
ATOM   5496 O  OD2 . ASP B 1 359 ? -22.512 -7.197  32.484  1.00 33.81 ? 406 ASP B OD2 1 
ATOM   5497 N  N   . ALA B 1 360 ? -19.690 -7.910  28.832  1.00 19.91 ? 407 ALA B N   1 
ATOM   5498 C  CA  . ALA B 1 360 ? -19.717 -7.594  27.414  1.00 21.80 ? 407 ALA B CA  1 
ATOM   5499 C  C   . ALA B 1 360 ? -20.592 -6.395  27.029  1.00 20.90 ? 407 ALA B C   1 
ATOM   5500 O  O   . ALA B 1 360 ? -20.466 -5.887  25.923  1.00 26.07 ? 407 ALA B O   1 
ATOM   5501 C  CB  . ALA B 1 360 ? -20.159 -8.855  26.655  1.00 24.45 ? 407 ALA B CB  1 
ATOM   5502 N  N   . ASP B 1 361 ? -21.475 -5.911  27.901  1.00 20.05 ? 408 ASP B N   1 
ATOM   5503 C  CA  . ASP B 1 361 ? -22.321 -4.771  27.583  1.00 23.01 ? 408 ASP B CA  1 
ATOM   5504 C  C   . ASP B 1 361 ? -21.747 -3.467  28.142  1.00 23.26 ? 408 ASP B C   1 
ATOM   5505 O  O   . ASP B 1 361 ? -22.176 -2.383  27.764  1.00 24.53 ? 408 ASP B O   1 
ATOM   5506 C  CB  . ASP B 1 361 ? -23.721 -4.968  28.137  1.00 27.04 ? 408 ASP B CB  1 
ATOM   5507 C  CG  . ASP B 1 361 ? -24.481 -6.120  27.504  1.00 31.78 ? 408 ASP B CG  1 
ATOM   5508 O  OD1 . ASP B 1 361 ? -24.500 -6.178  26.265  1.00 39.73 ? 408 ASP B OD1 1 
ATOM   5509 O  OD2 . ASP B 1 361 ? -24.993 -6.946  28.266  1.00 36.78 ? 408 ASP B OD2 1 
ATOM   5510 N  N   . ASP B 1 362 ? -20.751 -3.585  29.017  1.00 19.18 ? 409 ASP B N   1 
ATOM   5511 C  CA  . ASP B 1 362 ? -20.150 -2.419  29.647  1.00 18.05 ? 409 ASP B CA  1 
ATOM   5512 C  C   . ASP B 1 362 ? -19.139 -1.777  28.704  1.00 15.55 ? 409 ASP B C   1 
ATOM   5513 O  O   . ASP B 1 362 ? -18.763 -2.313  27.667  1.00 17.44 ? 409 ASP B O   1 
ATOM   5514 C  CB  . ASP B 1 362 ? -19.525 -2.823  30.962  1.00 16.55 ? 409 ASP B CB  1 
ATOM   5515 C  CG  . ASP B 1 362 ? -19.296 -1.680  31.944  1.00 16.18 ? 409 ASP B CG  1 
ATOM   5516 O  OD1 . ASP B 1 362 ? -19.824 -0.566  31.685  1.00 17.14 ? 409 ASP B OD1 1 
ATOM   5517 O  OD2 . ASP B 1 362 ? -18.625 -1.912  32.938  1.00 17.55 ? 409 ASP B OD2 1 
ATOM   5518 N  N   . TRP B 1 363 ? -18.644 -0.587  29.090  1.00 14.12 ? 410 TRP B N   1 
ATOM   5519 C  CA  . TRP B 1 363 ? -17.735 0.169   28.254  1.00 13.63 ? 410 TRP B CA  1 
ATOM   5520 C  C   . TRP B 1 363 ? -16.875 1.067   29.120  1.00 12.28 ? 410 TRP B C   1 
ATOM   5521 O  O   . TRP B 1 363 ? -17.282 1.509   30.188  1.00 13.99 ? 410 TRP B O   1 
ATOM   5522 C  CB  . TRP B 1 363 ? -18.480 0.968   27.166  1.00 14.65 ? 410 TRP B CB  1 
ATOM   5523 C  CG  . TRP B 1 363 ? -19.710 1.666   27.640  1.00 15.56 ? 410 TRP B CG  1 
ATOM   5524 C  CD1 . TRP B 1 363 ? -20.948 1.115   27.777  1.00 17.55 ? 410 TRP B CD1 1 
ATOM   5525 C  CD2 . TRP B 1 363 ? -19.851 3.056   27.940  1.00 15.60 ? 410 TRP B CD2 1 
ATOM   5526 N  NE1 . TRP B 1 363 ? -21.825 2.060   28.214  1.00 17.59 ? 410 TRP B NE1 1 
ATOM   5527 C  CE2 . TRP B 1 363 ? -21.197 3.269   28.303  1.00 16.86 ? 410 TRP B CE2 1 
ATOM   5528 C  CE3 . TRP B 1 363 ? -18.991 4.151   27.950  1.00 15.67 ? 410 TRP B CE3 1 
ATOM   5529 C  CZ2 . TRP B 1 363 ? -21.705 4.512   28.656  1.00 17.86 ? 410 TRP B CZ2 1 
ATOM   5530 C  CZ3 . TRP B 1 363 ? -19.503 5.392   28.279  1.00 16.72 ? 410 TRP B CZ3 1 
ATOM   5531 C  CH2 . TRP B 1 363 ? -20.840 5.567   28.636  1.00 18.97 ? 410 TRP B CH2 1 
ATOM   5532 N  N   . TRP B 1 364 ? -15.691 1.344   28.615  1.00 12.07 ? 411 TRP B N   1 
ATOM   5533 C  CA  . TRP B 1 364 ? -14.740 2.228   29.282  1.00 11.98 ? 411 TRP B CA  1 
ATOM   5534 C  C   . TRP B 1 364 ? -15.387 3.553   29.620  1.00 12.51 ? 411 TRP B C   1 
ATOM   5535 O  O   . TRP B 1 364 ? -15.894 4.227   28.746  1.00 13.96 ? 411 TRP B O   1 
ATOM   5536 C  CB  . TRP B 1 364 ? -13.558 2.486   28.350  1.00 12.25 ? 411 TRP B CB  1 
ATOM   5537 C  CG  . TRP B 1 364 ? -12.513 1.411   28.323  1.00 10.73 ? 411 TRP B CG  1 
ATOM   5538 C  CD1 . TRP B 1 364 ? -12.227 0.516   29.294  1.00 12.20 ? 411 TRP B CD1 1 
ATOM   5539 C  CD2 . TRP B 1 364 ? -11.482 1.252   27.327  1.00 11.81 ? 411 TRP B CD2 1 
ATOM   5540 N  NE1 . TRP B 1 364 ? -11.112 -0.216  28.957  1.00 12.66 ? 411 TRP B NE1 1 
ATOM   5541 C  CE2 . TRP B 1 364 ? -10.629 0.227   27.779  1.00 11.94 ? 411 TRP B CE2 1 
ATOM   5542 C  CE3 . TRP B 1 364 ? -11.204 1.894   26.118  1.00 12.96 ? 411 TRP B CE3 1 
ATOM   5543 C  CZ2 . TRP B 1 364 ? -9.516  -0.159  27.063  1.00 12.60 ? 411 TRP B CZ2 1 
ATOM   5544 C  CZ3 . TRP B 1 364 ? -10.076 1.522   25.416  1.00 13.50 ? 411 TRP B CZ3 1 
ATOM   5545 C  CH2 . TRP B 1 364 ? -9.254  0.498   25.898  1.00 13.27 ? 411 TRP B CH2 1 
ATOM   5546 N  N   . GLY B 1 365 ? -15.276 3.953   30.879  1.00 12.93 ? 412 GLY B N   1 
ATOM   5547 C  CA  . GLY B 1 365 ? -15.797 5.260   31.267  1.00 14.66 ? 412 GLY B CA  1 
ATOM   5548 C  C   . GLY B 1 365 ? -17.283 5.265   31.596  1.00 13.89 ? 412 GLY B C   1 
ATOM   5549 O  O   . GLY B 1 365 ? -17.818 6.334   31.886  1.00 14.69 ? 412 GLY B O   1 
ATOM   5550 N  N   . SER B 1 366 ? -17.967 4.128   31.570  1.00 14.12 ? 413 SER B N   1 
ATOM   5551 C  CA  . SER B 1 366 ? -19.402 4.127   31.786  1.00 14.20 ? 413 SER B CA  1 
ATOM   5552 C  C   . SER B 1 366 ? -19.770 4.687   33.152  1.00 15.12 ? 413 SER B C   1 
ATOM   5553 O  O   . SER B 1 366 ? -20.868 5.237   33.282  1.00 17.67 ? 413 SER B O   1 
ATOM   5554 C  CB  . SER B 1 366 ? -19.963 2.742   31.604  1.00 14.91 ? 413 SER B CB  1 
ATOM   5555 O  OG  . SER B 1 366 ? -19.516 1.867   32.622  1.00 15.64 ? 413 SER B OG  1 
ATOM   5556 N  N   . THR B 1 367 ? -18.945 4.527   34.185  1.00 14.06 ? 414 THR B N   1 
ATOM   5557 C  CA  . THR B 1 367 ? -19.341 5.035   35.495  1.00 14.99 ? 414 THR B CA  1 
ATOM   5558 C  C   . THR B 1 367 ? -19.249 6.552   35.535  1.00 16.37 ? 414 THR B C   1 
ATOM   5559 O  O   . THR B 1 367 ? -19.917 7.178   36.347  1.00 19.05 ? 414 THR B O   1 
ATOM   5560 C  CB  . THR B 1 367 ? -18.557 4.428   36.648  1.00 15.34 ? 414 THR B CB  1 
ATOM   5561 O  OG1 . THR B 1 367 ? -17.208 4.820   36.481  1.00 15.30 ? 414 THR B OG1 1 
ATOM   5562 C  CG2 . THR B 1 367 ? -18.673 2.920   36.718  1.00 17.21 ? 414 THR B CG2 1 
ATOM   5563 N  N   . LEU B 1 368 ? -18.446 7.174   34.694  1.00 15.43 ? 415 LEU B N   1 
ATOM   5564 C  CA  . LEU B 1 368 ? -18.312 8.631   34.637  1.00 15.57 ? 415 LEU B CA  1 
ATOM   5565 C  C   . LEU B 1 368 ? -19.372 9.240   33.737  1.00 18.98 ? 415 LEU B C   1 
ATOM   5566 O  O   . LEU B 1 368 ? -19.986 10.252  34.100  1.00 21.93 ? 415 LEU B O   1 
ATOM   5567 C  CB  . LEU B 1 368 ? -16.936 8.974   34.097  1.00 14.93 ? 415 LEU B CB  1 
ATOM   5568 C  CG  . LEU B 1 368 ? -16.656 10.471  33.910  1.00 16.21 ? 415 LEU B CG  1 
ATOM   5569 C  CD1 . LEU B 1 368 ? -16.870 11.245  35.211  1.00 18.14 ? 415 LEU B CD1 1 
ATOM   5570 C  CD2 . LEU B 1 368 ? -15.285 10.647  33.421  1.00 17.28 ? 415 LEU B CD2 1 
ATOM   5571 N  N   . PHE B 1 369 ? -19.578 8.679   32.551  1.00 18.36 ? 416 PHE B N   1 
ATOM   5572 C  CA  . PHE B 1 369 ? -20.470 9.295   31.582  1.00 20.63 ? 416 PHE B CA  1 
ATOM   5573 C  C   . PHE B 1 369 ? -21.908 8.880   31.813  1.00 27.43 ? 416 PHE B C   1 
ATOM   5574 O  O   . PHE B 1 369 ? -22.804 9.653   31.483  1.00 31.22 ? 416 PHE B O   1 
ATOM   5575 C  CB  . PHE B 1 369 ? -19.931 9.002   30.194  1.00 19.79 ? 416 PHE B CB  1 
ATOM   5576 C  CG  . PHE B 1 369 ? -18.691 9.819   29.888  1.00 18.67 ? 416 PHE B CG  1 
ATOM   5577 C  CD1 . PHE B 1 369 ? -18.820 11.128  29.455  1.00 20.54 ? 416 PHE B CD1 1 
ATOM   5578 C  CD2 . PHE B 1 369 ? -17.411 9.324   30.071  1.00 20.64 ? 416 PHE B CD2 1 
ATOM   5579 C  CE1 . PHE B 1 369 ? -17.710 11.898  29.189  1.00 20.73 ? 416 PHE B CE1 1 
ATOM   5580 C  CE2 . PHE B 1 369 ? -16.312 10.104  29.817  1.00 20.67 ? 416 PHE B CE2 1 
ATOM   5581 C  CZ  . PHE B 1 369 ? -16.468 11.389  29.362  1.00 21.77 ? 416 PHE B CZ  1 
ATOM   5582 N  N   . GLY B 1 370 ? -22.135 7.699   32.384  1.00 26.93 ? 417 GLY B N   1 
ATOM   5583 C  CA  . GLY B 1 370 ? -23.449 7.365   32.917  1.00 33.23 ? 417 GLY B CA  1 
ATOM   5584 C  C   . GLY B 1 370 ? -24.287 6.728   31.843  1.00 36.10 ? 417 GLY B C   1 
ATOM   5585 O  O   . GLY B 1 370 ? -23.636 6.155   30.964  1.00 39.59 ? 417 GLY B O   1 
HETATM 5586 C  CHA . HEM C 2 .   ? 9.551   -7.545  -1.474  1.00 10.73 ? 501 HEM A CHA 1 
HETATM 5587 C  CHB . HEM C 2 .   ? 7.593   -4.219  1.437   1.00 11.10 ? 501 HEM A CHB 1 
HETATM 5588 C  CHC . HEM C 2 .   ? 11.344  -1.308  0.644   1.00 11.32 ? 501 HEM A CHC 1 
HETATM 5589 C  CHD . HEM C 2 .   ? 13.325  -4.691  -2.172  1.00 11.69 ? 501 HEM A CHD 1 
HETATM 5590 C  C1A . HEM C 2 .   ? 8.649   -6.908  -0.633  1.00 10.53 ? 501 HEM A C1A 1 
HETATM 5591 C  C2A . HEM C 2 .   ? 7.412   -7.453  -0.175  1.00 10.12 ? 501 HEM A C2A 1 
HETATM 5592 C  C3A . HEM C 2 .   ? 6.841   -6.523  0.612   1.00 11.32 ? 501 HEM A C3A 1 
HETATM 5593 C  C4A . HEM C 2 .   ? 7.757   -5.403  0.668   1.00 10.27 ? 501 HEM A C4A 1 
HETATM 5594 C  CMA . HEM C 2 .   ? 5.537   -6.541  1.331   1.00 11.44 ? 501 HEM A CMA 1 
HETATM 5595 C  CAA . HEM C 2 .   ? 6.827   -8.782  -0.596  1.00 11.37 ? 501 HEM A CAA 1 
HETATM 5596 C  CBA . HEM C 2 .   ? 7.275   -9.966  0.279   1.00 11.23 ? 501 HEM A CBA 1 
HETATM 5597 C  CGA . HEM C 2 .   ? 8.687   -10.310 0.132   1.00 12.19 ? 501 HEM A CGA 1 
HETATM 5598 O  O1A . HEM C 2 .   ? 9.519   -9.862  0.955   1.00 13.03 ? 501 HEM A O1A 1 
HETATM 5599 O  O2A . HEM C 2 .   ? 9.048   -11.072 -0.811  1.00 12.57 ? 501 HEM A O2A 1 
HETATM 5600 C  C1B . HEM C 2 .   ? 8.473   -3.137  1.477   1.00 10.84 ? 501 HEM A C1B 1 
HETATM 5601 C  C2B . HEM C 2 .   ? 8.242   -1.961  2.282   1.00 11.23 ? 501 HEM A C2B 1 
HETATM 5602 C  C3B . HEM C 2 .   ? 9.284   -1.141  2.067   1.00 11.65 ? 501 HEM A C3B 1 
HETATM 5603 C  C4B . HEM C 2 .   ? 10.174  -1.815  1.115   1.00 11.09 ? 501 HEM A C4B 1 
HETATM 5604 C  CMB . HEM C 2 .   ? 7.075   -1.703  3.160   1.00 12.87 ? 501 HEM A CMB 1 
HETATM 5605 C  CAB . HEM C 2 .   ? 9.612   0.192   2.630   1.00 13.76 ? 501 HEM A CAB 1 
HETATM 5606 C  CBB . HEM C 2 .   ? 9.067   0.707   3.661   1.00 15.30 ? 501 HEM A CBB 1 
HETATM 5607 C  C1C . HEM C 2 .   ? 12.214  -1.931  -0.222  1.00 11.14 ? 501 HEM A C1C 1 
HETATM 5608 C  C2C . HEM C 2 .   ? 13.431  -1.428  -0.727  1.00 12.11 ? 501 HEM A C2C 1 
HETATM 5609 C  C3C . HEM C 2 .   ? 14.014  -2.378  -1.536  1.00 11.56 ? 501 HEM A C3C 1 
HETATM 5610 C  C4C . HEM C 2 .   ? 13.100  -3.484  -1.507  1.00 10.99 ? 501 HEM A C4C 1 
HETATM 5611 C  CMC . HEM C 2 .   ? 13.981  -0.089  -0.370  1.00 14.18 ? 501 HEM A CMC 1 
HETATM 5612 C  CAC . HEM C 2 .   ? 15.251  -2.371  -2.336  1.00 13.77 ? 501 HEM A CAC 1 
HETATM 5613 C  CBC . HEM C 2 .   ? 15.777  -1.295  -2.767  1.00 16.90 ? 501 HEM A CBC 1 
HETATM 5614 C  C1D . HEM C 2 .   ? 12.447  -5.793  -2.154  1.00 11.39 ? 501 HEM A C1D 1 
HETATM 5615 C  C2D . HEM C 2 .   ? 12.763  -7.060  -2.825  1.00 11.32 ? 501 HEM A C2D 1 
HETATM 5616 C  C3D . HEM C 2 .   ? 11.693  -7.842  -2.642  1.00 10.55 ? 501 HEM A C3D 1 
HETATM 5617 C  C4D . HEM C 2 .   ? 10.759  -7.081  -1.847  1.00 10.06 ? 501 HEM A C4D 1 
HETATM 5618 C  CMD . HEM C 2 .   ? 14.062  -7.337  -3.552  1.00 13.13 ? 501 HEM A CMD 1 
HETATM 5619 C  CAD . HEM C 2 .   ? 11.558  -9.242  -3.140  1.00 11.89 ? 501 HEM A CAD 1 
HETATM 5620 C  CBD . HEM C 2 .   ? 10.977  -9.298  -4.577  1.00 13.08 ? 501 HEM A CBD 1 
HETATM 5621 C  CGD . HEM C 2 .   ? 10.952  -10.680 -5.114  1.00 12.47 ? 501 HEM A CGD 1 
HETATM 5622 O  O1D . HEM C 2 .   ? 9.855   -11.274 -5.158  1.00 13.32 ? 501 HEM A O1D 1 
HETATM 5623 O  O2D . HEM C 2 .   ? 12.041  -11.201 -5.430  1.00 13.64 ? 501 HEM A O2D 1 
HETATM 5624 N  NA  . HEM C 2 .   ? 8.851   -5.651  -0.055  1.00 10.35 ? 501 HEM A NA  1 
HETATM 5625 N  NB  . HEM C 2 .   ? 9.606   -3.016  0.820   1.00 10.99 ? 501 HEM A NB  1 
HETATM 5626 N  NC  . HEM C 2 .   ? 12.039  -3.195  -0.721  1.00 10.78 ? 501 HEM A NC  1 
HETATM 5627 N  ND  . HEM C 2 .   ? 11.275  -5.855  -1.564  1.00 10.51 ? 501 HEM A ND  1 
HETATM 5628 FE FE  . HEM C 2 .   ? 10.373  -4.411  -0.492  1.00 10.77 ? 501 HEM A FE  1 
HETATM 5629 C  CHA . HEM D 2 .   ? 13.332  1.199   45.067  1.00 11.35 ? 501 HEM B CHA 1 
HETATM 5630 C  CHB . HEM D 2 .   ? 15.762  2.482   41.158  1.00 12.89 ? 501 HEM B CHB 1 
HETATM 5631 C  CHC . HEM D 2 .   ? 12.876  6.355   40.620  1.00 10.50 ? 501 HEM B CHC 1 
HETATM 5632 C  CHD . HEM D 2 .   ? 10.315  4.892   44.389  1.00 11.01 ? 501 HEM B CHD 1 
HETATM 5633 C  C1A . HEM D 2 .   ? 14.277  1.242   44.067  1.00 11.89 ? 501 HEM B C1A 1 
HETATM 5634 C  C2A . HEM D 2 .   ? 15.362  0.318   43.911  1.00 11.53 ? 501 HEM B C2A 1 
HETATM 5635 C  C3A . HEM D 2 .   ? 16.044  0.672   42.784  1.00 12.41 ? 501 HEM B C3A 1 
HETATM 5636 C  C4A . HEM D 2 .   ? 15.381  1.840   42.283  1.00 12.11 ? 501 HEM B C4A 1 
HETATM 5637 C  CMA . HEM D 2 .   ? 17.259  0.015   42.235  1.00 13.32 ? 501 HEM B CMA 1 
HETATM 5638 C  CAA . HEM D 2 .   ? 15.673  -0.829  44.848  1.00 11.97 ? 501 HEM B CAA 1 
HETATM 5639 C  CBA . HEM D 2 .   ? 15.009  -2.134  44.519  1.00 12.58 ? 501 HEM B CBA 1 
HETATM 5640 C  CGA . HEM D 2 .   ? 13.558  -2.123  44.649  1.00 12.85 ? 501 HEM B CGA 1 
HETATM 5641 O  O1A . HEM D 2 .   ? 12.878  -1.901  43.612  1.00 14.58 ? 501 HEM B O1A 1 
HETATM 5642 O  O2A . HEM D 2 .   ? 13.069  -2.324  45.755  1.00 13.76 ? 501 HEM B O2A 1 
HETATM 5643 C  C1B . HEM D 2 .   ? 15.148  3.657   40.667  1.00 12.31 ? 501 HEM B C1B 1 
HETATM 5644 C  C2B . HEM D 2 .   ? 15.578  4.324   39.468  1.00 13.13 ? 501 HEM B C2B 1 
HETATM 5645 C  C3B . HEM D 2 .   ? 14.812  5.426   39.298  1.00 11.70 ? 501 HEM B C3B 1 
HETATM 5646 C  C4B . HEM D 2 .   ? 13.849  5.419   40.392  1.00 11.12 ? 501 HEM B C4B 1 
HETATM 5647 C  CMB . HEM D 2 .   ? 16.727  3.938   38.566  1.00 15.04 ? 501 HEM B CMB 1 
HETATM 5648 C  CAB . HEM D 2 .   ? 14.800  6.472   38.259  1.00 13.43 ? 501 HEM B CAB 1 
HETATM 5649 C  CBB . HEM D 2 .   ? 15.354  6.360   37.100  1.00 16.01 ? 501 HEM B CBB 1 
HETATM 5650 C  C1C . HEM D 2 .   ? 11.935  6.326   41.608  1.00 10.89 ? 501 HEM B C1C 1 
HETATM 5651 C  C2C . HEM D 2 .   ? 10.871  7.229   41.780  1.00 10.71 ? 501 HEM B C2C 1 
HETATM 5652 C  C3C . HEM D 2 .   ? 10.160  6.855   42.865  1.00 11.25 ? 501 HEM B C3C 1 
HETATM 5653 C  C4C . HEM D 2 .   ? 10.778  5.635   43.341  1.00 11.53 ? 501 HEM B C4C 1 
HETATM 5654 C  CMC . HEM D 2 .   ? 10.616  8.410   40.887  1.00 12.74 ? 501 HEM B CMC 1 
HETATM 5655 C  CAC . HEM D 2 .   ? 8.968   7.440   43.504  1.00 12.01 ? 501 HEM B CAC 1 
HETATM 5656 C  CBC . HEM D 2 .   ? 8.593   8.679   43.504  1.00 14.96 ? 501 HEM B CBC 1 
HETATM 5657 C  C1D . HEM D 2 .   ? 10.902  3.713   44.849  1.00 11.22 ? 501 HEM B C1D 1 
HETATM 5658 C  C2D . HEM D 2 .   ? 10.389  2.914   45.957  1.00 11.46 ? 501 HEM B C2D 1 
HETATM 5659 C  C3D . HEM D 2 .   ? 11.253  1.897   46.159  1.00 11.52 ? 501 HEM B C3D 1 
HETATM 5660 C  C4D . HEM D 2 .   ? 12.283  2.062   45.165  1.00 11.56 ? 501 HEM B C4D 1 
HETATM 5661 C  CMD . HEM D 2 .   ? 9.125   3.235   46.671  1.00 13.29 ? 501 HEM B CMD 1 
HETATM 5662 C  CAD . HEM D 2 .   ? 11.091  0.793   47.168  1.00 11.87 ? 501 HEM B CAD 1 
HETATM 5663 C  CBD . HEM D 2 .   ? 11.698  1.209   48.474  1.00 13.40 ? 501 HEM B CBD 1 
HETATM 5664 C  CGD . HEM D 2 .   ? 11.454  0.136   49.498  1.00 13.88 ? 501 HEM B CGD 1 
HETATM 5665 O  O1D . HEM D 2 .   ? 12.413  -0.577  49.853  1.00 14.37 ? 501 HEM B O1D 1 
HETATM 5666 O  O2D . HEM D 2 .   ? 10.312  -0.003  49.969  1.00 15.50 ? 501 HEM B O2D 1 
HETATM 5667 N  NA  . HEM D 2 .   ? 14.309  2.170   43.046  1.00 11.34 ? 501 HEM B NA  1 
HETATM 5668 N  NB  . HEM D 2 .   ? 14.151  4.354   41.166  1.00 11.57 ? 501 HEM B NB  1 
HETATM 5669 N  NC  . HEM D 2 .   ? 11.869  5.353   42.564  1.00 10.87 ? 501 HEM B NC  1 
HETATM 5670 N  ND  . HEM D 2 .   ? 12.039  3.151   44.399  1.00 10.68 ? 501 HEM B ND  1 
HETATM 5671 FE FE  . HEM D 2 .   ? 13.205  3.844   42.932  1.00 11.07 ? 501 HEM B FE  1 
HETATM 5672 O  O   . HOH E 3 .   ? 0.508   10.370  5.894   1.00 36.70 ? 601 HOH A O   1 
HETATM 5673 O  O   . HOH E 3 .   ? 1.166   -20.549 3.084   1.00 33.75 ? 602 HOH A O   1 
HETATM 5674 O  O   . HOH E 3 .   ? -7.084  -2.726  -9.224  1.00 42.75 ? 603 HOH A O   1 
HETATM 5675 O  O   . HOH E 3 .   ? 12.067  -11.813 21.726  1.00 31.85 ? 604 HOH A O   1 
HETATM 5676 O  O   . HOH E 3 .   ? 8.440   -15.801 -11.027 1.00 36.28 ? 605 HOH A O   1 
HETATM 5677 O  O   . HOH E 3 .   ? -10.537 6.185   2.684   1.00 39.85 ? 606 HOH A O   1 
HETATM 5678 O  O   . HOH E 3 .   ? 17.330  -2.787  -12.708 1.00 29.76 ? 607 HOH A O   1 
HETATM 5679 O  O   . HOH E 3 .   ? 8.231   -21.504 -4.700  1.00 34.88 ? 608 HOH A O   1 
HETATM 5680 O  O   . HOH E 3 .   ? 13.256  -13.976 15.647  1.00 34.24 ? 609 HOH A O   1 
HETATM 5681 O  O   . HOH E 3 .   ? 23.711  -9.063  -4.777  1.00 24.74 ? 610 HOH A O   1 
HETATM 5682 O  O   . HOH E 3 .   ? 24.644  13.083  14.036  1.00 36.18 ? 611 HOH A O   1 
HETATM 5683 O  O   . HOH E 3 .   ? -0.796  -6.023  -15.111 1.00 40.34 ? 612 HOH A O   1 
HETATM 5684 O  O   . HOH E 3 .   ? 37.882  -15.076 -6.020  1.00 44.77 ? 613 HOH A O   1 
HETATM 5685 O  O   . HOH E 3 .   ? 39.112  -7.565  8.334   1.00 27.69 ? 614 HOH A O   1 
HETATM 5686 O  O   . HOH E 3 .   ? 48.083  9.087   20.140  1.00 41.91 ? 615 HOH A O   1 
HETATM 5687 O  O   . HOH E 3 .   ? 36.185  11.267  21.124  1.00 46.06 ? 616 HOH A O   1 
HETATM 5688 O  O   . HOH E 3 .   ? 37.675  -20.779 14.933  1.00 40.24 ? 617 HOH A O   1 
HETATM 5689 O  O   . HOH E 3 .   ? 32.414  -6.719  -6.998  1.00 35.17 ? 618 HOH A O   1 
HETATM 5690 O  O   . HOH E 3 .   ? 17.358  -12.685 27.553  1.00 25.62 ? 619 HOH A O   1 
HETATM 5691 O  O   . HOH E 3 .   ? 10.755  2.057   -12.503 1.00 28.68 ? 620 HOH A O   1 
HETATM 5692 O  O   . HOH E 3 .   ? -5.047  0.350   -7.441  1.00 36.57 ? 621 HOH A O   1 
HETATM 5693 O  O   . HOH E 3 .   ? 10.200  -8.168  -15.272 1.00 35.79 ? 622 HOH A O   1 
HETATM 5694 O  O   . HOH E 3 .   ? 36.495  0.041   34.732  1.00 43.22 ? 623 HOH A O   1 
HETATM 5695 O  O   . HOH E 3 .   ? 25.561  0.709   34.996  1.00 34.20 ? 624 HOH A O   1 
HETATM 5696 O  O   . HOH E 3 .   ? 39.740  6.114   -1.504  1.00 38.80 ? 625 HOH A O   1 
HETATM 5697 O  O   . HOH E 3 .   ? 35.326  11.291  11.871  1.00 40.22 ? 626 HOH A O   1 
HETATM 5698 O  O   . HOH E 3 .   ? 25.259  -17.227 12.139  1.00 26.45 ? 627 HOH A O   1 
HETATM 5699 O  O   . HOH E 3 .   ? 25.021  -13.211 34.276  1.00 37.58 ? 628 HOH A O   1 
HETATM 5700 O  O   . HOH E 3 .   ? 3.092   9.687   11.060  1.00 27.35 ? 629 HOH A O   1 
HETATM 5701 O  O   . HOH E 3 .   ? 16.875  -15.828 22.401  1.00 27.12 ? 630 HOH A O   1 
HETATM 5702 O  O   . HOH E 3 .   ? 31.448  -14.963 -3.263  1.00 25.87 ? 631 HOH A O   1 
HETATM 5703 O  O   . HOH E 3 .   ? 14.981  4.801   -12.618 1.00 40.69 ? 632 HOH A O   1 
HETATM 5704 O  O   . HOH E 3 .   ? 4.893   -17.211 6.722   1.00 20.63 ? 633 HOH A O   1 
HETATM 5705 O  O   . HOH E 3 .   ? 32.602  -7.646  -4.201  1.00 21.23 ? 634 HOH A O   1 
HETATM 5706 O  O   . HOH E 3 .   ? 11.006  -3.806  3.769   1.00 15.20 ? 635 HOH A O   1 
HETATM 5707 O  O   . HOH E 3 .   ? 38.428  -2.143  -5.085  1.00 41.60 ? 636 HOH A O   1 
HETATM 5708 O  O   . HOH E 3 .   ? 24.569  -8.431  14.162  1.00 12.33 ? 637 HOH A O   1 
HETATM 5709 O  O   . HOH E 3 .   ? -3.484  5.738   11.070  1.00 19.21 ? 638 HOH A O   1 
HETATM 5710 O  O   . HOH E 3 .   ? 34.771  -6.588  -2.947  1.00 22.25 ? 639 HOH A O   1 
HETATM 5711 O  O   . HOH E 3 .   ? 6.932   -3.073  -14.705 1.00 33.12 ? 640 HOH A O   1 
HETATM 5712 O  O   . HOH E 3 .   ? 15.366  -10.088 29.979  1.00 20.60 ? 641 HOH A O   1 
HETATM 5713 O  O   . HOH E 3 .   ? 7.940   -11.034 -3.265  1.00 13.18 ? 642 HOH A O   1 
HETATM 5714 O  O   . HOH E 3 .   ? 35.043  -1.934  29.843  1.00 32.87 ? 643 HOH A O   1 
HETATM 5715 O  O   . HOH E 3 .   ? 32.197  -1.018  29.284  1.00 24.74 ? 644 HOH A O   1 
HETATM 5716 O  O   . HOH E 3 .   ? -6.621  10.846  6.599   1.00 20.27 ? 645 HOH A O   1 
HETATM 5717 O  O   . HOH E 3 .   ? 29.800  -17.664 13.286  1.00 37.52 ? 646 HOH A O   1 
HETATM 5718 O  O   . HOH E 3 .   ? 25.775  9.163   -1.409  1.00 45.96 ? 647 HOH A O   1 
HETATM 5719 O  O   . HOH E 3 .   ? -0.185  -18.011 5.610   1.00 44.13 ? 648 HOH A O   1 
HETATM 5720 O  O   . HOH E 3 .   ? 14.271  -11.738 -3.995  1.00 16.02 ? 649 HOH A O   1 
HETATM 5721 O  O   . HOH E 3 .   ? 32.458  -20.679 15.006  1.00 33.54 ? 650 HOH A O   1 
HETATM 5722 O  O   . HOH E 3 .   ? 30.571  -4.628  -10.022 1.00 47.45 ? 651 HOH A O   1 
HETATM 5723 O  O   . HOH E 3 .   ? 36.910  9.796   8.968   1.00 39.93 ? 652 HOH A O   1 
HETATM 5724 O  O   . HOH E 3 .   ? 43.839  -3.564  22.588  1.00 36.94 ? 653 HOH A O   1 
HETATM 5725 O  O   . HOH E 3 .   ? 21.426  -5.817  -12.727 1.00 42.96 ? 654 HOH A O   1 
HETATM 5726 O  O   . HOH E 3 .   ? 25.130  -7.553  25.753  1.00 15.75 ? 655 HOH A O   1 
HETATM 5727 O  O   . HOH E 3 .   ? 19.302  -18.363 8.449   1.00 21.52 ? 656 HOH A O   1 
HETATM 5728 O  O   . HOH E 3 .   ? 28.233  -2.996  36.723  1.00 18.07 ? 657 HOH A O   1 
HETATM 5729 O  O   . HOH E 3 .   ? -6.021  7.697   7.757   1.00 21.03 ? 658 HOH A O   1 
HETATM 5730 O  O   . HOH E 3 .   ? 32.937  8.945   -0.789  1.00 46.38 ? 659 HOH A O   1 
HETATM 5731 O  O   . HOH E 3 .   ? 12.308  -8.020  4.333   1.00 14.48 ? 660 HOH A O   1 
HETATM 5732 O  O   . HOH E 3 .   ? 14.265  8.102   -2.239  1.00 37.62 ? 661 HOH A O   1 
HETATM 5733 O  O   . HOH E 3 .   ? 9.856   2.184   -3.261  1.00 17.23 ? 662 HOH A O   1 
HETATM 5734 O  O   . HOH E 3 .   ? 7.579   -1.379  9.281   1.00 14.25 ? 663 HOH A O   1 
HETATM 5735 O  O   . HOH E 3 .   ? 28.499  7.406   0.969   1.00 37.58 ? 664 HOH A O   1 
HETATM 5736 O  O   . HOH E 3 .   ? 19.794  -8.010  33.650  1.00 20.44 ? 665 HOH A O   1 
HETATM 5737 O  O   . HOH E 3 .   ? 5.597   10.192  -1.190  1.00 33.17 ? 666 HOH A O   1 
HETATM 5738 O  O   . HOH E 3 .   ? 28.664  -16.853 20.906  1.00 26.32 ? 667 HOH A O   1 
HETATM 5739 O  O   . HOH E 3 .   ? -3.264  14.816  12.430  1.00 17.38 ? 668 HOH A O   1 
HETATM 5740 O  O   . HOH E 3 .   ? 0.216   -0.640  -8.189  1.00 23.24 ? 669 HOH A O   1 
HETATM 5741 O  O   . HOH E 3 .   ? 31.344  -10.036 13.954  1.00 14.15 ? 670 HOH A O   1 
HETATM 5742 O  O   . HOH E 3 .   ? 44.022  -15.731 13.697  1.00 36.29 ? 671 HOH A O   1 
HETATM 5743 O  O   . HOH E 3 .   ? 36.542  -15.283 5.018   1.00 35.50 ? 672 HOH A O   1 
HETATM 5744 O  O   . HOH E 3 .   ? 24.425  -11.894 30.093  1.00 26.83 ? 673 HOH A O   1 
HETATM 5745 O  O   . HOH E 3 .   ? -7.250  -10.342 -2.353  1.00 37.37 ? 674 HOH A O   1 
HETATM 5746 O  O   . HOH E 3 .   ? 48.050  -1.041  18.372  1.00 31.63 ? 675 HOH A O   1 
HETATM 5747 O  O   . HOH E 3 .   ? 24.385  6.935   1.852   1.00 28.02 ? 676 HOH A O   1 
HETATM 5748 O  O   . HOH E 3 .   ? -10.298 0.616   -4.489  1.00 34.75 ? 677 HOH A O   1 
HETATM 5749 O  O   . HOH E 3 .   ? 6.350   1.064   -13.441 1.00 31.50 ? 678 HOH A O   1 
HETATM 5750 O  O   . HOH E 3 .   ? 35.935  -17.435 30.578  1.00 31.97 ? 679 HOH A O   1 
HETATM 5751 O  O   . HOH E 3 .   ? 16.047  -8.035  -6.137  1.00 16.27 ? 680 HOH A O   1 
HETATM 5752 O  O   . HOH E 3 .   ? 37.267  -8.852  10.478  1.00 26.82 ? 681 HOH A O   1 
HETATM 5753 O  O   . HOH E 3 .   ? 34.575  9.630   22.495  1.00 35.75 ? 682 HOH A O   1 
HETATM 5754 O  O   . HOH E 3 .   ? -6.322  -10.439 1.452   1.00 32.18 ? 683 HOH A O   1 
HETATM 5755 O  O   . HOH E 3 .   ? 3.496   10.943  7.030   1.00 31.00 ? 684 HOH A O   1 
HETATM 5756 O  O   . HOH E 3 .   ? 17.791  -0.368  -12.573 1.00 28.35 ? 685 HOH A O   1 
HETATM 5757 O  O   . HOH E 3 .   ? 36.751  7.658   1.111   1.00 33.77 ? 686 HOH A O   1 
HETATM 5758 O  O   . HOH E 3 .   ? 31.330  -6.148  44.442  1.00 40.05 ? 687 HOH A O   1 
HETATM 5759 O  O   . HOH E 3 .   ? 19.766  12.634  -1.767  1.00 34.29 ? 688 HOH A O   1 
HETATM 5760 O  O   . HOH E 3 .   ? 26.167  -14.259 8.878   1.00 14.38 ? 689 HOH A O   1 
HETATM 5761 O  O   . HOH E 3 .   ? 33.072  -13.959 12.482  1.00 17.25 ? 690 HOH A O   1 
HETATM 5762 O  O   . HOH E 3 .   ? 20.605  8.423   -1.921  1.00 22.52 ? 691 HOH A O   1 
HETATM 5763 O  O   . HOH E 3 .   ? -3.520  9.872   15.132  1.00 23.03 ? 692 HOH A O   1 
HETATM 5764 O  O   . HOH E 3 .   ? 37.282  -12.008 25.306  1.00 17.46 ? 693 HOH A O   1 
HETATM 5765 O  O   . HOH E 3 .   ? 49.654  4.889   20.137  1.00 23.83 ? 694 HOH A O   1 
HETATM 5766 O  O   . HOH E 3 .   ? 25.516  -10.205 26.412  1.00 15.29 ? 695 HOH A O   1 
HETATM 5767 O  O   . HOH E 3 .   ? 24.960  -15.089 20.783  1.00 14.73 ? 696 HOH A O   1 
HETATM 5768 O  O   . HOH E 3 .   ? 10.115  -15.979 -8.876  1.00 21.90 ? 697 HOH A O   1 
HETATM 5769 O  O   . HOH E 3 .   ? -2.725  -6.462  -7.852  1.00 22.17 ? 698 HOH A O   1 
HETATM 5770 O  O   . HOH E 3 .   ? 30.931  7.214   5.500   1.00 28.77 ? 699 HOH A O   1 
HETATM 5771 O  O   . HOH E 3 .   ? 14.818  -14.585 -3.676  1.00 27.60 ? 700 HOH A O   1 
HETATM 5772 O  O   . HOH E 3 .   ? 28.166  -19.100 26.696  1.00 41.73 ? 701 HOH A O   1 
HETATM 5773 O  O   . HOH E 3 .   ? 12.332  2.522   -2.042  1.00 20.04 ? 702 HOH A O   1 
HETATM 5774 O  O   . HOH E 3 .   ? 42.015  -11.226 19.483  1.00 42.82 ? 703 HOH A O   1 
HETATM 5775 O  O   . HOH E 3 .   ? 34.964  -1.939  40.264  1.00 25.53 ? 704 HOH A O   1 
HETATM 5776 O  O   . HOH E 3 .   ? 17.754  -14.307 29.683  1.00 28.55 ? 705 HOH A O   1 
HETATM 5777 O  O   . HOH E 3 .   ? 23.012  -8.884  -7.587  1.00 26.93 ? 706 HOH A O   1 
HETATM 5778 O  O   . HOH E 3 .   ? 33.046  5.134   31.416  1.00 33.36 ? 707 HOH A O   1 
HETATM 5779 O  O   . HOH E 3 .   ? -8.557  -6.750  -2.676  1.00 38.40 ? 708 HOH A O   1 
HETATM 5780 O  O   . HOH E 3 .   ? 34.782  5.194   28.955  1.00 49.75 ? 709 HOH A O   1 
HETATM 5781 O  O   . HOH E 3 .   ? 15.096  -22.228 10.837  1.00 51.43 ? 710 HOH A O   1 
HETATM 5782 O  O   . HOH E 3 .   ? 10.977  -15.953 9.614   1.00 20.23 ? 711 HOH A O   1 
HETATM 5783 O  O   . HOH E 3 .   ? 6.773   -16.251 -3.423  1.00 17.33 ? 712 HOH A O   1 
HETATM 5784 O  O   . HOH E 3 .   ? 27.397  -14.014 17.826  1.00 14.74 ? 713 HOH A O   1 
HETATM 5785 O  O   . HOH E 3 .   ? 17.722  -14.652 -7.395  1.00 26.01 ? 714 HOH A O   1 
HETATM 5786 O  O   . HOH E 3 .   ? 32.140  6.179   22.178  1.00 28.64 ? 715 HOH A O   1 
HETATM 5787 O  O   . HOH E 3 .   ? 9.928   -16.600 6.569   1.00 16.49 ? 716 HOH A O   1 
HETATM 5788 O  O   . HOH E 3 .   ? 4.343   -12.461 1.141   1.00 14.73 ? 717 HOH A O   1 
HETATM 5789 O  O   . HOH E 3 .   ? 14.706  5.483   -7.515  1.00 24.70 ? 718 HOH A O   1 
HETATM 5790 O  O   . HOH E 3 .   ? 11.661  -16.256 3.906   1.00 21.77 ? 719 HOH A O   1 
HETATM 5791 O  O   . HOH E 3 .   ? 27.134  -9.495  28.701  1.00 19.65 ? 720 HOH A O   1 
HETATM 5792 O  O   . HOH E 3 .   ? 12.108  8.759   -0.685  1.00 21.86 ? 721 HOH A O   1 
HETATM 5793 O  O   . HOH E 3 .   ? 32.618  -13.175 -12.078 1.00 57.82 ? 722 HOH A O   1 
HETATM 5794 O  O   . HOH E 3 .   ? 5.347   8.119   10.197  1.00 22.59 ? 723 HOH A O   1 
HETATM 5795 O  O   . HOH E 3 .   ? 11.182  -5.295  1.480   1.00 12.75 ? 724 HOH A O   1 
HETATM 5796 O  O   . HOH E 3 .   ? -4.429  7.052   0.365   1.00 23.23 ? 725 HOH A O   1 
HETATM 5797 O  O   . HOH E 3 .   ? -4.495  10.501  -0.667  1.00 28.64 ? 726 HOH A O   1 
HETATM 5798 O  O   . HOH E 3 .   ? 16.387  10.465  9.392   1.00 30.76 ? 727 HOH A O   1 
HETATM 5799 O  O   . HOH E 3 .   ? 8.870   8.672   -1.869  1.00 33.23 ? 728 HOH A O   1 
HETATM 5800 O  O   . HOH E 3 .   ? 12.531  -13.852 10.510  1.00 15.27 ? 729 HOH A O   1 
HETATM 5801 O  O   . HOH E 3 .   ? 25.926  -7.087  32.361  1.00 16.77 ? 730 HOH A O   1 
HETATM 5802 O  O   . HOH E 3 .   ? 37.418  -11.083 30.392  1.00 29.43 ? 731 HOH A O   1 
HETATM 5803 O  O   . HOH E 3 .   ? 36.832  -8.516  -3.012  1.00 24.24 ? 732 HOH A O   1 
HETATM 5804 O  O   . HOH E 3 .   ? 15.566  -9.944  -1.221  1.00 15.78 ? 733 HOH A O   1 
HETATM 5805 O  O   . HOH E 3 .   ? 25.125  0.598   -10.569 1.00 42.46 ? 734 HOH A O   1 
HETATM 5806 O  O   . HOH E 3 .   ? 0.554   4.659   -5.420  1.00 24.79 ? 735 HOH A O   1 
HETATM 5807 O  O   . HOH E 3 .   ? 3.438   -9.743  1.383   1.00 14.06 ? 736 HOH A O   1 
HETATM 5808 O  O   . HOH E 3 .   ? 31.636  -11.219 6.876   1.00 15.77 ? 737 HOH A O   1 
HETATM 5809 O  O   . HOH E 3 .   ? 29.986  12.815  14.966  1.00 43.83 ? 738 HOH A O   1 
HETATM 5810 O  O   . HOH E 3 .   ? 11.870  5.304   -3.809  1.00 33.63 ? 739 HOH A O   1 
HETATM 5811 O  O   . HOH E 3 .   ? -3.159  -6.919  -10.608 1.00 29.34 ? 740 HOH A O   1 
HETATM 5812 O  O   . HOH E 3 .   ? 18.081  14.306  0.396   1.00 27.81 ? 741 HOH A O   1 
HETATM 5813 O  O   . HOH E 3 .   ? 7.934   -8.299  13.729  1.00 28.98 ? 742 HOH A O   1 
HETATM 5814 O  O   . HOH E 3 .   ? 14.698  14.275  6.756   1.00 31.65 ? 743 HOH A O   1 
HETATM 5815 O  O   . HOH E 3 .   ? 30.121  9.677   7.004   1.00 40.51 ? 744 HOH A O   1 
HETATM 5816 O  O   . HOH E 3 .   ? 25.762  12.637  6.330   1.00 44.91 ? 745 HOH A O   1 
HETATM 5817 O  O   . HOH E 3 .   ? 5.468   14.028  21.496  1.00 42.66 ? 746 HOH A O   1 
HETATM 5818 O  O   . HOH E 3 .   ? 14.846  -15.292 9.907   1.00 13.68 ? 747 HOH A O   1 
HETATM 5819 O  O   . HOH E 3 .   ? 29.265  -16.592 10.739  1.00 25.84 ? 748 HOH A O   1 
HETATM 5820 O  O   . HOH E 3 .   ? 31.470  5.629   -5.232  1.00 38.62 ? 749 HOH A O   1 
HETATM 5821 O  O   . HOH E 3 .   ? -4.139  -9.523  -13.156 1.00 36.88 ? 750 HOH A O   1 
HETATM 5822 O  O   . HOH E 3 .   ? 25.814  -7.637  -5.502  1.00 23.33 ? 751 HOH A O   1 
HETATM 5823 O  O   . HOH E 3 .   ? 16.032  -2.936  20.161  1.00 24.48 ? 752 HOH A O   1 
HETATM 5824 O  O   . HOH E 3 .   ? 19.950  -7.058  10.422  1.00 13.70 ? 753 HOH A O   1 
HETATM 5825 O  O   . HOH E 3 .   ? 9.933   -2.446  23.146  1.00 31.29 ? 754 HOH A O   1 
HETATM 5826 O  O   . HOH E 3 .   ? 6.943   11.751  0.759   1.00 32.70 ? 755 HOH A O   1 
HETATM 5827 O  O   . HOH E 3 .   ? 28.764  5.300   6.087   1.00 18.76 ? 756 HOH A O   1 
HETATM 5828 O  O   . HOH E 3 .   ? 13.173  -17.643 12.374  1.00 34.81 ? 757 HOH A O   1 
HETATM 5829 O  O   . HOH E 3 .   ? -1.981  -21.042 -6.296  1.00 30.05 ? 758 HOH A O   1 
HETATM 5830 O  O   . HOH E 3 .   ? 37.256  -15.870 -3.029  1.00 42.48 ? 759 HOH A O   1 
HETATM 5831 O  O   . HOH E 3 .   ? 27.635  -17.858 13.350  1.00 28.00 ? 760 HOH A O   1 
HETATM 5832 O  O   . HOH E 3 .   ? 14.973  -16.207 13.733  1.00 26.54 ? 761 HOH A O   1 
HETATM 5833 O  O   . HOH E 3 .   ? 30.454  -19.941 27.909  1.00 25.83 ? 762 HOH A O   1 
HETATM 5834 O  O   . HOH E 3 .   ? 30.400  -9.914  36.418  1.00 28.32 ? 763 HOH A O   1 
HETATM 5835 O  O   . HOH E 3 .   ? 33.390  -15.732 25.515  1.00 28.72 ? 764 HOH A O   1 
HETATM 5836 O  O   . HOH E 3 .   ? 37.429  -5.818  25.965  1.00 27.06 ? 765 HOH A O   1 
HETATM 5837 O  O   . HOH E 3 .   ? 26.760  -12.270 32.426  1.00 31.73 ? 766 HOH A O   1 
HETATM 5838 O  O   . HOH E 3 .   ? 1.350   -13.403 -9.557  1.00 17.93 ? 767 HOH A O   1 
HETATM 5839 O  O   . HOH E 3 .   ? 18.103  -19.805 15.762  1.00 38.49 ? 768 HOH A O   1 
HETATM 5840 O  O   . HOH E 3 .   ? 31.451  -15.863 21.795  1.00 26.74 ? 769 HOH A O   1 
HETATM 5841 O  O   . HOH E 3 .   ? 1.180   -10.120 3.215   1.00 14.43 ? 770 HOH A O   1 
HETATM 5842 O  O   . HOH E 3 .   ? 34.783  3.152   -3.800  1.00 38.66 ? 771 HOH A O   1 
HETATM 5843 O  O   . HOH E 3 .   ? 28.360  -11.876 16.273  1.00 14.11 ? 772 HOH A O   1 
HETATM 5844 O  O   . HOH E 3 .   ? 7.868   -8.093  17.435  1.00 28.31 ? 773 HOH A O   1 
HETATM 5845 O  O   . HOH E 3 .   ? 30.322  -12.626 14.224  1.00 13.84 ? 774 HOH A O   1 
HETATM 5846 O  O   . HOH E 3 .   ? 15.518  -4.668  4.926   1.00 17.14 ? 775 HOH A O   1 
HETATM 5847 O  O   . HOH E 3 .   ? 16.337  -9.830  -3.985  1.00 14.47 ? 776 HOH A O   1 
HETATM 5848 O  O   . HOH E 3 .   ? -0.334  -14.326 9.085   1.00 40.75 ? 777 HOH A O   1 
HETATM 5849 O  O   . HOH E 3 .   ? 36.174  -8.011  27.437  1.00 21.54 ? 778 HOH A O   1 
HETATM 5850 O  O   . HOH E 3 .   ? -4.102  -0.146  6.706   1.00 21.53 ? 779 HOH A O   1 
HETATM 5851 O  O   . HOH E 3 .   ? 32.805  -18.981 17.705  1.00 32.66 ? 780 HOH A O   1 
HETATM 5852 O  O   . HOH E 3 .   ? 10.404  -9.191  15.874  1.00 23.28 ? 781 HOH A O   1 
HETATM 5853 O  O   . HOH E 3 .   ? 6.868   -14.052 -13.600 1.00 23.44 ? 782 HOH A O   1 
HETATM 5854 O  O   . HOH E 3 .   ? 30.415  -12.920 33.143  1.00 32.73 ? 783 HOH A O   1 
HETATM 5855 O  O   . HOH E 3 .   ? -0.207  -5.371  -8.462  1.00 16.65 ? 784 HOH A O   1 
HETATM 5856 O  O   . HOH E 3 .   ? 35.567  -4.189  -4.433  1.00 27.84 ? 785 HOH A O   1 
HETATM 5857 O  O   . HOH E 3 .   ? 4.771   -10.338 12.252  1.00 26.96 ? 786 HOH A O   1 
HETATM 5858 O  O   . HOH E 3 .   ? 28.317  4.257   26.615  1.00 20.26 ? 787 HOH A O   1 
HETATM 5859 O  O   . HOH E 3 .   ? 7.237   -18.869 5.564   1.00 26.61 ? 788 HOH A O   1 
HETATM 5860 O  O   . HOH E 3 .   ? 43.784  -11.594 9.054   1.00 35.97 ? 789 HOH A O   1 
HETATM 5861 O  O   . HOH E 3 .   ? -2.214  -7.953  -5.472  1.00 21.10 ? 790 HOH A O   1 
HETATM 5862 O  O   . HOH E 3 .   ? 11.186  4.503   20.467  1.00 42.06 ? 791 HOH A O   1 
HETATM 5863 O  O   . HOH E 3 .   ? 34.890  -4.647  37.163  1.00 27.90 ? 792 HOH A O   1 
HETATM 5864 O  O   . HOH E 3 .   ? 8.580   -18.284 -2.928  1.00 24.43 ? 793 HOH A O   1 
HETATM 5865 O  O   . HOH E 3 .   ? 3.388   -20.825 1.368   1.00 21.61 ? 794 HOH A O   1 
HETATM 5866 O  O   . HOH E 3 .   ? 26.179  7.063   -0.032  1.00 30.38 ? 795 HOH A O   1 
HETATM 5867 O  O   . HOH E 3 .   ? 23.560  -11.643 27.554  1.00 20.76 ? 796 HOH A O   1 
HETATM 5868 O  O   . HOH E 3 .   ? 39.385  -12.286 23.455  1.00 20.16 ? 797 HOH A O   1 
HETATM 5869 O  O   . HOH E 3 .   ? 13.518  -16.567 1.185   1.00 25.48 ? 798 HOH A O   1 
HETATM 5870 O  O   . HOH E 3 .   ? 33.953  -15.845 32.793  1.00 38.84 ? 799 HOH A O   1 
HETATM 5871 O  O   . HOH E 3 .   ? 20.174  17.374  6.623   1.00 38.53 ? 800 HOH A O   1 
HETATM 5872 O  O   . HOH E 3 .   ? 33.526  -4.314  39.848  1.00 25.74 ? 801 HOH A O   1 
HETATM 5873 O  O   . HOH E 3 .   ? 5.425   -17.590 -12.539 1.00 26.20 ? 802 HOH A O   1 
HETATM 5874 O  O   . HOH E 3 .   ? 14.908  -15.209 -7.689  1.00 26.54 ? 803 HOH A O   1 
HETATM 5875 O  O   . HOH E 3 .   ? 9.322   11.795  -1.003  1.00 43.84 ? 804 HOH A O   1 
HETATM 5876 O  O   . HOH E 3 .   ? 40.834  -14.470 22.835  1.00 29.86 ? 805 HOH A O   1 
HETATM 5877 O  O   . HOH E 3 .   ? 1.313   9.418   8.787   1.00 25.10 ? 806 HOH A O   1 
HETATM 5878 O  O   . HOH E 3 .   ? 5.305   -12.831 -15.835 1.00 32.96 ? 807 HOH A O   1 
HETATM 5879 O  O   . HOH E 3 .   ? 11.781  -0.173  22.680  1.00 28.09 ? 808 HOH A O   1 
HETATM 5880 O  O   . HOH E 3 .   ? -1.550  7.838   14.503  1.00 19.05 ? 809 HOH A O   1 
HETATM 5881 O  O   . HOH E 3 .   ? 32.765  -18.309 26.581  1.00 23.81 ? 810 HOH A O   1 
HETATM 5882 O  O   . HOH E 3 .   ? -3.218  -13.552 -3.975  1.00 24.12 ? 811 HOH A O   1 
HETATM 5883 O  O   . HOH E 3 .   ? 20.569  9.159   16.328  1.00 22.27 ? 812 HOH A O   1 
HETATM 5884 O  O   . HOH E 3 .   ? 13.885  -10.398 4.357   1.00 13.57 ? 813 HOH A O   1 
HETATM 5885 O  O   . HOH E 3 .   ? 11.098  -3.450  -14.523 1.00 35.05 ? 814 HOH A O   1 
HETATM 5886 O  O   . HOH E 3 .   ? 14.763  -18.577 -0.098  1.00 37.43 ? 815 HOH A O   1 
HETATM 5887 O  O   . HOH E 3 .   ? 18.947  -17.464 -7.311  1.00 38.08 ? 816 HOH A O   1 
HETATM 5888 O  O   . HOH E 3 .   ? 12.920  6.662   -5.894  1.00 31.97 ? 817 HOH A O   1 
HETATM 5889 O  O   . HOH E 3 .   ? 30.957  -18.096 8.770   1.00 26.94 ? 818 HOH A O   1 
HETATM 5890 O  O   . HOH E 3 .   ? 32.882  -20.526 8.955   1.00 42.52 ? 819 HOH A O   1 
HETATM 5891 O  O   . HOH E 3 .   ? 18.125  -2.425  21.970  1.00 27.01 ? 820 HOH A O   1 
HETATM 5892 O  O   . HOH E 3 .   ? -4.525  -9.245  -4.635  1.00 29.72 ? 821 HOH A O   1 
HETATM 5893 O  O   . HOH E 3 .   ? 43.291  -5.787  -0.136  1.00 32.45 ? 822 HOH A O   1 
HETATM 5894 O  O   . HOH E 3 .   ? 27.566  6.396   3.910   1.00 24.83 ? 823 HOH A O   1 
HETATM 5895 O  O   . HOH E 3 .   ? 23.973  -21.874 23.391  1.00 47.74 ? 824 HOH A O   1 
HETATM 5896 O  O   . HOH E 3 .   ? 14.484  -16.518 3.734   1.00 24.93 ? 825 HOH A O   1 
HETATM 5897 O  O   . HOH E 3 .   ? 4.728   -19.835 4.026   1.00 34.58 ? 826 HOH A O   1 
HETATM 5898 O  O   . HOH E 3 .   ? 39.074  -10.537 10.503  1.00 36.84 ? 827 HOH A O   1 
HETATM 5899 O  O   . HOH E 3 .   ? -4.249  -15.894 -1.546  1.00 32.15 ? 828 HOH A O   1 
HETATM 5900 O  O   . HOH E 3 .   ? 11.736  1.419   17.332  1.00 22.05 ? 829 HOH A O   1 
HETATM 5901 O  O   . HOH E 3 .   ? 25.699  8.554   3.679   1.00 33.18 ? 830 HOH A O   1 
HETATM 5902 O  O   . HOH E 3 .   ? 8.047   11.972  19.998  1.00 39.71 ? 831 HOH A O   1 
HETATM 5903 O  O   . HOH E 3 .   ? 12.974  -5.263  5.123   1.00 27.79 ? 832 HOH A O   1 
HETATM 5904 O  O   . HOH E 3 .   ? 33.402  -15.377 0.663   1.00 35.35 ? 833 HOH A O   1 
HETATM 5905 O  O   . HOH E 3 .   ? 13.614  -16.585 -2.826  1.00 33.61 ? 834 HOH A O   1 
HETATM 5906 O  O   . HOH E 3 .   ? 8.310   -10.462 20.144  1.00 43.09 ? 835 HOH A O   1 
HETATM 5907 O  O   . HOH E 3 .   ? -4.942  -11.988 -5.167  1.00 34.82 ? 836 HOH A O   1 
HETATM 5908 O  O   . HOH E 3 .   ? 22.751  -19.423 9.263   1.00 38.43 ? 837 HOH A O   1 
HETATM 5909 O  O   . HOH E 3 .   ? 26.375  -9.639  31.395  1.00 23.08 ? 838 HOH A O   1 
HETATM 5910 O  O   . HOH E 3 .   ? 1.940   -16.885 8.267   1.00 50.84 ? 839 HOH A O   1 
HETATM 5911 O  O   . HOH E 3 .   ? 42.294  -6.315  23.743  1.00 38.99 ? 840 HOH A O   1 
HETATM 5912 O  O   . HOH E 3 .   ? 16.209  6.416   -9.815  1.00 30.59 ? 841 HOH A O   1 
HETATM 5913 O  O   . HOH E 3 .   ? 6.287   -12.862 12.907  1.00 41.03 ? 842 HOH A O   1 
HETATM 5914 O  O   . HOH E 3 .   ? 22.910  9.266   -0.752  1.00 36.40 ? 843 HOH A O   1 
HETATM 5915 O  O   . HOH E 3 .   ? 22.175  0.970   -11.987 1.00 45.41 ? 844 HOH A O   1 
HETATM 5916 O  O   . HOH E 3 .   ? 48.166  2.688   21.116  1.00 34.35 ? 845 HOH A O   1 
HETATM 5917 O  O   . HOH E 3 .   ? 37.887  -10.411 27.573  1.00 21.97 ? 846 HOH A O   1 
HETATM 5918 O  O   . HOH E 3 .   ? 26.766  -16.929 9.458   1.00 25.71 ? 847 HOH A O   1 
HETATM 5919 O  O   . HOH E 3 .   ? -1.543  1.116   -7.327  1.00 39.38 ? 848 HOH A O   1 
HETATM 5920 O  O   . HOH E 3 .   ? 41.889  -10.858 23.645  1.00 45.53 ? 849 HOH A O   1 
HETATM 5921 O  O   . HOH E 3 .   ? 13.430  13.206  8.908   1.00 48.27 ? 850 HOH A O   1 
HETATM 5922 O  O   . HOH E 3 .   ? 20.601  0.244   -13.079 1.00 43.49 ? 851 HOH A O   1 
HETATM 5923 O  O   . HOH E 3 .   ? 6.780   -16.383 -15.072 1.00 32.33 ? 852 HOH A O   1 
HETATM 5924 O  O   . HOH E 3 .   ? -5.665  7.386   10.557  1.00 27.01 ? 853 HOH A O   1 
HETATM 5925 O  O   . HOH E 3 .   ? 6.096   -14.911 -17.368 1.00 42.01 ? 854 HOH A O   1 
HETATM 5926 O  O   . HOH E 3 .   ? 4.939   -0.829  -18.261 1.00 46.91 ? 855 HOH A O   1 
HETATM 5927 O  O   . HOH E 3 .   ? -8.524  4.636   -10.337 1.00 55.53 ? 856 HOH A O   1 
HETATM 5928 O  O   . HOH F 3 .   ? 3.806   -13.245 22.238  1.00 32.81 ? 601 HOH B O   1 
HETATM 5929 O  O   . HOH F 3 .   ? -6.840  -3.589  52.929  1.00 41.03 ? 602 HOH B O   1 
HETATM 5930 O  O   . HOH F 3 .   ? 6.112   2.121   57.033  1.00 40.01 ? 603 HOH B O   1 
HETATM 5931 O  O   . HOH F 3 .   ? 13.257  -3.079  57.248  1.00 38.58 ? 604 HOH B O   1 
HETATM 5932 O  O   . HOH F 3 .   ? -21.447 12.679  33.685  1.00 32.04 ? 605 HOH B O   1 
HETATM 5933 O  O   . HOH F 3 .   ? 5.780   5.519   19.396  1.00 29.38 ? 606 HOH B O   1 
HETATM 5934 O  O   . HOH F 3 .   ? -12.935 23.387  20.472  1.00 36.45 ? 607 HOH B O   1 
HETATM 5935 O  O   . HOH F 3 .   ? 29.059  9.143   43.182  1.00 51.15 ? 608 HOH B O   1 
HETATM 5936 O  O   . HOH F 3 .   ? -11.900 -9.069  -0.231  1.00 47.01 ? 609 HOH B O   1 
HETATM 5937 O  O   . HOH F 3 .   ? 23.945  14.046  50.915  1.00 39.96 ? 610 HOH B O   1 
HETATM 5938 O  O   . HOH F 3 .   ? -4.373  7.120   50.612  1.00 40.07 ? 611 HOH B O   1 
HETATM 5939 O  O   . HOH F 3 .   ? 1.856   19.767  37.591  1.00 39.29 ? 612 HOH B O   1 
HETATM 5940 O  O   . HOH F 3 .   ? 11.249  -3.273  55.084  1.00 30.03 ? 613 HOH B O   1 
HETATM 5941 O  O   . HOH F 3 .   ? -10.753 11.650  47.659  1.00 41.81 ? 614 HOH B O   1 
HETATM 5942 O  O   . HOH F 3 .   ? 14.766  -3.063  31.915  1.00 35.63 ? 615 HOH B O   1 
HETATM 5943 O  O   . HOH F 3 .   ? -20.933 17.166  35.744  1.00 37.96 ? 616 HOH B O   1 
HETATM 5944 O  O   . HOH F 3 .   ? 6.419   -10.955 16.740  1.00 35.24 ? 617 HOH B O   1 
HETATM 5945 O  O   . HOH F 3 .   ? -9.243  -9.085  34.102  1.00 25.98 ? 618 HOH B O   1 
HETATM 5946 O  O   . HOH F 3 .   ? 2.997   10.021  54.100  1.00 36.15 ? 619 HOH B O   1 
HETATM 5947 O  O   . HOH F 3 .   ? -9.626  0.368   48.337  1.00 22.51 ? 620 HOH B O   1 
HETATM 5948 O  O   . HOH F 3 .   ? 7.604   -5.275  12.153  1.00 28.65 ? 621 HOH B O   1 
HETATM 5949 O  O   . HOH F 3 .   ? -10.318 14.898  49.188  1.00 40.44 ? 622 HOH B O   1 
HETATM 5950 O  O   . HOH F 3 .   ? 1.280   -5.778  38.351  1.00 31.24 ? 623 HOH B O   1 
HETATM 5951 O  O   . HOH F 3 .   ? 22.278  12.295  29.619  1.00 42.80 ? 624 HOH B O   1 
HETATM 5952 O  O   . HOH F 3 .   ? 7.704   -9.621  31.930  1.00 23.14 ? 625 HOH B O   1 
HETATM 5953 O  O   . HOH F 3 .   ? 0.572   15.303  49.470  1.00 39.60 ? 626 HOH B O   1 
HETATM 5954 O  O   . HOH F 3 .   ? -3.981  -14.218 18.027  1.00 34.64 ? 627 HOH B O   1 
HETATM 5955 O  O   . HOH F 3 .   ? -2.650  17.965  21.034  1.00 26.20 ? 628 HOH B O   1 
HETATM 5956 O  O   . HOH F 3 .   ? 2.965   -14.217 25.709  1.00 25.28 ? 629 HOH B O   1 
HETATM 5957 O  O   . HOH F 3 .   ? -8.850  -6.283  51.599  1.00 39.34 ? 630 HOH B O   1 
HETATM 5958 O  O   . HOH F 3 .   ? -16.098 6.938   17.255  1.00 36.01 ? 631 HOH B O   1 
HETATM 5959 O  O   . HOH F 3 .   ? -8.648  9.377   48.374  1.00 28.62 ? 632 HOH B O   1 
HETATM 5960 O  O   . HOH F 3 .   ? 9.127   -10.755 24.966  1.00 30.11 ? 633 HOH B O   1 
HETATM 5961 O  O   . HOH F 3 .   ? 13.617  14.185  53.533  1.00 22.93 ? 634 HOH B O   1 
HETATM 5962 O  O   . HOH F 3 .   ? 16.123  -11.853 41.501  1.00 30.89 ? 635 HOH B O   1 
HETATM 5963 O  O   . HOH F 3 .   ? -6.877  17.692  44.696  1.00 37.73 ? 636 HOH B O   1 
HETATM 5964 O  O   . HOH F 3 .   ? -0.589  4.407   47.827  1.00 20.88 ? 637 HOH B O   1 
HETATM 5965 O  O   . HOH F 3 .   ? -9.084  7.403   46.356  1.00 17.69 ? 638 HOH B O   1 
HETATM 5966 O  O   . HOH F 3 .   ? -6.387  22.063  38.596  1.00 35.30 ? 639 HOH B O   1 
HETATM 5967 O  O   . HOH F 3 .   ? 15.035  14.485  51.081  1.00 19.41 ? 640 HOH B O   1 
HETATM 5968 O  O   . HOH F 3 .   ? -7.792  13.091  14.803  1.00 30.61 ? 641 HOH B O   1 
HETATM 5969 O  O   . HOH F 3 .   ? 17.827  -10.366 39.004  1.00 35.73 ? 642 HOH B O   1 
HETATM 5970 O  O   . HOH F 3 .   ? 7.363   11.850  52.912  1.00 30.17 ? 643 HOH B O   1 
HETATM 5971 O  O   . HOH F 3 .   ? -1.140  -8.511  32.751  1.00 16.58 ? 644 HOH B O   1 
HETATM 5972 O  O   . HOH F 3 .   ? 22.798  9.492   28.601  1.00 18.82 ? 645 HOH B O   1 
HETATM 5973 O  O   . HOH F 3 .   ? -11.235 0.434   12.344  1.00 31.93 ? 646 HOH B O   1 
HETATM 5974 O  O   . HOH F 3 .   ? 4.378   -5.806  41.220  1.00 34.58 ? 647 HOH B O   1 
HETATM 5975 O  O   . HOH F 3 .   ? 21.186  16.236  52.008  1.00 21.87 ? 648 HOH B O   1 
HETATM 5976 O  O   . HOH F 3 .   ? 28.836  4.847   29.201  1.00 20.18 ? 649 HOH B O   1 
HETATM 5977 O  O   . HOH F 3 .   ? 28.500  -5.822  44.073  1.00 36.95 ? 650 HOH B O   1 
HETATM 5978 O  O   . HOH F 3 .   ? 26.946  6.151   25.156  1.00 28.38 ? 651 HOH B O   1 
HETATM 5979 O  O   . HOH F 3 .   ? 14.154  -7.398  27.755  1.00 19.66 ? 652 HOH B O   1 
HETATM 5980 O  O   . HOH F 3 .   ? 7.222   -3.059  35.699  1.00 28.58 ? 653 HOH B O   1 
HETATM 5981 O  O   . HOH F 3 .   ? -19.960 22.428  21.240  1.00 33.62 ? 654 HOH B O   1 
HETATM 5982 O  O   . HOH F 3 .   ? -8.354  -11.334 26.779  1.00 23.11 ? 655 HOH B O   1 
HETATM 5983 O  O   . HOH F 3 .   ? -9.273  -1.981  30.418  1.00 11.55 ? 656 HOH B O   1 
HETATM 5984 O  O   . HOH F 3 .   ? -20.069 4.180   16.810  1.00 41.75 ? 657 HOH B O   1 
HETATM 5985 O  O   . HOH F 3 .   ? -4.276  -7.952  55.752  1.00 25.40 ? 658 HOH B O   1 
HETATM 5986 O  O   . HOH F 3 .   ? -7.521  18.869  24.267  1.00 31.15 ? 659 HOH B O   1 
HETATM 5987 O  O   . HOH F 3 .   ? -5.257  -5.109  37.104  1.00 14.46 ? 660 HOH B O   1 
HETATM 5988 O  O   . HOH F 3 .   ? 2.340   16.214  35.556  1.00 26.29 ? 661 HOH B O   1 
HETATM 5989 O  O   . HOH F 3 .   ? 14.547  -6.383  50.392  1.00 21.23 ? 662 HOH B O   1 
HETATM 5990 O  O   . HOH F 3 .   ? -4.856  -9.570  41.899  1.00 32.73 ? 663 HOH B O   1 
HETATM 5991 O  O   . HOH F 3 .   ? -2.329  -2.336  30.104  1.00 10.04 ? 664 HOH B O   1 
HETATM 5992 O  O   . HOH F 3 .   ? 7.479   -1.012  56.370  1.00 36.71 ? 665 HOH B O   1 
HETATM 5993 O  O   . HOH F 3 .   ? -5.225  -4.762  6.967   1.00 15.38 ? 666 HOH B O   1 
HETATM 5994 O  O   . HOH F 3 .   ? -2.981  -5.632  19.018  1.00 12.82 ? 667 HOH B O   1 
HETATM 5995 O  O   . HOH F 3 .   ? 15.412  10.679  42.730  1.00 16.74 ? 668 HOH B O   1 
HETATM 5996 O  O   . HOH F 3 .   ? -1.961  -1.282  7.249   1.00 26.15 ? 669 HOH B O   1 
HETATM 5997 O  O   . HOH F 3 .   ? 7.970   -0.562  48.717  1.00 17.44 ? 670 HOH B O   1 
HETATM 5998 O  O   . HOH F 3 .   ? 11.730  22.648  39.925  1.00 46.39 ? 671 HOH B O   1 
HETATM 5999 O  O   . HOH F 3 .   ? -10.841 20.209  45.678  1.00 37.72 ? 672 HOH B O   1 
HETATM 6000 O  O   . HOH F 3 .   ? -23.128 11.075  28.798  1.00 43.64 ? 673 HOH B O   1 
HETATM 6001 O  O   . HOH F 3 .   ? 34.641  5.145   45.412  1.00 36.05 ? 674 HOH B O   1 
HETATM 6002 O  O   . HOH F 3 .   ? 14.250  -1.551  48.080  1.00 15.20 ? 675 HOH B O   1 
HETATM 6003 O  O   . HOH F 3 .   ? -22.880 -3.868  31.723  1.00 33.36 ? 676 HOH B O   1 
HETATM 6004 O  O   . HOH F 3 .   ? 29.519  7.488   47.978  1.00 41.23 ? 677 HOH B O   1 
HETATM 6005 O  O   . HOH F 3 .   ? 8.191   -5.704  41.407  1.00 27.90 ? 678 HOH B O   1 
HETATM 6006 O  O   . HOH F 3 .   ? -10.951 8.433   44.713  1.00 17.49 ? 679 HOH B O   1 
HETATM 6007 O  O   . HOH F 3 .   ? 17.728  13.400  53.857  1.00 28.48 ? 680 HOH B O   1 
HETATM 6008 O  O   . HOH F 3 .   ? -13.520 13.920  45.007  1.00 34.80 ? 681 HOH B O   1 
HETATM 6009 O  O   . HOH F 3 .   ? -4.226  18.118  26.899  1.00 30.27 ? 682 HOH B O   1 
HETATM 6010 O  O   . HOH F 3 .   ? 6.336   17.946  38.609  1.00 16.28 ? 683 HOH B O   1 
HETATM 6011 O  O   . HOH F 3 .   ? -19.969 9.943   16.665  1.00 47.45 ? 684 HOH B O   1 
HETATM 6012 O  O   . HOH F 3 .   ? 20.353  15.648  36.677  1.00 39.95 ? 685 HOH B O   1 
HETATM 6013 O  O   . HOH F 3 .   ? 22.362  14.211  47.810  1.00 41.98 ? 686 HOH B O   1 
HETATM 6014 O  O   . HOH F 3 .   ? 31.444  -2.017  46.536  1.00 39.97 ? 687 HOH B O   1 
HETATM 6015 O  O   . HOH F 3 .   ? -18.135 25.911  20.874  1.00 20.83 ? 688 HOH B O   1 
HETATM 6016 O  O   . HOH F 3 .   ? -23.406 5.946   22.518  1.00 25.85 ? 689 HOH B O   1 
HETATM 6017 O  O   . HOH F 3 .   ? 2.783   16.975  22.174  1.00 31.23 ? 690 HOH B O   1 
HETATM 6018 O  O   . HOH F 3 .   ? 17.178  9.786   55.446  1.00 31.70 ? 691 HOH B O   1 
HETATM 6019 O  O   . HOH F 3 .   ? 4.930   -11.803 33.918  1.00 31.31 ? 692 HOH B O   1 
HETATM 6020 O  O   . HOH F 3 .   ? -22.275 19.530  34.071  1.00 37.40 ? 693 HOH B O   1 
HETATM 6021 O  O   . HOH F 3 .   ? -0.913  -10.872 39.460  1.00 31.82 ? 694 HOH B O   1 
HETATM 6022 O  O   . HOH F 3 .   ? 13.040  10.859  41.423  1.00 18.79 ? 695 HOH B O   1 
HETATM 6023 O  O   . HOH F 3 .   ? 4.661   -4.295  39.205  1.00 28.32 ? 696 HOH B O   1 
HETATM 6024 O  O   . HOH F 3 .   ? 8.135   21.494  36.865  1.00 35.33 ? 697 HOH B O   1 
HETATM 6025 O  O   . HOH F 3 .   ? -15.018 -2.106  40.556  1.00 36.26 ? 698 HOH B O   1 
HETATM 6026 O  O   . HOH F 3 .   ? 25.192  11.440  44.105  1.00 23.91 ? 699 HOH B O   1 
HETATM 6027 O  O   . HOH F 3 .   ? -11.797 -3.983  2.976   1.00 21.29 ? 700 HOH B O   1 
HETATM 6028 O  O   . HOH F 3 .   ? -13.612 8.640   15.642  1.00 42.02 ? 701 HOH B O   1 
HETATM 6029 O  O   . HOH F 3 .   ? -15.951 3.952   34.156  1.00 22.29 ? 702 HOH B O   1 
HETATM 6030 O  O   . HOH F 3 .   ? 4.109   -0.858  52.992  1.00 31.36 ? 703 HOH B O   1 
HETATM 6031 O  O   . HOH F 3 .   ? 3.102   -12.694 19.363  1.00 26.12 ? 704 HOH B O   1 
HETATM 6032 O  O   . HOH F 3 .   ? -0.284  -15.403 23.825  1.00 28.32 ? 705 HOH B O   1 
HETATM 6033 O  O   . HOH F 3 .   ? 5.532   -7.821  47.613  1.00 41.81 ? 706 HOH B O   1 
HETATM 6034 O  O   A HOH F 3 .   ? 11.988  2.635   41.532  0.50 14.12 ? 707 HOH B O   1 
HETATM 6035 O  O   B HOH F 3 .   ? 11.964  1.891   40.339  0.50 17.04 ? 707 HOH B O   1 
HETATM 6036 O  O   . HOH F 3 .   ? -4.216  16.582  31.847  1.00 21.80 ? 708 HOH B O   1 
HETATM 6037 O  O   . HOH F 3 .   ? 27.594  7.659   45.892  1.00 30.91 ? 709 HOH B O   1 
HETATM 6038 O  O   . HOH F 3 .   ? 7.149   3.947   49.251  1.00 15.62 ? 710 HOH B O   1 
HETATM 6039 O  O   . HOH F 3 .   ? -4.535  -10.819 26.518  1.00 12.21 ? 711 HOH B O   1 
HETATM 6040 O  O   . HOH F 3 .   ? 30.859  6.385   30.510  1.00 22.45 ? 712 HOH B O   1 
HETATM 6041 O  O   . HOH F 3 .   ? -14.368 1.704   32.752  1.00 22.92 ? 713 HOH B O   1 
HETATM 6042 O  O   . HOH F 3 .   ? 17.367  -5.391  44.895  1.00 18.16 ? 714 HOH B O   1 
HETATM 6043 O  O   . HOH F 3 .   ? 30.510  10.054  37.462  1.00 29.44 ? 715 HOH B O   1 
HETATM 6044 O  O   . HOH F 3 .   ? -12.191 0.768   7.419   1.00 40.44 ? 716 HOH B O   1 
HETATM 6045 O  O   . HOH F 3 .   ? -3.993  -8.167  19.344  1.00 13.13 ? 717 HOH B O   1 
HETATM 6046 O  O   . HOH F 3 .   ? 15.899  1.609   33.147  1.00 16.02 ? 718 HOH B O   1 
HETATM 6047 O  O   . HOH F 3 .   ? -15.843 2.568   50.572  1.00 37.18 ? 719 HOH B O   1 
HETATM 6048 O  O   . HOH F 3 .   ? 2.328   -9.984  12.287  1.00 24.79 ? 720 HOH B O   1 
HETATM 6049 O  O   . HOH F 3 .   ? -11.792 -4.593  33.217  1.00 15.40 ? 721 HOH B O   1 
HETATM 6050 O  O   . HOH F 3 .   ? -6.897  -15.590 30.267  1.00 32.11 ? 722 HOH B O   1 
HETATM 6051 O  O   . HOH F 3 .   ? -13.787 -2.254  5.924   1.00 40.46 ? 723 HOH B O   1 
HETATM 6052 O  O   . HOH F 3 .   ? 6.459   11.249  28.477  1.00 29.43 ? 724 HOH B O   1 
HETATM 6053 O  O   . HOH F 3 .   ? 9.245   -8.211  43.571  1.00 34.62 ? 725 HOH B O   1 
HETATM 6054 O  O   . HOH F 3 .   ? 26.327  2.471   53.792  1.00 32.98 ? 726 HOH B O   1 
HETATM 6055 O  O   . HOH F 3 .   ? -5.340  -8.007  16.856  1.00 15.40 ? 727 HOH B O   1 
HETATM 6056 O  O   . HOH F 3 .   ? -22.947 19.117  36.897  1.00 32.91 ? 728 HOH B O   1 
HETATM 6057 O  O   . HOH F 3 .   ? 17.227  -9.837  35.668  1.00 32.51 ? 729 HOH B O   1 
HETATM 6058 O  O   . HOH F 3 .   ? 18.808  -3.297  43.649  1.00 18.12 ? 730 HOH B O   1 
HETATM 6059 O  O   . HOH F 3 .   ? 12.807  16.258  39.708  1.00 27.30 ? 731 HOH B O   1 
HETATM 6060 O  O   . HOH F 3 .   ? -5.959  9.644   16.629  1.00 19.17 ? 732 HOH B O   1 
HETATM 6061 O  O   . HOH F 3 .   ? -3.205  -11.292 16.450  1.00 20.54 ? 733 HOH B O   1 
HETATM 6062 O  O   . HOH F 3 .   ? -13.446 7.181   45.228  1.00 20.45 ? 734 HOH B O   1 
HETATM 6063 O  O   . HOH F 3 .   ? 20.342  -2.246  54.951  1.00 24.08 ? 735 HOH B O   1 
HETATM 6064 O  O   . HOH F 3 .   ? 13.520  16.328  43.327  1.00 30.05 ? 736 HOH B O   1 
HETATM 6065 O  O   . HOH F 3 .   ? -23.334 8.696   22.392  1.00 23.41 ? 737 HOH B O   1 
HETATM 6066 O  O   . HOH F 3 .   ? 11.530  16.238  45.183  1.00 19.79 ? 738 HOH B O   1 
HETATM 6067 O  O   . HOH F 3 .   ? 13.161  18.394  28.820  1.00 30.48 ? 739 HOH B O   1 
HETATM 6068 O  O   . HOH F 3 .   ? 1.316   8.509   58.273  1.00 38.86 ? 740 HOH B O   1 
HETATM 6069 O  O   . HOH F 3 .   ? 7.028   0.306   45.340  1.00 15.92 ? 741 HOH B O   1 
HETATM 6070 O  O   . HOH F 3 .   ? -21.288 1.477   34.783  1.00 36.16 ? 742 HOH B O   1 
HETATM 6071 O  O   . HOH F 3 .   ? -8.168  0.673   12.742  1.00 19.21 ? 743 HOH B O   1 
HETATM 6072 O  O   . HOH F 3 .   ? 2.552   -0.807  33.487  1.00 13.33 ? 744 HOH B O   1 
HETATM 6073 O  O   . HOH F 3 .   ? 14.914  -9.823  56.527  1.00 40.55 ? 745 HOH B O   1 
HETATM 6074 O  O   . HOH F 3 .   ? -24.961 5.402   26.774  1.00 39.72 ? 746 HOH B O   1 
HETATM 6075 O  O   . HOH F 3 .   ? 6.569   -2.848  49.755  1.00 30.33 ? 747 HOH B O   1 
HETATM 6076 O  O   . HOH F 3 .   ? 9.593   5.370   22.598  1.00 24.47 ? 748 HOH B O   1 
HETATM 6077 O  O   . HOH F 3 .   ? -9.517  -0.349  37.447  1.00 13.39 ? 749 HOH B O   1 
HETATM 6078 O  O   . HOH F 3 .   ? 1.654   14.676  18.284  1.00 18.75 ? 750 HOH B O   1 
HETATM 6079 O  O   . HOH F 3 .   ? -9.020  17.466  41.754  1.00 29.79 ? 751 HOH B O   1 
HETATM 6080 O  O   . HOH F 3 .   ? -11.072 -10.189 25.278  1.00 27.70 ? 752 HOH B O   1 
HETATM 6081 O  O   . HOH F 3 .   ? 30.712  1.246   34.571  1.00 25.31 ? 753 HOH B O   1 
HETATM 6082 O  O   . HOH F 3 .   ? -9.484  18.840  27.387  1.00 26.41 ? 754 HOH B O   1 
HETATM 6083 O  O   . HOH F 3 .   ? -16.130 -4.969  4.024   1.00 45.70 ? 755 HOH B O   1 
HETATM 6084 O  O   . HOH F 3 .   ? 9.554   14.808  53.006  1.00 36.01 ? 756 HOH B O   1 
HETATM 6085 O  O   . HOH F 3 .   ? 7.897   8.430   58.252  1.00 34.13 ? 757 HOH B O   1 
HETATM 6086 O  O   . HOH F 3 .   ? -2.911  -14.144 46.040  1.00 20.61 ? 758 HOH B O   1 
HETATM 6087 O  O   . HOH F 3 .   ? 14.675  15.769  37.698  1.00 19.33 ? 759 HOH B O   1 
HETATM 6088 O  O   . HOH F 3 .   ? -8.946  -4.662  31.172  1.00 11.81 ? 760 HOH B O   1 
HETATM 6089 O  O   . HOH F 3 .   ? 10.152  -1.139  39.765  1.00 29.23 ? 761 HOH B O   1 
HETATM 6090 O  O   . HOH F 3 .   ? -15.923 -6.604  20.392  1.00 24.29 ? 762 HOH B O   1 
HETATM 6091 O  O   . HOH F 3 .   ? 8.536   22.350  27.263  1.00 37.98 ? 763 HOH B O   1 
HETATM 6092 O  O   . HOH F 3 .   ? -2.612  14.031  32.091  1.00 15.04 ? 764 HOH B O   1 
HETATM 6093 O  O   . HOH F 3 .   ? -13.899 -3.991  16.870  1.00 21.07 ? 765 HOH B O   1 
HETATM 6094 O  O   . HOH F 3 .   ? 27.866  1.195   35.269  1.00 28.33 ? 766 HOH B O   1 
HETATM 6095 O  O   . HOH F 3 .   ? 29.608  -4.695  47.560  1.00 43.05 ? 767 HOH B O   1 
HETATM 6096 O  O   . HOH F 3 .   ? 24.310  7.972   48.879  1.00 29.36 ? 768 HOH B O   1 
HETATM 6097 O  O   . HOH F 3 .   ? 25.967  2.046   51.073  1.00 26.32 ? 769 HOH B O   1 
HETATM 6098 O  O   . HOH F 3 .   ? 1.075   -13.409 9.587   1.00 34.87 ? 770 HOH B O   1 
HETATM 6099 O  O   . HOH F 3 .   ? -3.699  -7.393  12.621  1.00 14.28 ? 771 HOH B O   1 
HETATM 6100 O  O   . HOH F 3 .   ? 12.272  2.291   24.290  1.00 17.75 ? 772 HOH B O   1 
HETATM 6101 O  O   . HOH F 3 .   ? -9.642  19.753  35.753  1.00 19.88 ? 773 HOH B O   1 
HETATM 6102 O  O   . HOH F 3 .   ? 12.206  -7.903  50.693  1.00 33.44 ? 774 HOH B O   1 
HETATM 6103 O  O   . HOH F 3 .   ? 7.270   14.105  51.799  1.00 37.21 ? 775 HOH B O   1 
HETATM 6104 O  O   . HOH F 3 .   ? 35.776  7.041   35.882  1.00 41.07 ? 776 HOH B O   1 
HETATM 6105 O  O   . HOH F 3 .   ? 13.252  10.333  22.551  1.00 45.04 ? 777 HOH B O   1 
HETATM 6106 O  O   . HOH F 3 .   ? 20.993  -4.817  42.250  1.00 18.03 ? 778 HOH B O   1 
HETATM 6107 O  O   . HOH F 3 .   ? -6.576  -8.025  28.604  1.00 13.35 ? 779 HOH B O   1 
HETATM 6108 O  O   . HOH F 3 .   ? -14.460 -1.216  17.362  1.00 25.70 ? 780 HOH B O   1 
HETATM 6109 O  O   . HOH F 3 .   ? -8.680  -7.205  36.018  1.00 21.86 ? 781 HOH B O   1 
HETATM 6110 O  O   . HOH F 3 .   ? 0.265   5.346   50.373  1.00 21.62 ? 782 HOH B O   1 
HETATM 6111 O  O   . HOH F 3 .   ? -12.029 -5.008  6.877   1.00 26.12 ? 783 HOH B O   1 
HETATM 6112 O  O   . HOH F 3 .   ? 25.507  11.307  30.489  1.00 28.32 ? 784 HOH B O   1 
HETATM 6113 O  O   . HOH F 3 .   ? 17.067  -7.898  33.790  1.00 20.88 ? 785 HOH B O   1 
HETATM 6114 O  O   . HOH F 3 .   ? -2.443  -10.318 18.883  1.00 17.70 ? 786 HOH B O   1 
HETATM 6115 O  O   . HOH F 3 .   ? -11.177 11.255  45.087  1.00 22.42 ? 787 HOH B O   1 
HETATM 6116 O  O   . HOH F 3 .   ? 17.490  15.341  39.085  1.00 27.14 ? 788 HOH B O   1 
HETATM 6117 O  O   . HOH F 3 .   ? -8.746  -10.380 9.814   1.00 26.21 ? 789 HOH B O   1 
HETATM 6118 O  O   . HOH F 3 .   ? 14.799  -4.200  59.229  1.00 51.19 ? 790 HOH B O   1 
HETATM 6119 O  O   . HOH F 3 .   ? 1.219   22.434  40.004  1.00 39.95 ? 791 HOH B O   1 
HETATM 6120 O  O   . HOH F 3 .   ? 7.415   10.056  26.259  1.00 40.86 ? 792 HOH B O   1 
HETATM 6121 O  O   . HOH F 3 .   ? 15.724  4.655   17.543  1.00 23.12 ? 793 HOH B O   1 
HETATM 6122 O  O   . HOH F 3 .   ? 6.356   1.634   47.914  1.00 15.26 ? 794 HOH B O   1 
HETATM 6123 O  O   . HOH F 3 .   ? -13.322 -9.050  38.910  1.00 37.10 ? 795 HOH B O   1 
HETATM 6124 O  O   . HOH F 3 .   ? -3.139  17.874  29.379  1.00 27.80 ? 796 HOH B O   1 
HETATM 6125 O  O   . HOH F 3 .   ? 12.026  15.233  25.624  1.00 42.23 ? 797 HOH B O   1 
HETATM 6126 O  O   . HOH F 3 .   ? -17.967 -5.650  22.048  1.00 23.85 ? 798 HOH B O   1 
HETATM 6127 O  O   . HOH F 3 .   ? 29.076  9.441   21.734  1.00 34.40 ? 799 HOH B O   1 
HETATM 6128 O  O   . HOH F 3 .   ? -1.963  17.910  36.009  1.00 35.40 ? 800 HOH B O   1 
HETATM 6129 O  O   . HOH F 3 .   ? 15.238  -0.293  58.978  1.00 27.93 ? 801 HOH B O   1 
HETATM 6130 O  O   . HOH F 3 .   ? -7.612  -6.252  45.879  1.00 29.00 ? 802 HOH B O   1 
HETATM 6131 O  O   . HOH F 3 .   ? -7.990  5.698   8.218   1.00 25.18 ? 803 HOH B O   1 
HETATM 6132 O  O   . HOH F 3 .   ? 14.147  14.041  41.651  1.00 30.18 ? 804 HOH B O   1 
HETATM 6133 O  O   . HOH F 3 .   ? -17.158 21.609  30.175  1.00 22.22 ? 805 HOH B O   1 
HETATM 6134 O  O   . HOH F 3 .   ? -6.921  -5.294  29.177  1.00 12.50 ? 806 HOH B O   1 
HETATM 6135 O  O   . HOH F 3 .   ? 9.541   8.283   22.460  1.00 33.81 ? 807 HOH B O   1 
HETATM 6136 O  O   . HOH F 3 .   ? 9.072   -7.018  32.392  1.00 32.00 ? 808 HOH B O   1 
HETATM 6137 O  O   . HOH F 3 .   ? -20.478 3.787   19.372  1.00 21.58 ? 809 HOH B O   1 
HETATM 6138 O  O   . HOH F 3 .   ? 0.388   17.470  37.176  1.00 23.30 ? 810 HOH B O   1 
HETATM 6139 O  O   . HOH F 3 .   ? 25.103  -0.153  49.307  1.00 24.32 ? 811 HOH B O   1 
HETATM 6140 O  O   . HOH F 3 .   ? 14.775  12.621  25.387  1.00 42.78 ? 812 HOH B O   1 
HETATM 6141 O  O   . HOH F 3 .   ? 18.616  8.012   17.779  1.00 28.20 ? 813 HOH B O   1 
HETATM 6142 O  O   . HOH F 3 .   ? 23.850  3.808   51.057  1.00 19.39 ? 814 HOH B O   1 
HETATM 6143 O  O   . HOH F 3 .   ? -2.372  6.332   47.878  1.00 19.99 ? 815 HOH B O   1 
HETATM 6144 O  O   . HOH F 3 .   ? -10.789 -6.173  4.392   1.00 21.95 ? 816 HOH B O   1 
HETATM 6145 O  O   . HOH F 3 .   ? -15.564 0.641   47.874  1.00 35.22 ? 817 HOH B O   1 
HETATM 6146 O  O   . HOH F 3 .   ? -16.201 21.106  32.568  1.00 37.45 ? 818 HOH B O   1 
HETATM 6147 O  O   . HOH F 3 .   ? 9.830   21.629  34.502  1.00 25.25 ? 819 HOH B O   1 
HETATM 6148 O  O   . HOH F 3 .   ? 16.689  19.665  46.190  1.00 23.30 ? 820 HOH B O   1 
HETATM 6149 O  O   . HOH F 3 .   ? 19.846  -10.342 37.195  1.00 31.24 ? 821 HOH B O   1 
HETATM 6150 O  O   . HOH F 3 .   ? -4.181  -13.576 13.395  1.00 39.25 ? 822 HOH B O   1 
HETATM 6151 O  O   . HOH F 3 .   ? -2.786  5.407   13.742  1.00 15.84 ? 823 HOH B O   1 
HETATM 6152 O  O   . HOH F 3 .   ? -19.237 9.892   41.153  1.00 29.27 ? 824 HOH B O   1 
HETATM 6153 O  O   . HOH F 3 .   ? 4.149   -9.918  37.481  1.00 32.86 ? 825 HOH B O   1 
HETATM 6154 O  O   . HOH F 3 .   ? -21.507 -4.006  23.848  1.00 38.90 ? 826 HOH B O   1 
HETATM 6155 O  O   . HOH F 3 .   ? -9.476  -11.959 13.955  1.00 34.71 ? 827 HOH B O   1 
HETATM 6156 O  O   . HOH F 3 .   ? -19.212 -7.416  23.682  1.00 40.60 ? 828 HOH B O   1 
HETATM 6157 O  O   . HOH F 3 .   ? -4.580  19.456  42.591  1.00 31.81 ? 829 HOH B O   1 
HETATM 6158 O  O   . HOH F 3 .   ? -12.829 -11.211 29.963  1.00 30.61 ? 830 HOH B O   1 
HETATM 6159 O  O   . HOH F 3 .   ? 6.218   11.140  21.816  1.00 21.32 ? 831 HOH B O   1 
HETATM 6160 O  O   . HOH F 3 .   ? -5.796  -11.783 14.330  1.00 27.50 ? 832 HOH B O   1 
HETATM 6161 O  O   . HOH F 3 .   ? -16.621 19.496  18.310  1.00 30.15 ? 833 HOH B O   1 
HETATM 6162 O  O   . HOH F 3 .   ? 7.836   2.485   37.818  1.00 16.50 ? 834 HOH B O   1 
HETATM 6163 O  O   . HOH F 3 .   ? 25.539  14.447  33.675  1.00 39.16 ? 835 HOH B O   1 
HETATM 6164 O  O   . HOH F 3 .   ? -10.603 -7.358  38.232  1.00 27.68 ? 836 HOH B O   1 
HETATM 6165 O  O   . HOH F 3 .   ? 16.578  -13.150 48.001  1.00 28.60 ? 837 HOH B O   1 
HETATM 6166 O  O   . HOH F 3 .   ? -6.565  0.384   6.979   1.00 28.17 ? 838 HOH B O   1 
HETATM 6167 O  O   . HOH F 3 .   ? -20.743 9.998   37.094  1.00 38.30 ? 839 HOH B O   1 
HETATM 6168 O  O   . HOH F 3 .   ? 10.755  14.080  27.582  1.00 32.75 ? 840 HOH B O   1 
HETATM 6169 O  O   . HOH F 3 .   ? 24.736  -5.686  50.386  1.00 30.14 ? 841 HOH B O   1 
HETATM 6170 O  O   . HOH F 3 .   ? 6.720   -1.717  53.470  1.00 34.36 ? 842 HOH B O   1 
HETATM 6171 O  O   . HOH F 3 .   ? -13.001 -10.828 21.342  1.00 41.32 ? 843 HOH B O   1 
HETATM 6172 O  O   . HOH F 3 .   ? -3.435  4.684   50.382  1.00 34.70 ? 844 HOH B O   1 
HETATM 6173 O  O   . HOH F 3 .   ? -5.896  12.472  50.704  1.00 35.87 ? 845 HOH B O   1 
HETATM 6174 O  O   . HOH F 3 .   ? -16.535 0.653   33.017  1.00 41.70 ? 846 HOH B O   1 
HETATM 6175 O  O   . HOH F 3 .   ? 1.804   19.699  29.077  1.00 39.52 ? 847 HOH B O   1 
HETATM 6176 O  O   . HOH F 3 .   ? -8.746  19.117  46.827  1.00 43.08 ? 848 HOH B O   1 
HETATM 6177 O  O   . HOH F 3 .   ? -19.058 3.411   40.252  1.00 40.38 ? 849 HOH B O   1 
HETATM 6178 O  O   . HOH F 3 .   ? 11.008  -2.748  33.993  1.00 30.84 ? 850 HOH B O   1 
HETATM 6179 O  O   . HOH F 3 .   ? -18.420 -1.447  24.130  1.00 44.18 ? 851 HOH B O   1 
HETATM 6180 O  O   . HOH F 3 .   ? -26.461 4.953   31.182  1.00 46.53 ? 852 HOH B O   1 
HETATM 6181 O  O   . HOH F 3 .   ? 15.546  6.771   57.717  1.00 51.69 ? 853 HOH B O   1 
HETATM 6182 O  O   . HOH F 3 .   ? -5.886  18.334  48.203  1.00 49.29 ? 854 HOH B O   1 
HETATM 6183 O  O   . HOH F 3 .   ? 6.930   -4.564  53.708  1.00 51.21 ? 855 HOH B O   1 
HETATM 6184 O  O   . HOH F 3 .   ? -1.067  15.616  33.723  1.00 22.06 ? 856 HOH B O   1 
HETATM 6185 O  O   . HOH F 3 .   ? 13.666  10.470  55.158  1.00 35.10 ? 857 HOH B O   1 
HETATM 6186 O  O   . HOH F 3 .   ? 2.616   -7.419  40.131  1.00 34.63 ? 858 HOH B O   1 
HETATM 6187 O  O   . HOH F 3 .   ? -12.683 8.874   53.733  1.00 43.99 ? 859 HOH B O   1 
HETATM 6188 O  O   . HOH F 3 .   ? 2.561   -2.699  53.605  1.00 36.44 ? 860 HOH B O   1 
HETATM 6189 O  O   . HOH F 3 .   ? -23.617 15.867  23.440  1.00 39.55 ? 861 HOH B O   1 
HETATM 6190 O  O   . HOH F 3 .   ? 1.201   17.185  33.057  1.00 32.54 ? 862 HOH B O   1 
HETATM 6191 O  O   . HOH F 3 .   ? -16.219 -5.542  17.610  1.00 33.17 ? 863 HOH B O   1 
HETATM 6192 O  O   . HOH F 3 .   ? -12.034 -1.076  44.764  1.00 31.58 ? 864 HOH B O   1 
HETATM 6193 O  O   . HOH F 3 .   ? 23.636  9.882   50.513  1.00 34.42 ? 865 HOH B O   1 
HETATM 6194 O  O   . HOH F 3 .   ? 10.811  18.108  46.974  1.00 28.65 ? 866 HOH B O   1 
HETATM 6195 O  O   . HOH F 3 .   ? 4.425   23.478  43.280  1.00 46.05 ? 867 HOH B O   1 
HETATM 6196 O  O   . HOH F 3 .   ? -21.812 15.189  34.150  1.00 41.33 ? 868 HOH B O   1 
HETATM 6197 O  O   . HOH F 3 .   ? 25.191  -9.578  48.883  1.00 40.49 ? 869 HOH B O   1 
HETATM 6198 O  O   . HOH F 3 .   ? 26.876  -2.016  49.272  1.00 39.57 ? 870 HOH B O   1 
HETATM 6199 O  O   . HOH F 3 .   ? 15.820  -7.616  31.402  1.00 30.25 ? 871 HOH B O   1 
HETATM 6200 O  O   . HOH F 3 .   ? 0.932   -17.843 30.658  1.00 44.11 ? 872 HOH B O   1 
HETATM 6201 O  O   . HOH F 3 .   ? -17.001 24.268  18.029  1.00 47.68 ? 873 HOH B O   1 
HETATM 6202 O  O   . HOH F 3 .   ? 12.662  -1.105  34.859  1.00 57.49 ? 874 HOH B O   1 
HETATM 6203 O  O   . HOH F 3 .   ? -12.300 20.431  36.187  1.00 32.38 ? 875 HOH B O   1 
HETATM 6204 O  O   . HOH F 3 .   ? 7.475   -5.186  49.653  1.00 34.50 ? 876 HOH B O   1 
HETATM 6205 O  O   . HOH F 3 .   ? 11.256  -1.987  37.157  1.00 44.39 ? 877 HOH B O   1 
HETATM 6206 O  O   . HOH F 3 .   ? -4.663  -9.312  14.497  1.00 20.89 ? 878 HOH B O   1 
HETATM 6207 O  O   . HOH F 3 .   ? -10.064 5.144   6.326   1.00 34.65 ? 879 HOH B O   1 
HETATM 6208 O  O   . HOH F 3 .   ? -22.911 10.532  18.697  1.00 49.68 ? 880 HOH B O   1 
HETATM 6209 O  O   . HOH F 3 .   ? 4.323   19.159  37.207  1.00 37.35 ? 881 HOH B O   1 
HETATM 6210 O  O   . HOH F 3 .   ? -17.692 -0.615  38.611  1.00 39.41 ? 882 HOH B O   1 
HETATM 6211 O  O   . HOH F 3 .   ? -15.447 -9.329  20.905  1.00 34.21 ? 883 HOH B O   1 
HETATM 6212 O  O   . HOH F 3 .   ? -9.119  -14.847 28.985  1.00 36.29 ? 884 HOH B O   1 
HETATM 6213 O  O   . HOH F 3 .   ? 10.151  1.280   38.338  1.00 34.29 ? 885 HOH B O   1 
HETATM 6214 O  O   . HOH F 3 .   ? -20.281 1.027   19.458  1.00 38.74 ? 886 HOH B O   1 
HETATM 6215 O  O   . HOH F 3 .   ? 31.665  11.961  35.763  1.00 49.47 ? 887 HOH B O   1 
HETATM 6216 O  O   . HOH F 3 .   ? -1.238  5.482   52.323  1.00 50.25 ? 888 HOH B O   1 
HETATM 6217 O  O   . HOH F 3 .   ? -22.019 -0.095  24.321  1.00 48.68 ? 889 HOH B O   1 
HETATM 6218 O  O   . HOH F 3 .   ? 24.402  11.880  49.122  1.00 45.28 ? 890 HOH B O   1 
HETATM 6219 O  O   . HOH F 3 .   ? -6.829  -7.141  38.240  1.00 24.89 ? 891 HOH B O   1 
HETATM 6220 O  O   . HOH F 3 .   ? -19.060 26.033  18.339  1.00 42.36 ? 892 HOH B O   1 
HETATM 6221 O  O   . HOH F 3 .   ? 8.832   2.801   61.883  1.00 49.10 ? 893 HOH B O   1 
HETATM 6222 O  O   . HOH F 3 .   ? 26.605  8.717   47.802  1.00 41.96 ? 894 HOH B O   1 
HETATM 6223 O  O   . HOH F 3 .   ? -24.582 9.695   24.624  1.00 41.08 ? 895 HOH B O   1 
HETATM 6224 O  O   . HOH F 3 .   ? 5.723   22.295  32.690  1.00 43.68 ? 896 HOH B O   1 
HETATM 6225 O  O   . HOH F 3 .   ? 6.464   -10.532 14.129  1.00 34.19 ? 897 HOH B O   1 
HETATM 6226 O  O   . HOH F 3 .   ? -6.833  -7.698  41.153  1.00 38.46 ? 898 HOH B O   1 
HETATM 6227 O  O   . HOH F 3 .   ? 5.289   21.600  36.296  1.00 40.10 ? 899 HOH B O   1 
HETATM 6228 O  O   . HOH F 3 .   ? 12.407  24.396  44.630  1.00 41.77 ? 900 HOH B O   1 
HETATM 6229 O  O   . HOH F 3 .   ? 22.589  -16.127 52.894  1.00 56.02 ? 901 HOH B O   1 
# 
