data_9EPI
# 
_entry.id   9EPI 
# 
_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   9EPI         pdb_00009epi 10.2210/pdb9epi/pdb 
WWPDB D_1292137184 ?            ?                   
# 
_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                        9EPI 
_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 53 fs 10 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 syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   2   ? ? ? ? 
3 water       nat water                             18.015    535 ? ? ? ? 
# 
_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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 44   HOH HOH A . 
E 3 HOH 2   602 101  HOH HOH A . 
E 3 HOH 3   603 648  HOH HOH A . 
E 3 HOH 4   604 666  HOH HOH A . 
E 3 HOH 5   605 103  HOH HOH A . 
E 3 HOH 6   606 67   HOH HOH A . 
E 3 HOH 7   607 824  HOH HOH A . 
E 3 HOH 8   608 633  HOH HOH A . 
E 3 HOH 9   609 875  HOH HOH A . 
E 3 HOH 10  610 17   HOH HOH A . 
E 3 HOH 11  611 37   HOH HOH A . 
E 3 HOH 12  612 626  HOH HOH A . 
E 3 HOH 13  613 64   HOH HOH A . 
E 3 HOH 14  614 710  HOH HOH A . 
E 3 HOH 15  615 23   HOH HOH A . 
E 3 HOH 16  616 674  HOH HOH A . 
E 3 HOH 17  617 606  HOH HOH A . 
E 3 HOH 18  618 664  HOH HOH A . 
E 3 HOH 19  619 694  HOH HOH A . 
E 3 HOH 20  620 636  HOH HOH A . 
E 3 HOH 21  621 21   HOH HOH A . 
E 3 HOH 22  622 755  HOH HOH A . 
E 3 HOH 23  623 804  HOH HOH A . 
E 3 HOH 24  624 642  HOH HOH A . 
E 3 HOH 25  625 641  HOH HOH A . 
E 3 HOH 26  626 14   HOH HOH A . 
E 3 HOH 27  627 711  HOH HOH A . 
E 3 HOH 28  628 972  HOH HOH A . 
E 3 HOH 29  629 1    HOH HOH A . 
E 3 HOH 30  630 900  HOH HOH A . 
E 3 HOH 31  631 40   HOH HOH A . 
E 3 HOH 32  632 50   HOH HOH A . 
E 3 HOH 33  633 752  HOH HOH A . 
E 3 HOH 34  634 96   HOH HOH A . 
E 3 HOH 35  635 720  HOH HOH A . 
E 3 HOH 36  636 668  HOH HOH A . 
E 3 HOH 37  637 681  HOH HOH A . 
E 3 HOH 38  638 730  HOH HOH A . 
E 3 HOH 39  639 629  HOH HOH A . 
E 3 HOH 40  640 654  HOH HOH A . 
E 3 HOH 41  641 611  HOH HOH A . 
E 3 HOH 42  642 625  HOH HOH A . 
E 3 HOH 43  643 45   HOH HOH A . 
E 3 HOH 44  644 643  HOH HOH A . 
E 3 HOH 45  645 677  HOH HOH A . 
E 3 HOH 46  646 783  HOH HOH A . 
E 3 HOH 47  647 728  HOH HOH A . 
E 3 HOH 48  648 33   HOH HOH A . 
E 3 HOH 49  649 662  HOH HOH A . 
E 3 HOH 50  650 613  HOH HOH A . 
E 3 HOH 51  651 684  HOH HOH A . 
E 3 HOH 52  652 712  HOH HOH A . 
E 3 HOH 53  653 723  HOH HOH A . 
E 3 HOH 54  654 776  HOH HOH A . 
E 3 HOH 55  655 738  HOH HOH A . 
E 3 HOH 56  656 739  HOH HOH A . 
E 3 HOH 57  657 863  HOH HOH A . 
E 3 HOH 58  658 740  HOH HOH A . 
E 3 HOH 59  659 716  HOH HOH A . 
E 3 HOH 60  660 695  HOH HOH A . 
E 3 HOH 61  661 686  HOH HOH A . 
E 3 HOH 62  662 675  HOH HOH A . 
E 3 HOH 63  663 99   HOH HOH A . 
E 3 HOH 64  664 85   HOH HOH A . 
E 3 HOH 65  665 734  HOH HOH A . 
E 3 HOH 66  666 647  HOH HOH A . 
E 3 HOH 67  667 853  HOH HOH A . 
E 3 HOH 68  668 9    HOH HOH A . 
E 3 HOH 69  669 692  HOH HOH A . 
E 3 HOH 70  670 718  HOH HOH A . 
E 3 HOH 71  671 639  HOH HOH A . 
E 3 HOH 72  672 630  HOH HOH A . 
E 3 HOH 73  673 623  HOH HOH A . 
E 3 HOH 74  674 621  HOH HOH A . 
E 3 HOH 75  675 765  HOH HOH A . 
E 3 HOH 76  676 842  HOH HOH A . 
E 3 HOH 77  677 714  HOH HOH A . 
E 3 HOH 78  678 49   HOH HOH A . 
E 3 HOH 79  679 839  HOH HOH A . 
E 3 HOH 80  680 699  HOH HOH A . 
E 3 HOH 81  681 650  HOH HOH A . 
E 3 HOH 82  682 719  HOH HOH A . 
E 3 HOH 83  683 685  HOH HOH A . 
E 3 HOH 84  684 759  HOH HOH A . 
E 3 HOH 85  685 851  HOH HOH A . 
E 3 HOH 86  686 631  HOH HOH A . 
E 3 HOH 87  687 663  HOH HOH A . 
E 3 HOH 88  688 749  HOH HOH A . 
E 3 HOH 89  689 807  HOH HOH A . 
E 3 HOH 90  690 721  HOH HOH A . 
E 3 HOH 91  691 698  HOH HOH A . 
E 3 HOH 92  692 78   HOH HOH A . 
E 3 HOH 93  693 815  HOH HOH A . 
E 3 HOH 94  694 727  HOH HOH A . 
E 3 HOH 95  695 676  HOH HOH A . 
E 3 HOH 96  696 656  HOH HOH A . 
E 3 HOH 97  697 799  HOH HOH A . 
E 3 HOH 98  698 19   HOH HOH A . 
E 3 HOH 99  699 12   HOH HOH A . 
E 3 HOH 100 700 705  HOH HOH A . 
E 3 HOH 101 701 794  HOH HOH A . 
E 3 HOH 102 702 789  HOH HOH A . 
E 3 HOH 103 703 818  HOH HOH A . 
E 3 HOH 104 704 59   HOH HOH A . 
E 3 HOH 105 705 827  HOH HOH A . 
E 3 HOH 106 706 724  HOH HOH A . 
E 3 HOH 107 707 657  HOH HOH A . 
E 3 HOH 108 708 652  HOH HOH A . 
E 3 HOH 109 709 706  HOH HOH A . 
E 3 HOH 110 710 933  HOH HOH A . 
E 3 HOH 111 711 709  HOH HOH A . 
E 3 HOH 112 712 672  HOH HOH A . 
E 3 HOH 113 713 745  HOH HOH A . 
E 3 HOH 114 714 874  HOH HOH A . 
E 3 HOH 115 715 800  HOH HOH A . 
E 3 HOH 116 716 897  HOH HOH A . 
E 3 HOH 117 717 106  HOH HOH A . 
E 3 HOH 118 718 680  HOH HOH A . 
E 3 HOH 119 719 790  HOH HOH A . 
E 3 HOH 120 720 754  HOH HOH A . 
E 3 HOH 121 721 42   HOH HOH A . 
E 3 HOH 122 722 77   HOH HOH A . 
E 3 HOH 123 723 822  HOH HOH A . 
E 3 HOH 124 724 733  HOH HOH A . 
E 3 HOH 125 725 928  HOH HOH A . 
E 3 HOH 126 726 702  HOH HOH A . 
E 3 HOH 127 727 944  HOH HOH A . 
E 3 HOH 128 728 669  HOH HOH A . 
E 3 HOH 129 729 795  HOH HOH A . 
E 3 HOH 130 730 736  HOH HOH A . 
E 3 HOH 131 731 27   HOH HOH A . 
E 3 HOH 132 732 51   HOH HOH A . 
E 3 HOH 133 733 61   HOH HOH A . 
E 3 HOH 134 734 801  HOH HOH A . 
E 3 HOH 135 735 751  HOH HOH A . 
E 3 HOH 136 736 791  HOH HOH A . 
E 3 HOH 137 737 743  HOH HOH A . 
E 3 HOH 138 738 28   HOH HOH A . 
E 3 HOH 139 739 916  HOH HOH A . 
E 3 HOH 140 740 792  HOH HOH A . 
E 3 HOH 141 741 3    HOH HOH A . 
E 3 HOH 142 742 805  HOH HOH A . 
E 3 HOH 143 743 806  HOH HOH A . 
E 3 HOH 144 744 917  HOH HOH A . 
E 3 HOH 145 745 683  HOH HOH A . 
E 3 HOH 146 746 744  HOH HOH A . 
E 3 HOH 147 747 769  HOH HOH A . 
E 3 HOH 148 748 696  HOH HOH A . 
E 3 HOH 149 749 2    HOH HOH A . 
E 3 HOH 150 750 893  HOH HOH A . 
E 3 HOH 151 751 793  HOH HOH A . 
E 3 HOH 152 752 704  HOH HOH A . 
E 3 HOH 153 753 60   HOH HOH A . 
E 3 HOH 154 754 823  HOH HOH A . 
E 3 HOH 155 755 802  HOH HOH A . 
E 3 HOH 156 756 673  HOH HOH A . 
E 3 HOH 157 757 623  HOH HOH A . 
E 3 HOH 158 758 829  HOH HOH A . 
E 3 HOH 159 759 762  HOH HOH A . 
E 3 HOH 160 760 97   HOH HOH A . 
E 3 HOH 161 761 788  HOH HOH A . 
E 3 HOH 162 762 713  HOH HOH A . 
E 3 HOH 163 763 860  HOH HOH A . 
E 3 HOH 164 764 854  HOH HOH A . 
E 3 HOH 165 765 748  HOH HOH A . 
E 3 HOH 166 766 679  HOH HOH A . 
E 3 HOH 167 767 834  HOH HOH A . 
E 3 HOH 168 768 996  HOH HOH A . 
E 3 HOH 169 769 938  HOH HOH A . 
E 3 HOH 170 770 84   HOH HOH A . 
E 3 HOH 171 771 778  HOH HOH A . 
E 3 HOH 172 772 76   HOH HOH A . 
E 3 HOH 173 773 849  HOH HOH A . 
E 3 HOH 174 774 756  HOH HOH A . 
E 3 HOH 175 775 701  HOH HOH A . 
E 3 HOH 176 776 858  HOH HOH A . 
E 3 HOH 177 777 909  HOH HOH A . 
E 3 HOH 178 778 803  HOH HOH A . 
E 3 HOH 179 779 892  HOH HOH A . 
E 3 HOH 180 780 937  HOH HOH A . 
E 3 HOH 181 781 808  HOH HOH A . 
E 3 HOH 182 782 810  HOH HOH A . 
E 3 HOH 183 783 772  HOH HOH A . 
E 3 HOH 184 784 798  HOH HOH A . 
E 3 HOH 185 785 775  HOH HOH A . 
E 3 HOH 186 786 890  HOH HOH A . 
E 3 HOH 187 787 819  HOH HOH A . 
E 3 HOH 188 788 812  HOH HOH A . 
E 3 HOH 189 789 841  HOH HOH A . 
E 3 HOH 190 790 87   HOH HOH A . 
E 3 HOH 191 791 838  HOH HOH A . 
E 3 HOH 192 792 909  HOH HOH A . 
E 3 HOH 193 793 855  HOH HOH A . 
E 3 HOH 194 794 707  HOH HOH A . 
E 3 HOH 195 795 817  HOH HOH A . 
E 3 HOH 196 796 68   HOH HOH A . 
E 3 HOH 197 797 871  HOH HOH A . 
E 3 HOH 198 798 832  HOH HOH A . 
E 3 HOH 199 799 52   HOH HOH A . 
E 3 HOH 200 800 38   HOH HOH A . 
E 3 HOH 201 801 836  HOH HOH A . 
E 3 HOH 202 802 20   HOH HOH A . 
E 3 HOH 203 803 948  HOH HOH A . 
E 3 HOH 204 804 922  HOH HOH A . 
E 3 HOH 205 805 1016 HOH HOH A . 
E 3 HOH 206 806 921  HOH HOH A . 
E 3 HOH 207 807 924  HOH HOH A . 
E 3 HOH 208 808 820  HOH HOH A . 
E 3 HOH 209 809 899  HOH HOH A . 
E 3 HOH 210 810 889  HOH HOH A . 
E 3 HOH 211 811 89   HOH HOH A . 
E 3 HOH 212 812 80   HOH HOH A . 
E 3 HOH 213 813 905  HOH HOH A . 
E 3 HOH 214 814 54   HOH HOH A . 
E 3 HOH 215 815 895  HOH HOH A . 
E 3 HOH 216 816 878  HOH HOH A . 
E 3 HOH 217 817 848  HOH HOH A . 
E 3 HOH 218 818 884  HOH HOH A . 
E 3 HOH 219 819 651  HOH HOH A . 
E 3 HOH 220 820 18   HOH HOH A . 
E 3 HOH 221 821 845  HOH HOH A . 
E 3 HOH 222 822 90   HOH HOH A . 
E 3 HOH 223 823 864  HOH HOH A . 
E 3 HOH 224 824 30   HOH HOH A . 
E 3 HOH 225 825 920  HOH HOH A . 
E 3 HOH 226 826 911  HOH HOH A . 
E 3 HOH 227 827 843  HOH HOH A . 
E 3 HOH 228 828 869  HOH HOH A . 
E 3 HOH 229 829 986  HOH HOH A . 
E 3 HOH 230 830 946  HOH HOH A . 
E 3 HOH 231 831 988  HOH HOH A . 
E 3 HOH 232 832 877  HOH HOH A . 
E 3 HOH 233 833 104  HOH HOH A . 
E 3 HOH 234 834 8    HOH HOH A . 
E 3 HOH 235 835 919  HOH HOH A . 
E 3 HOH 236 836 895  HOH HOH A . 
E 3 HOH 237 837 879  HOH HOH A . 
E 3 HOH 238 838 7    HOH HOH A . 
E 3 HOH 239 839 968  HOH HOH A . 
E 3 HOH 240 840 954  HOH HOH A . 
E 3 HOH 241 841 969  HOH HOH A . 
E 3 HOH 242 842 71   HOH HOH A . 
E 3 HOH 243 843 687  HOH HOH A . 
E 3 HOH 244 844 1006 HOH HOH A . 
E 3 HOH 245 845 962  HOH HOH A . 
E 3 HOH 246 846 1003 HOH HOH A . 
E 3 HOH 247 847 872  HOH HOH A . 
E 3 HOH 248 848 982  HOH HOH A . 
E 3 HOH 249 849 998  HOH HOH A . 
E 3 HOH 250 850 74   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 1020 HOH HOH A . 
E 3 HOH 254 854 1036 HOH HOH A . 
E 3 HOH 255 855 965  HOH HOH A . 
F 3 HOH 1   601 771  HOH HOH B . 
F 3 HOH 2   602 874  HOH HOH B . 
F 3 HOH 3   603 797  HOH HOH B . 
F 3 HOH 4   604 658  HOH HOH B . 
F 3 HOH 5   605 43   HOH HOH B . 
F 3 HOH 6   606 845  HOH HOH B . 
F 3 HOH 7   607 609  HOH HOH B . 
F 3 HOH 8   608 624  HOH HOH B . 
F 3 HOH 9   609 710  HOH HOH B . 
F 3 HOH 10  610 652  HOH HOH B . 
F 3 HOH 11  611 714  HOH HOH B . 
F 3 HOH 12  612 865  HOH HOH B . 
F 3 HOH 13  613 606  HOH HOH B . 
F 3 HOH 14  614 706  HOH HOH B . 
F 3 HOH 15  615 607  HOH HOH B . 
F 3 HOH 16  616 35   HOH HOH B . 
F 3 HOH 17  617 611  HOH HOH B . 
F 3 HOH 18  618 698  HOH HOH B . 
F 3 HOH 19  619 708  HOH HOH B . 
F 3 HOH 20  620 637  HOH HOH B . 
F 3 HOH 21  621 612  HOH HOH B . 
F 3 HOH 22  622 601  HOH HOH B . 
F 3 HOH 23  623 726  HOH HOH B . 
F 3 HOH 24  624 695  HOH HOH B . 
F 3 HOH 25  625 618  HOH HOH B . 
F 3 HOH 26  626 772  HOH HOH B . 
F 3 HOH 27  627 752  HOH HOH B . 
F 3 HOH 28  628 25   HOH HOH B . 
F 3 HOH 29  629 817  HOH HOH B . 
F 3 HOH 30  630 36   HOH HOH B . 
F 3 HOH 31  631 26   HOH HOH B . 
F 3 HOH 32  632 696  HOH HOH B . 
F 3 HOH 33  633 853  HOH HOH B . 
F 3 HOH 34  634 621  HOH HOH B . 
F 3 HOH 35  635 616  HOH HOH B . 
F 3 HOH 36  636 610  HOH HOH B . 
F 3 HOH 37  637 713  HOH HOH B . 
F 3 HOH 38  638 956  HOH HOH B . 
F 3 HOH 39  639 5    HOH HOH B . 
F 3 HOH 40  640 699  HOH HOH B . 
F 3 HOH 41  641 641  HOH HOH B . 
F 3 HOH 42  642 619  HOH HOH B . 
F 3 HOH 43  643 693  HOH HOH B . 
F 3 HOH 44  644 720  HOH HOH B . 
F 3 HOH 45  645 93   HOH HOH B . 
F 3 HOH 46  646 614  HOH HOH B . 
F 3 HOH 47  647 754  HOH HOH B . 
F 3 HOH 48  648 16   HOH HOH B . 
F 3 HOH 49  649 654  HOH HOH B . 
F 3 HOH 50  650 646  HOH HOH B . 
F 3 HOH 51  651 678  HOH HOH B . 
F 3 HOH 52  652 775  HOH HOH B . 
F 3 HOH 53  653 24   HOH HOH B . 
F 3 HOH 54  654 668  HOH HOH B . 
F 3 HOH 55  655 645  HOH HOH B . 
F 3 HOH 56  656 657  HOH HOH B . 
F 3 HOH 57  657 728  HOH HOH B . 
F 3 HOH 58  658 682  HOH HOH B . 
F 3 HOH 59  659 655  HOH HOH B . 
F 3 HOH 60  660 94   HOH HOH B . 
F 3 HOH 61  661 826  HOH HOH B . 
F 3 HOH 62  662 763  HOH HOH B . 
F 3 HOH 63  663 737  HOH HOH B . 
F 3 HOH 64  664 801  HOH HOH B . 
F 3 HOH 65  665 636  HOH HOH B . 
F 3 HOH 66  666 818  HOH HOH B . 
F 3 HOH 67  667 681  HOH HOH B . 
F 3 HOH 68  668 662  HOH HOH B . 
F 3 HOH 69  669 873  HOH HOH B . 
F 3 HOH 70  670 866  HOH HOH B . 
F 3 HOH 71  671 676  HOH HOH B . 
F 3 HOH 72  672 904  HOH HOH B . 
F 3 HOH 73  673 763  HOH HOH B . 
F 3 HOH 74  674 758  HOH HOH B . 
F 3 HOH 75  675 708  HOH HOH B . 
F 3 HOH 76  676 638  HOH HOH B . 
F 3 HOH 77  677 806  HOH HOH B . 
F 3 HOH 78  678 651  HOH HOH B . 
F 3 HOH 79  679 700  HOH HOH B . 
F 3 HOH 80  680 702  HOH HOH B . 
F 3 HOH 81  681 707  HOH HOH B . 
F 3 HOH 82  682 861  HOH HOH B . 
F 3 HOH 83  683 685  HOH HOH B . 
F 3 HOH 84  684 738  HOH HOH B . 
F 3 HOH 85  685 769  HOH HOH B . 
F 3 HOH 86  686 829  HOH HOH B . 
F 3 HOH 87  687 780  HOH HOH B . 
F 3 HOH 88  688 762  HOH HOH B . 
F 3 HOH 89  689 730  HOH HOH B . 
F 3 HOH 90  690 794  HOH HOH B . 
F 3 HOH 91  691 800  HOH HOH B . 
F 3 HOH 92  692 813  HOH HOH B . 
F 3 HOH 93  693 848  HOH HOH B . 
F 3 HOH 94  694 688  HOH HOH B . 
F 3 HOH 95  695 785  HOH HOH B . 
F 3 HOH 96  696 630  HOH HOH B . 
F 3 HOH 97  697 83   HOH HOH B . 
F 3 HOH 98  698 644  HOH HOH B . 
F 3 HOH 99  699 683  HOH HOH B . 
F 3 HOH 100 700 100  HOH HOH B . 
F 3 HOH 101 701 625  HOH HOH B . 
F 3 HOH 102 702 819  HOH HOH B . 
F 3 HOH 103 703 107  HOH HOH B . 
F 3 HOH 104 704 887  HOH HOH B . 
F 3 HOH 105 705 832  HOH HOH B . 
F 3 HOH 106 706 58   HOH HOH B . 
F 3 HOH 107 707 91   HOH HOH B . 
F 3 HOH 108 708 782  HOH HOH B . 
F 3 HOH 109 709 753  HOH HOH B . 
F 3 HOH 110 710 740  HOH HOH B . 
F 3 HOH 111 711 724  HOH HOH B . 
F 3 HOH 112 712 786  HOH HOH B . 
F 3 HOH 113 713 739  HOH HOH B . 
F 3 HOH 114 714 757  HOH HOH B . 
F 3 HOH 115 715 912  HOH HOH B . 
F 3 HOH 116 716 631  HOH HOH B . 
F 3 HOH 117 717 855  HOH HOH B . 
F 3 HOH 118 718 732  HOH HOH B . 
F 3 HOH 119 719 709  HOH HOH B . 
F 3 HOH 120 720 690  HOH HOH B . 
F 3 HOH 121 721 666  HOH HOH B . 
F 3 HOH 122 722 834  HOH HOH B . 
F 3 HOH 123 723 862  HOH HOH B . 
F 3 HOH 124 724 10   HOH HOH B . 
F 3 HOH 125 725 735  HOH HOH B . 
F 3 HOH 126 726 674  HOH HOH B . 
F 3 HOH 127 727 776  HOH HOH B . 
F 3 HOH 128 728 751  HOH HOH B . 
F 3 HOH 129 729 742  HOH HOH B . 
F 3 HOH 130 730 736  HOH HOH B . 
F 3 HOH 131 731 640  HOH HOH B . 
F 3 HOH 132 732 816  HOH HOH B . 
F 3 HOH 133 733 860  HOH HOH B . 
F 3 HOH 134 734 770  HOH HOH B . 
F 3 HOH 135 735 656  HOH HOH B . 
F 3 HOH 136 736 840  HOH HOH B . 
F 3 HOH 137 737 628  HOH HOH B . 
F 3 HOH 138 738 642  HOH HOH B . 
F 3 HOH 139 739 703  HOH HOH B . 
F 3 HOH 140 740 767  HOH HOH B . 
F 3 HOH 141 741 774  HOH HOH B . 
F 3 HOH 142 742 796  HOH HOH B . 
F 3 HOH 143 743 865  HOH HOH B . 
F 3 HOH 144 744 799  HOH HOH B . 
F 3 HOH 145 745 802  HOH HOH B . 
F 3 HOH 146 746 716  HOH HOH B . 
F 3 HOH 147 747 629  HOH HOH B . 
F 3 HOH 148 748 870  HOH HOH B . 
F 3 HOH 149 749 822  HOH HOH B . 
F 3 HOH 150 750 756  HOH HOH B . 
F 3 HOH 151 751 824  HOH HOH B . 
F 3 HOH 152 752 792  HOH HOH B . 
F 3 HOH 153 753 704  HOH HOH B . 
F 3 HOH 154 754 882  HOH HOH B . 
F 3 HOH 155 755 773  HOH HOH B . 
F 3 HOH 156 756 718  HOH HOH B . 
F 3 HOH 157 757 839  HOH HOH B . 
F 3 HOH 158 758 727  HOH HOH B . 
F 3 HOH 159 759 639  HOH HOH B . 
F 3 HOH 160 760 793  HOH HOH B . 
F 3 HOH 161 761 633  HOH HOH B . 
F 3 HOH 162 762 779  HOH HOH B . 
F 3 HOH 163 763 759  HOH HOH B . 
F 3 HOH 164 764 947  HOH HOH B . 
F 3 HOH 165 765 830  HOH HOH B . 
F 3 HOH 166 766 797  HOH HOH B . 
F 3 HOH 167 767 715  HOH HOH B . 
F 3 HOH 168 768 803  HOH HOH B . 
F 3 HOH 169 769 765  HOH HOH B . 
F 3 HOH 170 770 852  HOH HOH B . 
F 3 HOH 171 771 889  HOH HOH B . 
F 3 HOH 172 772 770  HOH HOH B . 
F 3 HOH 173 773 837  HOH HOH B . 
F 3 HOH 174 774 75   HOH HOH B . 
F 3 HOH 175 775 812  HOH HOH B . 
F 3 HOH 176 776 744  HOH HOH B . 
F 3 HOH 177 777 743  HOH HOH B . 
F 3 HOH 178 778 864  HOH HOH B . 
F 3 HOH 179 779 781  HOH HOH B . 
F 3 HOH 180 780 789  HOH HOH B . 
F 3 HOH 181 781 701  HOH HOH B . 
F 3 HOH 182 782 795  HOH HOH B . 
F 3 HOH 183 783 649  HOH HOH B . 
F 3 HOH 184 784 747  HOH HOH B . 
F 3 HOH 185 785 844  HOH HOH B . 
F 3 HOH 186 786 749  HOH HOH B . 
F 3 HOH 187 787 791  HOH HOH B . 
F 3 HOH 188 788 29   HOH HOH B . 
F 3 HOH 189 789 731  HOH HOH B . 
F 3 HOH 190 790 815  HOH HOH B . 
F 3 HOH 191 791 810  HOH HOH B . 
F 3 HOH 192 792 863  HOH HOH B . 
F 3 HOH 193 793 854  HOH HOH B . 
F 3 HOH 194 794 673  HOH HOH B . 
F 3 HOH 195 795 804  HOH HOH B . 
F 3 HOH 196 796 888  HOH HOH B . 
F 3 HOH 197 797 868  HOH HOH B . 
F 3 HOH 198 798 828  HOH HOH B . 
F 3 HOH 199 799 741  HOH HOH B . 
F 3 HOH 200 800 857  HOH HOH B . 
F 3 HOH 201 801 32   HOH HOH B . 
F 3 HOH 202 802 851  HOH HOH B . 
F 3 HOH 203 803 47   HOH HOH B . 
F 3 HOH 204 804 838  HOH HOH B . 
F 3 HOH 205 805 891  HOH HOH B . 
F 3 HOH 206 806 92   HOH HOH B . 
F 3 HOH 207 807 755  HOH HOH B . 
F 3 HOH 208 808 745  HOH HOH B . 
F 3 HOH 209 809 760  HOH HOH B . 
F 3 HOH 210 810 872  HOH HOH B . 
F 3 HOH 211 811 809  HOH HOH B . 
F 3 HOH 212 812 784  HOH HOH B . 
F 3 HOH 213 813 905  HOH HOH B . 
F 3 HOH 214 814 935  HOH HOH B . 
F 3 HOH 215 815 877  HOH HOH B . 
F 3 HOH 216 816 761  HOH HOH B . 
F 3 HOH 217 817 856  HOH HOH B . 
F 3 HOH 218 818 896  HOH HOH B . 
F 3 HOH 219 819 859  HOH HOH B . 
F 3 HOH 220 820 843  HOH HOH B . 
F 3 HOH 221 821 57   HOH HOH B . 
F 3 HOH 222 822 827  HOH HOH B . 
F 3 HOH 223 823 901  HOH HOH B . 
F 3 HOH 224 824 86   HOH HOH B . 
F 3 HOH 225 825 831  HOH HOH B . 
F 3 HOH 226 826 88   HOH HOH B . 
F 3 HOH 227 827 878  HOH HOH B . 
F 3 HOH 228 828 886  HOH HOH B . 
F 3 HOH 229 829 850  HOH HOH B . 
F 3 HOH 230 830 777  HOH HOH B . 
F 3 HOH 231 831 22   HOH HOH B . 
F 3 HOH 232 832 823  HOH HOH B . 
F 3 HOH 233 833 748  HOH HOH B . 
F 3 HOH 234 834 56   HOH HOH B . 
F 3 HOH 235 835 892  HOH HOH B . 
F 3 HOH 236 836 932  HOH HOH B . 
F 3 HOH 237 837 899  HOH HOH B . 
F 3 HOH 238 838 798  HOH HOH B . 
F 3 HOH 239 839 907  HOH HOH B . 
F 3 HOH 240 840 608  HOH HOH B . 
F 3 HOH 241 841 913  HOH HOH B . 
F 3 HOH 242 842 102  HOH HOH B . 
F 3 HOH 243 843 95   HOH HOH B . 
F 3 HOH 244 844 933  HOH HOH B . 
F 3 HOH 245 845 79   HOH HOH B . 
F 3 HOH 246 846 31   HOH HOH B . 
F 3 HOH 247 847 959  HOH HOH B . 
F 3 HOH 248 848 931  HOH HOH B . 
F 3 HOH 249 849 712  HOH HOH B . 
F 3 HOH 250 850 807  HOH HOH B . 
F 3 HOH 251 851 62   HOH HOH B . 
F 3 HOH 252 852 920  HOH HOH B . 
F 3 HOH 253 853 808  HOH HOH B . 
F 3 HOH 254 854 966  HOH HOH B . 
F 3 HOH 255 855 660  HOH HOH B . 
F 3 HOH 256 856 963  HOH HOH B . 
F 3 HOH 257 857 65   HOH HOH B . 
F 3 HOH 258 858 917  HOH HOH B . 
F 3 HOH 259 859 910  HOH HOH B . 
F 3 HOH 260 860 691  HOH HOH B . 
F 3 HOH 261 861 937  HOH HOH B . 
F 3 HOH 262 862 950  HOH HOH B . 
F 3 HOH 263 863 944  HOH HOH B . 
F 3 HOH 264 864 958  HOH HOH B . 
F 3 HOH 265 865 983  HOH HOH B . 
F 3 HOH 266 866 971  HOH HOH B . 
F 3 HOH 267 867 973  HOH HOH B . 
F 3 HOH 268 868 949  HOH HOH B . 
F 3 HOH 269 869 939  HOH HOH B . 
F 3 HOH 270 870 982  HOH HOH B . 
F 3 HOH 271 871 991  HOH HOH B . 
F 3 HOH 272 872 105  HOH HOH B . 
F 3 HOH 273 873 929  HOH HOH B . 
F 3 HOH 274 874 1004 HOH HOH B . 
F 3 HOH 275 875 1001 HOH HOH B . 
F 3 HOH 276 876 1005 HOH HOH B . 
F 3 HOH 277 877 1000 HOH HOH B . 
F 3 HOH 278 878 615  HOH HOH B . 
F 3 HOH 279 879 98   HOH HOH B . 
F 3 HOH 280 880 1007 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          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        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                     9EPI 
_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                         9EPI 
_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                   9EPI 
_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         2023-09-06 
_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                                       9EPI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.39 
_reflns.d_resolution_low                               34.10 
_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                                     144168 
_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                                76.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.83 
_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                                   0.900 
_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                                    1.39 
_reflns_shell.d_res_low                                     1.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.85 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7214 
_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                               50.6 
_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                                  0.351 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.25 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.05 
_refine.aniso_B[2][2]                            -0.33 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.10 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               17.971 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.961 
_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                                 9EPI 
_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                            1.39 
_refine.ls_d_res_low                             34.10 
_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                     137006 
_refine.ls_number_reflns_R_free                  7127 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17159 
_refine.ls_R_factor_R_free                       0.19423 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17042 
_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                       0.056 
_refine.pdbx_overall_ESU_R_Free                  0.058 
_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                             1.235 
_refine.overall_SU_ML                            0.047 
_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                       1.39 
_refine_hist.d_res_low                        34.10 
_refine_hist.number_atoms_solvent             535 
_refine_hist.number_atoms_total               6165 
_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' ? 0.011  0.012  5816  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  5409  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.813  1.849  7923  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.619  1.788  12392 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.365  5.000  732   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.350  5.000  62    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.797 10.000 876   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.093  0.200  826   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  7219  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  1471  ? 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' ? 1.675  1.672  2904  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.673  1.671  2903  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.447  3.000  3629  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.448  3.000  3630  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.020  2.010  2912  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.021  2.010  2910  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.688  3.503  4289  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.788  17.67  6445  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.739  17.43  6394  ? 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                       1.390 
_refine_ls_shell.d_res_low                        1.42 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             526 
_refine_ls_shell.number_reflns_R_work             10094 
_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                  0.368 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.368 
# 
_struct.entry_id                     9EPI 
_struct.title                        'DtpAa Y389F 53 fs 10 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        9EPI 
_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 9EPI A 1 ? 373 ? A0A7U9DT46 48 ? 420 ? 48 420 
2 1 9EPI 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 9EPI PHE A 342 ? UNP A0A7U9DT46 TYR 389 'engineered mutation' 389 1 
2 9EPI 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)' 6990  ? 
1 MORE         -62   ? 
1 'SSA (A^2)'  26990 ? 
# 
_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 ? ? ? ? ? ? ? 2.095 ? ? 
metalc2 metalc ? ? C HEM .   FE  ? ? ? 1_555 E HOH . O  ? ? A HEM 501 A HOH 717 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc3 metalc ? ? B HIS 279 NE2 ? ? ? 1_555 D HEM . FE ? ? B HIS 326 B HEM 501 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
metalc4 metalc ? ? D HEM .   FE  ? ? ? 1_555 F HOH . O  A ? B HEM 501 B HOH 703 1_555 ? ? ? ? ? ? ? 2.263 ? ? 
# 
_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 92.5  ? 
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 92.0  ? 
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 90.7  ? 
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 94.3  ? 
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 88.3  ? 
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 95.6  ? 
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 89.3  ? 
9  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 172.4 ? 
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 90.7  ? 
11 NE2 ? A HIS 279 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 717 ? 1_555 170.2 ? 
12 NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 717 ? 1_555 81.4  ? 
13 NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 717 ? 1_555 80.5  ? 
14 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 717 ? 1_555 91.7  ? 
15 ND  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 717 ? 1_555 92.0  ? 
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 94.5  ? 
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 93.2  ? 
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 89.2  ? 
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 96.2  ? 
20 NA  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NC ? D HEM . ? B HEM 501 ? 1_555 169.2 ? 
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 88.2  ? 
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 98.4  ? 
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 90.4  ? 
24 NB  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 168.3 ? 
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 90.0  ? 
26 NE2 ? B HIS 279 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  A F HOH . ? B HOH 703 ? 1_555 174.2 ? 
27 NA  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  A F HOH . ? B HOH 703 ? 1_555 81.8  ? 
28 NB  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  A F HOH . ? B HOH 703 ? 1_555 82.3  ? 
29 NC  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  A F HOH . ? B HOH 703 ? 1_555 87.4  ? 
30 ND  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  A F HOH . ? B HOH 703 ? 1_555 86.0  ? 
# 
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 LEU A 135 ? O LEU A 182 N PHE A 34  ? N PHE A 81  
AA1 3 4 N PHE A 31  ? N PHE A 78  O GLN A 168 ? O GLN A 215 
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 ALA B 33  ? N ALA B 80  O TRP B 166 ? O TRP B 213 
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                   9EPI 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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 766 ? ? O B HOH 772 ? ? 1.82 
2 1 O A HOH 602 ? ? O A HOH 604 ? ? 2.06 
3 1 O B HOH 747 ? ? O B HOH 843 ? ? 2.11 
4 1 O A HOH 772 ? ? O A HOH 849 ? ? 2.14 
# 
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 115.59 120.30 -4.71 0.50 N 
2 1 NE A ARG 199 ? ? CZ A ARG 199 ? ? NH2 A ARG 199 ? ? 117.24 120.30 -3.06 0.50 N 
3 1 NE A ARG 251 ? ? CZ A ARG 251 ? ? NH1 A ARG 251 ? ? 123.83 120.30 3.53  0.50 N 
4 1 NE B ARG 251 ? ? CZ B ARG 251 ? ? NH1 B ARG 251 ? ? 124.19 120.30 3.89  0.50 N 
5 1 NE B ARG 251 ? ? CZ B ARG 251 ? ? NH2 B ARG 251 ? ? 116.27 120.30 -4.03 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  ? ? -117.29 -73.00  
2 1 ASN A 243 ? ? -116.44 -156.04 
3 1 ARG A 343 ? ? -147.70 36.45   
4 1 ASP A 349 ? ? -119.82 62.24   
5 1 PRO A 402 ? ? -59.60  171.64  
6 1 ARG B 343 ? ? -147.11 43.36   
7 1 PRO B 402 ? ? -58.98  172.83  
# 
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 242 ? ? 0.099 'SIDE CHAIN' 
2 1 ARG B 242 ? ? 0.101 'SIDE CHAIN' 
3 1 ARG B 251 ? ? 0.081 'SIDE CHAIN' 
4 1 ARG B 279 ? ? 0.077 'SIDE CHAIN' 
5 1 ARG B 313 ? ? 0.085 'SIDE CHAIN' 
# 
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                 10 
_pdbx_serial_crystallography_measurement.pulse_duration               46 
_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                    9EPI 
_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   ? 17.316  -18.410 23.476  1.00 32.14 ? 55  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 8   ? 18.279  -17.887 24.469  1.00 29.63 ? 55  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 8   ? 19.707  -18.320 24.144  1.00 26.47 ? 55  GLY A C   1 
ATOM   4    O  O   . GLY A 1 8   ? 20.646  -17.826 24.755  1.00 25.30 ? 55  GLY A O   1 
ATOM   5    N  N   . SER A 1 9   ? 19.850  -19.187 23.135  1.00 26.67 ? 56  SER A N   1 
ATOM   6    C  CA  . SER A 1 9   ? 21.126  -19.794 22.806  1.00 26.82 ? 56  SER A CA  1 
ATOM   7    C  C   . SER A 1 9   ? 22.084  -18.757 22.217  1.00 22.49 ? 56  SER A C   1 
ATOM   8    O  O   . SER A 1 9   ? 21.715  -17.647 21.842  1.00 21.41 ? 56  SER A O   1 
ATOM   9    C  CB  . SER A 1 9   ? 20.922  -20.985 21.883  1.00 31.89 ? 56  SER A CB  1 
ATOM   10   O  OG  . SER A 1 9   ? 20.472  -20.580 20.595  1.00 35.84 ? 56  SER A OG  1 
ATOM   11   N  N   . ALA A 1 10  ? 23.375  -19.086 22.267  1.00 21.69 ? 57  ALA A N   1 
ATOM   12   C  CA  . ALA A 1 10  ? 24.408  -18.275 21.668  1.00 20.46 ? 57  ALA A CA  1 
ATOM   13   C  C   . ALA A 1 10  ? 24.524  -18.611 20.186  1.00 20.31 ? 57  ALA A C   1 
ATOM   14   O  O   . ALA A 1 10  ? 24.247  -19.712 19.719  1.00 22.70 ? 57  ALA A O   1 
ATOM   15   C  CB  . ALA A 1 10  ? 25.712  -18.470 22.402  1.00 21.95 ? 57  ALA A CB  1 
ATOM   16   N  N   . VAL A 1 11  ? 24.899  -17.600 19.426  1.00 15.90 ? 58  VAL A N   1 
ATOM   17   C  CA  . VAL A 1 11  ? 25.277  -17.751 18.039  1.00 14.90 ? 58  VAL A CA  1 
ATOM   18   C  C   . VAL A 1 11  ? 26.783  -17.675 17.996  1.00 14.26 ? 58  VAL A C   1 
ATOM   19   O  O   . VAL A 1 11  ? 27.380  -16.749 18.524  1.00 14.97 ? 58  VAL A O   1 
ATOM   20   C  CB  . VAL A 1 11  ? 24.653  -16.644 17.186  1.00 15.81 ? 58  VAL A CB  1 
ATOM   21   C  CG1 . VAL A 1 11  ? 25.151  -16.679 15.764  1.00 15.94 ? 58  VAL A CG1 1 
ATOM   22   C  CG2 . VAL A 1 11  ? 23.141  -16.717 17.191  1.00 17.48 ? 58  VAL A CG2 1 
ATOM   23   N  N   . PRO A 1 12  ? 27.464  -18.660 17.370  1.00 15.44 ? 59  PRO A N   1 
ATOM   24   C  CA  . PRO A 1 12  ? 28.924  -18.599 17.346  1.00 16.37 ? 59  PRO A CA  1 
ATOM   25   C  C   . PRO A 1 12  ? 29.428  -17.311 16.727  1.00 15.81 ? 59  PRO A C   1 
ATOM   26   O  O   . PRO A 1 12  ? 28.958  -16.850 15.687  1.00 16.51 ? 59  PRO A O   1 
ATOM   27   C  CB  . PRO A 1 12  ? 29.345  -19.819 16.558  1.00 18.97 ? 59  PRO A CB  1 
ATOM   28   C  CG  . PRO A 1 12  ? 28.121  -20.707 16.488  1.00 19.75 ? 59  PRO A CG  1 
ATOM   29   C  CD  . PRO A 1 12  ? 26.885  -19.833 16.681  1.00 17.94 ? 59  PRO A CD  1 
ATOM   30   N  N   . PHE A 1 13  ? 30.477  -16.763 17.327  1.00 15.62 ? 60  PHE A N   1 
ATOM   31   C  CA  . PHE A 1 13  ? 31.009  -15.476 16.937  1.00 14.87 ? 60  PHE A CA  1 
ATOM   32   C  C   . PHE A 1 13  ? 32.025  -15.613 15.824  1.00 16.07 ? 60  PHE A C   1 
ATOM   33   O  O   . PHE A 1 13  ? 32.112  -14.757 14.934  1.00 15.33 ? 60  PHE A O   1 
ATOM   34   C  CB  . PHE A 1 13  ? 31.613  -14.812 18.166  1.00 15.44 ? 60  PHE A CB  1 
ATOM   35   C  CG  . PHE A 1 13  ? 32.303  -13.497 17.904  1.00 16.00 ? 60  PHE A CG  1 
ATOM   36   C  CD1 . PHE A 1 13  ? 31.579  -12.369 17.556  1.00 15.25 ? 60  PHE A CD1 1 
ATOM   37   C  CD2 . PHE A 1 13  ? 33.677  -13.382 17.941  1.00 16.32 ? 60  PHE A CD2 1 
ATOM   38   C  CE1 . PHE A 1 13  ? 32.206  -11.180 17.264  1.00 16.28 ? 60  PHE A CE1 1 
ATOM   39   C  CE2 . PHE A 1 13  ? 34.291  -12.182 17.655  1.00 17.13 ? 60  PHE A CE2 1 
ATOM   40   C  CZ  . PHE A 1 13  ? 33.557  -11.080 17.311  1.00 15.98 ? 60  PHE A CZ  1 
ATOM   41   N  N   . HIS A 1 14  ? 32.858  -16.657 15.925  1.00 16.06 ? 61  HIS A N   1 
ATOM   42   C  CA  . HIS A 1 14  ? 33.925  -16.879 14.972  1.00 15.20 ? 61  HIS A CA  1 
ATOM   43   C  C   . HIS A 1 14  ? 33.399  -17.550 13.703  1.00 14.91 ? 61  HIS A C   1 
ATOM   44   O  O   . HIS A 1 14  ? 32.407  -18.300 13.685  1.00 16.86 ? 61  HIS A O   1 
ATOM   45   C  CB  . HIS A 1 14  ? 35.010  -17.774 15.571  1.00 14.76 ? 61  HIS A CB  1 
ATOM   46   C  CG  . HIS A 1 14  ? 35.732  -17.148 16.703  1.00 16.06 ? 61  HIS A CG  1 
ATOM   47   N  ND1 . HIS A 1 14  ? 36.106  -17.915 17.798  1.00 17.80 ? 61  HIS A ND1 1 
ATOM   48   C  CD2 . HIS A 1 14  ? 36.182  -15.918 16.958  1.00 16.62 ? 61  HIS A CD2 1 
ATOM   49   C  CE1 . HIS A 1 14  ? 36.791  -17.132 18.637  1.00 18.20 ? 61  HIS A CE1 1 
ATOM   50   N  NE2 . HIS A 1 14  ? 36.825  -15.919 18.165  1.00 16.29 ? 61  HIS A NE2 1 
ATOM   51   N  N   . GLY A 1 15  ? 34.105  -17.291 12.619  1.00 16.49 ? 62  GLY A N   1 
ATOM   52   C  CA  . GLY A 1 15  ? 33.737  -17.901 11.358  1.00 17.07 ? 62  GLY A CA  1 
ATOM   53   C  C   . GLY A 1 15  ? 34.415  -17.197 10.206  1.00 16.20 ? 62  GLY A C   1 
ATOM   54   O  O   . GLY A 1 15  ? 35.078  -16.170 10.383  1.00 16.81 ? 62  GLY A O   1 
ATOM   55   N  N   . ALA A 1 16  ? 34.234  -17.786 9.021   1.00 17.08 ? 63  ALA A N   1 
ATOM   56   C  CA  . ALA A 1 16  ? 34.775  -17.187 7.815   1.00 17.64 ? 63  ALA A CA  1 
ATOM   57   C  C   . ALA A 1 16  ? 34.045  -15.884 7.499   1.00 16.46 ? 63  ALA A C   1 
ATOM   58   O  O   . ALA A 1 16  ? 34.614  -14.978 6.931   1.00 16.82 ? 63  ALA A O   1 
ATOM   59   C  CB  . ALA A 1 16  ? 34.658  -18.162 6.660   1.00 20.17 ? 63  ALA A CB  1 
ATOM   60   N  N   . HIS A 1 17  ? 32.789  -15.827 7.929   1.00 16.36 ? 64  HIS A N   1 
ATOM   61   C  CA  . HIS A 1 17  ? 31.981  -14.640 7.769   1.00 15.96 ? 64  HIS A CA  1 
ATOM   62   C  C   . HIS A 1 17  ? 31.563  -14.165 9.154   1.00 15.81 ? 64  HIS A C   1 
ATOM   63   O  O   . HIS A 1 17  ? 31.526  -14.922 10.112  1.00 15.78 ? 64  HIS A O   1 
ATOM   64   C  CB  . HIS A 1 17  ? 30.712  -14.949 6.982   1.00 16.48 ? 64  HIS A CB  1 
ATOM   65   C  CG  . HIS A 1 17  ? 30.954  -15.674 5.689   1.00 17.12 ? 64  HIS A CG  1 
ATOM   66   N  ND1 . HIS A 1 17  ? 31.673  -15.125 4.657   1.00 16.74 ? 64  HIS A ND1 1 
ATOM   67   C  CD2 . HIS A 1 17  ? 30.625  -16.907 5.336   1.00 18.40 ? 64  HIS A CD2 1 
ATOM   68   C  CE1 . HIS A 1 17  ? 31.755  -16.033 3.698   1.00 18.85 ? 64  HIS A CE1 1 
ATOM   69   N  NE2 . HIS A 1 17  ? 31.143  -17.108 4.085   1.00 18.60 ? 64  HIS A NE2 1 
ATOM   70   N  N   . GLN A 1 18  ? 31.232  -12.877 9.255   1.00 12.99 ? 65  GLN A N   1 
ATOM   71   C  CA  . GLN A 1 18  ? 30.606  -12.373 10.461  1.00 13.23 ? 65  GLN A CA  1 
ATOM   72   C  C   . GLN A 1 18  ? 29.188  -12.918 10.579  1.00 13.41 ? 65  GLN A C   1 
ATOM   73   O  O   . GLN A 1 18  ? 28.500  -13.078 9.594   1.00 14.43 ? 65  GLN A O   1 
ATOM   74   C  CB  . GLN A 1 18  ? 30.523  -10.850 10.427  1.00 12.60 ? 65  GLN A CB  1 
ATOM   75   C  CG  . GLN A 1 18  ? 31.883  -10.189 10.537  1.00 12.78 ? 65  GLN A CG  1 
ATOM   76   C  CD  . GLN A 1 18  ? 31.764  -8.711  10.803  1.00 14.16 ? 65  GLN A CD  1 
ATOM   77   O  OE1 . GLN A 1 18  ? 31.269  -8.288  11.835  1.00 14.23 ? 65  GLN A OE1 1 
ATOM   78   N  NE2 . GLN A 1 18  ? 32.138  -7.887  9.850   1.00 14.03 ? 65  GLN A NE2 1 
ATOM   79   N  N   . ALA A 1 19  ? 28.798  -13.213 11.802  1.00 13.18 ? 66  ALA A N   1 
ATOM   80   C  CA  . ALA A 1 19  ? 27.418  -13.549 12.100  1.00 12.76 ? 66  ALA A CA  1 
ATOM   81   C  C   . ALA A 1 19  ? 26.583  -12.288 11.993  1.00 13.26 ? 66  ALA A C   1 
ATOM   82   O  O   . ALA A 1 19  ? 27.123  -11.189 11.939  1.00 15.02 ? 66  ALA A O   1 
ATOM   83   C  CB  . ALA A 1 19  ? 27.321  -14.143 13.478  1.00 13.74 ? 66  ALA A CB  1 
ATOM   84   N  N   . GLY A 1 20  ? 25.264  -12.465 11.940  1.00 12.69 ? 67  GLY A N   1 
ATOM   85   C  CA  . GLY A 1 20  ? 24.379  -11.327 11.872  1.00 13.90 ? 67  GLY A CA  1 
ATOM   86   C  C   . GLY A 1 20  ? 23.907  -10.992 10.470  1.00 14.42 ? 67  GLY A C   1 
ATOM   87   O  O   . GLY A 1 20  ? 23.229  -9.987  10.317  1.00 13.46 ? 67  GLY A O   1 
ATOM   88   N  N   . ILE A 1 21  ? 24.262  -11.813 9.479   1.00 13.30 ? 68  ILE A N   1 
ATOM   89   C  CA  . ILE A 1 21  ? 23.930  -11.588 8.092   1.00 13.35 ? 68  ILE A CA  1 
ATOM   90   C  C   . ILE A 1 21  ? 23.044  -12.726 7.616   1.00 14.61 ? 68  ILE A C   1 
ATOM   91   O  O   . ILE A 1 21  ? 21.835  -12.586 7.490   1.00 14.67 ? 68  ILE A O   1 
ATOM   92   C  CB  . ILE A 1 21  ? 25.206  -11.386 7.261   1.00 14.62 ? 68  ILE A CB  1 
ATOM   93   C  CG1 . ILE A 1 21  ? 26.013  -10.237 7.826   1.00 17.77 ? 68  ILE A CG1 1 
ATOM   94   C  CG2 . ILE A 1 21  ? 24.840  -11.153 5.798   1.00 16.42 ? 68  ILE A CG2 1 
ATOM   95   C  CD1 . ILE A 1 21  ? 27.390  -10.041 7.205   1.00 21.33 ? 68  ILE A CD1 1 
ATOM   96   N  N   . ALA A 1 22  ? 23.641  -13.897 7.432   1.00 13.51 ? 69  ALA A N   1 
ATOM   97   C  CA  . ALA A 1 22  ? 22.898  -15.095 7.067   1.00 15.43 ? 69  ALA A CA  1 
ATOM   98   C  C   . ALA A 1 22  ? 22.192  -15.742 8.249   1.00 15.73 ? 69  ALA A C   1 
ATOM   99   O  O   . ALA A 1 22  ? 21.324  -16.582 8.037   1.00 18.12 ? 69  ALA A O   1 
ATOM   100  C  CB  . ALA A 1 22  ? 23.843  -16.123 6.437   1.00 17.59 ? 69  ALA A CB  1 
ATOM   101  N  N   . THR A 1 23  ? 22.620  -15.410 9.470   1.00 14.56 ? 70  THR A N   1 
ATOM   102  C  CA  . THR A 1 23  ? 22.023  -15.846 10.721  1.00 14.21 ? 70  THR A CA  1 
ATOM   103  C  C   . THR A 1 23  ? 20.532  -15.661 10.667  1.00 14.22 ? 70  THR A C   1 
ATOM   104  O  O   . THR A 1 23  ? 20.067  -14.646 10.157  1.00 12.94 ? 70  THR A O   1 
ATOM   105  C  CB  . THR A 1 23  ? 22.563  -14.968 11.859  1.00 15.39 ? 70  THR A CB  1 
ATOM   106  O  OG1 . THR A 1 23  ? 23.974  -14.925 11.785  1.00 18.83 ? 70  THR A OG1 1 
ATOM   107  C  CG2 . THR A 1 23  ? 22.100  -15.449 13.225  1.00 18.83 ? 70  THR A CG2 1 
ATOM   108  N  N   . PRO A 1 24  ? 19.724  -16.541 11.296  1.00 14.33 ? 71  PRO A N   1 
ATOM   109  C  CA  . PRO A 1 24  ? 18.308  -16.266 11.497  1.00 13.73 ? 71  PRO A CA  1 
ATOM   110  C  C   . PRO A 1 24  ? 18.130  -14.896 12.117  1.00 13.23 ? 71  PRO A C   1 
ATOM   111  O  O   . PRO A 1 24  ? 18.882  -14.447 12.985  1.00 13.54 ? 71  PRO A O   1 
ATOM   112  C  CB  . PRO A 1 24  ? 17.889  -17.422 12.423  1.00 14.71 ? 71  PRO A CB  1 
ATOM   113  C  CG  . PRO A 1 24  ? 18.805  -18.555 12.009  1.00 15.64 ? 71  PRO A CG  1 
ATOM   114  C  CD  . PRO A 1 24  ? 20.129  -17.845 11.868  1.00 14.73 ? 71  PRO A CD  1 
ATOM   115  N  N   . VAL A 1 25  ? 17.075  -14.229 11.655  1.00 12.36 ? 72  VAL A N   1 
ATOM   116  C  CA  . VAL A 1 25  ? 16.871  -12.861 12.054  1.00 12.19 ? 72  VAL A CA  1 
ATOM   117  C  C   . VAL A 1 25  ? 16.258  -12.783 13.439  1.00 12.00 ? 72  VAL A C   1 
ATOM   118  O  O   . VAL A 1 25  ? 15.190  -13.344 13.675  1.00 14.14 ? 72  VAL A O   1 
ATOM   119  C  CB  . VAL A 1 25  ? 15.985  -12.109 11.058  1.00 12.92 ? 72  VAL A CB  1 
ATOM   120  C  CG1 . VAL A 1 25  ? 15.831  -10.662 11.453  1.00 13.74 ? 72  VAL A CG1 1 
ATOM   121  C  CG2 . VAL A 1 25  ? 16.549  -12.197 9.665   1.00 12.39 ? 72  VAL A CG2 1 
ATOM   122  N  N   . GLN A 1 26  ? 16.952  -12.084 14.321  1.00 12.93 ? 73  GLN A N   1 
ATOM   123  C  CA  . GLN A 1 26  ? 16.573  -12.000 15.698  1.00 12.16 ? 73  GLN A CA  1 
ATOM   124  C  C   . GLN A 1 26  ? 15.499  -10.930 15.869  1.00 13.46 ? 73  GLN A C   1 
ATOM   125  O  O   . GLN A 1 26  ? 15.280  -10.068 15.014  1.00 13.18 ? 73  GLN A O   1 
ATOM   126  C  CB  . GLN A 1 26  ? 17.786  -11.691 16.561  1.00 12.48 ? 73  GLN A CB  1 
ATOM   127  C  CG  . GLN A 1 26  ? 18.945  -12.655 16.337  1.00 12.49 ? 73  GLN A CG  1 
ATOM   128  C  CD  . GLN A 1 26  ? 19.992  -12.095 15.408  1.00 13.04 ? 73  GLN A CD  1 
ATOM   129  O  OE1 . GLN A 1 26  ? 19.674  -11.566 14.344  1.00 12.72 ? 73  GLN A OE1 1 
ATOM   130  N  NE2 . GLN A 1 26  ? 21.254  -12.211 15.797  1.00 13.57 ? 73  GLN A NE2 1 
ATOM   131  N  N   . ASP A 1 27  ? 14.844  -10.927 17.033  1.00 12.80 ? 74  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 27  ? 13.674  -10.070 17.173  1.00 14.37 ? 74  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 27  ? 13.998  -8.595  17.255  1.00 14.10 ? 74  ASP A C   1 
ATOM   134  O  O   . ASP A 1 27  ? 13.142  -7.775  16.900  1.00 16.00 ? 74  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 27  ? 12.867  -10.521 18.375  1.00 16.00 ? 74  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 27  ? 12.186  -11.858 18.216  1.00 22.29 ? 74  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 27  ? 11.998  -12.288 17.086  1.00 27.17 ? 74  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 27  ? 11.920  -12.466 19.261  1.00 26.30 ? 74  ASP A OD2 1 
ATOM   139  N  N   . ARG A 1 28  ? 15.152  -8.194  17.747  1.00 13.57 ? 75  ARG A N   1 
ATOM   140  C  CA  A ARG A 1 28  ? 15.404  -6.794  18.027  0.50 13.21 ? 75  ARG A CA  1 
ATOM   141  C  CA  B ARG A 1 28  ? 15.414  -6.801  18.054  0.50 14.07 ? 75  ARG A CA  1 
ATOM   142  C  C   . ARG A 1 28  ? 16.714  -6.342  17.409  1.00 14.16 ? 75  ARG A C   1 
ATOM   143  O  O   . ARG A 1 28  ? 17.661  -7.106  17.262  1.00 14.36 ? 75  ARG A O   1 
ATOM   144  C  CB  A ARG A 1 28  ? 15.540  -6.532  19.529  0.50 13.63 ? 75  ARG A CB  1 
ATOM   145  C  CB  B ARG A 1 28  ? 15.606  -6.613  19.564  0.50 15.89 ? 75  ARG A CB  1 
ATOM   146  C  CG  A ARG A 1 28  ? 14.302  -6.937  20.308  0.50 14.72 ? 75  ARG A CG  1 
ATOM   147  C  CG  B ARG A 1 28  ? 14.665  -7.396  20.468  0.50 18.57 ? 75  ARG A CG  1 
ATOM   148  C  CD  A ARG A 1 28  ? 13.179  -5.965  20.120  0.50 15.86 ? 75  ARG A CD  1 
ATOM   149  C  CD  B ARG A 1 28  ? 13.321  -6.751  20.558  0.50 20.93 ? 75  ARG A CD  1 
ATOM   150  N  NE  A ARG A 1 28  ? 13.542  -4.615  20.560  0.50 14.86 ? 75  ARG A NE  1 
ATOM   151  N  NE  B ARG A 1 28  ? 12.335  -7.381  19.691  0.50 21.54 ? 75  ARG A NE  1 
ATOM   152  C  CZ  A ARG A 1 28  ? 12.760  -3.787  21.216  0.50 15.54 ? 75  ARG A CZ  1 
ATOM   153  C  CZ  B ARG A 1 28  ? 11.103  -7.764  20.057  0.50 18.02 ? 75  ARG A CZ  1 
ATOM   154  N  NH1 A ARG A 1 28  ? 11.641  -4.248  21.747  0.50 16.40 ? 75  ARG A NH1 1 
ATOM   155  N  NH1 B ARG A 1 28  ? 10.753  -7.705  21.364  0.50 17.53 ? 75  ARG A NH1 1 
ATOM   156  N  NH2 A ARG A 1 28  ? 13.168  -2.539  21.389  0.50 16.30 ? 75  ARG A NH2 1 
ATOM   157  N  NH2 B ARG A 1 28  ? 10.250  -7.969  19.066  0.50 11.74 ? 75  ARG A NH2 1 
ATOM   158  N  N   . LEU A 1 29  ? 16.790  -5.059  17.131  1.00 12.42 ? 76  LEU A N   1 
ATOM   159  C  CA  . LEU A 1 29  ? 17.952  -4.407  16.592  1.00 12.21 ? 76  LEU A CA  1 
ATOM   160  C  C   . LEU A 1 29  ? 18.336  -3.210  17.424  1.00 13.59 ? 76  LEU A C   1 
ATOM   161  O  O   . LEU A 1 29  ? 17.479  -2.371  17.784  1.00 13.90 ? 76  LEU A O   1 
ATOM   162  C  CB  . LEU A 1 29  ? 17.616  -3.943  15.177  1.00 13.44 ? 76  LEU A CB  1 
ATOM   163  C  CG  . LEU A 1 29  ? 18.660  -3.065  14.482  1.00 13.63 ? 76  LEU A CG  1 
ATOM   164  C  CD1 . LEU A 1 29  ? 19.878  -3.866  14.054  1.00 16.38 ? 76  LEU A CD1 1 
ATOM   165  C  CD2 . LEU A 1 29  ? 18.064  -2.340  13.288  1.00 14.78 ? 76  LEU A CD2 1 
ATOM   166  N  N   . HIS A 1 30  ? 19.639  -3.014  17.609  1.00 13.11 ? 77  HIS A N   1 
ATOM   167  C  CA  . HIS A 1 30  ? 20.173  -1.733  18.007  1.00 13.16 ? 77  HIS A CA  1 
ATOM   168  C  C   . HIS A 1 30  ? 21.370  -1.454  17.125  1.00 12.72 ? 77  HIS A C   1 
ATOM   169  O  O   . HIS A 1 30  ? 22.381  -2.168  17.141  1.00 13.92 ? 77  HIS A O   1 
ATOM   170  C  CB  . HIS A 1 30  ? 20.583  -1.722  19.475  1.00 14.27 ? 77  HIS A CB  1 
ATOM   171  C  CG  . HIS A 1 30  ? 20.924  -0.400  20.006  1.00 16.76 ? 77  HIS A CG  1 
ATOM   172  N  ND1 . HIS A 1 30  ? 20.718  -0.192  21.354  1.00 22.15 ? 77  HIS A ND1 1 
ATOM   173  C  CD2 . HIS A 1 30  ? 21.470  0.692   19.513  1.00 19.90 ? 77  HIS A CD2 1 
ATOM   174  C  CE1 . HIS A 1 30  ? 21.074  1.050   21.629  1.00 22.20 ? 77  HIS A CE1 1 
ATOM   175  N  NE2 . HIS A 1 30  ? 21.548  1.627   20.549  1.00 20.78 ? 77  HIS A NE2 1 
ATOM   176  N  N   . PHE A 1 31  ? 21.207  -0.502  16.224  1.00 13.03 ? 78  PHE A N   1 
ATOM   177  C  CA  . PHE A 1 31  ? 22.203  -0.188  15.225  1.00 12.67 ? 78  PHE A CA  1 
ATOM   178  C  C   . PHE A 1 31  ? 22.860  1.134   15.589  1.00 13.76 ? 78  PHE A C   1 
ATOM   179  O  O   . PHE A 1 31  ? 22.148  2.101   15.880  1.00 16.81 ? 78  PHE A O   1 
ATOM   180  C  CB  . PHE A 1 31  ? 21.514  -0.098  13.866  1.00 13.93 ? 78  PHE A CB  1 
ATOM   181  C  CG  . PHE A 1 31  ? 22.476  -0.031  12.699  1.00 14.07 ? 78  PHE A CG  1 
ATOM   182  C  CD1 . PHE A 1 31  ? 23.106  1.163   12.338  1.00 15.07 ? 78  PHE A CD1 1 
ATOM   183  C  CD2 . PHE A 1 31  ? 22.735  -1.158  11.946  1.00 15.41 ? 78  PHE A CD2 1 
ATOM   184  C  CE1 . PHE A 1 31  ? 23.971  1.195   11.242  1.00 15.92 ? 78  PHE A CE1 1 
ATOM   185  C  CE2 . PHE A 1 31  ? 23.601  -1.092  10.875  1.00 16.48 ? 78  PHE A CE2 1 
ATOM   186  C  CZ  . PHE A 1 31  ? 24.210  0.084   10.543  1.00 16.23 ? 78  PHE A CZ  1 
ATOM   187  N  N   . ALA A 1 32  ? 24.169  1.178   15.639  1.00 13.73 ? 79  ALA A N   1 
ATOM   188  C  CA  . ALA A 1 32  ? 24.861  2.420   15.921  1.00 15.13 ? 79  ALA A CA  1 
ATOM   189  C  C   . ALA A 1 32  ? 25.882  2.706   14.846  1.00 15.66 ? 79  ALA A C   1 
ATOM   190  O  O   . ALA A 1 32  ? 26.661  1.835   14.480  1.00 15.61 ? 79  ALA A O   1 
ATOM   191  C  CB  . ALA A 1 32  ? 25.534  2.381   17.291  1.00 16.47 ? 79  ALA A CB  1 
ATOM   192  N  N   . ALA A 1 33  ? 25.934  3.970   14.415  1.00 14.73 ? 80  ALA A N   1 
ATOM   193  C  CA  . ALA A 1 33  ? 26.997  4.455   13.565  1.00 15.22 ? 80  ALA A CA  1 
ATOM   194  C  C   . ALA A 1 33  ? 27.917  5.338   14.398  1.00 14.86 ? 80  ALA A C   1 
ATOM   195  O  O   . ALA A 1 33  ? 27.439  6.154   15.178  1.00 17.88 ? 80  ALA A O   1 
ATOM   196  C  CB  . ALA A 1 33  ? 26.412  5.271   12.393  1.00 17.69 ? 80  ALA A CB  1 
ATOM   197  N  N   . PHE A 1 34  ? 29.205  5.166   14.216  1.00 15.65 ? 81  PHE A N   1 
ATOM   198  C  CA  . PHE A 1 34  ? 30.211  5.885   14.987  1.00 15.57 ? 81  PHE A CA  1 
ATOM   199  C  C   . PHE A 1 34  ? 31.101  6.661   14.041  1.00 17.35 ? 81  PHE A C   1 
ATOM   200  O  O   . PHE A 1 34  ? 31.364  6.205   12.947  1.00 17.72 ? 81  PHE A O   1 
ATOM   201  C  CB  . PHE A 1 34  ? 31.130  4.943   15.757  1.00 17.44 ? 81  PHE A CB  1 
ATOM   202  C  CG  . PHE A 1 34  ? 30.502  4.033   16.797  1.00 16.31 ? 81  PHE A CG  1 
ATOM   203  C  CD1 . PHE A 1 34  ? 29.854  2.857   16.430  1.00 18.75 ? 81  PHE A CD1 1 
ATOM   204  C  CD2 . PHE A 1 34  ? 30.618  4.333   18.152  1.00 19.90 ? 81  PHE A CD2 1 
ATOM   205  C  CE1 . PHE A 1 34  ? 29.303  2.050   17.406  1.00 20.20 ? 81  PHE A CE1 1 
ATOM   206  C  CE2 . PHE A 1 34  ? 30.087  3.498   19.112  1.00 22.01 ? 81  PHE A CE2 1 
ATOM   207  C  CZ  . PHE A 1 34  ? 29.439  2.371   18.734  1.00 20.59 ? 81  PHE A CZ  1 
ATOM   208  N  N   . ASP A 1 35  ? 31.572  7.812   14.523  1.00 17.31 ? 82  ASP A N   1 
ATOM   209  C  CA  . ASP A 1 35  ? 32.647  8.546   13.865  1.00 18.44 ? 82  ASP A CA  1 
ATOM   210  C  C   . ASP A 1 35  ? 33.922  8.353   14.678  1.00 16.67 ? 82  ASP A C   1 
ATOM   211  O  O   . ASP A 1 35  ? 33.845  8.247   15.893  1.00 18.24 ? 82  ASP A O   1 
ATOM   212  C  CB  . ASP A 1 35  ? 32.286  10.018  13.695  1.00 18.43 ? 82  ASP A CB  1 
ATOM   213  C  CG  . ASP A 1 35  ? 31.270  10.255  12.585  1.00 20.11 ? 82  ASP A CG  1 
ATOM   214  O  OD1 . ASP A 1 35  ? 31.184  9.390   11.670  1.00 20.27 ? 82  ASP A OD1 1 
ATOM   215  O  OD2 . ASP A 1 35  ? 30.598  11.299  12.642  1.00 22.25 ? 82  ASP A OD2 1 
ATOM   216  N  N   . VAL A 1 36  ? 35.064  8.370   14.001  1.00 18.91 ? 83  VAL A N   1 
ATOM   217  C  CA  . VAL A 1 36  ? 36.353  8.177   14.644  1.00 20.83 ? 83  VAL A CA  1 
ATOM   218  C  C   . VAL A 1 36  ? 36.961  9.540   14.967  1.00 21.48 ? 83  VAL A C   1 
ATOM   219  O  O   . VAL A 1 36  ? 36.853  10.456  14.163  1.00 22.86 ? 83  VAL A O   1 
ATOM   220  C  CB  . VAL A 1 36  ? 37.257  7.369   13.706  1.00 21.52 ? 83  VAL A CB  1 
ATOM   221  C  CG1 . VAL A 1 36  ? 38.673  7.269   14.262  1.00 24.70 ? 83  VAL A CG1 1 
ATOM   222  C  CG2 . VAL A 1 36  ? 36.688  5.990   13.415  1.00 22.27 ? 83  VAL A CG2 1 
ATOM   223  N  N   . THR A 1 37  ? 37.461  9.671   16.206  1.00 22.21 ? 84  THR A N   1 
ATOM   224  C  CA  . THR A 1 37  ? 38.017  10.929  16.685  1.00 24.32 ? 84  THR A CA  1 
ATOM   225  C  C   . THR A 1 37  ? 39.503  10.826  16.996  1.00 26.31 ? 84  THR A C   1 
ATOM   226  O  O   . THR A 1 37  ? 40.036  11.760  17.575  1.00 35.31 ? 84  THR A O   1 
ATOM   227  C  CB  . THR A 1 37  ? 37.263  11.413  17.914  1.00 25.83 ? 84  THR A CB  1 
ATOM   228  O  OG1 . THR A 1 37  ? 37.359  10.437  18.946  1.00 27.68 ? 84  THR A OG1 1 
ATOM   229  C  CG2 . THR A 1 37  ? 35.800  11.642  17.589  1.00 26.18 ? 84  THR A CG2 1 
ATOM   230  N  N   . THR A 1 38  ? 40.164  9.741   16.631  1.00 23.97 ? 85  THR A N   1 
ATOM   231  C  CA  . THR A 1 38  ? 41.602  9.638   16.827  1.00 24.60 ? 85  THR A CA  1 
ATOM   232  C  C   . THR A 1 38  ? 42.253  9.644   15.458  1.00 27.01 ? 85  THR A C   1 
ATOM   233  O  O   . THR A 1 38  ? 41.691  9.119   14.501  1.00 26.69 ? 85  THR A O   1 
ATOM   234  C  CB  . THR A 1 38  ? 41.986  8.379   17.601  1.00 26.15 ? 85  THR A CB  1 
ATOM   235  O  OG1 . THR A 1 38  ? 43.414  8.334   17.659  1.00 26.06 ? 85  THR A OG1 1 
ATOM   236  C  CG2 . THR A 1 38  ? 41.563  7.096   16.905  1.00 27.06 ? 85  THR A CG2 1 
ATOM   237  N  N   . GLU A 1 39  ? 43.455  10.224  15.358  1.00 27.36 ? 86  GLU A N   1 
ATOM   238  C  CA  . GLU A 1 39  ? 44.221  10.127  14.137  1.00 27.91 ? 86  GLU A CA  1 
ATOM   239  C  C   . GLU A 1 39  ? 45.343  9.104   14.291  1.00 27.27 ? 86  GLU A C   1 
ATOM   240  O  O   . GLU A 1 39  ? 46.109  8.906   13.344  1.00 33.50 ? 86  GLU A O   1 
ATOM   241  C  CB  . GLU A 1 39  ? 44.780  11.498  13.745  1.00 32.22 ? 86  GLU A CB  1 
ATOM   242  C  CG  . GLU A 1 39  ? 43.727  12.440  13.162  1.00 39.02 ? 86  GLU A CG  1 
ATOM   243  C  CD  . GLU A 1 39  ? 44.052  13.910  13.417  1.00 50.84 ? 86  GLU A CD  1 
ATOM   244  O  OE1 . GLU A 1 39  ? 43.167  14.776  13.215  1.00 59.89 ? 86  GLU A OE1 1 
ATOM   245  O  OE2 . GLU A 1 39  ? 45.193  14.194  13.847  1.00 53.43 ? 86  GLU A OE2 1 
ATOM   246  N  N   . ASP A 1 40  ? 45.365  8.393   15.437  1.00 23.40 ? 87  ASP A N   1 
ATOM   247  C  CA  . ASP A 1 40  ? 46.428  7.447   15.731  1.00 22.42 ? 87  ASP A CA  1 
ATOM   248  C  C   . ASP A 1 40  ? 46.000  6.048   15.278  1.00 23.05 ? 87  ASP A C   1 
ATOM   249  O  O   . ASP A 1 40  ? 45.155  5.422   15.911  1.00 22.69 ? 87  ASP A O   1 
ATOM   250  C  CB  . ASP A 1 40  ? 46.829  7.577   17.189  1.00 22.93 ? 87  ASP A CB  1 
ATOM   251  C  CG  . ASP A 1 40  ? 47.919  6.627   17.667  1.00 25.73 ? 87  ASP A CG  1 
ATOM   252  O  OD1 . ASP A 1 40  ? 48.300  5.733   16.915  1.00 27.89 ? 87  ASP A OD1 1 
ATOM   253  O  OD2 . ASP A 1 40  ? 48.437  6.849   18.778  1.00 31.20 ? 87  ASP A OD2 1 
ATOM   254  N  N   . ARG A 1 41  ? 46.603  5.582   14.193  1.00 22.82 ? 88  ARG A N   1 
ATOM   255  C  CA  . ARG A 1 41  ? 46.352  4.258   13.643  1.00 26.21 ? 88  ARG A CA  1 
ATOM   256  C  C   . ARG A 1 41  ? 46.530  3.154   14.684  1.00 25.58 ? 88  ARG A C   1 
ATOM   257  O  O   . ARG A 1 41  ? 45.705  2.243   14.811  1.00 23.93 ? 88  ARG A O   1 
ATOM   258  C  CB  . ARG A 1 41  ? 47.260  4.003   12.446  1.00 27.92 ? 88  ARG A CB  1 
ATOM   259  C  CG  . ARG A 1 41  ? 47.004  2.648   11.818  1.00 32.26 ? 88  ARG A CG  1 
ATOM   260  C  CD  . ARG A 1 41  ? 47.819  2.527   10.567  1.00 37.26 ? 88  ARG A CD  1 
ATOM   261  N  NE  . ARG A 1 41  ? 47.787  1.139   10.111  1.00 37.63 ? 88  ARG A NE  1 
ATOM   262  C  CZ  . ARG A 1 41  ? 47.464  0.748   8.900   1.00 40.68 ? 88  ARG A CZ  1 
ATOM   263  N  NH1 . ARG A 1 41  ? 47.589  -0.521  8.585   1.00 38.26 ? 88  ARG A NH1 1 
ATOM   264  N  NH2 . ARG A 1 41  ? 47.062  1.628   8.004   1.00 43.79 ? 88  ARG A NH2 1 
ATOM   265  N  N   . ALA A 1 42  ? 47.644  3.181   15.423  1.00 24.19 ? 89  ALA A N   1 
ATOM   266  C  CA  . ALA A 1 42  ? 47.883  2.178   16.450  1.00 24.08 ? 89  ALA A CA  1 
ATOM   267  C  C   . ALA A 1 42  ? 46.760  2.163   17.485  1.00 24.08 ? 89  ALA A C   1 
ATOM   268  O  O   . ALA A 1 42  ? 46.380  1.121   17.996  1.00 21.21 ? 89  ALA A O   1 
ATOM   269  C  CB  . ALA A 1 42  ? 49.202  2.453   17.155  1.00 25.52 ? 89  ALA A CB  1 
ATOM   270  N  N   . ALA A 1 43  ? 46.285  3.344   17.849  1.00 22.43 ? 90  ALA A N   1 
ATOM   271  C  CA  . ALA A 1 43  ? 45.268  3.487   18.883  1.00 23.08 ? 90  ALA A CA  1 
ATOM   272  C  C   . ALA A 1 43  ? 43.944  2.901   18.381  1.00 25.32 ? 90  ALA A C   1 
ATOM   273  O  O   . ALA A 1 43  ? 43.194  2.300   19.139  1.00 23.38 ? 90  ALA A O   1 
ATOM   274  C  CB  . ALA A 1 43  ? 45.115  4.934   19.279  1.00 26.87 ? 90  ALA A CB  1 
ATOM   275  N  N   . PHE A 1 44  ? 43.680  3.078   17.095  1.00 23.73 ? 91  PHE A N   1 
ATOM   276  C  CA  . PHE A 1 44  ? 42.480  2.529   16.484  1.00 20.06 ? 91  PHE A CA  1 
ATOM   277  C  C   . PHE A 1 44  ? 42.572  1.011   16.397  1.00 20.66 ? 91  PHE A C   1 
ATOM   278  O  O   . PHE A 1 44  ? 41.590  0.321   16.685  1.00 20.65 ? 91  PHE A O   1 
ATOM   279  C  CB  . PHE A 1 44  ? 42.233  3.198   15.135  1.00 20.58 ? 91  PHE A CB  1 
ATOM   280  C  CG  . PHE A 1 44  ? 40.873  2.800   14.572  1.00 20.59 ? 91  PHE A CG  1 
ATOM   281  C  CD1 . PHE A 1 44  ? 39.722  3.309   15.141  1.00 24.74 ? 91  PHE A CD1 1 
ATOM   282  C  CD2 . PHE A 1 44  ? 40.768  1.965   13.483  1.00 21.69 ? 91  PHE A CD2 1 
ATOM   283  C  CE1 . PHE A 1 44  ? 38.476  2.944   14.652  1.00 24.74 ? 91  PHE A CE1 1 
ATOM   284  C  CE2 . PHE A 1 44  ? 39.520  1.600   13.002  1.00 23.65 ? 91  PHE A CE2 1 
ATOM   285  C  CZ  . PHE A 1 44  ? 38.390  2.093   13.587  1.00 23.74 ? 91  PHE A CZ  1 
ATOM   286  N  N   . VAL A 1 45  ? 43.733  0.467   16.022  1.00 20.16 ? 92  VAL A N   1 
ATOM   287  C  CA  . VAL A 1 45  ? 43.927  -0.964  15.990  1.00 20.04 ? 92  VAL A CA  1 
ATOM   288  C  C   . VAL A 1 45  ? 43.719  -1.531  17.392  1.00 22.28 ? 92  VAL A C   1 
ATOM   289  O  O   . VAL A 1 45  ? 43.065  -2.555  17.559  1.00 21.05 ? 92  VAL A O   1 
ATOM   290  C  CB  . VAL A 1 45  ? 45.302  -1.332  15.409  1.00 22.52 ? 92  VAL A CB  1 
ATOM   291  C  CG1 . VAL A 1 45  ? 45.660  -2.790  15.684  1.00 22.55 ? 92  VAL A CG1 1 
ATOM   292  C  CG2 . VAL A 1 45  ? 45.307  -1.034  13.917  1.00 24.78 ? 92  VAL A CG2 1 
ATOM   293  N  N   . ALA A 1 46  ? 44.245  -0.840  18.416  1.00 21.67 ? 93  ALA A N   1 
ATOM   294  C  CA  . ALA A 1 46  ? 44.102  -1.318  19.772  1.00 21.40 ? 93  ALA A CA  1 
ATOM   295  C  C   . ALA A 1 46  ? 42.621  -1.390  20.138  1.00 19.93 ? 93  ALA A C   1 
ATOM   296  O  O   . ALA A 1 46  ? 42.211  -2.354  20.762  1.00 20.50 ? 93  ALA A O   1 
ATOM   297  C  CB  . ALA A 1 46  ? 44.877  -0.444  20.728  1.00 23.67 ? 93  ALA A CB  1 
ATOM   298  N  N   . LEU A 1 47  ? 41.832  -0.411  19.706  1.00 19.45 ? 94  LEU A N   1 
ATOM   299  C  CA  . LEU A 1 47  ? 40.402  -0.390  19.955  1.00 18.65 ? 94  LEU A CA  1 
ATOM   300  C  C   . LEU A 1 47  ? 39.721  -1.570  19.270  1.00 17.69 ? 94  LEU A C   1 
ATOM   301  O  O   . LEU A 1 47  ? 38.872  -2.229  19.883  1.00 18.94 ? 94  LEU A O   1 
ATOM   302  C  CB  . LEU A 1 47  ? 39.785  0.923   19.482  1.00 21.74 ? 94  LEU A CB  1 
ATOM   303  C  CG  . LEU A 1 47  ? 38.250  0.958   19.543  1.00 22.90 ? 94  LEU A CG  1 
ATOM   304  C  CD1 . LEU A 1 47  ? 37.804  0.895   20.984  1.00 25.08 ? 94  LEU A CD1 1 
ATOM   305  C  CD2 . LEU A 1 47  ? 37.653  2.150   18.850  1.00 26.89 ? 94  LEU A CD2 1 
ATOM   306  N  N   . LEU A 1 48  ? 40.067  -1.822  18.019  1.00 17.91 ? 95  LEU A N   1 
ATOM   307  C  CA  . LEU A 1 48  ? 39.436  -2.931  17.310  1.00 16.91 ? 95  LEU A CA  1 
ATOM   308  C  C   . LEU A 1 48  ? 39.688  -4.223  18.074  1.00 17.17 ? 95  LEU A C   1 
ATOM   309  O  O   . LEU A 1 48  ? 38.819  -5.076  18.181  1.00 16.45 ? 95  LEU A O   1 
ATOM   310  C  CB  . LEU A 1 48  ? 39.940  -3.000  15.866  1.00 17.61 ? 95  LEU A CB  1 
ATOM   311  C  CG  . LEU A 1 48  ? 39.452  -1.892  14.930  1.00 18.84 ? 95  LEU A CG  1 
ATOM   312  C  CD1 . LEU A 1 48  ? 40.189  -2.078  13.620  1.00 20.40 ? 95  LEU A CD1 1 
ATOM   313  C  CD2 . LEU A 1 48  ? 37.930  -1.866  14.781  1.00 21.68 ? 95  LEU A CD2 1 
ATOM   314  N  N   . LYS A 1 49  ? 40.899  -4.398  18.613  1.00 17.01 ? 96  LYS A N   1 
ATOM   315  C  CA  . LYS A 1 49  ? 41.195  -5.620  19.344  1.00 16.83 ? 96  LYS A CA  1 
ATOM   316  C  C   . LYS A 1 49  ? 40.407  -5.687  20.654  1.00 18.04 ? 96  LYS A C   1 
ATOM   317  O  O   . LYS A 1 49  ? 39.912  -6.749  21.014  1.00 18.33 ? 96  LYS A O   1 
ATOM   318  C  CB  . LYS A 1 49  ? 42.702  -5.720  19.575  1.00 18.75 ? 96  LYS A CB  1 
ATOM   319  C  CG  . LYS A 1 49  ? 43.483  -5.943  18.318  1.00 19.18 ? 96  LYS A CG  1 
ATOM   320  C  CD  . LYS A 1 49  ? 44.996  -5.954  18.521  1.00 23.20 ? 96  LYS A CD  1 
ATOM   321  C  CE  . LYS A 1 49  ? 45.669  -6.406  17.273  1.00 26.72 ? 96  LYS A CE  1 
ATOM   322  N  NZ  . LYS A 1 49  ? 47.121  -6.460  17.465  1.00 31.85 ? 96  LYS A NZ  1 
ATOM   323  N  N   . GLU A 1 50  ? 40.309  -4.578  21.366  1.00 17.07 ? 97  GLU A N   1 
ATOM   324  C  CA  . GLU A 1 50  ? 39.564  -4.541  22.612  1.00 17.27 ? 97  GLU A CA  1 
ATOM   325  C  C   . GLU A 1 50  ? 38.069  -4.783  22.349  1.00 17.25 ? 97  GLU A C   1 
ATOM   326  O  O   . GLU A 1 50  ? 37.380  -5.462  23.114  1.00 16.45 ? 97  GLU A O   1 
ATOM   327  C  CB  . GLU A 1 50  ? 39.813  -3.230  23.353  1.00 21.86 ? 97  GLU A CB  1 
ATOM   328  C  CG  . GLU A 1 50  ? 39.380  -3.304  24.810  1.00 30.68 ? 97  GLU A CG  1 
ATOM   329  C  CD  . GLU A 1 50  ? 39.842  -2.074  25.579  1.00 37.09 ? 97  GLU A CD  1 
ATOM   330  O  OE1 . GLU A 1 50  ? 40.654  -1.289  25.015  1.00 41.88 ? 97  GLU A OE1 1 
ATOM   331  O  OE2 . GLU A 1 50  ? 39.355  -1.902  26.716  1.00 42.62 ? 97  GLU A OE2 1 
ATOM   332  N  N   . TRP A 1 51  ? 37.542  -4.176  21.282  1.00 17.16 ? 98  TRP A N   1 
ATOM   333  C  CA  . TRP A 1 51  ? 36.164  -4.441  20.901  1.00 15.91 ? 98  TRP A CA  1 
ATOM   334  C  C   . TRP A 1 51  ? 35.920  -5.900  20.552  1.00 15.33 ? 98  TRP A C   1 
ATOM   335  O  O   . TRP A 1 51  ? 34.876  -6.461  20.901  1.00 15.31 ? 98  TRP A O   1 
ATOM   336  C  CB  . TRP A 1 51  ? 35.779  -3.550  19.712  1.00 14.97 ? 98  TRP A CB  1 
ATOM   337  C  CG  . TRP A 1 51  ? 35.218  -2.220  20.091  1.00 15.59 ? 98  TRP A CG  1 
ATOM   338  C  CD1 . TRP A 1 51  ? 35.166  -1.635  21.316  1.00 15.56 ? 98  TRP A CD1 1 
ATOM   339  C  CD2 . TRP A 1 51  ? 34.528  -1.317  19.200  1.00 16.48 ? 98  TRP A CD2 1 
ATOM   340  N  NE1 . TRP A 1 51  ? 34.502  -0.438  21.251  1.00 17.51 ? 98  TRP A NE1 1 
ATOM   341  C  CE2 . TRP A 1 51  ? 34.120  -0.207  19.959  1.00 17.14 ? 98  TRP A CE2 1 
ATOM   342  C  CE3 . TRP A 1 51  ? 34.245  -1.354  17.838  1.00 19.27 ? 98  TRP A CE3 1 
ATOM   343  C  CZ2 . TRP A 1 51  ? 33.424  0.861   19.409  1.00 19.00 ? 98  TRP A CZ2 1 
ATOM   344  C  CZ3 . TRP A 1 51  ? 33.530  -0.310  17.296  1.00 21.55 ? 98  TRP A CZ3 1 
ATOM   345  C  CH2 . TRP A 1 51  ? 33.105  0.768   18.080  1.00 19.50 ? 98  TRP A CH2 1 
ATOM   346  N  N   . THR A 1 52  ? 36.866  -6.534  19.843  1.00 15.51 ? 99  THR A N   1 
ATOM   347  C  CA  . THR A 1 52  ? 36.708  -7.948  19.492  1.00 15.04 ? 99  THR A CA  1 
ATOM   348  C  C   . THR A 1 52  ? 36.655  -8.812  20.751  1.00 14.35 ? 99  THR A C   1 
ATOM   349  O  O   . THR A 1 52  ? 35.805  -9.697  20.883  1.00 14.14 ? 99  THR A O   1 
ATOM   350  C  CB  . THR A 1 52  ? 37.824  -8.442  18.581  1.00 16.19 ? 99  THR A CB  1 
ATOM   351  O  OG1 . THR A 1 52  ? 37.866  -7.575  17.452  1.00 16.01 ? 99  THR A OG1 1 
ATOM   352  C  CG2 . THR A 1 52  ? 37.526  -9.845  18.095  1.00 17.10 ? 99  THR A CG2 1 
ATOM   353  N  N   . ALA A 1 53  ? 37.533  -8.520  21.704  1.00 15.25 ? 100 ALA A N   1 
ATOM   354  C  CA  . ALA A 1 53  ? 37.558  -9.268  22.946  1.00 14.72 ? 100 ALA A CA  1 
ATOM   355  C  C   . ALA A 1 53  ? 36.238  -9.114  23.683  1.00 14.39 ? 100 ALA A C   1 
ATOM   356  O  O   . ALA A 1 53  ? 35.670  -10.068 24.206  1.00 15.05 ? 100 ALA A O   1 
ATOM   357  C  CB  . ALA A 1 53  ? 38.711  -8.820  23.804  1.00 14.25 ? 100 ALA A CB  1 
ATOM   358  N  N   . ALA A 1 54  ? 35.742  -7.869  23.700  1.00 14.59 ? 101 ALA A N   1 
ATOM   359  C  CA  . ALA A 1 54  ? 34.459  -7.625  24.333  1.00 15.17 ? 101 ALA A CA  1 
ATOM   360  C  C   . ALA A 1 54  ? 33.332  -8.372  23.629  1.00 14.40 ? 101 ALA A C   1 
ATOM   361  O  O   . ALA A 1 54  ? 32.461  -8.966  24.258  1.00 14.75 ? 101 ALA A O   1 
ATOM   362  C  CB  . ALA A 1 54  ? 34.171  -6.145  24.405  1.00 15.48 ? 101 ALA A CB  1 
ATOM   363  N  N   . ALA A 1 55  ? 33.353  -8.350  22.298  1.00 14.74 ? 102 ALA A N   1 
ATOM   364  C  CA  . ALA A 1 55  ? 32.326  -9.021  21.535  1.00 13.73 ? 102 ALA A CA  1 
ATOM   365  C  C   . ALA A 1 55  ? 32.297  -10.521 21.821  1.00 15.25 ? 102 ALA A C   1 
ATOM   366  O  O   . ALA A 1 55  ? 31.234  -11.128 21.866  1.00 14.82 ? 102 ALA A O   1 
ATOM   367  C  CB  . ALA A 1 55  ? 32.515  -8.756  20.054  1.00 14.60 ? 102 ALA A CB  1 
ATOM   368  N  N   . ARG A 1 56  ? 33.476  -11.148 21.946  1.00 14.10 ? 103 ARG A N   1 
ATOM   369  C  CA  . ARG A 1 56  ? 33.512  -12.560 22.312  1.00 15.30 ? 103 ARG A CA  1 
ATOM   370  C  C   . ARG A 1 56  ? 32.801  -12.834 23.637  1.00 16.69 ? 103 ARG A C   1 
ATOM   371  O  O   . ARG A 1 56  ? 32.073  -13.804 23.790  1.00 18.25 ? 103 ARG A O   1 
ATOM   372  C  CB  . ARG A 1 56  ? 34.944  -13.100 22.460  1.00 17.68 ? 103 ARG A CB  1 
ATOM   373  C  CG  . ARG A 1 56  ? 35.596  -13.318 21.116  1.00 18.22 ? 103 ARG A CG  1 
ATOM   374  C  CD  . ARG A 1 56  ? 36.954  -13.924 21.407  1.00 17.27 ? 103 ARG A CD  1 
ATOM   375  N  NE  . ARG A 1 56  ? 37.612  -13.929 20.116  1.00 16.69 ? 103 ARG A NE  1 
ATOM   376  C  CZ  . ARG A 1 56  ? 38.548  -13.130 19.710  1.00 16.34 ? 103 ARG A CZ  1 
ATOM   377  N  NH1 . ARG A 1 56  ? 39.004  -12.182 20.466  1.00 17.07 ? 103 ARG A NH1 1 
ATOM   378  N  NH2 . ARG A 1 56  ? 38.979  -13.267 18.476  1.00 17.29 ? 103 ARG A NH2 1 
ATOM   379  N  N   . ARG A 1 57  ? 32.978  -11.961 24.617  1.00 14.58 ? 104 ARG A N   1 
ATOM   380  C  CA  A ARG A 1 57  ? 32.305  -12.122 25.887  0.50 14.63 ? 104 ARG A CA  1 
ATOM   381  C  CA  B ARG A 1 57  ? 32.306  -12.125 25.890  0.50 15.33 ? 104 ARG A CA  1 
ATOM   382  C  C   . ARG A 1 57  ? 30.814  -11.881 25.714  1.00 14.08 ? 104 ARG A C   1 
ATOM   383  O  O   . ARG A 1 57  ? 29.992  -12.669 26.129  1.00 14.09 ? 104 ARG A O   1 
ATOM   384  C  CB  A ARG A 1 57  ? 32.842  -11.134 26.924  0.50 14.04 ? 104 ARG A CB  1 
ATOM   385  C  CB  B ARG A 1 57  ? 32.842  -11.161 26.953  0.50 15.74 ? 104 ARG A CB  1 
ATOM   386  C  CG  A ARG A 1 57  ? 34.326  -11.278 27.243  0.50 15.30 ? 104 ARG A CG  1 
ATOM   387  C  CG  B ARG A 1 57  ? 34.276  -11.359 27.439  0.50 18.13 ? 104 ARG A CG  1 
ATOM   388  C  CD  A ARG A 1 57  ? 34.631  -12.564 27.944  0.50 14.81 ? 104 ARG A CD  1 
ATOM   389  C  CD  B ARG A 1 57  ? 34.432  -12.286 28.625  0.50 19.71 ? 104 ARG A CD  1 
ATOM   390  N  NE  A ARG A 1 57  ? 34.174  -12.506 29.336  0.50 15.44 ? 104 ARG A NE  1 
ATOM   391  N  NE  B ARG A 1 57  ? 34.538  -13.687 28.212  0.50 22.28 ? 104 ARG A NE  1 
ATOM   392  C  CZ  A ARG A 1 57  ? 34.298  -13.480 30.219  0.50 16.50 ? 104 ARG A CZ  1 
ATOM   393  C  CZ  B ARG A 1 57  ? 34.669  -14.667 29.084  0.50 22.07 ? 104 ARG A CZ  1 
ATOM   394  N  NH1 A ARG A 1 57  ? 34.613  -14.700 29.814  0.50 18.36 ? 104 ARG A NH1 1 
ATOM   395  N  NH1 B ARG A 1 57  ? 34.443  -14.412 30.376  0.50 21.79 ? 104 ARG A NH1 1 
ATOM   396  N  NH2 A ARG A 1 57  ? 34.013  -13.218 31.471  0.50 20.56 ? 104 ARG A NH2 1 
ATOM   397  N  NH2 B ARG A 1 57  ? 34.944  -15.882 28.635  0.50 25.55 ? 104 ARG A NH2 1 
ATOM   398  N  N   . LEU A 1 58  ? 30.457  -10.765 25.062  1.00 13.76 ? 105 LEU A N   1 
ATOM   399  C  CA  . LEU A 1 58  ? 29.055  -10.372 24.995  1.00 13.79 ? 105 LEU A CA  1 
ATOM   400  C  C   . LEU A 1 58  ? 28.217  -11.416 24.285  1.00 12.65 ? 105 LEU A C   1 
ATOM   401  O  O   . LEU A 1 58  ? 27.101  -11.708 24.708  1.00 14.19 ? 105 LEU A O   1 
ATOM   402  C  CB  . LEU A 1 58  ? 28.952  -9.045  24.253  1.00 14.89 ? 105 LEU A CB  1 
ATOM   403  C  CG  . LEU A 1 58  ? 29.529  -7.828  24.978  1.00 15.47 ? 105 LEU A CG  1 
ATOM   404  C  CD1 . LEU A 1 58  ? 29.722  -6.666  23.979  1.00 17.02 ? 105 LEU A CD1 1 
ATOM   405  C  CD2 . LEU A 1 58  ? 28.651  -7.381  26.114  1.00 17.95 ? 105 LEU A CD2 1 
ATOM   406  N  N   . THR A 1 59  ? 28.738  -11.973 23.185  1.00 12.56 ? 106 THR A N   1 
ATOM   407  C  CA  . THR A 1 59  ? 27.932  -12.880 22.399  1.00 13.66 ? 106 THR A CA  1 
ATOM   408  C  C   . THR A 1 59  ? 27.817  -14.236 23.078  1.00 14.33 ? 106 THR A C   1 
ATOM   409  O  O   . THR A 1 59  ? 26.912  -14.981 22.739  1.00 15.52 ? 106 THR A O   1 
ATOM   410  C  CB  . THR A 1 59  ? 28.498  -13.057 20.981  1.00 13.30 ? 106 THR A CB  1 
ATOM   411  O  OG1 . THR A 1 59  ? 29.849  -13.521 21.066  1.00 15.14 ? 106 THR A OG1 1 
ATOM   412  C  CG2 . THR A 1 59  ? 28.385  -11.779 20.192  1.00 13.75 ? 106 THR A CG2 1 
ATOM   413  N  N   . ALA A 1 60  ? 28.615  -14.493 24.130  1.00 15.22 ? 107 ALA A N   1 
ATOM   414  C  CA  . ALA A 1 60  ? 28.482  -15.710 24.901  1.00 16.70 ? 107 ALA A CA  1 
ATOM   415  C  C   . ALA A 1 60  ? 27.725  -15.488 26.208  1.00 18.38 ? 107 ALA A C   1 
ATOM   416  O  O   . ALA A 1 60  ? 27.571  -16.444 26.992  1.00 20.33 ? 107 ALA A O   1 
ATOM   417  C  CB  . ALA A 1 60  ? 29.866  -16.271 25.163  1.00 17.44 ? 107 ALA A CB  1 
ATOM   418  N  N   . GLY A 1 61  ? 27.205  -14.267 26.420  1.00 15.46 ? 108 GLY A N   1 
ATOM   419  C  CA  . GLY A 1 61  ? 26.445  -13.940 27.604  1.00 15.88 ? 108 GLY A CA  1 
ATOM   420  C  C   . GLY A 1 61  ? 27.315  -13.667 28.821  1.00 17.17 ? 108 GLY A C   1 
ATOM   421  O  O   . GLY A 1 61  ? 26.797  -13.660 29.933  1.00 21.88 ? 108 GLY A O   1 
ATOM   422  N  N   . HIS A 1 62  ? 28.596  -13.389 28.625  1.00 15.88 ? 109 HIS A N   1 
ATOM   423  C  CA  . HIS A 1 62  ? 29.489  -13.036 29.712  1.00 15.34 ? 109 HIS A CA  1 
ATOM   424  C  C   . HIS A 1 62  ? 29.717  -11.530 29.762  1.00 17.20 ? 109 HIS A C   1 
ATOM   425  O  O   . HIS A 1 62  ? 29.590  -10.815 28.772  1.00 17.37 ? 109 HIS A O   1 
ATOM   426  C  CB  . HIS A 1 62  ? 30.858  -13.703 29.546  1.00 16.25 ? 109 HIS A CB  1 
ATOM   427  C  CG  . HIS A 1 62  ? 30.750  -15.173 29.422  1.00 21.00 ? 109 HIS A CG  1 
ATOM   428  N  ND1 . HIS A 1 62  ? 29.935  -15.934 30.226  1.00 25.56 ? 109 HIS A ND1 1 
ATOM   429  C  CD2 . HIS A 1 62  ? 31.268  -15.983 28.503  1.00 20.39 ? 109 HIS A CD2 1 
ATOM   430  C  CE1 . HIS A 1 62  ? 30.026  -17.208 29.811  1.00 27.38 ? 109 HIS A CE1 1 
ATOM   431  N  NE2 . HIS A 1 62  ? 30.834  -17.243 28.771  1.00 23.46 ? 109 HIS A NE2 1 
ATOM   432  N  N   . ALA A 1 63  ? 30.026  -11.034 30.951  1.00 17.61 ? 110 ALA A N   1 
ATOM   433  C  CA  . ALA A 1 63  ? 30.325  -9.625  31.123  1.00 17.25 ? 110 ALA A CA  1 
ATOM   434  C  C   . ALA A 1 63  ? 31.657  -9.296  30.496  1.00 17.13 ? 110 ALA A C   1 
ATOM   435  O  O   . ALA A 1 63  ? 32.546  -10.142 30.432  1.00 17.64 ? 110 ALA A O   1 
ATOM   436  C  CB  . ALA A 1 63  ? 30.357  -9.299  32.616  1.00 20.81 ? 110 ALA A CB  1 
ATOM   437  N  N   . VAL A 1 64  ? 31.835  -8.037  30.119  1.00 15.93 ? 111 VAL A N   1 
ATOM   438  C  CA  . VAL A 1 64  ? 33.090  -7.586  29.554  1.00 17.36 ? 111 VAL A CA  1 
ATOM   439  C  C   . VAL A 1 64  ? 34.126  -7.386  30.657  1.00 19.26 ? 111 VAL A C   1 
ATOM   440  O  O   . VAL A 1 64  ? 33.814  -7.172  31.837  1.00 18.80 ? 111 VAL A O   1 
ATOM   441  C  CB  . VAL A 1 64  ? 32.954  -6.316  28.701  1.00 21.80 ? 111 VAL A CB  1 
ATOM   442  C  CG1 . VAL A 1 64  ? 31.964  -6.525  27.576  1.00 23.94 ? 111 VAL A CG1 1 
ATOM   443  C  CG2 . VAL A 1 64  ? 32.558  -5.112  29.491  1.00 24.65 ? 111 VAL A CG2 1 
ATOM   444  N  N   . GLY A 1 65  ? 35.383  -7.502  30.227  1.00 21.28 ? 112 GLY A N   1 
ATOM   445  C  CA  . GLY A 1 65  ? 36.549  -7.280  31.049  1.00 20.47 ? 112 GLY A CA  1 
ATOM   446  C  C   . GLY A 1 65  ? 36.507  -8.129  32.314  1.00 20.64 ? 112 GLY A C   1 
ATOM   447  O  O   . GLY A 1 65  ? 36.219  -9.339  32.273  1.00 20.95 ? 112 GLY A O   1 
ATOM   448  N  N   . GLU A 1 66  ? 36.728  -7.460  33.446  1.00 22.28 ? 113 GLU A N   1 
ATOM   449  C  CA  . GLU A 1 66  ? 36.744  -8.180  34.706  1.00 25.81 ? 113 GLU A CA  1 
ATOM   450  C  C   . GLU A 1 66  ? 35.373  -8.258  35.375  1.00 25.52 ? 113 GLU A C   1 
ATOM   451  O  O   . GLU A 1 66  ? 35.274  -8.719  36.504  1.00 31.04 ? 113 GLU A O   1 
ATOM   452  C  CB  . GLU A 1 66  ? 37.854  -7.626  35.597  1.00 29.96 ? 113 GLU A CB  1 
ATOM   453  C  CG  . GLU A 1 66  ? 39.198  -8.230  35.196  1.00 39.67 ? 113 GLU A CG  1 
ATOM   454  C  CD  . GLU A 1 66  ? 40.446  -7.699  35.867  1.00 49.72 ? 113 GLU A CD  1 
ATOM   455  O  OE1 . GLU A 1 66  ? 40.371  -6.727  36.654  1.00 56.19 ? 113 GLU A OE1 1 
ATOM   456  O  OE2 . GLU A 1 66  ? 41.507  -8.290  35.570  1.00 62.32 ? 113 GLU A OE2 1 
ATOM   457  N  N   . GLY A 1 67  ? 34.301  -7.850  34.681  1.00 21.26 ? 114 GLY A N   1 
ATOM   458  C  CA  . GLY A 1 67  ? 32.956  -8.146  35.114  1.00 20.02 ? 114 GLY A CA  1 
ATOM   459  C  C   . GLY A 1 67  ? 32.208  -6.884  35.543  1.00 18.02 ? 114 GLY A C   1 
ATOM   460  O  O   . GLY A 1 67  ? 32.729  -5.776  35.455  1.00 18.45 ? 114 GLY A O   1 
ATOM   461  N  N   . ALA A 1 68  ? 31.035  -7.120  36.119  1.00 20.92 ? 115 ALA A N   1 
ATOM   462  C  CA  . ALA A 1 68  ? 30.082  -6.082  36.471  1.00 19.32 ? 115 ALA A CA  1 
ATOM   463  C  C   . ALA A 1 68  ? 30.108  -5.738  37.957  1.00 20.89 ? 115 ALA A C   1 
ATOM   464  O  O   . ALA A 1 68  ? 29.493  -4.764  38.375  1.00 21.92 ? 115 ALA A O   1 
ATOM   465  C  CB  . ALA A 1 68  ? 28.722  -6.525  36.015  1.00 21.13 ? 115 ALA A CB  1 
ATOM   466  N  N   . TYR A 1 69  ? 30.796  -6.550  38.767  1.00 21.47 ? 116 TYR A N   1 
ATOM   467  C  CA  . TYR A 1 69  ? 30.861  -6.319  40.199  1.00 23.48 ? 116 TYR A CA  1 
ATOM   468  C  C   . TYR A 1 69  ? 32.001  -7.180  40.735  1.00 26.07 ? 116 TYR A C   1 
ATOM   469  O  O   . TYR A 1 69  ? 32.651  -7.858  39.964  1.00 25.63 ? 116 TYR A O   1 
ATOM   470  C  CB  . TYR A 1 69  ? 29.510  -6.588  40.846  1.00 24.34 ? 116 TYR A CB  1 
ATOM   471  C  CG  . TYR A 1 69  ? 29.044  -8.026  40.802  1.00 26.75 ? 116 TYR A CG  1 
ATOM   472  C  CD1 . TYR A 1 69  ? 28.355  -8.533  39.708  1.00 28.30 ? 116 TYR A CD1 1 
ATOM   473  C  CD2 . TYR A 1 69  ? 29.274  -8.867  41.886  1.00 29.35 ? 116 TYR A CD2 1 
ATOM   474  C  CE1 . TYR A 1 69  ? 27.919  -9.848  39.690  1.00 32.62 ? 116 TYR A CE1 1 
ATOM   475  C  CE2 . TYR A 1 69  ? 28.842  -10.179 41.877  1.00 32.74 ? 116 TYR A CE2 1 
ATOM   476  C  CZ  . TYR A 1 69  ? 28.162  -10.668 40.779  1.00 33.97 ? 116 TYR A CZ  1 
ATOM   477  O  OH  . TYR A 1 69  ? 27.746  -11.969 40.774  1.00 39.82 ? 116 TYR A OH  1 
ATOM   478  N  N   . GLY A 1 70  ? 32.307  -7.042  42.030  1.00 32.50 ? 117 GLY A N   1 
ATOM   479  C  CA  . GLY A 1 70  ? 33.362  -7.831  42.656  1.00 35.00 ? 117 GLY A CA  1 
ATOM   480  C  C   . GLY A 1 70  ? 34.769  -7.303  42.370  1.00 35.97 ? 117 GLY A C   1 
ATOM   481  O  O   . GLY A 1 70  ? 35.761  -7.934  42.741  1.00 39.82 ? 117 GLY A O   1 
ATOM   482  N  N   . GLY A 1 71  ? 34.887  -6.148  41.705  1.00 31.56 ? 118 GLY A N   1 
ATOM   483  C  CA  . GLY A 1 71  ? 36.181  -5.521  41.502  1.00 32.78 ? 118 GLY A CA  1 
ATOM   484  C  C   . GLY A 1 71  ? 36.541  -4.589  42.656  1.00 29.87 ? 118 GLY A C   1 
ATOM   485  O  O   . GLY A 1 71  ? 35.838  -4.550  43.671  1.00 31.83 ? 118 GLY A O   1 
ATOM   486  N  N   . LEU A 1 72  ? 37.597  -3.806  42.435  1.00 30.53 ? 119 LEU A N   1 
ATOM   487  C  CA  . LEU A 1 72  ? 37.986  -2.761  43.364  1.00 34.05 ? 119 LEU A CA  1 
ATOM   488  C  C   . LEU A 1 72  ? 36.791  -1.830  43.572  1.00 32.25 ? 119 LEU A C   1 
ATOM   489  O  O   . LEU A 1 72  ? 36.283  -1.285  42.594  1.00 29.91 ? 119 LEU A O   1 
ATOM   490  C  CB  . LEU A 1 72  ? 39.177  -1.995  42.798  1.00 41.02 ? 119 LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 72  ? 40.457  -2.805  42.561  1.00 46.93 ? 119 LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 72  ? 41.423  -2.032  41.677  1.00 47.02 ? 119 LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 72  ? 41.115  -3.178  43.875  1.00 49.85 ? 119 LEU A CD2 1 
ATOM   494  N  N   . PRO A 1 73  ? 36.297  -1.622  44.816  1.00 29.98 ? 120 PRO A N   1 
ATOM   495  C  CA  . PRO A 1 73  ? 35.234  -0.643  45.082  1.00 28.38 ? 120 PRO A CA  1 
ATOM   496  C  C   . PRO A 1 73  ? 35.430  0.761   44.519  1.00 27.11 ? 120 PRO A C   1 
ATOM   497  O  O   . PRO A 1 73  ? 34.455  1.416   44.156  1.00 24.03 ? 120 PRO A O   1 
ATOM   498  C  CB  . PRO A 1 73  ? 35.096  -0.593  46.630  1.00 29.90 ? 120 PRO A CB  1 
ATOM   499  C  CG  . PRO A 1 73  ? 36.213  -1.481  47.171  1.00 32.29 ? 120 PRO A CG  1 
ATOM   500  C  CD  . PRO A 1 73  ? 36.677  -2.371  46.032  1.00 31.75 ? 120 PRO A CD  1 
ATOM   501  N  N   . GLU A 1 74  ? 36.682  1.241   44.409  1.00 25.85 ? 121 GLU A N   1 
ATOM   502  C  CA  . GLU A 1 74  ? 36.927  2.619   44.043  1.00 24.37 ? 121 GLU A CA  1 
ATOM   503  C  C   . GLU A 1 74  ? 37.017  2.798   42.526  1.00 21.90 ? 121 GLU A C   1 
ATOM   504  O  O   . GLU A 1 74  ? 37.242  3.910   42.070  1.00 25.83 ? 121 GLU A O   1 
ATOM   505  C  CB  . GLU A 1 74  ? 38.158  3.177   44.776  1.00 29.04 ? 121 GLU A CB  1 
ATOM   506  C  CG  . GLU A 1 74  ? 39.448  2.422   44.475  1.00 35.29 ? 121 GLU A CG  1 
ATOM   507  C  CD  . GLU A 1 74  ? 39.832  1.323   45.454  1.00 43.17 ? 121 GLU A CD  1 
ATOM   508  O  OE1 . GLU A 1 74  ? 38.951  0.542   45.898  1.00 45.28 ? 121 GLU A OE1 1 
ATOM   509  O  OE2 . GLU A 1 74  ? 41.053  1.239   45.755  1.00 50.01 ? 121 GLU A OE2 1 
ATOM   510  N  N   . ALA A 1 75  ? 36.853  1.717   41.746  1.00 22.90 ? 122 ALA A N   1 
ATOM   511  C  CA  . ALA A 1 75  ? 36.908  1.802   40.293  1.00 23.63 ? 122 ALA A CA  1 
ATOM   512  C  C   . ALA A 1 75  ? 35.524  1.556   39.699  1.00 20.21 ? 122 ALA A C   1 
ATOM   513  O  O   . ALA A 1 75  ? 34.674  0.862   40.270  1.00 20.89 ? 122 ALA A O   1 
ATOM   514  C  CB  . ALA A 1 75  ? 37.876  0.800   39.723  1.00 26.82 ? 122 ALA A CB  1 
ATOM   515  N  N   . PRO A 1 76  ? 35.253  2.189   38.543  1.00 21.14 ? 123 PRO A N   1 
ATOM   516  C  CA  . PRO A 1 76  ? 34.012  1.904   37.838  1.00 20.57 ? 123 PRO A CA  1 
ATOM   517  C  C   . PRO A 1 76  ? 34.080  0.455   37.390  1.00 21.52 ? 123 PRO A C   1 
ATOM   518  O  O   . PRO A 1 76  ? 35.152  -0.005  36.989  1.00 20.31 ? 123 PRO A O   1 
ATOM   519  C  CB  . PRO A 1 76  ? 34.026  2.851   36.649  1.00 22.32 ? 123 PRO A CB  1 
ATOM   520  C  CG  . PRO A 1 76  ? 35.229  3.767   36.819  1.00 26.22 ? 123 PRO A CG  1 
ATOM   521  C  CD  . PRO A 1 76  ? 36.120  3.145   37.842  1.00 22.65 ? 123 PRO A CD  1 
ATOM   522  N  N   . PRO A 1 77  ? 32.957  -0.286  37.399  1.00 19.95 ? 124 PRO A N   1 
ATOM   523  C  CA  . PRO A 1 77  ? 32.952  -1.647  36.884  1.00 21.00 ? 124 PRO A CA  1 
ATOM   524  C  C   . PRO A 1 77  ? 33.284  -1.668  35.398  1.00 19.89 ? 124 PRO A C   1 
ATOM   525  O  O   . PRO A 1 77  ? 32.913  -0.786  34.626  1.00 19.02 ? 124 PRO A O   1 
ATOM   526  C  CB  . PRO A 1 77  ? 31.559  -2.183  37.149  1.00 20.57 ? 124 PRO A CB  1 
ATOM   527  C  CG  . PRO A 1 77  ? 30.725  -0.964  37.412  1.00 24.51 ? 124 PRO A CG  1 
ATOM   528  C  CD  . PRO A 1 77  ? 31.636  0.141   37.896  1.00 21.72 ? 124 PRO A CD  1 
ATOM   529  N  N   . ASP A 1 78  ? 33.937  -2.750  34.981  1.00 19.22 ? 125 ASP A N   1 
ATOM   530  C  CA  . ASP A 1 78  ? 34.297  -2.899  33.587  1.00 19.00 ? 125 ASP A CA  1 
ATOM   531  C  C   . ASP A 1 78  ? 33.083  -3.144  32.700  1.00 16.85 ? 125 ASP A C   1 
ATOM   532  O  O   . ASP A 1 78  ? 33.080  -2.723  31.554  1.00 20.07 ? 125 ASP A O   1 
ATOM   533  C  CB  . ASP A 1 78  ? 35.250  -4.057  33.372  1.00 21.27 ? 125 ASP A CB  1 
ATOM   534  C  CG  . ASP A 1 78  ? 36.720  -3.773  33.628  1.00 25.74 ? 125 ASP A CG  1 
ATOM   535  O  OD1 . ASP A 1 78  ? 37.072  -2.609  33.866  1.00 24.82 ? 125 ASP A OD1 1 
ATOM   536  O  OD2 . ASP A 1 78  ? 37.485  -4.744  33.558  1.00 25.88 ? 125 ASP A OD2 1 
ATOM   537  N  N   . ASP A 1 79  ? 32.062  -3.784  33.230  1.00 15.87 ? 126 ASP A N   1 
ATOM   538  C  CA  . ASP A 1 79  ? 30.812  -4.037  32.550  1.00 14.43 ? 126 ASP A CA  1 
ATOM   539  C  C   . ASP A 1 79  ? 29.727  -3.233  33.278  1.00 15.69 ? 126 ASP A C   1 
ATOM   540  O  O   . ASP A 1 79  ? 29.658  -3.287  34.487  1.00 16.09 ? 126 ASP A O   1 
ATOM   541  C  CB  . ASP A 1 79  ? 30.479  -5.525  32.508  1.00 15.26 ? 126 ASP A CB  1 
ATOM   542  C  CG  . ASP A 1 79  ? 29.310  -5.856  31.602  1.00 16.34 ? 126 ASP A CG  1 
ATOM   543  O  OD1 . ASP A 1 79  ? 28.189  -5.488  31.959  1.00 15.59 ? 126 ASP A OD1 1 
ATOM   544  O  OD2 . ASP A 1 79  ? 29.556  -6.438  30.523  1.00 18.16 ? 126 ASP A OD2 1 
ATOM   545  N  N   . THR A 1 80  ? 28.789  -2.636  32.544  1.00 14.62 ? 127 THR A N   1 
ATOM   546  C  CA  . THR A 1 80  ? 27.782  -1.743  33.146  1.00 13.93 ? 127 THR A CA  1 
ATOM   547  C  C   . THR A 1 80  ? 26.657  -2.510  33.834  1.00 15.60 ? 127 THR A C   1 
ATOM   548  O  O   . THR A 1 80  ? 25.884  -1.900  34.576  1.00 16.55 ? 127 THR A O   1 
ATOM   549  C  CB  . THR A 1 80  ? 27.250  -0.795  32.065  1.00 14.10 ? 127 THR A CB  1 
ATOM   550  O  OG1 . THR A 1 80  ? 26.660  -1.545  30.996  1.00 14.72 ? 127 THR A OG1 1 
ATOM   551  C  CG2 . THR A 1 80  ? 28.355  0.085   31.511  1.00 15.45 ? 127 THR A CG2 1 
ATOM   552  N  N   . GLY A 1 81  ? 26.558  -3.837  33.645  1.00 14.41 ? 128 GLY A N   1 
ATOM   553  C  CA  . GLY A 1 81  ? 25.837  -4.685  34.559  1.00 15.55 ? 128 GLY A CA  1 
ATOM   554  C  C   . GLY A 1 81  ? 24.383  -4.969  34.202  1.00 14.54 ? 128 GLY A C   1 
ATOM   555  O  O   . GLY A 1 81  ? 23.770  -5.832  34.820  1.00 17.30 ? 128 GLY A O   1 
ATOM   556  N  N   . GLU A 1 82  ? 23.790  -4.287  33.210  1.00 14.96 ? 129 GLU A N   1 
ATOM   557  C  CA  . GLU A 1 82  ? 22.362  -4.440  32.985  1.00 13.71 ? 129 GLU A CA  1 
ATOM   558  C  C   . GLU A 1 82  ? 21.983  -5.713  32.242  1.00 15.40 ? 129 GLU A C   1 
ATOM   559  O  O   . GLU A 1 82  ? 20.798  -5.983  32.109  1.00 17.37 ? 129 GLU A O   1 
ATOM   560  C  CB  . GLU A 1 82  ? 21.714  -3.217  32.338  1.00 13.92 ? 129 GLU A CB  1 
ATOM   561  C  CG  . GLU A 1 82  ? 22.026  -3.041  30.857  1.00 14.86 ? 129 GLU A CG  1 
ATOM   562  C  CD  . GLU A 1 82  ? 23.330  -2.353  30.562  1.00 15.15 ? 129 GLU A CD  1 
ATOM   563  O  OE1 . GLU A 1 82  ? 24.200  -2.257  31.437  1.00 15.18 ? 129 GLU A OE1 1 
ATOM   564  O  OE2 . GLU A 1 82  ? 23.408  -1.807  29.454  1.00 15.08 ? 129 GLU A OE2 1 
ATOM   565  N  N   . ALA A 1 83  ? 22.975  -6.505  31.808  1.00 14.83 ? 130 ALA A N   1 
ATOM   566  C  CA  . ALA A 1 83  ? 22.701  -7.799  31.202  1.00 14.49 ? 130 ALA A CA  1 
ATOM   567  C  C   . ALA A 1 83  ? 23.025  -8.954  32.161  1.00 16.05 ? 130 ALA A C   1 
ATOM   568  O  O   . ALA A 1 83  ? 23.002  -10.109 31.754  1.00 18.25 ? 130 ALA A O   1 
ATOM   569  C  CB  . ALA A 1 83  ? 23.455  -7.960  29.885  1.00 14.08 ? 130 ALA A CB  1 
ATOM   570  N  N   . LEU A 1 84  ? 23.341  -8.666  33.417  1.00 15.46 ? 131 LEU A N   1 
ATOM   571  C  CA  . LEU A 1 84  ? 23.640  -9.752  34.325  1.00 17.98 ? 131 LEU A CA  1 
ATOM   572  C  C   . LEU A 1 84  ? 22.423  -10.646 34.431  1.00 18.39 ? 131 LEU A C   1 
ATOM   573  O  O   . LEU A 1 84  ? 21.290  -10.187 34.512  1.00 20.88 ? 131 LEU A O   1 
ATOM   574  C  CB  . LEU A 1 84  ? 24.026  -9.241  35.705  1.00 18.79 ? 131 LEU A CB  1 
ATOM   575  C  CG  . LEU A 1 84  ? 25.411  -8.632  35.809  1.00 22.78 ? 131 LEU A CG  1 
ATOM   576  C  CD1 . LEU A 1 84  ? 25.504  -7.975  37.183  1.00 25.27 ? 131 LEU A CD1 1 
ATOM   577  C  CD2 . LEU A 1 84  ? 26.465  -9.707  35.646  1.00 25.10 ? 131 LEU A CD2 1 
ATOM   578  N  N   . GLY A 1 85  ? 22.678  -11.959 34.409  1.00 21.10 ? 132 GLY A N   1 
ATOM   579  C  CA  . GLY A 1 85  ? 21.584  -12.895 34.597  1.00 21.39 ? 132 GLY A CA  1 
ATOM   580  C  C   . GLY A 1 85  ? 20.778  -13.155 33.336  1.00 23.89 ? 132 GLY A C   1 
ATOM   581  O  O   . GLY A 1 85  ? 19.771  -13.852 33.387  1.00 26.43 ? 132 GLY A O   1 
ATOM   582  N  N   . LEU A 1 86  ? 21.192  -12.575 32.199  1.00 19.85 ? 133 LEU A N   1 
ATOM   583  C  CA  . LEU A 1 86  ? 20.449  -12.789 30.968  1.00 19.99 ? 133 LEU A CA  1 
ATOM   584  C  C   . LEU A 1 86  ? 21.221  -13.770 30.105  1.00 17.23 ? 133 LEU A C   1 
ATOM   585  O  O   . LEU A 1 86  ? 22.457  -13.799 30.098  1.00 22.08 ? 133 LEU A O   1 
ATOM   586  C  CB  . LEU A 1 86  ? 20.182  -11.501 30.184  1.00 17.52 ? 133 LEU A CB  1 
ATOM   587  C  CG  . LEU A 1 86  ? 19.491  -10.389 30.981  1.00 19.04 ? 133 LEU A CG  1 
ATOM   588  C  CD1 . LEU A 1 86  ? 19.257  -9.234  30.053  1.00 18.34 ? 133 LEU A CD1 1 
ATOM   589  C  CD2 . LEU A 1 86  ? 18.209  -10.883 31.591  1.00 19.82 ? 133 LEU A CD2 1 
ATOM   590  N  N   . LYS A 1 87  ? 20.459  -14.493 29.279  1.00 19.15 ? 134 LYS A N   1 
ATOM   591  C  CA  . LYS A 1 87  ? 21.031  -15.425 28.332  1.00 18.39 ? 134 LYS A CA  1 
ATOM   592  C  C   . LYS A 1 87  ? 21.605  -14.647 27.167  1.00 17.57 ? 134 LYS A C   1 
ATOM   593  O  O   . LYS A 1 87  ? 21.265  -13.488 26.960  1.00 16.52 ? 134 LYS A O   1 
ATOM   594  C  CB  . LYS A 1 87  ? 19.959  -16.411 27.868  1.00 21.72 ? 134 LYS A CB  1 
ATOM   595  C  CG  . LYS A 1 87  ? 19.520  -17.411 28.928  1.00 26.79 ? 134 LYS A CG  1 
ATOM   596  C  CD  . LYS A 1 87  ? 20.636  -18.348 29.391  1.00 35.59 ? 134 LYS A CD  1 
ATOM   597  C  CE  . LYS A 1 87  ? 20.572  -19.740 28.823  1.00 43.56 ? 134 LYS A CE  1 
ATOM   598  N  NZ  . LYS A 1 87  ? 21.724  -20.533 29.266  1.00 45.70 ? 134 LYS A NZ  1 
ATOM   599  N  N   . PRO A 1 88  ? 22.485  -15.286 26.367  1.00 17.42 ? 135 PRO A N   1 
ATOM   600  C  CA  . PRO A 1 88  ? 23.017  -14.639 25.168  1.00 17.50 ? 135 PRO A CA  1 
ATOM   601  C  C   . PRO A 1 88  ? 21.947  -14.117 24.223  1.00 15.57 ? 135 PRO A C   1 
ATOM   602  O  O   . PRO A 1 88  ? 22.181  -13.130 23.507  1.00 16.01 ? 135 PRO A O   1 
ATOM   603  C  CB  . PRO A 1 88  ? 23.911  -15.730 24.537  1.00 18.39 ? 135 PRO A CB  1 
ATOM   604  C  CG  . PRO A 1 88  ? 24.160  -16.757 25.600  1.00 19.58 ? 135 PRO A CG  1 
ATOM   605  C  CD  . PRO A 1 88  ? 23.023  -16.642 26.592  1.00 18.43 ? 135 PRO A CD  1 
ATOM   606  N  N   . SER A 1 89  ? 20.797  -14.781 24.155  1.00 14.01 ? 136 SER A N   1 
ATOM   607  C  CA  . SER A 1 89  ? 19.663  -14.262 23.418  1.00 15.05 ? 136 SER A CA  1 
ATOM   608  C  C   . SER A 1 89  ? 19.994  -14.052 21.938  1.00 15.12 ? 136 SER A C   1 
ATOM   609  O  O   . SER A 1 89  ? 19.493  -13.111 21.301  1.00 15.15 ? 136 SER A O   1 
ATOM   610  C  CB  . SER A 1 89  ? 19.142  -12.996 24.045  1.00 18.11 ? 136 SER A CB  1 
ATOM   611  O  OG  . SER A 1 89  ? 18.959  -13.192 25.457  1.00 20.91 ? 136 SER A OG  1 
ATOM   612  N  N   . ARG A 1 90  ? 20.791  -14.968 21.375  1.00 13.81 ? 137 ARG A N   1 
ATOM   613  C  CA  . ARG A 1 90  ? 21.161  -14.962 19.964  1.00 12.91 ? 137 ARG A CA  1 
ATOM   614  C  C   . ARG A 1 90  ? 21.830  -13.655 19.583  1.00 13.46 ? 137 ARG A C   1 
ATOM   615  O  O   . ARG A 1 90  ? 21.736  -13.283 18.412  1.00 13.45 ? 137 ARG A O   1 
ATOM   616  C  CB  . ARG A 1 90  ? 19.969  -15.302 19.081  1.00 14.68 ? 137 ARG A CB  1 
ATOM   617  C  CG  . ARG A 1 90  ? 19.439  -16.697 19.346  1.00 16.11 ? 137 ARG A CG  1 
ATOM   618  C  CD  . ARG A 1 90  ? 18.585  -17.177 18.177  1.00 17.68 ? 137 ARG A CD  1 
ATOM   619  N  NE  . ARG A 1 90  ? 17.423  -16.308 17.980  1.00 18.05 ? 137 ARG A NE  1 
ATOM   620  C  CZ  . ARG A 1 90  ? 16.642  -16.284 16.922  1.00 20.18 ? 137 ARG A CZ  1 
ATOM   621  N  NH1 . ARG A 1 90  ? 15.643  -15.423 16.835  1.00 19.73 ? 137 ARG A NH1 1 
ATOM   622  N  NH2 . ARG A 1 90  ? 16.831  -17.161 15.956  1.00 23.04 ? 137 ARG A NH2 1 
ATOM   623  N  N   . LEU A 1 91  ? 22.525  -12.969 20.490  1.00 11.55 ? 138 LEU A N   1 
ATOM   624  C  CA  . LEU A 1 91  ? 23.210  -11.732 20.165  1.00 12.12 ? 138 LEU A CA  1 
ATOM   625  C  C   . LEU A 1 91  ? 24.214  -11.979 19.051  1.00 12.68 ? 138 LEU A C   1 
ATOM   626  O  O   . LEU A 1 91  ? 25.084  -12.845 19.156  1.00 12.78 ? 138 LEU A O   1 
ATOM   627  C  CB  . LEU A 1 91  ? 23.913  -11.143 21.368  1.00 11.83 ? 138 LEU A CB  1 
ATOM   628  C  CG  . LEU A 1 91  ? 24.721  -9.881  21.125  1.00 13.08 ? 138 LEU A CG  1 
ATOM   629  C  CD1 . LEU A 1 91  ? 23.796  -8.673  20.756  1.00 13.08 ? 138 LEU A CD1 1 
ATOM   630  C  CD2 . LEU A 1 91  ? 25.558  -9.565  22.350  1.00 13.88 ? 138 LEU A CD2 1 
ATOM   631  N  N   . THR A 1 92  ? 24.164  -11.147 18.004  1.00 12.16 ? 139 THR A N   1 
ATOM   632  C  CA  . THR A 1 92  ? 25.226  -11.036 17.043  1.00 11.70 ? 139 THR A CA  1 
ATOM   633  C  C   . THR A 1 92  ? 25.673  -9.588  17.009  1.00 11.80 ? 139 THR A C   1 
ATOM   634  O  O   . THR A 1 92  ? 24.865  -8.673  17.213  1.00 12.69 ? 139 THR A O   1 
ATOM   635  C  CB  . THR A 1 92  ? 24.820  -11.529 15.662  1.00 11.51 ? 139 THR A CB  1 
ATOM   636  O  OG1 . THR A 1 92  ? 23.684  -10.797 15.194  1.00 11.91 ? 139 THR A OG1 1 
ATOM   637  C  CG2 . THR A 1 92  ? 24.508  -12.999 15.628  1.00 12.09 ? 139 THR A CG2 1 
ATOM   638  N  N   . LEU A 1 93  ? 26.961  -9.383  16.736  1.00 11.82 ? 140 LEU A N   1 
ATOM   639  C  CA  . LEU A 1 93  ? 27.540  -8.064  16.626  1.00 12.05 ? 140 LEU A CA  1 
ATOM   640  C  C   . LEU A 1 93  ? 28.285  -8.071  15.308  1.00 13.03 ? 140 LEU A C   1 
ATOM   641  O  O   . LEU A 1 93  ? 29.242  -8.820  15.164  1.00 14.80 ? 140 LEU A O   1 
ATOM   642  C  CB  . LEU A 1 93  ? 28.478  -7.759  17.782  1.00 12.46 ? 140 LEU A CB  1 
ATOM   643  C  CG  . LEU A 1 93  ? 27.831  -7.614  19.156  1.00 15.39 ? 140 LEU A CG  1 
ATOM   644  C  CD1 . LEU A 1 93  ? 28.907  -7.572  20.216  1.00 16.27 ? 140 LEU A CD1 1 
ATOM   645  C  CD2 . LEU A 1 93  ? 26.993  -6.363  19.211  1.00 16.44 ? 140 LEU A CD2 1 
ATOM   646  N  N   . THR A 1 94  ? 27.905  -7.171  14.410  1.00 12.57 ? 141 THR A N   1 
ATOM   647  C  CA  . THR A 1 94  ? 28.433  -7.108  13.057  1.00 11.80 ? 141 THR A CA  1 
ATOM   648  C  C   . THR A 1 94  ? 28.996  -5.716  12.871  1.00 12.99 ? 141 THR A C   1 
ATOM   649  O  O   . THR A 1 94  ? 28.269  -4.741  13.027  1.00 14.61 ? 141 THR A O   1 
ATOM   650  C  CB  . THR A 1 94  ? 27.314  -7.413  12.057  1.00 13.92 ? 141 THR A CB  1 
ATOM   651  O  OG1 . THR A 1 94  ? 26.584  -8.574  12.448  1.00 13.83 ? 141 THR A OG1 1 
ATOM   652  C  CG2 . THR A 1 94  ? 27.871  -7.587  10.659  1.00 15.31 ? 141 THR A CG2 1 
ATOM   653  N  N   . ILE A 1 95  ? 30.270  -5.618  12.509  1.00 11.80 ? 142 ILE A N   1 
ATOM   654  C  CA  . ILE A 1 95  ? 30.932  -4.332  12.340  1.00 13.13 ? 142 ILE A CA  1 
ATOM   655  C  C   . ILE A 1 95  ? 31.050  -4.035  10.843  1.00 12.68 ? 142 ILE A C   1 
ATOM   656  O  O   . ILE A 1 95  ? 31.217  -4.923  10.031  1.00 13.75 ? 142 ILE A O   1 
ATOM   657  C  CB  . ILE A 1 95  ? 32.304  -4.308  13.042  1.00 15.25 ? 142 ILE A CB  1 
ATOM   658  C  CG1 . ILE A 1 95  ? 32.877  -2.880  13.127  1.00 16.37 ? 142 ILE A CG1 1 
ATOM   659  C  CG2 . ILE A 1 95  ? 33.297  -5.253  12.406  1.00 15.26 ? 142 ILE A CG2 1 
ATOM   660  C  CD1 . ILE A 1 95  ? 34.115  -2.773  13.998  1.00 17.77 ? 142 ILE A CD1 1 
ATOM   661  N  N   . GLY A 1 96  ? 30.918  -2.755  10.524  1.00 13.56 ? 143 GLY A N   1 
ATOM   662  C  CA  . GLY A 1 96  ? 31.167  -2.313  9.168   1.00 14.38 ? 143 GLY A CA  1 
ATOM   663  C  C   . GLY A 1 96  ? 31.963  -1.019  9.161   1.00 14.42 ? 143 GLY A C   1 
ATOM   664  O  O   . GLY A 1 96  ? 31.963  -0.245  10.108  1.00 15.56 ? 143 GLY A O   1 
ATOM   665  N  N   . PHE A 1 97  ? 32.603  -0.772  8.028   1.00 14.99 ? 144 PHE A N   1 
ATOM   666  C  CA  . PHE A 1 97  ? 33.431  0.420   7.835   1.00 15.36 ? 144 PHE A CA  1 
ATOM   667  C  C   . PHE A 1 97  ? 32.835  1.288   6.725   1.00 15.08 ? 144 PHE A C   1 
ATOM   668  O  O   . PHE A 1 97  ? 32.606  0.826   5.625   1.00 16.42 ? 144 PHE A O   1 
ATOM   669  C  CB  . PHE A 1 97  ? 34.842  0.007   7.429   1.00 16.86 ? 144 PHE A CB  1 
ATOM   670  C  CG  . PHE A 1 97  ? 35.535  -0.888  8.428   1.00 16.76 ? 144 PHE A CG  1 
ATOM   671  C  CD1 . PHE A 1 97  ? 35.388  -0.662  9.779   1.00 19.80 ? 144 PHE A CD1 1 
ATOM   672  C  CD2 . PHE A 1 97  ? 36.368  -1.900  7.999   1.00 20.90 ? 144 PHE A CD2 1 
ATOM   673  C  CE1 . PHE A 1 97  ? 36.051  -1.464  10.701  1.00 20.37 ? 144 PHE A CE1 1 
ATOM   674  C  CE2 . PHE A 1 97  ? 37.019  -2.702  8.924   1.00 23.29 ? 144 PHE A CE2 1 
ATOM   675  C  CZ  . PHE A 1 97  ? 36.874  -2.452  10.265  1.00 22.53 ? 144 PHE A CZ  1 
ATOM   676  N  N   . GLY A 1 98  ? 32.647  2.571   7.014   1.00 15.58 ? 145 GLY A N   1 
ATOM   677  C  CA  . GLY A 1 98  ? 32.041  3.498   6.063   1.00 16.71 ? 145 GLY A CA  1 
ATOM   678  C  C   . GLY A 1 98  ? 33.079  4.108   5.133   1.00 17.06 ? 145 GLY A C   1 
ATOM   679  O  O   . GLY A 1 98  ? 34.267  4.128   5.452   1.00 18.04 ? 145 GLY A O   1 
ATOM   680  N  N   . PRO A 1 99  ? 32.644  4.636   3.972   1.00 18.98 ? 146 PRO A N   1 
ATOM   681  C  CA  . PRO A 1 99  ? 33.593  5.276   3.049   1.00 18.27 ? 146 PRO A CA  1 
ATOM   682  C  C   . PRO A 1 99  ? 34.496  6.315   3.699   1.00 19.59 ? 146 PRO A C   1 
ATOM   683  O  O   . PRO A 1 99  ? 35.672  6.402   3.349   1.00 21.17 ? 146 PRO A O   1 
ATOM   684  C  CB  . PRO A 1 99  ? 32.696  5.929   1.971   1.00 20.22 ? 146 PRO A CB  1 
ATOM   685  C  CG  . PRO A 1 99  ? 31.277  5.453   2.238   1.00 22.62 ? 146 PRO A CG  1 
ATOM   686  C  CD  . PRO A 1 99  ? 31.254  4.605   3.492   1.00 19.65 ? 146 PRO A CD  1 
ATOM   687  N  N   . SER A 1 100 ? 33.949  7.082   4.634   1.00 18.71 ? 147 SER A N   1 
ATOM   688  C  CA  . SER A 1 100 ? 34.685  8.162   5.288   1.00 20.79 ? 147 SER A CA  1 
ATOM   689  C  C   . SER A 1 100 ? 35.861  7.644   6.115   1.00 24.15 ? 147 SER A C   1 
ATOM   690  O  O   . SER A 1 100 ? 36.825  8.382   6.317   1.00 23.51 ? 147 SER A O   1 
ATOM   691  C  CB  . SER A 1 100 ? 33.780  9.039   6.100   1.00 21.43 ? 147 SER A CB  1 
ATOM   692  O  OG  . SER A 1 100 ? 32.975  8.291   7.013   1.00 22.38 ? 147 SER A OG  1 
ATOM   693  N  N   . LEU A 1 101 ? 35.823  6.389   6.561   1.00 20.49 ? 148 LEU A N   1 
ATOM   694  C  CA  . LEU A 1 101 ? 36.949  5.824   7.307   1.00 20.32 ? 148 LEU A CA  1 
ATOM   695  C  C   . LEU A 1 101 ? 38.230  5.866   6.474   1.00 21.87 ? 148 LEU A C   1 
ATOM   696  O  O   . LEU A 1 101 ? 39.307  6.050   7.030   1.00 21.50 ? 148 LEU A O   1 
ATOM   697  C  CB  . LEU A 1 101 ? 36.674  4.393   7.755   1.00 22.04 ? 148 LEU A CB  1 
ATOM   698  C  CG  . LEU A 1 101 ? 37.732  3.764   8.675   1.00 22.32 ? 148 LEU A CG  1 
ATOM   699  C  CD1 . LEU A 1 101 ? 37.719  4.490   9.987   1.00 24.47 ? 148 LEU A CD1 1 
ATOM   700  C  CD2 . LEU A 1 101 ? 37.538  2.263   8.888   1.00 24.76 ? 148 LEU A CD2 1 
ATOM   701  N  N   . PHE A 1 102 ? 38.102  5.695   5.162   1.00 21.32 ? 149 PHE A N   1 
ATOM   702  C  CA  . PHE A 1 102 ? 39.245  5.445   4.296   1.00 23.71 ? 149 PHE A CA  1 
ATOM   703  C  C   . PHE A 1 102 ? 39.997  6.759   4.035   1.00 28.41 ? 149 PHE A C   1 
ATOM   704  O  O   . PHE A 1 102 ? 41.081  6.727   3.466   1.00 31.90 ? 149 PHE A O   1 
ATOM   705  C  CB  . PHE A 1 102 ? 38.790  4.716   3.025   1.00 23.02 ? 149 PHE A CB  1 
ATOM   706  C  CG  . PHE A 1 102 ? 38.264  3.324   3.339   1.00 21.42 ? 149 PHE A CG  1 
ATOM   707  C  CD1 . PHE A 1 102 ? 36.922  3.116   3.672   1.00 23.34 ? 149 PHE A CD1 1 
ATOM   708  C  CD2 . PHE A 1 102 ? 39.126  2.237   3.346   1.00 22.29 ? 149 PHE A CD2 1 
ATOM   709  C  CE1 . PHE A 1 102 ? 36.473  1.851   3.993   1.00 24.87 ? 149 PHE A CE1 1 
ATOM   710  C  CE2 . PHE A 1 102 ? 38.677  0.977   3.668   1.00 23.28 ? 149 PHE A CE2 1 
ATOM   711  C  CZ  . PHE A 1 102 ? 37.347  0.790   4.000   1.00 24.41 ? 149 PHE A CZ  1 
ATOM   712  N  N   . THR A 1 103 ? 39.522  7.884   4.579   1.00 27.54 ? 150 THR A N   1 
ATOM   713  C  CA  . THR A 1 103 ? 40.285  9.128   4.513   1.00 28.81 ? 150 THR A CA  1 
ATOM   714  C  C   . THR A 1 103 ? 41.263  9.216   5.686   1.00 31.53 ? 150 THR A C   1 
ATOM   715  O  O   . THR A 1 103 ? 41.969  10.214  5.796   1.00 32.61 ? 150 THR A O   1 
ATOM   716  C  CB  . THR A 1 103 ? 39.358  10.343  4.511   1.00 28.70 ? 150 THR A CB  1 
ATOM   717  O  OG1 . THR A 1 103 ? 38.728  10.413  5.782   1.00 31.45 ? 150 THR A OG1 1 
ATOM   718  C  CG2 . THR A 1 103 ? 38.313  10.312  3.413   1.00 31.87 ? 150 THR A CG2 1 
ATOM   719  N  N   . ARG A 1 104 ? 41.273  8.210   6.574   1.00 30.17 ? 151 ARG A N   1 
ATOM   720  C  CA  . ARG A 1 104 ? 42.109  8.200   7.760   1.00 30.48 ? 151 ARG A CA  1 
ATOM   721  C  C   . ARG A 1 104 ? 43.115  7.053   7.660   1.00 27.98 ? 151 ARG A C   1 
ATOM   722  O  O   . ARG A 1 104 ? 42.950  6.130   6.873   1.00 28.50 ? 151 ARG A O   1 
ATOM   723  C  CB  . ARG A 1 104 ? 41.234  8.039   9.012   1.00 36.20 ? 151 ARG A CB  1 
ATOM   724  C  CG  . ARG A 1 104 ? 40.133  9.080   9.169   1.00 41.13 ? 151 ARG A CG  1 
ATOM   725  C  CD  . ARG A 1 104 ? 39.452  8.988   10.528  1.00 45.58 ? 151 ARG A CD  1 
ATOM   726  N  NE  . ARG A 1 104 ? 38.722  10.233  10.788  1.00 50.61 ? 151 ARG A NE  1 
ATOM   727  C  CZ  . ARG A 1 104 ? 39.090  11.152  11.677  1.00 48.03 ? 151 ARG A CZ  1 
ATOM   728  N  NH1 . ARG A 1 104 ? 39.995  10.879  12.606  1.00 40.38 ? 151 ARG A NH1 1 
ATOM   729  N  NH2 . ARG A 1 104 ? 38.513  12.338  11.653  1.00 51.65 ? 151 ARG A NH2 1 
ATOM   730  N  N   . PHE A 1 105 ? 44.187  7.147   8.460   1.00 29.24 ? 152 PHE A N   1 
ATOM   731  C  CA  . PHE A 1 105 ? 45.097  6.052   8.756   1.00 29.25 ? 152 PHE A CA  1 
ATOM   732  C  C   . PHE A 1 105 ? 45.794  5.485   7.517   1.00 26.69 ? 152 PHE A C   1 
ATOM   733  O  O   . PHE A 1 105 ? 46.205  4.336   7.551   1.00 31.56 ? 152 PHE A O   1 
ATOM   734  C  CB  . PHE A 1 105 ? 44.362  4.904   9.469   1.00 28.87 ? 152 PHE A CB  1 
ATOM   735  C  CG  . PHE A 1 105 ? 43.502  5.322   10.653  1.00 26.36 ? 152 PHE A CG  1 
ATOM   736  C  CD1 . PHE A 1 105 ? 44.008  6.130   11.663  1.00 27.06 ? 152 PHE A CD1 1 
ATOM   737  C  CD2 . PHE A 1 105 ? 42.210  4.840   10.800  1.00 27.88 ? 152 PHE A CD2 1 
ATOM   738  C  CE1 . PHE A 1 105 ? 43.232  6.466   12.761  1.00 26.79 ? 152 PHE A CE1 1 
ATOM   739  C  CE2 . PHE A 1 105 ? 41.423  5.230   11.872  1.00 27.04 ? 152 PHE A CE2 1 
ATOM   740  C  CZ  . PHE A 1 105 ? 41.944  6.006   12.868  1.00 26.41 ? 152 PHE A CZ  1 
ATOM   741  N  N   . GLY A 1 106 ? 45.929  6.273   6.449   1.00 29.38 ? 153 GLY A N   1 
ATOM   742  C  CA  . GLY A 1 106 ? 46.621  5.851   5.237   1.00 29.53 ? 153 GLY A CA  1 
ATOM   743  C  C   . GLY A 1 106 ? 45.856  4.790   4.453   1.00 31.29 ? 153 GLY A C   1 
ATOM   744  O  O   . GLY A 1 106 ? 46.464  4.022   3.701   1.00 32.39 ? 153 GLY A O   1 
ATOM   745  N  N   . LEU A 1 107 ? 44.519  4.778   4.615   1.00 30.01 ? 154 LEU A N   1 
ATOM   746  C  CA  . LEU A 1 107 ? 43.672  3.736   4.050   1.00 29.74 ? 154 LEU A CA  1 
ATOM   747  C  C   . LEU A 1 107 ? 43.094  4.098   2.679   1.00 27.39 ? 154 LEU A C   1 
ATOM   748  O  O   . LEU A 1 107 ? 42.399  3.277   2.094   1.00 27.06 ? 154 LEU A O   1 
ATOM   749  C  CB  . LEU A 1 107 ? 42.525  3.463   5.024   1.00 28.13 ? 154 LEU A CB  1 
ATOM   750  C  CG  . LEU A 1 107 ? 42.937  2.861   6.367   1.00 27.83 ? 154 LEU A CG  1 
ATOM   751  C  CD1 . LEU A 1 107 ? 41.704  2.820   7.260   1.00 27.66 ? 154 LEU A CD1 1 
ATOM   752  C  CD2 . LEU A 1 107 ? 43.550  1.488   6.228   1.00 28.13 ? 154 LEU A CD2 1 
ATOM   753  N  N   . ALA A 1 108 ? 43.407  5.286   2.131   1.00 31.70 ? 155 ALA A N   1 
ATOM   754  C  CA  . ALA A 1 108 ? 42.742  5.762   0.918   1.00 33.75 ? 155 ALA A CA  1 
ATOM   755  C  C   . ALA A 1 108 ? 42.725  4.710   -0.194  1.00 31.45 ? 155 ALA A C   1 
ATOM   756  O  O   . ALA A 1 108 ? 41.691  4.461   -0.823  1.00 29.32 ? 155 ALA A O   1 
ATOM   757  C  CB  . ALA A 1 108 ? 43.389  7.058   0.451   1.00 36.88 ? 155 ALA A CB  1 
ATOM   758  N  N   . ASP A 1 109 ? 43.855  4.049   -0.429  1.00 30.12 ? 156 ASP A N   1 
ATOM   759  C  CA  . ASP A 1 109 ? 43.979  3.161   -1.574  1.00 32.35 ? 156 ASP A CA  1 
ATOM   760  C  C   . ASP A 1 109 ? 43.282  1.823   -1.346  1.00 29.51 ? 156 ASP A C   1 
ATOM   761  O  O   . ASP A 1 109 ? 43.225  0.981   -2.243  1.00 29.28 ? 156 ASP A O   1 
ATOM   762  C  CB  . ASP A 1 109 ? 45.431  2.791   -1.839  1.00 35.63 ? 156 ASP A CB  1 
ATOM   763  C  CG  . ASP A 1 109 ? 46.297  3.862   -2.473  1.00 42.64 ? 156 ASP A CG  1 
ATOM   764  O  OD1 . ASP A 1 109 ? 45.745  4.899   -2.887  1.00 40.26 ? 156 ASP A OD1 1 
ATOM   765  O  OD2 . ASP A 1 109 ? 47.520  3.637   -2.521  1.00 45.72 ? 156 ASP A OD2 1 
ATOM   766  N  N   . LEU A 1 110 ? 42.779  1.593   -0.124  1.00 25.59 ? 157 LEU A N   1 
ATOM   767  C  CA  . LEU A 1 110 ? 42.223  0.291   0.202   1.00 25.26 ? 157 LEU A CA  1 
ATOM   768  C  C   . LEU A 1 110 ? 40.698  0.339   0.184   1.00 22.55 ? 157 LEU A C   1 
ATOM   769  O  O   . LEU A 1 110 ? 40.070  -0.689  0.458   1.00 22.93 ? 157 LEU A O   1 
ATOM   770  C  CB  . LEU A 1 110 ? 42.773  -0.215  1.533   1.00 27.81 ? 157 LEU A CB  1 
ATOM   771  C  CG  . LEU A 1 110 ? 44.080  -1.017  1.443   1.00 32.89 ? 157 LEU A CG  1 
ATOM   772  C  CD1 . LEU A 1 110 ? 44.966  -0.716  0.256   1.00 38.79 ? 157 LEU A CD1 1 
ATOM   773  C  CD2 . LEU A 1 110 ? 44.841  -0.803  2.736   1.00 36.71 ? 157 LEU A CD2 1 
ATOM   774  N  N   . ARG A 1 111 ? 40.121  1.502   -0.137  1.00 21.28 ? 158 ARG A N   1 
ATOM   775  C  CA  . ARG A 1 111 ? 38.669  1.586   -0.204  1.00 23.80 ? 158 ARG A CA  1 
ATOM   776  C  C   . ARG A 1 111 ? 38.180  0.688   -1.334  1.00 24.12 ? 158 ARG A C   1 
ATOM   777  O  O   . ARG A 1 111 ? 38.603  0.830   -2.472  1.00 22.66 ? 158 ARG A O   1 
ATOM   778  C  CB  . ARG A 1 111 ? 38.173  3.010   -0.430  1.00 23.94 ? 158 ARG A CB  1 
ATOM   779  C  CG  . ARG A 1 111 ? 36.650  3.073   -0.493  1.00 24.71 ? 158 ARG A CG  1 
ATOM   780  C  CD  . ARG A 1 111 ? 36.197  4.435   -0.839  1.00 26.89 ? 158 ARG A CD  1 
ATOM   781  N  NE  . ARG A 1 111 ? 34.778  4.408   -1.204  1.00 27.93 ? 158 ARG A NE  1 
ATOM   782  C  CZ  . ARG A 1 111 ? 34.022  5.477   -1.295  1.00 25.30 ? 158 ARG A CZ  1 
ATOM   783  N  NH1 . ARG A 1 111 ? 34.523  6.665   -1.004  1.00 28.60 ? 158 ARG A NH1 1 
ATOM   784  N  NH2 . ARG A 1 111 ? 32.766  5.343   -1.669  1.00 26.75 ? 158 ARG A NH2 1 
ATOM   785  N  N   . PRO A 1 112 ? 37.251  -0.258  -1.071  1.00 21.06 ? 159 PRO A N   1 
ATOM   786  C  CA  . PRO A 1 112 ? 36.762  -1.152  -2.113  1.00 21.91 ? 159 PRO A CA  1 
ATOM   787  C  C   . PRO A 1 112 ? 35.938  -0.360  -3.119  1.00 21.45 ? 159 PRO A C   1 
ATOM   788  O  O   . PRO A 1 112 ? 35.115  0.480   -2.741  1.00 21.68 ? 159 PRO A O   1 
ATOM   789  C  CB  . PRO A 1 112 ? 35.877  -2.152  -1.352  1.00 21.94 ? 159 PRO A CB  1 
ATOM   790  C  CG  . PRO A 1 112 ? 36.226  -1.938  0.098   1.00 22.22 ? 159 PRO A CG  1 
ATOM   791  C  CD  . PRO A 1 112 ? 36.625  -0.506  0.245   1.00 21.59 ? 159 PRO A CD  1 
ATOM   792  N  N   . GLU A 1 113 ? 36.119  -0.678  -4.402  1.00 23.76 ? 160 GLU A N   1 
ATOM   793  C  CA  . GLU A 1 113 ? 35.253  -0.153  -5.444  1.00 25.91 ? 160 GLU A CA  1 
ATOM   794  C  C   . GLU A 1 113 ? 33.789  -0.523  -5.179  1.00 22.24 ? 160 GLU A C   1 
ATOM   795  O  O   . GLU A 1 113 ? 32.903  0.257   -5.498  1.00 22.45 ? 160 GLU A O   1 
ATOM   796  C  CB  . GLU A 1 113 ? 35.673  -0.717  -6.800  1.00 31.70 ? 160 GLU A CB  1 
ATOM   797  C  CG  . GLU A 1 113 ? 36.934  -0.057  -7.330  1.00 40.68 ? 160 GLU A CG  1 
ATOM   798  C  CD  . GLU A 1 113 ? 36.633  1.295   -7.943  1.00 45.75 ? 160 GLU A CD  1 
ATOM   799  O  OE1 . GLU A 1 113 ? 37.004  2.316   -7.327  1.00 52.82 ? 160 GLU A OE1 1 
ATOM   800  O  OE2 . GLU A 1 113 ? 36.020  1.316   -9.029  1.00 51.39 ? 160 GLU A OE2 1 
ATOM   801  N  N   . ALA A 1 114 ? 33.538  -1.712  -4.616  1.00 21.96 ? 161 ALA A N   1 
ATOM   802  C  CA  . ALA A 1 114 ? 32.170  -2.152  -4.388  1.00 22.33 ? 161 ALA A CA  1 
ATOM   803  C  C   . ALA A 1 114 ? 31.500  -1.325  -3.298  1.00 22.35 ? 161 ALA A C   1 
ATOM   804  O  O   . ALA A 1 114 ? 30.283  -1.404  -3.149  1.00 21.57 ? 161 ALA A O   1 
ATOM   805  C  CB  . ALA A 1 114 ? 32.148  -3.593  -4.013  1.00 23.17 ? 161 ALA A CB  1 
ATOM   806  N  N   . LEU A 1 115 ? 32.296  -0.593  -2.519  1.00 20.12 ? 162 LEU A N   1 
ATOM   807  C  CA  . LEU A 1 115 ? 31.785  0.320   -1.518  1.00 19.63 ? 162 LEU A CA  1 
ATOM   808  C  C   . LEU A 1 115 ? 31.497  1.666   -2.174  1.00 21.46 ? 162 LEU A C   1 
ATOM   809  O  O   . LEU A 1 115 ? 32.199  2.665   -1.994  1.00 24.36 ? 162 LEU A O   1 
ATOM   810  C  CB  . LEU A 1 115 ? 32.714  0.462   -0.313  1.00 19.82 ? 162 LEU A CB  1 
ATOM   811  C  CG  . LEU A 1 115 ? 32.172  1.366   0.799   1.00 19.67 ? 162 LEU A CG  1 
ATOM   812  C  CD1 . LEU A 1 115 ? 30.928  0.836   1.423   1.00 21.14 ? 162 LEU A CD1 1 
ATOM   813  C  CD2 . LEU A 1 115 ? 33.225  1.538   1.860   1.00 18.96 ? 162 LEU A CD2 1 
ATOM   814  N  N   . ALA A 1 116 ? 30.387  1.688   -2.903  1.00 21.39 ? 163 ALA A N   1 
ATOM   815  C  CA  . ALA A 1 116 ? 30.053  2.819   -3.761  1.00 23.26 ? 163 ALA A CA  1 
ATOM   816  C  C   . ALA A 1 116 ? 29.209  3.823   -3.000  1.00 26.50 ? 163 ALA A C   1 
ATOM   817  O  O   . ALA A 1 116 ? 28.330  3.432   -2.237  1.00 25.81 ? 163 ALA A O   1 
ATOM   818  C  CB  . ALA A 1 116 ? 29.309  2.306   -4.982  1.00 24.43 ? 163 ALA A CB  1 
ATOM   819  N  N   . ASP A 1 117 ? 29.414  5.118   -3.269  1.00 24.23 ? 164 ASP A N   1 
ATOM   820  C  CA  . ASP A 1 117 ? 28.483  6.108   -2.762  1.00 25.64 ? 164 ASP A CA  1 
ATOM   821  C  C   . ASP A 1 117 ? 27.195  5.953   -3.559  1.00 24.90 ? 164 ASP A C   1 
ATOM   822  O  O   . ASP A 1 117 ? 27.219  5.638   -4.751  1.00 28.20 ? 164 ASP A O   1 
ATOM   823  C  CB  . ASP A 1 117 ? 29.037  7.512   -2.837  1.00 27.92 ? 164 ASP A CB  1 
ATOM   824  C  CG  . ASP A 1 117 ? 30.278  7.751   -1.987  1.00 35.12 ? 164 ASP A CG  1 
ATOM   825  O  OD1 . ASP A 1 117 ? 30.224  7.464   -0.780  1.00 33.70 ? 164 ASP A OD1 1 
ATOM   826  O  OD2 . ASP A 1 117 ? 31.270  8.258   -2.543  1.00 40.35 ? 164 ASP A OD2 1 
ATOM   827  N  N   . LEU A 1 118 ? 26.085  6.136   -2.868  1.00 23.28 ? 165 LEU A N   1 
ATOM   828  C  CA  . LEU A 1 118 ? 24.790  5.992   -3.507  1.00 21.74 ? 165 LEU A CA  1 
ATOM   829  C  C   . LEU A 1 118 ? 24.522  7.264   -4.285  1.00 23.49 ? 165 LEU A C   1 
ATOM   830  O  O   . LEU A 1 118 ? 24.845  8.329   -3.788  1.00 24.38 ? 165 LEU A O   1 
ATOM   831  C  CB  . LEU A 1 118 ? 23.696  5.787   -2.466  1.00 20.93 ? 165 LEU A CB  1 
ATOM   832  C  CG  . LEU A 1 118 ? 23.826  4.502   -1.646  1.00 20.20 ? 165 LEU A CG  1 
ATOM   833  C  CD1 . LEU A 1 118 ? 22.716  4.408   -0.637  1.00 20.78 ? 165 LEU A CD1 1 
ATOM   834  C  CD2 . LEU A 1 118 ? 23.895  3.288   -2.531  1.00 20.65 ? 165 LEU A CD2 1 
ATOM   835  N  N   . PRO A 1 119 ? 23.864  7.180   -5.452  1.00 26.85 ? 166 PRO A N   1 
ATOM   836  C  CA  . PRO A 1 119 ? 23.399  8.388   -6.128  1.00 28.39 ? 166 PRO A CA  1 
ATOM   837  C  C   . PRO A 1 119 ? 22.185  8.922   -5.379  1.00 27.82 ? 166 PRO A C   1 
ATOM   838  O  O   . PRO A 1 119 ? 21.655  8.259   -4.491  1.00 24.34 ? 166 PRO A O   1 
ATOM   839  C  CB  . PRO A 1 119 ? 23.079  7.839   -7.522  1.00 30.04 ? 166 PRO A CB  1 
ATOM   840  C  CG  . PRO A 1 119 ? 22.547  6.457   -7.256  1.00 30.46 ? 166 PRO A CG  1 
ATOM   841  C  CD  . PRO A 1 119 ? 23.425  5.944   -6.109  1.00 27.56 ? 166 PRO A CD  1 
ATOM   842  N  N   . LYS A 1 120 ? 21.759  10.144  -5.709  1.00 26.32 ? 167 LYS A N   1 
ATOM   843  C  CA  . LYS A 1 120 ? 20.521  10.690  -5.195  1.00 29.19 ? 167 LYS A CA  1 
ATOM   844  C  C   . LYS A 1 120 ? 19.398  9.966   -5.921  1.00 25.53 ? 167 LYS A C   1 
ATOM   845  O  O   . LYS A 1 120 ? 19.499  9.676   -7.112  1.00 27.95 ? 167 LYS A O   1 
ATOM   846  C  CB  . LYS A 1 120 ? 20.390  12.196  -5.474  1.00 39.51 ? 167 LYS A CB  1 
ATOM   847  C  CG  . LYS A 1 120 ? 21.537  13.087  -5.004  1.00 52.00 ? 167 LYS A CG  1 
ATOM   848  C  CD  . LYS A 1 120 ? 22.459  13.662  -6.086  1.00 62.68 ? 167 LYS A CD  1 
ATOM   849  C  CE  . LYS A 1 120 ? 23.562  12.759  -6.612  1.00 66.08 ? 167 LYS A CE  1 
ATOM   850  N  NZ  . LYS A 1 120 ? 23.233  11.976  -7.814  1.00 62.72 ? 167 LYS A NZ  1 
ATOM   851  N  N   . PHE A 1 121 ? 18.368  9.605   -5.171  1.00 20.57 ? 168 PHE A N   1 
ATOM   852  C  CA  . PHE A 1 121 ? 17.188  8.994   -5.724  1.00 21.44 ? 168 PHE A CA  1 
ATOM   853  C  C   . PHE A 1 121 ? 16.045  9.992   -5.624  1.00 20.60 ? 168 PHE A C   1 
ATOM   854  O  O   . PHE A 1 121 ? 15.903  10.742  -4.664  1.00 21.67 ? 168 PHE A O   1 
ATOM   855  C  CB  . PHE A 1 121 ? 16.844  7.695   -4.982  1.00 19.62 ? 168 PHE A CB  1 
ATOM   856  C  CG  . PHE A 1 121 ? 17.906  6.629   -5.169  1.00 19.64 ? 168 PHE A CG  1 
ATOM   857  C  CD1 . PHE A 1 121 ? 18.066  5.939   -6.369  1.00 20.02 ? 168 PHE A CD1 1 
ATOM   858  C  CD2 . PHE A 1 121 ? 18.758  6.319   -4.121  1.00 20.17 ? 168 PHE A CD2 1 
ATOM   859  C  CE1 . PHE A 1 121 ? 19.062  5.009   -6.521  1.00 22.02 ? 168 PHE A CE1 1 
ATOM   860  C  CE2 . PHE A 1 121 ? 19.709  5.337   -4.276  1.00 19.78 ? 168 PHE A CE2 1 
ATOM   861  C  CZ  . PHE A 1 121 ? 19.861  4.692   -5.454  1.00 21.16 ? 168 PHE A CZ  1 
ATOM   862  N  N   . PRO A 1 122 ? 15.133  9.990   -6.620  1.00 25.86 ? 169 PRO A N   1 
ATOM   863  C  CA  . PRO A 1 122 ? 13.960  10.851  -6.542  1.00 27.67 ? 169 PRO A CA  1 
ATOM   864  C  C   . PRO A 1 122 ? 13.234  10.590  -5.231  1.00 26.53 ? 169 PRO A C   1 
ATOM   865  O  O   . PRO A 1 122 ? 13.094  9.440   -4.811  1.00 27.25 ? 169 PRO A O   1 
ATOM   866  C  CB  . PRO A 1 122 ? 13.077  10.481  -7.748  1.00 29.62 ? 169 PRO A CB  1 
ATOM   867  C  CG  . PRO A 1 122 ? 13.959  9.623   -8.619  1.00 30.81 ? 169 PRO A CG  1 
ATOM   868  C  CD  . PRO A 1 122 ? 15.129  9.104   -7.788  1.00 27.31 ? 169 PRO A CD  1 
ATOM   869  N  N   . GLY A 1 123 ? 12.774  11.667  -4.603  1.00 24.58 ? 170 GLY A N   1 
ATOM   870  C  CA  . GLY A 1 123 ? 12.004  11.575  -3.386  1.00 23.52 ? 170 GLY A CA  1 
ATOM   871  C  C   . GLY A 1 123 ? 12.874  11.550  -2.118  1.00 21.28 ? 170 GLY A C   1 
ATOM   872  O  O   . GLY A 1 123 ? 12.315  11.698  -1.034  1.00 25.86 ? 170 GLY A O   1 
ATOM   873  N  N   . ASP A 1 124 ? 14.214  11.449  -2.254  1.00 21.63 ? 171 ASP A N   1 
ATOM   874  C  CA  . ASP A 1 124 ? 15.087  11.390  -1.071  1.00 21.02 ? 171 ASP A CA  1 
ATOM   875  C  C   . ASP A 1 124 ? 14.873  12.660  -0.254  1.00 23.14 ? 171 ASP A C   1 
ATOM   876  O  O   . ASP A 1 124 ? 14.772  13.764  -0.813  1.00 23.69 ? 171 ASP A O   1 
ATOM   877  C  CB  . ASP A 1 124 ? 16.573  11.365  -1.419  1.00 23.64 ? 171 ASP A CB  1 
ATOM   878  C  CG  . ASP A 1 124 ? 17.293  10.071  -1.793  1.00 25.92 ? 171 ASP A CG  1 
ATOM   879  O  OD1 . ASP A 1 124 ? 16.669  9.003   -1.678  1.00 24.21 ? 171 ASP A OD1 1 
ATOM   880  O  OD2 . ASP A 1 124 ? 18.486  10.182  -2.236  1.00 28.40 ? 171 ASP A OD2 1 
ATOM   881  N  N   . ASN A 1 125 ? 14.865  12.536  1.066   1.00 19.24 ? 172 ASN A N   1 
ATOM   882  C  CA  . ASN A 1 125 ? 14.930  13.684  1.957   1.00 20.01 ? 172 ASN A CA  1 
ATOM   883  C  C   . ASN A 1 125 ? 15.837  13.303  3.136   1.00 16.44 ? 172 ASN A C   1 
ATOM   884  O  O   . ASN A 1 125 ? 15.345  13.117  4.239   1.00 18.80 ? 172 ASN A O   1 
ATOM   885  C  CB  . ASN A 1 125 ? 13.525  14.063  2.376   1.00 23.48 ? 172 ASN A CB  1 
ATOM   886  C  CG  . ASN A 1 125 ? 13.460  15.329  3.192   1.00 30.38 ? 172 ASN A CG  1 
ATOM   887  O  OD1 . ASN A 1 125 ? 14.400  16.131  3.193   1.00 34.14 ? 172 ASN A OD1 1 
ATOM   888  N  ND2 . ASN A 1 125 ? 12.361  15.511  3.900   1.00 39.14 ? 172 ASN A ND2 1 
ATOM   889  N  N   . LEU A 1 126 ? 17.126  13.168  2.837   1.00 19.47 ? 173 LEU A N   1 
ATOM   890  C  CA  . LEU A 1 126 ? 18.084  12.593  3.777   1.00 19.11 ? 173 LEU A CA  1 
ATOM   891  C  C   . LEU A 1 126 ? 18.511  13.602  4.841   1.00 22.74 ? 173 LEU A C   1 
ATOM   892  O  O   . LEU A 1 126 ? 19.017  14.683  4.543   1.00 23.92 ? 173 LEU A O   1 
ATOM   893  C  CB  . LEU A 1 126 ? 19.286  12.036  3.029   1.00 19.19 ? 173 LEU A CB  1 
ATOM   894  C  CG  . LEU A 1 126 ? 18.994  11.046  1.903   1.00 20.05 ? 173 LEU A CG  1 
ATOM   895  C  CD1 . LEU A 1 126 ? 20.294  10.592  1.321   1.00 22.62 ? 173 LEU A CD1 1 
ATOM   896  C  CD2 . LEU A 1 126 ? 18.202  9.824   2.369   1.00 22.12 ? 173 LEU A CD2 1 
ATOM   897  N  N   . ASP A 1 127 ? 18.347  13.223  6.108   1.00 20.19 ? 174 ASP A N   1 
ATOM   898  C  CA  . ASP A 1 127 ? 18.885  13.975  7.229   1.00 20.41 ? 174 ASP A CA  1 
ATOM   899  C  C   . ASP A 1 127 ? 20.373  13.660  7.360   1.00 22.04 ? 174 ASP A C   1 
ATOM   900  O  O   . ASP A 1 127 ? 20.749  12.531  7.629   1.00 19.79 ? 174 ASP A O   1 
ATOM   901  C  CB  . ASP A 1 127 ? 18.109  13.650  8.486   1.00 22.28 ? 174 ASP A CB  1 
ATOM   902  C  CG  . ASP A 1 127 ? 18.605  14.343  9.737   1.00 27.67 ? 174 ASP A CG  1 
ATOM   903  O  OD1 . ASP A 1 127 ? 19.623  15.016  9.639   1.00 32.10 ? 174 ASP A OD1 1 
ATOM   904  O  OD2 . ASP A 1 127 ? 17.956  14.183  10.757  1.00 33.24 ? 174 ASP A OD2 1 
ATOM   905  N  N   . ARG A 1 128 ? 21.249  14.649  7.162   1.00 21.44 ? 175 ARG A N   1 
ATOM   906  C  CA  . ARG A 1 128 ? 22.683  14.384  7.124   1.00 24.23 ? 175 ARG A CA  1 
ATOM   907  C  C   . ARG A 1 128 ? 23.206  13.967  8.500   1.00 24.51 ? 175 ARG A C   1 
ATOM   908  O  O   . ARG A 1 128 ? 24.207  13.242  8.574   1.00 25.61 ? 175 ARG A O   1 
ATOM   909  C  CB  . ARG A 1 128 ? 23.473  15.588  6.574   1.00 31.43 ? 175 ARG A CB  1 
ATOM   910  C  CG  . ARG A 1 128 ? 23.784  15.463  5.086   1.00 41.85 ? 175 ARG A CG  1 
ATOM   911  C  CD  . ARG A 1 128 ? 24.714  16.565  4.551   1.00 49.39 ? 175 ARG A CD  1 
ATOM   912  N  NE  . ARG A 1 128 ? 23.952  17.674  3.964   1.00 59.69 ? 175 ARG A NE  1 
ATOM   913  C  CZ  . ARG A 1 128 ? 23.404  17.705  2.746   1.00 67.45 ? 175 ARG A CZ  1 
ATOM   914  N  NH1 . ARG A 1 128 ? 22.518  18.643  2.449   1.00 67.57 ? 175 ARG A NH1 1 
ATOM   915  N  NH2 . ARG A 1 128 ? 23.687  16.776  1.846   1.00 70.11 ? 175 ARG A NH2 1 
ATOM   916  N  N   . ALA A 1 129 ? 22.501  14.341  9.562   1.00 26.73 ? 176 ALA A N   1 
ATOM   917  C  CA  . ALA A 1 129 ? 22.931  14.018  10.919  1.00 31.11 ? 176 ALA A CA  1 
ATOM   918  C  C   . ALA A 1 129 ? 22.689  12.544  11.218  1.00 31.27 ? 176 ALA A C   1 
ATOM   919  O  O   . ALA A 1 129 ? 23.351  11.982  12.094  1.00 39.50 ? 176 ALA A O   1 
ATOM   920  C  CB  . ALA A 1 129 ? 22.196  14.863  11.944  1.00 30.12 ? 176 ALA A CB  1 
ATOM   921  N  N   . ARG A 1 130 ? 21.695  11.953  10.548  1.00 24.43 ? 177 ARG A N   1 
ATOM   922  C  CA  . ARG A 1 130 ? 21.317  10.564  10.776  1.00 27.10 ? 177 ARG A CA  1 
ATOM   923  C  C   . ARG A 1 130 ? 21.637  9.738   9.527   1.00 20.73 ? 177 ARG A C   1 
ATOM   924  O  O   . ARG A 1 130 ? 20.960  8.768   9.209   1.00 24.23 ? 177 ARG A O   1 
ATOM   925  C  CB  . ARG A 1 130 ? 19.880  10.540  11.293  1.00 31.87 ? 177 ARG A CB  1 
ATOM   926  C  CG  . ARG A 1 130 ? 19.832  11.402  12.555  1.00 40.25 ? 177 ARG A CG  1 
ATOM   927  C  CD  . ARG A 1 130 ? 18.607  11.203  13.411  1.00 46.87 ? 177 ARG A CD  1 
ATOM   928  N  NE  . ARG A 1 130 ? 18.535  9.783   13.765  1.00 53.95 ? 177 ARG A NE  1 
ATOM   929  C  CZ  . ARG A 1 130 ? 17.455  9.144   14.188  1.00 51.13 ? 177 ARG A CZ  1 
ATOM   930  N  NH1 . ARG A 1 130 ? 16.329  9.813   14.382  1.00 49.97 ? 177 ARG A NH1 1 
ATOM   931  N  NH2 . ARG A 1 130 ? 17.531  7.846   14.440  1.00 46.20 ? 177 ARG A NH2 1 
ATOM   932  N  N   . SER A 1 131 ? 22.708  10.122  8.837   1.00 17.95 ? 178 SER A N   1 
ATOM   933  C  CA  . SER A 1 131 ? 23.211  9.456   7.656   1.00 17.08 ? 178 SER A CA  1 
ATOM   934  C  C   . SER A 1 131 ? 24.711  9.304   7.869   1.00 18.07 ? 178 SER A C   1 
ATOM   935  O  O   . SER A 1 131 ? 25.285  9.994   8.732   1.00 19.87 ? 178 SER A O   1 
ATOM   936  C  CB  . SER A 1 131 ? 22.900  10.229  6.403   1.00 19.48 ? 178 SER A CB  1 
ATOM   937  O  OG  . SER A 1 131 ? 21.495  10.283  6.204   1.00 19.81 ? 178 SER A OG  1 
ATOM   938  N  N   . GLY A 1 132 ? 25.315  8.469   7.040   1.00 17.61 ? 179 GLY A N   1 
ATOM   939  C  CA  . GLY A 1 132 ? 26.742  8.213   7.028   1.00 17.60 ? 179 GLY A CA  1 
ATOM   940  C  C   . GLY A 1 132 ? 27.257  7.646   8.338   1.00 17.82 ? 179 GLY A C   1 
ATOM   941  O  O   . GLY A 1 132 ? 26.549  6.962   9.063   1.00 19.40 ? 179 GLY A O   1 
ATOM   942  N  N   . GLY A 1 133 ? 28.541  7.880   8.584   1.00 17.48 ? 180 GLY A N   1 
ATOM   943  C  CA  . GLY A 1 133 ? 29.233  7.251   9.705   1.00 16.44 ? 180 GLY A CA  1 
ATOM   944  C  C   . GLY A 1 133 ? 30.521  6.577   9.259   1.00 15.89 ? 180 GLY A C   1 
ATOM   945  O  O   . GLY A 1 133 ? 30.563  5.897   8.265   1.00 18.36 ? 180 GLY A O   1 
ATOM   946  N  N   . ASP A 1 134 ? 31.597  6.749   10.040  1.00 15.88 ? 181 ASP A N   1 
ATOM   947  C  CA  . ASP A 1 134 ? 32.859  6.100   9.741   1.00 15.91 ? 181 ASP A CA  1 
ATOM   948  C  C   . ASP A 1 134 ? 32.762  4.590   9.966   1.00 13.99 ? 181 ASP A C   1 
ATOM   949  O  O   . ASP A 1 134 ? 33.491  3.815   9.335   1.00 16.34 ? 181 ASP A O   1 
ATOM   950  C  CB  . ASP A 1 134 ? 33.964  6.624   10.654  1.00 16.22 ? 181 ASP A CB  1 
ATOM   951  C  CG  . ASP A 1 134 ? 34.388  8.058   10.369  1.00 20.89 ? 181 ASP A CG  1 
ATOM   952  O  OD1 . ASP A 1 134 ? 34.208  8.487   9.227   1.00 23.17 ? 181 ASP A OD1 1 
ATOM   953  O  OD2 . ASP A 1 134 ? 34.756  8.751   11.336  1.00 20.75 ? 181 ASP A OD2 1 
ATOM   954  N  N   . LEU A 1 135 ? 31.968  4.172   10.946  1.00 14.84 ? 182 LEU A N   1 
ATOM   955  C  CA  . LEU A 1 135 ? 31.780  2.740   11.144  1.00 18.20 ? 182 LEU A CA  1 
ATOM   956  C  C   . LEU A 1 135 ? 30.428  2.453   11.776  1.00 14.65 ? 182 LEU A C   1 
ATOM   957  O  O   . LEU A 1 135 ? 29.722  3.347   12.217  1.00 16.92 ? 182 LEU A O   1 
ATOM   958  C  CB  . LEU A 1 135 ? 32.941  2.174   11.927  1.00 26.72 ? 182 LEU A CB  1 
ATOM   959  C  CG  . LEU A 1 135 ? 33.041  2.584   13.378  1.00 25.62 ? 182 LEU A CG  1 
ATOM   960  C  CD1 . LEU A 1 135 ? 32.451  1.526   14.289  1.00 29.52 ? 182 LEU A CD1 1 
ATOM   961  C  CD2 . LEU A 1 135 ? 34.499  2.783   13.722  1.00 34.31 ? 182 LEU A CD2 1 
ATOM   962  N  N   . CYS A 1 136 ? 30.033  1.177   11.736  1.00 13.76 ? 183 CYS A N   1 
ATOM   963  C  CA  . CYS A 1 136 ? 28.772  0.779   12.322  1.00 14.18 ? 183 CYS A CA  1 
ATOM   964  C  C   . CYS A 1 136 ? 28.957  -0.494  13.112  1.00 13.23 ? 183 CYS A C   1 
ATOM   965  O  O   . CYS A 1 136 ? 29.852  -1.271  12.882  1.00 14.16 ? 183 CYS A O   1 
ATOM   966  C  CB  . CYS A 1 136 ? 27.642  0.545   11.322  1.00 14.85 ? 183 CYS A CB  1 
ATOM   967  S  SG  . CYS A 1 136 ? 27.893  -0.848  10.229  1.00 17.16 ? 183 CYS A SG  1 
ATOM   968  N  N   . VAL A 1 137 ? 28.099  -0.639  14.107  1.00 14.44 ? 184 VAL A N   1 
ATOM   969  C  CA  . VAL A 1 137 ? 27.923  -1.903  14.781  1.00 13.86 ? 184 VAL A CA  1 
ATOM   970  C  C   . VAL A 1 137 ? 26.427  -2.185  14.728  1.00 12.93 ? 184 VAL A C   1 
ATOM   971  O  O   . VAL A 1 137 ? 25.606  -1.419  15.225  1.00 14.67 ? 184 VAL A O   1 
ATOM   972  C  CB  . VAL A 1 137 ? 28.488  -1.914  16.203  1.00 15.03 ? 184 VAL A CB  1 
ATOM   973  C  CG1 . VAL A 1 137 ? 28.148  -3.237  16.876  1.00 16.45 ? 184 VAL A CG1 1 
ATOM   974  C  CG2 . VAL A 1 137 ? 29.997  -1.640  16.184  1.00 16.11 ? 184 VAL A CG2 1 
ATOM   975  N  N   . GLN A 1 138 ? 26.088  -3.337  14.157  1.00 11.58 ? 185 GLN A N   1 
ATOM   976  C  CA  . GLN A 1 138 ? 24.741  -3.853  14.145  1.00 11.64 ? 185 GLN A CA  1 
ATOM   977  C  C   . GLN A 1 138 ? 24.641  -4.854  15.277  1.00 12.90 ? 185 GLN A C   1 
ATOM   978  O  O   . GLN A 1 138 ? 25.320  -5.888  15.251  1.00 13.84 ? 185 GLN A O   1 
ATOM   979  C  CB  . GLN A 1 138 ? 24.467  -4.589  12.837  1.00 12.45 ? 185 GLN A CB  1 
ATOM   980  C  CG  . GLN A 1 138 ? 23.085  -5.235  12.784  1.00 12.65 ? 185 GLN A CG  1 
ATOM   981  C  CD  . GLN A 1 138 ? 22.985  -6.121  11.569  1.00 13.32 ? 185 GLN A CD  1 
ATOM   982  O  OE1 . GLN A 1 138 ? 22.616  -5.664  10.465  1.00 15.02 ? 185 GLN A OE1 1 
ATOM   983  N  NE2 . GLN A 1 138 ? 23.316  -7.389  11.741  1.00 12.56 ? 185 GLN A NE2 1 
ATOM   984  N  N   . ALA A 1 139 ? 23.823  -4.557  16.271  1.00 11.57 ? 186 ALA A N   1 
ATOM   985  C  CA  . ALA A 1 139 ? 23.573  -5.506  17.355  1.00 11.77 ? 186 ALA A CA  1 
ATOM   986  C  C   . ALA A 1 139 ? 22.172  -6.062  17.208  1.00 12.53 ? 186 ALA A C   1 
ATOM   987  O  O   . ALA A 1 139 ? 21.186  -5.310  17.216  1.00 14.78 ? 186 ALA A O   1 
ATOM   988  C  CB  . ALA A 1 139 ? 23.742  -4.850  18.714  1.00 12.08 ? 186 ALA A CB  1 
ATOM   989  N  N   . CYS A 1 140 ? 22.051  -7.360  17.031  1.00 11.74 ? 187 CYS A N   1 
ATOM   990  C  CA  . CYS A 1 140 ? 20.760  -7.995  16.917  1.00 12.12 ? 187 CYS A CA  1 
ATOM   991  C  C   . CYS A 1 140 ? 20.668  -9.008  18.040  1.00 12.53 ? 187 CYS A C   1 
ATOM   992  O  O   . CYS A 1 140 ? 21.616  -9.739  18.267  1.00 13.68 ? 187 CYS A O   1 
ATOM   993  C  CB  . CYS A 1 140 ? 20.615  -8.740  15.604  1.00 12.80 ? 187 CYS A CB  1 
ATOM   994  S  SG  . CYS A 1 140 ? 20.597  -7.628  14.162  1.00 14.16 ? 187 CYS A SG  1 
ATOM   995  N  N   . ALA A 1 141 ? 19.511  -9.128  18.680  1.00 12.41 ? 188 ALA A N   1 
ATOM   996  C  CA  . ALA A 1 141 ? 19.320  -10.104 19.731  1.00 11.64 ? 188 ALA A CA  1 
ATOM   997  C  C   . ALA A 1 141 ? 17.836  -10.277 19.912  1.00 13.54 ? 188 ALA A C   1 
ATOM   998  O  O   . ALA A 1 141 ? 17.057  -9.453  19.456  1.00 13.71 ? 188 ALA A O   1 
ATOM   999  C  CB  . ALA A 1 141 ? 19.990  -9.652  21.000  1.00 12.93 ? 188 ALA A CB  1 
ATOM   1000 N  N   . ASP A 1 142 ? 17.441  -11.289 20.660  1.00 13.75 ? 189 ASP A N   1 
ATOM   1001 C  CA  . ASP A 1 142 ? 16.028  -11.440 20.920  1.00 14.26 ? 189 ASP A CA  1 
ATOM   1002 C  C   . ASP A 1 142 ? 15.589  -10.636 22.135  1.00 14.03 ? 189 ASP A C   1 
ATOM   1003 O  O   . ASP A 1 142 ? 14.390  -10.491 22.316  1.00 20.23 ? 189 ASP A O   1 
ATOM   1004 C  CB  . ASP A 1 142 ? 15.689  -12.889 21.119  1.00 15.56 ? 189 ASP A CB  1 
ATOM   1005 C  CG  . ASP A 1 142 ? 15.859  -13.713 19.861  1.00 17.15 ? 189 ASP A CG  1 
ATOM   1006 O  OD1 . ASP A 1 142 ? 15.580  -13.210 18.757  1.00 15.15 ? 189 ASP A OD1 1 
ATOM   1007 O  OD2 . ASP A 1 142 ? 16.249  -14.872 20.007  1.00 20.58 ? 189 ASP A OD2 1 
ATOM   1008 N  N   . ASP A 1 143 ? 16.535  -10.092 22.874  1.00 14.16 ? 190 ASP A N   1 
ATOM   1009 C  CA  . ASP A 1 143 ? 16.292  -9.332  24.071  1.00 14.12 ? 190 ASP A CA  1 
ATOM   1010 C  C   . ASP A 1 143 ? 16.838  -7.941  23.826  1.00 14.09 ? 190 ASP A C   1 
ATOM   1011 O  O   . ASP A 1 143 ? 18.042  -7.722  23.680  1.00 14.08 ? 190 ASP A O   1 
ATOM   1012 C  CB  . ASP A 1 143 ? 16.982  -10.013 25.242  1.00 14.64 ? 190 ASP A CB  1 
ATOM   1013 C  CG  . ASP A 1 143 ? 16.654  -9.391  26.595  1.00 17.01 ? 190 ASP A CG  1 
ATOM   1014 O  OD1 . ASP A 1 143 ? 16.575  -8.135  26.630  1.00 18.30 ? 190 ASP A OD1 1 
ATOM   1015 O  OD2 . ASP A 1 143 ? 16.584  -10.154 27.620  1.00 17.65 ? 190 ASP A OD2 1 
ATOM   1016 N  N   . PRO A 1 144 ? 15.992  -6.902  23.898  1.00 13.69 ? 191 PRO A N   1 
ATOM   1017 C  CA  . PRO A 1 144 ? 16.486  -5.545  23.672  1.00 14.35 ? 191 PRO A CA  1 
ATOM   1018 C  C   . PRO A 1 144 ? 17.508  -5.077  24.676  1.00 14.13 ? 191 PRO A C   1 
ATOM   1019 O  O   . PRO A 1 144 ? 18.384  -4.273  24.359  1.00 16.02 ? 191 PRO A O   1 
ATOM   1020 C  CB  . PRO A 1 144 ? 15.191  -4.695  23.733  1.00 17.00 ? 191 PRO A CB  1 
ATOM   1021 C  CG  . PRO A 1 144 ? 14.291  -5.476  24.657  1.00 16.13 ? 191 PRO A CG  1 
ATOM   1022 C  CD  . PRO A 1 144 ? 14.581  -6.942  24.317  1.00 15.70 ? 191 PRO A CD  1 
ATOM   1023 N  N   . GLN A 1 145 ? 17.433  -5.602  25.913  1.00 12.90 ? 192 GLN A N   1 
ATOM   1024 C  CA  . GLN A 1 145 ? 18.353  -5.178  26.939  1.00 13.66 ? 192 GLN A CA  1 
ATOM   1025 C  C   . GLN A 1 145 ? 19.755  -5.673  26.604  1.00 12.76 ? 192 GLN A C   1 
ATOM   1026 O  O   . GLN A 1 145 ? 20.756  -4.992  26.884  1.00 13.62 ? 192 GLN A O   1 
ATOM   1027 C  CB  . GLN A 1 145 ? 17.819  -5.558  28.322  1.00 14.63 ? 192 GLN A CB  1 
ATOM   1028 C  CG  . GLN A 1 145 ? 18.590  -4.887  29.436  1.00 16.89 ? 192 GLN A CG  1 
ATOM   1029 C  CD  . GLN A 1 145 ? 17.682  -4.623  30.614  1.00 16.86 ? 192 GLN A CD  1 
ATOM   1030 O  OE1 . GLN A 1 145 ? 16.472  -4.409  30.467  1.00 21.41 ? 192 GLN A OE1 1 
ATOM   1031 N  NE2 . GLN A 1 145 ? 18.257  -4.801  31.778  1.00 17.38 ? 192 GLN A NE2 1 
ATOM   1032 N  N   . VAL A 1 146 ? 19.810  -6.887  26.047  1.00 14.53 ? 193 VAL A N   1 
ATOM   1033 C  CA  . VAL A 1 146 ? 21.070  -7.485  25.666  1.00 13.62 ? 193 VAL A CA  1 
ATOM   1034 C  C   . VAL A 1 146 ? 21.680  -6.667  24.539  1.00 13.17 ? 193 VAL A C   1 
ATOM   1035 O  O   . VAL A 1 146 ? 22.886  -6.397  24.547  1.00 13.86 ? 193 VAL A O   1 
ATOM   1036 C  CB  . VAL A 1 146 ? 20.805  -8.933  25.260  1.00 14.11 ? 193 VAL A CB  1 
ATOM   1037 C  CG1 . VAL A 1 146 ? 22.018  -9.569  24.587  1.00 16.24 ? 193 VAL A CG1 1 
ATOM   1038 C  CG2 . VAL A 1 146 ? 20.466  -9.758  26.492  1.00 15.09 ? 193 VAL A CG2 1 
ATOM   1039 N  N   . ALA A 1 147 ? 20.847  -6.220  23.598  1.00 13.20 ? 194 ALA A N   1 
ATOM   1040 C  CA  . ALA A 1 147 ? 21.378  -5.426  22.499  1.00 13.36 ? 194 ALA A CA  1 
ATOM   1041 C  C   . ALA A 1 147 ? 21.863  -4.044  22.937  1.00 13.36 ? 194 ALA A C   1 
ATOM   1042 O  O   . ALA A 1 147 ? 22.960  -3.611  22.557  1.00 14.78 ? 194 ALA A O   1 
ATOM   1043 C  CB  . ALA A 1 147 ? 20.340  -5.310  21.401  1.00 14.33 ? 194 ALA A CB  1 
ATOM   1044 N  N   . VAL A 1 148 ? 21.094  -3.345  23.799  1.00 15.26 ? 195 VAL A N   1 
ATOM   1045 C  CA  . VAL A 1 148 ? 21.497  -2.031  24.285  1.00 16.67 ? 195 VAL A CA  1 
ATOM   1046 C  C   . VAL A 1 148 ? 22.792  -2.136  25.094  1.00 14.01 ? 195 VAL A C   1 
ATOM   1047 O  O   . VAL A 1 148 ? 23.712  -1.366  24.924  1.00 15.13 ? 195 VAL A O   1 
ATOM   1048 C  CB  . VAL A 1 148 ? 20.403  -1.338  25.117  1.00 19.63 ? 195 VAL A CB  1 
ATOM   1049 C  CG1 . VAL A 1 148 ? 20.925  -0.019  25.657  1.00 23.37 ? 195 VAL A CG1 1 
ATOM   1050 C  CG2 . VAL A 1 148 ? 19.165  -1.156  24.279  1.00 24.94 ? 195 VAL A CG2 1 
ATOM   1051 N  N   . HIS A 1 149 ? 22.905  -3.170  25.953  1.00 13.67 ? 196 HIS A N   1 
ATOM   1052 C  CA  . HIS A 1 149 ? 24.078  -3.399  26.761  1.00 14.17 ? 196 HIS A CA  1 
ATOM   1053 C  C   . HIS A 1 149 ? 25.303  -3.501  25.878  1.00 12.89 ? 196 HIS A C   1 
ATOM   1054 O  O   . HIS A 1 149 ? 26.380  -2.981  26.188  1.00 13.58 ? 196 HIS A O   1 
ATOM   1055 C  CB  . HIS A 1 149 ? 23.856  -4.650  27.623  1.00 14.56 ? 196 HIS A CB  1 
ATOM   1056 C  CG  . HIS A 1 149 ? 25.052  -5.043  28.402  1.00 14.44 ? 196 HIS A CG  1 
ATOM   1057 N  ND1 . HIS A 1 149 ? 25.820  -6.103  27.952  1.00 14.13 ? 196 HIS A ND1 1 
ATOM   1058 C  CD2 . HIS A 1 149 ? 25.584  -4.637  29.559  1.00 14.73 ? 196 HIS A CD2 1 
ATOM   1059 C  CE1 . HIS A 1 149 ? 26.802  -6.294  28.821  1.00 15.15 ? 196 HIS A CE1 1 
ATOM   1060 N  NE2 . HIS A 1 149 ? 26.689  -5.430  29.815  1.00 14.76 ? 196 HIS A NE2 1 
ATOM   1061 N  N   . ALA A 1 150 ? 25.160  -4.266  24.776  1.00 13.65 ? 197 ALA A N   1 
ATOM   1062 C  CA  . ALA A 1 150 ? 26.319  -4.485  23.915  1.00 13.30 ? 197 ALA A CA  1 
ATOM   1063 C  C   . ALA A 1 150 ? 26.796  -3.157  23.325  1.00 12.24 ? 197 ALA A C   1 
ATOM   1064 O  O   . ALA A 1 150 ? 27.980  -2.814  23.352  1.00 14.30 ? 197 ALA A O   1 
ATOM   1065 C  CB  . ALA A 1 150 ? 25.987  -5.485  22.871  1.00 14.10 ? 197 ALA A CB  1 
ATOM   1066 N  N   . ILE A 1 151 ? 25.870  -2.382  22.765  1.00 12.81 ? 198 ILE A N   1 
ATOM   1067 C  CA  . ILE A 1 151 ? 26.229  -1.104  22.162  1.00 13.27 ? 198 ILE A CA  1 
ATOM   1068 C  C   . ILE A 1 151 ? 26.799  -0.125  23.192  1.00 13.54 ? 198 ILE A C   1 
ATOM   1069 O  O   . ILE A 1 151 ? 27.827  0.516   22.962  1.00 15.39 ? 198 ILE A O   1 
ATOM   1070 C  CB  . ILE A 1 151 ? 25.030  -0.507  21.409  1.00 14.29 ? 198 ILE A CB  1 
ATOM   1071 C  CG1 . ILE A 1 151 ? 24.619  -1.344  20.196  1.00 17.18 ? 198 ILE A CG1 1 
ATOM   1072 C  CG2 . ILE A 1 151 ? 25.341  0.941   21.036  1.00 16.74 ? 198 ILE A CG2 1 
ATOM   1073 C  CD1 . ILE A 1 151 ? 25.663  -1.429  19.120  1.00 18.84 ? 198 ILE A CD1 1 
ATOM   1074 N  N   . ARG A 1 152 ? 26.146  -0.065  24.351  1.00 13.93 ? 199 ARG A N   1 
ATOM   1075 C  CA  . ARG A 1 152 ? 26.611  0.823   25.408  1.00 13.65 ? 199 ARG A CA  1 
ATOM   1076 C  C   . ARG A 1 152 ? 28.035  0.521   25.852  1.00 14.80 ? 199 ARG A C   1 
ATOM   1077 O  O   . ARG A 1 152 ? 28.850  1.414   26.079  1.00 15.63 ? 199 ARG A O   1 
ATOM   1078 C  CB  . ARG A 1 152 ? 25.635  0.676   26.561  1.00 14.13 ? 199 ARG A CB  1 
ATOM   1079 C  CG  . ARG A 1 152 ? 26.048  1.452   27.796  1.00 15.72 ? 199 ARG A CG  1 
ATOM   1080 C  CD  . ARG A 1 152 ? 25.125  1.057   28.841  1.00 16.33 ? 199 ARG A CD  1 
ATOM   1081 N  NE  . ARG A 1 152 ? 25.336  1.678   30.147  1.00 13.77 ? 199 ARG A NE  1 
ATOM   1082 C  CZ  . ARG A 1 152 ? 24.375  1.558   30.991  1.00 14.44 ? 199 ARG A CZ  1 
ATOM   1083 N  NH1 . ARG A 1 152 ? 23.274  0.862   30.710  1.00 16.15 ? 199 ARG A NH1 1 
ATOM   1084 N  NH2 . ARG A 1 152 ? 24.532  2.123   32.163  1.00 15.06 ? 199 ARG A NH2 1 
ATOM   1085 N  N   . ASN A 1 153 ? 28.362  -0.777  26.013  1.00 14.04 ? 200 ASN A N   1 
ATOM   1086 C  CA  . ASN A 1 153 ? 29.674  -1.160  26.476  1.00 13.90 ? 200 ASN A CA  1 
ATOM   1087 C  C   . ASN A 1 153 ? 30.726  -0.979  25.406  1.00 14.24 ? 200 ASN A C   1 
ATOM   1088 O  O   . ASN A 1 153 ? 31.827  -0.546  25.708  1.00 16.87 ? 200 ASN A O   1 
ATOM   1089 C  CB  . ASN A 1 153 ? 29.683  -2.556  27.074  1.00 14.25 ? 200 ASN A CB  1 
ATOM   1090 C  CG  . ASN A 1 153 ? 29.112  -2.528  28.472  1.00 15.71 ? 200 ASN A CG  1 
ATOM   1091 O  OD1 . ASN A 1 153 ? 29.869  -2.390  29.436  1.00 17.32 ? 200 ASN A OD1 1 
ATOM   1092 N  ND2 . ASN A 1 153 ? 27.796  -2.499  28.597  1.00 15.72 ? 200 ASN A ND2 1 
ATOM   1093 N  N   . LEU A 1 154 ? 30.392  -1.272  24.151  1.00 14.88 ? 201 LEU A N   1 
ATOM   1094 C  CA  . LEU A 1 154 ? 31.311  -0.932  23.080  1.00 14.61 ? 201 LEU A CA  1 
ATOM   1095 C  C   . LEU A 1 154 ? 31.595  0.578   23.064  1.00 14.62 ? 201 LEU A C   1 
ATOM   1096 O  O   . LEU A 1 154 ? 32.745  0.990   22.926  1.00 15.66 ? 201 LEU A O   1 
ATOM   1097 C  CB  . LEU A 1 154 ? 30.784  -1.462  21.758  1.00 16.28 ? 201 LEU A CB  1 
ATOM   1098 C  CG  . LEU A 1 154 ? 30.758  -2.987  21.623  1.00 18.38 ? 201 LEU A CG  1 
ATOM   1099 C  CD1 . LEU A 1 154 ? 30.109  -3.343  20.302  1.00 21.30 ? 201 LEU A CD1 1 
ATOM   1100 C  CD2 . LEU A 1 154 ? 32.143  -3.564  21.704  1.00 19.77 ? 201 LEU A CD2 1 
ATOM   1101 N  N   . ALA A 1 155 ? 30.573  1.412   23.126  1.00 15.60 ? 202 ALA A N   1 
ATOM   1102 C  CA  . ALA A 1 155 ? 30.812  2.849   23.075  1.00 16.10 ? 202 ALA A CA  1 
ATOM   1103 C  C   . ALA A 1 155 ? 31.690  3.313   24.228  1.00 17.77 ? 202 ALA A C   1 
ATOM   1104 O  O   . ALA A 1 155 ? 32.548  4.154   24.037  1.00 19.89 ? 202 ALA A O   1 
ATOM   1105 C  CB  . ALA A 1 155 ? 29.491  3.578   23.053  1.00 17.01 ? 202 ALA A CB  1 
ATOM   1106 N  N   . ARG A 1 156 ? 31.464  2.751   25.409  1.00 17.05 ? 203 ARG A N   1 
ATOM   1107 C  CA  . ARG A 1 156 ? 32.240  3.103   26.577  1.00 18.08 ? 203 ARG A CA  1 
ATOM   1108 C  C   . ARG A 1 156 ? 33.715  2.760   26.398  1.00 18.93 ? 203 ARG A C   1 
ATOM   1109 O  O   . ARG A 1 156 ? 34.597  3.587   26.662  1.00 19.99 ? 203 ARG A O   1 
ATOM   1110 C  CB  . ARG A 1 156 ? 31.572  2.453   27.779  1.00 18.26 ? 203 ARG A CB  1 
ATOM   1111 C  CG  . ARG A 1 156 ? 32.274  2.769   29.088  1.00 21.28 ? 203 ARG A CG  1 
ATOM   1112 C  CD  . ARG A 1 156 ? 31.404  2.230   30.199  1.00 20.90 ? 203 ARG A CD  1 
ATOM   1113 N  NE  . ARG A 1 156 ? 32.127  2.463   31.451  1.00 25.08 ? 203 ARG A NE  1 
ATOM   1114 C  CZ  . ARG A 1 156 ? 32.578  1.515   32.229  1.00 26.81 ? 203 ARG A CZ  1 
ATOM   1115 N  NH1 . ARG A 1 156 ? 32.481  0.262   31.863  1.00 26.09 ? 203 ARG A NH1 1 
ATOM   1116 N  NH2 . ARG A 1 156 ? 33.099  1.850   33.394  1.00 29.23 ? 203 ARG A NH2 1 
ATOM   1117 N  N   . ILE A 1 157 ? 33.986  1.531   25.954  1.00 18.17 ? 204 ILE A N   1 
ATOM   1118 C  CA  . ILE A 1 157 ? 35.343  1.096   25.688  1.00 20.10 ? 204 ILE A CA  1 
ATOM   1119 C  C   . ILE A 1 157 ? 36.009  2.051   24.693  1.00 20.12 ? 204 ILE A C   1 
ATOM   1120 O  O   . ILE A 1 157 ? 37.197  2.317   24.769  1.00 21.82 ? 204 ILE A O   1 
ATOM   1121 C  CB  . ILE A 1 157 ? 35.316  -0.357  25.187  1.00 20.61 ? 204 ILE A CB  1 
ATOM   1122 C  CG1 . ILE A 1 157 ? 34.975  -1.307  26.310  1.00 22.48 ? 204 ILE A CG1 1 
ATOM   1123 C  CG2 . ILE A 1 157 ? 36.633  -0.747  24.509  1.00 21.70 ? 204 ILE A CG2 1 
ATOM   1124 C  CD1 . ILE A 1 157 ? 34.612  -2.690  25.813  1.00 23.48 ? 204 ILE A CD1 1 
ATOM   1125 N  N   . GLY A 1 158 ? 35.235  2.538   23.716  1.00 18.78 ? 205 GLY A N   1 
ATOM   1126 C  CA  . GLY A 1 158 ? 35.736  3.389   22.649  1.00 21.14 ? 205 GLY A CA  1 
ATOM   1127 C  C   . GLY A 1 158 ? 35.871  4.874   23.003  1.00 22.72 ? 205 GLY A C   1 
ATOM   1128 O  O   . GLY A 1 158 ? 36.321  5.642   22.149  1.00 20.61 ? 205 GLY A O   1 
ATOM   1129 N  N   . PHE A 1 159 ? 35.473  5.261   24.221  1.00 22.78 ? 206 PHE A N   1 
ATOM   1130 C  CA  . PHE A 1 159 ? 35.505  6.667   24.631  1.00 26.43 ? 206 PHE A CA  1 
ATOM   1131 C  C   . PHE A 1 159 ? 36.878  7.266   24.330  1.00 24.98 ? 206 PHE A C   1 
ATOM   1132 O  O   . PHE A 1 159 ? 37.911  6.666   24.623  1.00 25.79 ? 206 PHE A O   1 
ATOM   1133 C  CB  . PHE A 1 159 ? 35.142  6.829   26.114  1.00 30.16 ? 206 PHE A CB  1 
ATOM   1134 C  CG  . PHE A 1 159 ? 35.209  8.273   26.608  1.00 37.77 ? 206 PHE A CG  1 
ATOM   1135 C  CD1 . PHE A 1 159 ? 34.125  9.134   26.444  1.00 43.36 ? 206 PHE A CD1 1 
ATOM   1136 C  CD2 . PHE A 1 159 ? 36.366  8.767   27.212  1.00 48.08 ? 206 PHE A CD2 1 
ATOM   1137 C  CE1 . PHE A 1 159 ? 34.196  10.451  26.881  1.00 49.30 ? 206 PHE A CE1 1 
ATOM   1138 C  CE2 . PHE A 1 159 ? 36.434  10.090  27.646  1.00 49.73 ? 206 PHE A CE2 1 
ATOM   1139 C  CZ  . PHE A 1 159 ? 35.351  10.926  27.480  1.00 48.44 ? 206 PHE A CZ  1 
ATOM   1140 N  N   . GLY A 1 160 ? 36.866  8.443   23.692  1.00 27.25 ? 207 GLY A N   1 
ATOM   1141 C  CA  . GLY A 1 160 ? 38.080  9.153   23.333  1.00 28.97 ? 207 GLY A CA  1 
ATOM   1142 C  C   . GLY A 1 160 ? 38.593  8.781   21.942  1.00 28.83 ? 207 GLY A C   1 
ATOM   1143 O  O   . GLY A 1 160 ? 39.462  9.465   21.404  1.00 30.37 ? 207 GLY A O   1 
ATOM   1144 N  N   . LYS A 1 161 ? 38.098  7.671   21.359  1.00 23.31 ? 208 LYS A N   1 
ATOM   1145 C  CA  . LYS A 1 161 ? 38.576  7.214   20.066  1.00 20.57 ? 208 LYS A CA  1 
ATOM   1146 C  C   . LYS A 1 161 ? 37.456  7.221   19.026  1.00 18.63 ? 208 LYS A C   1 
ATOM   1147 O  O   . LYS A 1 161 ? 37.719  7.361   17.837  1.00 20.54 ? 208 LYS A O   1 
ATOM   1148 C  CB  . LYS A 1 161 ? 39.215  5.821   20.162  1.00 23.83 ? 208 LYS A CB  1 
ATOM   1149 C  CG  . LYS A 1 161 ? 40.527  5.744   20.962  1.00 26.78 ? 208 LYS A CG  1 
ATOM   1150 C  CD  . LYS A 1 161 ? 41.055  4.323   21.062  1.00 29.41 ? 208 LYS A CD  1 
ATOM   1151 C  CE  . LYS A 1 161 ? 42.290  4.143   21.937  1.00 30.66 ? 208 LYS A CE  1 
ATOM   1152 N  NZ  . LYS A 1 161 ? 42.773  2.745   21.902  1.00 31.87 ? 208 LYS A NZ  1 
ATOM   1153 N  N   . VAL A 1 162 ? 36.228  7.036   19.500  1.00 19.44 ? 209 VAL A N   1 
ATOM   1154 C  CA  . VAL A 1 162 ? 35.053  7.020   18.642  1.00 18.94 ? 209 VAL A CA  1 
ATOM   1155 C  C   . VAL A 1 162 ? 33.928  7.695   19.404  1.00 18.67 ? 209 VAL A C   1 
ATOM   1156 O  O   . VAL A 1 162 ? 33.942  7.726   20.625  1.00 20.81 ? 209 VAL A O   1 
ATOM   1157 C  CB  . VAL A 1 162 ? 34.607  5.614   18.165  1.00 18.97 ? 209 VAL A CB  1 
ATOM   1158 C  CG1 . VAL A 1 162 ? 35.683  4.909   17.335  1.00 20.96 ? 209 VAL A CG1 1 
ATOM   1159 C  CG2 . VAL A 1 162 ? 34.131  4.718   19.293  1.00 21.19 ? 209 VAL A CG2 1 
ATOM   1160 N  N   . VAL A 1 163 ? 32.964  8.273   18.672  1.00 19.36 ? 210 VAL A N   1 
ATOM   1161 C  CA  . VAL A 1 163 ? 31.763  8.853   19.240  1.00 20.18 ? 210 VAL A CA  1 
ATOM   1162 C  C   . VAL A 1 163 ? 30.583  8.262   18.481  1.00 20.53 ? 210 VAL A C   1 
ATOM   1163 O  O   . VAL A 1 163 ? 30.719  7.986   17.322  1.00 20.05 ? 210 VAL A O   1 
ATOM   1164 C  CB  . VAL A 1 163 ? 31.680  10.398  19.157  1.00 23.63 ? 210 VAL A CB  1 
ATOM   1165 C  CG1 . VAL A 1 163 ? 32.625  11.086  20.135  1.00 30.05 ? 210 VAL A CG1 1 
ATOM   1166 C  CG2 . VAL A 1 163 ? 31.889  10.913  17.736  1.00 24.54 ? 210 VAL A CG2 1 
ATOM   1167 N  N   . VAL A 1 164 ? 29.417  8.182   19.096  1.00 20.15 ? 211 VAL A N   1 
ATOM   1168 C  CA  . VAL A 1 164 ? 28.246  7.749   18.370  1.00 20.49 ? 211 VAL A CA  1 
ATOM   1169 C  C   . VAL A 1 164 ? 27.746  8.913   17.548  1.00 20.89 ? 211 VAL A C   1 
ATOM   1170 O  O   . VAL A 1 164 ? 27.499  10.008  18.062  1.00 24.47 ? 211 VAL A O   1 
ATOM   1171 C  CB  . VAL A 1 164 ? 27.137  7.214   19.286  1.00 18.65 ? 211 VAL A CB  1 
ATOM   1172 C  CG1 . VAL A 1 164 ? 25.927  6.837   18.440  1.00 20.70 ? 211 VAL A CG1 1 
ATOM   1173 C  CG2 . VAL A 1 164 ? 27.669  6.042   20.114  1.00 22.31 ? 211 VAL A CG2 1 
ATOM   1174 N  N   . ARG A 1 165 ? 27.616  8.663   16.256  1.00 16.48 ? 212 ARG A N   1 
ATOM   1175 C  CA  . ARG A 1 165 ? 27.077  9.647   15.339  1.00 16.50 ? 212 ARG A CA  1 
ATOM   1176 C  C   . ARG A 1 165 ? 25.556  9.610   15.309  1.00 17.39 ? 212 ARG A C   1 
ATOM   1177 O  O   . ARG A 1 165 ? 24.881  10.625  15.442  1.00 20.39 ? 212 ARG A O   1 
ATOM   1178 C  CB  . ARG A 1 165 ? 27.624  9.392   13.939  1.00 17.54 ? 212 ARG A CB  1 
ATOM   1179 C  CG  . ARG A 1 165 ? 27.064  10.374  12.919  1.00 18.83 ? 212 ARG A CG  1 
ATOM   1180 C  CD  . ARG A 1 165 ? 27.634  10.066  11.542  1.00 19.35 ? 212 ARG A CD  1 
ATOM   1181 N  NE  . ARG A 1 165 ? 27.140  11.024  10.552  1.00 20.88 ? 212 ARG A NE  1 
ATOM   1182 C  CZ  . ARG A 1 165 ? 27.665  12.224  10.334  1.00 27.46 ? 212 ARG A CZ  1 
ATOM   1183 N  NH1 . ARG A 1 165 ? 28.814  12.560  10.895  1.00 27.72 ? 212 ARG A NH1 1 
ATOM   1184 N  NH2 . ARG A 1 165 ? 27.077  13.075  9.494   1.00 26.83 ? 212 ARG A NH2 1 
ATOM   1185 N  N   . TRP A 1 166 ? 24.983  8.421   15.126  1.00 17.47 ? 213 TRP A N   1 
ATOM   1186 C  CA  . TRP A 1 166 ? 23.546  8.243   15.197  1.00 16.25 ? 213 TRP A CA  1 
ATOM   1187 C  C   . TRP A 1 166 ? 23.247  6.786   15.542  1.00 16.68 ? 213 TRP A C   1 
ATOM   1188 O  O   . TRP A 1 166 ? 24.091  5.943   15.391  1.00 16.40 ? 213 TRP A O   1 
ATOM   1189 C  CB  . TRP A 1 166 ? 22.841  8.665   13.886  1.00 16.61 ? 213 TRP A CB  1 
ATOM   1190 C  CG  . TRP A 1 166 ? 23.276  7.948   12.641  1.00 16.37 ? 213 TRP A CG  1 
ATOM   1191 C  CD1 . TRP A 1 166 ? 24.222  8.368   11.749  1.00 16.90 ? 213 TRP A CD1 1 
ATOM   1192 C  CD2 . TRP A 1 166 ? 22.772  6.699   12.124  1.00 16.65 ? 213 TRP A CD2 1 
ATOM   1193 N  NE1 . TRP A 1 166 ? 24.373  7.472   10.736  1.00 16.83 ? 213 TRP A NE1 1 
ATOM   1194 C  CE2 . TRP A 1 166 ? 23.481  6.445   10.931  1.00 17.41 ? 213 TRP A CE2 1 
ATOM   1195 C  CE3 . TRP A 1 166 ? 21.813  5.782   12.567  1.00 17.88 ? 213 TRP A CE3 1 
ATOM   1196 C  CZ2 . TRP A 1 166 ? 23.264  5.290   10.191  1.00 17.81 ? 213 TRP A CZ2 1 
ATOM   1197 C  CZ3 . TRP A 1 166 ? 21.597  4.646   11.815  1.00 19.87 ? 213 TRP A CZ3 1 
ATOM   1198 C  CH2 . TRP A 1 166 ? 22.308  4.423   10.644  1.00 18.72 ? 213 TRP A CH2 1 
ATOM   1199 N  N   . SER A 1 167 ? 22.049  6.520   16.018  1.00 15.32 ? 214 SER A N   1 
ATOM   1200 C  CA  . SER A 1 167 ? 21.656  5.161   16.317  1.00 17.56 ? 214 SER A CA  1 
ATOM   1201 C  C   . SER A 1 167 ? 20.210  4.960   15.893  1.00 18.67 ? 214 SER A C   1 
ATOM   1202 O  O   . SER A 1 167 ? 19.475  5.918   15.625  1.00 18.05 ? 214 SER A O   1 
ATOM   1203 C  CB  . SER A 1 167 ? 21.902  4.830   17.751  1.00 22.13 ? 214 SER A CB  1 
ATOM   1204 O  OG  . SER A 1 167 ? 21.006  5.538   18.571  1.00 25.43 ? 214 SER A OG  1 
ATOM   1205 N  N   . GLN A 1 168 ? 19.811  3.694   15.778  1.00 15.89 ? 215 GLN A N   1 
ATOM   1206 C  CA  . GLN A 1 168 ? 18.453  3.366   15.432  1.00 16.01 ? 215 GLN A CA  1 
ATOM   1207 C  C   . GLN A 1 168 ? 18.117  2.064   16.132  1.00 15.38 ? 215 GLN A C   1 
ATOM   1208 O  O   . GLN A 1 168 ? 18.842  1.061   16.015  1.00 16.06 ? 215 GLN A O   1 
ATOM   1209 C  CB  . GLN A 1 168 ? 18.280  3.128   13.930  1.00 17.13 ? 215 GLN A CB  1 
ATOM   1210 C  CG  . GLN A 1 168 ? 16.849  2.811   13.531  1.00 18.62 ? 215 GLN A CG  1 
ATOM   1211 C  CD  . GLN A 1 168 ? 15.871  3.944   13.752  1.00 20.29 ? 215 GLN A CD  1 
ATOM   1212 O  OE1 . GLN A 1 168 ? 16.069  5.052   13.220  1.00 22.60 ? 215 GLN A OE1 1 
ATOM   1213 N  NE2 . GLN A 1 168 ? 14.892  3.734   14.612  1.00 19.68 ? 215 GLN A NE2 1 
ATOM   1214 N  N   . LEU A 1 169 ? 17.055  2.077   16.886  1.00 14.21 ? 216 LEU A N   1 
ATOM   1215 C  CA  . LEU A 1 169 ? 16.509  0.868   17.462  1.00 16.18 ? 216 LEU A CA  1 
ATOM   1216 C  C   . LEU A 1 169 ? 15.364  0.352   16.604  1.00 16.00 ? 216 LEU A C   1 
ATOM   1217 O  O   . LEU A 1 169 ? 14.585  1.154   16.066  1.00 16.87 ? 216 LEU A O   1 
ATOM   1218 C  CB  . LEU A 1 169 ? 16.068  1.075   18.898  1.00 19.52 ? 216 LEU A CB  1 
ATOM   1219 C  CG  . LEU A 1 169 ? 17.252  1.046   19.877  1.00 22.81 ? 216 LEU A CG  1 
ATOM   1220 C  CD1 . LEU A 1 169 ? 17.918  2.413   19.970  1.00 25.03 ? 216 LEU A CD1 1 
ATOM   1221 C  CD2 . LEU A 1 169 ? 16.863  0.523   21.239  1.00 26.99 ? 216 LEU A CD2 1 
ATOM   1222 N  N   . GLY A 1 170 ? 15.297  -0.966  16.445  1.00 13.24 ? 217 GLY A N   1 
ATOM   1223 C  CA  . GLY A 1 170 ? 14.234  -1.662  15.758  1.00 13.32 ? 217 GLY A CA  1 
ATOM   1224 C  C   . GLY A 1 170 ? 13.490  -2.561  16.721  1.00 14.01 ? 217 GLY A C   1 
ATOM   1225 O  O   . GLY A 1 170 ? 14.089  -3.416  17.364  1.00 15.33 ? 217 GLY A O   1 
ATOM   1226 N  N   . PHE A 1 171 ? 12.181  -2.344  16.864  1.00 12.42 ? 218 PHE A N   1 
ATOM   1227 C  CA  . PHE A 1 171 ? 11.417  -3.043  17.883  1.00 12.36 ? 218 PHE A CA  1 
ATOM   1228 C  C   . PHE A 1 171 ? 11.012  -4.425  17.437  1.00 13.43 ? 218 PHE A C   1 
ATOM   1229 O  O   . PHE A 1 171 ? 10.729  -5.279  18.278  1.00 15.06 ? 218 PHE A O   1 
ATOM   1230 C  CB  . PHE A 1 171 ? 10.213  -2.270  18.419  1.00 12.62 ? 218 PHE A CB  1 
ATOM   1231 C  CG  . PHE A 1 171 ? 9.083   -2.097  17.428  1.00 13.53 ? 218 PHE A CG  1 
ATOM   1232 C  CD1 . PHE A 1 171 ? 8.230   -3.137  17.171  1.00 14.17 ? 218 PHE A CD1 1 
ATOM   1233 C  CD2 . PHE A 1 171 ? 8.915   -0.926  16.742  1.00 15.25 ? 218 PHE A CD2 1 
ATOM   1234 C  CE1 . PHE A 1 171 ? 7.217   -3.023  16.236  1.00 14.01 ? 218 PHE A CE1 1 
ATOM   1235 C  CE2 . PHE A 1 171 ? 7.876   -0.779  15.848  1.00 14.85 ? 218 PHE A CE2 1 
ATOM   1236 C  CZ  . PHE A 1 171 ? 7.045   -1.818  15.585  1.00 14.76 ? 218 PHE A CZ  1 
ATOM   1237 N  N   . GLY A 1 172 ? 11.005  -4.663  16.139  1.00 12.67 ? 219 GLY A N   1 
ATOM   1238 C  CA  . GLY A 1 172 ? 10.606  -5.945  15.611  1.00 12.98 ? 219 GLY A CA  1 
ATOM   1239 C  C   . GLY A 1 172 ? 11.123  -6.082  14.191  1.00 13.57 ? 219 GLY A C   1 
ATOM   1240 O  O   . GLY A 1 172 ? 11.310  -5.106  13.468  1.00 13.48 ? 219 GLY A O   1 
ATOM   1241 N  N   . LYS A 1 173 ? 11.353  -7.319  13.815  1.00 13.05 ? 220 LYS A N   1 
ATOM   1242 C  CA  . LYS A 1 173 ? 11.957  -7.633  12.534  1.00 13.27 ? 220 LYS A CA  1 
ATOM   1243 C  C   . LYS A 1 173 ? 10.915  -7.529  11.433  1.00 13.02 ? 220 LYS A C   1 
ATOM   1244 O  O   . LYS A 1 173 ? 9.716   -7.785  11.645  1.00 15.19 ? 220 LYS A O   1 
ATOM   1245 C  CB  . LYS A 1 173 ? 12.554  -9.039  12.587  1.00 13.30 ? 220 LYS A CB  1 
ATOM   1246 C  CG  . LYS A 1 173 ? 11.536  -10.163 12.738  1.00 15.32 ? 220 LYS A CG  1 
ATOM   1247 C  CD  . LYS A 1 173 ? 12.216  -11.504 13.031  1.00 18.01 ? 220 LYS A CD  1 
ATOM   1248 C  CE  . LYS A 1 173 ? 11.284  -12.600 13.291  1.00 20.49 ? 220 LYS A CE  1 
ATOM   1249 N  NZ  . LYS A 1 173 ? 12.044  -13.855 13.421  1.00 23.30 ? 220 LYS A NZ  1 
ATOM   1250 N  N   . THR A 1 174 ? 11.405  -7.203  10.239  1.00 12.06 ? 221 THR A N   1 
ATOM   1251 C  CA  A THR A 1 174 ? 10.548  -7.268  9.071   0.50 12.81 ? 221 THR A CA  1 
ATOM   1252 C  CA  B THR A 1 174 ? 10.613  -7.154  9.016   0.50 12.20 ? 221 THR A CA  1 
ATOM   1253 C  C   . THR A 1 174 ? 11.335  -7.918  7.927   1.00 12.95 ? 221 THR A C   1 
ATOM   1254 O  O   . THR A 1 174 ? 11.310  -7.485  6.790   1.00 14.64 ? 221 THR A O   1 
ATOM   1255 C  CB  A THR A 1 174 ? 10.008  -5.846  8.860   0.50 13.85 ? 221 THR A CB  1 
ATOM   1256 C  CB  B THR A 1 174 ? 10.371  -5.731  8.484   0.50 11.58 ? 221 THR A CB  1 
ATOM   1257 O  OG1 A THR A 1 174 ? 9.052   -5.950  7.815   0.50 14.92 ? 221 THR A OG1 1 
ATOM   1258 O  OG1 B THR A 1 174 ? 11.568  -5.036  8.137   0.50 12.18 ? 221 THR A OG1 1 
ATOM   1259 C  CG2 A THR A 1 174 ? 11.099  -4.829  8.615   0.50 12.51 ? 221 THR A CG2 1 
ATOM   1260 C  CG2 B THR A 1 174 ? 9.518   -4.968  9.470   0.50 11.97 ? 221 THR A CG2 1 
ATOM   1261 N  N   . SER A 1 175 ? 12.002  -9.001  8.295   1.00 11.78 ? 222 SER A N   1 
ATOM   1262 C  CA  . SER A 1 175 ? 12.840  -9.720  7.362   1.00 11.54 ? 222 SER A CA  1 
ATOM   1263 C  C   . SER A 1 175 ? 12.912  -11.168 7.802   1.00 11.91 ? 222 SER A C   1 
ATOM   1264 O  O   . SER A 1 175 ? 12.605  -11.504 8.947   1.00 13.35 ? 222 SER A O   1 
ATOM   1265 C  CB  . SER A 1 175 ? 14.177  -9.086  7.260   1.00 12.12 ? 222 SER A CB  1 
ATOM   1266 O  OG  . SER A 1 175 ? 14.724  -8.890  8.558   1.00 12.59 ? 222 SER A OG  1 
ATOM   1267 N  N   . SER A 1 176 ? 13.418  -12.005 6.901   1.00 11.71 ? 223 SER A N   1 
ATOM   1268 C  CA  . SER A 1 176 ? 13.524  -13.431 7.152   1.00 12.56 ? 223 SER A CA  1 
ATOM   1269 C  C   . SER A 1 176 ? 14.695  -14.005 6.389   1.00 12.43 ? 223 SER A C   1 
ATOM   1270 O  O   . SER A 1 176 ? 14.762  -13.806 5.177   1.00 13.73 ? 223 SER A O   1 
ATOM   1271 C  CB  . SER A 1 176 ? 12.294  -14.146 6.751   1.00 13.86 ? 223 SER A CB  1 
ATOM   1272 O  OG  . SER A 1 176 ? 12.468  -15.551 6.923   1.00 15.05 ? 223 SER A OG  1 
ATOM   1273 N  N   . THR A 1 177 ? 15.534  -14.802 7.066   1.00 12.23 ? 224 THR A N   1 
ATOM   1274 C  CA  . THR A 1 177 ? 16.517  -15.666 6.422   1.00 12.55 ? 224 THR A CA  1 
ATOM   1275 C  C   . THR A 1 177 ? 16.155  -17.127 6.680   1.00 14.96 ? 224 THR A C   1 
ATOM   1276 O  O   . THR A 1 177 ? 17.029  -17.977 6.528   1.00 15.06 ? 224 THR A O   1 
ATOM   1277 C  CB  . THR A 1 177 ? 17.912  -15.312 6.935   1.00 13.33 ? 224 THR A CB  1 
ATOM   1278 O  OG1 . THR A 1 177 ? 17.918  -15.448 8.342   1.00 13.76 ? 224 THR A OG1 1 
ATOM   1279 C  CG2 . THR A 1 177 ? 18.294  -13.896 6.536   1.00 14.24 ? 224 THR A CG2 1 
ATOM   1280 N  N   . THR A 1 178 ? 14.922  -17.382 7.131   1.00 13.49 ? 225 THR A N   1 
ATOM   1281 C  CA  . THR A 1 178 ? 14.494  -18.726 7.544   1.00 14.68 ? 225 THR A CA  1 
ATOM   1282 C  C   . THR A 1 178 ? 13.112  -18.961 6.955   1.00 15.63 ? 225 THR A C   1 
ATOM   1283 O  O   . THR A 1 178 ? 12.117  -18.732 7.626   1.00 17.31 ? 225 THR A O   1 
ATOM   1284 C  CB  . THR A 1 178 ? 14.513  -18.871 9.052   1.00 16.29 ? 225 THR A CB  1 
ATOM   1285 O  OG1 . THR A 1 178 ? 13.701  -17.832 9.602   1.00 16.16 ? 225 THR A OG1 1 
ATOM   1286 C  CG2 . THR A 1 178 ? 15.916  -18.793 9.622   1.00 16.83 ? 225 THR A CG2 1 
ATOM   1287 N  N   . PRO A 1 179 ? 13.025  -19.435 5.701   1.00 17.19 ? 226 PRO A N   1 
ATOM   1288 C  CA  . PRO A 1 179 ? 11.730  -19.633 5.055   1.00 19.73 ? 226 PRO A CA  1 
ATOM   1289 C  C   . PRO A 1 179 ? 10.875  -20.722 5.702   1.00 21.06 ? 226 PRO A C   1 
ATOM   1290 O  O   . PRO A 1 179 ? 9.680   -20.759 5.442   1.00 26.15 ? 226 PRO A O   1 
ATOM   1291 C  CB  . PRO A 1 179 ? 12.072  -19.951 3.606   1.00 22.49 ? 226 PRO A CB  1 
ATOM   1292 C  CG  . PRO A 1 179 ? 13.509  -20.438 3.652   1.00 21.99 ? 226 PRO A CG  1 
ATOM   1293 C  CD  . PRO A 1 179 ? 14.169  -19.724 4.812   1.00 19.72 ? 226 PRO A CD  1 
ATOM   1294 N  N   . ASP A 1 180 ? 11.470  -21.545 6.573   1.00 21.68 ? 227 ASP A N   1 
ATOM   1295 C  CA  . ASP A 1 180 ? 10.722  -22.581 7.279   1.00 25.26 ? 227 ASP A CA  1 
ATOM   1296 C  C   . ASP A 1 180 ? 9.868   -21.981 8.395   1.00 25.44 ? 227 ASP A C   1 
ATOM   1297 O  O   . ASP A 1 180 ? 9.040   -22.668 8.976   1.00 26.69 ? 227 ASP A O   1 
ATOM   1298 C  CB  . ASP A 1 180 ? 11.637  -23.681 7.804   1.00 25.21 ? 227 ASP A CB  1 
ATOM   1299 C  CG  . ASP A 1 180 ? 12.809  -23.193 8.647   1.00 33.41 ? 227 ASP A CG  1 
ATOM   1300 O  OD1 . ASP A 1 180 ? 13.511  -22.247 8.189   1.00 36.90 ? 227 ASP A OD1 1 
ATOM   1301 O  OD2 . ASP A 1 180 ? 13.035  -23.777 9.727   1.00 38.49 ? 227 ASP A OD2 1 
ATOM   1302 N  N   . LYS A 1 181 ? 10.111  -20.718 8.759   1.00 19.93 ? 228 LYS A N   1 
ATOM   1303 C  CA  . LYS A 1 181 ? 9.465   -20.069 9.876   1.00 21.46 ? 228 LYS A CA  1 
ATOM   1304 C  C   . LYS A 1 181 ? 8.544   -18.982 9.334   1.00 18.57 ? 228 LYS A C   1 
ATOM   1305 O  O   . LYS A 1 181 ? 8.662   -18.604 8.171   1.00 18.01 ? 228 LYS A O   1 
ATOM   1306 C  CB  . LYS A 1 181 ? 10.480  -19.398 10.805  1.00 25.63 ? 228 LYS A CB  1 
ATOM   1307 C  CG  . LYS A 1 181 ? 11.172  -20.262 11.861  1.00 36.38 ? 228 LYS A CG  1 
ATOM   1308 C  CD  . LYS A 1 181 ? 11.783  -21.577 11.417  1.00 45.83 ? 228 LYS A CD  1 
ATOM   1309 C  CE  . LYS A 1 181 ? 12.260  -22.342 12.624  1.00 49.19 ? 228 LYS A CE  1 
ATOM   1310 N  NZ  . LYS A 1 181 ? 12.880  -23.615 12.250  1.00 56.74 ? 228 LYS A NZ  1 
ATOM   1311 N  N   . GLN A 1 182 ? 7.625   -18.532 10.189  1.00 18.25 ? 229 GLN A N   1 
ATOM   1312 C  CA  . GLN A 1 182 ? 6.615   -17.562 9.773   1.00 17.44 ? 229 GLN A CA  1 
ATOM   1313 C  C   . GLN A 1 182 ? 7.298   -16.277 9.332   1.00 16.11 ? 229 GLN A C   1 
ATOM   1314 O  O   . GLN A 1 182 ? 8.208   -15.770 9.961   1.00 16.89 ? 229 GLN A O   1 
ATOM   1315 C  CB  . GLN A 1 182 ? 5.684   -17.198 10.920  1.00 22.54 ? 229 GLN A CB  1 
ATOM   1316 C  CG  . GLN A 1 182 ? 4.541   -16.255 10.566  1.00 28.41 ? 229 GLN A CG  1 
ATOM   1317 C  CD  . GLN A 1 182 ? 3.497   -16.115 11.667  1.00 37.37 ? 229 GLN A CD  1 
ATOM   1318 O  OE1 . GLN A 1 182 ? 3.565   -15.227 12.529  1.00 43.61 ? 229 GLN A OE1 1 
ATOM   1319 N  NE2 . GLN A 1 182 ? 2.529   -17.016 11.673  1.00 42.48 ? 229 GLN A NE2 1 
ATOM   1320 N  N   . THR A 1 183 ? 6.808   -15.720 8.246   1.00 13.12 ? 230 THR A N   1 
ATOM   1321 C  CA  . THR A 1 183 ? 7.342   -14.461 7.725   1.00 12.66 ? 230 THR A CA  1 
ATOM   1322 C  C   . THR A 1 183 ? 6.718   -13.314 8.528   1.00 12.07 ? 230 THR A C   1 
ATOM   1323 O  O   . THR A 1 183 ? 5.493   -13.295 8.664   1.00 13.34 ? 230 THR A O   1 
ATOM   1324 C  CB  . THR A 1 183 ? 6.999   -14.320 6.251   1.00 12.55 ? 230 THR A CB  1 
ATOM   1325 O  OG1 . THR A 1 183 ? 7.452   -15.495 5.600   1.00 13.52 ? 230 THR A OG1 1 
ATOM   1326 C  CG2 . THR A 1 183 ? 7.620   -13.085 5.642   1.00 13.28 ? 230 THR A CG2 1 
ATOM   1327 N  N   . PRO A 1 184 ? 7.517   -12.374 9.059   1.00 12.06 ? 231 PRO A N   1 
ATOM   1328 C  CA  . PRO A 1 184 ? 6.979   -11.270 9.844   1.00 12.06 ? 231 PRO A CA  1 
ATOM   1329 C  C   . PRO A 1 184 ? 6.315   -10.226 8.969   1.00 12.11 ? 231 PRO A C   1 
ATOM   1330 O  O   . PRO A 1 184 ? 6.534   -10.190 7.768   1.00 13.46 ? 231 PRO A O   1 
ATOM   1331 C  CB  . PRO A 1 184 ? 8.230   -10.721 10.538  1.00 12.43 ? 231 PRO A CB  1 
ATOM   1332 C  CG  . PRO A 1 184 ? 9.313   -10.946 9.552   1.00 14.77 ? 231 PRO A CG  1 
ATOM   1333 C  CD  . PRO A 1 184 ? 8.981   -12.282 8.935   1.00 12.30 ? 231 PRO A CD  1 
ATOM   1334 N  N   . ARG A 1 185 ? 5.450   -9.430  9.576   1.00 10.89 ? 232 ARG A N   1 
ATOM   1335 C  CA  . ARG A 1 185 ? 4.796   -8.335  8.878   1.00 11.52 ? 232 ARG A CA  1 
ATOM   1336 C  C   . ARG A 1 185 ? 5.408   -6.992  9.257   1.00 11.19 ? 232 ARG A C   1 
ATOM   1337 O  O   . ARG A 1 185 ? 5.779   -6.730  10.403  1.00 12.08 ? 232 ARG A O   1 
ATOM   1338 C  CB  . ARG A 1 185 ? 3.323   -8.289  9.232   1.00 12.18 ? 232 ARG A CB  1 
ATOM   1339 C  CG  . ARG A 1 185 ? 2.629   -9.525  8.656   1.00 12.70 ? 232 ARG A CG  1 
ATOM   1340 C  CD  . ARG A 1 185 ? 1.157   -9.521  8.910   1.00 14.10 ? 232 ARG A CD  1 
ATOM   1341 N  NE  . ARG A 1 185 ? 0.558   -10.785 8.516   1.00 15.12 ? 232 ARG A NE  1 
ATOM   1342 C  CZ  . ARG A 1 185 ? -0.134  -10.966 7.422   1.00 14.70 ? 232 ARG A CZ  1 
ATOM   1343 N  NH1 . ARG A 1 185 ? -0.320  -9.993  6.553   1.00 14.66 ? 232 ARG A NH1 1 
ATOM   1344 N  NH2 . ARG A 1 185 ? -0.617  -12.186 7.150   1.00 15.63 ? 232 ARG A NH2 1 
ATOM   1345 N  N   . ASN A 1 186 ? 5.483   -6.109  8.280   1.00 10.77 ? 233 ASN A N   1 
ATOM   1346 C  CA  . ASN A 1 186 ? 5.857   -4.710  8.509   1.00 10.99 ? 233 ASN A CA  1 
ATOM   1347 C  C   . ASN A 1 186 ? 4.619   -3.924  8.994   1.00 12.06 ? 233 ASN A C   1 
ATOM   1348 O  O   . ASN A 1 186 ? 3.526   -4.475  9.108   1.00 11.06 ? 233 ASN A O   1 
ATOM   1349 C  CB  . ASN A 1 186 ? 6.490   -4.106  7.269   1.00 12.12 ? 233 ASN A CB  1 
ATOM   1350 C  CG  . ASN A 1 186 ? 5.589   -4.204  6.079   1.00 12.63 ? 233 ASN A CG  1 
ATOM   1351 O  OD1 . ASN A 1 186 ? 4.393   -3.858  6.161   1.00 12.54 ? 233 ASN A OD1 1 
ATOM   1352 N  ND2 . ASN A 1 186 ? 6.167   -4.628  4.960   1.00 13.70 ? 233 ASN A ND2 1 
ATOM   1353 N  N   . LEU A 1 187 ? 4.804   -2.628  9.261   1.00 11.29 ? 234 LEU A N   1 
ATOM   1354 C  CA  . LEU A 1 187 ? 3.727   -1.819  9.805   1.00 11.56 ? 234 LEU A CA  1 
ATOM   1355 C  C   . LEU A 1 187 ? 2.682   -1.406  8.786   1.00 13.08 ? 234 LEU A C   1 
ATOM   1356 O  O   . LEU A 1 187 ? 1.638   -0.900  9.181   1.00 14.35 ? 234 LEU A O   1 
ATOM   1357 C  CB  . LEU A 1 187 ? 4.311   -0.587  10.502  1.00 12.39 ? 234 LEU A CB  1 
ATOM   1358 C  CG  . LEU A 1 187 ? 5.024   -0.918  11.812  1.00 14.84 ? 234 LEU A CG  1 
ATOM   1359 C  CD1 . LEU A 1 187 ? 5.698   0.367   12.309  1.00 15.97 ? 234 LEU A CD1 1 
ATOM   1360 C  CD2 . LEU A 1 187 ? 4.063   -1.530  12.824  1.00 18.44 ? 234 LEU A CD2 1 
ATOM   1361 N  N   . LEU A 1 188 ? 2.868   -1.739  7.525   1.00 11.06 ? 235 LEU A N   1 
ATOM   1362 C  CA  . LEU A 1 188 ? 1.789   -1.623  6.548   1.00 11.31 ? 235 LEU A CA  1 
ATOM   1363 C  C   . LEU A 1 188 ? 0.916   -2.867  6.552   1.00 11.95 ? 235 LEU A C   1 
ATOM   1364 O  O   . LEU A 1 188 ? -0.079  -2.914  5.840   1.00 14.21 ? 235 LEU A O   1 
ATOM   1365 C  CB  . LEU A 1 188 ? 2.342   -1.373  5.158   1.00 12.09 ? 235 LEU A CB  1 
ATOM   1366 C  CG  . LEU A 1 188 ? 3.256   -0.171  4.994   1.00 12.84 ? 235 LEU A CG  1 
ATOM   1367 C  CD1 . LEU A 1 188 ? 3.654   0.014   3.532   1.00 15.08 ? 235 LEU A CD1 1 
ATOM   1368 C  CD2 . LEU A 1 188 ? 2.616   1.100   5.551   1.00 14.31 ? 235 LEU A CD2 1 
ATOM   1369 N  N   . GLY A 1 189 ? 1.257   -3.884  7.331   1.00 11.47 ? 236 GLY A N   1 
ATOM   1370 C  CA  . GLY A 1 189 ? 0.438   -5.054  7.496   1.00 11.18 ? 236 GLY A CA  1 
ATOM   1371 C  C   . GLY A 1 189 ? 0.729   -6.199  6.537   1.00 11.05 ? 236 GLY A C   1 
ATOM   1372 O  O   . GLY A 1 189 ? -0.008  -7.174  6.560   1.00 13.22 ? 236 GLY A O   1 
ATOM   1373 N  N   . PHE A 1 190 ? 1.759   -6.067  5.724   1.00 10.56 ? 237 PHE A N   1 
ATOM   1374 C  CA  . PHE A 1 190 ? 2.131   -7.109  4.778   1.00 10.80 ? 237 PHE A CA  1 
ATOM   1375 C  C   . PHE A 1 190 ? 3.321   -7.902  5.282   1.00 11.65 ? 237 PHE A C   1 
ATOM   1376 O  O   . PHE A 1 190 ? 4.243   -7.355  5.863   1.00 12.07 ? 237 PHE A O   1 
ATOM   1377 C  CB  . PHE A 1 190 ? 2.484   -6.474  3.440   1.00 10.77 ? 237 PHE A CB  1 
ATOM   1378 C  CG  . PHE A 1 190 ? 1.282   -6.134  2.598   1.00 12.21 ? 237 PHE A CG  1 
ATOM   1379 C  CD1 . PHE A 1 190 ? 0.461   -5.055  2.906   1.00 12.75 ? 237 PHE A CD1 1 
ATOM   1380 C  CD2 . PHE A 1 190 ? 0.919   -6.942  1.522   1.00 13.69 ? 237 PHE A CD2 1 
ATOM   1381 C  CE1 . PHE A 1 190 ? -0.646  -4.758  2.125   1.00 13.03 ? 237 PHE A CE1 1 
ATOM   1382 C  CE2 . PHE A 1 190 ? -0.211  -6.655  0.786   1.00 13.28 ? 237 PHE A CE2 1 
ATOM   1383 C  CZ  . PHE A 1 190 ? -1.003  -5.596  1.084   1.00 13.54 ? 237 PHE A CZ  1 
ATOM   1384 N  N   . LYS A 1 191 ? 3.326   -9.194  4.957   1.00 10.44 ? 238 LYS A N   1 
ATOM   1385 C  CA  . LYS A 1 191 ? 4.463   -10.040 5.179   1.00 10.64 ? 238 LYS A CA  1 
ATOM   1386 C  C   . LYS A 1 191 ? 5.649   -9.512  4.377   1.00 11.10 ? 238 LYS A C   1 
ATOM   1387 O  O   . LYS A 1 191 ? 5.488   -9.109  3.229   1.00 12.05 ? 238 LYS A O   1 
ATOM   1388 C  CB  . LYS A 1 191 ? 4.177   -11.474 4.707   1.00 11.65 ? 238 LYS A CB  1 
ATOM   1389 C  CG  . LYS A 1 191 ? 3.143   -12.203 5.525   1.00 12.75 ? 238 LYS A CG  1 
ATOM   1390 C  CD  . LYS A 1 191 ? 2.892   -13.598 4.913   1.00 13.25 ? 238 LYS A CD  1 
ATOM   1391 C  CE  . LYS A 1 191 ? 1.930   -14.424 5.716   1.00 15.05 ? 238 LYS A CE  1 
ATOM   1392 N  NZ  . LYS A 1 191 ? 1.587   -15.697 5.059   1.00 15.93 ? 238 LYS A NZ  1 
ATOM   1393 N  N   . ASP A 1 192 ? 6.819   -9.481  4.995   1.00 11.36 ? 239 ASP A N   1 
ATOM   1394 C  CA  . ASP A 1 192 ? 8.006   -8.887  4.420   1.00 10.90 ? 239 ASP A CA  1 
ATOM   1395 C  C   . ASP A 1 192 ? 9.154   -9.834  4.688   1.00 12.61 ? 239 ASP A C   1 
ATOM   1396 O  O   . ASP A 1 192 ? 9.475   -10.073 5.840   1.00 13.38 ? 239 ASP A O   1 
ATOM   1397 C  CB  . ASP A 1 192 ? 8.240   -7.522  5.045   1.00 11.72 ? 239 ASP A CB  1 
ATOM   1398 C  CG  . ASP A 1 192 ? 9.043   -6.545  4.222   1.00 13.90 ? 239 ASP A CG  1 
ATOM   1399 O  OD1 . ASP A 1 192 ? 9.774   -6.950  3.317   1.00 12.62 ? 239 ASP A OD1 1 
ATOM   1400 O  OD2 . ASP A 1 192 ? 8.907   -5.356  4.536   1.00 13.44 ? 239 ASP A OD2 1 
ATOM   1401 N  N   . GLY A 1 193 ? 9.665   -10.459 3.616   1.00 11.87 ? 240 GLY A N   1 
ATOM   1402 C  CA  . GLY A 1 193 ? 10.755  -11.402 3.695   1.00 12.57 ? 240 GLY A CA  1 
ATOM   1403 C  C   . GLY A 1 193 ? 10.499  -12.705 2.982   1.00 12.34 ? 240 GLY A C   1 
ATOM   1404 O  O   . GLY A 1 193 ? 11.372  -13.542 3.054   1.00 14.22 ? 240 GLY A O   1 
ATOM   1405 N  N   . THR A 1 194 ? 9.359   -12.897 2.327   1.00 11.48 ? 241 THR A N   1 
ATOM   1406 C  CA  . THR A 1 194 ? 9.075   -14.163 1.680   1.00 11.85 ? 241 THR A CA  1 
ATOM   1407 C  C   . THR A 1 194 ? 10.180  -14.585 0.714   1.00 12.60 ? 241 THR A C   1 
ATOM   1408 O  O   . THR A 1 194 ? 10.639  -15.714 0.775   1.00 13.71 ? 241 THR A O   1 
ATOM   1409 C  CB  . THR A 1 194 ? 7.728   -14.061 0.979   1.00 12.20 ? 241 THR A CB  1 
ATOM   1410 O  OG1 . THR A 1 194 ? 6.738   -13.680 1.919   1.00 12.62 ? 241 THR A OG1 1 
ATOM   1411 C  CG2 . THR A 1 194 ? 7.355   -15.347 0.270   1.00 13.40 ? 241 THR A CG2 1 
ATOM   1412 N  N   . ARG A 1 195 ? 10.502  -13.720 -0.240  1.00 12.42 ? 242 ARG A N   1 
ATOM   1413 C  CA  . ARG A 1 195 ? 11.481  -14.033 -1.260  1.00 12.96 ? 242 ARG A CA  1 
ATOM   1414 C  C   . ARG A 1 195 ? 12.782  -13.302 -0.948  1.00 13.34 ? 242 ARG A C   1 
ATOM   1415 O  O   . ARG A 1 195 ? 13.080  -12.254 -1.516  1.00 15.47 ? 242 ARG A O   1 
ATOM   1416 C  CB  . ARG A 1 195 ? 10.983  -13.738 -2.676  1.00 13.10 ? 242 ARG A CB  1 
ATOM   1417 C  CG  . ARG A 1 195 ? 10.129  -14.865 -3.232  1.00 14.15 ? 242 ARG A CG  1 
ATOM   1418 C  CD  . ARG A 1 195 ? 9.505   -14.657 -4.580  1.00 14.07 ? 242 ARG A CD  1 
ATOM   1419 N  NE  . ARG A 1 195 ? 10.477  -14.073 -5.499  1.00 14.41 ? 242 ARG A NE  1 
ATOM   1420 C  CZ  . ARG A 1 195 ? 11.576  -14.645 -5.937  1.00 16.04 ? 242 ARG A CZ  1 
ATOM   1421 N  NH1 . ARG A 1 195 ? 12.539  -13.898 -6.399  1.00 15.75 ? 242 ARG A NH1 1 
ATOM   1422 N  NH2 . ARG A 1 195 ? 11.722  -15.957 -5.899  1.00 19.47 ? 242 ARG A NH2 1 
ATOM   1423 N  N   . ASN A 1 196 ? 13.547  -13.876 -0.040  1.00 14.18 ? 243 ASN A N   1 
ATOM   1424 C  CA  . ASN A 1 196 ? 14.817  -13.344 0.383   1.00 14.00 ? 243 ASN A CA  1 
ATOM   1425 C  C   . ASN A 1 196 ? 15.887  -14.363 -0.013  1.00 17.40 ? 243 ASN A C   1 
ATOM   1426 O  O   . ASN A 1 196 ? 15.849  -14.942 -1.123  1.00 22.02 ? 243 ASN A O   1 
ATOM   1427 C  CB  . ASN A 1 196 ? 14.684  -12.857 1.827   1.00 13.44 ? 243 ASN A CB  1 
ATOM   1428 C  CG  . ASN A 1 196 ? 15.811  -11.945 2.242   1.00 13.22 ? 243 ASN A CG  1 
ATOM   1429 O  OD1 . ASN A 1 196 ? 16.289  -11.092 1.488   1.00 14.11 ? 243 ASN A OD1 1 
ATOM   1430 N  ND2 . ASN A 1 196 ? 16.259  -12.080 3.460   1.00 13.31 ? 243 ASN A ND2 1 
ATOM   1431 N  N   . ILE A 1 197 ? 16.995  -14.330 0.671   1.00 17.10 ? 244 ILE A N   1 
ATOM   1432 C  CA  . ILE A 1 197 ? 17.980  -15.396 0.614   1.00 16.25 ? 244 ILE A CA  1 
ATOM   1433 C  C   . ILE A 1 197 ? 17.983  -16.039 1.978   1.00 18.33 ? 244 ILE A C   1 
ATOM   1434 O  O   . ILE A 1 197 ? 17.955  -15.336 2.994   1.00 19.72 ? 244 ILE A O   1 
ATOM   1435 C  CB  . ILE A 1 197 ? 19.353  -14.836 0.219   1.00 17.84 ? 244 ILE A CB  1 
ATOM   1436 C  CG1 . ILE A 1 197 ? 19.298  -14.147 -1.119  1.00 18.02 ? 244 ILE A CG1 1 
ATOM   1437 C  CG2 . ILE A 1 197 ? 20.415  -15.939 0.242   1.00 20.48 ? 244 ILE A CG2 1 
ATOM   1438 C  CD1 . ILE A 1 197 ? 20.604  -13.456 -1.491  1.00 18.53 ? 244 ILE A CD1 1 
ATOM   1439 N  N   . ALA A 1 198 ? 17.913  -17.358 2.009   1.00 16.26 ? 245 ALA A N   1 
ATOM   1440 C  CA  . ALA A 1 198 ? 17.915  -18.086 3.251   1.00 16.75 ? 245 ALA A CA  1 
ATOM   1441 C  C   . ALA A 1 198 ? 19.352  -18.379 3.654   1.00 17.46 ? 245 ALA A C   1 
ATOM   1442 O  O   . ALA A 1 198 ? 20.218  -18.560 2.813   1.00 19.00 ? 245 ALA A O   1 
ATOM   1443 C  CB  . ALA A 1 198 ? 17.102  -19.346 3.112   1.00 17.72 ? 245 ALA A CB  1 
ATOM   1444 N  N   . GLY A 1 199 ? 19.574  -18.538 4.953   1.00 17.57 ? 246 GLY A N   1 
ATOM   1445 C  CA  . GLY A 1 199 ? 20.896  -18.837 5.501   1.00 18.88 ? 246 GLY A CA  1 
ATOM   1446 C  C   . GLY A 1 199 ? 21.411  -20.223 5.088   1.00 23.55 ? 246 GLY A C   1 
ATOM   1447 O  O   . GLY A 1 199 ? 22.614  -20.463 5.084   1.00 27.59 ? 246 GLY A O   1 
ATOM   1448 N  N   . THR A 1 200 ? 20.526  -21.109 4.641   1.00 21.95 ? 247 THR A N   1 
ATOM   1449 C  CA  . THR A 1 200 ? 20.912  -22.437 4.176   1.00 26.25 ? 247 THR A CA  1 
ATOM   1450 C  C   . THR A 1 200 ? 21.327  -22.410 2.704   1.00 24.98 ? 247 THR A C   1 
ATOM   1451 O  O   . THR A 1 200 ? 21.870  -23.406 2.221   1.00 26.82 ? 247 THR A O   1 
ATOM   1452 C  CB  . THR A 1 200 ? 19.758  -23.429 4.386   1.00 26.75 ? 247 THR A CB  1 
ATOM   1453 O  OG1 . THR A 1 200 ? 18.567  -22.919 3.794   1.00 30.66 ? 247 THR A OG1 1 
ATOM   1454 C  CG2 . THR A 1 200 ? 19.500  -23.683 5.859   1.00 33.81 ? 247 THR A CG2 1 
ATOM   1455 N  N   . GLU A 1 201 ? 21.026  -21.328 1.967   1.00 20.06 ? 248 GLU A N   1 
ATOM   1456 C  CA  . GLU A 1 201 ? 21.262  -21.300 0.531   1.00 19.36 ? 248 GLU A CA  1 
ATOM   1457 C  C   . GLU A 1 201 ? 22.697  -20.865 0.250   1.00 19.62 ? 248 GLU A C   1 
ATOM   1458 O  O   . GLU A 1 201 ? 22.946  -19.745 -0.201  1.00 20.78 ? 248 GLU A O   1 
ATOM   1459 C  CB  . GLU A 1 201 ? 20.235  -20.389 -0.138  1.00 21.02 ? 248 GLU A CB  1 
ATOM   1460 C  CG  . GLU A 1 201 ? 18.816  -20.926 -0.037  1.00 21.85 ? 248 GLU A CG  1 
ATOM   1461 C  CD  . GLU A 1 201 ? 17.725  -20.043 -0.604  1.00 25.56 ? 248 GLU A CD  1 
ATOM   1462 O  OE1 . GLU A 1 201 ? 17.793  -18.815 -0.502  1.00 21.93 ? 248 GLU A OE1 1 
ATOM   1463 O  OE2 . GLU A 1 201 ? 16.737  -20.603 -1.119  1.00 33.11 ? 248 GLU A OE2 1 
ATOM   1464 N  N   . LYS A 1 202 ? 23.657  -21.764 0.509   1.00 22.36 ? 249 LYS A N   1 
ATOM   1465 C  CA  . LYS A 1 202 ? 25.074  -21.434 0.436   1.00 24.75 ? 249 LYS A CA  1 
ATOM   1466 C  C   . LYS A 1 202 ? 25.451  -20.916 -0.951  1.00 22.14 ? 249 LYS A C   1 
ATOM   1467 O  O   . LYS A 1 202 ? 26.226  -19.970 -1.071  1.00 21.47 ? 249 LYS A O   1 
ATOM   1468 C  CB  . LYS A 1 202 ? 25.944  -22.669 0.714   1.00 30.49 ? 249 LYS A CB  1 
ATOM   1469 C  CG  . LYS A 1 202 ? 25.868  -23.179 2.146   1.00 42.71 ? 249 LYS A CG  1 
ATOM   1470 C  CD  . LYS A 1 202 ? 26.541  -22.248 3.148   1.00 49.10 ? 249 LYS A CD  1 
ATOM   1471 C  CE  . LYS A 1 202 ? 26.998  -22.936 4.401   1.00 53.89 ? 249 LYS A CE  1 
ATOM   1472 N  NZ  . LYS A 1 202 ? 27.711  -21.989 5.269   1.00 58.34 ? 249 LYS A NZ  1 
ATOM   1473 N  N   . ASP A 1 203 ? 24.926  -21.540 -2.008  1.00 23.10 ? 250 ASP A N   1 
ATOM   1474 C  CA  . ASP A 1 203 ? 25.271  -21.136 -3.366  1.00 25.70 ? 250 ASP A CA  1 
ATOM   1475 C  C   . ASP A 1 203 ? 24.805  -19.704 -3.630  1.00 20.63 ? 250 ASP A C   1 
ATOM   1476 O  O   . ASP A 1 203 ? 25.536  -18.889 -4.208  1.00 21.50 ? 250 ASP A O   1 
ATOM   1477 C  CB  . ASP A 1 203 ? 24.758  -22.136 -4.398  1.00 32.24 ? 250 ASP A CB  1 
ATOM   1478 C  CG  . ASP A 1 203 ? 25.497  -23.465 -4.434  1.00 41.32 ? 250 ASP A CG  1 
ATOM   1479 O  OD1 . ASP A 1 203 ? 26.591  -23.551 -3.820  1.00 46.38 ? 250 ASP A OD1 1 
ATOM   1480 O  OD2 . ASP A 1 203 ? 24.964  -24.409 -5.059  1.00 48.81 ? 250 ASP A OD2 1 
ATOM   1481 N  N   . ARG A 1 204 ? 23.598  -19.351 -3.167  1.00 18.91 ? 251 ARG A N   1 
ATOM   1482 C  CA  . ARG A 1 204 ? 23.073  -18.010 -3.384  1.00 18.13 ? 251 ARG A CA  1 
ATOM   1483 C  C   . ARG A 1 204 ? 23.788  -16.940 -2.558  1.00 17.41 ? 251 ARG A C   1 
ATOM   1484 O  O   . ARG A 1 204 ? 23.988  -15.831 -3.050  1.00 17.05 ? 251 ARG A O   1 
ATOM   1485 C  CB  . ARG A 1 204 ? 21.570  -17.935 -3.098  1.00 19.35 ? 251 ARG A CB  1 
ATOM   1486 C  CG  . ARG A 1 204 ? 20.749  -18.865 -3.993  1.00 23.80 ? 251 ARG A CG  1 
ATOM   1487 C  CD  . ARG A 1 204 ? 19.264  -18.768 -3.685  1.00 23.77 ? 251 ARG A CD  1 
ATOM   1488 N  NE  . ARG A 1 204 ? 18.701  -17.560 -4.284  1.00 24.44 ? 251 ARG A NE  1 
ATOM   1489 C  CZ  . ARG A 1 204 ? 17.708  -16.813 -3.825  1.00 21.59 ? 251 ARG A CZ  1 
ATOM   1490 N  NH1 . ARG A 1 204 ? 17.093  -17.029 -2.662  1.00 21.26 ? 251 ARG A NH1 1 
ATOM   1491 N  NH2 . ARG A 1 204 ? 17.292  -15.840 -4.584  1.00 23.07 ? 251 ARG A NH2 1 
ATOM   1492 N  N   . LEU A 1 205 ? 24.191  -17.287 -1.343  1.00 16.54 ? 252 LEU A N   1 
ATOM   1493 C  CA  . LEU A 1 205 ? 25.003  -16.398 -0.538  1.00 17.15 ? 252 LEU A CA  1 
ATOM   1494 C  C   . LEU A 1 205 ? 26.338  -16.137 -1.234  1.00 17.21 ? 252 LEU A C   1 
ATOM   1495 O  O   . LEU A 1 205 ? 26.756  -14.999 -1.303  1.00 16.86 ? 252 LEU A O   1 
ATOM   1496 C  CB  . LEU A 1 205 ? 25.175  -16.987 0.855   1.00 18.03 ? 252 LEU A CB  1 
ATOM   1497 C  CG  . LEU A 1 205 ? 23.908  -17.058 1.696   1.00 18.33 ? 252 LEU A CG  1 
ATOM   1498 C  CD1 . LEU A 1 205 ? 24.115  -17.980 2.859   1.00 21.09 ? 252 LEU A CD1 1 
ATOM   1499 C  CD2 . LEU A 1 205 ? 23.487  -15.679 2.156   1.00 20.81 ? 252 LEU A CD2 1 
ATOM   1500 N  N   . ASP A 1 206 ? 27.025  -17.191 -1.734  1.00 18.30 ? 253 ASP A N   1 
ATOM   1501 C  CA  . ASP A 1 206 ? 28.272  -16.960 -2.455  1.00 19.82 ? 253 ASP A CA  1 
ATOM   1502 C  C   . ASP A 1 206 ? 28.053  -16.101 -3.700  1.00 19.34 ? 253 ASP A C   1 
ATOM   1503 O  O   . ASP A 1 206 ? 28.875  -15.251 -4.027  1.00 22.00 ? 253 ASP A O   1 
ATOM   1504 C  CB  . ASP A 1 206 ? 28.957  -18.281 -2.812  1.00 21.08 ? 253 ASP A CB  1 
ATOM   1505 C  CG  . ASP A 1 206 ? 29.572  -19.051 -1.649  1.00 26.38 ? 253 ASP A CG  1 
ATOM   1506 O  OD1 . ASP A 1 206 ? 29.779  -18.475 -0.570  1.00 29.03 ? 253 ASP A OD1 1 
ATOM   1507 O  OD2 . ASP A 1 206 ? 29.813  -20.252 -1.816  1.00 32.43 ? 253 ASP A OD2 1 
ATOM   1508 N  N   . ARG A 1 207 ? 26.915  -16.262 -4.399  1.00 18.00 ? 254 ARG A N   1 
ATOM   1509 C  CA  . ARG A 1 207 ? 26.721  -15.541 -5.644  1.00 20.40 ? 254 ARG A CA  1 
ATOM   1510 C  C   . ARG A 1 207 ? 26.374  -14.072 -5.395  1.00 18.86 ? 254 ARG A C   1 
ATOM   1511 O  O   . ARG A 1 207 ? 26.827  -13.177 -6.102  1.00 20.53 ? 254 ARG A O   1 
ATOM   1512 C  CB  . ARG A 1 207 ? 25.612  -16.218 -6.451  1.00 24.13 ? 254 ARG A CB  1 
ATOM   1513 C  CG  . ARG A 1 207 ? 25.399  -15.550 -7.804  1.00 30.57 ? 254 ARG A CG  1 
ATOM   1514 C  CD  . ARG A 1 207 ? 24.700  -16.479 -8.802  1.00 38.54 ? 254 ARG A CD  1 
ATOM   1515 N  NE  . ARG A 1 207 ? 24.221  -15.707 -9.957  1.00 49.17 ? 254 ARG A NE  1 
ATOM   1516 C  CZ  . ARG A 1 207 ? 23.102  -15.952 -10.659 1.00 53.39 ? 254 ARG A CZ  1 
ATOM   1517 N  NH1 . ARG A 1 207 ? 22.425  -17.075 -10.481 1.00 52.50 ? 254 ARG A NH1 1 
ATOM   1518 N  NH2 . ARG A 1 207 ? 22.676  -15.086 -11.565 1.00 55.06 ? 254 ARG A NH2 1 
ATOM   1519 N  N   . PHE A 1 208 ? 25.557  -13.810 -4.354  1.00 17.33 ? 255 PHE A N   1 
ATOM   1520 C  CA  . PHE A 1 208 ? 24.923  -12.523 -4.192  1.00 15.39 ? 255 PHE A CA  1 
ATOM   1521 C  C   . PHE A 1 208 ? 25.314  -11.724 -2.953  1.00 14.48 ? 255 PHE A C   1 
ATOM   1522 O  O   . PHE A 1 208 ? 25.007  -10.545 -2.926  1.00 16.06 ? 255 PHE A O   1 
ATOM   1523 C  CB  . PHE A 1 208 ? 23.408  -12.713 -4.141  1.00 17.44 ? 255 PHE A CB  1 
ATOM   1524 C  CG  . PHE A 1 208 ? 22.840  -13.254 -5.440  1.00 19.32 ? 255 PHE A CG  1 
ATOM   1525 C  CD1 . PHE A 1 208 ? 22.964  -12.523 -6.613  1.00 21.31 ? 255 PHE A CD1 1 
ATOM   1526 C  CD2 . PHE A 1 208 ? 22.121  -14.434 -5.457  1.00 21.49 ? 255 PHE A CD2 1 
ATOM   1527 C  CE1 . PHE A 1 208 ? 22.392  -13.002 -7.792  1.00 21.69 ? 255 PHE A CE1 1 
ATOM   1528 C  CE2 . PHE A 1 208 ? 21.560  -14.899 -6.652  1.00 23.01 ? 255 PHE A CE2 1 
ATOM   1529 C  CZ  . PHE A 1 208 ? 21.701  -14.170 -7.790  1.00 22.31 ? 255 PHE A CZ  1 
ATOM   1530 N  N   . VAL A 1 209 ? 25.963  -12.333 -1.973  1.00 15.05 ? 256 VAL A N   1 
ATOM   1531 C  CA  . VAL A 1 209 ? 26.130  -11.686 -0.681  1.00 15.47 ? 256 VAL A CA  1 
ATOM   1532 C  C   . VAL A 1 209 ? 27.593  -11.554 -0.303  1.00 14.91 ? 256 VAL A C   1 
ATOM   1533 O  O   . VAL A 1 209 ? 27.991  -10.466 0.097   1.00 16.36 ? 256 VAL A O   1 
ATOM   1534 C  CB  . VAL A 1 209 ? 25.330  -12.430 0.389   1.00 16.00 ? 256 VAL A CB  1 
ATOM   1535 C  CG1 . VAL A 1 209 ? 25.635  -11.924 1.794   1.00 15.88 ? 256 VAL A CG1 1 
ATOM   1536 C  CG2 . VAL A 1 209 ? 23.863  -12.300 0.070   1.00 16.86 ? 256 VAL A CG2 1 
ATOM   1537 N  N   . TRP A 1 210 ? 28.388  -12.640 -0.390  1.00 15.10 ? 257 TRP A N   1 
ATOM   1538 C  CA  . TRP A 1 210 ? 29.780  -12.577 0.048   1.00 15.64 ? 257 TRP A CA  1 
ATOM   1539 C  C   . TRP A 1 210 ? 30.702  -12.051 -1.025  1.00 17.63 ? 257 TRP A C   1 
ATOM   1540 O  O   . TRP A 1 210 ? 30.619  -12.535 -2.146  1.00 19.45 ? 257 TRP A O   1 
ATOM   1541 C  CB  . TRP A 1 210 ? 30.285  -13.953 0.484   1.00 16.43 ? 257 TRP A CB  1 
ATOM   1542 C  CG  . TRP A 1 210 ? 29.450  -14.615 1.541   1.00 15.85 ? 257 TRP A CG  1 
ATOM   1543 C  CD1 . TRP A 1 210 ? 28.923  -15.848 1.441   1.00 17.00 ? 257 TRP A CD1 1 
ATOM   1544 C  CD2 . TRP A 1 210 ? 29.011  -14.062 2.799   1.00 14.62 ? 257 TRP A CD2 1 
ATOM   1545 N  NE1 . TRP A 1 210 ? 28.196  -16.128 2.567   1.00 19.04 ? 257 TRP A NE1 1 
ATOM   1546 C  CE2 . TRP A 1 210 ? 28.220  -15.054 3.412   1.00 15.71 ? 257 TRP A CE2 1 
ATOM   1547 C  CE3 . TRP A 1 210 ? 29.213  -12.848 3.459   1.00 16.97 ? 257 TRP A CE3 1 
ATOM   1548 C  CZ2 . TRP A 1 210 ? 27.640  -14.861 4.674   1.00 18.35 ? 257 TRP A CZ2 1 
ATOM   1549 C  CZ3 . TRP A 1 210 ? 28.680  -12.692 4.725   1.00 17.99 ? 257 TRP A CZ3 1 
ATOM   1550 C  CH2 . TRP A 1 210 ? 27.853  -13.654 5.281   1.00 16.86 ? 257 TRP A CH2 1 
ATOM   1551 N  N   . ALA A 1 211 ? 31.588  -11.130 -0.658  1.00 17.60 ? 258 ALA A N   1 
ATOM   1552 C  CA  . ALA A 1 211 ? 32.651  -10.683 -1.546  1.00 19.04 ? 258 ALA A CA  1 
ATOM   1553 C  C   . ALA A 1 211 ? 33.686  -11.797 -1.764  1.00 20.10 ? 258 ALA A C   1 
ATOM   1554 O  O   . ALA A 1 211 ? 34.026  -12.576 -0.869  1.00 20.64 ? 258 ALA A O   1 
ATOM   1555 C  CB  . ALA A 1 211 ? 33.273  -9.440  -0.972  1.00 19.65 ? 258 ALA A CB  1 
ATOM   1556 N  N   . ALA A 1 212 ? 34.122  -11.928 -3.022  1.00 21.47 ? 259 ALA A N   1 
ATOM   1557 C  CA  . ALA A 1 212 ? 35.078  -12.960 -3.384  1.00 24.31 ? 259 ALA A CA  1 
ATOM   1558 C  C   . ALA A 1 212 ? 36.416  -12.295 -3.667  1.00 23.15 ? 259 ALA A C   1 
ATOM   1559 O  O   . ALA A 1 212 ? 36.461  -11.106 -3.960  1.00 25.90 ? 259 ALA A O   1 
ATOM   1560 C  CB  . ALA A 1 212 ? 34.581  -13.724 -4.582  1.00 27.09 ? 259 ALA A CB  1 
ATOM   1561 N  N   . GLU A 1 213 ? 37.505  -13.081 -3.605  1.00 27.48 ? 260 GLU A N   1 
ATOM   1562 C  CA  . GLU A 1 213 ? 38.821  -12.526 -3.864  1.00 29.56 ? 260 GLU A CA  1 
ATOM   1563 C  C   . GLU A 1 213 ? 38.876  -11.907 -5.255  1.00 29.62 ? 260 GLU A C   1 
ATOM   1564 O  O   . GLU A 1 213 ? 39.445  -10.828 -5.435  1.00 30.43 ? 260 GLU A O   1 
ATOM   1565 C  CB  . GLU A 1 213 ? 39.951  -13.548 -3.764  1.00 34.38 ? 260 GLU A CB  1 
ATOM   1566 C  CG  . GLU A 1 213 ? 41.300  -12.855 -3.934  1.00 41.43 ? 260 GLU A CG  1 
ATOM   1567 C  CD  . GLU A 1 213 ? 42.528  -13.648 -3.548  1.00 46.97 ? 260 GLU A CD  1 
ATOM   1568 O  OE1 . GLU A 1 213 ? 42.413  -14.888 -3.440  1.00 49.53 ? 260 GLU A OE1 1 
ATOM   1569 O  OE2 . GLU A 1 213 ? 43.566  -12.993 -3.308  1.00 50.60 ? 260 GLU A OE2 1 
ATOM   1570 N  N   . LYS A 1 214 ? 38.244  -12.579 -6.214  1.00 30.58 ? 261 LYS A N   1 
ATOM   1571 C  CA  . LYS A 1 214 ? 38.346  -12.148 -7.602  1.00 33.67 ? 261 LYS A CA  1 
ATOM   1572 C  C   . LYS A 1 214 ? 37.619  -10.825 -7.820  1.00 31.41 ? 261 LYS A C   1 
ATOM   1573 O  O   . LYS A 1 214 ? 37.791  -10.224 -8.865  1.00 27.79 ? 261 LYS A O   1 
ATOM   1574 C  CB  . LYS A 1 214 ? 37.868  -13.185 -8.627  1.00 38.28 ? 261 LYS A CB  1 
ATOM   1575 C  CG  . LYS A 1 214 ? 36.401  -13.628 -8.545  1.00 44.91 ? 261 LYS A CG  1 
ATOM   1576 C  CD  . LYS A 1 214 ? 36.066  -14.880 -9.351  1.00 55.29 ? 261 LYS A CD  1 
ATOM   1577 C  CE  . LYS A 1 214 ? 36.012  -14.658 -10.835 1.00 62.02 ? 261 LYS A CE  1 
ATOM   1578 N  NZ  . LYS A 1 214 ? 34.748  -14.034 -11.243 1.00 65.35 ? 261 LYS A NZ  1 
ATOM   1579 N  N   . ASP A 1 215 ? 36.800  -10.350 -6.857  1.00 27.00 ? 262 ASP A N   1 
ATOM   1580 C  CA  . ASP A 1 215 ? 36.082  -9.101  -7.065  1.00 25.68 ? 262 ASP A CA  1 
ATOM   1581 C  C   . ASP A 1 215 ? 36.995  -7.877  -7.015  1.00 26.41 ? 262 ASP A C   1 
ATOM   1582 O  O   . ASP A 1 215 ? 36.584  -6.804  -7.434  1.00 33.18 ? 262 ASP A O   1 
ATOM   1583 C  CB  . ASP A 1 215 ? 34.945  -8.937  -6.070  1.00 24.46 ? 262 ASP A CB  1 
ATOM   1584 C  CG  . ASP A 1 215 ? 33.931  -10.063 -6.143  1.00 26.06 ? 262 ASP A CG  1 
ATOM   1585 O  OD1 . ASP A 1 215 ? 33.924  -10.776 -7.165  1.00 25.27 ? 262 ASP A OD1 1 
ATOM   1586 O  OD2 . ASP A 1 215 ? 33.159  -10.260 -5.172  1.00 22.06 ? 262 ASP A OD2 1 
ATOM   1587 N  N   . GLY A 1 216 ? 38.213  -8.020  -6.497  1.00 25.93 ? 263 GLY A N   1 
ATOM   1588 C  CA  . GLY A 1 216 ? 39.185  -6.957  -6.691  1.00 26.85 ? 263 GLY A CA  1 
ATOM   1589 C  C   . GLY A 1 216 ? 39.747  -6.381  -5.405  1.00 27.24 ? 263 GLY A C   1 
ATOM   1590 O  O   . GLY A 1 216 ? 40.682  -5.590  -5.467  1.00 31.04 ? 263 GLY A O   1 
ATOM   1591 N  N   . THR A 1 217 ? 39.201  -6.758  -4.237  1.00 24.83 ? 264 THR A N   1 
ATOM   1592 C  CA  . THR A 1 217 ? 39.659  -6.155  -3.002  1.00 23.44 ? 264 THR A CA  1 
ATOM   1593 C  C   . THR A 1 217 ? 39.954  -7.297  -2.044  1.00 24.39 ? 264 THR A C   1 
ATOM   1594 O  O   . THR A 1 217 ? 39.046  -7.795  -1.384  1.00 23.87 ? 264 THR A O   1 
ATOM   1595 C  CB  . THR A 1 217 ? 38.613  -5.191  -2.440  1.00 27.59 ? 264 THR A CB  1 
ATOM   1596 O  OG1 . THR A 1 217 ? 38.316  -4.135  -3.360  1.00 28.02 ? 264 THR A OG1 1 
ATOM   1597 C  CG2 . THR A 1 217 ? 39.075  -4.567  -1.144  1.00 26.97 ? 264 THR A CG2 1 
ATOM   1598 N  N   . PRO A 1 218 ? 41.185  -7.858  -2.033  1.00 25.57 ? 265 PRO A N   1 
ATOM   1599 C  CA  . PRO A 1 218 ? 41.461  -9.047  -1.245  1.00 23.57 ? 265 PRO A CA  1 
ATOM   1600 C  C   . PRO A 1 218 ? 41.099  -9.005  0.235   1.00 21.93 ? 265 PRO A C   1 
ATOM   1601 O  O   . PRO A 1 218 ? 40.630  -10.025 0.730   1.00 24.21 ? 265 PRO A O   1 
ATOM   1602 C  CB  . PRO A 1 218 ? 42.970  -9.278  -1.451  1.00 27.69 ? 265 PRO A CB  1 
ATOM   1603 C  CG  . PRO A 1 218 ? 43.242  -8.669  -2.816  1.00 30.56 ? 265 PRO A CG  1 
ATOM   1604 C  CD  . PRO A 1 218 ? 42.281  -7.506  -2.947  1.00 27.58 ? 265 PRO A CD  1 
ATOM   1605 N  N   . TRP A 1 219 ? 41.288  -7.858  0.903   1.00 22.26 ? 266 TRP A N   1 
ATOM   1606 C  CA  . TRP A 1 219 ? 41.006  -7.772  2.333   1.00 21.31 ? 266 TRP A CA  1 
ATOM   1607 C  C   . TRP A 1 219 ? 39.529  -8.001  2.621   1.00 21.11 ? 266 TRP A C   1 
ATOM   1608 O  O   . TRP A 1 219 ? 39.203  -8.357  3.742   1.00 21.15 ? 266 TRP A O   1 
ATOM   1609 C  CB  . TRP A 1 219 ? 41.458  -6.477  3.003   1.00 21.22 ? 266 TRP A CB  1 
ATOM   1610 C  CG  . TRP A 1 219 ? 40.723  -5.211  2.655   1.00 21.38 ? 266 TRP A CG  1 
ATOM   1611 C  CD1 . TRP A 1 219 ? 41.071  -4.287  1.711   1.00 21.15 ? 266 TRP A CD1 1 
ATOM   1612 C  CD2 . TRP A 1 219 ? 39.572  -4.669  3.337   1.00 21.02 ? 266 TRP A CD2 1 
ATOM   1613 N  NE1 . TRP A 1 219 ? 40.186  -3.245  1.728   1.00 21.28 ? 266 TRP A NE1 1 
ATOM   1614 C  CE2 . TRP A 1 219 ? 39.253  -3.448  2.717   1.00 20.97 ? 266 TRP A CE2 1 
ATOM   1615 C  CE3 . TRP A 1 219 ? 38.775  -5.107  4.400   1.00 20.80 ? 266 TRP A CE3 1 
ATOM   1616 C  CZ2 . TRP A 1 219 ? 38.201  -2.654  3.130   1.00 22.16 ? 266 TRP A CZ2 1 
ATOM   1617 C  CZ3 . TRP A 1 219 ? 37.731  -4.314  4.810   1.00 19.04 ? 266 TRP A CZ3 1 
ATOM   1618 C  CH2 . TRP A 1 219 ? 37.434  -3.110  4.180   1.00 20.32 ? 266 TRP A CH2 1 
ATOM   1619 N  N   . MET A 1 220 ? 38.667  -7.815  1.621   1.00 20.05 ? 267 MET A N   1 
ATOM   1620 C  CA  . MET A 1 220 ? 37.238  -7.972  1.837   1.00 17.81 ? 267 MET A CA  1 
ATOM   1621 C  C   . MET A 1 220 ? 36.715  -9.367  1.553   1.00 18.69 ? 267 MET A C   1 
ATOM   1622 O  O   . MET A 1 220 ? 35.519  -9.548  1.623   1.00 18.06 ? 267 MET A O   1 
ATOM   1623 C  CB  . MET A 1 220 ? 36.458  -6.981  0.967   1.00 18.24 ? 267 MET A CB  1 
ATOM   1624 C  CG  . MET A 1 220 ? 36.241  -5.662  1.639   1.00 17.15 ? 267 MET A CG  1 
ATOM   1625 S  SD  . MET A 1 220 ? 35.133  -5.741  3.075   1.00 18.34 ? 267 MET A SD  1 
ATOM   1626 C  CE  . MET A 1 220 ? 33.599  -6.224  2.278   1.00 19.14 ? 267 MET A CE  1 
ATOM   1627 N  N   . THR A 1 221 ? 37.539  -10.318 1.082   1.00 20.66 ? 268 THR A N   1 
ATOM   1628 C  CA  . THR A 1 221 ? 37.071  -11.661 0.789   1.00 20.45 ? 268 THR A CA  1 
ATOM   1629 C  C   . THR A 1 221 ? 36.362  -12.238 2.007   1.00 18.79 ? 268 THR A C   1 
ATOM   1630 O  O   . THR A 1 221 ? 36.964  -12.378 3.063   1.00 20.50 ? 268 THR A O   1 
ATOM   1631 C  CB  . THR A 1 221 ? 38.244  -12.570 0.390   1.00 22.91 ? 268 THR A CB  1 
ATOM   1632 O  OG1 . THR A 1 221 ? 38.871  -11.954 -0.735  1.00 25.96 ? 268 THR A OG1 1 
ATOM   1633 C  CG2 . THR A 1 221 ? 37.771  -13.960 0.017   1.00 23.53 ? 268 THR A CG2 1 
ATOM   1634 N  N   . GLY A 1 222 ? 35.105  -12.632 1.808   1.00 17.72 ? 269 GLY A N   1 
ATOM   1635 C  CA  . GLY A 1 222 ? 34.280  -13.220 2.866   1.00 16.91 ? 269 GLY A CA  1 
ATOM   1636 C  C   . GLY A 1 222 ? 33.450  -12.171 3.592   1.00 15.08 ? 269 GLY A C   1 
ATOM   1637 O  O   . GLY A 1 222 ? 32.688  -12.521 4.468   1.00 16.97 ? 269 GLY A O   1 
ATOM   1638 N  N   . GLY A 1 223 ? 33.660  -10.896 3.284   1.00 14.95 ? 270 GLY A N   1 
ATOM   1639 C  CA  . GLY A 1 223 ? 32.837  -9.844  3.820   1.00 15.00 ? 270 GLY A CA  1 
ATOM   1640 C  C   . GLY A 1 223 ? 31.644  -9.610  2.912   1.00 15.13 ? 270 GLY A C   1 
ATOM   1641 O  O   . GLY A 1 223 ? 31.357  -10.380 1.996   1.00 16.45 ? 270 GLY A O   1 
ATOM   1642 N  N   . SER A 1 224 ? 30.966  -8.502  3.164   1.00 14.24 ? 271 SER A N   1 
ATOM   1643 C  CA  . SER A 1 224 ? 29.776  -8.124  2.418   1.00 14.02 ? 271 SER A CA  1 
ATOM   1644 C  C   . SER A 1 224 ? 29.647  -6.617  2.473   1.00 14.95 ? 271 SER A C   1 
ATOM   1645 O  O   . SER A 1 224 ? 30.450  -5.947  3.119   1.00 16.46 ? 271 SER A O   1 
ATOM   1646 C  CB  . SER A 1 224 ? 28.548  -8.813  2.984   1.00 14.69 ? 271 SER A CB  1 
ATOM   1647 O  OG  . SER A 1 224 ? 27.425  -8.631  2.147   1.00 15.84 ? 271 SER A OG  1 
ATOM   1648 N  N   . TYR A 1 225 ? 28.672  -6.071  1.763   1.00 13.98 ? 272 TYR A N   1 
ATOM   1649 C  CA  . TYR A 1 225 ? 28.460  -4.643  1.746   1.00 13.51 ? 272 TYR A CA  1 
ATOM   1650 C  C   . TYR A 1 225 ? 27.036  -4.384  2.225   1.00 13.75 ? 272 TYR A C   1 
ATOM   1651 O  O   . TYR A 1 225 ? 26.099  -5.076  1.803   1.00 15.35 ? 272 TYR A O   1 
ATOM   1652 C  CB  . TYR A 1 225 ? 28.654  -4.005  0.370   1.00 14.39 ? 272 TYR A CB  1 
ATOM   1653 C  CG  . TYR A 1 225 ? 30.095  -4.212  -0.063  1.00 13.45 ? 272 TYR A CG  1 
ATOM   1654 C  CD1 . TYR A 1 225 ? 30.500  -5.357  -0.725  1.00 15.67 ? 272 TYR A CD1 1 
ATOM   1655 C  CD2 . TYR A 1 225 ? 31.040  -3.259  0.257   1.00 15.04 ? 272 TYR A CD2 1 
ATOM   1656 C  CE1 . TYR A 1 225 ? 31.835  -5.563  -1.059  1.00 16.39 ? 272 TYR A CE1 1 
ATOM   1657 C  CE2 . TYR A 1 225 ? 32.368  -3.466  -0.040  1.00 15.69 ? 272 TYR A CE2 1 
ATOM   1658 C  CZ  . TYR A 1 225 ? 32.758  -4.613  -0.694  1.00 16.86 ? 272 TYR A CZ  1 
ATOM   1659 O  OH  . TYR A 1 225 ? 34.065  -4.811  -1.023  1.00 18.97 ? 272 TYR A OH  1 
ATOM   1660 N  N   . LEU A 1 226 ? 26.897  -3.364  3.047   1.00 13.16 ? 273 LEU A N   1 
ATOM   1661 C  CA  . LEU A 1 226 ? 25.620  -3.089  3.704   1.00 13.18 ? 273 LEU A CA  1 
ATOM   1662 C  C   . LEU A 1 226 ? 25.128  -1.719  3.278   1.00 14.02 ? 273 LEU A C   1 
ATOM   1663 O  O   . LEU A 1 226 ? 25.897  -0.760  3.261   1.00 14.16 ? 273 LEU A O   1 
ATOM   1664 C  CB  . LEU A 1 226 ? 25.864  -3.052  5.212   1.00 13.45 ? 273 LEU A CB  1 
ATOM   1665 C  CG  . LEU A 1 226 ? 24.689  -2.599  6.065   1.00 15.66 ? 273 LEU A CG  1 
ATOM   1666 C  CD1 . LEU A 1 226 ? 23.508  -3.529  5.868   1.00 15.49 ? 273 LEU A CD1 1 
ATOM   1667 C  CD2 . LEU A 1 226 ? 25.137  -2.564  7.535   1.00 18.41 ? 273 LEU A CD2 1 
ATOM   1668 N  N   . VAL A 1 227 ? 23.850  -1.652  2.890   1.00 12.89 ? 274 VAL A N   1 
ATOM   1669 C  CA  . VAL A 1 227 ? 23.137  -0.399  2.711   1.00 13.11 ? 274 VAL A CA  1 
ATOM   1670 C  C   . VAL A 1 227 ? 22.094  -0.311  3.811   1.00 13.05 ? 274 VAL A C   1 
ATOM   1671 O  O   . VAL A 1 227 ? 21.275  -1.237  3.977   1.00 14.74 ? 274 VAL A O   1 
ATOM   1672 C  CB  . VAL A 1 227 ? 22.469  -0.303  1.334   1.00 15.13 ? 274 VAL A CB  1 
ATOM   1673 C  CG1 . VAL A 1 227 ? 21.558  0.903   1.239   1.00 16.68 ? 274 VAL A CG1 1 
ATOM   1674 C  CG2 . VAL A 1 227 ? 23.469  -0.388  0.189   1.00 15.05 ? 274 VAL A CG2 1 
ATOM   1675 N  N   . ALA A 1 228 ? 22.063  0.825   4.488   1.00 12.09 ? 275 ALA A N   1 
ATOM   1676 C  CA  . ALA A 1 228 ? 21.030  1.138   5.451   1.00 12.15 ? 275 ALA A CA  1 
ATOM   1677 C  C   . ALA A 1 228 ? 20.220  2.319   4.971   1.00 13.98 ? 275 ALA A C   1 
ATOM   1678 O  O   . ALA A 1 228 ? 20.805  3.313   4.546   1.00 14.83 ? 275 ALA A O   1 
ATOM   1679 C  CB  . ALA A 1 228 ? 21.671  1.434   6.758   1.00 13.61 ? 275 ALA A CB  1 
ATOM   1680 N  N   . ARG A 1 229 ? 18.899  2.167   4.976   1.00 12.38 ? 276 ARG A N   1 
ATOM   1681 C  CA  . ARG A 1 229 ? 18.014  3.283   4.661   1.00 13.45 ? 276 ARG A CA  1 
ATOM   1682 C  C   . ARG A 1 229 ? 16.940  3.423   5.719   1.00 13.31 ? 276 ARG A C   1 
ATOM   1683 O  O   . ARG A 1 229 ? 16.215  2.470   6.017   1.00 13.80 ? 276 ARG A O   1 
ATOM   1684 C  CB  . ARG A 1 229 ? 17.361  3.064   3.303   1.00 14.44 ? 276 ARG A CB  1 
ATOM   1685 C  CG  . ARG A 1 229 ? 18.308  2.905   2.137   1.00 15.75 ? 276 ARG A CG  1 
ATOM   1686 C  CD  . ARG A 1 229 ? 19.027  4.170   1.707   1.00 16.95 ? 276 ARG A CD  1 
ATOM   1687 N  NE  . ARG A 1 229 ? 18.091  4.999   0.947   1.00 16.08 ? 276 ARG A NE  1 
ATOM   1688 C  CZ  . ARG A 1 229 ? 18.432  5.995   0.158   1.00 16.11 ? 276 ARG A CZ  1 
ATOM   1689 N  NH1 . ARG A 1 229 ? 19.698  6.373   0.071   1.00 18.13 ? 276 ARG A NH1 1 
ATOM   1690 N  NH2 . ARG A 1 229 ? 17.473  6.559   -0.593  1.00 17.62 ? 276 ARG A NH2 1 
ATOM   1691 N  N   . ARG A 1 230 ? 16.848  4.606   6.331   1.00 12.83 ? 277 ARG A N   1 
ATOM   1692 C  CA  . ARG A 1 230 ? 15.772  4.880   7.250   1.00 12.80 ? 277 ARG A CA  1 
ATOM   1693 C  C   . ARG A 1 230 ? 14.590  5.383   6.446   1.00 14.00 ? 277 ARG A C   1 
ATOM   1694 O  O   . ARG A 1 230 ? 14.735  6.364   5.740   1.00 14.12 ? 277 ARG A O   1 
ATOM   1695 C  CB  . ARG A 1 230 ? 16.257  5.896   8.288   1.00 14.76 ? 277 ARG A CB  1 
ATOM   1696 C  CG  . ARG A 1 230 ? 15.222  6.152   9.362   1.00 17.66 ? 277 ARG A CG  1 
ATOM   1697 C  CD  . ARG A 1 230 ? 15.770  7.157   10.419  1.00 24.62 ? 277 ARG A CD  1 
ATOM   1698 N  NE  . ARG A 1 230 ? 15.001  7.141   11.670  1.00 31.67 ? 277 ARG A NE  1 
ATOM   1699 C  CZ  . ARG A 1 230 ? 14.196  8.112   12.042  1.00 37.59 ? 277 ARG A CZ  1 
ATOM   1700 N  NH1 . ARG A 1 230 ? 14.092  9.189   11.270  1.00 39.44 ? 277 ARG A NH1 1 
ATOM   1701 N  NH2 . ARG A 1 230 ? 13.488  8.000   13.153  1.00 39.81 ? 277 ARG A NH2 1 
ATOM   1702 N  N   . ILE A 1 231 ? 13.463  4.679   6.493   1.00 12.45 ? 278 ILE A N   1 
ATOM   1703 C  CA  . ILE A 1 231 ? 12.326  4.966   5.628   1.00 12.44 ? 278 ILE A CA  1 
ATOM   1704 C  C   . ILE A 1 231 ? 11.107  5.289   6.484   1.00 12.90 ? 278 ILE A C   1 
ATOM   1705 O  O   . ILE A 1 231 ? 10.645  4.455   7.265   1.00 14.18 ? 278 ILE A O   1 
ATOM   1706 C  CB  . ILE A 1 231 ? 12.036  3.796   4.672   1.00 13.51 ? 278 ILE A CB  1 
ATOM   1707 C  CG1 . ILE A 1 231 ? 13.247  3.388   3.924   1.00 14.47 ? 278 ILE A CG1 1 
ATOM   1708 C  CG2 . ILE A 1 231 ? 10.875  4.141   3.725   1.00 14.71 ? 278 ILE A CG2 1 
ATOM   1709 C  CD1 . ILE A 1 231 ? 13.052  2.162   3.044   1.00 14.99 ? 278 ILE A CD1 1 
ATOM   1710 N  N   . ARG A 1 232 ? 10.589  6.512   6.355   1.00 12.96 ? 279 ARG A N   1 
ATOM   1711 C  CA  . ARG A 1 232 ? 9.389   6.880   7.059   1.00 13.99 ? 279 ARG A CA  1 
ATOM   1712 C  C   . ARG A 1 232 ? 8.209   6.371   6.264   1.00 14.52 ? 279 ARG A C   1 
ATOM   1713 O  O   . ARG A 1 232 ? 8.261   6.394   5.045   1.00 15.87 ? 279 ARG A O   1 
ATOM   1714 C  CB  . ARG A 1 232 ? 9.344   8.415   7.074   1.00 18.09 ? 279 ARG A CB  1 
ATOM   1715 C  CG  . ARG A 1 232 ? 8.007   8.962   7.537   1.00 24.96 ? 279 ARG A CG  1 
ATOM   1716 C  CD  . ARG A 1 232 ? 7.966   10.492  7.542   1.00 33.59 ? 279 ARG A CD  1 
ATOM   1717 N  NE  . ARG A 1 232 ? 9.142   11.091  8.179   1.00 43.66 ? 279 ARG A NE  1 
ATOM   1718 C  CZ  . ARG A 1 232 ? 9.529   10.843  9.416   1.00 49.88 ? 279 ARG A CZ  1 
ATOM   1719 N  NH1 . ARG A 1 232 ? 8.775   10.078  10.186  1.00 57.42 ? 279 ARG A NH1 1 
ATOM   1720 N  NH2 . ARG A 1 232 ? 10.660  11.362  9.872   1.00 52.07 ? 279 ARG A NH2 1 
ATOM   1721 N  N   . MET A 1 233 ? 7.160   5.942   6.972   1.00 13.87 ? 280 MET A N   1 
ATOM   1722 C  CA  . MET A 1 233 ? 5.944   5.462   6.338   1.00 13.63 ? 280 MET A CA  1 
ATOM   1723 C  C   . MET A 1 233 ? 4.842   6.470   6.607   1.00 13.60 ? 280 MET A C   1 
ATOM   1724 O  O   . MET A 1 233 ? 4.663   6.907   7.725   1.00 15.36 ? 280 MET A O   1 
ATOM   1725 C  CB  . MET A 1 233 ? 5.518   4.110   6.920   1.00 15.27 ? 280 MET A CB  1 
ATOM   1726 C  CG  . MET A 1 233 ? 6.411   2.987   6.498   1.00 17.02 ? 280 MET A CG  1 
ATOM   1727 S  SD  . MET A 1 233 ? 6.020   1.511   7.494   1.00 21.63 ? 280 MET A SD  1 
ATOM   1728 C  CE  . MET A 1 233 ? 6.758   0.214   6.491   1.00 23.07 ? 280 MET A CE  1 
ATOM   1729 N  N   . HIS A 1 234 ? 4.104   6.807   5.574   1.00 13.26 ? 281 HIS A N   1 
ATOM   1730 C  CA  . HIS A 1 234 ? 2.989   7.732   5.693   1.00 13.85 ? 281 HIS A CA  1 
ATOM   1731 C  C   . HIS A 1 234 ? 1.737   6.955   6.080   1.00 12.58 ? 281 HIS A C   1 
ATOM   1732 O  O   . HIS A 1 234 ? 0.916   6.619   5.210   1.00 14.18 ? 281 HIS A O   1 
ATOM   1733 C  CB  . HIS A 1 234 ? 2.785   8.435   4.357   1.00 15.15 ? 281 HIS A CB  1 
ATOM   1734 C  CG  . HIS A 1 234 ? 3.913   9.261   3.895   1.00 15.06 ? 281 HIS A CG  1 
ATOM   1735 N  ND1 . HIS A 1 234 ? 4.689   9.953   4.787   1.00 18.14 ? 281 HIS A ND1 1 
ATOM   1736 C  CD2 . HIS A 1 234 ? 4.451   9.454   2.683   1.00 16.59 ? 281 HIS A CD2 1 
ATOM   1737 C  CE1 . HIS A 1 234 ? 5.661   10.573  4.099   1.00 18.37 ? 281 HIS A CE1 1 
ATOM   1738 N  NE2 . HIS A 1 234 ? 5.532   10.270  2.821   1.00 18.51 ? 281 HIS A NE2 1 
ATOM   1739 N  N   . ILE A 1 235 ? 1.645   6.569   7.341   1.00 13.57 ? 282 ILE A N   1 
ATOM   1740 C  CA  . ILE A 1 235 ? 0.595   5.654   7.749   1.00 14.63 ? 282 ILE A CA  1 
ATOM   1741 C  C   . ILE A 1 235 ? -0.788  6.288   7.662   1.00 13.72 ? 282 ILE A C   1 
ATOM   1742 O  O   . ILE A 1 235 ? -1.733  5.566   7.381   1.00 13.88 ? 282 ILE A O   1 
ATOM   1743 C  CB  . ILE A 1 235 ? 0.820   4.995   9.116   1.00 19.43 ? 282 ILE A CB  1 
ATOM   1744 C  CG1 . ILE A 1 235 ? 0.982   5.962   10.202  1.00 21.77 ? 282 ILE A CG1 1 
ATOM   1745 C  CG2 . ILE A 1 235 ? 1.996   3.990   9.042   1.00 21.41 ? 282 ILE A CG2 1 
ATOM   1746 C  CD1 . ILE A 1 235 ? 0.889   5.314   11.587  1.00 26.13 ? 282 ILE A CD1 1 
ATOM   1747 N  N   . GLU A 1 236 ? -0.932  7.612   7.865   1.00 11.70 ? 283 GLU A N   1 
ATOM   1748 C  CA  . GLU A 1 236 ? -2.244  8.195   7.697   1.00 11.41 ? 283 GLU A CA  1 
ATOM   1749 C  C   . GLU A 1 236 ? -2.735  7.945   6.267   1.00 12.20 ? 283 GLU A C   1 
ATOM   1750 O  O   . GLU A 1 236 ? -3.901  7.603   6.064   1.00 13.48 ? 283 GLU A O   1 
ATOM   1751 C  CB  . GLU A 1 236 ? -2.192  9.703   7.974   1.00 12.82 ? 283 GLU A CB  1 
ATOM   1752 C  CG  . GLU A 1 236 ? -3.551  10.364  7.826   1.00 12.63 ? 283 GLU A CG  1 
ATOM   1753 C  CD  . GLU A 1 236 ? -3.623  11.851  8.016   1.00 13.10 ? 283 GLU A CD  1 
ATOM   1754 O  OE1 . GLU A 1 236 ? -2.639  12.458  8.472   1.00 13.59 ? 283 GLU A OE1 1 
ATOM   1755 O  OE2 . GLU A 1 236 ? -4.662  12.378  7.592   1.00 13.88 ? 283 GLU A OE2 1 
ATOM   1756 N  N   . THR A 1 237 ? -1.831  8.178   5.311   1.00 13.06 ? 284 THR A N   1 
ATOM   1757 C  CA  . THR A 1 237 ? -2.165  8.083   3.894   1.00 13.11 ? 284 THR A CA  1 
ATOM   1758 C  C   . THR A 1 237 ? -2.496  6.628   3.551   1.00 13.28 ? 284 THR A C   1 
ATOM   1759 O  O   . THR A 1 237 ? -3.481  6.307   2.897   1.00 15.42 ? 284 THR A O   1 
ATOM   1760 C  CB  . THR A 1 237 ? -0.979  8.652   3.124   1.00 13.93 ? 284 THR A CB  1 
ATOM   1761 O  OG1 . THR A 1 237 ? -0.480  9.848   3.763   1.00 17.01 ? 284 THR A OG1 1 
ATOM   1762 C  CG2 . THR A 1 237 ? -1.350  8.802   1.674   1.00 16.21 ? 284 THR A CG2 1 
ATOM   1763 N  N   . TRP A 1 238 ? -1.659  5.724   4.068   1.00 12.38 ? 285 TRP A N   1 
ATOM   1764 C  CA  . TRP A 1 238 ? -1.842  4.295   3.829   1.00 11.73 ? 285 TRP A CA  1 
ATOM   1765 C  C   . TRP A 1 238 ? -3.140  3.777   4.416   1.00 12.25 ? 285 TRP A C   1 
ATOM   1766 O  O   . TRP A 1 238 ? -3.852  2.957   3.794   1.00 13.48 ? 285 TRP A O   1 
ATOM   1767 C  CB  . TRP A 1 238 ? -0.680  3.554   4.456   1.00 12.20 ? 285 TRP A CB  1 
ATOM   1768 C  CG  . TRP A 1 238 ? -0.736  2.064   4.295   1.00 11.76 ? 285 TRP A CG  1 
ATOM   1769 C  CD1 . TRP A 1 238 ? -1.033  1.164   5.258   1.00 11.64 ? 285 TRP A CD1 1 
ATOM   1770 C  CD2 . TRP A 1 238 ? -0.461  1.314   3.103   1.00 12.68 ? 285 TRP A CD2 1 
ATOM   1771 N  NE1 . TRP A 1 238 ? -0.932  -0.098  4.775   1.00 12.52 ? 285 TRP A NE1 1 
ATOM   1772 C  CE2 . TRP A 1 238 ? -0.589  -0.049  3.464   1.00 11.94 ? 285 TRP A CE2 1 
ATOM   1773 C  CE3 . TRP A 1 238 ? -0.112  1.633   1.789   1.00 14.06 ? 285 TRP A CE3 1 
ATOM   1774 C  CZ2 . TRP A 1 238 ? -0.361  -1.073  2.554   1.00 13.11 ? 285 TRP A CZ2 1 
ATOM   1775 C  CZ3 . TRP A 1 238 ? 0.117   0.613   0.892   1.00 14.54 ? 285 TRP A CZ3 1 
ATOM   1776 C  CH2 . TRP A 1 238 ? -0.022  -0.721  1.279   1.00 14.52 ? 285 TRP A CH2 1 
ATOM   1777 N  N   . ASP A 1 239 ? -3.448  4.177   5.645   1.00 12.61 ? 286 ASP A N   1 
ATOM   1778 C  CA  . ASP A 1 239 ? -4.562  3.603   6.375   1.00 13.47 ? 286 ASP A CA  1 
ATOM   1779 C  C   . ASP A 1 239 ? -5.912  4.016   5.810   1.00 15.91 ? 286 ASP A C   1 
ATOM   1780 O  O   . ASP A 1 239 ? -6.874  3.294   6.051   1.00 19.73 ? 286 ASP A O   1 
ATOM   1781 C  CB  . ASP A 1 239 ? -4.462  3.903   7.866   1.00 14.17 ? 286 ASP A CB  1 
ATOM   1782 C  CG  . ASP A 1 239 ? -3.394  3.104   8.587   1.00 13.91 ? 286 ASP A CG  1 
ATOM   1783 O  OD1 . ASP A 1 239 ? -2.867  2.148   8.002   1.00 14.29 ? 286 ASP A OD1 1 
ATOM   1784 O  OD2 . ASP A 1 239 ? -3.154  3.423   9.772   1.00 14.00 ? 286 ASP A OD2 1 
ATOM   1785 N  N   . ARG A 1 240 ? -5.951  5.053   4.971   1.00 13.69 ? 287 ARG A N   1 
ATOM   1786 C  CA  . ARG A 1 240 ? -7.202  5.392   4.294   1.00 15.03 ? 287 ARG A CA  1 
ATOM   1787 C  C   . ARG A 1 240 ? -7.316  4.781   2.909   1.00 16.78 ? 287 ARG A C   1 
ATOM   1788 O  O   . ARG A 1 240 ? -8.360  4.970   2.264   1.00 19.05 ? 287 ARG A O   1 
ATOM   1789 C  CB  . ARG A 1 240 ? -7.429  6.898   4.229   1.00 16.82 ? 287 ARG A CB  1 
ATOM   1790 C  CG  . ARG A 1 240 ? -6.457  7.698   3.397   1.00 16.91 ? 287 ARG A CG  1 
ATOM   1791 C  CD  . ARG A 1 240 ? -7.024  9.137   3.340   1.00 18.42 ? 287 ARG A CD  1 
ATOM   1792 N  NE  . ARG A 1 240 ? -6.169  9.998   2.529   1.00 17.71 ? 287 ARG A NE  1 
ATOM   1793 C  CZ  . ARG A 1 240 ? -5.069  10.623  2.935   1.00 15.93 ? 287 ARG A CZ  1 
ATOM   1794 N  NH1 . ARG A 1 240 ? -4.211  11.090  2.037   1.00 17.62 ? 287 ARG A NH1 1 
ATOM   1795 N  NH2 . ARG A 1 240 ? -4.762  10.704  4.220   1.00 16.89 ? 287 ARG A NH2 1 
ATOM   1796 N  N   . ALA A 1 241 ? -6.266  4.109   2.429   1.00 15.15 ? 288 ALA A N   1 
ATOM   1797 C  CA  . ALA A 1 241 ? -6.309  3.404   1.171   1.00 15.07 ? 288 ALA A CA  1 
ATOM   1798 C  C   . ALA A 1 241 ? -7.176  2.157   1.280   1.00 16.72 ? 288 ALA A C   1 
ATOM   1799 O  O   . ALA A 1 241 ? -7.262  1.501   2.330   1.00 17.44 ? 288 ALA A O   1 
ATOM   1800 C  CB  . ALA A 1 241 ? -4.893  3.098   0.692   1.00 14.72 ? 288 ALA A CB  1 
ATOM   1801 N  N   . SER A 1 242 ? -7.887  1.841   0.183   1.00 14.87 ? 289 SER A N   1 
ATOM   1802 C  CA  . SER A 1 242 ? -8.658  0.606   0.145   1.00 14.60 ? 289 SER A CA  1 
ATOM   1803 C  C   . SER A 1 242 ? -7.767  -0.625  0.159   1.00 14.07 ? 289 SER A C   1 
ATOM   1804 O  O   . SER A 1 242 ? -6.597  -0.545  -0.183  1.00 13.89 ? 289 SER A O   1 
ATOM   1805 C  CB  . SER A 1 242 ? -9.548  0.526   -1.057  1.00 14.72 ? 289 SER A CB  1 
ATOM   1806 O  OG  . SER A 1 242 ? -8.774  0.506   -2.236  1.00 16.87 ? 289 SER A OG  1 
ATOM   1807 N  N   . LEU A 1 243 ? -8.356  -1.732  0.586   1.00 13.94 ? 290 LEU A N   1 
ATOM   1808 C  CA  . LEU A 1 243 ? -7.713  -3.034  0.528   1.00 14.63 ? 290 LEU A CA  1 
ATOM   1809 C  C   . LEU A 1 243 ? -7.145  -3.287  -0.863  1.00 15.28 ? 290 LEU A C   1 
ATOM   1810 O  O   . LEU A 1 243 ? -6.009  -3.673  -1.034  1.00 15.05 ? 290 LEU A O   1 
ATOM   1811 C  CB  . LEU A 1 243 ? -8.662  -4.151  0.950   1.00 16.61 ? 290 LEU A CB  1 
ATOM   1812 C  CG  . LEU A 1 243 ? -8.061  -5.557  0.973   1.00 17.75 ? 290 LEU A CG  1 
ATOM   1813 C  CD1 . LEU A 1 243 ? -6.860  -5.659  1.918   1.00 18.53 ? 290 LEU A CD1 1 
ATOM   1814 C  CD2 . LEU A 1 243 ? -9.124  -6.582  1.335   1.00 19.57 ? 290 LEU A CD2 1 
ATOM   1815 N  N   . GLN A 1 244 ? -7.962  -3.061  -1.898  1.00 15.42 ? 291 GLN A N   1 
ATOM   1816 C  CA  . GLN A 1 244 ? -7.488  -3.334  -3.239  1.00 16.93 ? 291 GLN A CA  1 
ATOM   1817 C  C   . GLN A 1 244 ? -6.287  -2.465  -3.601  1.00 14.27 ? 291 GLN A C   1 
ATOM   1818 O  O   . GLN A 1 244 ? -5.330  -2.940  -4.200  1.00 15.55 ? 291 GLN A O   1 
ATOM   1819 C  CB  . GLN A 1 244 ? -8.595  -3.105  -4.271  1.00 20.70 ? 291 GLN A CB  1 
ATOM   1820 C  CG  . GLN A 1 244 ? -8.215  -3.642  -5.648  1.00 26.54 ? 291 GLN A CG  1 
ATOM   1821 C  CD  . GLN A 1 244 ? -7.929  -5.134  -5.648  1.00 31.69 ? 291 GLN A CD  1 
ATOM   1822 O  OE1 . GLN A 1 244 ? -8.787  -5.961  -5.313  1.00 36.83 ? 291 GLN A OE1 1 
ATOM   1823 N  NE2 . GLN A 1 244 ? -6.707  -5.515  -6.008  1.00 34.34 ? 291 GLN A NE2 1 
ATOM   1824 N  N   . GLU A 1 245 ? -6.307  -1.188  -3.214  1.00 14.67 ? 292 GLU A N   1 
ATOM   1825 C  CA  A GLU A 1 245 ? -5.201  -0.306  -3.508  0.50 15.36 ? 292 GLU A CA  1 
ATOM   1826 C  CA  B GLU A 1 245 ? -5.213  -0.275  -3.478  0.50 14.70 ? 292 GLU A CA  1 
ATOM   1827 C  C   . GLU A 1 245 ? -3.941  -0.827  -2.825  1.00 14.53 ? 292 GLU A C   1 
ATOM   1828 O  O   . GLU A 1 245 ? -2.866  -0.859  -3.427  1.00 14.43 ? 292 GLU A O   1 
ATOM   1829 C  CB  A GLU A 1 245 ? -5.409  1.129   -3.046  0.50 17.30 ? 292 GLU A CB  1 
ATOM   1830 C  CB  B GLU A 1 245 ? -5.612  1.127   -3.003  0.50 15.73 ? 292 GLU A CB  1 
ATOM   1831 C  CG  A GLU A 1 245 ? -4.262  2.031   -3.493  0.50 20.90 ? 292 GLU A CG  1 
ATOM   1832 C  CG  B GLU A 1 245 ? -6.474  1.916   -4.001  0.50 17.47 ? 292 GLU A CG  1 
ATOM   1833 C  CD  A GLU A 1 245 ? -4.527  3.510   -3.302  0.50 22.71 ? 292 GLU A CD  1 
ATOM   1834 C  CD  B GLU A 1 245 ? -7.264  3.101   -3.453  0.50 21.19 ? 292 GLU A CD  1 
ATOM   1835 O  OE1 A GLU A 1 245 ? -5.651  3.878   -2.881  0.50 27.38 ? 292 GLU A OE1 1 
ATOM   1836 O  OE1 B GLU A 1 245 ? -7.449  3.283   -2.243  0.50 19.65 ? 292 GLU A OE1 1 
ATOM   1837 O  OE2 A GLU A 1 245 ? -3.599  4.278   -3.612  0.50 24.87 ? 292 GLU A OE2 1 
ATOM   1838 O  OE2 B GLU A 1 245 ? -7.707  3.906   -4.293  0.50 30.87 ? 292 GLU A OE2 1 
ATOM   1839 N  N   . GLN A 1 246 ? -4.075  -1.238  -1.562  1.00 13.04 ? 293 GLN A N   1 
ATOM   1840 C  CA  . GLN A 1 246 ? -2.917  -1.747  -0.840  1.00 12.78 ? 293 GLN A CA  1 
ATOM   1841 C  C   . GLN A 1 246 ? -2.323  -2.969  -1.527  1.00 13.33 ? 293 GLN A C   1 
ATOM   1842 O  O   . GLN A 1 246 ? -1.112  -3.106  -1.677  1.00 13.67 ? 293 GLN A O   1 
ATOM   1843 C  CB  . GLN A 1 246 ? -3.273  -2.065  0.590   1.00 11.63 ? 293 GLN A CB  1 
ATOM   1844 C  CG  . GLN A 1 246 ? -3.647  -0.834  1.420   1.00 12.11 ? 293 GLN A CG  1 
ATOM   1845 C  CD  . GLN A 1 246 ? -3.789  -1.144  2.888   1.00 14.12 ? 293 GLN A CD  1 
ATOM   1846 O  OE1 . GLN A 1 246 ? -3.593  -2.269  3.359   1.00 14.21 ? 293 GLN A OE1 1 
ATOM   1847 N  NE2 . GLN A 1 246 ? -4.082  -0.108  3.653   1.00 15.74 ? 293 GLN A NE2 1 
ATOM   1848 N  N   . GLU A 1 247 ? -3.191  -3.920  -1.899  1.00 12.56 ? 294 GLU A N   1 
ATOM   1849 C  CA  . GLU A 1 247 ? -2.716  -5.142  -2.504  1.00 13.13 ? 294 GLU A CA  1 
ATOM   1850 C  C   . GLU A 1 247 ? -2.136  -4.843  -3.866  1.00 12.88 ? 294 GLU A C   1 
ATOM   1851 O  O   . GLU A 1 247 ? -1.157  -5.471  -4.240  1.00 14.35 ? 294 GLU A O   1 
ATOM   1852 C  CB  . GLU A 1 247 ? -3.841  -6.166  -2.585  1.00 12.50 ? 294 GLU A CB  1 
ATOM   1853 C  CG  . GLU A 1 247 ? -4.311  -6.629  -1.214  1.00 13.22 ? 294 GLU A CG  1 
ATOM   1854 C  CD  . GLU A 1 247 ? -5.320  -7.751  -1.192  1.00 15.95 ? 294 GLU A CD  1 
ATOM   1855 O  OE1 . GLU A 1 247 ? -5.960  -7.990  -2.249  1.00 19.51 ? 294 GLU A OE1 1 
ATOM   1856 O  OE2 . GLU A 1 247 ? -5.437  -8.389  -0.148  1.00 14.91 ? 294 GLU A OE2 1 
ATOM   1857 N  N   . ASP A 1 248 ? -2.711  -3.885  -4.585  1.00 13.57 ? 295 ASP A N   1 
ATOM   1858 C  CA  . ASP A 1 248 ? -2.171  -3.540  -5.885  1.00 13.98 ? 295 ASP A CA  1 
ATOM   1859 C  C   . ASP A 1 248 ? -0.800  -2.907  -5.785  1.00 15.04 ? 295 ASP A C   1 
ATOM   1860 O  O   . ASP A 1 248 ? 0.026   -3.033  -6.688  1.00 15.11 ? 295 ASP A O   1 
ATOM   1861 C  CB  . ASP A 1 248 ? -3.102  -2.558  -6.578  1.00 15.54 ? 295 ASP A CB  1 
ATOM   1862 C  CG  . ASP A 1 248 ? -4.349  -3.125  -7.259  1.00 19.73 ? 295 ASP A CG  1 
ATOM   1863 O  OD1 . ASP A 1 248 ? -4.475  -4.335  -7.336  1.00 21.95 ? 295 ASP A OD1 1 
ATOM   1864 O  OD2 . ASP A 1 248 ? -5.228  -2.294  -7.604  1.00 23.41 ? 295 ASP A OD2 1 
ATOM   1865 N  N   . VAL A 1 249 ? -0.551  -2.158  -4.707  1.00 14.48 ? 296 VAL A N   1 
ATOM   1866 C  CA  . VAL A 1 249 ? 0.733   -1.534  -4.505  1.00 14.15 ? 296 VAL A CA  1 
ATOM   1867 C  C   . VAL A 1 249 ? 1.832   -2.596  -4.495  1.00 12.85 ? 296 VAL A C   1 
ATOM   1868 O  O   . VAL A 1 249 ? 2.941   -2.378  -5.012  1.00 14.02 ? 296 VAL A O   1 
ATOM   1869 C  CB  . VAL A 1 249 ? 0.734   -0.694  -3.213  1.00 14.05 ? 296 VAL A CB  1 
ATOM   1870 C  CG1 . VAL A 1 249 ? 2.132   -0.431  -2.675  1.00 15.29 ? 296 VAL A CG1 1 
ATOM   1871 C  CG2 . VAL A 1 249 ? -0.067  0.594   -3.396  1.00 14.79 ? 296 VAL A CG2 1 
ATOM   1872 N  N   . PHE A 1 250 ? 1.568   -3.735  -3.854  1.00 12.62 ? 297 PHE A N   1 
ATOM   1873 C  CA  . PHE A 1 250 ? 2.577   -4.767  -3.673  1.00 12.57 ? 297 PHE A CA  1 
ATOM   1874 C  C   . PHE A 1 250 ? 2.591   -5.835  -4.757  1.00 12.70 ? 297 PHE A C   1 
ATOM   1875 O  O   . PHE A 1 250 ? 3.667   -6.292  -5.146  1.00 14.61 ? 297 PHE A O   1 
ATOM   1876 C  CB  . PHE A 1 250 ? 2.471   -5.403  -2.282  1.00 12.89 ? 297 PHE A CB  1 
ATOM   1877 C  CG  . PHE A 1 250 ? 3.012   -4.473  -1.216  1.00 11.87 ? 297 PHE A CG  1 
ATOM   1878 C  CD1 . PHE A 1 250 ? 4.360   -4.181  -1.207  1.00 12.63 ? 297 PHE A CD1 1 
ATOM   1879 C  CD2 . PHE A 1 250 ? 2.190   -3.888  -0.279  1.00 13.98 ? 297 PHE A CD2 1 
ATOM   1880 C  CE1 . PHE A 1 250 ? 4.874   -3.278  -0.319  1.00 13.12 ? 297 PHE A CE1 1 
ATOM   1881 C  CE2 . PHE A 1 250 ? 2.722   -2.984  0.642   1.00 14.40 ? 297 PHE A CE2 1 
ATOM   1882 C  CZ  . PHE A 1 250 ? 4.052   -2.693  0.604   1.00 14.30 ? 297 PHE A CZ  1 
ATOM   1883 N  N   . GLY A 1 251 ? 1.430   -6.269  -5.197  1.00 12.09 ? 298 GLY A N   1 
ATOM   1884 C  CA  . GLY A 1 251 ? 1.288   -7.411  -6.080  1.00 13.17 ? 298 GLY A CA  1 
ATOM   1885 C  C   . GLY A 1 251 ? 1.103   -8.722  -5.330  1.00 13.81 ? 298 GLY A C   1 
ATOM   1886 O  O   . GLY A 1 251 ? 1.154   -9.791  -5.941  1.00 13.87 ? 298 GLY A O   1 
ATOM   1887 N  N   . ARG A 1 252 ? 0.851   -8.672  -4.008  1.00 13.22 ? 299 ARG A N   1 
ATOM   1888 C  CA  . ARG A 1 252 ? 0.532   -9.820  -3.185  1.00 13.36 ? 299 ARG A CA  1 
ATOM   1889 C  C   . ARG A 1 252 ? -0.703  -9.473  -2.371  1.00 13.08 ? 299 ARG A C   1 
ATOM   1890 O  O   . ARG A 1 252 ? -0.947  -8.293  -2.154  1.00 13.73 ? 299 ARG A O   1 
ATOM   1891 C  CB  . ARG A 1 252 ? 1.670   -10.137 -2.226  1.00 13.35 ? 299 ARG A CB  1 
ATOM   1892 C  CG  . ARG A 1 252 ? 2.861   -10.746 -2.919  1.00 12.91 ? 299 ARG A CG  1 
ATOM   1893 C  CD  . ARG A 1 252 ? 4.013   -11.009 -1.981  1.00 12.60 ? 299 ARG A CD  1 
ATOM   1894 N  NE  . ARG A 1 252 ? 5.134   -11.728 -2.586  1.00 14.26 ? 299 ARG A NE  1 
ATOM   1895 C  CZ  . ARG A 1 252 ? 5.297   -13.026 -2.675  1.00 13.35 ? 299 ARG A CZ  1 
ATOM   1896 N  NH1 . ARG A 1 252 ? 4.405   -13.897 -2.228  1.00 12.82 ? 299 ARG A NH1 1 
ATOM   1897 N  NH2 . ARG A 1 252 ? 6.441   -13.466 -3.167  1.00 15.84 ? 299 ARG A NH2 1 
ATOM   1898 N  N   . ASP A 1 253 ? -1.515  -10.447 -1.990  1.00 12.82 ? 300 ASP A N   1 
ATOM   1899 C  CA  . ASP A 1 253 ? -2.683  -10.216 -1.167  1.00 13.08 ? 300 ASP A CA  1 
ATOM   1900 C  C   . ASP A 1 253 ? -2.213  -9.999  0.265   1.00 13.51 ? 300 ASP A C   1 
ATOM   1901 O  O   . ASP A 1 253 ? -1.142  -10.445 0.681   1.00 13.61 ? 300 ASP A O   1 
ATOM   1902 C  CB  . ASP A 1 253 ? -3.702  -11.346 -1.276  1.00 13.76 ? 300 ASP A CB  1 
ATOM   1903 C  CG  . ASP A 1 253 ? -3.292  -12.595 -0.512  1.00 17.78 ? 300 ASP A CG  1 
ATOM   1904 O  OD1 . ASP A 1 253 ? -2.422  -13.301 -0.957  1.00 24.35 ? 300 ASP A OD1 1 
ATOM   1905 O  OD2 . ASP A 1 253 ? -3.732  -12.780 0.613   1.00 22.43 ? 300 ASP A OD2 1 
ATOM   1906 N  N   . LYS A 1 254 ? -3.089  -9.393  1.070   1.00 12.67 ? 301 LYS A N   1 
ATOM   1907 C  CA  . LYS A 1 254 ? -2.643  -8.961  2.381   1.00 13.96 ? 301 LYS A CA  1 
ATOM   1908 C  C   . LYS A 1 254 ? -2.653  -10.104 3.381   1.00 14.38 ? 301 LYS A C   1 
ATOM   1909 O  O   . LYS A 1 254 ? -1.724  -10.223 4.181   1.00 16.58 ? 301 LYS A O   1 
ATOM   1910 C  CB  . LYS A 1 254 ? -3.438  -7.753  2.840   1.00 13.78 ? 301 LYS A CB  1 
ATOM   1911 C  CG  . LYS A 1 254 ? -2.812  -7.048  4.028   1.00 14.48 ? 301 LYS A CG  1 
ATOM   1912 C  CD  . LYS A 1 254 ? -3.417  -5.681  4.307   1.00 14.57 ? 301 LYS A CD  1 
ATOM   1913 C  CE  . LYS A 1 254 ? -2.578  -4.964  5.311   1.00 13.22 ? 301 LYS A CE  1 
ATOM   1914 N  NZ  . LYS A 1 254 ? -3.136  -3.646  5.610   1.00 13.04 ? 301 LYS A NZ  1 
ATOM   1915 N  N   . GLY A 1 255 ? -3.697  -10.919 3.325   1.00 13.81 ? 302 GLY A N   1 
ATOM   1916 C  CA  . GLY A 1 255 ? -3.940  -11.976 4.304   1.00 15.40 ? 302 GLY A CA  1 
ATOM   1917 C  C   . GLY A 1 255 ? -2.906  -13.092 4.247   1.00 15.06 ? 302 GLY A C   1 
ATOM   1918 O  O   . GLY A 1 255 ? -2.219  -13.398 5.216   1.00 17.68 ? 302 GLY A O   1 
ATOM   1919 N  N   . GLU A 1 256 ? -2.786  -13.712 3.086   1.00 14.87 ? 303 GLU A N   1 
ATOM   1920 C  CA  . GLU A 1 256 ? -1.876  -14.828 2.905   1.00 14.20 ? 303 GLU A CA  1 
ATOM   1921 C  C   . GLU A 1 256 ? -0.509  -14.335 2.440   1.00 13.21 ? 303 GLU A C   1 
ATOM   1922 O  O   . GLU A 1 256 ? 0.507   -14.972 2.715   1.00 13.88 ? 303 GLU A O   1 
ATOM   1923 C  CB  . GLU A 1 256 ? -2.515  -15.786 1.902   1.00 16.26 ? 303 GLU A CB  1 
ATOM   1924 C  CG  . GLU A 1 256 ? -1.600  -16.908 1.413   1.00 16.61 ? 303 GLU A CG  1 
ATOM   1925 C  CD  . GLU A 1 256 ? -1.134  -17.889 2.467   1.00 19.65 ? 303 GLU A CD  1 
ATOM   1926 O  OE1 . GLU A 1 256 ? -1.858  -17.986 3.504   1.00 23.24 ? 303 GLU A OE1 1 
ATOM   1927 O  OE2 . GLU A 1 256 ? -0.131  -18.616 2.296   1.00 17.96 ? 303 GLU A OE2 1 
ATOM   1928 N  N   . GLY A 1 257 ? -0.474  -13.201 1.738   1.00 12.97 ? 304 GLY A N   1 
ATOM   1929 C  CA  . GLY A 1 257 ? 0.747   -12.746 1.126   1.00 12.62 ? 304 GLY A CA  1 
ATOM   1930 C  C   . GLY A 1 257 ? 1.136   -13.570 -0.097  1.00 12.87 ? 304 GLY A C   1 
ATOM   1931 O  O   . GLY A 1 257 ? 2.297   -13.634 -0.440  1.00 13.14 ? 304 GLY A O   1 
ATOM   1932 N  N   . ALA A 1 258 ? 0.138   -14.142 -0.767  1.00 12.37 ? 305 ALA A N   1 
ATOM   1933 C  CA  . ALA A 1 258 ? 0.397   -14.873 -2.014  1.00 12.85 ? 305 ALA A CA  1 
ATOM   1934 C  C   . ALA A 1 258 ? 0.538   -13.866 -3.125  1.00 12.83 ? 305 ALA A C   1 
ATOM   1935 O  O   . ALA A 1 258 ? -0.092  -12.818 -3.134  1.00 13.30 ? 305 ALA A O   1 
ATOM   1936 C  CB  . ALA A 1 258 ? -0.726  -15.834 -2.323  1.00 14.59 ? 305 ALA A CB  1 
ATOM   1937 N  N   . PRO A 1 259 ? 1.318   -14.183 -4.164  1.00 13.08 ? 306 PRO A N   1 
ATOM   1938 C  CA  . PRO A 1 259 ? 1.268   -13.387 -5.375  1.00 13.41 ? 306 PRO A CA  1 
ATOM   1939 C  C   . PRO A 1 259 ? -0.146  -13.307 -5.923  1.00 14.36 ? 306 PRO A C   1 
ATOM   1940 O  O   . PRO A 1 259 ? -0.897  -14.277 -5.775  1.00 15.28 ? 306 PRO A O   1 
ATOM   1941 C  CB  . PRO A 1 259 ? 2.189   -14.130 -6.360  1.00 15.81 ? 306 PRO A CB  1 
ATOM   1942 C  CG  . PRO A 1 259 ? 2.965   -15.106 -5.534  1.00 16.31 ? 306 PRO A CG  1 
ATOM   1943 C  CD  . PRO A 1 259 ? 2.099   -15.416 -4.313  1.00 14.17 ? 306 PRO A CD  1 
ATOM   1944 N  N   . VAL A 1 260 ? -0.514  -12.184 -6.511  1.00 14.66 ? 307 VAL A N   1 
ATOM   1945 C  CA  . VAL A 1 260 ? -1.847  -11.986 -7.044  1.00 17.01 ? 307 VAL A CA  1 
ATOM   1946 C  C   . VAL A 1 260 ? -2.198  -13.174 -7.939  1.00 16.63 ? 307 VAL A C   1 
ATOM   1947 O  O   . VAL A 1 260 ? -1.396  -13.617 -8.745  1.00 17.29 ? 307 VAL A O   1 
ATOM   1948 C  CB  . VAL A 1 260 ? -1.937  -10.641 -7.782  1.00 19.90 ? 307 VAL A CB  1 
ATOM   1949 C  CG1 . VAL A 1 260 ? -1.033  -10.558 -9.000  1.00 22.10 ? 307 VAL A CG1 1 
ATOM   1950 C  CG2 . VAL A 1 260 ? -3.377  -10.310 -8.143  1.00 21.96 ? 307 VAL A CG2 1 
ATOM   1951 N  N   . GLY A 1 261 ? -3.405  -13.688 -7.729  1.00 16.78 ? 308 GLY A N   1 
ATOM   1952 C  CA  . GLY A 1 261 ? -3.904  -14.817 -8.522  1.00 17.52 ? 308 GLY A CA  1 
ATOM   1953 C  C   . GLY A 1 261 ? -3.690  -16.158 -7.840  1.00 19.20 ? 308 GLY A C   1 
ATOM   1954 O  O   . GLY A 1 261 ? -4.447  -17.116 -8.091  1.00 22.31 ? 308 GLY A O   1 
ATOM   1955 N  N   . LYS A 1 262 ? -2.668  -16.263 -6.995  1.00 15.70 ? 309 LYS A N   1 
ATOM   1956 C  CA  . LYS A 1 262 ? -2.269  -17.537 -6.443  1.00 15.18 ? 309 LYS A CA  1 
ATOM   1957 C  C   . LYS A 1 262 ? -2.736  -17.709 -5.009  1.00 16.08 ? 309 LYS A C   1 
ATOM   1958 O  O   . LYS A 1 262 ? -3.235  -16.771 -4.406  1.00 17.75 ? 309 LYS A O   1 
ATOM   1959 C  CB  . LYS A 1 262 ? -0.754  -17.703 -6.602  1.00 14.89 ? 309 LYS A CB  1 
ATOM   1960 C  CG  . LYS A 1 262 ? -0.306  -17.765 -8.032  1.00 16.07 ? 309 LYS A CG  1 
ATOM   1961 C  CD  . LYS A 1 262 ? 1.094   -18.287 -8.203  1.00 15.08 ? 309 LYS A CD  1 
ATOM   1962 C  CE  . LYS A 1 262 ? 1.477   -18.551 -9.599  1.00 15.51 ? 309 LYS A CE  1 
ATOM   1963 N  NZ  . LYS A 1 262 ? 2.792   -19.135 -9.706  1.00 14.61 ? 309 LYS A NZ  1 
ATOM   1964 N  N   . ALA A 1 263 ? -2.561  -18.912 -4.482  1.00 16.44 ? 310 ALA A N   1 
ATOM   1965 C  CA  . ALA A 1 263 ? -3.204  -19.322 -3.248  1.00 17.49 ? 310 ALA A CA  1 
ATOM   1966 C  C   . ALA A 1 263 ? -2.290  -19.194 -2.035  1.00 15.89 ? 310 ALA A C   1 
ATOM   1967 O  O   . ALA A 1 263 ? -2.773  -19.016 -0.926  1.00 18.38 ? 310 ALA A O   1 
ATOM   1968 C  CB  . ALA A 1 263 ? -3.679  -20.757 -3.386  1.00 21.65 ? 310 ALA A CB  1 
ATOM   1969 N  N   . LYS A 1 264 ? -0.978  -19.379 -2.197  1.00 14.34 ? 311 LYS A N   1 
ATOM   1970 C  CA  . LYS A 1 264 ? -0.103  -19.537 -1.058  1.00 14.87 ? 311 LYS A CA  1 
ATOM   1971 C  C   . LYS A 1 264 ? 1.073   -18.567 -1.133  1.00 13.27 ? 311 LYS A C   1 
ATOM   1972 O  O   . LYS A 1 264 ? 1.509   -18.211 -2.205  1.00 14.02 ? 311 LYS A O   1 
ATOM   1973 C  CB  . LYS A 1 264 ? 0.475   -20.951 -0.984  1.00 17.98 ? 311 LYS A CB  1 
ATOM   1974 C  CG  . LYS A 1 264 ? -0.610  -22.009 -0.822  1.00 20.54 ? 311 LYS A CG  1 
ATOM   1975 C  CD  . LYS A 1 264 ? -1.292  -21.964 0.530   1.00 24.35 ? 311 LYS A CD  1 
ATOM   1976 C  CE  . LYS A 1 264 ? -2.494  -22.830 0.500   1.00 29.96 ? 311 LYS A CE  1 
ATOM   1977 N  NZ  . LYS A 1 264 ? -3.245  -22.713 1.730   1.00 30.54 ? 311 LYS A NZ  1 
ATOM   1978 N  N   . GLU A 1 265 ? 1.525   -18.151 0.033   1.00 14.86 ? 312 GLU A N   1 
ATOM   1979 C  CA  . GLU A 1 265 ? 2.625   -17.227 0.191   1.00 12.90 ? 312 GLU A CA  1 
ATOM   1980 C  C   . GLU A 1 265 ? 3.805   -17.558 -0.707  1.00 13.08 ? 312 GLU A C   1 
ATOM   1981 O  O   . GLU A 1 265 ? 4.370   -16.674 -1.333  1.00 14.11 ? 312 GLU A O   1 
ATOM   1982 C  CB  . GLU A 1 265 ? 3.019   -17.190 1.662   1.00 12.62 ? 312 GLU A CB  1 
ATOM   1983 C  CG  . GLU A 1 265 ? 4.114   -16.159 1.942   1.00 13.30 ? 312 GLU A CG  1 
ATOM   1984 C  CD  . GLU A 1 265 ? 4.722   -16.209 3.309   1.00 13.85 ? 312 GLU A CD  1 
ATOM   1985 O  OE1 . GLU A 1 265 ? 4.120   -16.844 4.209   1.00 14.84 ? 312 GLU A OE1 1 
ATOM   1986 O  OE2 . GLU A 1 265 ? 5.835   -15.667 3.437   1.00 13.70 ? 312 GLU A OE2 1 
ATOM   1987 N  N   . ARG A 1 266 ? 4.230   -18.811 -0.686  1.00 13.51 ? 313 ARG A N   1 
ATOM   1988 C  CA  . ARG A 1 266 ? 5.485   -19.208 -1.296  1.00 14.26 ? 313 ARG A CA  1 
ATOM   1989 C  C   . ARG A 1 266 ? 5.325   -19.697 -2.733  1.00 13.17 ? 313 ARG A C   1 
ATOM   1990 O  O   . ARG A 1 266 ? 6.319   -20.137 -3.305  1.00 15.31 ? 313 ARG A O   1 
ATOM   1991 C  CB  . ARG A 1 266 ? 6.227   -20.218 -0.429  1.00 14.25 ? 313 ARG A CB  1 
ATOM   1992 C  CG  . ARG A 1 266 ? 6.668   -19.494 0.837   1.00 16.57 ? 313 ARG A CG  1 
ATOM   1993 C  CD  . ARG A 1 266 ? 7.678   -20.265 1.637   1.00 19.85 ? 313 ARG A CD  1 
ATOM   1994 N  NE  . ARG A 1 266 ? 8.176   -19.450 2.749   1.00 21.82 ? 313 ARG A NE  1 
ATOM   1995 C  CZ  . ARG A 1 266 ? 9.049   -18.445 2.653   1.00 20.33 ? 313 ARG A CZ  1 
ATOM   1996 N  NH1 . ARG A 1 266 ? 9.750   -18.238 1.556   1.00 21.66 ? 313 ARG A NH1 1 
ATOM   1997 N  NH2 . ARG A 1 266 ? 9.294   -17.733 3.731   1.00 23.79 ? 313 ARG A NH2 1 
ATOM   1998 N  N   . ASP A 1 267 ? 4.107   -19.635 -3.277  1.00 12.93 ? 314 ASP A N   1 
ATOM   1999 C  CA  . ASP A 1 267 ? 3.945   -19.837 -4.699  1.00 13.76 ? 314 ASP A CA  1 
ATOM   2000 C  C   . ASP A 1 267 ? 4.734   -18.756 -5.424  1.00 15.69 ? 314 ASP A C   1 
ATOM   2001 O  O   . ASP A 1 267 ? 4.843   -17.613 -4.941  1.00 15.11 ? 314 ASP A O   1 
ATOM   2002 C  CB  . ASP A 1 267 ? 2.498   -19.854 -5.110  1.00 14.61 ? 314 ASP A CB  1 
ATOM   2003 C  CG  . ASP A 1 267 ? 1.661   -21.011 -4.579  1.00 15.80 ? 314 ASP A CG  1 
ATOM   2004 O  OD1 . ASP A 1 267 ? 2.250   -22.052 -4.199  1.00 17.94 ? 314 ASP A OD1 1 
ATOM   2005 O  OD2 . ASP A 1 267 ? 0.416   -20.829 -4.564  1.00 17.87 ? 314 ASP A OD2 1 
ATOM   2006 N  N   . GLU A 1 268 ? 5.256   -19.089 -6.603  1.00 13.59 ? 315 GLU A N   1 
ATOM   2007 C  CA  . GLU A 1 268 ? 6.139   -18.154 -7.289  1.00 14.11 ? 315 GLU A CA  1 
ATOM   2008 C  C   . GLU A 1 268 ? 5.331   -17.039 -7.904  1.00 14.18 ? 315 GLU A C   1 
ATOM   2009 O  O   . GLU A 1 268 ? 4.282   -17.232 -8.519  1.00 14.94 ? 315 GLU A O   1 
ATOM   2010 C  CB  . GLU A 1 268 ? 6.941   -18.893 -8.353  1.00 18.24 ? 315 GLU A CB  1 
ATOM   2011 C  CG  . GLU A 1 268 ? 8.078   -19.662 -7.686  1.00 23.62 ? 315 GLU A CG  1 
ATOM   2012 C  CD  . GLU A 1 268 ? 9.080   -18.926 -6.809  1.00 27.47 ? 315 GLU A CD  1 
ATOM   2013 O  OE1 . GLU A 1 268 ? 9.645   -19.642 -5.955  1.00 35.57 ? 315 GLU A OE1 1 
ATOM   2014 O  OE2 . GLU A 1 268 ? 9.320   -17.691 -6.890  1.00 29.74 ? 315 GLU A OE2 1 
ATOM   2015 N  N   . PRO A 1 269 ? 5.808   -15.794 -7.832  1.00 13.80 ? 316 PRO A N   1 
ATOM   2016 C  CA  . PRO A 1 269 ? 5.118   -14.725 -8.509  1.00 14.45 ? 316 PRO A CA  1 
ATOM   2017 C  C   . PRO A 1 269 ? 5.017   -14.932 -10.005 1.00 15.55 ? 316 PRO A C   1 
ATOM   2018 O  O   . PRO A 1 269 ? 5.967   -15.399 -10.605 1.00 17.98 ? 316 PRO A O   1 
ATOM   2019 C  CB  . PRO A 1 269 ? 5.929   -13.473 -8.213  1.00 16.75 ? 316 PRO A CB  1 
ATOM   2020 C  CG  . PRO A 1 269 ? 6.994   -13.894 -7.284  1.00 19.30 ? 316 PRO A CG  1 
ATOM   2021 C  CD  . PRO A 1 269 ? 7.005   -15.392 -7.095  1.00 15.46 ? 316 PRO A CD  1 
ATOM   2022 N  N   . PHE A 1 270 ? 3.852   -14.570 -10.527 1.00 15.31 ? 317 PHE A N   1 
ATOM   2023 C  CA  . PHE A 1 270 ? 3.620   -14.439 -11.951 1.00 15.21 ? 317 PHE A CA  1 
ATOM   2024 C  C   . PHE A 1 270 ? 3.505   -12.945 -12.225 1.00 14.29 ? 317 PHE A C   1 
ATOM   2025 O  O   . PHE A 1 270 ? 2.471   -12.343 -12.002 1.00 15.83 ? 317 PHE A O   1 
ATOM   2026 C  CB  . PHE A 1 270 ? 2.439   -15.303 -12.366 1.00 16.44 ? 317 PHE A CB  1 
ATOM   2027 C  CG  . PHE A 1 270 ? 2.207   -15.280 -13.864 1.00 17.86 ? 317 PHE A CG  1 
ATOM   2028 C  CD1 . PHE A 1 270 ? 2.958   -16.082 -14.703 1.00 20.65 ? 317 PHE A CD1 1 
ATOM   2029 C  CD2 . PHE A 1 270 ? 1.195   -14.504 -14.401 1.00 20.91 ? 317 PHE A CD2 1 
ATOM   2030 C  CE1 . PHE A 1 270 ? 2.745   -16.056 -16.075 1.00 22.55 ? 317 PHE A CE1 1 
ATOM   2031 C  CE2 . PHE A 1 270 ? 0.978   -14.478 -15.768 1.00 22.24 ? 317 PHE A CE2 1 
ATOM   2032 C  CZ  . PHE A 1 270 ? 1.748   -15.260 -16.600 1.00 22.48 ? 317 PHE A CZ  1 
ATOM   2033 N  N   . LEU A 1 271 ? 4.604   -12.368 -12.668 1.00 15.04 ? 318 LEU A N   1 
ATOM   2034 C  CA  . LEU A 1 271 ? 4.764   -10.910 -12.630 1.00 14.89 ? 318 LEU A CA  1 
ATOM   2035 C  C   . LEU A 1 271 ? 3.788   -10.195 -13.570 1.00 16.35 ? 318 LEU A C   1 
ATOM   2036 O  O   . LEU A 1 271 ? 3.325   -9.094  -13.277 1.00 17.32 ? 318 LEU A O   1 
ATOM   2037 C  CB  . LEU A 1 271 ? 6.207   -10.526 -12.936 1.00 17.95 ? 318 LEU A CB  1 
ATOM   2038 C  CG  . LEU A 1 271 ? 7.274   -10.956 -11.921 1.00 20.87 ? 318 LEU A CG  1 
ATOM   2039 C  CD1 . LEU A 1 271 ? 8.631   -10.374 -12.304 1.00 24.25 ? 318 LEU A CD1 1 
ATOM   2040 C  CD2 . LEU A 1 271 ? 6.896   -10.604 -10.493 1.00 22.38 ? 318 LEU A CD2 1 
ATOM   2041 N  N   . LYS A 1 272 ? 3.418   -10.834 -14.681 1.00 18.28 ? 319 LYS A N   1 
ATOM   2042 C  CA  . LYS A 1 272 ? 2.570   -10.163 -15.649 1.00 20.46 ? 319 LYS A CA  1 
ATOM   2043 C  C   . LYS A 1 272 ? 1.165   -9.916  -15.132 1.00 19.41 ? 319 LYS A C   1 
ATOM   2044 O  O   . LYS A 1 272 ? 0.451   -9.089  -15.704 1.00 21.58 ? 319 LYS A O   1 
ATOM   2045 C  CB  . LYS A 1 272 ? 2.532   -10.952 -16.970 1.00 26.95 ? 319 LYS A CB  1 
ATOM   2046 C  CG  . LYS A 1 272 ? 3.780   -10.721 -17.786 1.00 33.23 ? 319 LYS A CG  1 
ATOM   2047 C  CD  . LYS A 1 272 ? 3.853   -11.535 -19.076 1.00 40.26 ? 319 LYS A CD  1 
ATOM   2048 C  CE  . LYS A 1 272 ? 5.235   -11.501 -19.679 1.00 46.96 ? 319 LYS A CE  1 
ATOM   2049 N  NZ  . LYS A 1 272 ? 5.785   -10.145 -19.820 1.00 48.21 ? 319 LYS A NZ  1 
ATOM   2050 N  N   . ALA A 1 273 ? 0.766   -10.594 -14.053 1.00 16.88 ? 320 ALA A N   1 
ATOM   2051 C  CA  . ALA A 1 273 ? -0.546  -10.378 -13.458 1.00 17.31 ? 320 ALA A CA  1 
ATOM   2052 C  C   . ALA A 1 273 ? -0.559  -9.171  -12.503 1.00 16.50 ? 320 ALA A C   1 
ATOM   2053 O  O   . ALA A 1 273 ? -1.622  -8.782  -12.057 1.00 20.89 ? 320 ALA A O   1 
ATOM   2054 C  CB  . ALA A 1 273 ? -1.019  -11.618 -12.742 1.00 18.35 ? 320 ALA A CB  1 
ATOM   2055 N  N   . MET A 1 274 ? 0.621   -8.691  -12.116 1.00 16.51 ? 321 MET A N   1 
ATOM   2056 C  CA  . MET A 1 274 ? 0.726   -7.549  -11.234 1.00 16.68 ? 321 MET A CA  1 
ATOM   2057 C  C   . MET A 1 274 ? 0.629   -6.267  -12.041 1.00 17.64 ? 321 MET A C   1 
ATOM   2058 O  O   . MET A 1 274 ? 0.930   -6.230  -13.229 1.00 18.95 ? 321 MET A O   1 
ATOM   2059 C  CB  . MET A 1 274 ? 2.079   -7.590  -10.531 1.00 16.43 ? 321 MET A CB  1 
ATOM   2060 C  CG  . MET A 1 274 ? 2.215   -8.787  -9.651  1.00 15.62 ? 321 MET A CG  1 
ATOM   2061 S  SD  . MET A 1 274 ? 3.820   -8.857  -8.860  1.00 16.87 ? 321 MET A SD  1 
ATOM   2062 C  CE  . MET A 1 274 ? 3.679   -10.447 -8.063  1.00 16.99 ? 321 MET A CE  1 
ATOM   2063 N  N   . LYS A 1 275 ? 0.259   -5.179  -11.360 1.00 16.41 ? 322 LYS A N   1 
ATOM   2064 C  CA  . LYS A 1 275 ? 0.309   -3.871  -11.969 1.00 16.25 ? 322 LYS A CA  1 
ATOM   2065 C  C   . LYS A 1 275 ? 1.754   -3.559  -12.346 1.00 15.57 ? 322 LYS A C   1 
ATOM   2066 O  O   . LYS A 1 275 ? 2.697   -3.997  -11.700 1.00 16.68 ? 322 LYS A O   1 
ATOM   2067 C  CB  . LYS A 1 275 ? -0.261  -2.790  -11.063 1.00 18.82 ? 322 LYS A CB  1 
ATOM   2068 C  CG  . LYS A 1 275 ? -1.667  -3.014  -10.591 1.00 26.30 ? 322 LYS A CG  1 
ATOM   2069 C  CD  . LYS A 1 275 ? -2.688  -2.983  -11.710 1.00 32.32 ? 322 LYS A CD  1 
ATOM   2070 C  CE  . LYS A 1 275 ? -4.076  -3.221  -11.222 1.00 37.07 ? 322 LYS A CE  1 
ATOM   2071 N  NZ  . LYS A 1 275 ? -4.669  -1.978  -10.713 1.00 42.68 ? 322 LYS A NZ  1 
ATOM   2072 N  N   . PRO A 1 276 ? 1.989   -2.741  -13.395 1.00 17.65 ? 323 PRO A N   1 
ATOM   2073 C  CA  . PRO A 1 276 ? 3.332   -2.450  -13.829 1.00 18.53 ? 323 PRO A CA  1 
ATOM   2074 C  C   . PRO A 1 276 ? 4.168   -1.691  -12.817 1.00 16.67 ? 323 PRO A C   1 
ATOM   2075 O  O   . PRO A 1 276 ? 5.398   -1.729  -12.920 1.00 20.23 ? 323 PRO A O   1 
ATOM   2076 C  CB  . PRO A 1 276 ? 3.156   -1.569  -15.105 1.00 22.89 ? 323 PRO A CB  1 
ATOM   2077 C  CG  . PRO A 1 276 ? 1.682   -1.605  -15.425 1.00 24.69 ? 323 PRO A CG  1 
ATOM   2078 C  CD  . PRO A 1 276 ? 0.936   -2.173  -14.263 1.00 21.48 ? 323 PRO A CD  1 
ATOM   2079 N  N   . ASP A 1 277 ? 3.512   -1.053  -11.849 1.00 15.49 ? 324 ASP A N   1 
ATOM   2080 C  CA  . ASP A 1 277 ? 4.210   -0.268  -10.850 1.00 17.55 ? 324 ASP A CA  1 
ATOM   2081 C  C   . ASP A 1 277 ? 4.165   -0.968  -9.507  1.00 15.69 ? 324 ASP A C   1 
ATOM   2082 O  O   . ASP A 1 277 ? 4.470   -0.346  -8.480  1.00 16.47 ? 324 ASP A O   1 
ATOM   2083 C  CB  . ASP A 1 277 ? 3.647   1.142   -10.697 1.00 19.08 ? 324 ASP A CB  1 
ATOM   2084 C  CG  . ASP A 1 277 ? 2.140   1.254   -10.476 1.00 23.85 ? 324 ASP A CG  1 
ATOM   2085 O  OD1 . ASP A 1 277 ? 1.434   0.218   -10.467 1.00 22.34 ? 324 ASP A OD1 1 
ATOM   2086 O  OD2 . ASP A 1 277 ? 1.656   2.394   -10.245 1.00 26.52 ? 324 ASP A OD2 1 
ATOM   2087 N  N   . ALA A 1 278 ? 3.794   -2.246  -9.483  1.00 14.22 ? 325 ALA A N   1 
ATOM   2088 C  CA  . ALA A 1 278 ? 3.737   -2.969  -8.203  1.00 13.83 ? 325 ALA A CA  1 
ATOM   2089 C  C   . ALA A 1 278 ? 5.160   -3.145  -7.691  1.00 12.47 ? 325 ALA A C   1 
ATOM   2090 O  O   . ALA A 1 278 ? 6.088   -3.468  -8.404  1.00 13.14 ? 325 ALA A O   1 
ATOM   2091 C  CB  . ALA A 1 278 ? 3.047   -4.305  -8.374  1.00 15.25 ? 325 ALA A CB  1 
ATOM   2092 N  N   . HIS A 1 279 ? 5.281   -3.052  -6.361  1.00 12.30 ? 326 HIS A N   1 
ATOM   2093 C  CA  . HIS A 1 279 ? 6.579   -3.166  -5.720  1.00 12.85 ? 326 HIS A CA  1 
ATOM   2094 C  C   . HIS A 1 279 ? 7.289   -4.472  -6.048  1.00 12.58 ? 326 HIS A C   1 
ATOM   2095 O  O   . HIS A 1 279 ? 8.477   -4.445  -6.338  1.00 13.18 ? 326 HIS A O   1 
ATOM   2096 C  CB  . HIS A 1 279 ? 6.407   -2.933  -4.224  1.00 11.90 ? 326 HIS A CB  1 
ATOM   2097 C  CG  . HIS A 1 279 ? 7.662   -2.992  -3.440  1.00 11.78 ? 326 HIS A CG  1 
ATOM   2098 N  ND1 . HIS A 1 279 ? 8.604   -1.993  -3.429  1.00 12.12 ? 326 HIS A ND1 1 
ATOM   2099 C  CD2 . HIS A 1 279 ? 8.143   -3.972  -2.609  1.00 11.73 ? 326 HIS A CD2 1 
ATOM   2100 C  CE1 . HIS A 1 279 ? 9.616   -2.380  -2.649  1.00 12.84 ? 326 HIS A CE1 1 
ATOM   2101 N  NE2 . HIS A 1 279 ? 9.346   -3.556  -2.101  1.00 12.23 ? 326 HIS A NE2 1 
ATOM   2102 N  N   . VAL A 1 280 ? 6.597   -5.602  -5.893  1.00 12.50 ? 327 VAL A N   1 
ATOM   2103 C  CA  . VAL A 1 280 ? 7.219   -6.890  -6.121  1.00 12.91 ? 327 VAL A CA  1 
ATOM   2104 C  C   . VAL A 1 280 ? 7.661   -7.001  -7.561  1.00 14.10 ? 327 VAL A C   1 
ATOM   2105 O  O   . VAL A 1 280 ? 8.723   -7.544  -7.800  1.00 15.04 ? 327 VAL A O   1 
ATOM   2106 C  CB  . VAL A 1 280 ? 6.315   -8.044  -5.693  1.00 13.41 ? 327 VAL A CB  1 
ATOM   2107 C  CG1 . VAL A 1 280 ? 6.849   -9.391  -6.139  1.00 14.88 ? 327 VAL A CG1 1 
ATOM   2108 C  CG2 . VAL A 1 280 ? 6.134   -8.029  -4.178  1.00 14.05 ? 327 VAL A CG2 1 
ATOM   2109 N  N   . ARG A 1 281 ? 6.810   -6.527  -8.471  1.00 13.89 ? 328 ARG A N   1 
ATOM   2110 C  CA  . ARG A 1 281 ? 7.195   -6.609  -9.877  1.00 14.98 ? 328 ARG A CA  1 
ATOM   2111 C  C   . ARG A 1 281 ? 8.493   -5.846  -10.156 1.00 16.23 ? 328 ARG A C   1 
ATOM   2112 O  O   . ARG A 1 281 ? 9.368   -6.353  -10.877 1.00 18.11 ? 328 ARG A O   1 
ATOM   2113 C  CB  . ARG A 1 281 ? 6.014   -6.129  -10.715 1.00 15.51 ? 328 ARG A CB  1 
ATOM   2114 C  CG  . ARG A 1 281 ? 6.315   -6.215  -12.207 1.00 16.91 ? 328 ARG A CG  1 
ATOM   2115 C  CD  . ARG A 1 281 ? 5.038   -6.161  -12.970 1.00 19.60 ? 328 ARG A CD  1 
ATOM   2116 N  NE  . ARG A 1 281 ? 5.321   -6.168  -14.402 1.00 24.55 ? 328 ARG A NE  1 
ATOM   2117 C  CZ  . ARG A 1 281 ? 4.385   -6.150  -15.353 1.00 25.99 ? 328 ARG A CZ  1 
ATOM   2118 N  NH1 . ARG A 1 281 ? 3.121   -6.092  -15.041 1.00 23.02 ? 328 ARG A NH1 1 
ATOM   2119 N  NH2 . ARG A 1 281 ? 4.737   -6.178  -16.624 1.00 30.20 ? 328 ARG A NH2 1 
ATOM   2120 N  N   . LEU A 1 282 ? 8.640   -4.634  -9.605  1.00 13.00 ? 329 LEU A N   1 
ATOM   2121 C  CA  . LEU A 1 282 ? 9.780   -3.788  -9.900  1.00 14.02 ? 329 LEU A CA  1 
ATOM   2122 C  C   . LEU A 1 282 ? 11.028  -4.249  -9.169  1.00 14.47 ? 329 LEU A C   1 
ATOM   2123 O  O   . LEU A 1 282 ? 12.124  -4.044  -9.634  1.00 14.58 ? 329 LEU A O   1 
ATOM   2124 C  CB  . LEU A 1 282 ? 9.425   -2.357  -9.524  1.00 13.59 ? 329 LEU A CB  1 
ATOM   2125 C  CG  . LEU A 1 282 ? 8.378   -1.665  -10.391 1.00 14.94 ? 329 LEU A CG  1 
ATOM   2126 C  CD1 . LEU A 1 282 ? 8.045   -0.332  -9.816  1.00 16.38 ? 329 LEU A CD1 1 
ATOM   2127 C  CD2 . LEU A 1 282 ? 8.889   -1.542  -11.809 1.00 17.50 ? 329 LEU A CD2 1 
ATOM   2128 N  N   . ALA A 1 283 ? 10.847  -4.872  -7.986  1.00 12.98 ? 330 ALA A N   1 
ATOM   2129 C  CA  . ALA A 1 283 ? 11.980  -5.270  -7.164  1.00 14.56 ? 330 ALA A CA  1 
ATOM   2130 C  C   . ALA A 1 283 ? 12.502  -6.651  -7.482  1.00 13.56 ? 330 ALA A C   1 
ATOM   2131 O  O   . ALA A 1 283 ? 13.600  -6.981  -7.029  1.00 14.32 ? 330 ALA A O   1 
ATOM   2132 C  CB  . ALA A 1 283 ? 11.585  -5.206  -5.679  1.00 13.83 ? 330 ALA A CB  1 
ATOM   2133 N  N   . HIS A 1 284 ? 11.717  -7.484  -8.173  1.00 13.72 ? 331 HIS A N   1 
ATOM   2134 C  CA  . HIS A 1 284 ? 12.060  -8.887  -8.388  1.00 14.22 ? 331 HIS A CA  1 
ATOM   2135 C  C   . HIS A 1 284 ? 13.349  -9.001  -9.190  1.00 14.74 ? 331 HIS A C   1 
ATOM   2136 O  O   . HIS A 1 284 ? 13.577  -8.188  -10.068 1.00 15.42 ? 331 HIS A O   1 
ATOM   2137 C  CB  . HIS A 1 284 ? 10.919  -9.539  -9.171  1.00 15.58 ? 331 HIS A CB  1 
ATOM   2138 C  CG  . HIS A 1 284 ? 10.949  -11.007 -9.194  1.00 15.32 ? 331 HIS A CG  1 
ATOM   2139 N  ND1 . HIS A 1 284 ? 11.761  -11.718 -10.071 1.00 16.31 ? 331 HIS A ND1 1 
ATOM   2140 C  CD2 . HIS A 1 284 ? 10.217  -11.932 -8.529  1.00 16.39 ? 331 HIS A CD2 1 
ATOM   2141 C  CE1 . HIS A 1 284 ? 11.556  -13.009 -9.900  1.00 17.55 ? 331 HIS A CE1 1 
ATOM   2142 N  NE2 . HIS A 1 284 ? 10.615  -13.183 -8.974  1.00 17.31 ? 331 HIS A NE2 1 
ATOM   2143 N  N   . PRO A 1 285 ? 14.226  -9.980  -8.892  1.00 14.89 ? 332 PRO A N   1 
ATOM   2144 C  CA  . PRO A 1 285 ? 15.461  -10.176 -9.645  1.00 16.96 ? 332 PRO A CA  1 
ATOM   2145 C  C   . PRO A 1 285 ? 15.250  -10.230 -11.152 1.00 17.39 ? 332 PRO A C   1 
ATOM   2146 O  O   . PRO A 1 285 ? 16.092  -9.692  -11.873 1.00 17.94 ? 332 PRO A O   1 
ATOM   2147 C  CB  . PRO A 1 285 ? 15.977  -11.502 -9.072  1.00 17.02 ? 332 PRO A CB  1 
ATOM   2148 C  CG  . PRO A 1 285 ? 15.522  -11.459 -7.648  1.00 17.68 ? 332 PRO A CG  1 
ATOM   2149 C  CD  . PRO A 1 285 ? 14.133  -10.933 -7.758  1.00 15.07 ? 332 PRO A CD  1 
ATOM   2150 N  N   . ASP A 1 286 ? 14.130  -10.790 -11.600 1.00 18.82 ? 333 ASP A N   1 
ATOM   2151 C  CA  . ASP A 1 286 ? 13.924  -10.971 -13.027 1.00 18.41 ? 333 ASP A CA  1 
ATOM   2152 C  C   . ASP A 1 286 ? 13.701  -9.631  -13.724 1.00 21.86 ? 333 ASP A C   1 
ATOM   2153 O  O   . ASP A 1 286 ? 13.836  -9.562  -14.959 1.00 22.63 ? 333 ASP A O   1 
ATOM   2154 C  CB  . ASP A 1 286 ? 12.738  -11.859 -13.330 1.00 21.75 ? 333 ASP A CB  1 
ATOM   2155 C  CG  . ASP A 1 286 ? 12.902  -13.340 -13.047 1.00 24.71 ? 333 ASP A CG  1 
ATOM   2156 O  OD1 . ASP A 1 286 ? 13.989  -13.768 -12.672 1.00 28.22 ? 333 ASP A OD1 1 
ATOM   2157 O  OD2 . ASP A 1 286 ? 11.911  -14.041 -13.201 1.00 30.48 ? 333 ASP A OD2 1 
ATOM   2158 N  N   . SER A 1 287 ? 13.294  -8.605  -12.955 1.00 17.90 ? 334 SER A N   1 
ATOM   2159 C  CA  . SER A 1 287 ? 13.069  -7.256  -13.437 1.00 16.91 ? 334 SER A CA  1 
ATOM   2160 C  C   . SER A 1 287 ? 14.356  -6.441  -13.355 1.00 18.44 ? 334 SER A C   1 
ATOM   2161 O  O   . SER A 1 287 ? 14.392  -5.335  -13.859 1.00 21.35 ? 334 SER A O   1 
ATOM   2162 C  CB  . SER A 1 287 ? 11.954  -6.523  -12.732 1.00 18.37 ? 334 SER A CB  1 
ATOM   2163 O  OG  . SER A 1 287 ? 10.738  -7.240  -12.843 1.00 21.13 ? 334 SER A OG  1 
ATOM   2164 N  N   . ASN A 1 288 ? 15.444  -6.988  -12.799 1.00 17.60 ? 335 ASN A N   1 
ATOM   2165 C  CA  . ASN A 1 288 ? 16.643  -6.230  -12.498 1.00 16.77 ? 335 ASN A CA  1 
ATOM   2166 C  C   . ASN A 1 288 ? 17.891  -6.977  -12.940 1.00 18.23 ? 335 ASN A C   1 
ATOM   2167 O  O   . ASN A 1 288 ? 18.943  -6.859  -12.320 1.00 20.48 ? 335 ASN A O   1 
ATOM   2168 C  CB  . ASN A 1 288 ? 16.743  -5.932  -11.005 1.00 17.24 ? 335 ASN A CB  1 
ATOM   2169 C  CG  . ASN A 1 288 ? 15.692  -4.948  -10.604 1.00 16.97 ? 335 ASN A CG  1 
ATOM   2170 O  OD1 . ASN A 1 288 ? 15.822  -3.750  -10.872 1.00 19.92 ? 335 ASN A OD1 1 
ATOM   2171 N  ND2 . ASN A 1 288 ? 14.627  -5.396  -9.953  1.00 16.95 ? 335 ASN A ND2 1 
ATOM   2172 N  N   . GLY A 1 289 ? 17.774  -7.710  -14.052 1.00 19.67 ? 336 GLY A N   1 
ATOM   2173 C  CA  . GLY A 1 289 ? 18.898  -8.453  -14.596 1.00 21.70 ? 336 GLY A CA  1 
ATOM   2174 C  C   . GLY A 1 289 ? 19.492  -9.455  -13.614 1.00 20.59 ? 336 GLY A C   1 
ATOM   2175 O  O   . GLY A 1 289 ? 20.673  -9.792  -13.678 1.00 22.48 ? 336 GLY A O   1 
ATOM   2176 N  N   . GLY A 1 290 ? 18.660  -9.961  -12.698 1.00 20.02 ? 337 GLY A N   1 
ATOM   2177 C  CA  . GLY A 1 290 ? 19.082  -10.998 -11.779 1.00 19.38 ? 337 GLY A CA  1 
ATOM   2178 C  C   . GLY A 1 290 ? 19.526  -10.458 -10.412 1.00 17.62 ? 337 GLY A C   1 
ATOM   2179 O  O   . GLY A 1 290 ? 19.921  -11.267 -9.579  1.00 19.89 ? 337 GLY A O   1 
ATOM   2180 N  N   . ALA A 1 291 ? 19.564  -9.133  -10.242 1.00 17.68 ? 338 ALA A N   1 
ATOM   2181 C  CA  . ALA A 1 291 ? 20.035  -8.527  -9.010  1.00 18.43 ? 338 ALA A CA  1 
ATOM   2182 C  C   . ALA A 1 291 ? 19.179  -9.024  -7.853  1.00 16.45 ? 338 ALA A C   1 
ATOM   2183 O  O   . ALA A 1 291 ? 17.939  -8.926  -7.900  1.00 17.17 ? 338 ALA A O   1 
ATOM   2184 C  CB  . ALA A 1 291 ? 19.970  -7.057  -9.103  1.00 18.73 ? 338 ALA A CB  1 
ATOM   2185 N  N   . THR A 1 292 ? 19.880  -9.516  -6.830  1.00 16.52 ? 339 THR A N   1 
ATOM   2186 C  CA  . THR A 1 292 ? 19.252  -10.163 -5.683  1.00 16.00 ? 339 THR A CA  1 
ATOM   2187 C  C   . THR A 1 292 ? 19.946  -9.627  -4.440  1.00 17.09 ? 339 THR A C   1 
ATOM   2188 O  O   . THR A 1 292 ? 21.171  -9.452  -4.434  1.00 19.85 ? 339 THR A O   1 
ATOM   2189 C  CB  . THR A 1 292 ? 19.385  -11.673 -5.794  1.00 17.49 ? 339 THR A CB  1 
ATOM   2190 O  OG1 . THR A 1 292 ? 18.817  -12.170 -7.004  1.00 18.55 ? 339 THR A OG1 1 
ATOM   2191 C  CG2 . THR A 1 292 ? 18.627  -12.401 -4.712  1.00 16.45 ? 339 THR A CG2 1 
ATOM   2192 N  N   . LEU A 1 293 ? 19.158  -9.395  -3.384  1.00 15.08 ? 340 LEU A N   1 
ATOM   2193 C  CA  . LEU A 1 293 ? 19.655  -8.801  -2.154  1.00 16.57 ? 340 LEU A CA  1 
ATOM   2194 C  C   . LEU A 1 293 ? 19.332  -9.714  -0.993  1.00 14.73 ? 340 LEU A C   1 
ATOM   2195 O  O   . LEU A 1 293 ? 18.366  -10.459 -1.043  1.00 16.07 ? 340 LEU A O   1 
ATOM   2196 C  CB  . LEU A 1 293 ? 18.869  -7.512  -1.871  1.00 19.17 ? 340 LEU A CB  1 
ATOM   2197 C  CG  . LEU A 1 293 ? 18.863  -6.419  -2.923  1.00 21.16 ? 340 LEU A CG  1 
ATOM   2198 C  CD1 . LEU A 1 293 ? 17.949  -5.282  -2.503  1.00 24.70 ? 340 LEU A CD1 1 
ATOM   2199 C  CD2 . LEU A 1 293 ? 20.281  -5.914  -3.065  1.00 26.51 ? 340 LEU A CD2 1 
ATOM   2200 N  N   . LEU A 1 294 ? 20.097  -9.596  0.082   1.00 12.25 ? 341 LEU A N   1 
ATOM   2201 C  CA  . LEU A 1 294 ? 19.672  -10.144 1.369   1.00 12.47 ? 341 LEU A CA  1 
ATOM   2202 C  C   . LEU A 1 294 ? 19.138  -9.013  2.248   1.00 12.02 ? 341 LEU A C   1 
ATOM   2203 O  O   . LEU A 1 294 ? 19.874  -8.159  2.693   1.00 13.46 ? 341 LEU A O   1 
ATOM   2204 C  CB  . LEU A 1 294 ? 20.802  -10.929 2.042   1.00 13.09 ? 341 LEU A CB  1 
ATOM   2205 C  CG  . LEU A 1 294 ? 20.422  -11.725 3.278   1.00 13.92 ? 341 LEU A CG  1 
ATOM   2206 C  CD1 . LEU A 1 294 ? 21.527  -12.749 3.499   1.00 16.13 ? 341 LEU A CD1 1 
ATOM   2207 C  CD2 . LEU A 1 294 ? 20.185  -10.881 4.503   1.00 15.21 ? 341 LEU A CD2 1 
ATOM   2208 N  N   . ARG A 1 295 ? 17.830  -8.985  2.437   1.00 11.20 ? 342 ARG A N   1 
ATOM   2209 C  CA  . ARG A 1 295 ? 17.156  -7.961  3.199   1.00 11.03 ? 342 ARG A CA  1 
ATOM   2210 C  C   . ARG A 1 295 ? 17.085  -8.385  4.645   1.00 11.34 ? 342 ARG A C   1 
ATOM   2211 O  O   . ARG A 1 295 ? 16.769  -9.542  4.933   1.00 13.06 ? 342 ARG A O   1 
ATOM   2212 C  CB  . ARG A 1 295 ? 15.735  -7.746  2.679   1.00 11.75 ? 342 ARG A CB  1 
ATOM   2213 C  CG  . ARG A 1 295 ? 15.726  -7.147  1.288   1.00 11.54 ? 342 ARG A CG  1 
ATOM   2214 C  CD  . ARG A 1 295 ? 14.358  -7.004  0.740   1.00 12.33 ? 342 ARG A CD  1 
ATOM   2215 N  NE  . ARG A 1 295 ? 13.873  -8.323  0.356   1.00 12.02 ? 342 ARG A NE  1 
ATOM   2216 C  CZ  . ARG A 1 295 ? 12.672  -8.802  0.548   1.00 12.60 ? 342 ARG A CZ  1 
ATOM   2217 N  NH1 . ARG A 1 295 ? 11.763  -8.095  1.165   1.00 12.31 ? 342 ARG A NH1 1 
ATOM   2218 N  NH2 . ARG A 1 295 ? 12.369  -10.031 0.164   1.00 14.03 ? 342 ARG A NH2 1 
ATOM   2219 N  N   . ARG A 1 296 ? 17.351  -7.459  5.555   1.00 12.08 ? 343 ARG A N   1 
ATOM   2220 C  CA  . ARG A 1 296 ? 17.492  -7.820  6.956   1.00 11.31 ? 343 ARG A CA  1 
ATOM   2221 C  C   . ARG A 1 296 ? 17.011  -6.691  7.857   1.00 11.39 ? 343 ARG A C   1 
ATOM   2222 O  O   . ARG A 1 296 ? 17.569  -6.465  8.921   1.00 12.55 ? 343 ARG A O   1 
ATOM   2223 C  CB  . ARG A 1 296 ? 18.896  -8.340  7.257   1.00 11.43 ? 343 ARG A CB  1 
ATOM   2224 C  CG  . ARG A 1 296 ? 18.945  -9.386  8.363   1.00 11.96 ? 343 ARG A CG  1 
ATOM   2225 C  CD  . ARG A 1 296 ? 20.370  -9.855  8.630   1.00 12.28 ? 343 ARG A CD  1 
ATOM   2226 N  NE  . ARG A 1 296 ? 20.362  -11.024 9.535   1.00 11.42 ? 343 ARG A NE  1 
ATOM   2227 C  CZ  . ARG A 1 296 ? 20.330  -10.960 10.851  1.00 13.00 ? 343 ARG A CZ  1 
ATOM   2228 N  NH1 . ARG A 1 296 ? 20.123  -9.802  11.467  1.00 12.75 ? 343 ARG A NH1 1 
ATOM   2229 N  NH2 . ARG A 1 296 ? 20.445  -12.076 11.558  1.00 12.61 ? 343 ARG A NH2 1 
ATOM   2230 N  N   . GLY A 1 297 ? 15.965  -6.003  7.438   1.00 10.97 ? 344 GLY A N   1 
ATOM   2231 C  CA  . GLY A 1 297 ? 15.501  -4.812  8.154   1.00 12.07 ? 344 GLY A CA  1 
ATOM   2232 C  C   . GLY A 1 297 ? 14.533  -5.086  9.293   1.00 11.00 ? 344 GLY A C   1 
ATOM   2233 O  O   . GLY A 1 297 ? 14.124  -6.197  9.577   1.00 10.50 ? 344 GLY A O   1 
ATOM   2234 N  N   . TYR A 1 298 ? 14.184  -3.972  9.954   1.00 11.23 ? 345 TYR A N   1 
ATOM   2235 C  CA  . TYR A 1 298 ? 13.419  -3.912  11.184  1.00 11.25 ? 345 TYR A CA  1 
ATOM   2236 C  C   . TYR A 1 298 ? 12.477  -2.724  11.121  1.00 11.07 ? 345 TYR A C   1 
ATOM   2237 O  O   . TYR A 1 298 ? 12.816  -1.691  10.527  1.00 12.92 ? 345 TYR A O   1 
ATOM   2238 C  CB  . TYR A 1 298 ? 14.344  -3.737  12.400  1.00 10.91 ? 345 TYR A CB  1 
ATOM   2239 C  CG  . TYR A 1 298 ? 15.107  -5.001  12.753  1.00 11.74 ? 345 TYR A CG  1 
ATOM   2240 C  CD1 . TYR A 1 298 ? 16.227  -5.400  12.041  1.00 12.85 ? 345 TYR A CD1 1 
ATOM   2241 C  CD2 . TYR A 1 298 ? 14.707  -5.782  13.827  1.00 11.84 ? 345 TYR A CD2 1 
ATOM   2242 C  CE1 . TYR A 1 298 ? 16.911  -6.553  12.373  1.00 12.40 ? 345 TYR A CE1 1 
ATOM   2243 C  CE2 . TYR A 1 298 ? 15.370  -6.950  14.158  1.00 12.39 ? 345 TYR A CE2 1 
ATOM   2244 C  CZ  . TYR A 1 298 ? 16.472  -7.331  13.418  1.00 13.31 ? 345 TYR A CZ  1 
ATOM   2245 O  OH  . TYR A 1 298 ? 17.166  -8.505  13.702  1.00 13.39 ? 345 TYR A OH  1 
ATOM   2246 N  N   . SER A 1 299 ? 11.392  -2.814  11.886  1.00 12.01 ? 346 SER A N   1 
ATOM   2247 C  CA  . SER A 1 299 ? 10.454  -1.705  12.059  1.00 11.24 ? 346 SER A CA  1 
ATOM   2248 C  C   . SER A 1 299 ? 10.903  -0.788  13.172  1.00 12.38 ? 346 SER A C   1 
ATOM   2249 O  O   . SER A 1 299 ? 11.518  -1.239  14.153  1.00 12.10 ? 346 SER A O   1 
ATOM   2250 C  CB  . SER A 1 299 ? 9.080   -2.164  12.425  1.00 12.15 ? 346 SER A CB  1 
ATOM   2251 O  OG  . SER A 1 299 ? 8.512   -2.888  11.340  1.00 14.60 ? 346 SER A OG  1 
ATOM   2252 N  N   . PHE A 1 300 ? 10.474  0.472   13.098  1.00 11.55 ? 347 PHE A N   1 
ATOM   2253 C  CA  . PHE A 1 300 ? 10.697  1.389   14.197  1.00 11.81 ? 347 PHE A CA  1 
ATOM   2254 C  C   . PHE A 1 300 ? 9.494   2.300   14.372  1.00 12.52 ? 347 PHE A C   1 
ATOM   2255 O  O   . PHE A 1 300 ? 8.695   2.485   13.473  1.00 12.95 ? 347 PHE A O   1 
ATOM   2256 C  CB  . PHE A 1 300 ? 11.970  2.236   14.030  1.00 12.91 ? 347 PHE A CB  1 
ATOM   2257 C  CG  . PHE A 1 300 ? 11.941  3.245   12.900  1.00 14.95 ? 347 PHE A CG  1 
ATOM   2258 C  CD1 . PHE A 1 300 ? 11.410  4.517   13.064  1.00 17.39 ? 347 PHE A CD1 1 
ATOM   2259 C  CD2 . PHE A 1 300 ? 12.508  2.961   11.671  1.00 15.75 ? 347 PHE A CD2 1 
ATOM   2260 C  CE1 . PHE A 1 300 ? 11.372  5.434   12.006  1.00 20.37 ? 347 PHE A CE1 1 
ATOM   2261 C  CE2 . PHE A 1 300 ? 12.508  3.870   10.645  1.00 18.60 ? 347 PHE A CE2 1 
ATOM   2262 C  CZ  . PHE A 1 300 ? 11.932  5.097   10.801  1.00 20.95 ? 347 PHE A CZ  1 
ATOM   2263 N  N   . THR A 1 301 ? 9.375   2.838   15.596  1.00 13.93 ? 348 THR A N   1 
ATOM   2264 C  CA  . THR A 1 301 ? 8.517   3.981   15.870  1.00 15.05 ? 348 THR A CA  1 
ATOM   2265 C  C   . THR A 1 301 ? 9.224   4.818   16.902  1.00 19.13 ? 348 THR A C   1 
ATOM   2266 O  O   . THR A 1 301 ? 9.593   4.297   17.958  1.00 22.54 ? 348 THR A O   1 
ATOM   2267 C  CB  . THR A 1 301 ? 7.137   3.548   16.318  1.00 18.96 ? 348 THR A CB  1 
ATOM   2268 O  OG1 . THR A 1 301 ? 6.447   4.774   16.605  1.00 20.10 ? 348 THR A OG1 1 
ATOM   2269 C  CG2 . THR A 1 301 ? 7.085   2.635   17.530  1.00 18.50 ? 348 THR A CG2 1 
ATOM   2270 N  N   . ASP A 1 302 ? 9.401   6.093   16.575  1.00 19.27 ? 349 ASP A N   1 
ATOM   2271 C  CA  . ASP A 1 302 ? 10.166  6.985   17.436  1.00 23.13 ? 349 ASP A CA  1 
ATOM   2272 C  C   . ASP A 1 302 ? 9.215   8.101   17.848  1.00 25.42 ? 349 ASP A C   1 
ATOM   2273 O  O   . ASP A 1 302 ? 9.333   9.239   17.410  1.00 36.50 ? 349 ASP A O   1 
ATOM   2274 C  CB  . ASP A 1 302 ? 11.428  7.500   16.740  1.00 31.68 ? 349 ASP A CB  1 
ATOM   2275 C  CG  . ASP A 1 302 ? 12.480  6.463   16.340  1.00 34.05 ? 349 ASP A CG  1 
ATOM   2276 O  OD1 . ASP A 1 302 ? 12.505  5.333   16.896  1.00 35.17 ? 349 ASP A OD1 1 
ATOM   2277 O  OD2 . ASP A 1 302 ? 13.249  6.756   15.411  1.00 46.53 ? 349 ASP A OD2 1 
ATOM   2278 N  N   . GLY A 1 303 ? 8.166   7.720   18.544  1.00 19.56 ? 350 GLY A N   1 
ATOM   2279 C  CA  . GLY A 1 303 ? 7.299   8.678   19.195  1.00 19.33 ? 350 GLY A CA  1 
ATOM   2280 C  C   . GLY A 1 303 ? 6.139   9.109   18.306  1.00 16.98 ? 350 GLY A C   1 
ATOM   2281 O  O   . GLY A 1 303 ? 5.528   8.344   17.582  1.00 20.03 ? 350 GLY A O   1 
ATOM   2282 N  N   . THR A 1 304 ? 5.757   10.364  18.484  1.00 19.39 ? 351 THR A N   1 
ATOM   2283 C  CA  . THR A 1 304 ? 4.801   10.988  17.597  1.00 17.90 ? 351 THR A CA  1 
ATOM   2284 C  C   . THR A 1 304 ? 5.544   11.936  16.666  1.00 21.20 ? 351 THR A C   1 
ATOM   2285 O  O   . THR A 1 304 ? 6.728   12.285  16.827  1.00 23.86 ? 351 THR A O   1 
ATOM   2286 C  CB  . THR A 1 304 ? 3.728   11.706  18.394  1.00 23.74 ? 351 THR A CB  1 
ATOM   2287 O  OG1 . THR A 1 304 ? 4.417   12.738  19.085  1.00 28.75 ? 351 THR A OG1 1 
ATOM   2288 C  CG2 . THR A 1 304 ? 2.985   10.783  19.324  1.00 21.94 ? 351 THR A CG2 1 
ATOM   2289 N  N   . ASP A 1 305 ? 4.806   12.400  15.665  1.00 19.57 ? 352 ASP A N   1 
ATOM   2290 C  CA  . ASP A 1 305 ? 5.380   13.300  14.678  1.00 20.35 ? 352 ASP A CA  1 
ATOM   2291 C  C   . ASP A 1 305 ? 5.091   14.761  15.006  1.00 20.21 ? 352 ASP A C   1 
ATOM   2292 O  O   . ASP A 1 305 ? 5.423   15.633  14.185  1.00 22.46 ? 352 ASP A O   1 
ATOM   2293 C  CB  . ASP A 1 305 ? 4.828   13.033  13.297  1.00 19.28 ? 352 ASP A CB  1 
ATOM   2294 C  CG  . ASP A 1 305 ? 3.325   13.088  13.114  1.00 19.41 ? 352 ASP A CG  1 
ATOM   2295 O  OD1 . ASP A 1 305 ? 2.604   13.474  14.068  1.00 17.14 ? 352 ASP A OD1 1 
ATOM   2296 O  OD2 . ASP A 1 305 ? 2.902   12.648  12.023  1.00 20.42 ? 352 ASP A OD2 1 
ATOM   2297 N  N   . GLY A 1 306 ? 4.462   15.045  16.143  1.00 17.66 ? 353 GLY A N   1 
ATOM   2298 C  CA  . GLY A 1 306 ? 4.108   16.392  16.547  1.00 18.37 ? 353 GLY A CA  1 
ATOM   2299 C  C   . GLY A 1 306 ? 2.865   16.969  15.867  1.00 18.65 ? 353 GLY A C   1 
ATOM   2300 O  O   . GLY A 1 306 ? 2.450   18.091  16.158  1.00 22.79 ? 353 GLY A O   1 
ATOM   2301 N  N   . LEU A 1 307 ? 2.246   16.158  15.001  1.00 16.70 ? 354 LEU A N   1 
ATOM   2302 C  CA  . LEU A 1 307 ? 1.021   16.518  14.282  1.00 17.79 ? 354 LEU A CA  1 
ATOM   2303 C  C   . LEU A 1 307 ? -0.091  15.548  14.652  1.00 16.84 ? 354 LEU A C   1 
ATOM   2304 O  O   . LEU A 1 307 ? -1.011  15.379  13.896  1.00 17.27 ? 354 LEU A O   1 
ATOM   2305 C  CB  . LEU A 1 307 ? 1.275   16.469  12.782  1.00 19.43 ? 354 LEU A CB  1 
ATOM   2306 C  CG  . LEU A 1 307 ? 2.385   17.415  12.299  1.00 24.02 ? 354 LEU A CG  1 
ATOM   2307 C  CD1 . LEU A 1 307 ? 3.006   16.940  11.016  1.00 27.69 ? 354 LEU A CD1 1 
ATOM   2308 C  CD2 . LEU A 1 307 ? 1.725   18.776  12.142  1.00 26.84 ? 354 LEU A CD2 1 
ATOM   2309 N  N   . GLY A 1 308 ? -0.032  14.914  15.822  1.00 14.24 ? 355 GLY A N   1 
ATOM   2310 C  CA  . GLY A 1 308 ? -1.168  14.156  16.301  1.00 14.38 ? 355 GLY A CA  1 
ATOM   2311 C  C   . GLY A 1 308 ? -1.118  12.689  15.911  1.00 13.01 ? 355 GLY A C   1 
ATOM   2312 O  O   . GLY A 1 308 ? -2.090  11.988  16.133  1.00 13.27 ? 355 GLY A O   1 
ATOM   2313 N  N   . ARG A 1 309 ? -0.006  12.217  15.346  1.00 13.33 ? 356 ARG A N   1 
ATOM   2314 C  CA  . ARG A 1 309 ? 0.045   10.871  14.782  1.00 13.07 ? 356 ARG A CA  1 
ATOM   2315 C  C   . ARG A 1 309 ? 1.249   10.098  15.292  1.00 14.62 ? 356 ARG A C   1 
ATOM   2316 O  O   . ARG A 1 309 ? 2.251   10.669  15.667  1.00 14.14 ? 356 ARG A O   1 
ATOM   2317 C  CB  . ARG A 1 309 ? 0.220   10.928  13.260  1.00 14.71 ? 356 ARG A CB  1 
ATOM   2318 C  CG  . ARG A 1 309 ? -0.901  11.718  12.594  1.00 15.18 ? 356 ARG A CG  1 
ATOM   2319 C  CD  . ARG A 1 309 ? -0.744  11.819  11.113  1.00 14.89 ? 356 ARG A CD  1 
ATOM   2320 N  NE  . ARG A 1 309 ? 0.506   12.515  10.833  1.00 16.46 ? 356 ARG A NE  1 
ATOM   2321 C  CZ  . ARG A 1 309 ? 0.944   12.667  9.614   1.00 15.08 ? 356 ARG A CZ  1 
ATOM   2322 N  NH1 . ARG A 1 309 ? 0.142   12.435  8.590   1.00 15.98 ? 356 ARG A NH1 1 
ATOM   2323 N  NH2 . ARG A 1 309 ? 2.143   13.145  9.454   1.00 18.21 ? 356 ARG A NH2 1 
ATOM   2324 N  N   . LEU A 1 310 ? 1.163   8.774   15.286  1.00 13.95 ? 357 LEU A N   1 
ATOM   2325 C  CA  . LEU A 1 310 ? 2.342   7.983   15.549  1.00 16.32 ? 357 LEU A CA  1 
ATOM   2326 C  C   . LEU A 1 310 ? 3.347   8.131   14.427  1.00 16.58 ? 357 LEU A C   1 
ATOM   2327 O  O   . LEU A 1 310 ? 2.928   8.197   13.286  1.00 19.27 ? 357 LEU A O   1 
ATOM   2328 C  CB  . LEU A 1 310 ? 1.972   6.509   15.624  1.00 18.43 ? 357 LEU A CB  1 
ATOM   2329 C  CG  . LEU A 1 310 ? 1.083   6.082   16.771  1.00 21.45 ? 357 LEU A CG  1 
ATOM   2330 C  CD1 . LEU A 1 310 ? 0.790   4.619   16.560  1.00 23.74 ? 357 LEU A CD1 1 
ATOM   2331 C  CD2 . LEU A 1 310 ? 1.813   6.263   18.078  1.00 24.26 ? 357 LEU A CD2 1 
ATOM   2332 N  N   . ASP A 1 311 ? 4.619   8.124   14.779  1.00 16.30 ? 358 ASP A N   1 
ATOM   2333 C  CA  . ASP A 1 311 ? 5.706   8.040   13.835  1.00 19.86 ? 358 ASP A CA  1 
ATOM   2334 C  C   . ASP A 1 311 ? 5.867   6.553   13.533  1.00 22.27 ? 358 ASP A C   1 
ATOM   2335 O  O   . ASP A 1 311 ? 5.609   5.681   14.367  1.00 26.26 ? 358 ASP A O   1 
ATOM   2336 C  CB  . ASP A 1 311 ? 6.961   8.584   14.476  1.00 25.79 ? 358 ASP A CB  1 
ATOM   2337 C  CG  . ASP A 1 311 ? 8.189   8.240   13.661  1.00 31.18 ? 358 ASP A CG  1 
ATOM   2338 O  OD1 . ASP A 1 311 ? 8.378   8.957   12.670  1.00 28.97 ? 358 ASP A OD1 1 
ATOM   2339 O  OD2 . ASP A 1 311 ? 8.875   7.245   14.018  1.00 31.76 ? 358 ASP A OD2 1 
ATOM   2340 N  N   . ALA A 1 312 ? 6.181   6.219   12.302  1.00 16.38 ? 359 ALA A N   1 
ATOM   2341 C  CA  . ALA A 1 312 ? 6.343   4.802   11.989  1.00 18.94 ? 359 ALA A CA  1 
ATOM   2342 C  C   . ALA A 1 312 ? 7.265   4.727   10.802  1.00 16.02 ? 359 ALA A C   1 
ATOM   2343 O  O   . ALA A 1 312 ? 7.248   5.576   9.917   1.00 16.71 ? 359 ALA A O   1 
ATOM   2344 C  CB  . ALA A 1 312 ? 5.036   4.144   11.678  1.00 23.68 ? 359 ALA A CB  1 
ATOM   2345 N  N   . GLY A 1 313 ? 8.096   3.699   10.782  1.00 13.83 ? 360 GLY A N   1 
ATOM   2346 C  CA  . GLY A 1 313 ? 8.899   3.479   9.623   1.00 16.10 ? 360 GLY A CA  1 
ATOM   2347 C  C   . GLY A 1 313 ? 9.549   2.100   9.645   1.00 13.67 ? 360 GLY A C   1 
ATOM   2348 O  O   . GLY A 1 313 ? 9.209   1.208   10.420  1.00 13.56 ? 360 GLY A O   1 
ATOM   2349 N  N   . LEU A 1 314 ? 10.452  2.000   8.698   1.00 11.85 ? 361 LEU A N   1 
ATOM   2350 C  CA  . LEU A 1 314 ? 11.174  0.772   8.438   1.00 11.78 ? 361 LEU A CA  1 
ATOM   2351 C  C   . LEU A 1 314 ? 12.631  1.132   8.272   1.00 11.48 ? 361 LEU A C   1 
ATOM   2352 O  O   . LEU A 1 314 ? 12.981  1.995   7.489   1.00 12.24 ? 361 LEU A O   1 
ATOM   2353 C  CB  . LEU A 1 314 ? 10.563  0.059   7.230   1.00 13.70 ? 361 LEU A CB  1 
ATOM   2354 C  CG  . LEU A 1 314 ? 10.916  -1.412  7.059   1.00 14.79 ? 361 LEU A CG  1 
ATOM   2355 C  CD1 . LEU A 1 314 ? 9.829   -2.165  6.370   1.00 13.99 ? 361 LEU A CD1 1 
ATOM   2356 C  CD2 . LEU A 1 314 ? 12.209  -1.573  6.320   1.00 16.73 ? 361 LEU A CD2 1 
ATOM   2357 N  N   . PHE A 1 315 ? 13.493  0.465   9.035   1.00 10.70 ? 362 PHE A N   1 
ATOM   2358 C  CA  . PHE A 1 315 ? 14.923  0.628   8.927   1.00 11.95 ? 362 PHE A CA  1 
ATOM   2359 C  C   . PHE A 1 315 ? 15.388  -0.500  8.022   1.00 11.48 ? 362 PHE A C   1 
ATOM   2360 O  O   . PHE A 1 315 ? 15.514  -1.661  8.422   1.00 12.79 ? 362 PHE A O   1 
ATOM   2361 C  CB  . PHE A 1 315 ? 15.577  0.673   10.294  1.00 12.92 ? 362 PHE A CB  1 
ATOM   2362 C  CG  . PHE A 1 315 ? 17.061  0.974   10.239  1.00 14.71 ? 362 PHE A CG  1 
ATOM   2363 C  CD1 . PHE A 1 315 ? 17.494  2.226   9.831   1.00 16.23 ? 362 PHE A CD1 1 
ATOM   2364 C  CD2 . PHE A 1 315 ? 18.017  0.062   10.659  1.00 15.85 ? 362 PHE A CD2 1 
ATOM   2365 C  CE1 . PHE A 1 315 ? 18.839  2.552   9.850   1.00 16.10 ? 362 PHE A CE1 1 
ATOM   2366 C  CE2 . PHE A 1 315 ? 19.344  0.401   10.679  1.00 15.21 ? 362 PHE A CE2 1 
ATOM   2367 C  CZ  . PHE A 1 315 ? 19.752  1.631   10.281  1.00 15.72 ? 362 PHE A CZ  1 
ATOM   2368 N  N   . PHE A 1 316 ? 15.612  -0.145  6.777   1.00 11.31 ? 363 PHE A N   1 
ATOM   2369 C  CA  . PHE A 1 316 ? 15.860  -1.106  5.728   1.00 11.20 ? 363 PHE A CA  1 
ATOM   2370 C  C   . PHE A 1 316 ? 17.341  -1.417  5.710   1.00 12.75 ? 363 PHE A C   1 
ATOM   2371 O  O   . PHE A 1 316 ? 18.143  -0.514  5.659   1.00 12.49 ? 363 PHE A O   1 
ATOM   2372 C  CB  . PHE A 1 316 ? 15.417  -0.476  4.401   1.00 12.85 ? 363 PHE A CB  1 
ATOM   2373 C  CG  . PHE A 1 316 ? 15.634  -1.419  3.235   1.00 12.78 ? 363 PHE A CG  1 
ATOM   2374 C  CD1 . PHE A 1 316 ? 14.648  -2.355  2.938   1.00 13.86 ? 363 PHE A CD1 1 
ATOM   2375 C  CD2 . PHE A 1 316 ? 16.773  -1.368  2.465   1.00 14.82 ? 363 PHE A CD2 1 
ATOM   2376 C  CE1 . PHE A 1 316 ? 14.796  -3.208  1.845   1.00 15.74 ? 363 PHE A CE1 1 
ATOM   2377 C  CE2 . PHE A 1 316 ? 16.924  -2.244  1.403   1.00 15.63 ? 363 PHE A CE2 1 
ATOM   2378 C  CZ  . PHE A 1 316 ? 15.923  -3.142  1.109   1.00 15.16 ? 363 PHE A CZ  1 
ATOM   2379 N  N   . LEU A 1 317 ? 17.716  -2.695  5.775   1.00 11.21 ? 364 LEU A N   1 
ATOM   2380 C  CA  . LEU A 1 317 ? 19.104  -3.098  5.694   1.00 11.76 ? 364 LEU A CA  1 
ATOM   2381 C  C   . LEU A 1 317 ? 19.196  -4.107  4.580   1.00 13.37 ? 364 LEU A C   1 
ATOM   2382 O  O   . LEU A 1 317 ? 18.429  -5.066  4.532   1.00 14.71 ? 364 LEU A O   1 
ATOM   2383 C  CB  . LEU A 1 317 ? 19.544  -3.738  7.000   1.00 13.68 ? 364 LEU A CB  1 
ATOM   2384 C  CG  . LEU A 1 317 ? 19.586  -2.808  8.199   1.00 13.61 ? 364 LEU A CG  1 
ATOM   2385 C  CD1 . LEU A 1 317 ? 19.721  -3.554  9.516   1.00 15.48 ? 364 LEU A CD1 1 
ATOM   2386 C  CD2 . LEU A 1 317 ? 20.666  -1.785  8.060   1.00 16.35 ? 364 LEU A CD2 1 
ATOM   2387 N  N   . ALA A 1 318 ? 20.181  -3.942  3.728   1.00 12.58 ? 365 ALA A N   1 
ATOM   2388 C  CA  . ALA A 1 318 ? 20.428  -4.944  2.726   1.00 13.17 ? 365 ALA A CA  1 
ATOM   2389 C  C   . ALA A 1 318 ? 21.914  -5.220  2.624   1.00 12.79 ? 365 ALA A C   1 
ATOM   2390 O  O   . ALA A 1 318 ? 22.704  -4.306  2.620   1.00 13.54 ? 365 ALA A O   1 
ATOM   2391 C  CB  . ALA A 1 318 ? 19.918  -4.484  1.408   1.00 16.05 ? 365 ALA A CB  1 
ATOM   2392 N  N   . TYR A 1 319 ? 22.214  -6.506  2.550   1.00 11.97 ? 366 TYR A N   1 
ATOM   2393 C  CA  . TYR A 1 319 ? 23.542  -7.026  2.341   1.00 12.39 ? 366 TYR A CA  1 
ATOM   2394 C  C   . TYR A 1 319 ? 23.651  -7.556  0.918   1.00 12.36 ? 366 TYR A C   1 
ATOM   2395 O  O   . TYR A 1 319 ? 22.712  -8.148  0.386   1.00 13.59 ? 366 TYR A O   1 
ATOM   2396 C  CB  . TYR A 1 319 ? 23.839  -8.134  3.330   1.00 13.80 ? 366 TYR A CB  1 
ATOM   2397 C  CG  . TYR A 1 319 ? 23.965  -7.648  4.744   1.00 12.92 ? 366 TYR A CG  1 
ATOM   2398 C  CD1 . TYR A 1 319 ? 25.193  -7.215  5.222   1.00 14.35 ? 366 TYR A CD1 1 
ATOM   2399 C  CD2 . TYR A 1 319 ? 22.874  -7.593  5.589   1.00 14.23 ? 366 TYR A CD2 1 
ATOM   2400 C  CE1 . TYR A 1 319 ? 25.352  -6.826  6.534   1.00 13.78 ? 366 TYR A CE1 1 
ATOM   2401 C  CE2 . TYR A 1 319 ? 23.007  -7.122  6.877   1.00 14.28 ? 366 TYR A CE2 1 
ATOM   2402 C  CZ  . TYR A 1 319 ? 24.247  -6.768  7.360   1.00 14.65 ? 366 TYR A CZ  1 
ATOM   2403 O  OH  . TYR A 1 319 ? 24.435  -6.339  8.637   1.00 16.86 ? 366 TYR A OH  1 
ATOM   2404 N  N   . GLN A 1 320 ? 24.829  -7.321  0.347   1.00 12.94 ? 367 GLN A N   1 
ATOM   2405 C  CA  . GLN A 1 320 ? 25.062  -7.703  -1.035  1.00 14.32 ? 367 GLN A CA  1 
ATOM   2406 C  C   . GLN A 1 320 ? 26.559  -7.800  -1.283  1.00 13.14 ? 367 GLN A C   1 
ATOM   2407 O  O   . GLN A 1 320 ? 27.334  -7.144  -0.615  1.00 14.09 ? 367 GLN A O   1 
ATOM   2408 C  CB  . GLN A 1 320 ? 24.436  -6.718  -2.017  1.00 14.19 ? 367 GLN A CB  1 
ATOM   2409 C  CG  . GLN A 1 320 ? 24.952  -5.291  -1.892  1.00 14.77 ? 367 GLN A CG  1 
ATOM   2410 C  CD  . GLN A 1 320 ? 23.937  -4.354  -1.289  1.00 18.69 ? 367 GLN A CD  1 
ATOM   2411 O  OE1 . GLN A 1 320 ? 22.969  -3.953  -1.947  1.00 21.45 ? 367 GLN A OE1 1 
ATOM   2412 N  NE2 . GLN A 1 320 ? 24.038  -4.073  0.003   1.00 16.74 ? 367 GLN A NE2 1 
ATOM   2413 N  N   . ARG A 1 321 ? 26.908  -8.503  -2.360  1.00 15.15 ? 368 ARG A N   1 
ATOM   2414 C  CA  . ARG A 1 321 ? 28.296  -8.674  -2.767  1.00 14.80 ? 368 ARG A CA  1 
ATOM   2415 C  C   . ARG A 1 321 ? 28.919  -7.408  -3.345  1.00 16.32 ? 368 ARG A C   1 
ATOM   2416 O  O   . ARG A 1 321 ? 30.131  -7.224  -3.251  1.00 16.49 ? 368 ARG A O   1 
ATOM   2417 C  CB  . ARG A 1 321 ? 28.275  -9.787  -3.818  1.00 15.96 ? 368 ARG A CB  1 
ATOM   2418 C  CG  . ARG A 1 321 ? 29.633  -10.122 -4.422  1.00 17.11 ? 368 ARG A CG  1 
ATOM   2419 C  CD  . ARG A 1 321 ? 29.510  -11.489 -5.084  1.00 18.88 ? 368 ARG A CD  1 
ATOM   2420 N  NE  . ARG A 1 321 ? 30.748  -11.798 -5.824  1.00 21.83 ? 368 ARG A NE  1 
ATOM   2421 C  CZ  . ARG A 1 321 ? 30.860  -12.793 -6.685  1.00 27.27 ? 368 ARG A CZ  1 
ATOM   2422 N  NH1 . ARG A 1 321 ? 29.827  -13.582 -6.906  1.00 26.67 ? 368 ARG A NH1 1 
ATOM   2423 N  NH2 . ARG A 1 321 ? 32.007  -13.011 -7.311  1.00 27.38 ? 368 ARG A NH2 1 
ATOM   2424 N  N   . ASP A 1 322 ? 28.094  -6.537  -3.924  1.00 14.92 ? 369 ASP A N   1 
ATOM   2425 C  CA  . ASP A 1 322 ? 28.565  -5.297  -4.538  1.00 15.85 ? 369 ASP A CA  1 
ATOM   2426 C  C   . ASP A 1 322 ? 27.413  -4.307  -4.549  1.00 15.74 ? 369 ASP A C   1 
ATOM   2427 O  O   . ASP A 1 322 ? 26.349  -4.644  -5.047  1.00 16.20 ? 369 ASP A O   1 
ATOM   2428 C  CB  . ASP A 1 322 ? 29.021  -5.552  -5.967  1.00 16.81 ? 369 ASP A CB  1 
ATOM   2429 C  CG  . ASP A 1 322 ? 29.787  -4.368  -6.546  1.00 20.55 ? 369 ASP A CG  1 
ATOM   2430 O  OD1 . ASP A 1 322 ? 29.461  -3.213  -6.247  1.00 19.49 ? 369 ASP A OD1 1 
ATOM   2431 O  OD2 . ASP A 1 322 ? 30.756  -4.636  -7.331  1.00 25.16 ? 369 ASP A OD2 1 
ATOM   2432 N  N   . ILE A 1 323 ? 27.558  -3.140  -3.951  1.00 16.86 ? 370 ILE A N   1 
ATOM   2433 C  CA  . ILE A 1 323 ? 26.464  -2.175  -3.893  1.00 15.52 ? 370 ILE A CA  1 
ATOM   2434 C  C   . ILE A 1 323 ? 25.996  -1.794  -5.291  1.00 17.80 ? 370 ILE A C   1 
ATOM   2435 O  O   . ILE A 1 323 ? 24.811  -1.531  -5.521  1.00 17.67 ? 370 ILE A O   1 
ATOM   2436 C  CB  . ILE A 1 323 ? 26.890  -0.966  -3.060  1.00 16.74 ? 370 ILE A CB  1 
ATOM   2437 C  CG1 . ILE A 1 323 ? 26.962  -1.365  -1.587  1.00 19.05 ? 370 ILE A CG1 1 
ATOM   2438 C  CG2 . ILE A 1 323 ? 25.953  0.220   -3.245  1.00 18.84 ? 370 ILE A CG2 1 
ATOM   2439 C  CD1 . ILE A 1 323 ? 27.670  -0.349  -0.734  1.00 20.83 ? 370 ILE A CD1 1 
ATOM   2440 N  N   . ARG A 1 324 ? 26.951  -1.805  -6.220  1.00 16.99 ? 371 ARG A N   1 
ATOM   2441 C  CA  . ARG A 1 324 ? 26.677  -1.339  -7.563  1.00 18.67 ? 371 ARG A CA  1 
ATOM   2442 C  C   . ARG A 1 324 ? 25.820  -2.334  -8.306  1.00 16.66 ? 371 ARG A C   1 
ATOM   2443 O  O   . ARG A 1 324 ? 25.139  -1.907  -9.267  1.00 21.46 ? 371 ARG A O   1 
ATOM   2444 C  CB  . ARG A 1 324 ? 27.977  -1.222  -8.353  1.00 18.56 ? 371 ARG A CB  1 
ATOM   2445 C  CG  . ARG A 1 324 ? 28.809  -0.069  -7.809  1.00 20.14 ? 371 ARG A CG  1 
ATOM   2446 C  CD  . ARG A 1 324 ? 30.220  -0.079  -8.384  1.00 21.51 ? 371 ARG A CD  1 
ATOM   2447 N  NE  . ARG A 1 324 ? 30.937  -1.330  -8.134  1.00 22.83 ? 371 ARG A NE  1 
ATOM   2448 C  CZ  . ARG A 1 324 ? 32.100  -1.659  -8.631  1.00 27.96 ? 371 ARG A CZ  1 
ATOM   2449 N  NH1 . ARG A 1 324 ? 32.723  -0.799  -9.417  1.00 29.76 ? 371 ARG A NH1 1 
ATOM   2450 N  NH2 . ARG A 1 324 ? 32.648  -2.827  -8.365  1.00 25.92 ? 371 ARG A NH2 1 
ATOM   2451 N  N   . THR A 1 325 ? 25.768  -3.598  -7.883  1.00 17.43 ? 372 THR A N   1 
ATOM   2452 C  CA  . THR A 1 325 ? 25.001  -4.633  -8.564  1.00 18.46 ? 372 THR A CA  1 
ATOM   2453 C  C   . THR A 1 325 ? 23.869  -5.213  -7.719  1.00 17.26 ? 372 THR A C   1 
ATOM   2454 O  O   . THR A 1 325 ? 23.174  -6.140  -8.133  1.00 21.50 ? 372 THR A O   1 
ATOM   2455 C  CB  . THR A 1 325 ? 25.915  -5.747  -9.059  1.00 21.64 ? 372 THR A CB  1 
ATOM   2456 O  OG1 . THR A 1 325 ? 26.526  -6.383  -7.945  1.00 21.80 ? 372 THR A OG1 1 
ATOM   2457 C  CG2 . THR A 1 325 ? 26.962  -5.230  -10.036 1.00 23.57 ? 372 THR A CG2 1 
ATOM   2458 N  N   . GLY A 1 326 ? 23.649  -4.621  -6.556  1.00 16.61 ? 373 GLY A N   1 
ATOM   2459 C  CA  . GLY A 1 326 ? 22.635  -5.083  -5.632  1.00 16.31 ? 373 GLY A CA  1 
ATOM   2460 C  C   . GLY A 1 326 ? 21.657  -3.946  -5.442  1.00 15.56 ? 373 GLY A C   1 
ATOM   2461 O  O   . GLY A 1 326 ? 20.739  -3.756  -6.231  1.00 16.89 ? 373 GLY A O   1 
ATOM   2462 N  N   . PHE A 1 327 ? 21.856  -3.159  -4.398  1.00 15.72 ? 374 PHE A N   1 
ATOM   2463 C  CA  . PHE A 1 327 ? 20.903  -2.136  -4.034  1.00 16.06 ? 374 PHE A CA  1 
ATOM   2464 C  C   . PHE A 1 327 ? 20.696  -1.100  -5.136  1.00 16.95 ? 374 PHE A C   1 
ATOM   2465 O  O   . PHE A 1 327 ? 19.580  -0.685  -5.380  1.00 16.28 ? 374 PHE A O   1 
ATOM   2466 C  CB  . PHE A 1 327 ? 21.363  -1.458  -2.750  1.00 15.31 ? 374 PHE A CB  1 
ATOM   2467 C  CG  . PHE A 1 327 ? 20.453  -0.344  -2.273  1.00 15.79 ? 374 PHE A CG  1 
ATOM   2468 C  CD1 . PHE A 1 327 ? 19.293  -0.665  -1.576  1.00 16.88 ? 374 PHE A CD1 1 
ATOM   2469 C  CD2 . PHE A 1 327 ? 20.647  0.976   -2.640  1.00 16.29 ? 374 PHE A CD2 1 
ATOM   2470 C  CE1 . PHE A 1 327 ? 18.401  0.317   -1.187  1.00 16.70 ? 374 PHE A CE1 1 
ATOM   2471 C  CE2 . PHE A 1 327 ? 19.769  1.957   -2.208  1.00 15.35 ? 374 PHE A CE2 1 
ATOM   2472 C  CZ  . PHE A 1 327 ? 18.630  1.637   -1.512  1.00 17.40 ? 374 PHE A CZ  1 
ATOM   2473 N  N   . VAL A 1 328 ? 21.762  -0.616  -5.766  1.00 15.93 ? 375 VAL A N   1 
ATOM   2474 C  CA  . VAL A 1 328 ? 21.580  0.511   -6.673  1.00 16.87 ? 375 VAL A CA  1 
ATOM   2475 C  C   . VAL A 1 328 ? 20.652  0.155   -7.822  1.00 16.86 ? 375 VAL A C   1 
ATOM   2476 O  O   . VAL A 1 328 ? 19.697  0.897   -8.038  1.00 17.69 ? 375 VAL A O   1 
ATOM   2477 C  CB  . VAL A 1 328 ? 22.929  1.059   -7.170  1.00 19.06 ? 375 VAL A CB  1 
ATOM   2478 C  CG1 . VAL A 1 328 ? 22.743  2.093   -8.277  1.00 21.03 ? 375 VAL A CG1 1 
ATOM   2479 C  CG2 . VAL A 1 328 ? 23.716  1.690   -6.022  1.00 20.55 ? 375 VAL A CG2 1 
ATOM   2480 N  N   . PRO A 1 329 ? 20.863  -0.918  -8.603  1.00 16.48 ? 376 PRO A N   1 
ATOM   2481 C  CA  . PRO A 1 329 ? 19.908  -1.234  -9.667  1.00 16.95 ? 376 PRO A CA  1 
ATOM   2482 C  C   . PRO A 1 329 ? 18.473  -1.389  -9.205  1.00 17.17 ? 376 PRO A C   1 
ATOM   2483 O  O   . PRO A 1 329 ? 17.554  -0.908  -9.846  1.00 16.64 ? 376 PRO A O   1 
ATOM   2484 C  CB  . PRO A 1 329 ? 20.387  -2.485  -10.334 1.00 18.66 ? 376 PRO A CB  1 
ATOM   2485 C  CG  . PRO A 1 329 ? 21.600  -2.934  -9.554  1.00 20.89 ? 376 PRO A CG  1 
ATOM   2486 C  CD  . PRO A 1 329 ? 22.020  -1.828  -8.615  1.00 17.45 ? 376 PRO A CD  1 
ATOM   2487 N  N   . VAL A 1 330 ? 18.281  -2.067  -8.073  1.00 16.28 ? 377 VAL A N   1 
ATOM   2488 C  CA  . VAL A 1 330 ? 16.949  -2.336  -7.632  1.00 15.20 ? 377 VAL A CA  1 
ATOM   2489 C  C   . VAL A 1 330 ? 16.295  -1.026  -7.199  1.00 14.51 ? 377 VAL A C   1 
ATOM   2490 O  O   . VAL A 1 330 ? 15.173  -0.746  -7.606  1.00 14.79 ? 377 VAL A O   1 
ATOM   2491 C  CB  . VAL A 1 330 ? 16.955  -3.409  -6.536  1.00 15.89 ? 377 VAL A CB  1 
ATOM   2492 C  CG1 . VAL A 1 330 ? 15.562  -3.628  -6.005  1.00 16.58 ? 377 VAL A CG1 1 
ATOM   2493 C  CG2 . VAL A 1 330 ? 17.546  -4.704  -7.063  1.00 16.71 ? 377 VAL A CG2 1 
ATOM   2494 N  N   . GLN A 1 331 ? 16.975  -0.193  -6.412  1.00 14.52 ? 378 GLN A N   1 
ATOM   2495 C  CA  . GLN A 1 331 ? 16.374  1.065   -6.006  1.00 14.95 ? 378 GLN A CA  1 
ATOM   2496 C  C   . GLN A 1 331 ? 16.114  1.969   -7.226  1.00 15.50 ? 378 GLN A C   1 
ATOM   2497 O  O   . GLN A 1 331 ? 15.110  2.672   -7.258  1.00 16.75 ? 378 GLN A O   1 
ATOM   2498 C  CB  . GLN A 1 331 ? 17.232  1.749   -4.921  1.00 16.01 ? 378 GLN A CB  1 
ATOM   2499 C  CG  . GLN A 1 331 ? 16.718  3.081   -4.398  1.00 16.66 ? 378 GLN A CG  1 
ATOM   2500 C  CD  . GLN A 1 331 ? 15.365  3.020   -3.739  1.00 19.29 ? 378 GLN A CD  1 
ATOM   2501 O  OE1 . GLN A 1 331 ? 15.010  2.039   -3.092  1.00 20.55 ? 378 GLN A OE1 1 
ATOM   2502 N  NE2 . GLN A 1 331 ? 14.587  4.075   -3.878  1.00 23.78 ? 378 GLN A NE2 1 
ATOM   2503 N  N   . ARG A 1 332 ? 17.018  2.002   -8.199  1.00 16.61 ? 379 ARG A N   1 
ATOM   2504 C  CA  . ARG A 1 332 ? 16.777  2.785   -9.416  1.00 17.74 ? 379 ARG A CA  1 
ATOM   2505 C  C   . ARG A 1 332 ? 15.474  2.342   -10.086 1.00 17.40 ? 379 ARG A C   1 
ATOM   2506 O  O   . ARG A 1 332 ? 14.656  3.162   -10.503 1.00 18.45 ? 379 ARG A O   1 
ATOM   2507 C  CB  . ARG A 1 332 ? 17.932  2.613   -10.406 1.00 20.65 ? 379 ARG A CB  1 
ATOM   2508 C  CG  . ARG A 1 332 ? 19.153  3.459   -10.096 1.00 25.23 ? 379 ARG A CG  1 
ATOM   2509 C  CD  . ARG A 1 332 ? 20.074  3.729   -11.292 1.00 34.67 ? 379 ARG A CD  1 
ATOM   2510 N  NE  . ARG A 1 332 ? 21.031  4.811   -11.007 1.00 40.23 ? 379 ARG A NE  1 
ATOM   2511 C  CZ  . ARG A 1 332 ? 20.694  6.052   -10.602 1.00 48.75 ? 379 ARG A CZ  1 
ATOM   2512 N  NH1 . ARG A 1 332 ? 19.427  6.372   -10.382 1.00 53.93 ? 379 ARG A NH1 1 
ATOM   2513 N  NH2 . ARG A 1 332 ? 21.615  6.984   -10.412 1.00 47.40 ? 379 ARG A NH2 1 
ATOM   2514 N  N   . ASN A 1 333 ? 15.208  1.024   -10.095 1.00 16.25 ? 380 ASN A N   1 
ATOM   2515 C  CA  . ASN A 1 333 ? 14.012  0.502   -10.709 1.00 15.82 ? 380 ASN A CA  1 
ATOM   2516 C  C   . ASN A 1 333 ? 12.749  0.819   -9.921  1.00 16.95 ? 380 ASN A C   1 
ATOM   2517 O  O   . ASN A 1 333 ? 11.648  0.668   -10.458 1.00 19.18 ? 380 ASN A O   1 
ATOM   2518 C  CB  . ASN A 1 333 ? 14.113  -0.982  -10.921 1.00 17.46 ? 380 ASN A CB  1 
ATOM   2519 C  CG  . ASN A 1 333 ? 13.368  -1.403  -12.162 1.00 19.11 ? 380 ASN A CG  1 
ATOM   2520 O  OD1 . ASN A 1 333 ? 13.556  -0.781  -13.234 1.00 20.24 ? 380 ASN A OD1 1 
ATOM   2521 N  ND2 . ASN A 1 333 ? 12.600  -2.480  -12.067 1.00 17.34 ? 380 ASN A ND2 1 
ATOM   2522 N  N   . LEU A 1 334 ? 12.899  1.201   -8.648  1.00 14.76 ? 381 LEU A N   1 
ATOM   2523 C  CA  . LEU A 1 334 ? 11.747  1.559   -7.829  1.00 14.69 ? 381 LEU A CA  1 
ATOM   2524 C  C   . LEU A 1 334 ? 11.361  3.024   -8.020  1.00 16.40 ? 381 LEU A C   1 
ATOM   2525 O  O   . LEU A 1 334 ? 10.486  3.527   -7.302  1.00 16.85 ? 381 LEU A O   1 
ATOM   2526 C  CB  . LEU A 1 334 ? 11.994  1.273   -6.352  1.00 15.90 ? 381 LEU A CB  1 
ATOM   2527 C  CG  . LEU A 1 334 ? 12.270  -0.197  -6.026  1.00 16.72 ? 381 LEU A CG  1 
ATOM   2528 C  CD1 . LEU A 1 334 ? 12.381  -0.387  -4.488  1.00 17.13 ? 381 LEU A CD1 1 
ATOM   2529 C  CD2 . LEU A 1 334 ? 11.257  -1.126  -6.552  1.00 17.25 ? 381 LEU A CD2 1 
ATOM   2530 N  N   . ALA A 1 335 ? 11.969  3.723   -9.008  1.00 16.30 ? 382 ALA A N   1 
ATOM   2531 C  CA  . ALA A 1 335 ? 11.582  5.104   -9.212  1.00 18.32 ? 382 ALA A CA  1 
ATOM   2532 C  C   . ALA A 1 335 ? 10.092  5.277   -9.476  1.00 18.14 ? 382 ALA A C   1 
ATOM   2533 O  O   . ALA A 1 335 ? 9.562   6.325   -9.115  1.00 20.38 ? 382 ALA A O   1 
ATOM   2534 C  CB  . ALA A 1 335 ? 12.371  5.707   -10.344 1.00 19.68 ? 382 ALA A CB  1 
ATOM   2535 N  N   . THR A 1 336 ? 9.433   4.282   -10.092 1.00 16.49 ? 383 THR A N   1 
ATOM   2536 C  CA  . THR A 1 336 ? 8.019   4.373   -10.439 1.00 18.85 ? 383 THR A CA  1 
ATOM   2537 C  C   . THR A 1 336 ? 7.135   3.544   -9.507  1.00 17.49 ? 383 THR A C   1 
ATOM   2538 O  O   . THR A 1 336 ? 5.955   3.361   -9.762  1.00 18.82 ? 383 THR A O   1 
ATOM   2539 C  CB  . THR A 1 336 ? 7.780   3.925   -11.884 1.00 19.53 ? 383 THR A CB  1 
ATOM   2540 O  OG1 . THR A 1 336 ? 8.217   2.599   -12.094 1.00 22.12 ? 383 THR A OG1 1 
ATOM   2541 C  CG2 . THR A 1 336 ? 8.539   4.776   -12.892 1.00 22.64 ? 383 THR A CG2 1 
ATOM   2542 N  N   . ASP A 1 337 ? 7.717   3.021   -8.436  1.00 16.03 ? 384 ASP A N   1 
ATOM   2543 C  CA  . ASP A 1 337 ? 6.990   2.142   -7.527  1.00 14.80 ? 384 ASP A CA  1 
ATOM   2544 C  C   . ASP A 1 337 ? 5.759   2.832   -6.967  1.00 13.42 ? 384 ASP A C   1 
ATOM   2545 O  O   . ASP A 1 337 ? 5.840   3.945   -6.427  1.00 14.73 ? 384 ASP A O   1 
ATOM   2546 C  CB  . ASP A 1 337 ? 7.948   1.788   -6.404  1.00 14.40 ? 384 ASP A CB  1 
ATOM   2547 C  CG  . ASP A 1 337 ? 7.561   0.654   -5.470  1.00 15.42 ? 384 ASP A CG  1 
ATOM   2548 O  OD1 . ASP A 1 337 ? 6.426   0.193   -5.495  1.00 12.99 ? 384 ASP A OD1 1 
ATOM   2549 O  OD2 . ASP A 1 337 ? 8.453   0.290   -4.715  1.00 15.54 ? 384 ASP A OD2 1 
ATOM   2550 N  N   . ALA A 1 338 ? 4.619   2.134   -6.982  1.00 13.25 ? 385 ALA A N   1 
ATOM   2551 C  CA  . ALA A 1 338 ? 3.400   2.604   -6.351  1.00 13.79 ? 385 ALA A CA  1 
ATOM   2552 C  C   . ALA A 1 338 ? 3.605   2.847   -4.861  1.00 13.77 ? 385 ALA A C   1 
ATOM   2553 O  O   . ALA A 1 338 ? 2.919   3.663   -4.288  1.00 15.78 ? 385 ALA A O   1 
ATOM   2554 C  CB  . ALA A 1 338 ? 2.290   1.607   -6.566  1.00 14.77 ? 385 ALA A CB  1 
ATOM   2555 N  N   . LEU A 1 339 ? 4.569   2.133   -4.264  1.00 13.13 ? 386 LEU A N   1 
ATOM   2556 C  CA  . LEU A 1 339 ? 4.851   2.281   -2.848  1.00 12.66 ? 386 LEU A CA  1 
ATOM   2557 C  C   . LEU A 1 339 ? 5.397   3.665   -2.516  1.00 13.63 ? 386 LEU A C   1 
ATOM   2558 O  O   . LEU A 1 339 ? 5.258   4.138   -1.388  1.00 12.71 ? 386 LEU A O   1 
ATOM   2559 C  CB  . LEU A 1 339 ? 5.833   1.210   -2.404  1.00 13.12 ? 386 LEU A CB  1 
ATOM   2560 C  CG  . LEU A 1 339 ? 6.111   1.148   -0.897  1.00 14.93 ? 386 LEU A CG  1 
ATOM   2561 C  CD1 . LEU A 1 339 ? 4.877   0.928   -0.050  1.00 15.51 ? 386 LEU A CD1 1 
ATOM   2562 C  CD2 . LEU A 1 339 ? 7.163   0.087   -0.634  1.00 14.80 ? 386 LEU A CD2 1 
ATOM   2563 N  N   . ASN A 1 340 ? 5.958   4.359   -3.507  1.00 13.19 ? 387 ASN A N   1 
ATOM   2564 C  CA  . ASN A 1 340 ? 6.571   5.635   -3.192  1.00 14.31 ? 387 ASN A CA  1 
ATOM   2565 C  C   . ASN A 1 340 ? 5.569   6.674   -2.681  1.00 15.08 ? 387 ASN A C   1 
ATOM   2566 O  O   . ASN A 1 340 ? 5.981   7.618   -2.033  1.00 16.11 ? 387 ASN A O   1 
ATOM   2567 C  CB  . ASN A 1 340 ? 7.289   6.218   -4.399  1.00 15.61 ? 387 ASN A CB  1 
ATOM   2568 C  CG  . ASN A 1 340 ? 8.478   5.409   -4.830  1.00 16.35 ? 387 ASN A CG  1 
ATOM   2569 O  OD1 . ASN A 1 340 ? 9.073   4.700   -4.024  1.00 20.32 ? 387 ASN A OD1 1 
ATOM   2570 N  ND2 . ASN A 1 340 ? 8.868   5.566   -6.082  1.00 19.07 ? 387 ASN A ND2 1 
ATOM   2571 N  N   . GLU A 1 341 ? 4.282   6.526   -2.982  1.00 15.02 ? 388 GLU A N   1 
ATOM   2572 C  CA  . GLU A 1 341 ? 3.259   7.410   -2.459  1.00 17.20 ? 388 GLU A CA  1 
ATOM   2573 C  C   . GLU A 1 341 ? 3.181   7.380   -0.940  1.00 17.23 ? 388 GLU A C   1 
ATOM   2574 O  O   . GLU A 1 341 ? 2.670   8.299   -0.309  1.00 18.63 ? 388 GLU A O   1 
ATOM   2575 C  CB  . GLU A 1 341 ? 1.928   6.997   -3.100  1.00 20.64 ? 388 GLU A CB  1 
ATOM   2576 C  CG  . GLU A 1 341 ? 0.713   7.761   -2.596  1.00 28.79 ? 388 GLU A CG  1 
ATOM   2577 C  CD  . GLU A 1 341 ? 0.642   9.220   -3.025  1.00 36.86 ? 388 GLU A CD  1 
ATOM   2578 O  OE1 . GLU A 1 341 ? -0.275  9.884   -2.490  1.00 51.37 ? 388 GLU A OE1 1 
ATOM   2579 O  OE2 . GLU A 1 341 ? 1.450   9.685   -3.865  1.00 35.98 ? 388 GLU A OE2 1 
ATOM   2580 N  N   . PHE A 1 342 ? 3.702   6.314   -0.333  1.00 13.87 ? 389 PHE A N   1 
ATOM   2581 C  CA  . PHE A 1 342 ? 3.474   6.040   1.062   1.00 14.27 ? 389 PHE A CA  1 
ATOM   2582 C  C   . PHE A 1 342 ? 4.748   6.012   1.894   1.00 13.67 ? 389 PHE A C   1 
ATOM   2583 O  O   . PHE A 1 342 ? 4.621   5.737   3.094   1.00 14.65 ? 389 PHE A O   1 
ATOM   2584 C  CB  . PHE A 1 342 ? 2.776   4.693   1.223   1.00 15.09 ? 389 PHE A CB  1 
ATOM   2585 C  CG  . PHE A 1 342 ? 1.463   4.608   0.465   1.00 13.76 ? 389 PHE A CG  1 
ATOM   2586 C  CD1 . PHE A 1 342 ? 0.332   5.262   0.950   1.00 15.39 ? 389 PHE A CD1 1 
ATOM   2587 C  CD2 . PHE A 1 342 ? 1.410   3.965   -0.756  1.00 15.94 ? 389 PHE A CD2 1 
ATOM   2588 C  CE1 . PHE A 1 342 ? -0.860  5.184   0.252   1.00 15.29 ? 389 PHE A CE1 1 
ATOM   2589 C  CE2 . PHE A 1 342 ? 0.224   3.927   -1.457  1.00 16.48 ? 389 PHE A CE2 1 
ATOM   2590 C  CZ  . PHE A 1 342 ? -0.893  4.542   -0.958  1.00 15.24 ? 389 PHE A CZ  1 
ATOM   2591 N  N   . ILE A 1 343 ? 5.895   6.345   1.328   1.00 13.21 ? 390 ILE A N   1 
ATOM   2592 C  CA  . ILE A 1 343 ? 7.161   6.251   2.053   1.00 13.72 ? 390 ILE A CA  1 
ATOM   2593 C  C   . ILE A 1 343 ? 8.039   7.427   1.681   1.00 15.73 ? 390 ILE A C   1 
ATOM   2594 O  O   . ILE A 1 343 ? 7.810   8.080   0.677   1.00 15.73 ? 390 ILE A O   1 
ATOM   2595 C  CB  . ILE A 1 343 ? 7.904   4.944   1.764   1.00 14.34 ? 390 ILE A CB  1 
ATOM   2596 C  CG1 . ILE A 1 343 ? 8.341   4.851   0.312   1.00 14.90 ? 390 ILE A CG1 1 
ATOM   2597 C  CG2 . ILE A 1 343 ? 7.069   3.748   2.191   1.00 15.99 ? 390 ILE A CG2 1 
ATOM   2598 C  CD1 . ILE A 1 343 ? 9.357   3.750   0.055   1.00 16.84 ? 390 ILE A CD1 1 
ATOM   2599 N  N   . GLN A 1 344 ? 9.037   7.678   2.510   1.00 14.59 ? 391 GLN A N   1 
ATOM   2600 C  CA  . GLN A 1 344 ? 10.090  8.609   2.177   1.00 15.22 ? 391 GLN A CA  1 
ATOM   2601 C  C   . GLN A 1 344 ? 11.376  8.126   2.817   1.00 13.71 ? 391 GLN A C   1 
ATOM   2602 O  O   . GLN A 1 344 ? 11.387  7.850   4.014   1.00 15.08 ? 391 GLN A O   1 
ATOM   2603 C  CB  . GLN A 1 344 ? 9.752   9.999   2.706   1.00 18.30 ? 391 GLN A CB  1 
ATOM   2604 C  CG  . GLN A 1 344 ? 10.679  11.065  2.144   1.00 20.09 ? 391 GLN A CG  1 
ATOM   2605 C  CD  . GLN A 1 344 ? 10.261  12.451  2.581   1.00 26.10 ? 391 GLN A CD  1 
ATOM   2606 O  OE1 . GLN A 1 344 ? 10.108  12.718  3.771   1.00 28.92 ? 391 GLN A OE1 1 
ATOM   2607 N  NE2 . GLN A 1 344 ? 10.045  13.324  1.616   1.00 32.03 ? 391 GLN A NE2 1 
ATOM   2608 N  N   . HIS A 1 345 ? 12.450  8.088   2.030   1.00 13.98 ? 392 HIS A N   1 
ATOM   2609 C  CA  . HIS A 1 345 ? 13.754  7.781   2.593   1.00 13.74 ? 392 HIS A CA  1 
ATOM   2610 C  C   . HIS A 1 345 ? 14.305  9.029   3.255   1.00 15.81 ? 392 HIS A C   1 
ATOM   2611 O  O   . HIS A 1 345 ? 14.442  10.059  2.587   1.00 16.85 ? 392 HIS A O   1 
ATOM   2612 C  CB  . HIS A 1 345 ? 14.674  7.281   1.510   1.00 15.43 ? 392 HIS A CB  1 
ATOM   2613 C  CG  . HIS A 1 345 ? 14.265  6.005   0.884   1.00 15.00 ? 392 HIS A CG  1 
ATOM   2614 N  ND1 . HIS A 1 345 ? 15.166  4.971   0.779   1.00 15.09 ? 392 HIS A ND1 1 
ATOM   2615 C  CD2 . HIS A 1 345 ? 13.153  5.598   0.278   1.00 14.74 ? 392 HIS A CD2 1 
ATOM   2616 C  CE1 . HIS A 1 345 ? 14.580  3.952   0.164   1.00 17.04 ? 392 HIS A CE1 1 
ATOM   2617 N  NE2 . HIS A 1 345 ? 13.363  4.327   -0.200  1.00 16.33 ? 392 HIS A NE2 1 
ATOM   2618 N  N   . VAL A 1 346 ? 14.688  8.920   4.520   1.00 14.47 ? 393 VAL A N   1 
ATOM   2619 C  CA  . VAL A 1 346 ? 15.112  10.071  5.297   1.00 14.21 ? 393 VAL A CA  1 
ATOM   2620 C  C   . VAL A 1 346 ? 16.460  9.847   5.979   1.00 17.17 ? 393 VAL A C   1 
ATOM   2621 O  O   . VAL A 1 346 ? 16.904  10.727  6.677   1.00 16.71 ? 393 VAL A O   1 
ATOM   2622 C  CB  . VAL A 1 346 ? 14.049  10.423  6.343   1.00 16.50 ? 393 VAL A CB  1 
ATOM   2623 C  CG1 . VAL A 1 346 ? 12.764  10.936  5.705   1.00 19.08 ? 393 VAL A CG1 1 
ATOM   2624 C  CG2 . VAL A 1 346 ? 13.756  9.287   7.308   1.00 18.10 ? 393 VAL A CG2 1 
ATOM   2625 N  N   . GLY A 1 347 ? 17.147  8.740   5.730   1.00 15.32 ? 394 GLY A N   1 
ATOM   2626 C  CA  . GLY A 1 347 ? 18.480  8.519   6.265   1.00 15.08 ? 394 GLY A CA  1 
ATOM   2627 C  C   . GLY A 1 347 ? 19.136  7.453   5.437   1.00 14.80 ? 394 GLY A C   1 
ATOM   2628 O  O   . GLY A 1 347 ? 18.442  6.597   4.862   1.00 16.01 ? 394 GLY A O   1 
ATOM   2629 N  N   . SER A 1 348 ? 20.450  7.535   5.261   1.00 13.76 ? 395 SER A N   1 
ATOM   2630 C  CA  . SER A 1 348 ? 21.165  6.621   4.409   1.00 14.38 ? 395 SER A CA  1 
ATOM   2631 C  C   . SER A 1 348 ? 22.594  6.436   4.892   1.00 14.36 ? 395 SER A C   1 
ATOM   2632 O  O   . SER A 1 348 ? 23.228  7.390   5.323   1.00 16.16 ? 395 SER A O   1 
ATOM   2633 C  CB  . SER A 1 348 ? 21.138  7.145   3.006   1.00 15.25 ? 395 SER A CB  1 
ATOM   2634 O  OG  . SER A 1 348 ? 21.709  6.236   2.094   1.00 16.47 ? 395 SER A OG  1 
ATOM   2635 N  N   . ALA A 1 349 ? 23.099  5.200   4.777   1.00 14.99 ? 396 ALA A N   1 
ATOM   2636 C  CA  . ALA A 1 349 ? 24.501  4.929   4.989   1.00 14.34 ? 396 ALA A CA  1 
ATOM   2637 C  C   . ALA A 1 349 ? 24.907  3.669   4.255   1.00 15.51 ? 396 ALA A C   1 
ATOM   2638 O  O   . ALA A 1 349 ? 24.117  2.757   4.061   1.00 17.29 ? 396 ALA A O   1 
ATOM   2639 C  CB  . ALA A 1 349 ? 24.787  4.836   6.462   1.00 14.89 ? 396 ALA A CB  1 
ATOM   2640 N  N   . VAL A 1 350 ? 26.181  3.605   3.893   1.00 14.60 ? 397 VAL A N   1 
ATOM   2641 C  CA  . VAL A 1 350 ? 26.741  2.403   3.325   1.00 14.40 ? 397 VAL A CA  1 
ATOM   2642 C  C   . VAL A 1 350 ? 27.981  1.992   4.125   1.00 14.32 ? 397 VAL A C   1 
ATOM   2643 O  O   . VAL A 1 350 ? 28.719  2.846   4.607   1.00 15.03 ? 397 VAL A O   1 
ATOM   2644 C  CB  . VAL A 1 350 ? 27.075  2.529   1.834   1.00 16.52 ? 397 VAL A CB  1 
ATOM   2645 C  CG1 . VAL A 1 350 ? 25.789  2.801   1.073   1.00 17.99 ? 397 VAL A CG1 1 
ATOM   2646 C  CG2 . VAL A 1 350 ? 28.094  3.620   1.578   1.00 19.02 ? 397 VAL A CG2 1 
ATOM   2647 N  N   . PHE A 1 351 ? 28.223  0.688   4.193   1.00 13.69 ? 398 PHE A N   1 
ATOM   2648 C  CA  . PHE A 1 351 ? 29.355  0.156   4.930   1.00 14.77 ? 398 PHE A CA  1 
ATOM   2649 C  C   . PHE A 1 351 ? 29.906  -1.088  4.261   1.00 15.24 ? 398 PHE A C   1 
ATOM   2650 O  O   . PHE A 1 351 ? 29.175  -1.913  3.701   1.00 14.68 ? 398 PHE A O   1 
ATOM   2651 C  CB  . PHE A 1 351 ? 28.975  -0.227  6.352   1.00 13.22 ? 398 PHE A CB  1 
ATOM   2652 C  CG  . PHE A 1 351 ? 28.384  0.916   7.146   1.00 14.21 ? 398 PHE A CG  1 
ATOM   2653 C  CD1 . PHE A 1 351 ? 29.188  1.809   7.849   1.00 14.53 ? 398 PHE A CD1 1 
ATOM   2654 C  CD2 . PHE A 1 351 ? 27.006  1.094   7.186   1.00 15.25 ? 398 PHE A CD2 1 
ATOM   2655 C  CE1 . PHE A 1 351 ? 28.621  2.855   8.547   1.00 14.78 ? 398 PHE A CE1 1 
ATOM   2656 C  CE2 . PHE A 1 351 ? 26.446  2.104   7.936   1.00 15.34 ? 398 PHE A CE2 1 
ATOM   2657 C  CZ  . PHE A 1 351 ? 27.239  2.989   8.585   1.00 15.33 ? 398 PHE A CZ  1 
ATOM   2658 N  N   . ALA A 1 352 ? 31.229  -1.229  4.339   1.00 14.26 ? 399 ALA A N   1 
ATOM   2659 C  CA  . ALA A 1 352 ? 31.922  -2.464  4.057   1.00 15.33 ? 399 ALA A CA  1 
ATOM   2660 C  C   . ALA A 1 352 ? 32.024  -3.291  5.322   1.00 13.69 ? 399 ALA A C   1 
ATOM   2661 O  O   . ALA A 1 352 ? 32.596  -2.813  6.297   1.00 15.23 ? 399 ALA A O   1 
ATOM   2662 C  CB  . ALA A 1 352 ? 33.304  -2.144  3.527   1.00 15.75 ? 399 ALA A CB  1 
ATOM   2663 N  N   . VAL A 1 353 ? 31.445  -4.471  5.283   1.00 14.95 ? 400 VAL A N   1 
ATOM   2664 C  CA  . VAL A 1 353 ? 31.389  -5.372  6.413   1.00 14.59 ? 400 VAL A CA  1 
ATOM   2665 C  C   . VAL A 1 353 ? 32.494  -6.384  6.217   1.00 14.37 ? 400 VAL A C   1 
ATOM   2666 O  O   . VAL A 1 353 ? 32.460  -7.191  5.300   1.00 15.54 ? 400 VAL A O   1 
ATOM   2667 C  CB  . VAL A 1 353 ? 29.989  -5.997  6.489   1.00 16.30 ? 400 VAL A CB  1 
ATOM   2668 C  CG1 . VAL A 1 353 ? 29.879  -7.041  7.586   1.00 17.43 ? 400 VAL A CG1 1 
ATOM   2669 C  CG2 . VAL A 1 353 ? 28.945  -4.911  6.689   1.00 18.54 ? 400 VAL A CG2 1 
ATOM   2670 N  N   . PRO A 1 354 ? 33.570  -6.300  7.034   1.00 14.20 ? 401 PRO A N   1 
ATOM   2671 C  CA  . PRO A 1 354 ? 34.703  -7.185  6.752   1.00 14.91 ? 401 PRO A CA  1 
ATOM   2672 C  C   . PRO A 1 354 ? 34.417  -8.659  6.955   1.00 15.64 ? 401 PRO A C   1 
ATOM   2673 O  O   . PRO A 1 354 ? 33.372  -9.068  7.487   1.00 15.10 ? 401 PRO A O   1 
ATOM   2674 C  CB  . PRO A 1 354 ? 35.769  -6.665  7.698   1.00 16.42 ? 401 PRO A CB  1 
ATOM   2675 C  CG  . PRO A 1 354 ? 35.020  -6.016  8.765   1.00 16.63 ? 401 PRO A CG  1 
ATOM   2676 C  CD  . PRO A 1 354 ? 33.822  -5.340  8.100   1.00 14.61 ? 401 PRO A CD  1 
ATOM   2677 N  N   . PRO A 1 355 ? 35.367  -9.527  6.588   1.00 15.44 ? 402 PRO A N   1 
ATOM   2678 C  CA  . PRO A 1 355 ? 35.248  -10.941 6.873   1.00 15.87 ? 402 PRO A CA  1 
ATOM   2679 C  C   . PRO A 1 355 ? 35.135  -11.221 8.366   1.00 15.12 ? 402 PRO A C   1 
ATOM   2680 O  O   . PRO A 1 355 ? 35.346  -10.349 9.209   1.00 17.04 ? 402 PRO A O   1 
ATOM   2681 C  CB  . PRO A 1 355 ? 36.481  -11.593 6.213   1.00 18.35 ? 402 PRO A CB  1 
ATOM   2682 C  CG  . PRO A 1 355 ? 37.357  -10.457 5.796   1.00 18.96 ? 402 PRO A CG  1 
ATOM   2683 C  CD  . PRO A 1 355 ? 36.601  -9.159  5.891   1.00 17.78 ? 402 PRO A CD  1 
ATOM   2684 N  N   . GLY A 1 356 ? 34.851  -12.482 8.622   1.00 15.62 ? 403 GLY A N   1 
ATOM   2685 C  CA  . GLY A 1 356 ? 34.644  -13.002 9.948   1.00 15.19 ? 403 GLY A CA  1 
ATOM   2686 C  C   . GLY A 1 356 ? 35.948  -13.018 10.720  1.00 16.64 ? 403 GLY A C   1 
ATOM   2687 O  O   . GLY A 1 356 ? 37.052  -12.921 10.153  1.00 17.46 ? 403 GLY A O   1 
ATOM   2688 N  N   . VAL A 1 357 ? 35.768  -13.126 12.029  1.00 15.18 ? 404 VAL A N   1 
ATOM   2689 C  CA  . VAL A 1 357 ? 36.878  -13.293 12.947  1.00 15.42 ? 404 VAL A CA  1 
ATOM   2690 C  C   . VAL A 1 357 ? 37.153  -14.781 13.027  1.00 14.90 ? 404 VAL A C   1 
ATOM   2691 O  O   . VAL A 1 357 ? 36.290  -15.544 13.434  1.00 15.77 ? 404 VAL A O   1 
ATOM   2692 C  CB  . VAL A 1 357 ? 36.446  -12.735 14.309  1.00 16.42 ? 404 VAL A CB  1 
ATOM   2693 C  CG1 . VAL A 1 357 ? 37.587  -12.846 15.324  1.00 17.62 ? 404 VAL A CG1 1 
ATOM   2694 C  CG2 . VAL A 1 357 ? 35.953  -11.288 14.208  1.00 18.43 ? 404 VAL A CG2 1 
ATOM   2695 N  N   . ARG A 1 358 ? 38.349  -15.209 12.550  1.00 16.28 ? 405 ARG A N   1 
ATOM   2696 C  CA  . ARG A 1 358 ? 38.584  -16.616 12.255  1.00 18.18 ? 405 ARG A CA  1 
ATOM   2697 C  C   . ARG A 1 358 ? 38.645  -17.497 13.506  1.00 17.42 ? 405 ARG A C   1 
ATOM   2698 O  O   . ARG A 1 358 ? 38.156  -18.638 13.488  1.00 20.30 ? 405 ARG A O   1 
ATOM   2699 C  CB  . ARG A 1 358 ? 39.882  -16.772 11.450  1.00 22.50 ? 405 ARG A CB  1 
ATOM   2700 C  CG  . ARG A 1 358 ? 39.874  -16.139 10.062  1.00 34.27 ? 405 ARG A CG  1 
ATOM   2701 C  CD  . ARG A 1 358 ? 38.620  -16.348 9.198   1.00 44.02 ? 405 ARG A CD  1 
ATOM   2702 N  NE  . ARG A 1 358 ? 38.340  -17.741 8.821   1.00 49.73 ? 405 ARG A NE  1 
ATOM   2703 C  CZ  . ARG A 1 358 ? 38.300  -18.245 7.585   1.00 52.73 ? 405 ARG A CZ  1 
ATOM   2704 N  NH1 . ARG A 1 358 ? 38.567  -17.492 6.535   1.00 55.40 ? 405 ARG A NH1 1 
ATOM   2705 N  NH2 . ARG A 1 358 ? 37.998  -19.519 7.399   1.00 55.46 ? 405 ARG A NH2 1 
ATOM   2706 N  N   . ASP A 1 359 ? 39.247  -16.944 14.565  1.00 16.56 ? 406 ASP A N   1 
ATOM   2707 C  CA  . ASP A 1 359 ? 39.534  -17.671 15.780  1.00 18.85 ? 406 ASP A CA  1 
ATOM   2708 C  C   . ASP A 1 359 ? 39.839  -16.654 16.869  1.00 18.17 ? 406 ASP A C   1 
ATOM   2709 O  O   . ASP A 1 359 ? 39.776  -15.448 16.667  1.00 16.63 ? 406 ASP A O   1 
ATOM   2710 C  CB  . ASP A 1 359 ? 40.668  -18.657 15.541  1.00 20.72 ? 406 ASP A CB  1 
ATOM   2711 C  CG  . ASP A 1 359 ? 41.976  -18.028 15.089  1.00 23.58 ? 406 ASP A CG  1 
ATOM   2712 O  OD1 . ASP A 1 359 ? 42.301  -16.902 15.499  1.00 22.10 ? 406 ASP A OD1 1 
ATOM   2713 O  OD2 . ASP A 1 359 ? 42.689  -18.701 14.308  1.00 33.14 ? 406 ASP A OD2 1 
ATOM   2714 N  N   . ALA A 1 360 ? 40.288  -17.151 18.038  1.00 17.32 ? 407 ALA A N   1 
ATOM   2715 C  CA  . ALA A 1 360 ? 40.442  -16.355 19.236  1.00 18.87 ? 407 ALA A CA  1 
ATOM   2716 C  C   . ALA A 1 360 ? 41.609  -15.386 19.154  1.00 19.45 ? 407 ALA A C   1 
ATOM   2717 O  O   . ALA A 1 360 ? 41.720  -14.493 19.991  1.00 21.29 ? 407 ALA A O   1 
ATOM   2718 C  CB  . ALA A 1 360 ? 40.621  -17.271 20.417  1.00 19.94 ? 407 ALA A CB  1 
ATOM   2719 N  N   . ASP A 1 361 ? 42.507  -15.588 18.184  1.00 20.24 ? 408 ASP A N   1 
ATOM   2720 C  CA  . ASP A 1 361 ? 43.640  -14.699 18.004  1.00 23.30 ? 408 ASP A CA  1 
ATOM   2721 C  C   . ASP A 1 361 ? 43.350  -13.603 16.981  1.00 21.36 ? 408 ASP A C   1 
ATOM   2722 O  O   . ASP A 1 361 ? 44.088  -12.621 16.926  1.00 24.29 ? 408 ASP A O   1 
ATOM   2723 C  CB  . ASP A 1 361 ? 44.850  -15.459 17.490  1.00 27.99 ? 408 ASP A CB  1 
ATOM   2724 C  CG  . ASP A 1 361 ? 45.889  -15.765 18.549  1.00 41.64 ? 408 ASP A CG  1 
ATOM   2725 O  OD1 . ASP A 1 361 ? 46.423  -14.789 19.147  1.00 45.86 ? 408 ASP A OD1 1 
ATOM   2726 O  OD2 . ASP A 1 361 ? 46.128  -16.963 18.756  1.00 47.64 ? 408 ASP A OD2 1 
ATOM   2727 N  N   . ASP A 1 362 ? 42.238  -13.734 16.261  1.00 18.53 ? 409 ASP A N   1 
ATOM   2728 C  CA  . ASP A 1 362 ? 41.904  -12.767 15.215  1.00 17.09 ? 409 ASP A CA  1 
ATOM   2729 C  C   . ASP A 1 362 ? 41.134  -11.592 15.803  1.00 18.92 ? 409 ASP A C   1 
ATOM   2730 O  O   . ASP A 1 362 ? 40.815  -11.563 16.968  1.00 18.99 ? 409 ASP A O   1 
ATOM   2731 C  CB  . ASP A 1 362 ? 41.151  -13.454 14.103  1.00 17.35 ? 409 ASP A CB  1 
ATOM   2732 C  CG  . ASP A 1 362 ? 41.122  -12.731 12.763  1.00 17.00 ? 409 ASP A CG  1 
ATOM   2733 O  OD1 . ASP A 1 362 ? 41.877  -11.784 12.618  1.00 20.00 ? 409 ASP A OD1 1 
ATOM   2734 O  OD2 . ASP A 1 362 ? 40.365  -13.169 11.906  1.00 20.42 ? 409 ASP A OD2 1 
ATOM   2735 N  N   . TRP A 1 363 ? 40.898  -10.571 14.983  1.00 17.18 ? 410 TRP A N   1 
ATOM   2736 C  CA  . TRP A 1 363 ? 40.240  -9.370  15.434  1.00 17.33 ? 410 TRP A CA  1 
ATOM   2737 C  C   . TRP A 1 363 ? 39.564  -8.683  14.258  1.00 16.69 ? 410 TRP A C   1 
ATOM   2738 O  O   . TRP A 1 363 ? 39.957  -8.808  13.109  1.00 17.81 ? 410 TRP A O   1 
ATOM   2739 C  CB  . TRP A 1 363 ? 41.223  -8.437  16.152  1.00 17.62 ? 410 TRP A CB  1 
ATOM   2740 C  CG  . TRP A 1 363 ? 42.574  -8.278  15.500  1.00 18.97 ? 410 TRP A CG  1 
ATOM   2741 C  CD1 . TRP A 1 363 ? 43.624  -9.160  15.546  1.00 20.96 ? 410 TRP A CD1 1 
ATOM   2742 C  CD2 . TRP A 1 363 ? 43.022  -7.150  14.724  1.00 19.75 ? 410 TRP A CD2 1 
ATOM   2743 N  NE1 . TRP A 1 363 ? 44.689  -8.659  14.851  1.00 24.82 ? 410 TRP A NE1 1 
ATOM   2744 C  CE2 . TRP A 1 363 ? 44.349  -7.431  14.341  1.00 22.15 ? 410 TRP A CE2 1 
ATOM   2745 C  CE3 . TRP A 1 363 ? 42.446  -5.937  14.321  1.00 20.90 ? 410 TRP A CE3 1 
ATOM   2746 C  CZ2 . TRP A 1 363 ? 45.090  -6.545  13.575  1.00 23.40 ? 410 TRP A CZ2 1 
ATOM   2747 C  CZ3 . TRP A 1 363 ? 43.191  -5.052  13.566  1.00 20.23 ? 410 TRP A CZ3 1 
ATOM   2748 C  CH2 . TRP A 1 363 ? 44.500  -5.364  13.198  1.00 22.66 ? 410 TRP A CH2 1 
ATOM   2749 N  N   . TRP A 1 364 ? 38.516  -7.947  14.607  1.00 15.19 ? 411 TRP A N   1 
ATOM   2750 C  CA  . TRP A 1 364 ? 37.745  -7.178  13.641  1.00 15.96 ? 411 TRP A CA  1 
ATOM   2751 C  C   . TRP A 1 364 ? 38.667  -6.263  12.840  1.00 17.18 ? 411 TRP A C   1 
ATOM   2752 O  O   . TRP A 1 364 ? 39.423  -5.492  13.431  1.00 18.26 ? 411 TRP A O   1 
ATOM   2753 C  CB  . TRP A 1 364 ? 36.723  -6.321  14.374  1.00 16.15 ? 411 TRP A CB  1 
ATOM   2754 C  CG  . TRP A 1 364 ? 35.438  -7.017  14.712  1.00 15.03 ? 411 TRP A CG  1 
ATOM   2755 C  CD1 . TRP A 1 364 ? 34.870  -8.082  14.098  1.00 17.11 ? 411 TRP A CD1 1 
ATOM   2756 C  CD2 . TRP A 1 364 ? 34.491  -6.547  15.678  1.00 16.02 ? 411 TRP A CD2 1 
ATOM   2757 N  NE1 . TRP A 1 364 ? 33.664  -8.374  14.678  1.00 16.59 ? 411 TRP A NE1 1 
ATOM   2758 C  CE2 . TRP A 1 364 ? 33.375  -7.420  15.612  1.00 15.92 ? 411 TRP A CE2 1 
ATOM   2759 C  CE3 . TRP A 1 364 ? 34.454  -5.459  16.552  1.00 18.15 ? 411 TRP A CE3 1 
ATOM   2760 C  CZ2 . TRP A 1 364 ? 32.242  -7.250  16.402  1.00 16.56 ? 411 TRP A CZ2 1 
ATOM   2761 C  CZ3 . TRP A 1 364 ? 33.314  -5.270  17.310  1.00 20.57 ? 411 TRP A CZ3 1 
ATOM   2762 C  CH2 . TRP A 1 364 ? 32.213  -6.131  17.194  1.00 18.20 ? 411 TRP A CH2 1 
ATOM   2763 N  N   . GLY A 1 365 ? 38.587  -6.371  11.517  1.00 17.40 ? 412 GLY A N   1 
ATOM   2764 C  CA  . GLY A 1 365 ? 39.352  -5.484  10.658  1.00 18.20 ? 412 GLY A CA  1 
ATOM   2765 C  C   . GLY A 1 365 ? 40.801  -5.925  10.466  1.00 19.61 ? 412 GLY A C   1 
ATOM   2766 O  O   . GLY A 1 365 ? 41.565  -5.202  9.840   1.00 18.63 ? 412 GLY A O   1 
ATOM   2767 N  N   . SER A 1 366 ? 41.203  -7.108  10.942  1.00 17.58 ? 413 SER A N   1 
ATOM   2768 C  CA  . SER A 1 366 ? 42.595  -7.534  10.844  1.00 17.69 ? 413 SER A CA  1 
ATOM   2769 C  C   . SER A 1 366 ? 43.081  -7.652  9.398   1.00 20.03 ? 413 SER A C   1 
ATOM   2770 O  O   . SER A 1 366 ? 44.295  -7.470  9.155   1.00 21.60 ? 413 SER A O   1 
ATOM   2771 C  CB  . SER A 1 366 ? 42.783  -8.848  11.545  1.00 18.69 ? 413 SER A CB  1 
ATOM   2772 O  OG  . SER A 1 366 ? 42.123  -9.891  10.845  1.00 17.86 ? 413 SER A OG  1 
ATOM   2773 N  N   . THR A 1 367 ? 42.185  -7.963  8.448   1.00 19.77 ? 414 THR A N   1 
ATOM   2774 C  CA  . THR A 1 367 ? 42.621  -8.103  7.065   1.00 18.58 ? 414 THR A CA  1 
ATOM   2775 C  C   . THR A 1 367 ? 42.897  -6.731  6.457   1.00 21.34 ? 414 THR A C   1 
ATOM   2776 O  O   . THR A 1 367 ? 43.692  -6.649  5.516   1.00 23.43 ? 414 THR A O   1 
ATOM   2777 C  CB  . THR A 1 367 ? 41.659  -8.904  6.191   1.00 19.85 ? 414 THR A CB  1 
ATOM   2778 O  OG1 . THR A 1 367 ? 40.432  -8.190  6.168   1.00 20.78 ? 414 THR A OG1 1 
ATOM   2779 C  CG2 . THR A 1 367 ? 41.422  -10.309 6.716   1.00 21.05 ? 414 THR A CG2 1 
ATOM   2780 N  N   . LEU A 1 368 ? 42.270  -5.683  6.971   1.00 18.97 ? 415 LEU A N   1 
ATOM   2781 C  CA  . LEU A 1 368 ? 42.463  -4.332  6.461   1.00 21.44 ? 415 LEU A CA  1 
ATOM   2782 C  C   . LEU A 1 368 ? 43.732  -3.711  7.048   1.00 24.66 ? 415 LEU A C   1 
ATOM   2783 O  O   . LEU A 1 368 ? 44.472  -3.018  6.344   1.00 26.79 ? 415 LEU A O   1 
ATOM   2784 C  CB  . LEU A 1 368 ? 41.245  -3.472  6.801   1.00 22.22 ? 415 LEU A CB  1 
ATOM   2785 C  CG  . LEU A 1 368 ? 41.322  -1.985  6.427   1.00 26.20 ? 415 LEU A CG  1 
ATOM   2786 C  CD1 . LEU A 1 368 ? 41.572  -1.844  4.954   1.00 26.06 ? 415 LEU A CD1 1 
ATOM   2787 C  CD2 . LEU A 1 368 ? 40.068  -1.249  6.845   1.00 27.78 ? 415 LEU A CD2 1 
ATOM   2788 N  N   . PHE A 1 369 ? 43.899  -3.886  8.360   1.00 24.59 ? 416 PHE A N   1 
ATOM   2789 C  CA  . PHE A 1 369 ? 44.950  -3.245  9.134   1.00 27.12 ? 416 PHE A CA  1 
ATOM   2790 C  C   . PHE A 1 369 ? 46.093  -4.251  9.277   1.00 30.43 ? 416 PHE A C   1 
ATOM   2791 O  O   . PHE A 1 369 ? 47.181  -3.642  9.181   1.00 35.49 ? 416 PHE A O   1 
ATOM   2792 C  CB  . PHE A 1 369 ? 44.406  -2.776  10.483  1.00 26.79 ? 416 PHE A CB  1 
ATOM   2793 C  CG  . PHE A 1 369 ? 43.450  -1.590  10.445  1.00 25.59 ? 416 PHE A CG  1 
ATOM   2794 C  CD1 . PHE A 1 369 ? 43.917  -0.286  10.371  1.00 24.85 ? 416 PHE A CD1 1 
ATOM   2795 C  CD2 . PHE A 1 369 ? 42.071  -1.775  10.483  1.00 25.19 ? 416 PHE A CD2 1 
ATOM   2796 C  CE1 . PHE A 1 369 ? 43.042  0.779   10.312  1.00 26.07 ? 416 PHE A CE1 1 
ATOM   2797 C  CE2 . PHE A 1 369 ? 41.202  -0.703  10.464  1.00 25.40 ? 416 PHE A CE2 1 
ATOM   2798 C  CZ  . PHE A 1 369 ? 41.691  0.579   10.385  1.00 27.06 ? 416 PHE A CZ  1 
ATOM   2799 N  N   . SER B 1 9   ? -0.997  -16.908 28.108  1.00 35.76 ? 56  SER B N   1 
ATOM   2800 C  CA  . SER B 1 9   ? -1.449  -16.672 26.706  1.00 33.37 ? 56  SER B CA  1 
ATOM   2801 C  C   . SER B 1 9   ? -2.261  -15.377 26.627  1.00 25.54 ? 56  SER B C   1 
ATOM   2802 O  O   . SER B 1 9   ? -1.901  -14.501 25.900  1.00 20.94 ? 56  SER B O   1 
ATOM   2803 C  CB  . SER B 1 9   ? -2.230  -17.823 26.159  1.00 44.75 ? 56  SER B CB  1 
ATOM   2804 O  OG  . SER B 1 9   ? -2.662  -17.532 24.838  1.00 48.53 ? 56  SER B OG  1 
ATOM   2805 N  N   . ALA B 1 10  ? -3.348  -15.260 27.374  1.00 23.53 ? 57  ALA B N   1 
ATOM   2806 C  CA  . ALA B 1 10  ? -4.157  -14.046 27.350  1.00 19.06 ? 57  ALA B CA  1 
ATOM   2807 C  C   . ALA B 1 10  ? -4.514  -13.691 28.776  1.00 18.74 ? 57  ALA B C   1 
ATOM   2808 O  O   . ALA B 1 10  ? -4.360  -14.484 29.700  1.00 19.85 ? 57  ALA B O   1 
ATOM   2809 C  CB  . ALA B 1 10  ? -5.383  -14.224 26.550  1.00 19.29 ? 57  ALA B CB  1 
ATOM   2810 N  N   . VAL B 1 11  ? -4.921  -12.446 28.935  1.00 13.46 ? 58  VAL B N   1 
ATOM   2811 C  CA  . VAL B 1 11  ? -5.358  -11.953 30.216  1.00 13.66 ? 58  VAL B CA  1 
ATOM   2812 C  C   . VAL B 1 11  ? -6.791  -11.514 30.050  1.00 14.02 ? 58  VAL B C   1 
ATOM   2813 O  O   . VAL B 1 11  ? -7.117  -10.784 29.114  1.00 13.56 ? 58  VAL B O   1 
ATOM   2814 C  CB  . VAL B 1 11  ? -4.467  -10.785 30.679  1.00 14.90 ? 58  VAL B CB  1 
ATOM   2815 C  CG1 . VAL B 1 11  ? -5.044  -10.132 31.923  1.00 16.28 ? 58  VAL B CG1 1 
ATOM   2816 C  CG2 . VAL B 1 11  ? -3.036  -11.239 30.899  1.00 16.30 ? 58  VAL B CG2 1 
ATOM   2817 N  N   . PRO B 1 12  ? -7.713  -11.930 30.927  1.00 13.73 ? 59  PRO B N   1 
ATOM   2818 C  CA  . PRO B 1 12  ? -9.098  -11.502 30.764  1.00 14.66 ? 59  PRO B CA  1 
ATOM   2819 C  C   . PRO B 1 12  ? -9.220  -9.979  30.753  1.00 13.68 ? 59  PRO B C   1 
ATOM   2820 O  O   . PRO B 1 12  ? -8.608  -9.285  31.550  1.00 15.52 ? 59  PRO B O   1 
ATOM   2821 C  CB  . PRO B 1 12  ? -9.794  -12.096 31.993  1.00 17.16 ? 59  PRO B CB  1 
ATOM   2822 C  CG  . PRO B 1 12  ? -8.854  -13.122 32.503  1.00 18.64 ? 59  PRO B CG  1 
ATOM   2823 C  CD  . PRO B 1 12  ? -7.461  -12.789 32.094  1.00 15.70 ? 59  PRO B CD  1 
ATOM   2824 N  N   . PHE B 1 13  ? -10.052 -9.500  29.856  1.00 13.77 ? 60  PHE B N   1 
ATOM   2825 C  CA  . PHE B 1 13  ? -10.310 -8.080  29.702  1.00 13.77 ? 60  PHE B CA  1 
ATOM   2826 C  C   . PHE B 1 13  ? -11.298 -7.576  30.745  1.00 13.66 ? 60  PHE B C   1 
ATOM   2827 O  O   . PHE B 1 13  ? -11.166 -6.463  31.228  1.00 13.31 ? 60  PHE B O   1 
ATOM   2828 C  CB  . PHE B 1 13  ? -10.836 -7.821  28.286  1.00 13.86 ? 60  PHE B CB  1 
ATOM   2829 C  CG  . PHE B 1 13  ? -11.137 -6.365  27.997  1.00 14.63 ? 60  PHE B CG  1 
ATOM   2830 C  CD1 . PHE B 1 13  ? -10.127 -5.420  27.880  1.00 15.53 ? 60  PHE B CD1 1 
ATOM   2831 C  CD2 . PHE B 1 13  ? -12.455 -5.926  27.924  1.00 16.31 ? 60  PHE B CD2 1 
ATOM   2832 C  CE1 . PHE B 1 13  ? -10.433 -4.100  27.666  1.00 15.92 ? 60  PHE B CE1 1 
ATOM   2833 C  CE2 . PHE B 1 13  ? -12.739 -4.612  27.626  1.00 18.55 ? 60  PHE B CE2 1 
ATOM   2834 C  CZ  . PHE B 1 13  ? -11.733 -3.698  27.553  1.00 16.64 ? 60  PHE B CZ  1 
ATOM   2835 N  N   . HIS B 1 14  ? -12.322 -8.373  31.028  1.00 14.99 ? 61  HIS B N   1 
ATOM   2836 C  CA  . HIS B 1 14  ? -13.378 -7.953  31.926  1.00 15.44 ? 61  HIS B CA  1 
ATOM   2837 C  C   . HIS B 1 14  ? -12.990 -8.187  33.366  1.00 17.29 ? 61  HIS B C   1 
ATOM   2838 O  O   . HIS B 1 14  ? -12.270 -9.123  33.735  1.00 19.34 ? 61  HIS B O   1 
ATOM   2839 C  CB  . HIS B 1 14  ? -14.685 -8.706  31.610  1.00 16.84 ? 61  HIS B CB  1 
ATOM   2840 C  CG  . HIS B 1 14  ? -15.113 -8.444  30.234  1.00 18.36 ? 61  HIS B CG  1 
ATOM   2841 N  ND1 . HIS B 1 14  ? -15.022 -9.346  29.199  1.00 25.19 ? 61  HIS B ND1 1 
ATOM   2842 C  CD2 . HIS B 1 14  ? -15.608 -7.324  29.692  1.00 18.47 ? 61  HIS B CD2 1 
ATOM   2843 C  CE1 . HIS B 1 14  ? -15.504 -8.783  28.090  1.00 26.50 ? 61  HIS B CE1 1 
ATOM   2844 N  NE2 . HIS B 1 14  ? -15.886 -7.550  28.364  1.00 21.69 ? 61  HIS B NE2 1 
ATOM   2845 N  N   . GLY B 1 15  ? -13.528 -7.347  34.231  1.00 15.52 ? 62  GLY B N   1 
ATOM   2846 C  CA  . GLY B 1 15  ? -13.278 -7.494  35.643  1.00 16.92 ? 62  GLY B CA  1 
ATOM   2847 C  C   . GLY B 1 15  ? -13.823 -6.301  36.407  1.00 15.82 ? 62  GLY B C   1 
ATOM   2848 O  O   . GLY B 1 15  ? -14.253 -5.329  35.824  1.00 16.48 ? 62  GLY B O   1 
ATOM   2849 N  N   . ALA B 1 16  ? -13.740 -6.391  37.727  1.00 15.58 ? 63  ALA B N   1 
ATOM   2850 C  CA  . ALA B 1 16  ? -14.059 -5.268  38.572  1.00 16.09 ? 63  ALA B CA  1 
ATOM   2851 C  C   . ALA B 1 16  ? -13.021 -4.163  38.379  1.00 14.55 ? 63  ALA B C   1 
ATOM   2852 O  O   . ALA B 1 16  ? -13.335 -2.994  38.543  1.00 15.05 ? 63  ALA B O   1 
ATOM   2853 C  CB  . ALA B 1 16  ? -14.042 -5.730  40.024  1.00 19.08 ? 63  ALA B CB  1 
ATOM   2854 N  N   . HIS B 1 17  ? -11.780 -4.581  38.096  1.00 13.76 ? 64  HIS B N   1 
ATOM   2855 C  CA  . HIS B 1 17  ? -10.679 -3.668  37.849  1.00 12.98 ? 64  HIS B CA  1 
ATOM   2856 C  C   . HIS B 1 17  ? -10.274 -3.826  36.403  1.00 12.76 ? 64  HIS B C   1 
ATOM   2857 O  O   . HIS B 1 17  ? -10.415 -4.908  35.843  1.00 14.00 ? 64  HIS B O   1 
ATOM   2858 C  CB  . HIS B 1 17  ? -9.488  -3.942  38.754  1.00 13.40 ? 64  HIS B CB  1 
ATOM   2859 C  CG  . HIS B 1 17  ? -9.861  -3.997  40.176  1.00 13.15 ? 64  HIS B CG  1 
ATOM   2860 N  ND1 . HIS B 1 17  ? -10.308 -2.935  40.901  1.00 14.65 ? 64  HIS B ND1 1 
ATOM   2861 C  CD2 . HIS B 1 17  ? -9.832  -5.068  40.996  1.00 16.13 ? 64  HIS B CD2 1 
ATOM   2862 C  CE1 . HIS B 1 17  ? -10.531 -3.371  42.151  1.00 16.33 ? 64  HIS B CE1 1 
ATOM   2863 N  NE2 . HIS B 1 17  ? -10.273 -4.661  42.217  1.00 16.98 ? 64  HIS B NE2 1 
ATOM   2864 N  N   . GLN B 1 18  ? -9.721  -2.759  35.818  1.00 12.01 ? 65  GLN B N   1 
ATOM   2865 C  CA  . GLN B 1 18  ? -9.044  -2.926  34.557  1.00 11.30 ? 65  GLN B CA  1 
ATOM   2866 C  C   . GLN B 1 18  ? -7.820  -3.798  34.774  1.00 11.27 ? 65  GLN B C   1 
ATOM   2867 O  O   . GLN B 1 18  ? -7.135  -3.723  35.767  1.00 12.34 ? 65  GLN B O   1 
ATOM   2868 C  CB  . GLN B 1 18  ? -8.634  -1.549  34.051  1.00 11.14 ? 65  GLN B CB  1 
ATOM   2869 C  CG  . GLN B 1 18  ? -9.795  -0.672  33.606  1.00 10.68 ? 65  GLN B CG  1 
ATOM   2870 C  CD  . GLN B 1 18  ? -9.264  0.511   32.842  1.00 11.49 ? 65  GLN B CD  1 
ATOM   2871 O  OE1 . GLN B 1 18  ? -8.738  0.352   31.738  1.00 12.48 ? 65  GLN B OE1 1 
ATOM   2872 N  NE2 . GLN B 1 18  ? -9.348  1.694   33.420  1.00 11.85 ? 65  GLN B NE2 1 
ATOM   2873 N  N   . ALA B 1 19  ? -7.551  -4.610  33.774  1.00 11.28 ? 66  ALA B N   1 
ATOM   2874 C  CA  . ALA B 1 19  ? -6.326  -5.361  33.727  1.00 11.44 ? 66  ALA B CA  1 
ATOM   2875 C  C   . ALA B 1 19  ? -5.165  -4.421  33.428  1.00 11.04 ? 66  ALA B C   1 
ATOM   2876 O  O   . ALA B 1 19  ? -5.396  -3.282  33.029  1.00 13.58 ? 66  ALA B O   1 
ATOM   2877 C  CB  . ALA B 1 19  ? -6.406  -6.454  32.673  1.00 12.46 ? 66  ALA B CB  1 
ATOM   2878 N  N   . GLY B 1 20  ? -3.944  -4.895  33.640  1.00 11.36 ? 67  GLY B N   1 
ATOM   2879 C  CA  . GLY B 1 20  ? -2.757  -4.124  33.377  1.00 11.24 ? 67  GLY B CA  1 
ATOM   2880 C  C   . GLY B 1 20  ? -2.224  -3.357  34.565  1.00 11.39 ? 67  GLY B C   1 
ATOM   2881 O  O   . GLY B 1 20  ? -1.344  -2.545  34.427  1.00 12.39 ? 67  GLY B O   1 
ATOM   2882 N  N   . ILE B 1 21  ? -2.767  -3.626  35.760  1.00 11.65 ? 68  ILE B N   1 
ATOM   2883 C  CA  . ILE B 1 21  ? -2.374  -2.936  36.986  1.00 11.88 ? 68  ILE B CA  1 
ATOM   2884 C  C   . ILE B 1 21  ? -1.804  -3.978  37.926  1.00 13.68 ? 68  ILE B C   1 
ATOM   2885 O  O   . ILE B 1 21  ? -0.598  -3.990  38.184  1.00 15.60 ? 68  ILE B O   1 
ATOM   2886 C  CB  . ILE B 1 21  ? -3.506  -2.128  37.595  1.00 13.90 ? 68  ILE B CB  1 
ATOM   2887 C  CG1 . ILE B 1 21  ? -4.001  -1.113  36.569  1.00 15.70 ? 68  ILE B CG1 1 
ATOM   2888 C  CG2 . ILE B 1 21  ? -3.027  -1.455  38.875  1.00 15.72 ? 68  ILE B CG2 1 
ATOM   2889 C  CD1 . ILE B 1 21  ? -5.296  -0.416  36.933  1.00 16.46 ? 68  ILE B CD1 1 
ATOM   2890 N  N   . ALA B 1 22  ? -2.668  -4.891  38.340  1.00 13.77 ? 69  ALA B N   1 
ATOM   2891 C  CA  . ALA B 1 22  ? -2.333  -5.981  39.247  1.00 14.54 ? 69  ALA B CA  1 
ATOM   2892 C  C   . ALA B 1 22  ? -2.104  -7.294  38.532  1.00 16.09 ? 69  ALA B C   1 
ATOM   2893 O  O   . ALA B 1 22  ? -1.785  -8.301  39.172  1.00 21.62 ? 69  ALA B O   1 
ATOM   2894 C  CB  . ALA B 1 22  ? -3.430  -6.174  40.273  1.00 15.95 ? 69  ALA B CB  1 
ATOM   2895 N  N   . THR B 1 23  ? -2.263  -7.325  37.222  1.00 13.65 ? 70  THR B N   1 
ATOM   2896 C  CA  . THR B 1 23  ? -2.080  -8.553  36.475  1.00 14.22 ? 70  THR B CA  1 
ATOM   2897 C  C   . THR B 1 23  ? -0.611  -8.669  36.128  1.00 15.96 ? 70  THR B C   1 
ATOM   2898 O  O   . THR B 1 23  ? 0.172   -7.724  36.260  1.00 14.83 ? 70  THR B O   1 
ATOM   2899 C  CB  . THR B 1 23  ? -3.035  -8.579  35.287  1.00 16.40 ? 70  THR B CB  1 
ATOM   2900 O  OG1 . THR B 1 23  ? -2.779  -7.430  34.487  1.00 15.23 ? 70  THR B OG1 1 
ATOM   2901 C  CG2 . THR B 1 23  ? -4.502  -8.637  35.697  1.00 17.68 ? 70  THR B CG2 1 
ATOM   2902 N  N   . PRO B 1 24  ? -0.145  -9.888  35.809  1.00 15.49 ? 71  PRO B N   1 
ATOM   2903 C  CA  . PRO B 1 24  ? 1.296   -10.051 35.653  1.00 15.43 ? 71  PRO B CA  1 
ATOM   2904 C  C   . PRO B 1 24  ? 1.939   -9.098  34.645  1.00 15.43 ? 71  PRO B C   1 
ATOM   2905 O  O   . PRO B 1 24  ? 1.390   -8.785  33.587  1.00 15.91 ? 71  PRO B O   1 
ATOM   2906 C  CB  . PRO B 1 24  ? 1.407   -11.519 35.220  1.00 17.62 ? 71  PRO B CB  1 
ATOM   2907 C  CG  . PRO B 1 24  ? 0.121   -12.166 35.730  1.00 19.73 ? 71  PRO B CG  1 
ATOM   2908 C  CD  . PRO B 1 24  ? -0.940  -11.099 35.619  1.00 17.96 ? 71  PRO B CD  1 
ATOM   2909 N  N   . VAL B 1 25  ? 3.136   -8.652  34.953  1.00 14.89 ? 72  VAL B N   1 
ATOM   2910 C  CA  . VAL B 1 25  ? 3.835   -7.625  34.238  1.00 15.79 ? 72  VAL B CA  1 
ATOM   2911 C  C   . VAL B 1 25  ? 4.364   -8.261  32.962  1.00 14.47 ? 72  VAL B C   1 
ATOM   2912 O  O   . VAL B 1 25  ? 5.179   -9.179  32.978  1.00 15.81 ? 72  VAL B O   1 
ATOM   2913 C  CB  . VAL B 1 25  ? 4.958   -6.938  35.031  1.00 17.95 ? 72  VAL B CB  1 
ATOM   2914 C  CG1 . VAL B 1 25  ? 5.649   -5.887  34.194  1.00 18.33 ? 72  VAL B CG1 1 
ATOM   2915 C  CG2 . VAL B 1 25  ? 4.454   -6.242  36.295  1.00 20.67 ? 72  VAL B CG2 1 
ATOM   2916 N  N   . GLN B 1 26  ? 3.972   -7.703  31.830  1.00 12.37 ? 73  GLN B N   1 
ATOM   2917 C  CA  . GLN B 1 26  ? 4.388   -8.209  30.549  1.00 11.79 ? 73  GLN B CA  1 
ATOM   2918 C  C   . GLN B 1 26  ? 5.676   -7.548  30.102  1.00 10.58 ? 73  GLN B C   1 
ATOM   2919 O  O   . GLN B 1 26  ? 6.166   -6.573  30.638  1.00 11.88 ? 73  GLN B O   1 
ATOM   2920 C  CB  . GLN B 1 26  ? 3.273   -7.931  29.537  1.00 11.12 ? 73  GLN B CB  1 
ATOM   2921 C  CG  . GLN B 1 26  ? 1.876   -8.355  30.002  1.00 10.82 ? 73  GLN B CG  1 
ATOM   2922 C  CD  . GLN B 1 26  ? 1.049   -7.238  30.573  1.00 10.94 ? 73  GLN B CD  1 
ATOM   2923 O  OE1 . GLN B 1 26  ? 1.537   -6.445  31.378  1.00 10.53 ? 73  GLN B OE1 1 
ATOM   2924 N  NE2 . GLN B 1 26  ? -0.187  -7.178  30.115  1.00 11.36 ? 73  GLN B NE2 1 
ATOM   2925 N  N   . ASP B 1 27  ? 6.262   -8.158  29.091  1.00 11.89 ? 74  ASP B N   1 
ATOM   2926 C  CA  . ASP B 1 27  ? 7.620   -7.794  28.730  1.00 12.48 ? 74  ASP B CA  1 
ATOM   2927 C  C   . ASP B 1 27  ? 7.752   -6.434  28.055  1.00 12.75 ? 74  ASP B C   1 
ATOM   2928 O  O   . ASP B 1 27  ? 8.839   -5.883  28.062  1.00 12.83 ? 74  ASP B O   1 
ATOM   2929 C  CB  . ASP B 1 27  ? 8.158   -8.850  27.779  1.00 13.33 ? 74  ASP B CB  1 
ATOM   2930 C  CG  . ASP B 1 27  ? 8.290   -10.272 28.329  1.00 15.46 ? 74  ASP B CG  1 
ATOM   2931 O  OD1 . ASP B 1 27  ? 8.054   -10.477 29.529  1.00 18.21 ? 74  ASP B OD1 1 
ATOM   2932 O  OD2 . ASP B 1 27  ? 8.701   -11.135 27.524  1.00 18.21 ? 74  ASP B OD2 1 
ATOM   2933 N  N   . ARG B 1 28  ? 6.702   -5.882  27.444  1.00 11.80 ? 75  ARG B N   1 
ATOM   2934 C  CA  . ARG B 1 28  ? 6.814   -4.706  26.617  1.00 11.60 ? 75  ARG B CA  1 
ATOM   2935 C  C   . ARG B 1 28  ? 5.660   -3.748  26.883  1.00 11.68 ? 75  ARG B C   1 
ATOM   2936 O  O   . ARG B 1 28  ? 4.572   -4.151  27.330  1.00 12.02 ? 75  ARG B O   1 
ATOM   2937 C  CB  . ARG B 1 28  ? 6.772   -5.072  25.131  1.00 12.74 ? 75  ARG B CB  1 
ATOM   2938 C  CG  . ARG B 1 28  ? 7.768   -6.149  24.730  1.00 15.15 ? 75  ARG B CG  1 
ATOM   2939 C  CD  . ARG B 1 28  ? 9.192   -5.738  24.790  1.00 17.01 ? 75  ARG B CD  1 
ATOM   2940 N  NE  . ARG B 1 28  ? 10.020  -6.902  24.429  1.00 21.66 ? 75  ARG B NE  1 
ATOM   2941 C  CZ  . ARG B 1 28  ? 10.920  -7.478  25.195  1.00 20.17 ? 75  ARG B CZ  1 
ATOM   2942 N  NH1 . ARG B 1 28  ? 11.147  -7.024  26.407  1.00 18.76 ? 75  ARG B NH1 1 
ATOM   2943 N  NH2 . ARG B 1 28  ? 11.615  -8.509  24.738  1.00 21.82 ? 75  ARG B NH2 1 
ATOM   2944 N  N   . LEU B 1 29  ? 5.912   -2.455  26.577  1.00 10.83 ? 76  LEU B N   1 
ATOM   2945 C  CA  . LEU B 1 29  ? 4.952   -1.381  26.787  1.00 10.54 ? 76  LEU B CA  1 
ATOM   2946 C  C   . LEU B 1 29  ? 4.900   -0.499  25.558  1.00 10.87 ? 76  LEU B C   1 
ATOM   2947 O  O   . LEU B 1 29  ? 5.943   -0.139  25.034  1.00 11.49 ? 76  LEU B O   1 
ATOM   2948 C  CB  . LEU B 1 29  ? 5.471   -0.512  27.913  1.00 11.50 ? 76  LEU B CB  1 
ATOM   2949 C  CG  . LEU B 1 29  ? 4.718   0.788   28.169  1.00 11.85 ? 76  LEU B CG  1 
ATOM   2950 C  CD1 . LEU B 1 29  ? 3.367   0.558   28.790  1.00 14.19 ? 76  LEU B CD1 1 
ATOM   2951 C  CD2 . LEU B 1 29  ? 5.537   1.750   29.031  1.00 13.50 ? 76  LEU B CD2 1 
ATOM   2952 N  N   . HIS B 1 30  ? 3.697   -0.086  25.183  1.00 10.21 ? 77  HIS B N   1 
ATOM   2953 C  CA  . HIS B 1 30  ? 3.489   1.084   24.354  1.00 10.30 ? 77  HIS B CA  1 
ATOM   2954 C  C   . HIS B 1 30  ? 2.463   1.913   25.095  1.00 10.54 ? 77  HIS B C   1 
ATOM   2955 O  O   . HIS B 1 30  ? 1.297   1.521   25.247  1.00 11.30 ? 77  HIS B O   1 
ATOM   2956 C  CB  . HIS B 1 30  ? 3.043   0.674   22.948  1.00 10.40 ? 77  HIS B CB  1 
ATOM   2957 C  CG  . HIS B 1 30  ? 3.078   1.797   22.015  1.00 11.55 ? 77  HIS B CG  1 
ATOM   2958 N  ND1 . HIS B 1 30  ? 2.583   1.667   20.749  1.00 14.97 ? 77  HIS B ND1 1 
ATOM   2959 C  CD2 . HIS B 1 30  ? 3.485   3.051   22.147  1.00 16.96 ? 77  HIS B CD2 1 
ATOM   2960 C  CE1 . HIS B 1 30  ? 2.805   2.804   20.096  1.00 15.66 ? 77  HIS B CE1 1 
ATOM   2961 N  NE2 . HIS B 1 30  ? 3.344   3.667   20.912  1.00 17.53 ? 77  HIS B NE2 1 
ATOM   2962 N  N   . PHE B 1 31  ? 2.898   3.083   25.562  1.00 10.74 ? 78  PHE B N   1 
ATOM   2963 C  CA  . PHE B 1 31  ? 2.035   3.995   26.305  1.00 11.25 ? 78  PHE B CA  1 
ATOM   2964 C  C   . PHE B 1 31  ? 1.765   5.199   25.431  1.00 11.79 ? 78  PHE B C   1 
ATOM   2965 O  O   . PHE B 1 31  ? 2.682   5.760   24.884  1.00 13.50 ? 78  PHE B O   1 
ATOM   2966 C  CB  . PHE B 1 31  ? 2.781   4.425   27.564  1.00 11.77 ? 78  PHE B CB  1 
ATOM   2967 C  CG  . PHE B 1 31  ? 1.897   5.140   28.549  1.00 12.24 ? 78  PHE B CG  1 
ATOM   2968 C  CD1 . PHE B 1 31  ? 1.602   6.478   28.406  1.00 13.59 ? 78  PHE B CD1 1 
ATOM   2969 C  CD2 . PHE B 1 31  ? 1.385   4.453   29.625  1.00 12.61 ? 78  PHE B CD2 1 
ATOM   2970 C  CE1 . PHE B 1 31  ? 0.792   7.115   29.342  1.00 14.13 ? 78  PHE B CE1 1 
ATOM   2971 C  CE2 . PHE B 1 31  ? 0.570   5.102   30.545  1.00 14.29 ? 78  PHE B CE2 1 
ATOM   2972 C  CZ  . PHE B 1 31  ? 0.277   6.429   30.389  1.00 14.42 ? 78  PHE B CZ  1 
ATOM   2973 N  N   . ALA B 1 32  ? 0.522   5.572   25.261  1.00 10.29 ? 79  ALA B N   1 
ATOM   2974 C  CA  . ALA B 1 32  ? 0.152   6.717   24.457  1.00 11.32 ? 79  ALA B CA  1 
ATOM   2975 C  C   . ALA B 1 32  ? -0.775  7.627   25.246  1.00 10.33 ? 79  ALA B C   1 
ATOM   2976 O  O   . ALA B 1 32  ? -1.749  7.182   25.852  1.00 12.28 ? 79  ALA B O   1 
ATOM   2977 C  CB  . ALA B 1 32  ? -0.527  6.313   23.182  1.00 13.15 ? 79  ALA B CB  1 
ATOM   2978 N  N   . ALA B 1 33  ? -0.478  8.926   25.148  1.00 10.39 ? 80  ALA B N   1 
ATOM   2979 C  CA  . ALA B 1 33  ? -1.358  9.959   25.632  1.00 10.05 ? 80  ALA B CA  1 
ATOM   2980 C  C   . ALA B 1 33  ? -2.064  10.574  24.442  1.00 10.20 ? 80  ALA B C   1 
ATOM   2981 O  O   . ALA B 1 33  ? -1.437  10.833  23.413  1.00 12.91 ? 80  ALA B O   1 
ATOM   2982 C  CB  . ALA B 1 33  ? -0.597  11.009  26.371  1.00 11.84 ? 80  ALA B CB  1 
ATOM   2983 N  N   . PHE B 1 34  ? -3.356  10.850  24.616  1.00 10.57 ? 81  PHE B N   1 
ATOM   2984 C  CA  . PHE B 1 34  ? -4.185  11.431  23.578  1.00 11.37 ? 81  PHE B CA  1 
ATOM   2985 C  C   . PHE B 1 34  ? -4.815  12.725  24.063  1.00 11.88 ? 81  PHE B C   1 
ATOM   2986 O  O   . PHE B 1 34  ? -5.123  12.862  25.236  1.00 12.49 ? 81  PHE B O   1 
ATOM   2987 C  CB  . PHE B 1 34  ? -5.346  10.491  23.222  1.00 11.15 ? 81  PHE B CB  1 
ATOM   2988 C  CG  . PHE B 1 34  ? -4.952  9.155   22.613  1.00 12.90 ? 81  PHE B CG  1 
ATOM   2989 C  CD1 . PHE B 1 34  ? -4.578  8.102   23.410  1.00 13.58 ? 81  PHE B CD1 1 
ATOM   2990 C  CD2 . PHE B 1 34  ? -5.041  8.973   21.256  1.00 14.70 ? 81  PHE B CD2 1 
ATOM   2991 C  CE1 . PHE B 1 34  ? -4.252  6.889   22.829  1.00 16.21 ? 81  PHE B CE1 1 
ATOM   2992 C  CE2 . PHE B 1 34  ? -4.766  7.750   20.694  1.00 16.17 ? 81  PHE B CE2 1 
ATOM   2993 C  CZ  . PHE B 1 34  ? -4.326  6.748   21.488  1.00 15.11 ? 81  PHE B CZ  1 
ATOM   2994 N  N   . ASP B 1 35  ? -5.015  13.643  23.126  1.00 11.10 ? 82  ASP B N   1 
ATOM   2995 C  CA  . ASP B 1 35  ? -5.807  14.844  23.367  1.00 12.19 ? 82  ASP B CA  1 
ATOM   2996 C  C   . ASP B 1 35  ? -7.089  14.745  22.588  1.00 12.69 ? 82  ASP B C   1 
ATOM   2997 O  O   . ASP B 1 35  ? -7.122  14.202  21.474  1.00 13.39 ? 82  ASP B O   1 
ATOM   2998 C  CB  . ASP B 1 35  ? -5.024  16.080  22.965  1.00 12.81 ? 82  ASP B CB  1 
ATOM   2999 C  CG  . ASP B 1 35  ? -3.946  16.503  23.935  1.00 14.54 ? 82  ASP B CG  1 
ATOM   3000 O  OD1 . ASP B 1 35  ? -4.042  16.084  25.128  1.00 15.33 ? 82  ASP B OD1 1 
ATOM   3001 O  OD2 . ASP B 1 35  ? -3.011  17.138  23.446  1.00 17.05 ? 82  ASP B OD2 1 
ATOM   3002 N  N   . VAL B 1 36  ? -8.167  15.196  23.209  1.00 13.44 ? 83  VAL B N   1 
ATOM   3003 C  CA  . VAL B 1 36  ? -9.496  15.133  22.619  1.00 13.41 ? 83  VAL B CA  1 
ATOM   3004 C  C   . VAL B 1 36  ? -9.750  16.389  21.812  1.00 15.92 ? 83  VAL B C   1 
ATOM   3005 O  O   . VAL B 1 36  ? -9.464  17.487  22.283  1.00 18.10 ? 83  VAL B O   1 
ATOM   3006 C  CB  . VAL B 1 36  ? -10.548 14.996  23.734  1.00 15.69 ? 83  VAL B CB  1 
ATOM   3007 C  CG1 . VAL B 1 36  ? -11.985 15.028  23.221  1.00 17.01 ? 83  VAL B CG1 1 
ATOM   3008 C  CG2 . VAL B 1 36  ? -10.281 13.767  24.560  1.00 17.63 ? 83  VAL B CG2 1 
ATOM   3009 N  N   . THR B 1 37  ? -10.271 16.217  20.595  1.00 15.63 ? 84  THR B N   1 
ATOM   3010 C  CA  . THR B 1 37  ? -10.475 17.352  19.704  1.00 17.61 ? 84  THR B CA  1 
ATOM   3011 C  C   . THR B 1 37  ? -11.941 17.730  19.581  1.00 20.26 ? 84  THR B C   1 
ATOM   3012 O  O   . THR B 1 37  ? -12.216 18.868  19.185  1.00 27.99 ? 84  THR B O   1 
ATOM   3013 C  CB  . THR B 1 37  ? -9.816  17.103  18.353  1.00 18.97 ? 84  THR B CB  1 
ATOM   3014 O  OG1 . THR B 1 37  ? -10.373 15.946  17.738  1.00 21.11 ? 84  THR B OG1 1 
ATOM   3015 C  CG2 . THR B 1 37  ? -8.330  16.898  18.532  1.00 20.83 ? 84  THR B CG2 1 
ATOM   3016 N  N   . THR B 1 38  ? -12.848 16.889  20.026  1.00 15.87 ? 85  THR B N   1 
ATOM   3017 C  CA  . THR B 1 38  ? -14.273 17.152  19.893  1.00 17.02 ? 85  THR B CA  1 
ATOM   3018 C  C   . THR B 1 38  ? -14.758 17.786  21.195  1.00 17.99 ? 85  THR B C   1 
ATOM   3019 O  O   . THR B 1 38  ? -14.251 17.505  22.286  1.00 19.03 ? 85  THR B O   1 
ATOM   3020 C  CB  . THR B 1 38  ? -15.024 15.849  19.575  1.00 20.04 ? 85  THR B CB  1 
ATOM   3021 O  OG1 . THR B 1 38  ? -16.412 16.177  19.451  1.00 19.81 ? 85  THR B OG1 1 
ATOM   3022 C  CG2 . THR B 1 38  ? -14.904 14.785  20.642  1.00 19.53 ? 85  THR B CG2 1 
ATOM   3023 N  N   . GLU B 1 39  ? -15.779 18.644  21.051  1.00 17.56 ? 86  GLU B N   1 
ATOM   3024 C  CA  . GLU B 1 39  ? -16.472 19.207  22.195  1.00 18.64 ? 86  GLU B CA  1 
ATOM   3025 C  C   . GLU B 1 39  ? -17.781 18.499  22.497  1.00 20.03 ? 86  GLU B C   1 
ATOM   3026 O  O   . GLU B 1 39  ? -18.414 18.833  23.487  1.00 21.70 ? 86  GLU B O   1 
ATOM   3027 C  CB  . GLU B 1 39  ? -16.929 20.643  21.919  1.00 20.70 ? 86  GLU B CB  1 
ATOM   3028 C  CG  . GLU B 1 39  ? -15.790 21.599  21.662  1.00 22.47 ? 86  GLU B CG  1 
ATOM   3029 C  CD  . GLU B 1 39  ? -16.248 23.026  21.341  1.00 23.24 ? 86  GLU B CD  1 
ATOM   3030 O  OE1 . GLU B 1 39  ? -17.454 23.310  21.271  1.00 26.11 ? 86  GLU B OE1 1 
ATOM   3031 O  OE2 . GLU B 1 39  ? -15.321 23.810  21.117  1.00 28.58 ? 86  GLU B OE2 1 
ATOM   3032 N  N   . ASP B 1 40  ? -18.137 17.494  21.687  1.00 18.43 ? 87  ASP B N   1 
ATOM   3033 C  CA  . ASP B 1 40  ? -19.446 16.858  21.699  1.00 19.79 ? 87  ASP B CA  1 
ATOM   3034 C  C   . ASP B 1 40  ? -19.352 15.623  22.587  1.00 18.32 ? 87  ASP B C   1 
ATOM   3035 O  O   . ASP B 1 40  ? -18.662 14.653  22.207  1.00 19.45 ? 87  ASP B O   1 
ATOM   3036 C  CB  . ASP B 1 40  ? -19.848 16.530  20.269  1.00 21.96 ? 87  ASP B CB  1 
ATOM   3037 C  CG  . ASP B 1 40  ? -21.130 15.749  19.986  1.00 27.34 ? 87  ASP B CG  1 
ATOM   3038 O  OD1 . ASP B 1 40  ? -21.698 15.175  20.882  1.00 26.50 ? 87  ASP B OD1 1 
ATOM   3039 O  OD2 . ASP B 1 40  ? -21.574 15.740  18.831  1.00 34.82 ? 87  ASP B OD2 1 
ATOM   3040 N  N   . ARG B 1 41  ? -20.012 15.655  23.738  1.00 18.85 ? 88  ARG B N   1 
ATOM   3041 C  CA  . ARG B 1 41  ? -20.005 14.571  24.695  1.00 17.46 ? 88  ARG B CA  1 
ATOM   3042 C  C   . ARG B 1 41  ? -20.525 13.286  24.062  1.00 19.31 ? 88  ARG B C   1 
ATOM   3043 O  O   . ARG B 1 41  ? -19.985 12.220  24.315  1.00 18.02 ? 88  ARG B O   1 
ATOM   3044 C  CB  . ARG B 1 41  ? -20.829 14.981  25.917  1.00 21.24 ? 88  ARG B CB  1 
ATOM   3045 C  CG  . ARG B 1 41  ? -20.934 13.920  26.988  1.00 21.74 ? 88  ARG B CG  1 
ATOM   3046 C  CD  . ARG B 1 41  ? -21.795 14.421  28.127  1.00 25.71 ? 88  ARG B CD  1 
ATOM   3047 N  NE  . ARG B 1 41  ? -22.006 13.409  29.154  1.00 28.35 ? 88  ARG B NE  1 
ATOM   3048 C  CZ  . ARG B 1 41  ? -21.827 13.597  30.449  1.00 33.24 ? 88  ARG B CZ  1 
ATOM   3049 N  NH1 . ARG B 1 41  ? -21.302 14.718  30.918  1.00 35.09 ? 88  ARG B NH1 1 
ATOM   3050 N  NH2 . ARG B 1 41  ? -22.162 12.625  31.274  1.00 34.73 ? 88  ARG B NH2 1 
ATOM   3051 N  N   . ALA B 1 42  ? -21.577 13.378  23.253  1.00 17.40 ? 89  ALA B N   1 
ATOM   3052 C  CA  . ALA B 1 42  ? -22.157 12.179  22.674  1.00 17.11 ? 89  ALA B CA  1 
ATOM   3053 C  C   . ALA B 1 42  ? -21.171 11.505  21.738  1.00 17.05 ? 89  ALA B C   1 
ATOM   3054 O  O   . ALA B 1 42  ? -21.088 10.275  21.724  1.00 18.31 ? 89  ALA B O   1 
ATOM   3055 C  CB  . ALA B 1 42  ? -23.438 12.503  21.941  1.00 18.90 ? 89  ALA B CB  1 
ATOM   3056 N  N   . ALA B 1 43  ? -20.445 12.294  20.969  1.00 16.02 ? 90  ALA B N   1 
ATOM   3057 C  CA  . ALA B 1 43  ? -19.423 11.787  20.085  1.00 17.75 ? 90  ALA B CA  1 
ATOM   3058 C  C   . ALA B 1 43  ? -18.310 11.120  20.887  1.00 16.17 ? 90  ALA B C   1 
ATOM   3059 O  O   . ALA B 1 43  ? -17.790 10.082  20.446  1.00 17.17 ? 90  ALA B O   1 
ATOM   3060 C  CB  . ALA B 1 43  ? -18.863 12.887  19.219  1.00 20.40 ? 90  ALA B CB  1 
ATOM   3061 N  N   . PHE B 1 44  ? -17.953 11.692  22.036  1.00 15.85 ? 91  PHE B N   1 
ATOM   3062 C  CA  . PHE B 1 44  ? -16.883 11.083  22.810  1.00 15.69 ? 91  PHE B CA  1 
ATOM   3063 C  C   . PHE B 1 44  ? -17.342 9.742   23.387  1.00 15.55 ? 91  PHE B C   1 
ATOM   3064 O  O   . PHE B 1 44  ? -16.594 8.768   23.422  1.00 15.73 ? 91  PHE B O   1 
ATOM   3065 C  CB  . PHE B 1 44  ? -16.449 12.076  23.879  1.00 16.00 ? 91  PHE B CB  1 
ATOM   3066 C  CG  . PHE B 1 44  ? -15.203 11.596  24.582  1.00 16.02 ? 91  PHE B CG  1 
ATOM   3067 C  CD1 . PHE B 1 44  ? -14.004 11.508  23.903  1.00 20.77 ? 91  PHE B CD1 1 
ATOM   3068 C  CD2 . PHE B 1 44  ? -15.268 11.247  25.916  1.00 17.36 ? 91  PHE B CD2 1 
ATOM   3069 C  CE1 . PHE B 1 44  ? -12.877 11.045  24.561  1.00 21.83 ? 91  PHE B CE1 1 
ATOM   3070 C  CE2 . PHE B 1 44  ? -14.122 10.765  26.563  1.00 18.50 ? 91  PHE B CE2 1 
ATOM   3071 C  CZ  . PHE B 1 44  ? -12.946 10.652  25.851  1.00 21.13 ? 91  PHE B CZ  1 
ATOM   3072 N  N   . VAL B 1 45  ? -18.567 9.680   23.923  1.00 15.28 ? 92  VAL B N   1 
ATOM   3073 C  CA  . VAL B 1 45  ? -19.101 8.444   24.462  1.00 15.30 ? 92  VAL B CA  1 
ATOM   3074 C  C   . VAL B 1 45  ? -19.123 7.375   23.376  1.00 14.50 ? 92  VAL B C   1 
ATOM   3075 O  O   . VAL B 1 45  ? -18.809 6.195   23.613  1.00 14.83 ? 92  VAL B O   1 
ATOM   3076 C  CB  . VAL B 1 45  ? -20.486 8.699   25.084  1.00 17.45 ? 92  VAL B CB  1 
ATOM   3077 C  CG1 . VAL B 1 45  ? -21.165 7.385   25.366  1.00 19.83 ? 92  VAL B CG1 1 
ATOM   3078 C  CG2 . VAL B 1 45  ? -20.377 9.516   26.367  1.00 19.55 ? 92  VAL B CG2 1 
ATOM   3079 N  N   . ALA B 1 46  ? -19.536 7.768   22.174  1.00 15.09 ? 93  ALA B N   1 
ATOM   3080 C  CA  . ALA B 1 46  ? -19.600 6.792   21.112  1.00 15.03 ? 93  ALA B CA  1 
ATOM   3081 C  C   . ALA B 1 46  ? -18.212 6.233   20.861  1.00 15.05 ? 93  ALA B C   1 
ATOM   3082 O  O   . ALA B 1 46  ? -18.061 5.040   20.592  1.00 16.24 ? 93  ALA B O   1 
ATOM   3083 C  CB  . ALA B 1 46  ? -20.153 7.448   19.878  1.00 15.78 ? 93  ALA B CB  1 
ATOM   3084 N  N   . LEU B 1 47  ? -17.202 7.092   20.906  1.00 15.51 ? 94  LEU B N   1 
ATOM   3085 C  CA  . LEU B 1 47  ? -15.830 6.646   20.748  1.00 14.18 ? 94  LEU B CA  1 
ATOM   3086 C  C   . LEU B 1 47  ? -15.435 5.676   21.856  1.00 12.66 ? 94  LEU B C   1 
ATOM   3087 O  O   . LEU B 1 47  ? -14.822 4.655   21.570  1.00 13.61 ? 94  LEU B O   1 
ATOM   3088 C  CB  . LEU B 1 47  ? -14.854 7.805   20.712  1.00 14.61 ? 94  LEU B CB  1 
ATOM   3089 C  CG  . LEU B 1 47  ? -13.392 7.387   20.621  1.00 17.81 ? 94  LEU B CG  1 
ATOM   3090 C  CD1 . LEU B 1 47  ? -13.113 6.661   19.347  1.00 19.45 ? 94  LEU B CD1 1 
ATOM   3091 C  CD2 . LEU B 1 47  ? -12.527 8.635   20.716  1.00 21.60 ? 94  LEU B CD2 1 
ATOM   3092 N  N   . LEU B 1 48  ? -15.721 5.978   23.116  1.00 13.42 ? 95  LEU B N   1 
ATOM   3093 C  CA  . LEU B 1 48  ? -15.384 5.059   24.192  1.00 13.47 ? 95  LEU B CA  1 
ATOM   3094 C  C   . LEU B 1 48  ? -16.022 3.698   23.953  1.00 13.76 ? 95  LEU B C   1 
ATOM   3095 O  O   . LEU B 1 48  ? -15.397 2.657   24.212  1.00 13.60 ? 95  LEU B O   1 
ATOM   3096 C  CB  . LEU B 1 48  ? -15.811 5.584   25.546  1.00 14.85 ? 95  LEU B CB  1 
ATOM   3097 C  CG  . LEU B 1 48  ? -15.034 6.826   25.984  1.00 15.92 ? 95  LEU B CG  1 
ATOM   3098 C  CD1 . LEU B 1 48  ? -15.653 7.390   27.214  1.00 17.32 ? 95  LEU B CD1 1 
ATOM   3099 C  CD2 . LEU B 1 48  ? -13.603 6.477   26.210  1.00 18.43 ? 95  LEU B CD2 1 
ATOM   3100 N  N   . LYS B 1 49  ? -17.255 3.639   23.443  1.00 13.31 ? 96  LYS B N   1 
ATOM   3101 C  CA  . LYS B 1 49  ? -17.871 2.359   23.189  1.00 12.46 ? 96  LYS B CA  1 
ATOM   3102 C  C   . LYS B 1 49  ? -17.157 1.619   22.060  1.00 12.76 ? 96  LYS B C   1 
ATOM   3103 O  O   . LYS B 1 49  ? -16.968 0.421   22.179  1.00 14.40 ? 96  LYS B O   1 
ATOM   3104 C  CB  . LYS B 1 49  ? -19.356 2.570   22.838  1.00 14.61 ? 96  LYS B CB  1 
ATOM   3105 C  CG  . LYS B 1 49  ? -20.149 2.981   24.022  1.00 17.22 ? 96  LYS B CG  1 
ATOM   3106 C  CD  . LYS B 1 49  ? -21.605 3.310   23.697  1.00 18.75 ? 96  LYS B CD  1 
ATOM   3107 C  CE  . LYS B 1 49  ? -22.333 3.683   24.941  1.00 20.37 ? 96  LYS B CE  1 
ATOM   3108 N  NZ  . LYS B 1 49  ? -23.705 4.146   24.651  1.00 24.32 ? 96  LYS B NZ  1 
ATOM   3109 N  N   . GLU B 1 50  ? -16.835 2.309   20.963  1.00 13.11 ? 97  GLU B N   1 
ATOM   3110 C  CA  . GLU B 1 50  ? -16.128 1.683   19.862  1.00 13.83 ? 97  GLU B CA  1 
ATOM   3111 C  C   . GLU B 1 50  ? -14.739 1.206   20.290  1.00 13.50 ? 97  GLU B C   1 
ATOM   3112 O  O   . GLU B 1 50  ? -14.293 0.120   19.898  1.00 14.34 ? 97  GLU B O   1 
ATOM   3113 C  CB  . GLU B 1 50  ? -15.966 2.638   18.698  1.00 16.31 ? 97  GLU B CB  1 
ATOM   3114 C  CG  . GLU B 1 50  ? -17.205 3.037   17.914  1.00 22.14 ? 97  GLU B CG  1 
ATOM   3115 C  CD  . GLU B 1 50  ? -16.751 3.705   16.610  1.00 29.19 ? 97  GLU B CD  1 
ATOM   3116 O  OE1 . GLU B 1 50  ? -17.158 4.871   16.479  1.00 38.92 ? 97  GLU B OE1 1 
ATOM   3117 O  OE2 . GLU B 1 50  ? -16.025 3.104   15.748  1.00 33.09 ? 97  GLU B OE2 1 
ATOM   3118 N  N   . TRP B 1 51  ? -14.029 2.009   21.065  1.00 12.27 ? 98  TRP B N   1 
ATOM   3119 C  CA  . TRP B 1 51  ? -12.747 1.583   21.596  1.00 12.87 ? 98  TRP B CA  1 
ATOM   3120 C  C   . TRP B 1 51  ? -12.867 0.362   22.506  1.00 12.78 ? 98  TRP B C   1 
ATOM   3121 O  O   . TRP B 1 51  ? -11.992 -0.509  22.438  1.00 13.21 ? 98  TRP B O   1 
ATOM   3122 C  CB  . TRP B 1 51  ? -12.099 2.737   22.377  1.00 13.15 ? 98  TRP B CB  1 
ATOM   3123 C  CG  . TRP B 1 51  ? -11.277 3.672   21.567  1.00 12.69 ? 98  TRP B CG  1 
ATOM   3124 C  CD1 . TRP B 1 51  ? -11.057 3.665   20.225  1.00 12.42 ? 98  TRP B CD1 1 
ATOM   3125 C  CD2 . TRP B 1 51  ? -10.365 4.644   22.109  1.00 13.73 ? 98  TRP B CD2 1 
ATOM   3126 N  NE1 . TRP B 1 51  ? -10.133 4.607   19.895  1.00 12.52 ? 98  TRP B NE1 1 
ATOM   3127 C  CE2 . TRP B 1 51  ? -9.652  5.191   21.022  1.00 12.51 ? 98  TRP B CE2 1 
ATOM   3128 C  CE3 . TRP B 1 51  ? -10.054 5.052   23.396  1.00 14.96 ? 98  TRP B CE3 1 
ATOM   3129 C  CZ2 . TRP B 1 51  ? -8.672  6.171   21.187  1.00 14.95 ? 98  TRP B CZ2 1 
ATOM   3130 C  CZ3 . TRP B 1 51  ? -9.068  6.006   23.574  1.00 17.68 ? 98  TRP B CZ3 1 
ATOM   3131 C  CH2 . TRP B 1 51  ? -8.406  6.573   22.468  1.00 17.00 ? 98  TRP B CH2 1 
ATOM   3132 N  N   . THR B 1 52  ? -13.898 0.287   23.351  1.00 11.33 ? 99  THR B N   1 
ATOM   3133 C  CA  . THR B 1 52  ? -14.091 -0.880  24.197  1.00 12.10 ? 99  THR B CA  1 
ATOM   3134 C  C   . THR B 1 52  ? -14.299 -2.135  23.359  1.00 12.13 ? 99  THR B C   1 
ATOM   3135 O  O   . THR B 1 52  ? -13.689 -3.166  23.590  1.00 13.18 ? 99  THR B O   1 
ATOM   3136 C  CB  . THR B 1 52  ? -15.238 -0.701  25.177  1.00 13.00 ? 99  THR B CB  1 
ATOM   3137 O  OG1 . THR B 1 52  ? -15.064 0.525   25.891  1.00 14.37 ? 99  THR B OG1 1 
ATOM   3138 C  CG2 . THR B 1 52  ? -15.239 -1.893  26.118  1.00 14.24 ? 99  THR B CG2 1 
ATOM   3139 N  N   . ALA B 1 53  ? -15.089 -2.021  22.306  1.00 12.43 ? 100 ALA B N   1 
ATOM   3140 C  CA  . ALA B 1 53  ? -15.327 -3.142  21.423  1.00 13.23 ? 100 ALA B CA  1 
ATOM   3141 C  C   . ALA B 1 53  ? -14.041 -3.577  20.753  1.00 12.96 ? 100 ALA B C   1 
ATOM   3142 O  O   . ALA B 1 53  ? -13.738 -4.766  20.661  1.00 13.20 ? 100 ALA B O   1 
ATOM   3143 C  CB  . ALA B 1 53  ? -16.394 -2.771  20.412  1.00 14.38 ? 100 ALA B CB  1 
ATOM   3144 N  N   . ALA B 1 54  ? -13.237 -2.626  20.306  1.00 11.95 ? 101 ALA B N   1 
ATOM   3145 C  CA  . ALA B 1 54  ? -11.936 -2.953  19.752  1.00 11.64 ? 101 ALA B CA  1 
ATOM   3146 C  C   . ALA B 1 54  ? -11.017 -3.624  20.751  1.00 12.47 ? 101 ALA B C   1 
ATOM   3147 O  O   . ALA B 1 54  ? -10.338 -4.604  20.426  1.00 12.35 ? 101 ALA B O   1 
ATOM   3148 C  CB  . ALA B 1 54  ? -11.301 -1.714  19.166  1.00 13.41 ? 101 ALA B CB  1 
ATOM   3149 N  N   . ALA B 1 55  ? -10.989 -3.117  21.976  1.00 12.80 ? 102 ALA B N   1 
ATOM   3150 C  CA  . ALA B 1 55  ? -10.115 -3.655  23.012  1.00 12.43 ? 102 ALA B CA  1 
ATOM   3151 C  C   . ALA B 1 55  ? -10.496 -5.092  23.310  1.00 11.94 ? 102 ALA B C   1 
ATOM   3152 O  O   . ALA B 1 55  ? -9.629  -5.940  23.537  1.00 12.82 ? 102 ALA B O   1 
ATOM   3153 C  CB  . ALA B 1 55  ? -10.222 -2.773  24.247  1.00 13.62 ? 102 ALA B CB  1 
ATOM   3154 N  N   . ARG B 1 56  ? -11.781 -5.412  23.282  1.00 12.54 ? 103 ARG B N   1 
ATOM   3155 C  CA  . ARG B 1 56  ? -12.195 -6.799  23.502  1.00 14.06 ? 103 ARG B CA  1 
ATOM   3156 C  C   . ARG B 1 56  ? -11.598 -7.713  22.455  1.00 15.22 ? 103 ARG B C   1 
ATOM   3157 O  O   . ARG B 1 56  ? -11.205 -8.839  22.770  1.00 15.97 ? 103 ARG B O   1 
ATOM   3158 C  CB  . ARG B 1 56  ? -13.712 -6.971  23.473  1.00 17.01 ? 103 ARG B CB  1 
ATOM   3159 C  CG  . ARG B 1 56  ? -14.362 -6.414  24.713  1.00 16.95 ? 103 ARG B CG  1 
ATOM   3160 C  CD  . ARG B 1 56  ? -15.817 -6.891  24.590  1.00 19.10 ? 103 ARG B CD  1 
ATOM   3161 N  NE  . ARG B 1 56  ? -16.415 -6.308  25.761  1.00 20.34 ? 103 ARG B NE  1 
ATOM   3162 C  CZ  . ARG B 1 56  ? -17.084 -5.197  25.827  1.00 18.31 ? 103 ARG B CZ  1 
ATOM   3163 N  NH1 . ARG B 1 56  ? -17.442 -4.560  24.729  1.00 22.19 ? 103 ARG B NH1 1 
ATOM   3164 N  NH2 . ARG B 1 56  ? -17.429 -4.741  27.015  1.00 20.28 ? 103 ARG B NH2 1 
ATOM   3165 N  N   . ARG B 1 57  ? -11.606 -7.279  21.196  1.00 12.95 ? 104 ARG B N   1 
ATOM   3166 C  CA  . ARG B 1 57  ? -11.054 -8.090  20.141  1.00 14.01 ? 104 ARG B CA  1 
ATOM   3167 C  C   . ARG B 1 57  ? -9.542  -8.145  20.296  1.00 14.07 ? 104 ARG B C   1 
ATOM   3168 O  O   . ARG B 1 57  ? -8.971  -9.224  20.273  1.00 13.99 ? 104 ARG B O   1 
ATOM   3169 C  CB  . ARG B 1 57  ? -11.379 -7.471  18.793  1.00 16.43 ? 104 ARG B CB  1 
ATOM   3170 C  CG  . ARG B 1 57  ? -12.850 -7.535  18.425  1.00 21.05 ? 104 ARG B CG  1 
ATOM   3171 C  CD  . ARG B 1 57  ? -13.210 -8.918  17.992  1.00 26.90 ? 104 ARG B CD  1 
ATOM   3172 N  NE  . ARG B 1 57  ? -14.489 -8.859  17.286  1.00 34.55 ? 104 ARG B NE  1 
ATOM   3173 C  CZ  . ARG B 1 57  ? -14.683 -8.224  16.129  1.00 37.79 ? 104 ARG B CZ  1 
ATOM   3174 N  NH1 . ARG B 1 57  ? -13.650 -7.856  15.386  1.00 39.67 ? 104 ARG B NH1 1 
ATOM   3175 N  NH2 . ARG B 1 57  ? -15.916 -7.992  15.705  1.00 36.88 ? 104 ARG B NH2 1 
ATOM   3176 N  N   . LEU B 1 58  ? -8.898  -6.987  20.498  1.00 12.01 ? 105 LEU B N   1 
ATOM   3177 C  CA  . LEU B 1 58  ? -7.445  -6.941  20.512  1.00 12.45 ? 105 LEU B CA  1 
ATOM   3178 C  C   . LEU B 1 58  ? -6.876  -7.844  21.598  1.00 12.31 ? 105 LEU B C   1 
ATOM   3179 O  O   . LEU B 1 58  ? -5.871  -8.524  21.376  1.00 11.86 ? 105 LEU B O   1 
ATOM   3180 C  CB  . LEU B 1 58  ? -6.975  -5.494  20.678  1.00 11.81 ? 105 LEU B CB  1 
ATOM   3181 C  CG  . LEU B 1 58  ? -7.229  -4.562  19.487  1.00 11.93 ? 105 LEU B CG  1 
ATOM   3182 C  CD1 . LEU B 1 58  ? -7.142  -3.095  19.946  1.00 13.59 ? 105 LEU B CD1 1 
ATOM   3183 C  CD2 . LEU B 1 58  ? -6.262  -4.827  18.345  1.00 14.09 ? 105 LEU B CD2 1 
ATOM   3184 N  N   . THR B 1 59  ? -7.458  -7.826  22.786  1.00 11.94 ? 106 THR B N   1 
ATOM   3185 C  CA  . THR B 1 59  ? -6.904  -8.558  23.905  1.00 12.44 ? 106 THR B CA  1 
ATOM   3186 C  C   . THR B 1 59  ? -7.118  -10.053 23.772  1.00 13.79 ? 106 THR B C   1 
ATOM   3187 O  O   . THR B 1 59  ? -6.465  -10.787 24.510  1.00 16.58 ? 106 THR B O   1 
ATOM   3188 C  CB  . THR B 1 59  ? -7.428  -8.026  25.247  1.00 12.58 ? 106 THR B CB  1 
ATOM   3189 O  OG1 . THR B 1 59  ? -8.858  -8.071  25.236  1.00 14.48 ? 106 THR B OG1 1 
ATOM   3190 C  CG2 . THR B 1 59  ? -6.955  -6.613  25.515  1.00 13.82 ? 106 THR B CG2 1 
ATOM   3191 N  N   . ALA B 1 60  ? -8.010  -10.467 22.885  1.00 13.40 ? 107 ALA B N   1 
ATOM   3192 C  CA  . ALA B 1 60  ? -8.226  -11.882 22.592  1.00 14.50 ? 107 ALA B CA  1 
ATOM   3193 C  C   . ALA B 1 60  ? -7.434  -12.314 21.376  1.00 16.78 ? 107 ALA B C   1 
ATOM   3194 O  O   . ALA B 1 60  ? -7.572  -13.460 20.933  1.00 19.41 ? 107 ALA B O   1 
ATOM   3195 C  CB  . ALA B 1 60  ? -9.663  -12.128 22.379  1.00 16.82 ? 107 ALA B CB  1 
ATOM   3196 N  N   . GLY B 1 61  ? -6.631  -11.444 20.792  1.00 14.48 ? 108 GLY B N   1 
ATOM   3197 C  CA  . GLY B 1 61  ? -5.789  -11.777 19.647  1.00 15.68 ? 108 GLY B CA  1 
ATOM   3198 C  C   . GLY B 1 61  ? -6.551  -11.690 18.331  1.00 17.48 ? 108 GLY B C   1 
ATOM   3199 O  O   . GLY B 1 61  ? -6.086  -12.205 17.317  1.00 19.87 ? 108 GLY B O   1 
ATOM   3200 N  N   . HIS B 1 62  ? -7.720  -11.061 18.313  1.00 15.64 ? 109 HIS B N   1 
ATOM   3201 C  CA  . HIS B 1 62  ? -8.529  -10.931 17.099  1.00 15.75 ? 109 HIS B CA  1 
ATOM   3202 C  C   . HIS B 1 62  ? -8.405  -9.529  16.497  1.00 16.29 ? 109 HIS B C   1 
ATOM   3203 O  O   . HIS B 1 62  ? -8.088  -8.550  17.178  1.00 16.13 ? 109 HIS B O   1 
ATOM   3204 C  CB  . HIS B 1 62  ? -10.015 -11.169 17.378  1.00 20.08 ? 109 HIS B CB  1 
ATOM   3205 C  CG  . HIS B 1 62  ? -10.280 -12.496 18.008  1.00 25.86 ? 109 HIS B CG  1 
ATOM   3206 N  ND1 . HIS B 1 62  ? -9.730  -13.628 17.464  1.00 33.38 ? 109 HIS B ND1 1 
ATOM   3207 C  CD2 . HIS B 1 62  ? -10.989 -12.891 19.090  1.00 30.50 ? 109 HIS B CD2 1 
ATOM   3208 C  CE1 . HIS B 1 62  ? -10.092 -14.684 18.204  1.00 35.64 ? 109 HIS B CE1 1 
ATOM   3209 N  NE2 . HIS B 1 62  ? -10.831 -14.263 19.207  1.00 30.61 ? 109 HIS B NE2 1 
ATOM   3210 N  N   . ALA B 1 63  ? -8.591  -9.426  15.179  1.00 16.72 ? 110 ALA B N   1 
ATOM   3211 C  CA  . ALA B 1 63  ? -8.578  -8.141  14.513  1.00 14.82 ? 110 ALA B CA  1 
ATOM   3212 C  C   . ALA B 1 63  ? -9.808  -7.337  14.905  1.00 16.41 ? 110 ALA B C   1 
ATOM   3213 O  O   . ALA B 1 63  ? -10.857 -7.892  15.262  1.00 17.95 ? 110 ALA B O   1 
ATOM   3214 C  CB  . ALA B 1 63  ? -8.582  -8.344  13.012  1.00 17.68 ? 110 ALA B CB  1 
ATOM   3215 N  N   . VAL B 1 64  ? -9.668  -6.010  14.813  1.00 13.49 ? 111 VAL B N   1 
ATOM   3216 C  CA  . VAL B 1 64  ? -10.781 -5.112  15.058  1.00 14.67 ? 111 VAL B CA  1 
ATOM   3217 C  C   . VAL B 1 64  ? -11.781 -5.193  13.920  1.00 17.38 ? 111 VAL B C   1 
ATOM   3218 O  O   . VAL B 1 64  ? -11.447 -5.489  12.758  1.00 17.70 ? 111 VAL B O   1 
ATOM   3219 C  CB  . VAL B 1 64  ? -10.350 -3.666  15.363  1.00 20.12 ? 111 VAL B CB  1 
ATOM   3220 C  CG1 . VAL B 1 64  ? -9.367  -3.653  16.508  1.00 19.78 ? 111 VAL B CG1 1 
ATOM   3221 C  CG2 . VAL B 1 64  ? -9.770  -2.929  14.193  1.00 23.01 ? 111 VAL B CG2 1 
ATOM   3222 N  N   . GLY B 1 65  ? -13.020 -4.858  14.275  1.00 19.05 ? 112 GLY B N   1 
ATOM   3223 C  CA  . GLY B 1 65  ? -14.045 -4.641  13.267  1.00 20.36 ? 112 GLY B CA  1 
ATOM   3224 C  C   . GLY B 1 65  ? -14.287 -5.921  12.467  1.00 21.44 ? 112 GLY B C   1 
ATOM   3225 O  O   . GLY B 1 65  ? -14.305 -7.010  13.020  1.00 24.48 ? 112 GLY B O   1 
ATOM   3226 N  N   . GLU B 1 66  ? -14.462 -5.756  11.160  1.00 22.67 ? 113 GLU B N   1 
ATOM   3227 C  CA  . GLU B 1 66  ? -14.686 -6.911  10.295  1.00 27.28 ? 113 GLU B CA  1 
ATOM   3228 C  C   . GLU B 1 66  ? -13.364 -7.544  9.858   1.00 26.15 ? 113 GLU B C   1 
ATOM   3229 O  O   . GLU B 1 66  ? -13.369 -8.460  9.041   1.00 28.78 ? 113 GLU B O   1 
ATOM   3230 C  CB  . GLU B 1 66  ? -15.505 -6.566  9.051   1.00 33.64 ? 113 GLU B CB  1 
ATOM   3231 C  CG  . GLU B 1 66  ? -16.826 -5.856  9.354   1.00 41.78 ? 113 GLU B CG  1 
ATOM   3232 C  CD  . GLU B 1 66  ? -17.779 -5.723  8.175   1.00 50.81 ? 113 GLU B CD  1 
ATOM   3233 O  OE1 . GLU B 1 66  ? -18.222 -4.582  7.891   1.00 55.17 ? 113 GLU B OE1 1 
ATOM   3234 O  OE2 . GLU B 1 66  ? -18.082 -6.761  7.535   1.00 57.63 ? 113 GLU B OE2 1 
ATOM   3235 N  N   . GLY B 1 67  ? -12.211 -7.039  10.327  1.00 20.73 ? 114 GLY B N   1 
ATOM   3236 C  CA  . GLY B 1 67  ? -10.972 -7.762  10.108  1.00 18.66 ? 114 GLY B CA  1 
ATOM   3237 C  C   . GLY B 1 67  ? -9.945  -6.956  9.303   1.00 15.94 ? 114 GLY B C   1 
ATOM   3238 O  O   . GLY B 1 67  ? -10.142 -5.801  8.964   1.00 16.84 ? 114 GLY B O   1 
ATOM   3239 N  N   . ALA B 1 68  ? -8.849  -7.638  8.967   1.00 15.95 ? 115 ALA B N   1 
ATOM   3240 C  CA  . ALA B 1 68  ? -7.726  -7.037  8.307   1.00 16.38 ? 115 ALA B CA  1 
ATOM   3241 C  C   . ALA B 1 68  ? -7.717  -7.292  6.803   1.00 17.84 ? 115 ALA B C   1 
ATOM   3242 O  O   . ALA B 1 68  ? -6.904  -6.704  6.090   1.00 16.43 ? 115 ALA B O   1 
ATOM   3243 C  CB  . ALA B 1 68  ? -6.469  -7.558  8.929   1.00 16.00 ? 115 ALA B CB  1 
ATOM   3244 N  N   . TYR B 1 69  ? -8.573  -8.208  6.341   1.00 16.89 ? 116 TYR B N   1 
ATOM   3245 C  CA  . TYR B 1 69  ? -8.624  -8.566  4.932   1.00 20.77 ? 116 TYR B CA  1 
ATOM   3246 C  C   . TYR B 1 69  ? -9.937  -9.301  4.696   1.00 23.05 ? 116 TYR B C   1 
ATOM   3247 O  O   . TYR B 1 69  ? -10.654 -9.597  5.626   1.00 22.36 ? 116 TYR B O   1 
ATOM   3248 C  CB  . TYR B 1 69  ? -7.417  -9.392  4.483   1.00 21.38 ? 116 TYR B CB  1 
ATOM   3249 C  CG  . TYR B 1 69  ? -7.351  -10.762 5.119   1.00 19.81 ? 116 TYR B CG  1 
ATOM   3250 C  CD1 . TYR B 1 69  ? -6.808  -10.951 6.372   1.00 21.03 ? 116 TYR B CD1 1 
ATOM   3251 C  CD2 . TYR B 1 69  ? -7.844  -11.890 4.470   1.00 23.95 ? 116 TYR B CD2 1 
ATOM   3252 C  CE1 . TYR B 1 69  ? -6.747  -12.199 6.964   1.00 23.39 ? 116 TYR B CE1 1 
ATOM   3253 C  CE2 . TYR B 1 69  ? -7.826  -13.133 5.073   1.00 26.09 ? 116 TYR B CE2 1 
ATOM   3254 C  CZ  . TYR B 1 69  ? -7.264  -13.294 6.321   1.00 26.28 ? 116 TYR B CZ  1 
ATOM   3255 O  OH  . TYR B 1 69  ? -7.191  -14.504 6.968   1.00 33.85 ? 116 TYR B OH  1 
ATOM   3256 N  N   . GLY B 1 70  ? -10.276 -9.472  3.421   1.00 25.66 ? 117 GLY B N   1 
ATOM   3257 C  CA  . GLY B 1 70  ? -11.405 -10.304 3.046   1.00 31.43 ? 117 GLY B CA  1 
ATOM   3258 C  C   . GLY B 1 70  ? -12.726 -9.537  3.039   1.00 33.09 ? 117 GLY B C   1 
ATOM   3259 O  O   . GLY B 1 70  ? -13.770 -10.123 2.767   1.00 36.38 ? 117 GLY B O   1 
ATOM   3260 N  N   . GLY B 1 71  ? -12.687 -8.228  3.307   1.00 31.17 ? 118 GLY B N   1 
ATOM   3261 C  CA  . GLY B 1 71  ? -13.880 -7.417  3.185   1.00 29.41 ? 118 GLY B CA  1 
ATOM   3262 C  C   . GLY B 1 71  ? -14.002 -6.850  1.776   1.00 29.60 ? 118 GLY B C   1 
ATOM   3263 O  O   . GLY B 1 71  ? -13.341 -7.296  0.842   1.00 29.11 ? 118 GLY B O   1 
ATOM   3264 N  N   . LEU B 1 72  ? -14.824 -5.812  1.662   1.00 27.03 ? 119 LEU B N   1 
ATOM   3265 C  CA  . LEU B 1 72  ? -15.041 -5.129  0.399   1.00 29.61 ? 119 LEU B CA  1 
ATOM   3266 C  C   . LEU B 1 72  ? -13.702 -4.630  -0.131  1.00 25.34 ? 119 LEU B C   1 
ATOM   3267 O  O   . LEU B 1 72  ? -12.996 -3.869  0.539   1.00 24.56 ? 119 LEU B O   1 
ATOM   3268 C  CB  . LEU B 1 72  ? -15.998 -3.960  0.620   1.00 37.67 ? 119 LEU B CB  1 
ATOM   3269 C  CG  . LEU B 1 72  ? -17.424 -4.312  1.055   1.00 44.53 ? 119 LEU B CG  1 
ATOM   3270 C  CD1 . LEU B 1 72  ? -18.078 -3.076  1.667   1.00 48.52 ? 119 LEU B CD1 1 
ATOM   3271 C  CD2 . LEU B 1 72  ? -18.224 -4.848  -0.126  1.00 44.00 ? 119 LEU B CD2 1 
ATOM   3272 N  N   . PRO B 1 73  ? -13.295 -5.011  -1.359  1.00 22.97 ? 120 PRO B N   1 
ATOM   3273 C  CA  . PRO B 1 73  ? -12.038 -4.493  -1.909  1.00 23.66 ? 120 PRO B CA  1 
ATOM   3274 C  C   . PRO B 1 73  ? -11.910 -2.971  -1.922  1.00 22.68 ? 120 PRO B C   1 
ATOM   3275 O  O   . PRO B 1 73  ? -10.804 -2.435  -1.800  1.00 19.96 ? 120 PRO B O   1 
ATOM   3276 C  CB  . PRO B 1 73  ? -12.025 -5.098  -3.338  1.00 26.73 ? 120 PRO B CB  1 
ATOM   3277 C  CG  . PRO B 1 73  ? -12.835 -6.377  -3.176  1.00 28.29 ? 120 PRO B CG  1 
ATOM   3278 C  CD  . PRO B 1 73  ? -13.937 -6.037  -2.207  1.00 27.22 ? 120 PRO B CD  1 
ATOM   3279 N  N   . GLU B 1 74  ? -13.028 -2.241  -2.085  1.00 20.76 ? 121 GLU B N   1 
ATOM   3280 C  CA  . GLU B 1 74  ? -12.982 -0.801  -2.262  1.00 22.60 ? 121 GLU B CA  1 
ATOM   3281 C  C   . GLU B 1 74  ? -13.031 -0.057  -0.922  1.00 21.53 ? 121 GLU B C   1 
ATOM   3282 O  O   . GLU B 1 74  ? -13.030 1.178   -0.890  1.00 23.45 ? 121 GLU B O   1 
ATOM   3283 C  CB  . GLU B 1 74  ? -14.164 -0.372  -3.143  1.00 29.86 ? 121 GLU B CB  1 
ATOM   3284 C  CG  . GLU B 1 74  ? -15.527 -0.783  -2.594  1.00 37.83 ? 121 GLU B CG  1 
ATOM   3285 C  CD  . GLU B 1 74  ? -16.056 -2.183  -2.919  1.00 41.46 ? 121 GLU B CD  1 
ATOM   3286 O  OE1 . GLU B 1 74  ? -15.405 -3.009  -3.610  1.00 40.97 ? 121 GLU B OE1 1 
ATOM   3287 O  OE2 . GLU B 1 74  ? -17.191 -2.429  -2.440  1.00 53.93 ? 121 GLU B OE2 1 
ATOM   3288 N  N   . ALA B 1 75  ? -13.031 -0.793  0.186   1.00 19.69 ? 122 ALA B N   1 
ATOM   3289 C  CA  . ALA B 1 75  ? -13.038 -0.174  1.508   1.00 19.51 ? 122 ALA B CA  1 
ATOM   3290 C  C   . ALA B 1 75  ? -11.677 -0.353  2.170   1.00 18.00 ? 122 ALA B C   1 
ATOM   3291 O  O   . ALA B 1 75  ? -11.020 -1.373  1.972   1.00 16.31 ? 122 ALA B O   1 
ATOM   3292 C  CB  . ALA B 1 75  ? -14.097 -0.769  2.367   1.00 22.15 ? 122 ALA B CB  1 
ATOM   3293 N  N   . PRO B 1 76  ? -11.236 0.626   2.977   1.00 18.26 ? 123 PRO B N   1 
ATOM   3294 C  CA  . PRO B 1 76  ? -10.036 0.416   3.788   1.00 17.64 ? 123 PRO B CA  1 
ATOM   3295 C  C   . PRO B 1 76  ? -10.355 -0.731  4.726   1.00 16.32 ? 123 PRO B C   1 
ATOM   3296 O  O   . PRO B 1 76  ? -11.457 -0.850  5.265   1.00 18.48 ? 123 PRO B O   1 
ATOM   3297 C  CB  . PRO B 1 76  ? -9.822  1.736   4.524   1.00 18.88 ? 123 PRO B CB  1 
ATOM   3298 C  CG  . PRO B 1 76  ? -10.745 2.706   3.803   1.00 22.94 ? 123 PRO B CG  1 
ATOM   3299 C  CD  . PRO B 1 76  ? -11.903 1.905   3.241   1.00 20.72 ? 123 PRO B CD  1 
ATOM   3300 N  N   . PRO B 1 77  ? -9.380  -1.599  5.044   1.00 16.12 ? 124 PRO B N   1 
ATOM   3301 C  CA  . PRO B 1 77  ? -9.606  -2.623  6.054   1.00 17.12 ? 124 PRO B CA  1 
ATOM   3302 C  C   . PRO B 1 77  ? -9.849  -2.017  7.438   1.00 16.84 ? 124 PRO B C   1 
ATOM   3303 O  O   . PRO B 1 77  ? -9.276  -0.999  7.776   1.00 16.94 ? 124 PRO B O   1 
ATOM   3304 C  CB  . PRO B 1 77  ? -8.338  -3.454  6.006   1.00 20.30 ? 124 PRO B CB  1 
ATOM   3305 C  CG  . PRO B 1 77  ? -7.316  -2.584  5.367   1.00 20.78 ? 124 PRO B CG  1 
ATOM   3306 C  CD  . PRO B 1 77  ? -8.052  -1.660  4.420   1.00 16.54 ? 124 PRO B CD  1 
ATOM   3307 N  N   . ASP B 1 78  ? -10.666 -2.685  8.238   1.00 16.45 ? 125 ASP B N   1 
ATOM   3308 C  CA  . ASP B 1 78  ? -11.006 -2.200  9.561   1.00 15.39 ? 125 ASP B CA  1 
ATOM   3309 C  C   . ASP B 1 78  ? -9.824  -2.326  10.508  1.00 15.21 ? 125 ASP B C   1 
ATOM   3310 O  O   . ASP B 1 78  ? -9.674  -1.494  11.398  1.00 18.33 ? 125 ASP B O   1 
ATOM   3311 C  CB  . ASP B 1 78  ? -12.161 -2.970  10.152  1.00 17.18 ? 125 ASP B CB  1 
ATOM   3312 C  CG  . ASP B 1 78  ? -13.562 -2.573  9.679   1.00 23.27 ? 125 ASP B CG  1 
ATOM   3313 O  OD1 . ASP B 1 78  ? -13.666 -1.633  8.881   1.00 26.12 ? 125 ASP B OD1 1 
ATOM   3314 O  OD2 . ASP B 1 78  ? -14.483 -3.287  10.106  1.00 27.22 ? 125 ASP B OD2 1 
ATOM   3315 N  N   . ASP B 1 79  ? -8.961  -3.315  10.290  1.00 13.72 ? 126 ASP B N   1 
ATOM   3316 C  CA  . ASP B 1 79  ? -7.774  -3.537  11.092  1.00 13.12 ? 126 ASP B CA  1 
ATOM   3317 C  C   . ASP B 1 79  ? -6.566  -3.405  10.190  1.00 12.35 ? 126 ASP B C   1 
ATOM   3318 O  O   . ASP B 1 79  ? -6.636  -3.860  9.069   1.00 13.90 ? 126 ASP B O   1 
ATOM   3319 C  CB  . ASP B 1 79  ? -7.841  -4.894  11.750  1.00 13.53 ? 126 ASP B CB  1 
ATOM   3320 C  CG  . ASP B 1 79  ? -6.716  -5.156  12.746  1.00 13.33 ? 126 ASP B CG  1 
ATOM   3321 O  OD1 . ASP B 1 79  ? -5.556  -5.236  12.287  1.00 13.34 ? 126 ASP B OD1 1 
ATOM   3322 O  OD2 . ASP B 1 79  ? -7.004  -5.304  13.942  1.00 15.20 ? 126 ASP B OD2 1 
ATOM   3323 N  N   . THR B 1 80  ? -5.527  -2.718  10.633  1.00 11.37 ? 127 THR B N   1 
ATOM   3324 C  CA  . THR B 1 80  ? -4.388  -2.422  9.788   1.00 11.18 ? 127 THR B CA  1 
ATOM   3325 C  C   . THR B 1 80  ? -3.487  -3.624  9.526   1.00 11.32 ? 127 THR B C   1 
ATOM   3326 O  O   . THR B 1 80  ? -2.643  -3.537  8.618   1.00 12.86 ? 127 THR B O   1 
ATOM   3327 C  CB  . THR B 1 80  ? -3.624  -1.230  10.363  1.00 12.08 ? 127 THR B CB  1 
ATOM   3328 O  OG1 . THR B 1 80  ? -3.127  -1.577  11.653  1.00 12.07 ? 127 THR B OG1 1 
ATOM   3329 C  CG2 . THR B 1 80  ? -4.503  0.007   10.389  1.00 12.82 ? 127 THR B CG2 1 
ATOM   3330 N  N   . GLY B 1 81  ? -3.652  -4.741  10.238  1.00 11.19 ? 128 GLY B N   1 
ATOM   3331 C  CA  . GLY B 1 81  ? -3.134  -6.027  9.778   1.00 11.36 ? 128 GLY B CA  1 
ATOM   3332 C  C   . GLY B 1 81  ? -1.778  -6.454  10.315  1.00 13.40 ? 128 GLY B C   1 
ATOM   3333 O  O   . GLY B 1 81  ? -1.387  -7.597  10.118  1.00 14.54 ? 128 GLY B O   1 
ATOM   3334 N  N   . GLU B 1 82  ? -1.021  -5.587  10.974  1.00 11.83 ? 129 GLU B N   1 
ATOM   3335 C  CA  . GLU B 1 82  ? 0.337   -5.936  11.356  1.00 12.27 ? 129 GLU B CA  1 
ATOM   3336 C  C   . GLU B 1 82  ? 0.409   -6.928  12.505  1.00 12.74 ? 129 GLU B C   1 
ATOM   3337 O  O   . GLU B 1 82  ? 1.519   -7.375  12.816  1.00 15.05 ? 129 GLU B O   1 
ATOM   3338 C  CB  . GLU B 1 82  ? 1.201   -4.700  11.583  1.00 12.98 ? 129 GLU B CB  1 
ATOM   3339 C  CG  . GLU B 1 82  ? 0.877   -3.904  12.849  1.00 13.05 ? 129 GLU B CG  1 
ATOM   3340 C  CD  . GLU B 1 82  ? -0.173  -2.852  12.683  1.00 13.07 ? 129 GLU B CD  1 
ATOM   3341 O  OE1 . GLU B 1 82  ? -1.025  -2.933  11.779  1.00 12.41 ? 129 GLU B OE1 1 
ATOM   3342 O  OE2 . GLU B 1 82  ? -0.122  -1.897  13.473  1.00 13.12 ? 129 GLU B OE2 1 
ATOM   3343 N  N   . ALA B 1 83  ? -0.707  -7.293  13.156  1.00 11.32 ? 130 ALA B N   1 
ATOM   3344 C  CA  . ALA B 1 83  ? -0.660  -8.326  14.192  1.00 12.28 ? 130 ALA B CA  1 
ATOM   3345 C  C   . ALA B 1 83  ? -1.213  -9.665  13.707  1.00 12.93 ? 130 ALA B C   1 
ATOM   3346 O  O   . ALA B 1 83  ? -1.377  -10.589 14.497  1.00 14.29 ? 130 ALA B O   1 
ATOM   3347 C  CB  . ALA B 1 83  ? -1.387  -7.858  15.436  1.00 13.49 ? 130 ALA B CB  1 
ATOM   3348 N  N   . LEU B 1 84  ? -1.567  -9.755  12.429  1.00 12.43 ? 131 LEU B N   1 
ATOM   3349 C  CA  . LEU B 1 84  ? -2.043  -11.028 11.937  1.00 14.52 ? 131 LEU B CA  1 
ATOM   3350 C  C   . LEU B 1 84  ? -0.952  -12.069 12.114  1.00 15.44 ? 131 LEU B C   1 
ATOM   3351 O  O   . LEU B 1 84  ? 0.228   -11.849 11.839  1.00 18.31 ? 131 LEU B O   1 
ATOM   3352 C  CB  . LEU B 1 84  ? -2.392  -10.958 10.473  1.00 14.43 ? 131 LEU B CB  1 
ATOM   3353 C  CG  . LEU B 1 84  ? -3.636  -10.166 10.121  1.00 18.09 ? 131 LEU B CG  1 
ATOM   3354 C  CD1 . LEU B 1 84  ? -3.608  -10.039 8.587   1.00 19.65 ? 131 LEU B CD1 1 
ATOM   3355 C  CD2 . LEU B 1 84  ? -4.866  -10.865 10.664  1.00 21.46 ? 131 LEU B CD2 1 
ATOM   3356 N  N   . GLY B 1 85  ? -1.375  -13.206 12.628  1.00 18.09 ? 132 GLY B N   1 
ATOM   3357 C  CA  . GLY B 1 85  ? -0.441  -14.300 12.835  1.00 19.20 ? 132 GLY B CA  1 
ATOM   3358 C  C   . GLY B 1 85  ? 0.246   -14.288 14.188  1.00 19.82 ? 132 GLY B C   1 
ATOM   3359 O  O   . GLY B 1 85  ? 0.985   -15.206 14.511  1.00 20.71 ? 132 GLY B O   1 
ATOM   3360 N  N   . LEU B 1 86  ? 0.011   -13.250 14.984  1.00 16.59 ? 133 LEU B N   1 
ATOM   3361 C  CA  . LEU B 1 86  ? 0.625   -13.155 16.291  1.00 16.29 ? 133 LEU B CA  1 
ATOM   3362 C  C   . LEU B 1 86  ? -0.375  -13.645 17.323  1.00 16.98 ? 133 LEU B C   1 
ATOM   3363 O  O   . LEU B 1 86  ? -1.569  -13.766 17.096  1.00 22.21 ? 133 LEU B O   1 
ATOM   3364 C  CB  . LEU B 1 86  ? 1.039   -11.711 16.576  1.00 16.57 ? 133 LEU B CB  1 
ATOM   3365 C  CG  . LEU B 1 86  ? 2.027   -11.097 15.575  1.00 16.84 ? 133 LEU B CG  1 
ATOM   3366 C  CD1 . LEU B 1 86  ? 2.422   -9.709  15.979  1.00 18.10 ? 133 LEU B CD1 1 
ATOM   3367 C  CD2 . LEU B 1 86  ? 3.282   -11.972 15.401  1.00 18.62 ? 133 LEU B CD2 1 
ATOM   3368 N  N   . LYS B 1 87  ? 0.158   -13.927 18.493  1.00 18.38 ? 134 LYS B N   1 
ATOM   3369 C  CA  . LYS B 1 87  ? -0.673  -14.418 19.578  1.00 18.78 ? 134 LYS B CA  1 
ATOM   3370 C  C   . LYS B 1 87  ? -1.185  -13.250 20.414  1.00 15.98 ? 134 LYS B C   1 
ATOM   3371 O  O   . LYS B 1 87  ? -0.684  -12.145 20.286  1.00 14.93 ? 134 LYS B O   1 
ATOM   3372 C  CB  . LYS B 1 87  ? 0.222   -15.250 20.504  1.00 22.35 ? 134 LYS B CB  1 
ATOM   3373 C  CG  . LYS B 1 87  ? 0.871   -16.503 19.882  1.00 32.76 ? 134 LYS B CG  1 
ATOM   3374 C  CD  . LYS B 1 87  ? -0.178  -17.535 19.485  1.00 41.29 ? 134 LYS B CD  1 
ATOM   3375 C  CE  . LYS B 1 87  ? 0.355   -18.934 19.244  1.00 48.80 ? 134 LYS B CE  1 
ATOM   3376 N  NZ  . LYS B 1 87  ? 0.962   -19.102 17.917  1.00 52.54 ? 134 LYS B NZ  1 
ATOM   3377 N  N   . PRO B 1 88  ? -2.153  -13.451 21.323  1.00 14.27 ? 135 PRO B N   1 
ATOM   3378 C  CA  . PRO B 1 88  ? -2.611  -12.366 22.193  1.00 15.68 ? 135 PRO B CA  1 
ATOM   3379 C  C   . PRO B 1 88  ? -1.483  -11.746 22.992  1.00 14.22 ? 135 PRO B C   1 
ATOM   3380 O  O   . PRO B 1 88  ? -1.522  -10.557 23.333  1.00 15.04 ? 135 PRO B O   1 
ATOM   3381 C  CB  . PRO B 1 88  ? -3.638  -12.999 23.125  1.00 17.03 ? 135 PRO B CB  1 
ATOM   3382 C  CG  . PRO B 1 88  ? -4.074  -14.243 22.422  1.00 19.43 ? 135 PRO B CG  1 
ATOM   3383 C  CD  . PRO B 1 88  ? -2.942  -14.685 21.514  1.00 16.34 ? 135 PRO B CD  1 
ATOM   3384 N  N   . SER B 1 89  ? -0.517  -12.558 23.385  1.00 12.70 ? 136 SER B N   1 
ATOM   3385 C  CA  A SER B 1 89  ? 0.697   -12.059 23.981  0.50 11.71 ? 136 SER B CA  1 
ATOM   3386 C  CA  B SER B 1 89  ? 0.713   -12.150 24.042  0.50 12.22 ? 136 SER B CA  1 
ATOM   3387 C  C   . SER B 1 89  ? 0.430   -11.387 25.326  1.00 11.94 ? 136 SER B C   1 
ATOM   3388 O  O   . SER B 1 89  ? 1.114   -10.431 25.675  1.00 12.07 ? 136 SER B O   1 
ATOM   3389 C  CB  A SER B 1 89  ? 1.344   -11.071 23.003  0.50 12.95 ? 136 SER B CB  1 
ATOM   3390 C  CB  B SER B 1 89  ? 1.617   -11.335 23.134  0.50 14.70 ? 136 SER B CB  1 
ATOM   3391 O  OG  A SER B 1 89  ? 2.732   -10.973 23.267  0.50 13.52 ? 136 SER B OG  1 
ATOM   3392 O  OG  B SER B 1 89  ? 1.862   -12.023 21.918  0.50 16.65 ? 136 SER B OG  1 
ATOM   3393 N  N   . ARG B 1 90  ? -0.570  -11.833 26.052  1.00 10.91 ? 137 ARG B N   1 
ATOM   3394 C  CA  . ARG B 1 90  ? -0.933  -11.240 27.315  1.00 11.77 ? 137 ARG B CA  1 
ATOM   3395 C  C   . ARG B 1 90  ? -1.226  -9.748  27.192  1.00 11.09 ? 137 ARG B C   1 
ATOM   3396 O  O   . ARG B 1 90  ? -1.078  -9.014  28.167  1.00 11.68 ? 137 ARG B O   1 
ATOM   3397 C  CB  . ARG B 1 90  ? 0.105   -11.506 28.397  1.00 12.11 ? 137 ARG B CB  1 
ATOM   3398 C  CG  . ARG B 1 90  ? 0.330   -12.996 28.676  1.00 12.41 ? 137 ARG B CG  1 
ATOM   3399 C  CD  . ARG B 1 90  ? 1.134   -13.246 29.887  1.00 12.57 ? 137 ARG B CD  1 
ATOM   3400 N  NE  . ARG B 1 90  ? 2.482   -12.673 29.838  1.00 12.53 ? 137 ARG B NE  1 
ATOM   3401 C  CZ  . ARG B 1 90  ? 3.272   -12.506 30.850  1.00 12.88 ? 137 ARG B CZ  1 
ATOM   3402 N  NH1 . ARG B 1 90  ? 4.470   -11.960 30.726  1.00 14.95 ? 137 ARG B NH1 1 
ATOM   3403 N  NH2 . ARG B 1 90  ? 2.882   -12.947 32.033  1.00 14.80 ? 137 ARG B NH2 1 
ATOM   3404 N  N   . LEU B 1 91  ? -1.750  -9.301  26.050  1.00 9.77  ? 138 LEU B N   1 
ATOM   3405 C  CA  . LEU B 1 91  ? -2.058  -7.894  25.873  1.00 9.86  ? 138 LEU B CA  1 
ATOM   3406 C  C   . LEU B 1 91  ? -3.071  -7.450  26.921  1.00 10.01 ? 138 LEU B C   1 
ATOM   3407 O  O   . LEU B 1 91  ? -4.147  -8.042  27.062  1.00 11.33 ? 138 LEU B O   1 
ATOM   3408 C  CB  . LEU B 1 91  ? -2.613  -7.638  24.499  1.00 10.02 ? 138 LEU B CB  1 
ATOM   3409 C  CG  . LEU B 1 91  ? -3.033  -6.191  24.225  1.00 10.33 ? 138 LEU B CG  1 
ATOM   3410 C  CD1 . LEU B 1 91  ? -1.858  -5.242  24.172  1.00 11.87 ? 138 LEU B CD1 1 
ATOM   3411 C  CD2 . LEU B 1 91  ? -3.810  -6.086  22.917  1.00 11.39 ? 138 LEU B CD2 1 
ATOM   3412 N  N   . THR B 1 92  ? -2.766  -6.322  27.562  1.00 10.34 ? 139 THR B N   1 
ATOM   3413 C  CA  . THR B 1 92  ? -3.735  -5.574  28.335  1.00 10.50 ? 139 THR B CA  1 
ATOM   3414 C  C   . THR B 1 92  ? -3.761  -4.140  27.829  1.00 10.12 ? 139 THR B C   1 
ATOM   3415 O  O   . THR B 1 92  ? -2.760  -3.629  27.360  1.00 10.31 ? 139 THR B O   1 
ATOM   3416 C  CB  . THR B 1 92  ? -3.483  -5.614  29.838  1.00 9.89  ? 139 THR B CB  1 
ATOM   3417 O  OG1 . THR B 1 92  ? -2.172  -5.104  30.105  1.00 10.35 ? 139 THR B OG1 1 
ATOM   3418 C  CG2 . THR B 1 92  ? -3.600  -7.022  30.361  1.00 11.37 ? 139 THR B CG2 1 
ATOM   3419 N  N   . LEU B 1 93  ? -4.938  -3.543  27.873  1.00 9.55  ? 140 LEU B N   1 
ATOM   3420 C  CA  . LEU B 1 93  ? -5.208  -2.161  27.459  1.00 9.56  ? 140 LEU B CA  1 
ATOM   3421 C  C   . LEU B 1 93  ? -5.887  -1.489  28.629  1.00 10.69 ? 140 LEU B C   1 
ATOM   3422 O  O   . LEU B 1 93  ? -6.977  -1.902  29.007  1.00 13.22 ? 140 LEU B O   1 
ATOM   3423 C  CB  . LEU B 1 93  ? -6.102  -2.147  26.234  1.00 10.58 ? 140 LEU B CB  1 
ATOM   3424 C  CG  . LEU B 1 93  ? -5.448  -2.715  24.970  1.00 11.77 ? 140 LEU B CG  1 
ATOM   3425 C  CD1 . LEU B 1 93  ? -6.473  -2.824  23.839  1.00 13.79 ? 140 LEU B CD1 1 
ATOM   3426 C  CD2 . LEU B 1 93  ? -4.290  -1.841  24.519  1.00 13.71 ? 140 LEU B CD2 1 
ATOM   3427 N  N   . THR B 1 94  ? -5.227  -0.465  29.165  1.00 10.46 ? 141 THR B N   1 
ATOM   3428 C  CA  . THR B 1 94  ? -5.719  0.218   30.355  1.00 9.69  ? 141 THR B CA  1 
ATOM   3429 C  C   . THR B 1 94  ? -5.910  1.684   29.987  1.00 10.52 ? 141 THR B C   1 
ATOM   3430 O  O   . THR B 1 94  ? -4.964  2.320   29.549  1.00 11.90 ? 141 THR B O   1 
ATOM   3431 C  CB  . THR B 1 94  ? -4.685  0.095   31.457  1.00 10.44 ? 141 THR B CB  1 
ATOM   3432 O  OG1 . THR B 1 94  ? -4.320  -1.278  31.617  1.00 11.83 ? 141 THR B OG1 1 
ATOM   3433 C  CG2 . THR B 1 94  ? -5.178  0.601   32.788  1.00 12.07 ? 141 THR B CG2 1 
ATOM   3434 N  N   . ILE B 1 95  ? -7.112  2.204   30.189  1.00 9.94  ? 142 ILE B N   1 
ATOM   3435 C  CA  . ILE B 1 95  ? -7.375  3.589   29.834  1.00 10.51 ? 142 ILE B CA  1 
ATOM   3436 C  C   . ILE B 1 95  ? -7.340  4.463   31.080  1.00 10.90 ? 142 ILE B C   1 
ATOM   3437 O  O   . ILE B 1 95  ? -7.687  4.017   32.165  1.00 11.14 ? 142 ILE B O   1 
ATOM   3438 C  CB  . ILE B 1 95  ? -8.728  3.691   29.111  1.00 11.81 ? 142 ILE B CB  1 
ATOM   3439 C  CG1 . ILE B 1 95  ? -8.889  5.066   28.445  1.00 14.03 ? 142 ILE B CG1 1 
ATOM   3440 C  CG2 . ILE B 1 95  ? -9.920  3.329   30.005  1.00 14.11 ? 142 ILE B CG2 1 
ATOM   3441 C  CD1 . ILE B 1 95  ? -10.027 5.150   27.445  1.00 15.70 ? 142 ILE B CD1 1 
ATOM   3442 N  N   . GLY B 1 96  ? -6.949  5.730   30.909  1.00 10.01 ? 143 GLY B N   1 
ATOM   3443 C  CA  . GLY B 1 96  ? -6.994  6.691   32.000  1.00 11.16 ? 143 GLY B CA  1 
ATOM   3444 C  C   . GLY B 1 96  ? -7.394  8.055   31.474  1.00 10.60 ? 143 GLY B C   1 
ATOM   3445 O  O   . GLY B 1 96  ? -7.200  8.358   30.315  1.00 11.34 ? 143 GLY B O   1 
ATOM   3446 N  N   . PHE B 1 97  ? -7.908  8.877   32.391  1.00 10.79 ? 144 PHE B N   1 
ATOM   3447 C  CA  . PHE B 1 97  ? -8.412  10.218  32.077  1.00 10.83 ? 144 PHE B CA  1 
ATOM   3448 C  C   . PHE B 1 97  ? -7.569  11.250  32.787  1.00 10.44 ? 144 PHE B C   1 
ATOM   3449 O  O   . PHE B 1 97  ? -7.432  11.206  34.005  1.00 11.59 ? 144 PHE B O   1 
ATOM   3450 C  CB  . PHE B 1 97  ? -9.865  10.338  32.529  1.00 12.60 ? 144 PHE B CB  1 
ATOM   3451 C  CG  . PHE B 1 97  ? -10.818 9.357   31.876  1.00 13.90 ? 144 PHE B CG  1 
ATOM   3452 C  CD1 . PHE B 1 97  ? -10.665 8.943   30.557  1.00 16.38 ? 144 PHE B CD1 1 
ATOM   3453 C  CD2 . PHE B 1 97  ? -11.856 8.817   32.623  1.00 15.91 ? 144 PHE B CD2 1 
ATOM   3454 C  CE1 . PHE B 1 97  ? -11.590 8.076   29.992  1.00 18.84 ? 144 PHE B CE1 1 
ATOM   3455 C  CE2 . PHE B 1 97  ? -12.735 7.928   32.063  1.00 18.20 ? 144 PHE B CE2 1 
ATOM   3456 C  CZ  . PHE B 1 97  ? -12.601 7.566   30.750  1.00 17.49 ? 144 PHE B CZ  1 
ATOM   3457 N  N   . GLY B 1 98  ? -7.042  12.215  32.048  1.00 10.70 ? 145 GLY B N   1 
ATOM   3458 C  CA  . GLY B 1 98  ? -6.234  13.268  32.639  1.00 11.03 ? 145 GLY B CA  1 
ATOM   3459 C  C   . GLY B 1 98  ? -7.068  14.411  33.192  1.00 11.74 ? 145 GLY B C   1 
ATOM   3460 O  O   . GLY B 1 98  ? -8.233  14.564  32.833  1.00 12.47 ? 145 GLY B O   1 
ATOM   3461 N  N   . PRO B 1 99  ? -6.460  15.261  34.033  1.00 12.29 ? 146 PRO B N   1 
ATOM   3462 C  CA  . PRO B 1 99  ? -7.214  16.384  34.618  1.00 13.09 ? 146 PRO B CA  1 
ATOM   3463 C  C   . PRO B 1 99  ? -7.844  17.248  33.543  1.00 14.04 ? 146 PRO B C   1 
ATOM   3464 O  O   . PRO B 1 99  ? -8.905  17.808  33.766  1.00 15.54 ? 146 PRO B O   1 
ATOM   3465 C  CB  . PRO B 1 99  ? -6.191  17.151  35.401  1.00 16.39 ? 146 PRO B CB  1 
ATOM   3466 C  CG  . PRO B 1 99  ? -5.029  16.259  35.545  1.00 16.99 ? 146 PRO B CG  1 
ATOM   3467 C  CD  . PRO B 1 99  ? -5.132  15.111  34.595  1.00 13.77 ? 146 PRO B CD  1 
ATOM   3468 N  N   . SER B 1 100 ? -7.185  17.400  32.399  1.00 12.95 ? 147 SER B N   1 
ATOM   3469 C  CA  . SER B 1 100 ? -7.639  18.309  31.370  1.00 13.66 ? 147 SER B CA  1 
ATOM   3470 C  C   . SER B 1 100 ? -8.941  17.828  30.716  1.00 13.79 ? 147 SER B C   1 
ATOM   3471 O  O   . SER B 1 100 ? -9.693  18.625  30.187  1.00 16.22 ? 147 SER B O   1 
ATOM   3472 C  CB  . SER B 1 100 ? -6.534  18.590  30.379  1.00 16.01 ? 147 SER B CB  1 
ATOM   3473 O  OG  . SER B 1 100 ? -6.005  17.375  29.854  1.00 15.54 ? 147 SER B OG  1 
ATOM   3474 N  N   . LEU B 1 101 ? -9.258  16.526  30.778  1.00 12.94 ? 148 LEU B N   1 
ATOM   3475 C  CA  . LEU B 1 101 ? -10.492 16.018  30.234  1.00 13.43 ? 148 LEU B CA  1 
ATOM   3476 C  C   . LEU B 1 101 ? -11.664 16.650  30.951  1.00 14.49 ? 148 LEU B C   1 
ATOM   3477 O  O   . LEU B 1 101 ? -12.709 16.806  30.348  1.00 15.01 ? 148 LEU B O   1 
ATOM   3478 C  CB  . LEU B 1 101 ? -10.482 14.497  30.371  1.00 14.03 ? 148 LEU B CB  1 
ATOM   3479 C  CG  . LEU B 1 101 ? -11.666 13.825  29.708  1.00 17.87 ? 148 LEU B CG  1 
ATOM   3480 C  CD1 . LEU B 1 101 ? -11.561 13.921  28.222  1.00 19.60 ? 148 LEU B CD1 1 
ATOM   3481 C  CD2 . LEU B 1 101 ? -11.828 12.384  30.141  1.00 21.14 ? 148 LEU B CD2 1 
ATOM   3482 N  N   . PHE B 1 102 ? -11.488 16.935  32.238  1.00 14.77 ? 149 PHE B N   1 
ATOM   3483 C  CA  . PHE B 1 102 ? -12.591 17.394  33.068  1.00 15.33 ? 149 PHE B CA  1 
ATOM   3484 C  C   . PHE B 1 102 ? -12.974 18.840  32.788  1.00 17.25 ? 149 PHE B C   1 
ATOM   3485 O  O   . PHE B 1 102 ? -14.038 19.229  33.241  1.00 22.62 ? 149 PHE B O   1 
ATOM   3486 C  CB  . PHE B 1 102 ? -12.285 17.140  34.538  1.00 14.60 ? 149 PHE B CB  1 
ATOM   3487 C  CG  . PHE B 1 102 ? -12.179 15.648  34.810  1.00 13.47 ? 149 PHE B CG  1 
ATOM   3488 C  CD1 . PHE B 1 102 ? -13.270 14.895  35.157  1.00 14.84 ? 149 PHE B CD1 1 
ATOM   3489 C  CD2 . PHE B 1 102 ? -10.937 15.006  34.711  1.00 14.99 ? 149 PHE B CD2 1 
ATOM   3490 C  CE1 . PHE B 1 102 ? -13.167 13.543  35.341  1.00 14.66 ? 149 PHE B CE1 1 
ATOM   3491 C  CE2 . PHE B 1 102 ? -10.845 13.635  34.907  1.00 14.76 ? 149 PHE B CE2 1 
ATOM   3492 C  CZ  . PHE B 1 102 ? -11.964 12.917  35.220  1.00 14.69 ? 149 PHE B CZ  1 
ATOM   3493 N  N   . THR B 1 103 ? -12.213 19.551  31.982  1.00 16.07 ? 150 THR B N   1 
ATOM   3494 C  CA  . THR B 1 103 ? -12.657 20.862  31.528  1.00 18.36 ? 150 THR B CA  1 
ATOM   3495 C  C   . THR B 1 103 ? -13.594 20.756  30.326  1.00 20.23 ? 150 THR B C   1 
ATOM   3496 O  O   . THR B 1 103 ? -14.113 21.777  29.843  1.00 21.46 ? 150 THR B O   1 
ATOM   3497 C  CB  . THR B 1 103 ? -11.427 21.701  31.195  1.00 20.40 ? 150 THR B CB  1 
ATOM   3498 O  OG1 . THR B 1 103 ? -10.871 21.234  29.980  1.00 22.27 ? 150 THR B OG1 1 
ATOM   3499 C  CG2 . THR B 1 103 ? -10.349 21.681  32.257  1.00 22.01 ? 150 THR B CG2 1 
ATOM   3500 N  N   . ARG B 1 104 ? -13.835 19.543  29.804  1.00 16.96 ? 151 ARG B N   1 
ATOM   3501 C  CA  . ARG B 1 104 ? -14.729 19.302  28.684  1.00 18.17 ? 151 ARG B CA  1 
ATOM   3502 C  C   . ARG B 1 104 ? -15.992 18.607  29.175  1.00 16.45 ? 151 ARG B C   1 
ATOM   3503 O  O   . ARG B 1 104 ? -16.029 18.043  30.272  1.00 15.87 ? 151 ARG B O   1 
ATOM   3504 C  CB  . ARG B 1 104 ? -14.127 18.371  27.615  1.00 20.63 ? 151 ARG B CB  1 
ATOM   3505 C  CG  . ARG B 1 104 ? -12.938 19.017  26.923  1.00 25.40 ? 151 ARG B CG  1 
ATOM   3506 C  CD  . ARG B 1 104 ? -12.383 18.205  25.747  1.00 26.78 ? 151 ARG B CD  1 
ATOM   3507 N  NE  . ARG B 1 104 ? -11.247 18.940  25.186  1.00 30.64 ? 151 ARG B NE  1 
ATOM   3508 C  CZ  . ARG B 1 104 ? -11.326 19.641  24.083  1.00 28.91 ? 151 ARG B CZ  1 
ATOM   3509 N  NH1 . ARG B 1 104 ? -12.354 19.467  23.273  1.00 27.59 ? 151 ARG B NH1 1 
ATOM   3510 N  NH2 . ARG B 1 104 ? -10.377 20.495  23.758  1.00 32.89 ? 151 ARG B NH2 1 
ATOM   3511 N  N   . PHE B 1 105 ? -17.047 18.634  28.349  1.00 16.33 ? 152 PHE B N   1 
ATOM   3512 C  CA  . PHE B 1 105 ? -18.200 17.763  28.483  1.00 19.18 ? 152 PHE B CA  1 
ATOM   3513 C  C   . PHE B 1 105 ? -18.965 17.981  29.790  1.00 19.34 ? 152 PHE B C   1 
ATOM   3514 O  O   . PHE B 1 105 ? -19.763 17.135  30.184  1.00 23.59 ? 152 PHE B O   1 
ATOM   3515 C  CB  . PHE B 1 105 ? -17.743 16.295  28.408  1.00 17.90 ? 152 PHE B CB  1 
ATOM   3516 C  CG  . PHE B 1 105 ? -16.890 15.974  27.193  1.00 16.70 ? 152 PHE B CG  1 
ATOM   3517 C  CD1 . PHE B 1 105 ? -17.234 16.390  25.911  1.00 17.45 ? 152 PHE B CD1 1 
ATOM   3518 C  CD2 . PHE B 1 105 ? -15.751 15.174  27.317  1.00 19.37 ? 152 PHE B CD2 1 
ATOM   3519 C  CE1 . PHE B 1 105 ? -16.416 16.090  24.824  1.00 17.77 ? 152 PHE B CE1 1 
ATOM   3520 C  CE2 . PHE B 1 105 ? -14.965 14.837  26.208  1.00 17.84 ? 152 PHE B CE2 1 
ATOM   3521 C  CZ  . PHE B 1 105 ? -15.301 15.288  24.983  1.00 18.45 ? 152 PHE B CZ  1 
ATOM   3522 N  N   . GLY B 1 106 ? -18.752 19.121  30.443  1.00 21.27 ? 153 GLY B N   1 
ATOM   3523 C  CA  . GLY B 1 106 ? -19.471 19.471  31.653  1.00 22.43 ? 153 GLY B CA  1 
ATOM   3524 C  C   . GLY B 1 106 ? -19.005 18.683  32.864  1.00 22.28 ? 153 GLY B C   1 
ATOM   3525 O  O   . GLY B 1 106 ? -19.755 18.525  33.825  1.00 24.87 ? 153 GLY B O   1 
ATOM   3526 N  N   . LEU B 1 107 ? -17.748 18.214  32.811  1.00 18.32 ? 154 LEU B N   1 
ATOM   3527 C  CA  . LEU B 1 107 ? -17.279 17.280  33.809  1.00 19.11 ? 154 LEU B CA  1 
ATOM   3528 C  C   . LEU B 1 107 ? -16.569 17.950  34.988  1.00 15.97 ? 154 LEU B C   1 
ATOM   3529 O  O   . LEU B 1 107 ? -16.081 17.217  35.822  1.00 17.04 ? 154 LEU B O   1 
ATOM   3530 C  CB  . LEU B 1 107 ? -16.324 16.292  33.125  1.00 18.33 ? 154 LEU B CB  1 
ATOM   3531 C  CG  . LEU B 1 107 ? -16.899 15.294  32.119  1.00 19.71 ? 154 LEU B CG  1 
ATOM   3532 C  CD1 . LEU B 1 107 ? -15.711 14.537  31.484  1.00 19.83 ? 154 LEU B CD1 1 
ATOM   3533 C  CD2 . LEU B 1 107 ? -17.814 14.272  32.748  1.00 24.26 ? 154 LEU B CD2 1 
ATOM   3534 N  N   . ALA B 1 108 ? -16.487 19.295  35.080  1.00 16.62 ? 155 ALA B N   1 
ATOM   3535 C  CA  . ALA B 1 108 ? -15.532 19.874  36.006  1.00 17.88 ? 155 ALA B CA  1 
ATOM   3536 C  C   . ALA B 1 108 ? -15.758 19.436  37.452  1.00 17.46 ? 155 ALA B C   1 
ATOM   3537 O  O   . ALA B 1 108 ? -14.794 19.193  38.190  1.00 20.50 ? 155 ALA B O   1 
ATOM   3538 C  CB  . ALA B 1 108 ? -15.521 21.398  35.897  1.00 20.14 ? 155 ALA B CB  1 
ATOM   3539 N  N   . ASP B 1 109 ? -17.027 19.282  37.878  1.00 15.43 ? 156 ASP B N   1 
ATOM   3540 C  CA  . ASP B 1 109 ? -17.341 18.876  39.219  1.00 15.95 ? 156 ASP B CA  1 
ATOM   3541 C  C   . ASP B 1 109 ? -17.203 17.382  39.499  1.00 16.59 ? 156 ASP B C   1 
ATOM   3542 O  O   . ASP B 1 109 ? -17.434 16.945  40.612  1.00 18.98 ? 156 ASP B O   1 
ATOM   3543 C  CB  . ASP B 1 109 ? -18.730 19.386  39.596  1.00 16.84 ? 156 ASP B CB  1 
ATOM   3544 C  CG  . ASP B 1 109 ? -19.857 18.940  38.687  1.00 18.14 ? 156 ASP B CG  1 
ATOM   3545 O  OD1 . ASP B 1 109 ? -19.603 18.254  37.647  1.00 21.72 ? 156 ASP B OD1 1 
ATOM   3546 O  OD2 . ASP B 1 109 ? -21.022 19.281  38.944  1.00 21.20 ? 156 ASP B OD2 1 
ATOM   3547 N  N   . LEU B 1 110 ? -16.782 16.593  38.491  1.00 14.82 ? 157 LEU B N   1 
ATOM   3548 C  CA  . LEU B 1 110 ? -16.600 15.161  38.671  1.00 15.24 ? 157 LEU B CA  1 
ATOM   3549 C  C   . LEU B 1 110 ? -15.107 14.816  38.646  1.00 14.99 ? 157 LEU B C   1 
ATOM   3550 O  O   . LEU B 1 110 ? -14.778 13.630  38.804  1.00 15.11 ? 157 LEU B O   1 
ATOM   3551 C  CB  . LEU B 1 110 ? -17.370 14.396  37.595  1.00 16.79 ? 157 LEU B CB  1 
ATOM   3552 C  CG  . LEU B 1 110 ? -18.885 14.369  37.795  1.00 20.50 ? 157 LEU B CG  1 
ATOM   3553 C  CD1 . LEU B 1 110 ? -19.631 13.815  36.620  1.00 22.24 ? 157 LEU B CD1 1 
ATOM   3554 C  CD2 . LEU B 1 110 ? -19.213 13.523  38.976  1.00 23.63 ? 157 LEU B CD2 1 
ATOM   3555 N  N   . ARG B 1 111 ? -14.218 15.813  38.585  1.00 13.93 ? 158 ARG B N   1 
ATOM   3556 C  CA  . ARG B 1 111 ? -12.800 15.539  38.730  1.00 13.89 ? 158 ARG B CA  1 
ATOM   3557 C  C   . ARG B 1 111 ? -12.548 15.035  40.142  1.00 14.39 ? 158 ARG B C   1 
ATOM   3558 O  O   . ARG B 1 111 ? -12.910 15.665  41.144  1.00 15.21 ? 158 ARG B O   1 
ATOM   3559 C  CB  . ARG B 1 111 ? -11.965 16.764  38.422  1.00 14.07 ? 158 ARG B CB  1 
ATOM   3560 C  CG  . ARG B 1 111 ? -10.483 16.479  38.632  1.00 15.87 ? 158 ARG B CG  1 
ATOM   3561 C  CD  . ARG B 1 111 ? -9.681  17.685  38.377  1.00 18.00 ? 158 ARG B CD  1 
ATOM   3562 N  NE  . ARG B 1 111 ? -8.290  17.408  38.750  1.00 17.69 ? 158 ARG B NE  1 
ATOM   3563 C  CZ  . ARG B 1 111 ? -7.385  18.341  38.558  1.00 17.73 ? 158 ARG B CZ  1 
ATOM   3564 N  NH1 . ARG B 1 111 ? -7.725  19.398  37.855  1.00 16.89 ? 158 ARG B NH1 1 
ATOM   3565 N  NH2 . ARG B 1 111 ? -6.154  18.158  39.000  1.00 17.71 ? 158 ARG B NH2 1 
ATOM   3566 N  N   . PRO B 1 112 ? -11.883 13.876  40.333  1.00 14.74 ? 159 PRO B N   1 
ATOM   3567 C  CA  . PRO B 1 112 ? -11.620 13.397  41.679  1.00 14.96 ? 159 PRO B CA  1 
ATOM   3568 C  C   . PRO B 1 112 ? -10.621 14.301  42.378  1.00 13.92 ? 159 PRO B C   1 
ATOM   3569 O  O   . PRO B 1 112 ? -9.649  14.738  41.760  1.00 14.32 ? 159 PRO B O   1 
ATOM   3570 C  CB  . PRO B 1 112 ? -11.048 11.992  41.468  1.00 15.15 ? 159 PRO B CB  1 
ATOM   3571 C  CG  . PRO B 1 112 ? -11.420 11.654  40.079  1.00 16.70 ? 159 PRO B CG  1 
ATOM   3572 C  CD  . PRO B 1 112 ? -11.519 12.910  39.262  1.00 15.54 ? 159 PRO B CD  1 
ATOM   3573 N  N   . GLU B 1 113 ? -10.845 14.513  43.686  1.00 17.45 ? 160 GLU B N   1 
ATOM   3574 C  CA  . GLU B 1 113 ? -9.864  15.246  44.457  1.00 18.16 ? 160 GLU B CA  1 
ATOM   3575 C  C   . GLU B 1 113 ? -8.524  14.504  44.487  1.00 16.50 ? 160 GLU B C   1 
ATOM   3576 O  O   . GLU B 1 113 ? -7.489  15.131  44.585  1.00 18.20 ? 160 GLU B O   1 
ATOM   3577 C  CB  . GLU B 1 113 ? -10.355 15.571  45.880  1.00 23.34 ? 160 GLU B CB  1 
ATOM   3578 C  CG  . GLU B 1 113 ? -11.433 16.646  45.882  1.00 31.16 ? 160 GLU B CG  1 
ATOM   3579 C  CD  . GLU B 1 113 ? -11.788 17.158  47.268  1.00 39.24 ? 160 GLU B CD  1 
ATOM   3580 O  OE1 . GLU B 1 113 ? -12.509 16.429  47.972  1.00 41.84 ? 160 GLU B OE1 1 
ATOM   3581 O  OE2 . GLU B 1 113 ? -11.311 18.255  47.639  1.00 48.48 ? 160 GLU B OE2 1 
ATOM   3582 N  N   . ALA B 1 114 ? -8.561  13.175  44.378  1.00 14.89 ? 161 ALA B N   1 
ATOM   3583 C  CA  . ALA B 1 114 ? -7.339  12.386  44.404  1.00 16.30 ? 161 ALA B CA  1 
ATOM   3584 C  C   . ALA B 1 114 ? -6.556  12.519  43.097  1.00 15.83 ? 161 ALA B C   1 
ATOM   3585 O  O   . ALA B 1 114 ? -5.385  12.147  43.060  1.00 14.78 ? 161 ALA B O   1 
ATOM   3586 C  CB  . ALA B 1 114 ? -7.684  10.940  44.669  1.00 17.31 ? 161 ALA B CB  1 
ATOM   3587 N  N   . LEU B 1 115 ? -7.174  13.036  42.043  1.00 14.42 ? 162 LEU B N   1 
ATOM   3588 C  CA  . LEU B 1 115 ? -6.458  13.355  40.836  1.00 13.99 ? 162 LEU B CA  1 
ATOM   3589 C  C   . LEU B 1 115 ? -5.879  14.758  40.987  1.00 14.22 ? 162 LEU B C   1 
ATOM   3590 O  O   . LEU B 1 115 ? -6.371  15.732  40.423  1.00 15.21 ? 162 LEU B O   1 
ATOM   3591 C  CB  . LEU B 1 115 ? -7.404  13.225  39.655  1.00 13.93 ? 162 LEU B CB  1 
ATOM   3592 C  CG  . LEU B 1 115 ? -6.751  13.449  38.282  1.00 14.53 ? 162 LEU B CG  1 
ATOM   3593 C  CD1 . LEU B 1 115 ? -5.658  12.441  38.046  1.00 15.68 ? 162 LEU B CD1 1 
ATOM   3594 C  CD2 . LEU B 1 115 ? -7.820  13.372  37.227  1.00 15.03 ? 162 LEU B CD2 1 
ATOM   3595 N  N   . ALA B 1 116 ? -4.780  14.829  41.710  1.00 15.52 ? 163 ALA B N   1 
ATOM   3596 C  CA  . ALA B 1 116 ? -4.140  16.085  42.041  1.00 16.20 ? 163 ALA B CA  1 
ATOM   3597 C  C   . ALA B 1 116 ? -3.117  16.430  40.971  1.00 17.51 ? 163 ALA B C   1 
ATOM   3598 O  O   . ALA B 1 116 ? -2.400  15.572  40.461  1.00 20.65 ? 163 ALA B O   1 
ATOM   3599 C  CB  . ALA B 1 116 ? -3.502  15.940  43.415  1.00 17.52 ? 163 ALA B CB  1 
ATOM   3600 N  N   . ASP B 1 117 ? -3.030  17.722  40.669  1.00 17.63 ? 164 ASP B N   1 
ATOM   3601 C  CA  . ASP B 1 117 ? -1.891  18.260  39.950  1.00 19.17 ? 164 ASP B CA  1 
ATOM   3602 C  C   . ASP B 1 117 ? -0.631  18.091  40.778  1.00 17.36 ? 164 ASP B C   1 
ATOM   3603 O  O   . ASP B 1 117 ? -0.596  18.339  41.972  1.00 20.94 ? 164 ASP B O   1 
ATOM   3604 C  CB  . ASP B 1 117 ? -2.066  19.739  39.693  1.00 22.91 ? 164 ASP B CB  1 
ATOM   3605 C  CG  . ASP B 1 117 ? -3.315  20.122  38.922  1.00 26.02 ? 164 ASP B CG  1 
ATOM   3606 O  OD1 . ASP B 1 117 ? -3.626  19.425  37.972  1.00 25.94 ? 164 ASP B OD1 1 
ATOM   3607 O  OD2 . ASP B 1 117 ? -3.859  21.187  39.232  1.00 35.37 ? 164 ASP B OD2 1 
ATOM   3608 N  N   . LEU B 1 118 ? 0.443   17.694  40.107  1.00 16.98 ? 165 LEU B N   1 
ATOM   3609 C  CA  . LEU B 1 118 ? 1.698   17.529  40.806  1.00 16.87 ? 165 LEU B CA  1 
ATOM   3610 C  C   . LEU B 1 118 ? 2.322   18.890  41.008  1.00 17.87 ? 165 LEU B C   1 
ATOM   3611 O  O   . LEU B 1 118 ? 2.229   19.786  40.177  1.00 20.72 ? 165 LEU B O   1 
ATOM   3612 C  CB  . LEU B 1 118 ? 2.639   16.668  39.981  1.00 15.76 ? 165 LEU B CB  1 
ATOM   3613 C  CG  . LEU B 1 118 ? 2.160   15.247  39.703  1.00 15.65 ? 165 LEU B CG  1 
ATOM   3614 C  CD1 . LEU B 1 118 ? 3.122   14.541  38.808  1.00 18.28 ? 165 LEU B CD1 1 
ATOM   3615 C  CD2 . LEU B 1 118 ? 1.953   14.496  40.996  1.00 17.86 ? 165 LEU B CD2 1 
ATOM   3616 N  N   . PRO B 1 119 ? 3.010   19.045  42.138  1.00 18.91 ? 166 PRO B N   1 
ATOM   3617 C  CA  . PRO B 1 119 ? 3.812   20.242  42.315  1.00 21.53 ? 166 PRO B CA  1 
ATOM   3618 C  C   . PRO B 1 119 ? 5.018   20.173  41.408  1.00 21.76 ? 166 PRO B C   1 
ATOM   3619 O  O   . PRO B 1 119 ? 5.387   19.113  40.881  1.00 18.77 ? 166 PRO B O   1 
ATOM   3620 C  CB  . PRO B 1 119 ? 4.206   20.193  43.766  1.00 22.51 ? 166 PRO B CB  1 
ATOM   3621 C  CG  . PRO B 1 119 ? 4.059   18.805  44.208  1.00 24.18 ? 166 PRO B CG  1 
ATOM   3622 C  CD  . PRO B 1 119 ? 3.070   18.108  43.260  1.00 19.80 ? 166 PRO B CD  1 
ATOM   3623 N  N   . LYS B 1 120 ? 5.689   21.315  41.295  1.00 20.58 ? 167 LYS B N   1 
ATOM   3624 C  CA  . LYS B 1 120 ? 6.994   21.353  40.696  1.00 21.95 ? 167 LYS B CA  1 
ATOM   3625 C  C   . LYS B 1 120 ? 7.942   20.712  41.711  1.00 23.29 ? 167 LYS B C   1 
ATOM   3626 O  O   . LYS B 1 120 ? 7.871   20.979  42.917  1.00 26.00 ? 167 LYS B O   1 
ATOM   3627 C  CB  . LYS B 1 120 ? 7.347   22.824  40.419  1.00 27.79 ? 167 LYS B CB  1 
ATOM   3628 C  CG  . LYS B 1 120 ? 8.610   23.005  39.590  1.00 37.27 ? 167 LYS B CG  1 
ATOM   3629 C  CD  . LYS B 1 120 ? 9.036   24.450  39.315  1.00 45.58 ? 167 LYS B CD  1 
ATOM   3630 C  CE  . LYS B 1 120 ? 9.637   25.140  40.505  1.00 52.56 ? 167 LYS B CE  1 
ATOM   3631 N  NZ  . LYS B 1 120 ? 9.752   26.588  40.298  1.00 58.56 ? 167 LYS B NZ  1 
ATOM   3632 N  N   . PHE B 1 121 ? 8.778   19.799  41.251  1.00 16.92 ? 168 PHE B N   1 
ATOM   3633 C  CA  . PHE B 1 121 ? 9.802   19.207  42.092  1.00 15.81 ? 168 PHE B CA  1 
ATOM   3634 C  C   . PHE B 1 121 ? 11.173  19.720  41.702  1.00 15.84 ? 168 PHE B C   1 
ATOM   3635 O  O   . PHE B 1 121 ? 11.473  20.015  40.541  1.00 15.16 ? 168 PHE B O   1 
ATOM   3636 C  CB  . PHE B 1 121 ? 9.831   17.675  41.989  1.00 15.65 ? 168 PHE B CB  1 
ATOM   3637 C  CG  . PHE B 1 121 ? 8.550   17.038  42.482  1.00 15.89 ? 168 PHE B CG  1 
ATOM   3638 C  CD1 . PHE B 1 121 ? 8.288   16.919  43.840  1.00 16.51 ? 168 PHE B CD1 1 
ATOM   3639 C  CD2 . PHE B 1 121 ? 7.610   16.539  41.601  1.00 15.94 ? 168 PHE B CD2 1 
ATOM   3640 C  CE1 . PHE B 1 121 ? 7.107   16.370  44.308  1.00 18.45 ? 168 PHE B CE1 1 
ATOM   3641 C  CE2 . PHE B 1 121 ? 6.416   16.007  42.100  1.00 16.58 ? 168 PHE B CE2 1 
ATOM   3642 C  CZ  . PHE B 1 121 ? 6.206   15.885  43.435  1.00 17.62 ? 168 PHE B CZ  1 
ATOM   3643 N  N   . PRO B 1 122 ? 12.073  19.838  42.691  1.00 15.95 ? 169 PRO B N   1 
ATOM   3644 C  CA  . PRO B 1 122 ? 13.429  20.295  42.410  1.00 16.58 ? 169 PRO B CA  1 
ATOM   3645 C  C   . PRO B 1 122 ? 14.043  19.458  41.308  1.00 17.49 ? 169 PRO B C   1 
ATOM   3646 O  O   . PRO B 1 122 ? 13.965  18.233  41.338  1.00 18.09 ? 169 PRO B O   1 
ATOM   3647 C  CB  . PRO B 1 122 ? 14.180  20.126  43.712  1.00 20.06 ? 169 PRO B CB  1 
ATOM   3648 C  CG  . PRO B 1 122 ? 13.105  20.090  44.765  1.00 19.73 ? 169 PRO B CG  1 
ATOM   3649 C  CD  . PRO B 1 122 ? 11.798  19.656  44.119  1.00 16.90 ? 169 PRO B CD  1 
ATOM   3650 N  N   . GLY B 1 123 ? 14.641  20.140  40.343  1.00 16.78 ? 170 GLY B N   1 
ATOM   3651 C  CA  . GLY B 1 123 ? 15.349  19.460  39.271  1.00 17.36 ? 170 GLY B CA  1 
ATOM   3652 C  C   . GLY B 1 123 ? 14.434  19.041  38.108  1.00 15.60 ? 170 GLY B C   1 
ATOM   3653 O  O   . GLY B 1 123 ? 14.991  18.560  37.144  1.00 19.04 ? 170 GLY B O   1 
ATOM   3654 N  N   . ASP B 1 124 ? 13.107  19.265  38.198  1.00 16.30 ? 171 ASP B N   1 
ATOM   3655 C  CA  . ASP B 1 124 ? 12.213  18.988  37.070  1.00 17.47 ? 171 ASP B CA  1 
ATOM   3656 C  C   . ASP B 1 124 ? 12.696  19.739  35.836  1.00 17.83 ? 171 ASP B C   1 
ATOM   3657 O  O   . ASP B 1 124 ? 13.050  20.922  35.893  1.00 18.63 ? 171 ASP B O   1 
ATOM   3658 C  CB  . ASP B 1 124 ? 10.814  19.513  37.321  1.00 18.75 ? 171 ASP B CB  1 
ATOM   3659 C  CG  . ASP B 1 124 ? 9.836   18.653  38.102  1.00 19.84 ? 171 ASP B CG  1 
ATOM   3660 O  OD1 . ASP B 1 124 ? 10.202  17.516  38.394  1.00 19.18 ? 171 ASP B OD1 1 
ATOM   3661 O  OD2 . ASP B 1 124 ? 8.739   19.250  38.428  1.00 23.59 ? 171 ASP B OD2 1 
ATOM   3662 N  N   . ASN B 1 125 ? 12.649  19.094  34.678  1.00 15.95 ? 172 ASN B N   1 
ATOM   3663 C  CA  . ASN B 1 125 ? 12.895  19.722  33.399  1.00 16.27 ? 172 ASN B CA  1 
ATOM   3664 C  C   . ASN B 1 125 ? 11.917  19.134  32.394  1.00 14.58 ? 172 ASN B C   1 
ATOM   3665 O  O   . ASN B 1 125 ? 12.316  18.455  31.448  1.00 17.01 ? 172 ASN B O   1 
ATOM   3666 C  CB  . ASN B 1 125 ? 14.312  19.478  32.925  1.00 19.87 ? 172 ASN B CB  1 
ATOM   3667 C  CG  . ASN B 1 125 ? 14.633  20.249  31.677  1.00 25.46 ? 172 ASN B CG  1 
ATOM   3668 O  OD1 . ASN B 1 125 ? 13.979  21.246  31.385  1.00 30.49 ? 172 ASN B OD1 1 
ATOM   3669 N  ND2 . ASN B 1 125 ? 15.631  19.778  30.946  1.00 31.90 ? 172 ASN B ND2 1 
ATOM   3670 N  N   . LEU B 1 126 ? 10.654  19.456  32.608  1.00 16.53 ? 173 LEU B N   1 
ATOM   3671 C  CA  . LEU B 1 126 ? 9.587   18.762  31.912  1.00 16.72 ? 173 LEU B CA  1 
ATOM   3672 C  C   . LEU B 1 126 ? 9.416   19.365  30.530  1.00 18.16 ? 173 LEU B C   1 
ATOM   3673 O  O   . LEU B 1 126 ? 9.282   20.578  30.390  1.00 20.69 ? 173 LEU B O   1 
ATOM   3674 C  CB  . LEU B 1 126 ? 8.291   18.865  32.702  1.00 17.04 ? 173 LEU B CB  1 
ATOM   3675 C  CG  . LEU B 1 126 ? 8.313   18.278  34.124  1.00 17.69 ? 173 LEU B CG  1 
ATOM   3676 C  CD1 . LEU B 1 126 ? 6.954   18.391  34.799  1.00 20.09 ? 173 LEU B CD1 1 
ATOM   3677 C  CD2 . LEU B 1 126 ? 8.788   16.849  34.095  1.00 18.00 ? 173 LEU B CD2 1 
ATOM   3678 N  N   . ASP B 1 127 ? 9.366   18.494  29.531  1.00 17.06 ? 174 ASP B N   1 
ATOM   3679 C  CA  . ASP B 1 127 ? 9.035   18.880  28.171  1.00 16.98 ? 174 ASP B CA  1 
ATOM   3680 C  C   . ASP B 1 127 ? 7.524   18.904  28.082  1.00 18.16 ? 174 ASP B C   1 
ATOM   3681 O  O   . ASP B 1 127 ? 6.865   17.872  28.242  1.00 16.56 ? 174 ASP B O   1 
ATOM   3682 C  CB  . ASP B 1 127 ? 9.697   17.905  27.233  1.00 17.46 ? 174 ASP B CB  1 
ATOM   3683 C  CG  . ASP B 1 127 ? 9.395   18.058  25.747  1.00 21.19 ? 174 ASP B CG  1 
ATOM   3684 O  OD1 . ASP B 1 127 ? 8.529   18.876  25.392  1.00 24.07 ? 174 ASP B OD1 1 
ATOM   3685 O  OD2 . ASP B 1 127 ? 10.030  17.317  24.972  1.00 28.99 ? 174 ASP B OD2 1 
ATOM   3686 N  N   . ARG B 1 128 ? 6.952   20.069  27.784  1.00 20.55 ? 175 ARG B N   1 
ATOM   3687 C  CA  . ARG B 1 128 ? 5.507   20.200  27.762  1.00 21.90 ? 175 ARG B CA  1 
ATOM   3688 C  C   . ARG B 1 128 ? 4.876   19.303  26.708  1.00 20.28 ? 175 ARG B C   1 
ATOM   3689 O  O   . ARG B 1 128 ? 3.751   18.849  26.892  1.00 22.38 ? 175 ARG B O   1 
ATOM   3690 C  CB  . ARG B 1 128 ? 5.158   21.650  27.445  1.00 28.70 ? 175 ARG B CB  1 
ATOM   3691 C  CG  . ARG B 1 128 ? 5.625   22.600  28.540  1.00 39.25 ? 175 ARG B CG  1 
ATOM   3692 C  CD  . ARG B 1 128 ? 5.533   24.075  28.096  1.00 53.82 ? 175 ARG B CD  1 
ATOM   3693 N  NE  . ARG B 1 128 ? 4.243   24.378  27.459  1.00 62.14 ? 175 ARG B NE  1 
ATOM   3694 C  CZ  . ARG B 1 128 ? 3.047   24.243  28.035  1.00 69.17 ? 175 ARG B CZ  1 
ATOM   3695 N  NH1 . ARG B 1 128 ? 2.954   23.953  29.321  1.00 71.34 ? 175 ARG B NH1 1 
ATOM   3696 N  NH2 . ARG B 1 128 ? 1.942   24.417  27.326  1.00 71.25 ? 175 ARG B NH2 1 
ATOM   3697 N  N   . ALA B 1 129 ? 5.603   19.035  25.630  1.00 20.63 ? 176 ALA B N   1 
ATOM   3698 C  CA  . ALA B 1 129 ? 5.087   18.234  24.533  1.00 21.82 ? 176 ALA B CA  1 
ATOM   3699 C  C   . ALA B 1 129 ? 5.055   16.746  24.892  1.00 22.04 ? 176 ALA B C   1 
ATOM   3700 O  O   . ALA B 1 129 ? 4.350   15.981  24.215  1.00 25.09 ? 176 ALA B O   1 
ATOM   3701 C  CB  . ALA B 1 129 ? 5.934   18.464  23.298  1.00 22.53 ? 176 ALA B CB  1 
ATOM   3702 N  N   . ARG B 1 130 ? 5.834   16.309  25.891  1.00 17.86 ? 177 ARG B N   1 
ATOM   3703 C  CA  . ARG B 1 130 ? 5.790   14.921  26.323  1.00 19.18 ? 177 ARG B CA  1 
ATOM   3704 C  C   . ARG B 1 130 ? 5.238   14.822  27.733  1.00 15.93 ? 177 ARG B C   1 
ATOM   3705 O  O   . ARG B 1 130 ? 5.579   13.924  28.501  1.00 18.94 ? 177 ARG B O   1 
ATOM   3706 C  CB  . ARG B 1 130 ? 7.182   14.302  26.180  1.00 25.19 ? 177 ARG B CB  1 
ATOM   3707 C  CG  . ARG B 1 130 ? 7.561   14.384  24.708  1.00 31.17 ? 177 ARG B CG  1 
ATOM   3708 C  CD  . ARG B 1 130 ? 8.995   14.004  24.434  1.00 38.88 ? 177 ARG B CD  1 
ATOM   3709 N  NE  . ARG B 1 130 ? 9.145   12.570  24.182  1.00 46.44 ? 177 ARG B NE  1 
ATOM   3710 C  CZ  . ARG B 1 130 ? 10.284  12.001  23.823  1.00 50.26 ? 177 ARG B CZ  1 
ATOM   3711 N  NH1 . ARG B 1 130 ? 11.383  12.727  23.698  1.00 54.96 ? 177 ARG B NH1 1 
ATOM   3712 N  NH2 . ARG B 1 130 ? 10.320  10.704  23.609  1.00 51.47 ? 177 ARG B NH2 1 
ATOM   3713 N  N   . SER B 1 131 ? 4.361   15.760  28.060  1.00 13.56 ? 178 SER B N   1 
ATOM   3714 C  CA  . SER B 1 131 ? 3.709   15.829  29.347  1.00 14.23 ? 178 SER B CA  1 
ATOM   3715 C  C   . SER B 1 131 ? 2.222   15.978  29.118  1.00 14.44 ? 178 SER B C   1 
ATOM   3716 O  O   . SER B 1 131 ? 1.808   16.434  28.058  1.00 16.94 ? 178 SER B O   1 
ATOM   3717 C  CB  . SER B 1 131 ? 4.231   16.972  30.172  1.00 14.88 ? 178 SER B CB  1 
ATOM   3718 O  OG  . SER B 1 131 ? 5.595   16.732  30.495  1.00 14.73 ? 178 SER B OG  1 
ATOM   3719 N  N   . GLY B 1 132 ? 1.454   15.679  30.151  1.00 13.83 ? 179 GLY B N   1 
ATOM   3720 C  CA  . GLY B 1 132 ? 0.011   15.850  30.123  1.00 12.91 ? 179 GLY B CA  1 
ATOM   3721 C  C   . GLY B 1 132 ? -0.684  14.929  29.139  1.00 13.28 ? 179 GLY B C   1 
ATOM   3722 O  O   . GLY B 1 132 ? -0.193  13.881  28.769  1.00 14.88 ? 179 GLY B O   1 
ATOM   3723 N  N   . GLY B 1 133 ? -1.895  15.328  28.811  1.00 12.30 ? 180 GLY B N   1 
ATOM   3724 C  CA  . GLY B 1 133 ? -2.751  14.602  27.908  1.00 12.48 ? 180 GLY B CA  1 
ATOM   3725 C  C   . GLY B 1 133 ? -4.103  14.409  28.538  1.00 11.85 ? 180 GLY B C   1 
ATOM   3726 O  O   . GLY B 1 133 ? -4.235  14.168  29.722  1.00 12.59 ? 180 GLY B O   1 
ATOM   3727 N  N   . ASP B 1 134 ? -5.120  14.489  27.703  1.00 11.42 ? 181 ASP B N   1 
ATOM   3728 C  CA  . ASP B 1 134 ? -6.474  14.301  28.161  1.00 11.90 ? 181 ASP B CA  1 
ATOM   3729 C  C   . ASP B 1 134 ? -6.781  12.864  28.528  1.00 13.12 ? 181 ASP B C   1 
ATOM   3730 O  O   . ASP B 1 134 ? -7.619  12.625  29.378  1.00 12.61 ? 181 ASP B O   1 
ATOM   3731 C  CB  . ASP B 1 134 ? -7.475  14.744  27.109  1.00 12.46 ? 181 ASP B CB  1 
ATOM   3732 C  CG  . ASP B 1 134 ? -7.457  16.216  26.752  1.00 14.60 ? 181 ASP B CG  1 
ATOM   3733 O  OD1 . ASP B 1 134 ? -7.229  17.016  27.657  1.00 16.97 ? 181 ASP B OD1 1 
ATOM   3734 O  OD2 . ASP B 1 134 ? -7.747  16.562  25.588  1.00 15.55 ? 181 ASP B OD2 1 
ATOM   3735 N  N   . LEU B 1 135 ? -6.182  11.916  27.800  1.00 12.76 ? 182 LEU B N   1 
ATOM   3736 C  CA  . LEU B 1 135 ? -6.370  10.540  28.222  1.00 14.45 ? 182 LEU B CA  1 
ATOM   3737 C  C   . LEU B 1 135 ? -5.151  9.732   27.858  1.00 12.59 ? 182 LEU B C   1 
ATOM   3738 O  O   . LEU B 1 135 ? -4.254  10.191  27.195  1.00 13.42 ? 182 LEU B O   1 
ATOM   3739 C  CB  . LEU B 1 135 ? -7.670  9.962   27.711  1.00 21.17 ? 182 LEU B CB  1 
ATOM   3740 C  CG  . LEU B 1 135 ? -7.734  9.803   26.209  1.00 22.48 ? 182 LEU B CG  1 
ATOM   3741 C  CD1 . LEU B 1 135 ? -7.293  8.429   25.802  1.00 30.24 ? 182 LEU B CD1 1 
ATOM   3742 C  CD2 . LEU B 1 135 ? -9.101  10.079  25.606  1.00 28.17 ? 182 LEU B CD2 1 
ATOM   3743 N  N   . CYS B 1 136 ? -5.074  8.530   28.418  1.00 11.70 ? 183 CYS B N   1 
ATOM   3744 C  CA  . CYS B 1 136 ? -3.980  7.638   28.093  1.00 10.80 ? 183 CYS B CA  1 
ATOM   3745 C  C   . CYS B 1 136 ? -4.531  6.246   27.792  1.00 10.48 ? 183 CYS B C   1 
ATOM   3746 O  O   . CYS B 1 136 ? -5.587  5.833   28.279  1.00 11.28 ? 183 CYS B O   1 
ATOM   3747 C  CB  . CYS B 1 136 ? -2.923  7.514   29.183  1.00 13.04 ? 183 CYS B CB  1 
ATOM   3748 S  SG  . CYS B 1 136 ? -3.497  6.731   30.700  1.00 14.75 ? 183 CYS B SG  1 
ATOM   3749 N  N   . VAL B 1 137 ? -3.747  5.513   27.004  1.00 10.73 ? 184 VAL B N   1 
ATOM   3750 C  CA  . VAL B 1 137 ? -3.890  4.074   26.894  1.00 10.28 ? 184 VAL B CA  1 
ATOM   3751 C  C   . VAL B 1 137 ? -2.534  3.438   27.152  1.00 10.42 ? 184 VAL B C   1 
ATOM   3752 O  O   . VAL B 1 137 ? -1.567  3.729   26.469  1.00 11.35 ? 184 VAL B O   1 
ATOM   3753 C  CB  . VAL B 1 137 ? -4.447  3.613   25.546  1.00 12.10 ? 184 VAL B CB  1 
ATOM   3754 C  CG1 . VAL B 1 137 ? -4.552  2.101   25.539  1.00 14.24 ? 184 VAL B CG1 1 
ATOM   3755 C  CG2 . VAL B 1 137 ? -5.785  4.270   25.292  1.00 13.73 ? 184 VAL B CG2 1 
ATOM   3756 N  N   . GLN B 1 138 ? -2.493  2.583   28.176  1.00 10.29 ? 185 GLN B N   1 
ATOM   3757 C  CA  . GLN B 1 138 ? -1.311  1.783   28.452  1.00 9.96  ? 185 GLN B CA  1 
ATOM   3758 C  C   . GLN B 1 138 ? -1.514  0.435   27.772  1.00 10.41 ? 185 GLN B C   1 
ATOM   3759 O  O   . GLN B 1 138 ? -2.428  -0.299  28.139  1.00 10.73 ? 185 GLN B O   1 
ATOM   3760 C  CB  . GLN B 1 138 ? -1.163  1.573   29.955  1.00 9.96  ? 185 GLN B CB  1 
ATOM   3761 C  CG  . GLN B 1 138 ? 0.008   0.695   30.365  1.00 10.56 ? 185 GLN B CG  1 
ATOM   3762 C  CD  . GLN B 1 138 ? -0.065  0.315   31.810  1.00 11.66 ? 185 GLN B CD  1 
ATOM   3763 O  OE1 . GLN B 1 138 ? 0.378   1.074   32.670  1.00 13.90 ? 185 GLN B OE1 1 
ATOM   3764 N  NE2 . GLN B 1 138 ? -0.740  -0.792  32.083  1.00 12.80 ? 185 GLN B NE2 1 
ATOM   3765 N  N   . ALA B 1 139 ? -0.676  0.102   26.788  1.00 9.85  ? 186 ALA B N   1 
ATOM   3766 C  CA  . ALA B 1 139 ? -0.748  -1.196  26.124  1.00 9.63  ? 186 ALA B CA  1 
ATOM   3767 C  C   . ALA B 1 139 ? 0.461   -2.004  26.541  1.00 9.99  ? 186 ALA B C   1 
ATOM   3768 O  O   . ALA B 1 139 ? 1.587   -1.585  26.324  1.00 11.79 ? 186 ALA B O   1 
ATOM   3769 C  CB  . ALA B 1 139 ? -0.781  -1.036  24.638  1.00 10.01 ? 186 ALA B CB  1 
ATOM   3770 N  N   . CYS B 1 140 ? 0.252   -3.104  27.231  1.00 9.61  ? 187 CYS B N   1 
ATOM   3771 C  CA  . CYS B 1 140 ? 1.337   -3.969  27.648  1.00 10.17 ? 187 CYS B CA  1 
ATOM   3772 C  C   . CYS B 1 140 ? 1.129   -5.336  27.041  1.00 10.30 ? 187 CYS B C   1 
ATOM   3773 O  O   . CYS B 1 140 ? 0.028   -5.868  27.060  1.00 11.77 ? 187 CYS B O   1 
ATOM   3774 C  CB  . CYS B 1 140 ? 1.398   -4.152  29.162  1.00 10.86 ? 187 CYS B CB  1 
ATOM   3775 S  SG  . CYS B 1 140 ? 1.728   -2.625  30.059  1.00 12.48 ? 187 CYS B SG  1 
ATOM   3776 N  N   . ALA B 1 141 ? 2.221   -5.910  26.519  1.00 10.55 ? 188 ALA B N   1 
ATOM   3777 C  CA  . ALA B 1 141 ? 2.151   -7.229  25.914  1.00 10.02 ? 188 ALA B CA  1 
ATOM   3778 C  C   . ALA B 1 141 ? 3.536   -7.798  25.908  1.00 11.73 ? 188 ALA B C   1 
ATOM   3779 O  O   . ALA B 1 141 ? 4.489   -7.081  26.082  1.00 11.36 ? 188 ALA B O   1 
ATOM   3780 C  CB  . ALA B 1 141 ? 1.609   -7.143  24.525  1.00 11.54 ? 188 ALA B CB  1 
ATOM   3781 N  N   . ASP B 1 142 ? 3.676   -9.080  25.625  1.00 11.16 ? 189 ASP B N   1 
ATOM   3782 C  CA  . ASP B 1 142 ? 5.008   -9.675  25.533  1.00 11.53 ? 189 ASP B CA  1 
ATOM   3783 C  C   . ASP B 1 142 ? 5.670   -9.446  24.189  1.00 12.93 ? 189 ASP B C   1 
ATOM   3784 O  O   . ASP B 1 142 ? 6.897   -9.498  24.111  1.00 17.10 ? 189 ASP B O   1 
ATOM   3785 C  CB  . ASP B 1 142 ? 4.941   -11.159 25.841  1.00 11.24 ? 189 ASP B CB  1 
ATOM   3786 C  CG  . ASP B 1 142 ? 4.541   -11.417 27.271  1.00 13.60 ? 189 ASP B CG  1 
ATOM   3787 O  OD1 . ASP B 1 142 ? 4.917   -10.628 28.153  1.00 13.01 ? 189 ASP B OD1 1 
ATOM   3788 O  OD2 . ASP B 1 142 ? 3.835   -12.445 27.461  1.00 15.45 ? 189 ASP B OD2 1 
ATOM   3789 N  N   . ASP B 1 143 ? 4.890   -9.085  23.187  1.00 11.88 ? 190 ASP B N   1 
ATOM   3790 C  CA  . ASP B 1 143 ? 5.369   -8.854  21.833  1.00 12.19 ? 190 ASP B CA  1 
ATOM   3791 C  C   . ASP B 1 143 ? 5.117   -7.384  21.564  1.00 12.16 ? 190 ASP B C   1 
ATOM   3792 O  O   . ASP B 1 143 ? 3.991   -6.930  21.638  1.00 12.66 ? 190 ASP B O   1 
ATOM   3793 C  CB  . ASP B 1 143 ? 4.596   -9.733  20.868  1.00 13.48 ? 190 ASP B CB  1 
ATOM   3794 C  CG  . ASP B 1 143 ? 5.023   -9.618  19.429  1.00 17.64 ? 190 ASP B CG  1 
ATOM   3795 O  OD1 . ASP B 1 143 ? 5.466   -8.518  19.035  1.00 18.03 ? 190 ASP B OD1 1 
ATOM   3796 O  OD2 . ASP B 1 143 ? 4.837   -10.603 18.694  1.00 20.88 ? 190 ASP B OD2 1 
ATOM   3797 N  N   . PRO B 1 144 ? 6.147   -6.581  21.287  1.00 11.94 ? 191 PRO B N   1 
ATOM   3798 C  CA  . PRO B 1 144 ? 5.916   -5.163  21.095  1.00 12.13 ? 191 PRO B CA  1 
ATOM   3799 C  C   . PRO B 1 144 ? 5.041   -4.842  19.897  1.00 12.31 ? 191 PRO B C   1 
ATOM   3800 O  O   . PRO B 1 144 ? 4.362   -3.829  19.866  1.00 13.13 ? 191 PRO B O   1 
ATOM   3801 C  CB  . PRO B 1 144 ? 7.323   -4.588  20.880  1.00 12.74 ? 191 PRO B CB  1 
ATOM   3802 C  CG  . PRO B 1 144 ? 8.133   -5.749  20.437  1.00 13.96 ? 191 PRO B CG  1 
ATOM   3803 C  CD  . PRO B 1 144 ? 7.535   -7.002  21.055  1.00 12.05 ? 191 PRO B CD  1 
ATOM   3804 N  N   . GLN B 1 145 ? 5.062   -5.682  18.864  1.00 11.07 ? 192 GLN B N   1 
ATOM   3805 C  CA  . GLN B 1 145 ? 4.208   -5.431  17.725  1.00 11.15 ? 192 GLN B CA  1 
ATOM   3806 C  C   . GLN B 1 145 ? 2.738   -5.561  18.059  1.00 10.84 ? 192 GLN B C   1 
ATOM   3807 O  O   . GLN B 1 145 ? 1.905   -4.848  17.508  1.00 11.60 ? 192 GLN B O   1 
ATOM   3808 C  CB  . GLN B 1 145 ? 4.578   -6.358  16.566  1.00 12.70 ? 192 GLN B CB  1 
ATOM   3809 C  CG  . GLN B 1 145 ? 3.883   -5.951  15.271  1.00 14.13 ? 192 GLN B CG  1 
ATOM   3810 C  CD  . GLN B 1 145 ? 4.814   -6.149  14.111  1.00 16.84 ? 192 GLN B CD  1 
ATOM   3811 O  OE1 . GLN B 1 145 ? 6.025   -5.891  14.187  1.00 18.68 ? 192 GLN B OE1 1 
ATOM   3812 N  NE2 . GLN B 1 145 ? 4.250   -6.612  13.008  1.00 16.25 ? 192 GLN B NE2 1 
ATOM   3813 N  N   . VAL B 1 146 ? 2.392   -6.449  19.010  1.00 10.08 ? 193 VAL B N   1 
ATOM   3814 C  CA  . VAL B 1 146 ? 1.014   -6.549  19.454  1.00 10.04 ? 193 VAL B CA  1 
ATOM   3815 C  C   . VAL B 1 146 ? 0.618   -5.243  20.143  1.00 10.52 ? 193 VAL B C   1 
ATOM   3816 O  O   . VAL B 1 146 ? -0.461  -4.751  19.929  1.00 11.00 ? 193 VAL B O   1 
ATOM   3817 C  CB  . VAL B 1 146 ? 0.821   -7.797  20.338  1.00 11.83 ? 193 VAL B CB  1 
ATOM   3818 C  CG1 . VAL B 1 146 ? -0.525  -7.813  21.063  1.00 13.12 ? 193 VAL B CG1 1 
ATOM   3819 C  CG2 . VAL B 1 146 ? 1.026   -9.072  19.506  1.00 12.39 ? 193 VAL B CG2 1 
ATOM   3820 N  N   . ALA B 1 147 ? 1.495   -4.701  20.963  1.00 10.14 ? 194 ALA B N   1 
ATOM   3821 C  CA  . ALA B 1 147 ? 1.182   -3.451  21.647  1.00 10.17 ? 194 ALA B CA  1 
ATOM   3822 C  C   . ALA B 1 147 ? 1.056   -2.295  20.666  1.00 11.07 ? 194 ALA B C   1 
ATOM   3823 O  O   . ALA B 1 147 ? 0.148   -1.495  20.771  1.00 10.71 ? 194 ALA B O   1 
ATOM   3824 C  CB  . ALA B 1 147 ? 2.220   -3.202  22.675  1.00 11.36 ? 194 ALA B CB  1 
ATOM   3825 N  N   . VAL B 1 148 ? 2.019   -2.155  19.771  1.00 10.90 ? 195 VAL B N   1 
ATOM   3826 C  CA  . VAL B 1 148 ? 1.999   -1.055  18.816  1.00 11.27 ? 195 VAL B CA  1 
ATOM   3827 C  C   . VAL B 1 148 ? 0.759   -1.158  17.940  1.00 11.77 ? 195 VAL B C   1 
ATOM   3828 O  O   . VAL B 1 148 ? 0.085   -0.173  17.675  1.00 11.17 ? 195 VAL B O   1 
ATOM   3829 C  CB  . VAL B 1 148 ? 3.283   -1.084  17.993  1.00 12.86 ? 195 VAL B CB  1 
ATOM   3830 C  CG1 . VAL B 1 148 ? 3.174   -0.123  16.834  1.00 14.80 ? 195 VAL B CG1 1 
ATOM   3831 C  CG2 . VAL B 1 148 ? 4.504   -0.756  18.840  1.00 14.34 ? 195 VAL B CG2 1 
ATOM   3832 N  N   . HIS B 1 149 ? 0.402   -2.351  17.496  1.00 10.41 ? 196 HIS B N   1 
ATOM   3833 C  CA  . HIS B 1 149 ? -0.803  -2.535  16.697  1.00 11.18 ? 196 HIS B CA  1 
ATOM   3834 C  C   . HIS B 1 149 ? -2.036  -2.038  17.429  1.00 9.91  ? 196 HIS B C   1 
ATOM   3835 O  O   . HIS B 1 149 ? -2.922  -1.429  16.840  1.00 10.99 ? 196 HIS B O   1 
ATOM   3836 C  CB  . HIS B 1 149 ? -0.930  -4.019  16.338  1.00 10.32 ? 196 HIS B CB  1 
ATOM   3837 C  CG  . HIS B 1 149 ? -2.221  -4.385  15.714  1.00 9.97  ? 196 HIS B CG  1 
ATOM   3838 N  ND1 . HIS B 1 149 ? -3.251  -4.966  16.431  1.00 11.82 ? 196 HIS B ND1 1 
ATOM   3839 C  CD2 . HIS B 1 149 ? -2.656  -4.275  14.450  1.00 11.01 ? 196 HIS B CD2 1 
ATOM   3840 C  CE1 . HIS B 1 149 ? -4.290  -5.163  15.637  1.00 11.71 ? 196 HIS B CE1 1 
ATOM   3841 N  NE2 . HIS B 1 149 ? -3.925  -4.799  14.407  1.00 11.73 ? 196 HIS B NE2 1 
ATOM   3842 N  N   . ALA B 1 150 ? -2.129  -2.341  18.724  1.00 10.00 ? 197 ALA B N   1 
ATOM   3843 C  CA  . ALA B 1 150 ? -3.263  -1.878  19.480  1.00 10.97 ? 197 ALA B CA  1 
ATOM   3844 C  C   . ALA B 1 150 ? -3.341  -0.363  19.489  1.00 10.46 ? 197 ALA B C   1 
ATOM   3845 O  O   . ALA B 1 150 ? -4.396  0.186   19.214  1.00 11.93 ? 197 ALA B O   1 
ATOM   3846 C  CB  . ALA B 1 150 ? -3.235  -2.431  20.864  1.00 11.36 ? 197 ALA B CB  1 
ATOM   3847 N  N   . ILE B 1 151 ? -2.245  0.316   19.781  1.00 10.32 ? 198 ILE B N   1 
ATOM   3848 C  CA  . ILE B 1 151 ? -2.280  1.776   19.831  1.00 10.60 ? 198 ILE B CA  1 
ATOM   3849 C  C   . ILE B 1 151 ? -2.585  2.367   18.461  1.00 10.61 ? 198 ILE B C   1 
ATOM   3850 O  O   . ILE B 1 151 ? -3.408  3.278   18.331  1.00 11.66 ? 198 ILE B O   1 
ATOM   3851 C  CB  . ILE B 1 151 ? -0.972  2.330   20.428  1.00 12.67 ? 198 ILE B CB  1 
ATOM   3852 C  CG1 . ILE B 1 151 ? -0.768  1.849   21.859  1.00 14.43 ? 198 ILE B CG1 1 
ATOM   3853 C  CG2 . ILE B 1 151 ? -0.898  3.849   20.321  1.00 13.60 ? 198 ILE B CG2 1 
ATOM   3854 C  CD1 . ILE B 1 151 ? -1.845  2.249   22.838  1.00 15.74 ? 198 ILE B CD1 1 
ATOM   3855 N  N   . ARG B 1 152 ? -1.973  1.808   17.417  1.00 10.41 ? 199 ARG B N   1 
ATOM   3856 C  CA  . ARG B 1 152 ? -2.129  2.337   16.089  1.00 11.26 ? 199 ARG B CA  1 
ATOM   3857 C  C   . ARG B 1 152 ? -3.588  2.222   15.703  1.00 11.51 ? 199 ARG B C   1 
ATOM   3858 O  O   . ARG B 1 152 ? -4.141  3.111   15.062  1.00 11.49 ? 199 ARG B O   1 
ATOM   3859 C  CB  . ARG B 1 152 ? -1.176  1.595   15.150  1.00 12.87 ? 199 ARG B CB  1 
ATOM   3860 C  CG  . ARG B 1 152 ? -1.008  2.138   13.735  1.00 14.60 ? 199 ARG B CG  1 
ATOM   3861 C  CD  . ARG B 1 152 ? -1.989  1.455   12.843  1.00 14.36 ? 199 ARG B CD  1 
ATOM   3862 N  NE  . ARG B 1 152 ? -1.616  1.703   11.436  1.00 13.31 ? 199 ARG B NE  1 
ATOM   3863 C  CZ  . ARG B 1 152 ? -0.677  1.045   10.760  1.00 13.32 ? 199 ARG B CZ  1 
ATOM   3864 N  NH1 . ARG B 1 152 ? 0.137   0.188   11.345  1.00 14.18 ? 199 ARG B NH1 1 
ATOM   3865 N  NH2 . ARG B 1 152 ? -0.615  1.184   9.441   1.00 12.16 ? 199 ARG B NH2 1 
ATOM   3866 N  N   . ASN B 1 153 ? -4.236  1.093   16.036  1.00 11.02 ? 200 ASN B N   1 
ATOM   3867 C  CA  . ASN B 1 153 ? -5.614  0.917   15.617  1.00 10.77 ? 200 ASN B CA  1 
ATOM   3868 C  C   . ASN B 1 153 ? -6.582  1.720   16.462  1.00 11.08 ? 200 ASN B C   1 
ATOM   3869 O  O   . ASN B 1 153 ? -7.539  2.266   15.943  1.00 12.40 ? 200 ASN B O   1 
ATOM   3870 C  CB  . ASN B 1 153 ? -5.993  -0.566  15.576  1.00 11.55 ? 200 ASN B CB  1 
ATOM   3871 C  CG  . ASN B 1 153 ? -5.495  -1.206  14.312  1.00 12.08 ? 200 ASN B CG  1 
ATOM   3872 O  OD1 . ASN B 1 153 ? -6.221  -1.271  13.316  1.00 13.26 ? 200 ASN B OD1 1 
ATOM   3873 N  ND2 . ASN B 1 153 ? -4.229  -1.522  14.249  1.00 12.86 ? 200 ASN B ND2 1 
ATOM   3874 N  N   . LEU B 1 154 ? -6.326  1.852   17.758  1.00 11.23 ? 201 LEU B N   1 
ATOM   3875 C  CA  . LEU B 1 154 ? -7.151  2.752   18.556  1.00 11.10 ? 201 LEU B CA  1 
ATOM   3876 C  C   . LEU B 1 154 ? -7.043  4.184   18.018  1.00 11.20 ? 201 LEU B C   1 
ATOM   3877 O  O   . LEU B 1 154 ? -8.041  4.889   17.949  1.00 12.26 ? 201 LEU B O   1 
ATOM   3878 C  CB  . LEU B 1 154 ? -6.774  2.627   20.039  1.00 11.89 ? 201 LEU B CB  1 
ATOM   3879 C  CG  . LEU B 1 154 ? -7.175  1.318   20.718  1.00 13.74 ? 201 LEU B CG  1 
ATOM   3880 C  CD1 . LEU B 1 154 ? -6.580  1.331   22.126  1.00 16.85 ? 201 LEU B CD1 1 
ATOM   3881 C  CD2 . LEU B 1 154 ? -8.653  1.100   20.749  1.00 17.97 ? 201 LEU B CD2 1 
ATOM   3882 N  N   . ALA B 1 155 ? -5.827  4.630   17.729  1.00 11.45 ? 202 ALA B N   1 
ATOM   3883 C  CA  . ALA B 1 155 ? -5.658  5.983   17.213  1.00 11.24 ? 202 ALA B CA  1 
ATOM   3884 C  C   . ALA B 1 155 ? -6.432  6.150   15.909  1.00 12.28 ? 202 ALA B C   1 
ATOM   3885 O  O   . ALA B 1 155 ? -7.055  7.185   15.682  1.00 13.93 ? 202 ALA B O   1 
ATOM   3886 C  CB  . ALA B 1 155 ? -4.203  6.277   17.027  1.00 11.95 ? 202 ALA B CB  1 
ATOM   3887 N  N   . ARG B 1 156 ? -6.392  5.151   15.050  1.00 11.91 ? 203 ARG B N   1 
ATOM   3888 C  CA  . ARG B 1 156 ? -7.112  5.235   13.781  1.00 13.16 ? 203 ARG B CA  1 
ATOM   3889 C  C   . ARG B 1 156 ? -8.614  5.296   13.981  1.00 13.42 ? 203 ARG B C   1 
ATOM   3890 O  O   . ARG B 1 156 ? -9.288  6.095   13.309  1.00 14.65 ? 203 ARG B O   1 
ATOM   3891 C  CB  . ARG B 1 156 ? -6.675  4.057   12.911  1.00 14.17 ? 203 ARG B CB  1 
ATOM   3892 C  CG  . ARG B 1 156 ? -7.405  4.019   11.578  1.00 14.92 ? 203 ARG B CG  1 
ATOM   3893 C  CD  . ARG B 1 156 ? -6.785  3.042   10.669  1.00 16.56 ? 203 ARG B CD  1 
ATOM   3894 N  NE  . ARG B 1 156 ? -7.565  3.030   9.424   1.00 19.42 ? 203 ARG B NE  1 
ATOM   3895 C  CZ  . ARG B 1 156 ? -8.388  2.048   9.089   1.00 20.84 ? 203 ARG B CZ  1 
ATOM   3896 N  NH1 . ARG B 1 156 ? -8.480  0.957   9.821   1.00 20.08 ? 203 ARG B NH1 1 
ATOM   3897 N  NH2 . ARG B 1 156 ? -9.096  2.189   7.971   1.00 23.30 ? 203 ARG B NH2 1 
ATOM   3898 N  N   . ILE B 1 157 ? -9.156  4.430   14.844  1.00 12.78 ? 204 ILE B N   1 
ATOM   3899 C  CA  . ILE B 1 157 ? -10.589 4.453   15.111  1.00 13.15 ? 204 ILE B CA  1 
ATOM   3900 C  C   . ILE B 1 157 ? -10.991 5.832   15.628  1.00 13.84 ? 204 ILE B C   1 
ATOM   3901 O  O   . ILE B 1 157 ? -12.087 6.316   15.349  1.00 16.79 ? 204 ILE B O   1 
ATOM   3902 C  CB  . ILE B 1 157 ? -10.939 3.344   16.123  1.00 15.81 ? 204 ILE B CB  1 
ATOM   3903 C  CG1 . ILE B 1 157 ? -10.786 1.960   15.469  1.00 15.60 ? 204 ILE B CG1 1 
ATOM   3904 C  CG2 . ILE B 1 157 ? -12.338 3.506   16.725  1.00 15.81 ? 204 ILE B CG2 1 
ATOM   3905 C  CD1 . ILE B 1 157 ? -10.651 0.835   16.480  1.00 17.26 ? 204 ILE B CD1 1 
ATOM   3906 N  N   . GLY B 1 158 ? -10.127 6.436   16.415  1.00 12.90 ? 205 GLY B N   1 
ATOM   3907 C  CA  . GLY B 1 158 ? -10.420 7.717   17.029  1.00 14.51 ? 205 GLY B CA  1 
ATOM   3908 C  C   . GLY B 1 158 ? -10.139 8.928   16.153  1.00 14.93 ? 205 GLY B C   1 
ATOM   3909 O  O   . GLY B 1 158 ? -10.355 10.043  16.613  1.00 15.17 ? 205 GLY B O   1 
ATOM   3910 N  N   . PHE B 1 159 ? -9.642  8.749   14.934  1.00 17.04 ? 206 PHE B N   1 
ATOM   3911 C  CA  . PHE B 1 159 ? -9.203  9.898   14.153  1.00 19.48 ? 206 PHE B CA  1 
ATOM   3912 C  C   . PHE B 1 159 ? -10.406 10.805  13.914  1.00 19.53 ? 206 PHE B C   1 
ATOM   3913 O  O   . PHE B 1 159 ? -11.527 10.379  13.646  1.00 21.25 ? 206 PHE B O   1 
ATOM   3914 C  CB  . PHE B 1 159 ? -8.534  9.441   12.852  1.00 25.62 ? 206 PHE B CB  1 
ATOM   3915 C  CG  . PHE B 1 159 ? -7.549  10.451  12.271  1.00 31.22 ? 206 PHE B CG  1 
ATOM   3916 C  CD1 . PHE B 1 159 ? -6.625  11.116  13.089  1.00 34.67 ? 206 PHE B CD1 1 
ATOM   3917 C  CD2 . PHE B 1 159 ? -7.576  10.757  10.921  1.00 32.61 ? 206 PHE B CD2 1 
ATOM   3918 C  CE1 . PHE B 1 159 ? -5.735  12.048  12.558  1.00 39.24 ? 206 PHE B CE1 1 
ATOM   3919 C  CE2 . PHE B 1 159 ? -6.674  11.667  10.391  1.00 33.56 ? 206 PHE B CE2 1 
ATOM   3920 C  CZ  . PHE B 1 159 ? -5.767  12.318  11.202  1.00 35.35 ? 206 PHE B CZ  1 
ATOM   3921 N  N   . GLY B 1 160 ? -10.146 12.100  14.138  1.00 20.34 ? 207 GLY B N   1 
ATOM   3922 C  CA  . GLY B 1 160 ? -11.166 13.121  14.059  1.00 20.30 ? 207 GLY B CA  1 
ATOM   3923 C  C   . GLY B 1 160 ? -11.733 13.510  15.414  1.00 22.08 ? 207 GLY B C   1 
ATOM   3924 O  O   . GLY B 1 160 ? -12.278 14.605  15.544  1.00 23.17 ? 207 GLY B O   1 
ATOM   3925 N  N   . LYS B 1 161 ? -11.587 12.641  16.425  1.00 16.28 ? 208 LYS B N   1 
ATOM   3926 C  CA  . LYS B 1 161 ? -12.080 12.919  17.763  1.00 17.11 ? 208 LYS B CA  1 
ATOM   3927 C  C   . LYS B 1 161 ? -10.929 13.039  18.767  1.00 15.18 ? 208 LYS B C   1 
ATOM   3928 O  O   . LYS B 1 161 ? -11.113 13.637  19.821  1.00 16.08 ? 208 LYS B O   1 
ATOM   3929 C  CB  . LYS B 1 161 ? -13.025 11.825  18.253  1.00 16.98 ? 208 LYS B CB  1 
ATOM   3930 C  CG  . LYS B 1 161 ? -14.316 11.723  17.395  1.00 19.52 ? 208 LYS B CG  1 
ATOM   3931 C  CD  . LYS B 1 161 ? -15.318 10.685  17.896  1.00 24.80 ? 208 LYS B CD  1 
ATOM   3932 C  CE  . LYS B 1 161 ? -16.470 10.450  16.950  1.00 27.70 ? 208 LYS B CE  1 
ATOM   3933 N  NZ  . LYS B 1 161 ? -17.530 9.647   17.603  1.00 28.47 ? 208 LYS B NZ  1 
ATOM   3934 N  N   . VAL B 1 162 ? -9.827  12.320  18.537  1.00 13.43 ? 209 VAL B N   1 
ATOM   3935 C  CA  . VAL B 1 162 ? -8.638  12.342  19.385  1.00 12.76 ? 209 VAL B CA  1 
ATOM   3936 C  C   . VAL B 1 162 ? -7.415  12.381  18.488  1.00 12.98 ? 209 VAL B C   1 
ATOM   3937 O  O   . VAL B 1 162 ? -7.440  11.923  17.335  1.00 14.73 ? 209 VAL B O   1 
ATOM   3938 C  CB  . VAL B 1 162 ? -8.472  11.149  20.354  1.00 14.52 ? 209 VAL B CB  1 
ATOM   3939 C  CG1 . VAL B 1 162 ? -9.627  11.139  21.340  1.00 15.11 ? 209 VAL B CG1 1 
ATOM   3940 C  CG2 . VAL B 1 162 ? -8.345  9.805   19.663  1.00 15.44 ? 209 VAL B CG2 1 
ATOM   3941 N  N   . VAL B 1 163 ? -6.333  12.911  19.035  1.00 12.62 ? 210 VAL B N   1 
ATOM   3942 C  CA  . VAL B 1 163 ? -5.017  12.889  18.389  1.00 12.23 ? 210 VAL B CA  1 
ATOM   3943 C  C   . VAL B 1 163 ? -4.051  12.296  19.391  1.00 12.55 ? 210 VAL B C   1 
ATOM   3944 O  O   . VAL B 1 163 ? -4.285  12.380  20.592  1.00 13.81 ? 210 VAL B O   1 
ATOM   3945 C  CB  . VAL B 1 163 ? -4.496  14.273  17.949  1.00 14.64 ? 210 VAL B CB  1 
ATOM   3946 C  CG1 . VAL B 1 163 ? -5.306  14.753  16.753  1.00 17.58 ? 210 VAL B CG1 1 
ATOM   3947 C  CG2 . VAL B 1 163 ? -4.552  15.286  19.082  1.00 16.22 ? 210 VAL B CG2 1 
ATOM   3948 N  N   . VAL B 1 164 ? -2.954  11.742  18.914  1.00 12.32 ? 211 VAL B N   1 
ATOM   3949 C  CA  . VAL B 1 164 ? -1.886  11.284  19.779  1.00 12.93 ? 211 VAL B CA  1 
ATOM   3950 C  C   . VAL B 1 164 ? -1.038  12.471  20.179  1.00 13.94 ? 211 VAL B C   1 
ATOM   3951 O  O   . VAL B 1 164 ? -0.428  13.110  19.349  1.00 16.65 ? 211 VAL B O   1 
ATOM   3952 C  CB  . VAL B 1 164 ? -1.029  10.218  19.088  1.00 15.55 ? 211 VAL B CB  1 
ATOM   3953 C  CG1 . VAL B 1 164 ? -0.046  9.613   20.110  1.00 17.43 ? 211 VAL B CG1 1 
ATOM   3954 C  CG2 . VAL B 1 164 ? -1.894  9.085   18.551  1.00 17.26 ? 211 VAL B CG2 1 
ATOM   3955 N  N   . ARG B 1 165 ? -0.887  12.680  21.481  1.00 11.64 ? 212 ARG B N   1 
ATOM   3956 C  CA  . ARG B 1 165 ? -0.097  13.782  21.981  1.00 11.94 ? 212 ARG B CA  1 
ATOM   3957 C  C   . ARG B 1 165 ? 1.347   13.353  22.131  1.00 14.05 ? 212 ARG B C   1 
ATOM   3958 O  O   . ARG B 1 165 ? 2.269   14.048  21.687  1.00 14.77 ? 212 ARG B O   1 
ATOM   3959 C  CB  . ARG B 1 165 ? -0.658  14.265  23.313  1.00 12.24 ? 212 ARG B CB  1 
ATOM   3960 C  CG  . ARG B 1 165 ? 0.036   15.470  23.910  1.00 14.41 ? 212 ARG B CG  1 
ATOM   3961 C  CD  . ARG B 1 165 ? -0.475  15.811  25.286  1.00 14.57 ? 212 ARG B CD  1 
ATOM   3962 N  NE  . ARG B 1 165 ? 0.236   16.957  25.845  1.00 17.00 ? 212 ARG B NE  1 
ATOM   3963 C  CZ  . ARG B 1 165 ? 0.052   18.212  25.501  1.00 21.46 ? 212 ARG B CZ  1 
ATOM   3964 N  NH1 . ARG B 1 165 ? -1.000  18.550  24.776  1.00 21.25 ? 212 ARG B NH1 1 
ATOM   3965 N  NH2 . ARG B 1 165 ? 0.924   19.145  25.868  1.00 24.24 ? 212 ARG B NH2 1 
ATOM   3966 N  N   . TRP B 1 166 ? 1.585   12.210  22.805  1.00 12.02 ? 213 TRP B N   1 
ATOM   3967 C  CA  . TRP B 1 166 ? 2.924   11.662  22.941  1.00 11.87 ? 213 TRP B CA  1 
ATOM   3968 C  C   . TRP B 1 166 ? 2.818   10.161  23.148  1.00 11.24 ? 213 TRP B C   1 
ATOM   3969 O  O   . TRP B 1 166 ? 1.766   9.664   23.510  1.00 12.53 ? 213 TRP B O   1 
ATOM   3970 C  CB  . TRP B 1 166 ? 3.747   12.348  24.051  1.00 12.35 ? 213 TRP B CB  1 
ATOM   3971 C  CG  . TRP B 1 166 ? 3.148   12.365  25.419  1.00 12.34 ? 213 TRP B CG  1 
ATOM   3972 C  CD1 . TRP B 1 166 ? 2.399   13.327  25.999  1.00 12.41 ? 213 TRP B CD1 1 
ATOM   3973 C  CD2 . TRP B 1 166 ? 3.282   11.334  26.408  1.00 11.61 ? 213 TRP B CD2 1 
ATOM   3974 N  NE1 . TRP B 1 166 ? 2.081   12.995  27.294  1.00 13.13 ? 213 TRP B NE1 1 
ATOM   3975 C  CE2 . TRP B 1 166 ? 2.611   11.773  27.564  1.00 13.39 ? 213 TRP B CE2 1 
ATOM   3976 C  CE3 . TRP B 1 166 ? 3.932   10.095  26.438  1.00 13.51 ? 213 TRP B CE3 1 
ATOM   3977 C  CZ2 . TRP B 1 166 ? 2.546   11.001  28.692  1.00 13.41 ? 213 TRP B CZ2 1 
ATOM   3978 C  CZ3 . TRP B 1 166 ? 3.812   9.300   27.562  1.00 14.74 ? 213 TRP B CZ3 1 
ATOM   3979 C  CH2 . TRP B 1 166 ? 3.167   9.769   28.685  1.00 15.43 ? 213 TRP B CH2 1 
ATOM   3980 N  N   . SER B 1 167 ? 3.918   9.453   22.845  1.00 12.64 ? 214 SER B N   1 
ATOM   3981 C  CA  . SER B 1 167 ? 3.960   8.011   22.787  1.00 13.28 ? 214 SER B CA  1 
ATOM   3982 C  C   . SER B 1 167 ? 5.296   7.572   23.344  1.00 14.70 ? 214 SER B C   1 
ATOM   3983 O  O   . SER B 1 167 ? 6.287   8.252   23.106  1.00 18.41 ? 214 SER B O   1 
ATOM   3984 C  CB  . SER B 1 167 ? 3.872   7.599   21.306  1.00 17.31 ? 214 SER B CB  1 
ATOM   3985 O  OG  . SER B 1 167 ? 4.080   6.225   21.049  1.00 26.34 ? 214 SER B OG  1 
ATOM   3986 N  N   . GLN B 1 168 ? 5.313   6.493   24.130  1.00 11.65 ? 215 GLN B N   1 
ATOM   3987 C  CA  . GLN B 1 168 ? 6.560   5.967   24.636  1.00 11.77 ? 215 GLN B CA  1 
ATOM   3988 C  C   . GLN B 1 168 ? 6.553   4.446   24.517  1.00 10.96 ? 215 GLN B C   1 
ATOM   3989 O  O   . GLN B 1 168 ? 5.652   3.780   25.028  1.00 12.66 ? 215 GLN B O   1 
ATOM   3990 C  CB  . GLN B 1 168 ? 6.690   6.333   26.122  1.00 13.72 ? 215 GLN B CB  1 
ATOM   3991 C  CG  . GLN B 1 168 ? 7.991   5.825   26.742  1.00 14.34 ? 215 GLN B CG  1 
ATOM   3992 C  CD  . GLN B 1 168 ? 9.180   6.587   26.205  1.00 17.15 ? 215 GLN B CD  1 
ATOM   3993 O  OE1 . GLN B 1 168 ? 9.259   7.815   26.293  1.00 18.86 ? 215 GLN B OE1 1 
ATOM   3994 N  NE2 . GLN B 1 168 ? 10.089  5.864   25.570  1.00 17.26 ? 215 GLN B NE2 1 
ATOM   3995 N  N   . LEU B 1 169 ? 7.611   3.874   23.929  1.00 12.26 ? 216 LEU B N   1 
ATOM   3996 C  CA  . LEU B 1 169 ? 7.826   2.429   23.946  1.00 13.59 ? 216 LEU B CA  1 
ATOM   3997 C  C   . LEU B 1 169 ? 8.710   2.099   25.132  1.00 12.78 ? 216 LEU B C   1 
ATOM   3998 O  O   . LEU B 1 169 ? 9.658   2.818   25.445  1.00 14.22 ? 216 LEU B O   1 
ATOM   3999 C  CB  . LEU B 1 169 ? 8.557   2.014   22.665  1.00 17.75 ? 216 LEU B CB  1 
ATOM   4000 C  CG  . LEU B 1 169 ? 8.110   0.756   21.915  1.00 27.94 ? 216 LEU B CG  1 
ATOM   4001 C  CD1 . LEU B 1 169 ? 6.619   0.648   21.706  1.00 30.53 ? 216 LEU B CD1 1 
ATOM   4002 C  CD2 . LEU B 1 169 ? 8.810   0.787   20.554  1.00 28.11 ? 216 LEU B CD2 1 
ATOM   4003 N  N   . GLY B 1 170 ? 8.499   0.962   25.747  1.00 12.44 ? 217 GLY B N   1 
ATOM   4004 C  CA  . GLY B 1 170 ? 9.356   0.481   26.801  1.00 12.68 ? 217 GLY B CA  1 
ATOM   4005 C  C   . GLY B 1 170 ? 9.503   -1.049  26.820  1.00 14.91 ? 217 GLY B C   1 
ATOM   4006 O  O   . GLY B 1 170 ? 8.806   -1.785  26.152  1.00 13.06 ? 217 GLY B O   1 
ATOM   4007 N  N   . PHE B 1 171 ? 10.477  -1.528  27.616  1.00 14.49 ? 218 PHE B N   1 
ATOM   4008 C  CA  . PHE B 1 171 ? 10.796  -2.946  27.757  1.00 14.83 ? 218 PHE B CA  1 
ATOM   4009 C  C   . PHE B 1 171 ? 11.198  -3.253  29.209  1.00 15.10 ? 218 PHE B C   1 
ATOM   4010 O  O   . PHE B 1 171 ? 11.666  -2.402  29.954  1.00 14.93 ? 218 PHE B O   1 
ATOM   4011 C  CB  . PHE B 1 171 ? 11.813  -3.363  26.694  1.00 14.60 ? 218 PHE B CB  1 
ATOM   4012 C  CG  . PHE B 1 171 ? 13.158  -2.657  26.788  1.00 15.72 ? 218 PHE B CG  1 
ATOM   4013 C  CD1 . PHE B 1 171 ? 14.113  -3.102  27.692  1.00 17.59 ? 218 PHE B CD1 1 
ATOM   4014 C  CD2 . PHE B 1 171 ? 13.452  -1.576  25.957  1.00 17.42 ? 218 PHE B CD2 1 
ATOM   4015 C  CE1 . PHE B 1 171 ? 15.363  -2.486  27.734  1.00 18.59 ? 218 PHE B CE1 1 
ATOM   4016 C  CE2 . PHE B 1 171 ? 14.667  -0.922  26.053  1.00 19.37 ? 218 PHE B CE2 1 
ATOM   4017 C  CZ  . PHE B 1 171 ? 15.633  -1.394  26.944  1.00 18.72 ? 218 PHE B CZ  1 
ATOM   4018 N  N   . GLY B 1 172 ? 10.822  -4.444  29.641  1.00 17.20 ? 219 GLY B N   1 
ATOM   4019 C  CA  . GLY B 1 172 ? 11.325  -4.993  30.880  1.00 16.93 ? 219 GLY B CA  1 
ATOM   4020 C  C   . GLY B 1 172 ? 12.136  -6.249  30.549  1.00 18.87 ? 219 GLY B C   1 
ATOM   4021 O  O   . GLY B 1 172 ? 13.156  -6.182  29.865  1.00 22.46 ? 219 GLY B O   1 
ATOM   4022 N  N   . LYS B 1 173 ? 11.704  -7.398  31.067  1.00 17.89 ? 220 LYS B N   1 
ATOM   4023 C  CA  . LYS B 1 173 ? 12.422  -8.635  30.837  1.00 20.05 ? 220 LYS B CA  1 
ATOM   4024 C  C   . LYS B 1 173 ? 11.907  -9.230  29.539  1.00 19.63 ? 220 LYS B C   1 
ATOM   4025 O  O   . LYS B 1 173 ? 10.872  -8.819  29.021  1.00 19.89 ? 220 LYS B O   1 
ATOM   4026 C  CB  . LYS B 1 173 ? 12.258  -9.627  31.988  1.00 25.07 ? 220 LYS B CB  1 
ATOM   4027 C  CG  . LYS B 1 173 ? 10.830  -9.934  32.362  1.00 31.23 ? 220 LYS B CG  1 
ATOM   4028 C  CD  . LYS B 1 173 ? 10.679  -11.066 33.377  1.00 37.62 ? 220 LYS B CD  1 
ATOM   4029 C  CE  . LYS B 1 173 ? 11.219  -10.637 34.704  1.00 39.94 ? 220 LYS B CE  1 
ATOM   4030 N  NZ  . LYS B 1 173 ? 11.109  -11.725 35.676  1.00 39.80 ? 220 LYS B NZ  1 
ATOM   4031 N  N   . THR B 1 174 ? 12.621  -10.219 29.032  1.00 18.87 ? 221 THR B N   1 
ATOM   4032 C  CA  . THR B 1 174 ? 12.170  -11.059 27.946  1.00 18.55 ? 221 THR B CA  1 
ATOM   4033 C  C   . THR B 1 174 ? 11.872  -12.434 28.548  1.00 20.42 ? 221 THR B C   1 
ATOM   4034 O  O   . THR B 1 174 ? 12.767  -13.168 28.966  1.00 21.34 ? 221 THR B O   1 
ATOM   4035 C  CB  . THR B 1 174 ? 13.245  -11.081 26.856  1.00 18.11 ? 221 THR B CB  1 
ATOM   4036 O  OG1 . THR B 1 174 ? 13.428  -9.725  26.429  1.00 18.80 ? 221 THR B OG1 1 
ATOM   4037 C  CG2 . THR B 1 174 ? 12.909  -12.007 25.702  1.00 18.04 ? 221 THR B CG2 1 
ATOM   4038 N  N   . SER B 1 175 ? 10.591  -12.776 28.618  1.00 19.53 ? 222 SER B N   1 
ATOM   4039 C  CA  . SER B 1 175 ? 10.108  -13.903 29.409  1.00 22.16 ? 222 SER B CA  1 
ATOM   4040 C  C   . SER B 1 175 ? 10.513  -15.242 28.807  1.00 25.78 ? 222 SER B C   1 
ATOM   4041 O  O   . SER B 1 175 ? 10.594  -16.219 29.547  1.00 30.47 ? 222 SER B O   1 
ATOM   4042 C  CB  . SER B 1 175 ? 8.621   -13.860 29.552  1.00 24.21 ? 222 SER B CB  1 
ATOM   4043 O  OG  . SER B 1 175 ? 8.288   -12.899 30.513  1.00 26.78 ? 222 SER B OG  1 
ATOM   4044 N  N   . SER B 1 176 ? 10.715  -15.298 27.487  1.00 25.33 ? 223 SER B N   1 
ATOM   4045 C  CA  . SER B 1 176 ? 11.059  -16.545 26.822  1.00 29.43 ? 223 SER B CA  1 
ATOM   4046 C  C   . SER B 1 176 ? 12.400  -17.064 27.341  1.00 31.71 ? 223 SER B C   1 
ATOM   4047 O  O   . SER B 1 176 ? 12.619  -18.270 27.359  1.00 33.23 ? 223 SER B O   1 
ATOM   4048 C  CB  . SER B 1 176 ? 11.087  -16.365 25.331  1.00 30.41 ? 223 SER B CB  1 
ATOM   4049 O  OG  . SER B 1 176 ? 12.087  -15.429 24.932  1.00 34.86 ? 223 SER B OG  1 
ATOM   4050 N  N   . THR B 1 177 ? 13.284  -16.160 27.785  1.00 29.29 ? 224 THR B N   1 
ATOM   4051 C  CA  . THR B 1 177 ? 14.650  -16.520 28.150  1.00 28.97 ? 224 THR B CA  1 
ATOM   4052 C  C   . THR B 1 177 ? 14.970  -16.202 29.613  1.00 30.74 ? 224 THR B C   1 
ATOM   4053 O  O   . THR B 1 177 ? 16.043  -16.557 30.092  1.00 34.32 ? 224 THR B O   1 
ATOM   4054 C  CB  . THR B 1 177 ? 15.623  -15.770 27.238  1.00 32.50 ? 224 THR B CB  1 
ATOM   4055 O  OG1 . THR B 1 177 ? 15.427  -14.392 27.527  1.00 37.28 ? 224 THR B OG1 1 
ATOM   4056 C  CG2 . THR B 1 177 ? 15.353  -15.952 25.759  1.00 39.67 ? 224 THR B CG2 1 
ATOM   4057 N  N   . THR B 1 178 ? 14.079  -15.502 30.335  1.00 25.00 ? 225 THR B N   1 
ATOM   4058 C  CA  . THR B 1 178 ? 14.372  -15.014 31.675  1.00 27.37 ? 225 THR B CA  1 
ATOM   4059 C  C   . THR B 1 178 ? 13.278  -15.542 32.592  1.00 30.50 ? 225 THR B C   1 
ATOM   4060 O  O   . THR B 1 178 ? 12.105  -15.245 32.351  1.00 35.22 ? 225 THR B O   1 
ATOM   4061 C  CB  . THR B 1 178 ? 14.409  -13.479 31.692  1.00 26.23 ? 225 THR B CB  1 
ATOM   4062 O  OG1 . THR B 1 178 ? 15.195  -12.993 30.597  1.00 28.56 ? 225 THR B OG1 1 
ATOM   4063 C  CG2 . THR B 1 178 ? 14.924  -12.901 33.000  1.00 25.07 ? 225 THR B CG2 1 
ATOM   4064 N  N   . PRO B 1 179 ? 13.606  -16.268 33.688  1.00 33.68 ? 226 PRO B N   1 
ATOM   4065 C  CA  . PRO B 1 179 ? 12.571  -16.794 34.584  1.00 36.01 ? 226 PRO B CA  1 
ATOM   4066 C  C   . PRO B 1 179 ? 11.711  -15.672 35.169  1.00 39.81 ? 226 PRO B C   1 
ATOM   4067 O  O   . PRO B 1 179 ? 12.194  -14.565 35.446  1.00 33.90 ? 226 PRO B O   1 
ATOM   4068 C  CB  . PRO B 1 179 ? 13.319  -17.595 35.694  1.00 38.15 ? 226 PRO B CB  1 
ATOM   4069 C  CG  . PRO B 1 179 ? 14.759  -17.668 35.218  1.00 37.14 ? 226 PRO B CG  1 
ATOM   4070 C  CD  . PRO B 1 179 ? 14.963  -16.572 34.168  1.00 37.13 ? 226 PRO B CD  1 
ATOM   4071 N  N   . ASP B 1 180 ? 10.434  -15.996 35.398  1.00 37.54 ? 227 ASP B N   1 
ATOM   4072 C  CA  . ASP B 1 180 ? 9.456   -15.012 35.824  1.00 42.79 ? 227 ASP B CA  1 
ATOM   4073 C  C   . ASP B 1 180 ? 9.846   -14.443 37.189  1.00 43.23 ? 227 ASP B C   1 
ATOM   4074 O  O   . ASP B 1 180 ? 9.497   -13.302 37.494  1.00 46.69 ? 227 ASP B O   1 
ATOM   4075 C  CB  . ASP B 1 180 ? 8.048   -15.596 35.809  1.00 50.15 ? 227 ASP B CB  1 
ATOM   4076 C  CG  . ASP B 1 180 ? 7.003   -14.778 36.557  1.00 58.14 ? 227 ASP B CG  1 
ATOM   4077 O  OD1 . ASP B 1 180 ? 7.009   -14.822 37.810  1.00 62.38 ? 227 ASP B OD1 1 
ATOM   4078 O  OD2 . ASP B 1 180 ? 6.226   -14.068 35.886  1.00 66.32 ? 227 ASP B OD2 1 
ATOM   4079 N  N   . LYS B 1 181 ? 10.548  -15.238 38.011  1.00 41.96 ? 228 LYS B N   1 
ATOM   4080 C  CA  . LYS B 1 181 ? 10.752  -14.876 39.406  1.00 45.86 ? 228 LYS B CA  1 
ATOM   4081 C  C   . LYS B 1 181 ? 12.004  -14.011 39.572  1.00 41.75 ? 228 LYS B C   1 
ATOM   4082 O  O   . LYS B 1 181 ? 12.249  -13.486 40.652  1.00 43.95 ? 228 LYS B O   1 
ATOM   4083 C  CB  . LYS B 1 181 ? 10.792  -16.118 40.312  1.00 51.66 ? 228 LYS B CB  1 
ATOM   4084 C  CG  . LYS B 1 181 ? 9.435   -16.569 40.863  1.00 53.23 ? 228 LYS B CG  1 
ATOM   4085 C  CD  . LYS B 1 181 ? 8.715   -15.497 41.678  1.00 59.22 ? 228 LYS B CD  1 
ATOM   4086 C  CE  . LYS B 1 181 ? 7.590   -16.009 42.532  1.00 62.49 ? 228 LYS B CE  1 
ATOM   4087 N  NZ  . LYS B 1 181 ? 6.414   -16.422 41.762  1.00 62.05 ? 228 LYS B NZ  1 
ATOM   4088 N  N   . GLN B 1 182 ? 12.805  -13.870 38.515  1.00 32.67 ? 229 GLN B N   1 
ATOM   4089 C  CA  . GLN B 1 182 ? 14.016  -13.062 38.584  1.00 28.37 ? 229 GLN B CA  1 
ATOM   4090 C  C   . GLN B 1 182 ? 13.621  -11.587 38.495  1.00 25.22 ? 229 GLN B C   1 
ATOM   4091 O  O   . GLN B 1 182 ? 12.823  -11.186 37.655  1.00 25.83 ? 229 GLN B O   1 
ATOM   4092 C  CB  . GLN B 1 182 ? 14.911  -13.552 37.451  1.00 29.31 ? 229 GLN B CB  1 
ATOM   4093 C  CG  . GLN B 1 182 ? 16.302  -12.934 37.410  1.00 30.31 ? 229 GLN B CG  1 
ATOM   4094 C  CD  . GLN B 1 182 ? 17.141  -13.577 36.329  1.00 35.01 ? 229 GLN B CD  1 
ATOM   4095 O  OE1 . GLN B 1 182 ? 17.305  -14.801 36.314  1.00 38.35 ? 229 GLN B OE1 1 
ATOM   4096 N  NE2 . GLN B 1 182 ? 17.661  -12.781 35.404  1.00 29.79 ? 229 GLN B NE2 1 
ATOM   4097 N  N   . THR B 1 183 ? 14.168  -10.765 39.398  1.00 22.99 ? 230 THR B N   1 
ATOM   4098 C  CA  . THR B 1 183 ? 13.913  -9.345  39.361  1.00 21.02 ? 230 THR B CA  1 
ATOM   4099 C  C   . THR B 1 183 ? 14.624  -8.784  38.124  1.00 17.64 ? 230 THR B C   1 
ATOM   4100 O  O   . THR B 1 183 ? 15.804  -9.085  37.929  1.00 21.29 ? 230 THR B O   1 
ATOM   4101 C  CB  . THR B 1 183 ? 14.416  -8.676  40.644  1.00 19.76 ? 230 THR B CB  1 
ATOM   4102 O  OG1 . THR B 1 183 ? 13.809  -9.461  41.696  1.00 23.29 ? 230 THR B OG1 1 
ATOM   4103 C  CG2 . THR B 1 183 ? 13.962  -7.230  40.716  1.00 20.46 ? 230 THR B CG2 1 
ATOM   4104 N  N   . PRO B 1 184 ? 13.938  -7.963  37.302  1.00 18.95 ? 231 PRO B N   1 
ATOM   4105 C  CA  . PRO B 1 184 ? 14.588  -7.289  36.173  1.00 17.80 ? 231 PRO B CA  1 
ATOM   4106 C  C   . PRO B 1 184 ? 15.600  -6.273  36.699  1.00 18.38 ? 231 PRO B C   1 
ATOM   4107 O  O   . PRO B 1 184 ? 15.470  -5.772  37.813  1.00 20.00 ? 231 PRO B O   1 
ATOM   4108 C  CB  . PRO B 1 184 ? 13.457  -6.584  35.405  1.00 22.34 ? 231 PRO B CB  1 
ATOM   4109 C  CG  . PRO B 1 184 ? 12.281  -6.513  36.344  1.00 25.51 ? 231 PRO B CG  1 
ATOM   4110 C  CD  . PRO B 1 184 ? 12.530  -7.572  37.396  1.00 21.16 ? 231 PRO B CD  1 
ATOM   4111 N  N   . ARG B 1 185 ? 16.598  -5.962  35.884  1.00 17.20 ? 232 ARG B N   1 
ATOM   4112 C  CA  . ARG B 1 185 ? 17.524  -4.880  36.185  1.00 16.32 ? 232 ARG B CA  1 
ATOM   4113 C  C   . ARG B 1 185 ? 17.126  -3.699  35.325  1.00 16.18 ? 232 ARG B C   1 
ATOM   4114 O  O   . ARG B 1 185 ? 16.715  -3.839  34.181  1.00 16.02 ? 232 ARG B O   1 
ATOM   4115 C  CB  . ARG B 1 185 ? 18.970  -5.259  35.879  1.00 17.08 ? 232 ARG B CB  1 
ATOM   4116 C  CG  . ARG B 1 185 ? 19.419  -6.330  36.847  1.00 17.58 ? 232 ARG B CG  1 
ATOM   4117 C  CD  . ARG B 1 185 ? 20.842  -6.720  36.669  1.00 18.47 ? 232 ARG B CD  1 
ATOM   4118 N  NE  . ARG B 1 185 ? 21.200  -7.800  37.594  1.00 18.90 ? 232 ARG B NE  1 
ATOM   4119 C  CZ  . ARG B 1 185 ? 21.946  -7.669  38.664  1.00 18.56 ? 232 ARG B CZ  1 
ATOM   4120 N  NH1 . ARG B 1 185 ? 22.306  -6.484  39.090  1.00 18.17 ? 232 ARG B NH1 1 
ATOM   4121 N  NH2 . ARG B 1 185 ? 22.224  -8.707  39.428  1.00 22.01 ? 232 ARG B NH2 1 
ATOM   4122 N  N   . ASN B 1 186 ? 17.253  -2.517  35.898  1.00 14.68 ? 233 ASN B N   1 
ATOM   4123 C  CA  . ASN B 1 186 ? 17.123  -1.295  35.136  1.00 14.83 ? 233 ASN B CA  1 
ATOM   4124 C  C   . ASN B 1 186 ? 18.438  -1.019  34.418  1.00 13.78 ? 233 ASN B C   1 
ATOM   4125 O  O   . ASN B 1 186 ? 19.407  -1.756  34.553  1.00 13.57 ? 233 ASN B O   1 
ATOM   4126 C  CB  . ASN B 1 186 ? 16.680  -0.138  36.036  1.00 15.11 ? 233 ASN B CB  1 
ATOM   4127 C  CG  . ASN B 1 186 ? 17.656  0.129   37.150  1.00 16.65 ? 233 ASN B CG  1 
ATOM   4128 O  OD1 . ASN B 1 186 ? 18.865  0.111   36.955  1.00 15.14 ? 233 ASN B OD1 1 
ATOM   4129 N  ND2 . ASN B 1 186 ? 17.140  0.401   38.335  1.00 17.38 ? 233 ASN B ND2 1 
ATOM   4130 N  N   . LEU B 1 187 ? 18.483  0.064   33.655  1.00 13.35 ? 234 LEU B N   1 
ATOM   4131 C  CA  . LEU B 1 187 ? 19.620  0.367   32.819  1.00 13.07 ? 234 LEU B CA  1 
ATOM   4132 C  C   . LEU B 1 187 ? 20.788  0.934   33.591  1.00 14.90 ? 234 LEU B C   1 
ATOM   4133 O  O   . LEU B 1 187 ? 21.850  1.151   33.019  1.00 15.80 ? 234 LEU B O   1 
ATOM   4134 C  CB  . LEU B 1 187 ? 19.241  1.273   31.665  1.00 13.49 ? 234 LEU B CB  1 
ATOM   4135 C  CG  . LEU B 1 187 ? 18.275  0.620   30.672  1.00 16.39 ? 234 LEU B CG  1 
ATOM   4136 C  CD1 . LEU B 1 187 ? 17.862  1.627   29.648  1.00 19.34 ? 234 LEU B CD1 1 
ATOM   4137 C  CD2 . LEU B 1 187 ? 18.915  -0.615  30.042  1.00 19.70 ? 234 LEU B CD2 1 
ATOM   4138 N  N   . LEU B 1 188 ? 20.623  1.126   34.888  1.00 12.75 ? 235 LEU B N   1 
ATOM   4139 C  CA  . LEU B 1 188 ? 21.759  1.448   35.744  1.00 12.82 ? 235 LEU B CA  1 
ATOM   4140 C  C   . LEU B 1 188 ? 22.409  0.152   36.239  1.00 14.40 ? 235 LEU B C   1 
ATOM   4141 O  O   . LEU B 1 188 ? 23.466  0.208   36.900  1.00 15.99 ? 235 LEU B O   1 
ATOM   4142 C  CB  . LEU B 1 188 ? 21.365  2.345   36.909  1.00 14.08 ? 235 LEU B CB  1 
ATOM   4143 C  CG  . LEU B 1 188 ? 20.822  3.716   36.529  1.00 13.58 ? 235 LEU B CG  1 
ATOM   4144 C  CD1 . LEU B 1 188 ? 20.572  4.482   37.817  1.00 16.79 ? 235 LEU B CD1 1 
ATOM   4145 C  CD2 . LEU B 1 188 ? 21.746  4.489   35.601  1.00 14.46 ? 235 LEU B CD2 1 
ATOM   4146 N  N   . GLY B 1 189 ? 21.836  -0.999  35.902  1.00 13.18 ? 236 GLY B N   1 
ATOM   4147 C  CA  . GLY B 1 189 ? 22.412  -2.304  36.220  1.00 12.63 ? 236 GLY B CA  1 
ATOM   4148 C  C   . GLY B 1 189 ? 22.019  -2.825  37.596  1.00 14.75 ? 236 GLY B C   1 
ATOM   4149 O  O   . GLY B 1 189 ? 22.542  -3.846  38.033  1.00 15.45 ? 236 GLY B O   1 
ATOM   4150 N  N   . PHE B 1 190 ? 21.053  -2.171  38.260  1.00 12.73 ? 237 PHE B N   1 
ATOM   4151 C  CA  . PHE B 1 190 ? 20.558  -2.602  39.546  1.00 13.43 ? 237 PHE B CA  1 
ATOM   4152 C  C   . PHE B 1 190 ? 19.224  -3.301  39.384  1.00 13.93 ? 237 PHE B C   1 
ATOM   4153 O  O   . PHE B 1 190 ? 18.388  -2.877  38.595  1.00 15.47 ? 237 PHE B O   1 
ATOM   4154 C  CB  . PHE B 1 190 ? 20.413  -1.424  40.518  1.00 12.95 ? 237 PHE B CB  1 
ATOM   4155 C  CG  . PHE B 1 190 ? 21.713  -1.026  41.174  1.00 13.01 ? 237 PHE B CG  1 
ATOM   4156 C  CD1 . PHE B 1 190 ? 22.708  -0.361  40.483  1.00 13.14 ? 237 PHE B CD1 1 
ATOM   4157 C  CD2 . PHE B 1 190 ? 21.956  -1.355  42.502  1.00 14.50 ? 237 PHE B CD2 1 
ATOM   4158 C  CE1 . PHE B 1 190 ? 23.901  -0.036  41.085  1.00 14.49 ? 237 PHE B CE1 1 
ATOM   4159 C  CE2 . PHE B 1 190 ? 23.162  -1.020  43.099  1.00 15.00 ? 237 PHE B CE2 1 
ATOM   4160 C  CZ  . PHE B 1 190 ? 24.127  -0.372  42.395  1.00 15.85 ? 237 PHE B CZ  1 
ATOM   4161 N  N   . LYS B 1 191 ? 19.018  -4.327  40.202  1.00 15.19 ? 238 LYS B N   1 
ATOM   4162 C  CA  . LYS B 1 191 ? 17.720  -4.962  40.264  1.00 14.83 ? 238 LYS B CA  1 
ATOM   4163 C  C   . LYS B 1 191 ? 16.676  -3.932  40.665  1.00 15.32 ? 238 LYS B C   1 
ATOM   4164 O  O   . LYS B 1 191 ? 16.909  -3.116  41.557  1.00 15.06 ? 238 LYS B O   1 
ATOM   4165 C  CB  . LYS B 1 191 ? 17.750  -6.079  41.305  1.00 15.10 ? 238 LYS B CB  1 
ATOM   4166 C  CG  . LYS B 1 191 ? 18.600  -7.263  40.921  1.00 17.43 ? 238 LYS B CG  1 
ATOM   4167 C  CD  . LYS B 1 191 ? 18.567  -8.364  41.958  1.00 17.64 ? 238 LYS B CD  1 
ATOM   4168 C  CE  . LYS B 1 191 ? 19.408  -9.541  41.604  1.00 20.84 ? 238 LYS B CE  1 
ATOM   4169 N  NZ  . LYS B 1 191 ? 19.361  -10.524 42.701  1.00 22.42 ? 238 LYS B NZ  1 
ATOM   4170 N  N   . ASP B 1 192 ? 15.501  -3.998  40.046  1.00 15.26 ? 239 ASP B N   1 
ATOM   4171 C  CA  . ASP B 1 192 ? 14.500  -2.973  40.188  1.00 15.03 ? 239 ASP B CA  1 
ATOM   4172 C  C   . ASP B 1 192 ? 13.156  -3.659  40.323  1.00 18.35 ? 239 ASP B C   1 
ATOM   4173 O  O   . ASP B 1 192 ? 12.643  -4.249  39.357  1.00 19.08 ? 239 ASP B O   1 
ATOM   4174 C  CB  . ASP B 1 192 ? 14.598  -1.950  39.059  1.00 16.54 ? 239 ASP B CB  1 
ATOM   4175 C  CG  . ASP B 1 192 ? 13.876  -0.648  39.315  1.00 20.12 ? 239 ASP B CG  1 
ATOM   4176 O  OD1 . ASP B 1 192 ? 12.895  -0.657  40.093  1.00 24.60 ? 239 ASP B OD1 1 
ATOM   4177 O  OD2 . ASP B 1 192 ? 14.355  0.356   38.839  1.00 18.96 ? 239 ASP B OD2 1 
ATOM   4178 N  N   . GLY B 1 193 ? 12.595  -3.579  41.531  1.00 15.63 ? 240 GLY B N   1 
ATOM   4179 C  CA  . GLY B 1 193 ? 11.263  -4.107  41.787  1.00 15.49 ? 240 GLY B CA  1 
ATOM   4180 C  C   . GLY B 1 193 ? 11.198  -5.024  43.003  1.00 15.00 ? 240 GLY B C   1 
ATOM   4181 O  O   . GLY B 1 193 ? 10.120  -5.554  43.285  1.00 17.74 ? 240 GLY B O   1 
ATOM   4182 N  N   . THR B 1 194 ? 12.304  -5.180  43.718  1.00 14.31 ? 241 THR B N   1 
ATOM   4183 C  CA  . THR B 1 194 ? 12.400  -6.081  44.837  1.00 14.89 ? 241 THR B CA  1 
ATOM   4184 C  C   . THR B 1 194 ? 11.299  -5.828  45.865  1.00 15.11 ? 241 THR B C   1 
ATOM   4185 O  O   . THR B 1 194 ? 10.593  -6.778  46.282  1.00 17.91 ? 241 THR B O   1 
ATOM   4186 C  CB  . THR B 1 194 ? 13.789  -5.961  45.458  1.00 16.37 ? 241 THR B CB  1 
ATOM   4187 O  OG1 . THR B 1 194 ? 14.779  -6.231  44.462  1.00 16.25 ? 241 THR B OG1 1 
ATOM   4188 C  CG2 . THR B 1 194 ? 13.890  -6.960  46.580  1.00 16.56 ? 241 THR B CG2 1 
ATOM   4189 N  N   . ARG B 1 195 ? 11.181  -4.586  46.324  1.00 14.06 ? 242 ARG B N   1 
ATOM   4190 C  CA  . ARG B 1 195 ? 10.200  -4.247  47.350  1.00 13.36 ? 242 ARG B CA  1 
ATOM   4191 C  C   . ARG B 1 195 ? 9.118   -3.401  46.705  1.00 14.49 ? 242 ARG B C   1 
ATOM   4192 O  O   . ARG B 1 195 ? 9.183   -2.179  46.641  1.00 16.09 ? 242 ARG B O   1 
ATOM   4193 C  CB  . ARG B 1 195 ? 10.756  -3.503  48.569  1.00 14.07 ? 242 ARG B CB  1 
ATOM   4194 C  CG  . ARG B 1 195 ? 11.362  -4.466  49.577  1.00 16.03 ? 242 ARG B CG  1 
ATOM   4195 C  CD  . ARG B 1 195 ? 12.064  -3.839  50.718  1.00 16.27 ? 242 ARG B CD  1 
ATOM   4196 N  NE  . ARG B 1 195 ? 11.271  -2.743  51.253  1.00 15.87 ? 242 ARG B NE  1 
ATOM   4197 C  CZ  . ARG B 1 195 ? 10.115  -2.828  51.847  1.00 17.27 ? 242 ARG B CZ  1 
ATOM   4198 N  NH1 . ARG B 1 195 ? 9.326   -1.773  51.888  1.00 18.97 ? 242 ARG B NH1 1 
ATOM   4199 N  NH2 . ARG B 1 195 ? 9.724   -3.988  52.355  1.00 20.13 ? 242 ARG B NH2 1 
ATOM   4200 N  N   . ASN B 1 196 ? 8.057   -4.077  46.278  1.00 15.01 ? 243 ASN B N   1 
ATOM   4201 C  CA  . ASN B 1 196 ? 6.990   -3.476  45.519  1.00 14.89 ? 243 ASN B CA  1 
ATOM   4202 C  C   . ASN B 1 196 ? 5.711   -4.141  46.019  1.00 17.68 ? 243 ASN B C   1 
ATOM   4203 O  O   . ASN B 1 196 ? 5.770   -5.226  46.599  1.00 23.07 ? 243 ASN B O   1 
ATOM   4204 C  CB  . ASN B 1 196 ? 7.210   -3.719  44.039  1.00 14.67 ? 243 ASN B CB  1 
ATOM   4205 C  CG  . ASN B 1 196 ? 6.388   -2.877  43.116  1.00 14.36 ? 243 ASN B CG  1 
ATOM   4206 O  OD1 . ASN B 1 196 ? 5.827   -1.858  43.508  1.00 13.89 ? 243 ASN B OD1 1 
ATOM   4207 N  ND2 . ASN B 1 196 ? 6.428   -3.261  41.861  1.00 17.10 ? 243 ASN B ND2 1 
ATOM   4208 N  N   . ILE B 1 197 ? 4.572   -3.606  45.640  1.00 15.72 ? 244 ILE B N   1 
ATOM   4209 C  CA  . ILE B 1 197 ? 3.314   -4.303  45.819  1.00 15.34 ? 244 ILE B CA  1 
ATOM   4210 C  C   . ILE B 1 197 ? 3.168   -5.311  44.696  1.00 17.48 ? 244 ILE B C   1 
ATOM   4211 O  O   . ILE B 1 197 ? 3.355   -4.948  43.532  1.00 21.34 ? 244 ILE B O   1 
ATOM   4212 C  CB  . ILE B 1 197 ? 2.145   -3.318  45.877  1.00 15.17 ? 244 ILE B CB  1 
ATOM   4213 C  CG1 . ILE B 1 197 ? 2.296   -2.322  47.022  1.00 15.55 ? 244 ILE B CG1 1 
ATOM   4214 C  CG2 . ILE B 1 197 ? 0.799   -4.049  45.949  1.00 17.58 ? 244 ILE B CG2 1 
ATOM   4215 C  CD1 . ILE B 1 197 ? 1.253   -1.225  47.011  1.00 17.83 ? 244 ILE B CD1 1 
ATOM   4216 N  N   . ALA B 1 198 ? 2.883   -6.566  45.049  1.00 17.80 ? 245 ALA B N   1 
ATOM   4217 C  CA  . ALA B 1 198 ? 2.724   -7.635  44.073  1.00 19.14 ? 245 ALA B CA  1 
ATOM   4218 C  C   . ALA B 1 198 ? 1.234   -7.811  43.808  1.00 18.12 ? 245 ALA B C   1 
ATOM   4219 O  O   . ALA B 1 198 ? 0.388   -7.557  44.654  1.00 18.51 ? 245 ALA B O   1 
ATOM   4220 C  CB  . ALA B 1 198 ? 3.346   -8.903  44.586  1.00 20.92 ? 245 ALA B CB  1 
ATOM   4221 N  N   . GLY B 1 199 ? 0.883   -8.264  42.598  1.00 20.36 ? 246 GLY B N   1 
ATOM   4222 C  CA  . GLY B 1 199 ? -0.517  -8.457  42.247  1.00 22.31 ? 246 GLY B CA  1 
ATOM   4223 C  C   . GLY B 1 199 ? -1.203  -9.566  43.035  1.00 20.05 ? 246 GLY B C   1 
ATOM   4224 O  O   . GLY B 1 199 ? -2.439  -9.615  43.116  1.00 21.88 ? 246 GLY B O   1 
ATOM   4225 N  N   . THR B 1 200 ? -0.412  -10.377 43.737  1.00 19.79 ? 247 THR B N   1 
ATOM   4226 C  CA  . THR B 1 200 ? -0.936  -11.390 44.633  1.00 19.36 ? 247 THR B CA  1 
ATOM   4227 C  C   . THR B 1 200 ? -1.419  -10.840 45.967  1.00 19.55 ? 247 THR B C   1 
ATOM   4228 O  O   . THR B 1 200 ? -2.165  -11.495 46.670  1.00 21.28 ? 247 THR B O   1 
ATOM   4229 C  CB  . THR B 1 200 ? 0.126   -12.462 44.853  1.00 23.11 ? 247 THR B CB  1 
ATOM   4230 O  OG1 . THR B 1 200 ? 1.278   -11.843 45.432  1.00 25.66 ? 247 THR B OG1 1 
ATOM   4231 C  CG2 . THR B 1 200 ? 0.542   -13.056 43.523  1.00 25.45 ? 247 THR B CG2 1 
ATOM   4232 N  N   . GLU B 1 201 ? -1.017  -9.618  46.325  1.00 16.74 ? 248 GLU B N   1 
ATOM   4233 C  CA  . GLU B 1 201 ? -1.262  -9.052  47.644  1.00 15.86 ? 248 GLU B CA  1 
ATOM   4234 C  C   . GLU B 1 201 ? -2.574  -8.277  47.654  1.00 17.64 ? 248 GLU B C   1 
ATOM   4235 O  O   . GLU B 1 201 ? -2.627  -7.047  47.604  1.00 15.56 ? 248 GLU B O   1 
ATOM   4236 C  CB  . GLU B 1 201 ? -0.057  -8.185  47.997  1.00 18.32 ? 248 GLU B CB  1 
ATOM   4237 C  CG  . GLU B 1 201 ? 1.253   -8.966  47.993  1.00 18.57 ? 248 GLU B CG  1 
ATOM   4238 C  CD  . GLU B 1 201 ? 2.308   -8.047  48.560  1.00 22.57 ? 248 GLU B CD  1 
ATOM   4239 O  OE1 . GLU B 1 201 ? 2.703   -7.126  47.884  1.00 20.25 ? 248 GLU B OE1 1 
ATOM   4240 O  OE2 . GLU B 1 201 ? 2.541   -8.095  49.768  1.00 32.11 ? 248 GLU B OE2 1 
ATOM   4241 N  N   . LYS B 1 202 ? -3.676  -9.026  47.715  1.00 17.30 ? 249 LYS B N   1 
ATOM   4242 C  CA  . LYS B 1 202 ? -4.981  -8.438  47.550  1.00 19.57 ? 249 LYS B CA  1 
ATOM   4243 C  C   . LYS B 1 202 ? -5.277  -7.377  48.602  1.00 17.66 ? 249 LYS B C   1 
ATOM   4244 O  O   . LYS B 1 202 ? -5.831  -6.339  48.268  1.00 17.95 ? 249 LYS B O   1 
ATOM   4245 C  CB  . LYS B 1 202 ? -6.064  -9.520  47.567  1.00 22.88 ? 249 LYS B CB  1 
ATOM   4246 C  CG  . LYS B 1 202 ? -6.232  -10.162 46.181  1.00 34.13 ? 249 LYS B CG  1 
ATOM   4247 C  CD  . LYS B 1 202 ? -7.679  -10.544 45.865  1.00 42.83 ? 249 LYS B CD  1 
ATOM   4248 C  CE  . LYS B 1 202 ? -7.861  -11.024 44.445  1.00 45.69 ? 249 LYS B CE  1 
ATOM   4249 N  NZ  . LYS B 1 202 ? -9.271  -11.337 44.167  1.00 45.03 ? 249 LYS B NZ  1 
ATOM   4250 N  N   . ASP B 1 203 ? -4.903  -7.576  49.875  1.00 17.64 ? 250 ASP B N   1 
ATOM   4251 C  CA  . ASP B 1 203 ? -5.192  -6.570  50.880  1.00 18.42 ? 250 ASP B CA  1 
ATOM   4252 C  C   . ASP B 1 203 ? -4.341  -5.319  50.662  1.00 16.57 ? 250 ASP B C   1 
ATOM   4253 O  O   . ASP B 1 203 ? -4.885  -4.239  50.802  1.00 17.43 ? 250 ASP B O   1 
ATOM   4254 C  CB  . ASP B 1 203 ? -4.974  -7.104  52.292  1.00 22.41 ? 250 ASP B CB  1 
ATOM   4255 C  CG  . ASP B 1 203 ? -5.510  -6.158  53.365  1.00 29.88 ? 250 ASP B CG  1 
ATOM   4256 O  OD1 . ASP B 1 203 ? -6.712  -5.766  53.271  1.00 36.22 ? 250 ASP B OD1 1 
ATOM   4257 O  OD2 . ASP B 1 203 ? -4.735  -5.776  54.264  1.00 34.11 ? 250 ASP B OD2 1 
ATOM   4258 N  N   . ARG B 1 204 ? -3.084  -5.489  50.285  1.00 16.00 ? 251 ARG B N   1 
ATOM   4259 C  CA  . ARG B 1 204 ? -2.199  -4.348  50.040  1.00 15.51 ? 251 ARG B CA  1 
ATOM   4260 C  C   . ARG B 1 204 ? -2.734  -3.553  48.856  1.00 15.70 ? 251 ARG B C   1 
ATOM   4261 O  O   . ARG B 1 204 ? -2.652  -2.328  48.827  1.00 15.08 ? 251 ARG B O   1 
ATOM   4262 C  CB  . ARG B 1 204 ? -0.728  -4.705  49.800  1.00 17.67 ? 251 ARG B CB  1 
ATOM   4263 C  CG  . ARG B 1 204 ? -0.034  -5.084  51.104  1.00 21.23 ? 251 ARG B CG  1 
ATOM   4264 C  CD  . ARG B 1 204 ? 1.402   -5.580  50.830  1.00 24.49 ? 251 ARG B CD  1 
ATOM   4265 N  NE  . ARG B 1 204 ? 2.276   -4.429  50.789  1.00 24.69 ? 251 ARG B NE  1 
ATOM   4266 C  CZ  . ARG B 1 204 ? 3.513   -4.276  50.324  1.00 23.36 ? 251 ARG B CZ  1 
ATOM   4267 N  NH1 . ARG B 1 204 ? 4.068   -5.062  49.428  1.00 20.71 ? 251 ARG B NH1 1 
ATOM   4268 N  NH2 . ARG B 1 204 ? 4.174   -3.226  50.762  1.00 26.74 ? 251 ARG B NH2 1 
ATOM   4269 N  N   . LEU B 1 205 ? -3.336  -4.216  47.881  1.00 14.08 ? 252 LEU B N   1 
ATOM   4270 C  CA  . LEU B 1 205 ? -3.908  -3.495  46.754  1.00 13.18 ? 252 LEU B CA  1 
ATOM   4271 C  C   . LEU B 1 205 ? -5.102  -2.678  47.183  1.00 14.29 ? 252 LEU B C   1 
ATOM   4272 O  O   . LEU B 1 205 ? -5.274  -1.541  46.762  1.00 13.22 ? 252 LEU B O   1 
ATOM   4273 C  CB  . LEU B 1 205 ? -4.280  -4.492  45.654  1.00 14.50 ? 252 LEU B CB  1 
ATOM   4274 C  CG  . LEU B 1 205 ? -3.112  -5.146  44.918  1.00 16.66 ? 252 LEU B CG  1 
ATOM   4275 C  CD1 . LEU B 1 205 ? -3.683  -6.310  44.114  1.00 20.17 ? 252 LEU B CD1 1 
ATOM   4276 C  CD2 . LEU B 1 205 ? -2.395  -4.153  44.007  1.00 17.70 ? 252 LEU B CD2 1 
ATOM   4277 N  N   . ASP B 1 206 ? -5.958  -3.259  48.016  1.00 14.75 ? 253 ASP B N   1 
ATOM   4278 C  CA  . ASP B 1 206 ? -7.094  -2.534  48.549  1.00 16.65 ? 253 ASP B CA  1 
ATOM   4279 C  C   . ASP B 1 206 ? -6.677  -1.334  49.392  1.00 17.38 ? 253 ASP B C   1 
ATOM   4280 O  O   . ASP B 1 206 ? -7.328  -0.288  49.353  1.00 19.10 ? 253 ASP B O   1 
ATOM   4281 C  CB  . ASP B 1 206 ? -7.979  -3.439  49.392  1.00 18.07 ? 253 ASP B CB  1 
ATOM   4282 C  CG  . ASP B 1 206 ? -8.839  -4.396  48.587  1.00 24.57 ? 253 ASP B CG  1 
ATOM   4283 O  OD1 . ASP B 1 206 ? -8.955  -4.192  47.388  1.00 25.00 ? 253 ASP B OD1 1 
ATOM   4284 O  OD2 . ASP B 1 206 ? -9.373  -5.357  49.183  1.00 26.31 ? 253 ASP B OD2 1 
ATOM   4285 N  N   . ARG B 1 207 ? -5.567  -1.468  50.124  1.00 14.82 ? 254 ARG B N   1 
ATOM   4286 C  CA  . ARG B 1 207 ? -5.155  -0.392  51.002  1.00 17.39 ? 254 ARG B CA  1 
ATOM   4287 C  C   . ARG B 1 207 ? -4.479  0.742   50.217  1.00 16.64 ? 254 ARG B C   1 
ATOM   4288 O  O   . ARG B 1 207 ? -4.681  1.925   50.512  1.00 17.51 ? 254 ARG B O   1 
ATOM   4289 C  CB  . ARG B 1 207 ? -4.215  -0.995  52.047  1.00 23.03 ? 254 ARG B CB  1 
ATOM   4290 C  CG  . ARG B 1 207 ? -3.495  0.009   52.932  1.00 32.26 ? 254 ARG B CG  1 
ATOM   4291 C  CD  . ARG B 1 207 ? -2.802  -0.703  54.108  1.00 40.47 ? 254 ARG B CD  1 
ATOM   4292 N  NE  . ARG B 1 207 ? -3.742  -0.962  55.210  1.00 51.85 ? 254 ARG B NE  1 
ATOM   4293 C  CZ  . ARG B 1 207 ? -4.244  -2.142  55.560  1.00 54.31 ? 254 ARG B CZ  1 
ATOM   4294 N  NH1 . ARG B 1 207 ? -5.133  -2.211  56.535  1.00 52.85 ? 254 ARG B NH1 1 
ATOM   4295 N  NH2 . ARG B 1 207 ? -3.885  -3.241  54.916  1.00 56.11 ? 254 ARG B NH2 1 
ATOM   4296 N  N   . PHE B 1 208 ? -3.685  0.396   49.205  1.00 14.28 ? 255 PHE B N   1 
ATOM   4297 C  CA  . PHE B 1 208 ? -2.740  1.347   48.640  1.00 13.68 ? 255 PHE B CA  1 
ATOM   4298 C  C   . PHE B 1 208 ? -2.961  1.635   47.164  1.00 13.26 ? 255 PHE B C   1 
ATOM   4299 O  O   . PHE B 1 208 ? -2.423  2.651   46.695  1.00 13.78 ? 255 PHE B O   1 
ATOM   4300 C  CB  . PHE B 1 208 ? -1.310  0.868   48.726  1.00 14.38 ? 255 PHE B CB  1 
ATOM   4301 C  CG  . PHE B 1 208 ? -0.837  0.756   50.164  1.00 14.19 ? 255 PHE B CG  1 
ATOM   4302 C  CD1 . PHE B 1 208 ? -0.730  1.905   50.918  1.00 15.54 ? 255 PHE B CD1 1 
ATOM   4303 C  CD2 . PHE B 1 208 ? -0.416  -0.448  50.690  1.00 17.10 ? 255 PHE B CD2 1 
ATOM   4304 C  CE1 . PHE B 1 208 ? -0.247  1.817   52.219  1.00 16.98 ? 255 PHE B CE1 1 
ATOM   4305 C  CE2 . PHE B 1 208 ? 0.068   -0.519  51.986  1.00 17.59 ? 255 PHE B CE2 1 
ATOM   4306 C  CZ  . PHE B 1 208 ? 0.143   0.622   52.730  1.00 18.14 ? 255 PHE B CZ  1 
ATOM   4307 N  N   . VAL B 1 209 ? -3.808  0.860   46.470  1.00 12.62 ? 256 VAL B N   1 
ATOM   4308 C  CA  . VAL B 1 209 ? -3.907  1.012   45.024  1.00 12.43 ? 256 VAL B CA  1 
ATOM   4309 C  C   . VAL B 1 209 ? -5.305  1.334   44.548  1.00 12.86 ? 256 VAL B C   1 
ATOM   4310 O  O   . VAL B 1 209 ? -5.460  2.247   43.750  1.00 13.39 ? 256 VAL B O   1 
ATOM   4311 C  CB  . VAL B 1 209 ? -3.362  -0.267  44.362  1.00 13.27 ? 256 VAL B CB  1 
ATOM   4312 C  CG1 . VAL B 1 209 ? -3.525  -0.234  42.857  1.00 14.68 ? 256 VAL B CG1 1 
ATOM   4313 C  CG2 . VAL B 1 209 ? -1.899  -0.460  44.669  1.00 16.28 ? 256 VAL B CG2 1 
ATOM   4314 N  N   . TRP B 1 210 ? -6.321  0.606   44.968  1.00 13.07 ? 257 TRP B N   1 
ATOM   4315 C  CA  . TRP B 1 210 ? -7.652  0.797   44.408  1.00 13.59 ? 257 TRP B CA  1 
ATOM   4316 C  C   . TRP B 1 210 ? -8.398  1.903   45.149  1.00 13.74 ? 257 TRP B C   1 
ATOM   4317 O  O   . TRP B 1 210 ? -8.425  1.944   46.388  1.00 15.84 ? 257 TRP B O   1 
ATOM   4318 C  CB  . TRP B 1 210 ? -8.520  -0.472  44.511  1.00 13.70 ? 257 TRP B CB  1 
ATOM   4319 C  CG  . TRP B 1 210 ? -7.898  -1.705  43.908  1.00 14.22 ? 257 TRP B CG  1 
ATOM   4320 C  CD1 . TRP B 1 210 ? -7.730  -2.908  44.528  1.00 15.74 ? 257 TRP B CD1 1 
ATOM   4321 C  CD2 . TRP B 1 210 ? -7.450  -1.878  42.549  1.00 13.74 ? 257 TRP B CD2 1 
ATOM   4322 N  NE1 . TRP B 1 210 ? -7.170  -3.795  43.659  1.00 17.25 ? 257 TRP B NE1 1 
ATOM   4323 C  CE2 . TRP B 1 210 ? -6.995  -3.210  42.433  1.00 15.00 ? 257 TRP B CE2 1 
ATOM   4324 C  CE3 . TRP B 1 210 ? -7.423  -1.049  41.421  1.00 15.37 ? 257 TRP B CE3 1 
ATOM   4325 C  CZ2 . TRP B 1 210 ? -6.501  -3.714  41.235  1.00 15.59 ? 257 TRP B CZ2 1 
ATOM   4326 C  CZ3 . TRP B 1 210 ? -6.902  -1.559  40.250  1.00 15.99 ? 257 TRP B CZ3 1 
ATOM   4327 C  CH2 . TRP B 1 210 ? -6.456  -2.864  40.159  1.00 15.91 ? 257 TRP B CH2 1 
ATOM   4328 N  N   . ALA B 1 211 ? -9.072  2.746   44.396  1.00 14.26 ? 258 ALA B N   1 
ATOM   4329 C  CA  . ALA B 1 211 ? -9.990  3.723   44.962  1.00 14.69 ? 258 ALA B CA  1 
ATOM   4330 C  C   . ALA B 1 211 ? -11.215 3.010   45.534  1.00 15.54 ? 258 ALA B C   1 
ATOM   4331 O  O   . ALA B 1 211 ? -11.777 2.098   44.933  1.00 17.19 ? 258 ALA B O   1 
ATOM   4332 C  CB  . ALA B 1 211 ? -10.386 4.676   43.853  1.00 16.10 ? 258 ALA B CB  1 
ATOM   4333 N  N   . ALA B 1 212 ? -11.607 3.462   46.736  1.00 18.41 ? 259 ALA B N   1 
ATOM   4334 C  CA  . ALA B 1 212 ? -12.770 2.962   47.451  1.00 19.21 ? 259 ALA B CA  1 
ATOM   4335 C  C   . ALA B 1 212 ? -13.909 3.983   47.338  1.00 20.40 ? 259 ALA B C   1 
ATOM   4336 O  O   . ALA B 1 212 ? -13.685 5.167   47.182  1.00 20.81 ? 259 ALA B O   1 
ATOM   4337 C  CB  . ALA B 1 212 ? -12.379 2.716   48.889  1.00 21.42 ? 259 ALA B CB  1 
ATOM   4338 N  N   . GLU B 1 213 ? -15.154 3.517   47.486  1.00 25.27 ? 260 GLU B N   1 
ATOM   4339 C  CA  . GLU B 1 213 ? -16.295 4.416   47.369  1.00 28.89 ? 260 GLU B CA  1 
ATOM   4340 C  C   . GLU B 1 213 ? -16.260 5.511   48.437  1.00 26.32 ? 260 GLU B C   1 
ATOM   4341 O  O   . GLU B 1 213 ? -16.608 6.657   48.175  1.00 28.81 ? 260 GLU B O   1 
ATOM   4342 C  CB  . GLU B 1 213 ? -17.597 3.634   47.506  1.00 34.48 ? 260 GLU B CB  1 
ATOM   4343 C  CG  . GLU B 1 213 ? -18.816 4.546   47.416  1.00 38.81 ? 260 GLU B CG  1 
ATOM   4344 C  CD  . GLU B 1 213 ? -20.066 3.743   47.089  1.00 47.62 ? 260 GLU B CD  1 
ATOM   4345 O  OE1 . GLU B 1 213 ? -21.027 3.741   47.882  1.00 59.62 ? 260 GLU B OE1 1 
ATOM   4346 O  OE2 . GLU B 1 213 ? -20.041 3.085   46.033  1.00 59.19 ? 260 GLU B OE2 1 
ATOM   4347 N  N   . LYS B 1 214 ? -15.785 5.170   49.635  1.00 24.10 ? 261 LYS B N   1 
ATOM   4348 C  CA  . LYS B 1 214 ? -15.769 6.140   50.719  1.00 29.23 ? 261 LYS B CA  1 
ATOM   4349 C  C   . LYS B 1 214 ? -14.663 7.176   50.542  1.00 25.03 ? 261 LYS B C   1 
ATOM   4350 O  O   . LYS B 1 214 ? -14.558 8.132   51.288  1.00 24.76 ? 261 LYS B O   1 
ATOM   4351 C  CB  . LYS B 1 214 ? -15.583 5.448   52.067  1.00 31.25 ? 261 LYS B CB  1 
ATOM   4352 C  CG  . LYS B 1 214 ? -14.211 4.844   52.252  1.00 36.31 ? 261 LYS B CG  1 
ATOM   4353 C  CD  . LYS B 1 214 ? -13.807 4.527   53.691  1.00 45.42 ? 261 LYS B CD  1 
ATOM   4354 C  CE  . LYS B 1 214 ? -12.481 3.814   53.734  1.00 52.48 ? 261 LYS B CE  1 
ATOM   4355 N  NZ  . LYS B 1 214 ? -11.831 3.940   55.044  1.00 56.02 ? 261 LYS B NZ  1 
ATOM   4356 N  N   . ASP B 1 215 ? -13.811 7.032   49.523  1.00 20.48 ? 262 ASP B N   1 
ATOM   4357 C  CA  . ASP B 1 215 ? -12.777 8.030   49.346  1.00 18.93 ? 262 ASP B CA  1 
ATOM   4358 C  C   . ASP B 1 215 ? -13.304 9.336   48.766  1.00 21.32 ? 262 ASP B C   1 
ATOM   4359 O  O   . ASP B 1 215 ? -12.581 10.328  48.792  1.00 26.39 ? 262 ASP B O   1 
ATOM   4360 C  CB  . ASP B 1 215 ? -11.678 7.510   48.426  1.00 19.17 ? 262 ASP B CB  1 
ATOM   4361 C  CG  . ASP B 1 215 ? -10.934 6.300   48.942  1.00 20.69 ? 262 ASP B CG  1 
ATOM   4362 O  OD1 . ASP B 1 215 ? -11.074 5.983   50.159  1.00 22.32 ? 262 ASP B OD1 1 
ATOM   4363 O  OD2 . ASP B 1 215 ? -10.177 5.678   48.140  1.00 17.65 ? 262 ASP B OD2 1 
ATOM   4364 N  N   . GLY B 1 216 ? -14.500 9.354   48.177  1.00 20.38 ? 263 GLY B N   1 
ATOM   4365 C  CA  . GLY B 1 216 ? -15.014 10.670  47.837  1.00 23.46 ? 263 GLY B CA  1 
ATOM   4366 C  C   . GLY B 1 216 ? -15.563 10.788  46.429  1.00 25.04 ? 263 GLY B C   1 
ATOM   4367 O  O   . GLY B 1 216 ? -16.318 11.712  46.149  1.00 25.72 ? 263 GLY B O   1 
ATOM   4368 N  N   . THR B 1 217 ? -15.174 9.878   45.529  1.00 20.65 ? 264 THR B N   1 
ATOM   4369 C  CA  . THR B 1 217 ? -15.587 9.980   44.143  1.00 20.19 ? 264 THR B CA  1 
ATOM   4370 C  C   . THR B 1 217 ? -16.181 8.657   43.718  1.00 19.21 ? 264 THR B C   1 
ATOM   4371 O  O   . THR B 1 217 ? -15.463 7.730   43.349  1.00 18.84 ? 264 THR B O   1 
ATOM   4372 C  CB  . THR B 1 217 ? -14.388 10.286  43.263  1.00 20.46 ? 264 THR B CB  1 
ATOM   4373 O  OG1 . THR B 1 217 ? -13.784 11.452  43.802  1.00 21.50 ? 264 THR B OG1 1 
ATOM   4374 C  CG2 . THR B 1 217 ? -14.826 10.554  41.834  1.00 22.61 ? 264 THR B CG2 1 
ATOM   4375 N  N   . PRO B 1 218 ? -17.500 8.485   43.811  1.00 19.63 ? 265 PRO B N   1 
ATOM   4376 C  CA  . PRO B 1 218 ? -18.092 7.180   43.576  1.00 19.93 ? 265 PRO B CA  1 
ATOM   4377 C  C   . PRO B 1 218 ? -17.801 6.574   42.209  1.00 18.30 ? 265 PRO B C   1 
ATOM   4378 O  O   . PRO B 1 218 ? -17.639 5.350   42.105  1.00 17.98 ? 265 PRO B O   1 
ATOM   4379 C  CB  . PRO B 1 218 ? -19.596 7.380   43.806  1.00 22.16 ? 265 PRO B CB  1 
ATOM   4380 C  CG  . PRO B 1 218 ? -19.653 8.572   44.736  1.00 23.16 ? 265 PRO B CG  1 
ATOM   4381 C  CD  . PRO B 1 218 ? -18.438 9.443   44.436  1.00 22.17 ? 265 PRO B CD  1 
ATOM   4382 N  N   . TRP B 1 219 ? -17.672 7.391   41.164  1.00 18.38 ? 266 TRP B N   1 
ATOM   4383 C  CA  . TRP B 1 219 ? -17.520 6.805   39.845  1.00 16.09 ? 266 TRP B CA  1 
ATOM   4384 C  C   . TRP B 1 219 ? -16.173 6.096   39.738  1.00 14.06 ? 266 TRP B C   1 
ATOM   4385 O  O   . TRP B 1 219 ? -15.967 5.297   38.841  1.00 15.13 ? 266 TRP B O   1 
ATOM   4386 C  CB  . TRP B 1 219 ? -17.714 7.831   38.723  1.00 15.64 ? 266 TRP B CB  1 
ATOM   4387 C  CG  . TRP B 1 219 ? -16.679 8.915   38.567  1.00 15.44 ? 266 TRP B CG  1 
ATOM   4388 C  CD1 . TRP B 1 219 ? -16.715 10.199  39.054  1.00 15.89 ? 266 TRP B CD1 1 
ATOM   4389 C  CD2 . TRP B 1 219 ? -15.453 8.816   37.836  1.00 14.32 ? 266 TRP B CD2 1 
ATOM   4390 N  NE1 . TRP B 1 219 ? -15.585 10.884  38.702  1.00 16.45 ? 266 TRP B NE1 1 
ATOM   4391 C  CE2 . TRP B 1 219 ? -14.794 10.071  37.919  1.00 14.71 ? 266 TRP B CE2 1 
ATOM   4392 C  CE3 . TRP B 1 219 ? -14.863 7.812   37.057  1.00 14.30 ? 266 TRP B CE3 1 
ATOM   4393 C  CZ2 . TRP B 1 219 ? -13.576 10.323  37.308  1.00 15.66 ? 266 TRP B CZ2 1 
ATOM   4394 C  CZ3 . TRP B 1 219 ? -13.667 8.082   36.451  1.00 17.45 ? 266 TRP B CZ3 1 
ATOM   4395 C  CH2 . TRP B 1 219 ? -13.012 9.307   36.586  1.00 16.32 ? 266 TRP B CH2 1 
ATOM   4396 N  N   . MET B 1 220 ? -15.212 6.450   40.602  1.00 13.73 ? 267 MET B N   1 
ATOM   4397 C  CA  . MET B 1 220 ? -13.862 5.904   40.539  1.00 13.27 ? 267 MET B CA  1 
ATOM   4398 C  C   . MET B 1 220 ? -13.679 4.640   41.384  1.00 14.56 ? 267 MET B C   1 
ATOM   4399 O  O   . MET B 1 220 ? -12.585 4.113   41.409  1.00 14.41 ? 267 MET B O   1 
ATOM   4400 C  CB  . MET B 1 220 ? -12.829 6.944   40.976  1.00 13.07 ? 267 MET B CB  1 
ATOM   4401 C  CG  . MET B 1 220 ? -12.312 7.806   39.891  1.00 13.73 ? 267 MET B CG  1 
ATOM   4402 S  SD  . MET B 1 220 ? -11.372 6.862   38.687  1.00 14.64 ? 267 MET B SD  1 
ATOM   4403 C  CE  . MET B 1 220 ? -9.951  6.374   39.662  1.00 15.34 ? 267 MET B CE  1 
ATOM   4404 N  N   . THR B 1 221 ? -14.720 4.143   42.077  1.00 15.25 ? 268 THR B N   1 
ATOM   4405 C  CA  . THR B 1 221 ? -14.587 2.963   42.915  1.00 15.62 ? 268 THR B CA  1 
ATOM   4406 C  C   . THR B 1 221 ? -14.060 1.786   42.085  1.00 13.70 ? 268 THR B C   1 
ATOM   4407 O  O   . THR B 1 221 ? -14.670 1.387   41.088  1.00 15.95 ? 268 THR B O   1 
ATOM   4408 C  CB  . THR B 1 221 ? -15.939 2.580   43.525  1.00 17.22 ? 268 THR B CB  1 
ATOM   4409 O  OG1 . THR B 1 221 ? -16.424 3.708   44.254  1.00 19.36 ? 268 THR B OG1 1 
ATOM   4410 C  CG2 . THR B 1 221 ? -15.800 1.378   44.438  1.00 17.65 ? 268 THR B CG2 1 
ATOM   4411 N  N   . GLY B 1 222 ? -12.943 1.227   42.503  1.00 13.43 ? 269 GLY B N   1 
ATOM   4412 C  CA  . GLY B 1 222 ? -12.347 0.126   41.786  1.00 13.55 ? 269 GLY B CA  1 
ATOM   4413 C  C   . GLY B 1 222 ? -11.330 0.568   40.746  1.00 13.33 ? 269 GLY B C   1 
ATOM   4414 O  O   . GLY B 1 222 ? -10.672 -0.277  40.140  1.00 14.21 ? 269 GLY B O   1 
ATOM   4415 N  N   . GLY B 1 223 ? -11.222 1.862   40.542  1.00 11.94 ? 270 GLY B N   1 
ATOM   4416 C  CA  . GLY B 1 223 ? -10.194 2.453   39.706  1.00 11.87 ? 270 GLY B CA  1 
ATOM   4417 C  C   . GLY B 1 223 ? -8.921  2.681   40.494  1.00 11.25 ? 270 GLY B C   1 
ATOM   4418 O  O   . GLY B 1 223 ? -8.776  2.234   41.630  1.00 12.99 ? 270 GLY B O   1 
ATOM   4419 N  N   . SER B 1 224 ? -7.995  3.426   39.902  1.00 11.22 ? 271 SER B N   1 
ATOM   4420 C  CA  . SER B 1 224 ? -6.753  3.776   40.555  1.00 10.66 ? 271 SER B CA  1 
ATOM   4421 C  C   . SER B 1 224 ? -6.271  5.075   39.922  1.00 11.17 ? 271 SER B C   1 
ATOM   4422 O  O   . SER B 1 224 ? -6.867  5.544   38.978  1.00 12.94 ? 271 SER B O   1 
ATOM   4423 C  CB  . SER B 1 224 ? -5.750  2.682   40.431  1.00 11.35 ? 271 SER B CB  1 
ATOM   4424 O  OG  . SER B 1 224 ? -4.568  2.881   41.206  1.00 12.69 ? 271 SER B OG  1 
ATOM   4425 N  N   . TYR B 1 225 ? -5.197  5.622   40.451  1.00 10.65 ? 272 TYR B N   1 
ATOM   4426 C  CA  . TYR B 1 225 ? -4.590  6.831   39.954  1.00 10.48 ? 272 TYR B CA  1 
ATOM   4427 C  C   . TYR B 1 225 ? -3.181  6.515   39.519  1.00 10.57 ? 272 TYR B C   1 
ATOM   4428 O  O   . TYR B 1 225 ? -2.413  5.819   40.218  1.00 12.51 ? 272 TYR B O   1 
ATOM   4429 C  CB  . TYR B 1 225 ? -4.585  7.980   40.975  1.00 10.78 ? 272 TYR B CB  1 
ATOM   4430 C  CG  . TYR B 1 225 ? -6.005  8.315   41.361  1.00 10.71 ? 272 TYR B CG  1 
ATOM   4431 C  CD1 . TYR B 1 225 ? -6.763  9.217   40.618  1.00 12.29 ? 272 TYR B CD1 1 
ATOM   4432 C  CD2 . TYR B 1 225 ? -6.638  7.664   42.401  1.00 12.27 ? 272 TYR B CD2 1 
ATOM   4433 C  CE1 . TYR B 1 225 ? -8.082  9.465   40.920  1.00 12.12 ? 272 TYR B CE1 1 
ATOM   4434 C  CE2 . TYR B 1 225 ? -7.980  7.879   42.681  1.00 12.83 ? 272 TYR B CE2 1 
ATOM   4435 C  CZ  . TYR B 1 225 ? -8.690  8.806   41.959  1.00 13.19 ? 272 TYR B CZ  1 
ATOM   4436 O  OH  . TYR B 1 225 ? -10.015 9.056   42.255  1.00 15.10 ? 272 TYR B OH  1 
ATOM   4437 N  N   . LEU B 1 226 ? -2.819  7.061   38.350  1.00 10.21 ? 273 LEU B N   1 
ATOM   4438 C  CA  . LEU B 1 226 ? -1.559  6.750   37.673  1.00 10.11 ? 273 LEU B CA  1 
ATOM   4439 C  C   . LEU B 1 226 ? -0.734  8.022   37.578  1.00 11.04 ? 273 LEU B C   1 
ATOM   4440 O  O   . LEU B 1 226 ? -1.220  9.069   37.144  1.00 11.98 ? 273 LEU B O   1 
ATOM   4441 C  CB  . LEU B 1 226 ? -1.870  6.211   36.287  1.00 11.26 ? 273 LEU B CB  1 
ATOM   4442 C  CG  . LEU B 1 226 ? -0.663  5.975   35.396  1.00 12.67 ? 273 LEU B CG  1 
ATOM   4443 C  CD1 . LEU B 1 226 ? 0.320   4.986   35.984  1.00 13.92 ? 273 LEU B CD1 1 
ATOM   4444 C  CD2 . LEU B 1 226 ? -1.214  5.494   34.047  1.00 14.65 ? 273 LEU B CD2 1 
ATOM   4445 N  N   . VAL B 1 227 ? 0.535   7.909   37.955  1.00 10.75 ? 274 VAL B N   1 
ATOM   4446 C  CA  . VAL B 1 227 ? 1.516   8.940   37.691  1.00 11.23 ? 274 VAL B CA  1 
ATOM   4447 C  C   . VAL B 1 227 ? 2.503   8.336   36.706  1.00 11.51 ? 274 VAL B C   1 
ATOM   4448 O  O   . VAL B 1 227 ? 3.041   7.257   36.938  1.00 12.26 ? 274 VAL B O   1 
ATOM   4449 C  CB  . VAL B 1 227 ? 2.224   9.409   38.970  1.00 11.96 ? 274 VAL B CB  1 
ATOM   4450 C  CG1 . VAL B 1 227 ? 3.420   10.293  38.618  1.00 14.50 ? 274 VAL B CG1 1 
ATOM   4451 C  CG2 . VAL B 1 227 ? 1.268   10.078  39.914  1.00 12.93 ? 274 VAL B CG2 1 
ATOM   4452 N  N   . ALA B 1 228 ? 2.776   9.069   35.630  1.00 10.08 ? 275 ALA B N   1 
ATOM   4453 C  CA  . ALA B 1 228 ? 3.771   8.680   34.650  1.00 11.07 ? 275 ALA B CA  1 
ATOM   4454 C  C   . ALA B 1 228 ? 4.878   9.721   34.667  1.00 10.73 ? 275 ALA B C   1 
ATOM   4455 O  O   . ALA B 1 228 ? 4.577   10.927  34.625  1.00 12.85 ? 275 ALA B O   1 
ATOM   4456 C  CB  . ALA B 1 228 ? 3.176   8.632   33.278  1.00 12.41 ? 275 ALA B CB  1 
ATOM   4457 N  N   . ARG B 1 229 ? 6.122   9.266   34.774  1.00 10.13 ? 276 ARG B N   1 
ATOM   4458 C  CA  . ARG B 1 229 ? 7.268   10.177  34.709  1.00 11.10 ? 276 ARG B CA  1 
ATOM   4459 C  C   . ARG B 1 229 ? 8.285   9.580   33.761  1.00 11.40 ? 276 ARG B C   1 
ATOM   4460 O  O   . ARG B 1 229 ? 8.735   8.462   33.930  1.00 12.86 ? 276 ARG B O   1 
ATOM   4461 C  CB  . ARG B 1 229 ? 7.976   10.432  36.025  1.00 12.13 ? 276 ARG B CB  1 
ATOM   4462 C  CG  . ARG B 1 229 ? 7.040   10.903  37.128  1.00 12.50 ? 276 ARG B CG  1 
ATOM   4463 C  CD  . ARG B 1 229 ? 6.659   12.360  37.022  1.00 13.32 ? 276 ARG B CD  1 
ATOM   4464 N  NE  . ARG B 1 229 ? 7.797   13.195  37.452  1.00 12.98 ? 276 ARG B NE  1 
ATOM   4465 C  CZ  . ARG B 1 229 ? 7.697   14.480  37.809  1.00 13.66 ? 276 ARG B CZ  1 
ATOM   4466 N  NH1 . ARG B 1 229 ? 6.578   15.138  37.743  1.00 14.33 ? 276 ARG B NH1 1 
ATOM   4467 N  NH2 . ARG B 1 229 ? 8.764   15.055  38.297  1.00 14.49 ? 276 ARG B NH2 1 
ATOM   4468 N  N   . ARG B 1 230 ? 8.637   10.352  32.751  1.00 11.72 ? 277 ARG B N   1 
ATOM   4469 C  CA  . ARG B 1 230 ? 9.706   9.953   31.872  1.00 11.10 ? 277 ARG B CA  1 
ATOM   4470 C  C   . ARG B 1 230 ? 11.029  10.429  32.476  1.00 11.32 ? 277 ARG B C   1 
ATOM   4471 O  O   . ARG B 1 230 ? 11.188  11.614  32.572  1.00 13.23 ? 277 ARG B O   1 
ATOM   4472 C  CB  . ARG B 1 230 ? 9.515   10.539  30.468  1.00 13.58 ? 277 ARG B CB  1 
ATOM   4473 C  CG  . ARG B 1 230 ? 10.489  9.933   29.477  1.00 15.28 ? 277 ARG B CG  1 
ATOM   4474 C  CD  . ARG B 1 230 ? 10.261  10.555  28.087  1.00 19.82 ? 277 ARG B CD  1 
ATOM   4475 N  NE  . ARG B 1 230 ? 11.057  9.862   27.067  1.00 20.04 ? 277 ARG B NE  1 
ATOM   4476 C  CZ  . ARG B 1 230 ? 12.213  10.297  26.616  1.00 23.97 ? 277 ARG B CZ  1 
ATOM   4477 N  NH1 . ARG B 1 230 ? 12.687  11.435  27.087  1.00 24.85 ? 277 ARG B NH1 1 
ATOM   4478 N  NH2 . ARG B 1 230 ? 12.896  9.614   25.708  1.00 21.59 ? 277 ARG B NH2 1 
ATOM   4479 N  N   . ILE B 1 231 ? 11.879  9.482   32.890  1.00 11.36 ? 278 ILE B N   1 
ATOM   4480 C  CA  . ILE B 1 231 ? 13.071  9.858   33.646  1.00 11.52 ? 278 ILE B CA  1 
ATOM   4481 C  C   . ILE B 1 231 ? 14.276  9.458   32.847  1.00 13.04 ? 278 ILE B C   1 
ATOM   4482 O  O   . ILE B 1 231 ? 14.591  8.268   32.721  1.00 15.42 ? 278 ILE B O   1 
ATOM   4483 C  CB  . ILE B 1 231 ? 13.091  9.204   35.032  1.00 11.62 ? 278 ILE B CB  1 
ATOM   4484 C  CG1 . ILE B 1 231 ? 11.804  9.439   35.763  1.00 12.53 ? 278 ILE B CG1 1 
ATOM   4485 C  CG2 . ILE B 1 231 ? 14.319  9.685   35.793  1.00 13.87 ? 278 ILE B CG2 1 
ATOM   4486 C  CD1 . ILE B 1 231 ? 11.670  8.728   37.091  1.00 13.56 ? 278 ILE B CD1 1 
ATOM   4487 N  N   . ARG B 1 232 ? 14.973  10.446  32.317  1.00 12.93 ? 279 ARG B N   1 
ATOM   4488 C  CA  . ARG B 1 232 ? 16.218  10.192  31.602  1.00 14.77 ? 279 ARG B CA  1 
ATOM   4489 C  C   . ARG B 1 232 ? 17.315  9.863   32.593  1.00 15.02 ? 279 ARG B C   1 
ATOM   4490 O  O   . ARG B 1 232 ? 17.391  10.454  33.654  1.00 15.16 ? 279 ARG B O   1 
ATOM   4491 C  CB  . ARG B 1 232 ? 16.585  11.459  30.824  1.00 17.96 ? 279 ARG B CB  1 
ATOM   4492 C  CG  . ARG B 1 232 ? 17.920  11.546  30.104  1.00 25.03 ? 279 ARG B CG  1 
ATOM   4493 C  CD  . ARG B 1 232 ? 18.066  10.488  29.062  1.00 28.87 ? 279 ARG B CD  1 
ATOM   4494 N  NE  . ARG B 1 232 ? 19.439  10.519  28.537  1.00 29.04 ? 279 ARG B NE  1 
ATOM   4495 C  CZ  . ARG B 1 232 ? 19.887  11.482  27.716  1.00 36.25 ? 279 ARG B CZ  1 
ATOM   4496 N  NH1 . ARG B 1 232 ? 19.045  12.253  27.049  1.00 30.81 ? 279 ARG B NH1 1 
ATOM   4497 N  NH2 . ARG B 1 232 ? 21.188  11.619  27.503  1.00 39.80 ? 279 ARG B NH2 1 
ATOM   4498 N  N   . MET B 1 233 ? 18.160  8.908   32.256  1.00 13.15 ? 280 MET B N   1 
ATOM   4499 C  CA  . MET B 1 233 ? 19.366  8.621   32.994  1.00 13.87 ? 280 MET B CA  1 
ATOM   4500 C  C   . MET B 1 233 ? 20.533  9.240   32.256  1.00 12.83 ? 280 MET B C   1 
ATOM   4501 O  O   . MET B 1 233 ? 20.649  9.171   31.024  1.00 14.93 ? 280 MET B O   1 
ATOM   4502 C  CB  . MET B 1 233 ? 19.582  7.113   33.108  1.00 13.97 ? 280 MET B CB  1 
ATOM   4503 C  CG  . MET B 1 233 ? 18.578  6.424   34.001  1.00 14.75 ? 280 MET B CG  1 
ATOM   4504 S  SD  . MET B 1 233 ? 18.573  4.659   33.619  1.00 15.42 ? 280 MET B SD  1 
ATOM   4505 C  CE  . MET B 1 233 ? 17.343  4.095   34.791  1.00 16.88 ? 280 MET B CE  1 
ATOM   4506 N  N   . HIS B 1 234 ? 21.473  9.774   33.047  1.00 13.69 ? 281 HIS B N   1 
ATOM   4507 C  CA  . HIS B 1 234 ? 22.716  10.254  32.480  1.00 14.24 ? 281 HIS B CA  1 
ATOM   4508 C  C   . HIS B 1 234 ? 23.710  9.099   32.462  1.00 13.51 ? 281 HIS B C   1 
ATOM   4509 O  O   . HIS B 1 234 ? 24.516  8.942   33.372  1.00 15.39 ? 281 HIS B O   1 
ATOM   4510 C  CB  . HIS B 1 234 ? 23.239  11.393  33.347  1.00 16.06 ? 281 HIS B CB  1 
ATOM   4511 C  CG  . HIS B 1 234 ? 22.329  12.558  33.434  1.00 18.49 ? 281 HIS B CG  1 
ATOM   4512 N  ND1 . HIS B 1 234 ? 21.733  13.126  32.332  1.00 24.49 ? 281 HIS B ND1 1 
ATOM   4513 C  CD2 . HIS B 1 234 ? 21.922  13.261  34.498  1.00 22.84 ? 281 HIS B CD2 1 
ATOM   4514 C  CE1 . HIS B 1 234 ? 20.961  14.151  32.763  1.00 23.06 ? 281 HIS B CE1 1 
ATOM   4515 N  NE2 . HIS B 1 234 ? 21.096  14.259  34.055  1.00 24.36 ? 281 HIS B NE2 1 
ATOM   4516 N  N   . ILE B 1 235 ? 23.549  8.240   31.468  1.00 13.65 ? 282 ILE B N   1 
ATOM   4517 C  CA  . ILE B 1 235 ? 24.183  6.936   31.397  1.00 14.31 ? 282 ILE B CA  1 
ATOM   4518 C  C   . ILE B 1 235 ? 25.692  7.087   31.470  1.00 14.77 ? 282 ILE B C   1 
ATOM   4519 O  O   . ILE B 1 235 ? 26.348  6.368   32.198  1.00 15.87 ? 282 ILE B O   1 
ATOM   4520 C  CB  . ILE B 1 235 ? 23.734  6.226   30.098  1.00 16.14 ? 282 ILE B CB  1 
ATOM   4521 C  CG1 . ILE B 1 235 ? 22.257  5.871   30.086  1.00 19.07 ? 282 ILE B CG1 1 
ATOM   4522 C  CG2 . ILE B 1 235 ? 24.590  5.005   29.799  1.00 18.02 ? 282 ILE B CG2 1 
ATOM   4523 C  CD1 . ILE B 1 235 ? 21.824  4.862   31.112  1.00 19.46 ? 282 ILE B CD1 1 
ATOM   4524 N  N   . GLU B 1 236 ? 26.239  8.022   30.711  1.00 15.11 ? 283 GLU B N   1 
ATOM   4525 C  CA  . GLU B 1 236 ? 27.689  8.064   30.520  1.00 17.26 ? 283 GLU B CA  1 
ATOM   4526 C  C   . GLU B 1 236 ? 28.343  8.616   31.779  1.00 18.48 ? 283 GLU B C   1 
ATOM   4527 O  O   . GLU B 1 236 ? 29.463  8.216   32.102  1.00 20.65 ? 283 GLU B O   1 
ATOM   4528 C  CB  . GLU B 1 236 ? 28.025  8.902   29.299  1.00 17.72 ? 283 GLU B CB  1 
ATOM   4529 C  CG  . GLU B 1 236 ? 27.562  8.289   27.980  1.00 19.09 ? 283 GLU B CG  1 
ATOM   4530 C  CD  . GLU B 1 236 ? 26.108  8.597   27.642  1.00 20.34 ? 283 GLU B CD  1 
ATOM   4531 O  OE1 . GLU B 1 236 ? 25.464  9.422   28.366  1.00 20.30 ? 283 GLU B OE1 1 
ATOM   4532 O  OE2 . GLU B 1 236 ? 25.671  7.938   26.678  1.00 21.39 ? 283 GLU B OE2 1 
ATOM   4533 N  N   . THR B 1 237 ? 27.630  9.456   32.540  1.00 17.58 ? 284 THR B N   1 
ATOM   4534 C  CA  . THR B 1 237 ? 28.120  9.930   33.824  1.00 17.92 ? 284 THR B CA  1 
ATOM   4535 C  C   . THR B 1 237 ? 28.092  8.799   34.858  1.00 16.70 ? 284 THR B C   1 
ATOM   4536 O  O   . THR B 1 237 ? 29.005  8.574   35.658  1.00 16.70 ? 284 THR B O   1 
ATOM   4537 C  CB  . THR B 1 237 ? 27.243  11.104  34.267  1.00 21.83 ? 284 THR B CB  1 
ATOM   4538 O  OG1 . THR B 1 237 ? 27.346  12.108  33.249  1.00 26.84 ? 284 THR B OG1 1 
ATOM   4539 C  CG2 . THR B 1 237 ? 27.630  11.577  35.652  1.00 25.90 ? 284 THR B CG2 1 
ATOM   4540 N  N   . TRP B 1 238 ? 26.970  8.085   34.923  1.00 14.80 ? 285 TRP B N   1 
ATOM   4541 C  CA  . TRP B 1 238 ? 26.816  6.955   35.810  1.00 13.19 ? 285 TRP B CA  1 
ATOM   4542 C  C   . TRP B 1 238 ? 27.906  5.899   35.607  1.00 14.55 ? 285 TRP B C   1 
ATOM   4543 O  O   . TRP B 1 238 ? 28.404  5.324   36.563  1.00 15.24 ? 285 TRP B O   1 
ATOM   4544 C  CB  . TRP B 1 238 ? 25.442  6.355   35.549  1.00 13.32 ? 285 TRP B CB  1 
ATOM   4545 C  CG  . TRP B 1 238 ? 25.178  5.125   36.357  1.00 12.56 ? 285 TRP B CG  1 
ATOM   4546 C  CD1 . TRP B 1 238 ? 25.222  3.850   35.876  1.00 13.68 ? 285 TRP B CD1 1 
ATOM   4547 C  CD2 . TRP B 1 238 ? 24.852  5.013   37.745  1.00 13.21 ? 285 TRP B CD2 1 
ATOM   4548 N  NE1 . TRP B 1 238 ? 24.891  2.975   36.864  1.00 13.15 ? 285 TRP B NE1 1 
ATOM   4549 C  CE2 . TRP B 1 238 ? 24.652  3.647   38.029  1.00 13.94 ? 285 TRP B CE2 1 
ATOM   4550 C  CE3 . TRP B 1 238 ? 24.675  5.932   38.779  1.00 14.55 ? 285 TRP B CE3 1 
ATOM   4551 C  CZ2 . TRP B 1 238 ? 24.297  3.192   39.300  1.00 14.68 ? 285 TRP B CZ2 1 
ATOM   4552 C  CZ3 . TRP B 1 238 ? 24.286  5.481   40.019  1.00 15.07 ? 285 TRP B CZ3 1 
ATOM   4553 C  CH2 . TRP B 1 238 ? 24.072  4.128   40.269  1.00 14.85 ? 285 TRP B CH2 1 
ATOM   4554 N  N   . ASP B 1 239 ? 28.220  5.602   34.352  1.00 14.05 ? 286 ASP B N   1 
ATOM   4555 C  CA  . ASP B 1 239 ? 29.156  4.531   34.042  1.00 14.56 ? 286 ASP B CA  1 
ATOM   4556 C  C   . ASP B 1 239 ? 30.578  4.909   34.431  1.00 16.06 ? 286 ASP B C   1 
ATOM   4557 O  O   . ASP B 1 239 ? 31.410  4.002   34.484  1.00 19.37 ? 286 ASP B O   1 
ATOM   4558 C  CB  . ASP B 1 239 ? 29.046  4.137   32.589  1.00 15.04 ? 286 ASP B CB  1 
ATOM   4559 C  CG  . ASP B 1 239 ? 27.772  3.426   32.198  1.00 13.67 ? 286 ASP B CG  1 
ATOM   4560 O  OD1 . ASP B 1 239 ? 27.099  2.912   33.111  1.00 14.16 ? 286 ASP B OD1 1 
ATOM   4561 O  OD2 . ASP B 1 239 ? 27.504  3.351   30.980  1.00 15.06 ? 286 ASP B OD2 1 
ATOM   4562 N  N   . ARG B 1 240 ? 30.828  6.181   34.688  1.00 15.80 ? 287 ARG B N   1 
ATOM   4563 C  CA  . ARG B 1 240 ? 32.128  6.628   35.196  1.00 17.42 ? 287 ARG B CA  1 
ATOM   4564 C  C   . ARG B 1 240 ? 32.204  6.602   36.716  1.00 18.56 ? 287 ARG B C   1 
ATOM   4565 O  O   . ARG B 1 240 ? 33.273  6.841   37.305  1.00 20.24 ? 287 ARG B O   1 
ATOM   4566 C  CB  . ARG B 1 240 ? 32.411  8.063   34.731  1.00 22.21 ? 287 ARG B CB  1 
ATOM   4567 C  CG  . ARG B 1 240 ? 32.732  8.205   33.258  1.00 26.69 ? 287 ARG B CG  1 
ATOM   4568 C  CD  . ARG B 1 240 ? 33.158  9.659   33.009  1.00 33.94 ? 287 ARG B CD  1 
ATOM   4569 N  NE  . ARG B 1 240 ? 32.637  10.087  31.708  1.00 45.21 ? 287 ARG B NE  1 
ATOM   4570 C  CZ  . ARG B 1 240 ? 33.016  9.621   30.526  1.00 55.02 ? 287 ARG B CZ  1 
ATOM   4571 N  NH1 . ARG B 1 240 ? 34.049  8.798   30.416  1.00 59.08 ? 287 ARG B NH1 1 
ATOM   4572 N  NH2 . ARG B 1 240 ? 32.366  10.010  29.443  1.00 61.70 ? 287 ARG B NH2 1 
ATOM   4573 N  N   . ALA B 1 241 ? 31.108  6.378   37.394  1.00 15.86 ? 288 ALA B N   1 
ATOM   4574 C  CA  . ALA B 1 241 ? 31.123  6.307   38.843  1.00 17.30 ? 288 ALA B CA  1 
ATOM   4575 C  C   . ALA B 1 241 ? 31.731  4.989   39.288  1.00 17.42 ? 288 ALA B C   1 
ATOM   4576 O  O   . ALA B 1 241 ? 31.535  3.945   38.672  1.00 18.75 ? 288 ALA B O   1 
ATOM   4577 C  CB  . ALA B 1 241 ? 29.718  6.459   39.396  1.00 18.95 ? 288 ALA B CB  1 
ATOM   4578 N  N   . SER B 1 242 ? 32.401  5.031   40.432  1.00 16.52 ? 289 SER B N   1 
ATOM   4579 C  CA  . SER B 1 242 ? 32.897  3.799   41.015  1.00 17.26 ? 289 SER B CA  1 
ATOM   4580 C  C   . SER B 1 242 ? 31.764  2.871   41.443  1.00 17.70 ? 289 SER B C   1 
ATOM   4581 O  O   . SER B 1 242 ? 30.646  3.303   41.749  1.00 16.73 ? 289 SER B O   1 
ATOM   4582 C  CB  . SER B 1 242 ? 33.797  4.105   42.183  1.00 18.55 ? 289 SER B CB  1 
ATOM   4583 O  OG  . SER B 1 242 ? 33.054  4.696   43.242  1.00 19.80 ? 289 SER B OG  1 
ATOM   4584 N  N   . LEU B 1 243 ? 32.078  1.580   41.530  1.00 17.69 ? 290 LEU B N   1 
ATOM   4585 C  CA  . LEU B 1 243 ? 31.157  0.615   42.065  1.00 16.98 ? 290 LEU B CA  1 
ATOM   4586 C  C   . LEU B 1 243 ? 30.662  1.052   43.437  1.00 16.16 ? 290 LEU B C   1 
ATOM   4587 O  O   . LEU B 1 243 ? 29.484  0.987   43.723  1.00 16.00 ? 290 LEU B O   1 
ATOM   4588 C  CB  . LEU B 1 243 ? 31.805  -0.753  42.167  1.00 18.47 ? 290 LEU B CB  1 
ATOM   4589 C  CG  . LEU B 1 243 ? 30.934  -1.837  42.799  1.00 20.77 ? 290 LEU B CG  1 
ATOM   4590 C  CD1 . LEU B 1 243 ? 29.731  -2.103  41.929  1.00 23.05 ? 290 LEU B CD1 1 
ATOM   4591 C  CD2 . LEU B 1 243 ? 31.745  -3.104  42.978  1.00 23.25 ? 290 LEU B CD2 1 
ATOM   4592 N  N   . GLN B 1 244 ? 31.555  1.519   44.300  1.00 17.92 ? 291 GLN B N   1 
ATOM   4593 C  CA  . GLN B 1 244 ? 31.125  1.965   45.620  1.00 18.06 ? 291 GLN B CA  1 
ATOM   4594 C  C   . GLN B 1 244 ? 30.128  3.117   45.526  1.00 17.13 ? 291 GLN B C   1 
ATOM   4595 O  O   . GLN B 1 244 ? 29.170  3.152   46.297  1.00 17.27 ? 291 GLN B O   1 
ATOM   4596 C  CB  . GLN B 1 244 ? 32.312  2.243   46.546  1.00 22.02 ? 291 GLN B CB  1 
ATOM   4597 C  CG  . GLN B 1 244 ? 31.864  2.533   47.982  1.00 26.74 ? 291 GLN B CG  1 
ATOM   4598 C  CD  . GLN B 1 244 ? 31.282  1.303   48.664  1.00 34.67 ? 291 GLN B CD  1 
ATOM   4599 O  OE1 . GLN B 1 244 ? 31.995  0.325   48.935  1.00 43.38 ? 291 GLN B OE1 1 
ATOM   4600 N  NE2 . GLN B 1 244 ? 29.972  1.294   48.908  1.00 37.40 ? 291 GLN B NE2 1 
ATOM   4601 N  N   . GLU B 1 245 ? 30.406  4.104   44.684  1.00 16.91 ? 292 GLU B N   1 
ATOM   4602 C  CA  . GLU B 1 245 ? 29.523  5.239   44.567  1.00 18.03 ? 292 GLU B CA  1 
ATOM   4603 C  C   . GLU B 1 245 ? 28.140  4.747   44.127  1.00 15.11 ? 292 GLU B C   1 
ATOM   4604 O  O   . GLU B 1 245 ? 27.128  5.220   44.618  1.00 15.53 ? 292 GLU B O   1 
ATOM   4605 C  CB  . GLU B 1 245 ? 30.097  6.225   43.563  1.00 21.48 ? 292 GLU B CB  1 
ATOM   4606 C  CG  . GLU B 1 245 ? 31.227  7.106   44.090  1.00 29.29 ? 292 GLU B CG  1 
ATOM   4607 C  CD  . GLU B 1 245 ? 31.756  7.820   42.847  1.00 37.68 ? 292 GLU B CD  1 
ATOM   4608 O  OE1 . GLU B 1 245 ? 32.797  7.414   42.280  1.00 37.84 ? 292 GLU B OE1 1 
ATOM   4609 O  OE2 . GLU B 1 245 ? 31.040  8.735   42.388  1.00 48.88 ? 292 GLU B OE2 1 
ATOM   4610 N  N   . GLN B 1 246 ? 28.095  3.835   43.148  1.00 14.27 ? 293 GLN B N   1 
ATOM   4611 C  CA  . GLN B 1 246 ? 26.808  3.365   42.639  1.00 13.92 ? 293 GLN B CA  1 
ATOM   4612 C  C   . GLN B 1 246 ? 26.005  2.659   43.723  1.00 15.29 ? 293 GLN B C   1 
ATOM   4613 O  O   . GLN B 1 246 ? 24.793  2.854   43.865  1.00 14.52 ? 293 GLN B O   1 
ATOM   4614 C  CB  . GLN B 1 246 ? 27.032  2.377   41.490  1.00 13.59 ? 293 GLN B CB  1 
ATOM   4615 C  CG  . GLN B 1 246 ? 27.664  3.007   40.256  1.00 14.04 ? 293 GLN B CG  1 
ATOM   4616 C  CD  . GLN B 1 246 ? 27.630  2.123   39.032  1.00 15.10 ? 293 GLN B CD  1 
ATOM   4617 O  OE1 . GLN B 1 246 ? 27.092  1.015   39.072  1.00 16.02 ? 293 GLN B OE1 1 
ATOM   4618 N  NE2 . GLN B 1 246 ? 28.208  2.581   37.923  1.00 16.46 ? 293 GLN B NE2 1 
ATOM   4619 N  N   . GLU B 1 247 ? 26.648  1.776   44.490  1.00 14.65 ? 294 GLU B N   1 
ATOM   4620 C  CA  . GLU B 1 247 ? 25.992  1.057   45.555  1.00 15.39 ? 294 GLU B CA  1 
ATOM   4621 C  C   . GLU B 1 247 ? 25.535  2.039   46.630  1.00 15.58 ? 294 GLU B C   1 
ATOM   4622 O  O   . GLU B 1 247 ? 24.486  1.854   47.224  1.00 17.53 ? 294 GLU B O   1 
ATOM   4623 C  CB  . GLU B 1 247 ? 26.938  -0.045  46.052  1.00 15.81 ? 294 GLU B CB  1 
ATOM   4624 C  CG  . GLU B 1 247 ? 27.232  -1.123  45.022  1.00 16.01 ? 294 GLU B CG  1 
ATOM   4625 C  CD  . GLU B 1 247 ? 28.010  -2.322  45.502  1.00 17.40 ? 294 GLU B CD  1 
ATOM   4626 O  OE1 . GLU B 1 247 ? 28.676  -2.185  46.546  1.00 22.33 ? 294 GLU B OE1 1 
ATOM   4627 O  OE2 . GLU B 1 247 ? 27.856  -3.372  44.843  1.00 17.56 ? 294 GLU B OE2 1 
ATOM   4628 N  N   . ASP B 1 248 ? 26.369  3.021   46.949  1.00 17.26 ? 295 ASP B N   1 
ATOM   4629 C  CA  . ASP B 1 248 ? 26.017  4.001   47.967  1.00 17.56 ? 295 ASP B CA  1 
ATOM   4630 C  C   . ASP B 1 248 ? 24.786  4.809   47.584  1.00 15.91 ? 295 ASP B C   1 
ATOM   4631 O  O   . ASP B 1 248 ? 23.979  5.173   48.442  1.00 16.80 ? 295 ASP B O   1 
ATOM   4632 C  CB  . ASP B 1 248 ? 27.186  4.917   48.234  1.00 18.40 ? 295 ASP B CB  1 
ATOM   4633 C  CG  . ASP B 1 248 ? 28.270  4.373   49.159  1.00 22.20 ? 295 ASP B CG  1 
ATOM   4634 O  OD1 . ASP B 1 248 ? 28.120  3.291   49.713  1.00 24.16 ? 295 ASP B OD1 1 
ATOM   4635 O  OD2 . ASP B 1 248 ? 29.246  5.087   49.295  1.00 25.61 ? 295 ASP B OD2 1 
ATOM   4636 N  N   . VAL B 1 249 ? 24.624  5.108   46.287  1.00 15.25 ? 296 VAL B N   1 
ATOM   4637 C  CA  . VAL B 1 249 ? 23.458  5.838   45.818  1.00 14.02 ? 296 VAL B CA  1 
ATOM   4638 C  C   . VAL B 1 249 ? 22.193  5.082   46.153  1.00 14.73 ? 296 VAL B C   1 
ATOM   4639 O  O   . VAL B 1 249 ? 21.212  5.720   46.512  1.00 15.50 ? 296 VAL B O   1 
ATOM   4640 C  CB  . VAL B 1 249 ? 23.588  6.057   44.301  1.00 15.38 ? 296 VAL B CB  1 
ATOM   4641 C  CG1 . VAL B 1 249 ? 22.243  6.411   43.692  1.00 15.78 ? 296 VAL B CG1 1 
ATOM   4642 C  CG2 . VAL B 1 249 ? 24.623  7.104   43.978  1.00 16.36 ? 296 VAL B CG2 1 
ATOM   4643 N  N   . PHE B 1 250 ? 22.192  3.738   46.029  1.00 14.26 ? 297 PHE B N   1 
ATOM   4644 C  CA  . PHE B 1 250 ? 20.965  2.996   46.243  1.00 15.40 ? 297 PHE B CA  1 
ATOM   4645 C  C   . PHE B 1 250 ? 20.794  2.470   47.662  1.00 16.15 ? 297 PHE B C   1 
ATOM   4646 O  O   . PHE B 1 250 ? 19.674  2.405   48.159  1.00 17.47 ? 297 PHE B O   1 
ATOM   4647 C  CB  . PHE B 1 250 ? 20.842  1.822   45.275  1.00 14.93 ? 297 PHE B CB  1 
ATOM   4648 C  CG  . PHE B 1 250 ? 20.442  2.321   43.900  1.00 13.27 ? 297 PHE B CG  1 
ATOM   4649 C  CD1 . PHE B 1 250 ? 19.175  2.850   43.710  1.00 13.40 ? 297 PHE B CD1 1 
ATOM   4650 C  CD2 . PHE B 1 250 ? 21.335  2.316   42.832  1.00 14.67 ? 297 PHE B CD2 1 
ATOM   4651 C  CE1 . PHE B 1 250 ? 18.816  3.366   42.498  1.00 15.04 ? 297 PHE B CE1 1 
ATOM   4652 C  CE2 . PHE B 1 250 ? 20.938  2.819   41.589  1.00 15.77 ? 297 PHE B CE2 1 
ATOM   4653 C  CZ  . PHE B 1 250 ? 19.685  3.346   41.446  1.00 15.97 ? 297 PHE B CZ  1 
ATOM   4654 N  N   . GLY B 1 251 ? 21.878  2.060   48.320  1.00 15.96 ? 298 GLY B N   1 
ATOM   4655 C  CA  . GLY B 1 251 ? 21.754  1.338   49.581  1.00 16.53 ? 298 GLY B CA  1 
ATOM   4656 C  C   . GLY B 1 251 ? 21.667  -0.181  49.426  1.00 17.08 ? 298 GLY B C   1 
ATOM   4657 O  O   . GLY B 1 251 ? 21.412  -0.884  50.413  1.00 17.98 ? 298 GLY B O   1 
ATOM   4658 N  N   . ARG B 1 252 ? 21.878  -0.696  48.207  1.00 15.78 ? 299 ARG B N   1 
ATOM   4659 C  CA  . ARG B 1 252 ? 21.908  -2.113  47.929  1.00 14.92 ? 299 ARG B CA  1 
ATOM   4660 C  C   . ARG B 1 252 ? 23.161  -2.363  47.116  1.00 16.68 ? 299 ARG B C   1 
ATOM   4661 O  O   . ARG B 1 252 ? 23.630  -1.459  46.439  1.00 16.93 ? 299 ARG B O   1 
ATOM   4662 C  CB  . ARG B 1 252 ? 20.642  -2.542  47.183  1.00 14.89 ? 299 ARG B CB  1 
ATOM   4663 C  CG  . ARG B 1 252 ? 19.359  -2.523  47.974  1.00 15.23 ? 299 ARG B CG  1 
ATOM   4664 C  CD  . ARG B 1 252 ? 18.124  -2.839  47.137  1.00 14.20 ? 299 ARG B CD  1 
ATOM   4665 N  NE  . ARG B 1 252 ? 16.897  -2.943  47.931  1.00 16.19 ? 299 ARG B NE  1 
ATOM   4666 C  CZ  . ARG B 1 252 ? 16.463  -4.048  48.484  1.00 16.04 ? 299 ARG B CZ  1 
ATOM   4667 N  NH1 . ARG B 1 252 ? 17.179  -5.165  48.507  1.00 16.54 ? 299 ARG B NH1 1 
ATOM   4668 N  NH2 . ARG B 1 252 ? 15.276  -4.022  49.023  1.00 17.40 ? 299 ARG B NH2 1 
ATOM   4669 N  N   . ASP B 1 253 ? 23.684  -3.588  47.152  1.00 16.74 ? 300 ASP B N   1 
ATOM   4670 C  CA  . ASP B 1 253 ? 24.827  -3.931  46.325  1.00 17.06 ? 300 ASP B CA  1 
ATOM   4671 C  C   . ASP B 1 253 ? 24.360  -4.232  44.908  1.00 16.65 ? 300 ASP B C   1 
ATOM   4672 O  O   . ASP B 1 253 ? 23.196  -4.548  44.665  1.00 17.25 ? 300 ASP B O   1 
ATOM   4673 C  CB  . ASP B 1 253 ? 25.635  -5.091  46.901  1.00 18.82 ? 300 ASP B CB  1 
ATOM   4674 C  CG  . ASP B 1 253 ? 24.975  -6.449  46.716  1.00 24.20 ? 300 ASP B CG  1 
ATOM   4675 O  OD1 . ASP B 1 253 ? 24.062  -6.765  47.456  1.00 28.89 ? 300 ASP B OD1 1 
ATOM   4676 O  OD2 . ASP B 1 253 ? 25.367  -7.191  45.794  1.00 32.27 ? 300 ASP B OD2 1 
ATOM   4677 N  N   . LYS B 1 254 ? 25.302  -4.182  43.973  1.00 16.59 ? 301 LYS B N   1 
ATOM   4678 C  CA  . LYS B 1 254 ? 24.924  -4.284  42.569  1.00 16.30 ? 301 LYS B CA  1 
ATOM   4679 C  C   . LYS B 1 254 ? 24.702  -5.733  42.134  1.00 18.90 ? 301 LYS B C   1 
ATOM   4680 O  O   . LYS B 1 254 ? 23.739  -6.002  41.445  1.00 21.47 ? 301 LYS B O   1 
ATOM   4681 C  CB  . LYS B 1 254 ? 25.942  -3.511  41.744  1.00 15.78 ? 301 LYS B CB  1 
ATOM   4682 C  CG  . LYS B 1 254 ? 25.514  -3.352  40.293  1.00 15.99 ? 301 LYS B CG  1 
ATOM   4683 C  CD  . LYS B 1 254 ? 26.312  -2.303  39.536  1.00 15.45 ? 301 LYS B CD  1 
ATOM   4684 C  CE  . LYS B 1 254 ? 25.572  -1.890  38.321  1.00 14.98 ? 301 LYS B CE  1 
ATOM   4685 N  NZ  . LYS B 1 254 ? 26.402  -1.038  37.454  1.00 16.11 ? 301 LYS B NZ  1 
ATOM   4686 N  N   . GLY B 1 255 ? 25.531  -6.664  42.594  1.00 19.42 ? 302 GLY B N   1 
ATOM   4687 C  CA  . GLY B 1 255 ? 25.447  -8.049  42.131  1.00 21.32 ? 302 GLY B CA  1 
ATOM   4688 C  C   . GLY B 1 255 ? 24.204  -8.785  42.611  1.00 19.73 ? 302 GLY B C   1 
ATOM   4689 O  O   . GLY B 1 255 ? 23.427  -9.295  41.822  1.00 24.45 ? 302 GLY B O   1 
ATOM   4690 N  N   . GLU B 1 256 ? 23.989  -8.796  43.916  1.00 19.72 ? 303 GLU B N   1 
ATOM   4691 C  CA  . GLU B 1 256 ? 22.897  -9.540  44.487  1.00 20.28 ? 303 GLU B CA  1 
ATOM   4692 C  C   . GLU B 1 256 ? 21.706  -8.611  44.695  1.00 18.67 ? 303 GLU B C   1 
ATOM   4693 O  O   . GLU B 1 256 ? 20.564  -9.074  44.688  1.00 19.99 ? 303 GLU B O   1 
ATOM   4694 C  CB  . GLU B 1 256 ? 23.365  -10.122 45.819  1.00 21.80 ? 303 GLU B CB  1 
ATOM   4695 C  CG  . GLU B 1 256 ? 22.263  -10.781 46.635  1.00 22.37 ? 303 GLU B CG  1 
ATOM   4696 C  CD  . GLU B 1 256 ? 21.536  -11.959 46.015  1.00 24.00 ? 303 GLU B CD  1 
ATOM   4697 O  OE1 . GLU B 1 256 ? 22.022  -12.503 45.017  1.00 29.61 ? 303 GLU B OE1 1 
ATOM   4698 O  OE2 . GLU B 1 256 ? 20.443  -12.303 46.490  1.00 24.59 ? 303 GLU B OE2 1 
ATOM   4699 N  N   . GLY B 1 257 ? 21.964  -7.305  44.872  1.00 17.71 ? 304 GLY B N   1 
ATOM   4700 C  CA  . GLY B 1 257 ? 20.862  -6.418  45.206  1.00 17.56 ? 304 GLY B CA  1 
ATOM   4701 C  C   . GLY B 1 257 ? 20.403  -6.514  46.650  1.00 16.83 ? 304 GLY B C   1 
ATOM   4702 O  O   . GLY B 1 257 ? 19.268  -6.171  46.973  1.00 17.08 ? 304 GLY B O   1 
ATOM   4703 N  N   . ALA B 1 258 ? 21.258  -7.058  47.536  1.00 18.53 ? 305 ALA B N   1 
ATOM   4704 C  CA  . ALA B 1 258 ? 20.935  -7.083  48.943  1.00 18.75 ? 305 ALA B CA  1 
ATOM   4705 C  C   . ALA B 1 258 ? 21.087  -5.707  49.560  1.00 16.37 ? 305 ALA B C   1 
ATOM   4706 O  O   . ALA B 1 258 ? 21.968  -4.938  49.194  1.00 17.56 ? 305 ALA B O   1 
ATOM   4707 C  CB  . ALA B 1 258 ? 21.839  -8.076  49.654  1.00 18.40 ? 305 ALA B CB  1 
ATOM   4708 N  N   . PRO B 1 259 ? 20.269  -5.364  50.570  1.00 17.28 ? 306 PRO B N   1 
ATOM   4709 C  CA  . PRO B 1 259 ? 20.511  -4.157  51.346  1.00 17.20 ? 306 PRO B CA  1 
ATOM   4710 C  C   . PRO B 1 259 ? 21.907  -4.230  51.952  1.00 19.79 ? 306 PRO B C   1 
ATOM   4711 O  O   . PRO B 1 259 ? 22.403  -5.310  52.276  1.00 21.09 ? 306 PRO B O   1 
ATOM   4712 C  CB  . PRO B 1 259 ? 19.435  -4.155  52.437  1.00 19.10 ? 306 PRO B CB  1 
ATOM   4713 C  CG  . PRO B 1 259 ? 18.378  -5.135  51.969  1.00 19.85 ? 306 PRO B CG  1 
ATOM   4714 C  CD  . PRO B 1 259 ? 19.134  -6.140  51.088  1.00 17.47 ? 306 PRO B CD  1 
ATOM   4715 N  N   . VAL B 1 260 ? 22.510  -3.076  52.145  1.00 20.32 ? 307 VAL B N   1 
ATOM   4716 C  CA  . VAL B 1 260 ? 23.821  -3.034  52.760  1.00 23.67 ? 307 VAL B CA  1 
ATOM   4717 C  C   . VAL B 1 260 ? 23.757  -3.749  54.116  1.00 23.40 ? 307 VAL B C   1 
ATOM   4718 O  O   . VAL B 1 260 ? 22.836  -3.565  54.913  1.00 24.52 ? 307 VAL B O   1 
ATOM   4719 C  CB  . VAL B 1 260 ? 24.310  -1.578  52.860  1.00 29.45 ? 307 VAL B CB  1 
ATOM   4720 C  CG1 . VAL B 1 260 ? 23.368  -0.756  53.719  1.00 30.25 ? 307 VAL B CG1 1 
ATOM   4721 C  CG2 . VAL B 1 260 ? 25.745  -1.484  53.370  1.00 34.06 ? 307 VAL B CG2 1 
ATOM   4722 N  N   . GLY B 1 261 ? 24.769  -4.594  54.359  1.00 28.01 ? 308 GLY B N   1 
ATOM   4723 C  CA  . GLY B 1 261 ? 24.884  -5.290  55.630  1.00 29.16 ? 308 GLY B CA  1 
ATOM   4724 C  C   . GLY B 1 261 ? 24.116  -6.604  55.630  1.00 31.70 ? 308 GLY B C   1 
ATOM   4725 O  O   . GLY B 1 261 ? 24.161  -7.336  56.617  1.00 33.73 ? 308 GLY B O   1 
ATOM   4726 N  N   . LYS B 1 262 ? 23.408  -6.909  54.531  1.00 27.63 ? 309 LYS B N   1 
ATOM   4727 C  CA  . LYS B 1 262 ? 22.603  -8.122  54.420  1.00 25.83 ? 309 LYS B CA  1 
ATOM   4728 C  C   . LYS B 1 262 ? 23.166  -8.981  53.301  1.00 25.77 ? 309 LYS B C   1 
ATOM   4729 O  O   . LYS B 1 262 ? 24.027  -8.520  52.572  1.00 29.46 ? 309 LYS B O   1 
ATOM   4730 C  CB  . LYS B 1 262 ? 21.130  -7.785  54.167  1.00 29.08 ? 309 LYS B CB  1 
ATOM   4731 C  CG  . LYS B 1 262 ? 20.453  -6.977  55.224  1.00 31.13 ? 309 LYS B CG  1 
ATOM   4732 C  CD  . LYS B 1 262 ? 20.090  -7.773  56.470  1.00 34.91 ? 309 LYS B CD  1 
ATOM   4733 C  CE  . LYS B 1 262 ? 19.585  -6.858  57.531  1.00 40.28 ? 309 LYS B CE  1 
ATOM   4734 N  NZ  . LYS B 1 262 ? 18.618  -7.532  58.393  1.00 44.55 ? 309 LYS B NZ  1 
ATOM   4735 N  N   . ALA B 1 263 ? 22.680  -10.225 53.157  1.00 25.57 ? 310 ALA B N   1 
ATOM   4736 C  CA  . ALA B 1 263 ? 23.291  -11.175 52.253  1.00 27.91 ? 310 ALA B CA  1 
ATOM   4737 C  C   . ALA B 1 263 ? 22.452  -11.385 50.989  1.00 24.76 ? 310 ALA B C   1 
ATOM   4738 O  O   . ALA B 1 263 ? 23.026  -11.683 49.944  1.00 28.76 ? 310 ALA B O   1 
ATOM   4739 C  CB  . ALA B 1 263 ? 23.533  -12.483 52.979  1.00 29.63 ? 310 ALA B CB  1 
ATOM   4740 N  N   . LYS B 1 264 ? 21.119  -11.311 51.091  1.00 25.61 ? 311 LYS B N   1 
ATOM   4741 C  CA  . LYS B 1 264 ? 20.247  -11.704 50.003  1.00 25.13 ? 311 LYS B CA  1 
ATOM   4742 C  C   . LYS B 1 264 ? 19.360  -10.555 49.529  1.00 20.60 ? 311 LYS B C   1 
ATOM   4743 O  O   . LYS B 1 264 ? 18.986  -9.693  50.319  1.00 21.14 ? 311 LYS B O   1 
ATOM   4744 C  CB  . LYS B 1 264 ? 19.324  -12.849 50.430  1.00 29.84 ? 311 LYS B CB  1 
ATOM   4745 C  CG  . LYS B 1 264 ? 20.066  -14.086 50.907  1.00 35.63 ? 311 LYS B CG  1 
ATOM   4746 C  CD  . LYS B 1 264 ? 19.131  -15.242 51.240  1.00 44.57 ? 311 LYS B CD  1 
ATOM   4747 C  CE  . LYS B 1 264 ? 18.305  -15.752 50.086  1.00 49.93 ? 311 LYS B CE  1 
ATOM   4748 N  NZ  . LYS B 1 264 ? 19.122  -16.278 48.987  1.00 52.33 ? 311 LYS B NZ  1 
ATOM   4749 N  N   . GLU B 1 265 ? 18.991  -10.597 48.248  1.00 21.63 ? 312 GLU B N   1 
ATOM   4750 C  CA  . GLU B 1 265 ? 18.145  -9.573  47.642  1.00 19.53 ? 312 GLU B CA  1 
ATOM   4751 C  C   . GLU B 1 265 ? 16.936  -9.243  48.510  1.00 19.99 ? 312 GLU B C   1 
ATOM   4752 O  O   . GLU B 1 265 ? 16.581  -8.077  48.737  1.00 19.98 ? 312 GLU B O   1 
ATOM   4753 C  CB  . GLU B 1 265 ? 17.681  -10.057 46.275  1.00 18.85 ? 312 GLU B CB  1 
ATOM   4754 C  CG  . GLU B 1 265 ? 16.804  -9.043  45.540  1.00 19.78 ? 312 GLU B CG  1 
ATOM   4755 C  CD  . GLU B 1 265 ? 16.126  -9.543  44.292  1.00 18.61 ? 312 GLU B CD  1 
ATOM   4756 O  OE1 . GLU B 1 265 ? 16.525  -10.588 43.736  1.00 20.66 ? 312 GLU B OE1 1 
ATOM   4757 O  OE2 . GLU B 1 265 ? 15.216  -8.860  43.833  1.00 18.81 ? 312 GLU B OE2 1 
ATOM   4758 N  N   . ARG B 1 266 ? 16.258  -10.288 48.973  1.00 19.14 ? 313 ARG B N   1 
ATOM   4759 C  CA  . ARG B 1 266 ? 14.964  -10.122 49.600  1.00 20.63 ? 313 ARG B CA  1 
ATOM   4760 C  C   . ARG B 1 266 ? 15.077  -9.966  51.119  1.00 18.80 ? 313 ARG B C   1 
ATOM   4761 O  O   . ARG B 1 266 ? 14.058  -9.827  51.787  1.00 21.69 ? 313 ARG B O   1 
ATOM   4762 C  CB  . ARG B 1 266 ? 14.006  -11.257 49.201  1.00 23.13 ? 313 ARG B CB  1 
ATOM   4763 C  CG  . ARG B 1 266 ? 13.597  -11.104 47.735  1.00 29.09 ? 313 ARG B CG  1 
ATOM   4764 C  CD  . ARG B 1 266 ? 12.422  -11.975 47.304  1.00 33.43 ? 313 ARG B CD  1 
ATOM   4765 N  NE  . ARG B 1 266 ? 12.109  -11.725 45.889  1.00 38.04 ? 313 ARG B NE  1 
ATOM   4766 C  CZ  . ARG B 1 266 ? 11.462  -10.658 45.394  1.00 40.96 ? 313 ARG B CZ  1 
ATOM   4767 N  NH1 . ARG B 1 266 ? 10.695  -9.903  46.167  1.00 36.50 ? 313 ARG B NH1 1 
ATOM   4768 N  NH2 . ARG B 1 266 ? 11.537  -10.383 44.096  1.00 41.65 ? 313 ARG B NH2 1 
ATOM   4769 N  N   . ASP B 1 267 ? 16.298  -9.952  51.665  1.00 19.66 ? 314 ASP B N   1 
ATOM   4770 C  CA  . ASP B 1 267 ? 16.481  -9.569  53.058  1.00 21.94 ? 314 ASP B CA  1 
ATOM   4771 C  C   . ASP B 1 267 ? 15.883  -8.184  53.273  1.00 22.05 ? 314 ASP B C   1 
ATOM   4772 O  O   . ASP B 1 267 ? 16.054  -7.308  52.429  1.00 21.39 ? 314 ASP B O   1 
ATOM   4773 C  CB  . ASP B 1 267 ? 17.949  -9.586  53.433  1.00 22.75 ? 314 ASP B CB  1 
ATOM   4774 C  CG  . ASP B 1 267 ? 18.537  -10.961 53.666  1.00 25.87 ? 314 ASP B CG  1 
ATOM   4775 O  OD1 . ASP B 1 267 ? 17.741  -11.912 53.759  1.00 33.41 ? 314 ASP B OD1 1 
ATOM   4776 O  OD2 . ASP B 1 267 ? 19.773  -11.070 53.633  1.00 26.67 ? 314 ASP B OD2 1 
ATOM   4777 N  N   . GLU B 1 268 ? 15.177  -7.968  54.390  1.00 24.25 ? 315 GLU B N   1 
ATOM   4778 C  CA  . GLU B 1 268 ? 14.548  -6.674  54.637  1.00 24.56 ? 315 GLU B CA  1 
ATOM   4779 C  C   . GLU B 1 268 ? 15.652  -5.673  54.971  1.00 24.49 ? 315 GLU B C   1 
ATOM   4780 O  O   . GLU B 1 268 ? 16.635  -5.974  55.657  1.00 24.67 ? 315 GLU B O   1 
ATOM   4781 C  CB  . GLU B 1 268 ? 13.445  -6.743  55.698  1.00 31.86 ? 315 GLU B CB  1 
ATOM   4782 C  CG  . GLU B 1 268 ? 12.185  -7.496  55.260  1.00 34.44 ? 315 GLU B CG  1 
ATOM   4783 C  CD  . GLU B 1 268 ? 11.327  -6.875  54.144  1.00 44.64 ? 315 GLU B CD  1 
ATOM   4784 O  OE1 . GLU B 1 268 ? 11.590  -5.755  53.671  1.00 37.80 ? 315 GLU B OE1 1 
ATOM   4785 O  OE2 . GLU B 1 268 ? 10.353  -7.528  53.735  1.00 48.00 ? 315 GLU B OE2 1 
ATOM   4786 N  N   . PRO B 1 269 ? 15.565  -4.451  54.427  1.00 22.21 ? 316 PRO B N   1 
ATOM   4787 C  CA  . PRO B 1 269 ? 16.593  -3.433  54.620  1.00 21.51 ? 316 PRO B CA  1 
ATOM   4788 C  C   . PRO B 1 269 ? 16.650  -2.946  56.059  1.00 22.24 ? 316 PRO B C   1 
ATOM   4789 O  O   . PRO B 1 269 ? 15.640  -2.876  56.755  1.00 25.76 ? 316 PRO B O   1 
ATOM   4790 C  CB  . PRO B 1 269 ? 16.196  -2.283  53.683  1.00 24.60 ? 316 PRO B CB  1 
ATOM   4791 C  CG  . PRO B 1 269 ? 14.794  -2.562  53.286  1.00 26.38 ? 316 PRO B CG  1 
ATOM   4792 C  CD  . PRO B 1 269 ? 14.493  -4.008  53.527  1.00 24.82 ? 316 PRO B CD  1 
ATOM   4793 N  N   . PHE B 1 270 ? 17.876  -2.648  56.485  1.00 22.96 ? 317 PHE B N   1 
ATOM   4794 C  CA  . PHE B 1 270 ? 18.112  -1.918  57.714  1.00 20.42 ? 317 PHE B CA  1 
ATOM   4795 C  C   . PHE B 1 270 ? 18.489  -0.512  57.274  1.00 18.88 ? 317 PHE B C   1 
ATOM   4796 O  O   . PHE B 1 270 ? 19.601  -0.280  56.821  1.00 19.82 ? 317 PHE B O   1 
ATOM   4797 C  CB  . PHE B 1 270 ? 19.180  -2.603  58.558  1.00 22.33 ? 317 PHE B CB  1 
ATOM   4798 C  CG  . PHE B 1 270 ? 19.593  -1.846  59.806  1.00 27.24 ? 317 PHE B CG  1 
ATOM   4799 C  CD1 . PHE B 1 270 ? 18.651  -1.232  60.625  1.00 36.00 ? 317 PHE B CD1 1 
ATOM   4800 C  CD2 . PHE B 1 270 ? 20.932  -1.745  60.151  1.00 30.42 ? 317 PHE B CD2 1 
ATOM   4801 C  CE1 . PHE B 1 270 ? 19.056  -0.560  61.773  1.00 37.56 ? 317 PHE B CE1 1 
ATOM   4802 C  CE2 . PHE B 1 270 ? 21.334  -1.068  61.299  1.00 34.32 ? 317 PHE B CE2 1 
ATOM   4803 C  CZ  . PHE B 1 270 ? 20.391  -0.467  62.099  1.00 37.20 ? 317 PHE B CZ  1 
ATOM   4804 N  N   . LEU B 1 271 ? 17.535  0.409   57.360  1.00 18.71 ? 318 LEU B N   1 
ATOM   4805 C  CA  . LEU B 1 271 ? 17.719  1.725   56.766  1.00 18.56 ? 318 LEU B CA  1 
ATOM   4806 C  C   . LEU B 1 271 ? 18.911  2.494   57.355  1.00 21.61 ? 318 LEU B C   1 
ATOM   4807 O  O   . LEU B 1 271 ? 19.552  3.274   56.661  1.00 20.73 ? 318 LEU B O   1 
ATOM   4808 C  CB  . LEU B 1 271 ? 16.428  2.539   56.831  1.00 21.16 ? 318 LEU B CB  1 
ATOM   4809 C  CG  . LEU B 1 271 ? 15.248  1.883   56.108  1.00 21.80 ? 318 LEU B CG  1 
ATOM   4810 C  CD1 . LEU B 1 271 ? 14.054  2.785   56.236  1.00 25.70 ? 318 LEU B CD1 1 
ATOM   4811 C  CD2 . LEU B 1 271 ? 15.549  1.619   54.684  1.00 22.64 ? 318 LEU B CD2 1 
ATOM   4812 N  N   . LYS B 1 272 ? 19.200  2.317   58.655  1.00 21.50 ? 319 LYS B N   1 
ATOM   4813 C  CA  . LYS B 1 272 ? 20.217  3.159   59.264  1.00 23.46 ? 319 LYS B CA  1 
ATOM   4814 C  C   . LYS B 1 272 ? 21.605  2.791   58.767  1.00 21.65 ? 319 LYS B C   1 
ATOM   4815 O  O   . LYS B 1 272 ? 22.544  3.559   58.987  1.00 25.75 ? 319 LYS B O   1 
ATOM   4816 C  CB  . LYS B 1 272 ? 20.250  3.065   60.794  1.00 31.93 ? 319 LYS B CB  1 
ATOM   4817 C  CG  . LYS B 1 272 ? 18.913  3.324   61.455  1.00 43.22 ? 319 LYS B CG  1 
ATOM   4818 C  CD  . LYS B 1 272 ? 18.249  4.657   61.126  1.00 47.68 ? 319 LYS B CD  1 
ATOM   4819 C  CE  . LYS B 1 272 ? 17.018  4.862   61.961  1.00 52.83 ? 319 LYS B CE  1 
ATOM   4820 N  NZ  . LYS B 1 272 ? 17.341  4.823   63.392  1.00 54.45 ? 319 LYS B NZ  1 
ATOM   4821 N  N   . ALA B 1 273 ? 21.765  1.634   58.125  1.00 22.36 ? 320 ALA B N   1 
ATOM   4822 C  CA  . ALA B 1 273 ? 23.067  1.238   57.622  1.00 20.38 ? 320 ALA B CA  1 
ATOM   4823 C  C   . ALA B 1 273 ? 23.341  1.927   56.283  1.00 19.59 ? 320 ALA B C   1 
ATOM   4824 O  O   . ALA B 1 273 ? 24.473  1.935   55.820  1.00 22.45 ? 320 ALA B O   1 
ATOM   4825 C  CB  . ALA B 1 273 ? 23.162  -0.242  57.478  1.00 23.00 ? 320 ALA B CB  1 
ATOM   4826 N  N   . MET B 1 274 ? 22.275  2.462   55.666  1.00 17.72 ? 321 MET B N   1 
ATOM   4827 C  CA  . MET B 1 274 ? 22.428  3.136   54.389  1.00 16.97 ? 321 MET B CA  1 
ATOM   4828 C  C   . MET B 1 274 ? 22.794  4.595   54.600  1.00 17.92 ? 321 MET B C   1 
ATOM   4829 O  O   . MET B 1 274 ? 22.513  5.163   55.627  1.00 18.86 ? 321 MET B O   1 
ATOM   4830 C  CB  . MET B 1 274 ? 21.109  3.087   53.620  1.00 17.89 ? 321 MET B CB  1 
ATOM   4831 C  CG  . MET B 1 274 ? 20.620  1.701   53.366  1.00 16.92 ? 321 MET B CG  1 
ATOM   4832 S  SD  . MET B 1 274 ? 19.050  1.748   52.487  1.00 18.91 ? 321 MET B SD  1 
ATOM   4833 C  CE  . MET B 1 274 ? 18.650  0.003   52.403  1.00 21.66 ? 321 MET B CE  1 
ATOM   4834 N  N   . LYS B 1 275 ? 23.388  5.221   53.587  1.00 17.58 ? 322 LYS B N   1 
ATOM   4835 C  CA  . LYS B 1 275 ? 23.639  6.647   53.658  1.00 17.40 ? 322 LYS B CA  1 
ATOM   4836 C  C   . LYS B 1 275 ? 22.332  7.403   53.743  1.00 18.74 ? 322 LYS B C   1 
ATOM   4837 O  O   . LYS B 1 275 ? 21.313  6.934   53.242  1.00 17.15 ? 322 LYS B O   1 
ATOM   4838 C  CB  . LYS B 1 275 ? 24.501  7.137   52.494  1.00 21.42 ? 322 LYS B CB  1 
ATOM   4839 C  CG  . LYS B 1 275 ? 25.938  6.656   52.605  1.00 28.08 ? 322 LYS B CG  1 
ATOM   4840 C  CD  . LYS B 1 275 ? 26.830  7.143   51.479  1.00 36.20 ? 322 LYS B CD  1 
ATOM   4841 C  CE  . LYS B 1 275 ? 28.257  7.365   51.901  1.00 42.37 ? 322 LYS B CE  1 
ATOM   4842 N  NZ  . LYS B 1 275 ? 28.798  6.265   52.705  1.00 48.62 ? 322 LYS B NZ  1 
ATOM   4843 N  N   . PRO B 1 276 ? 22.288  8.560   54.429  1.00 18.04 ? 323 PRO B N   1 
ATOM   4844 C  CA  . PRO B 1 276 ? 21.034  9.272   54.633  1.00 17.23 ? 323 PRO B CA  1 
ATOM   4845 C  C   . PRO B 1 276 ? 20.282  9.630   53.357  1.00 15.66 ? 323 PRO B C   1 
ATOM   4846 O  O   . PRO B 1 276 ? 19.059  9.733   53.374  1.00 19.43 ? 323 PRO B O   1 
ATOM   4847 C  CB  . PRO B 1 276 ? 21.488  10.536  55.421  1.00 20.00 ? 323 PRO B CB  1 
ATOM   4848 C  CG  . PRO B 1 276 ? 22.754  10.114  56.099  1.00 20.83 ? 323 PRO B CG  1 
ATOM   4849 C  CD  . PRO B 1 276 ? 23.411  9.110   55.223  1.00 19.85 ? 323 PRO B CD  1 
ATOM   4850 N  N   . ASP B 1 277 ? 21.014  9.884   52.283  1.00 15.99 ? 324 ASP B N   1 
ATOM   4851 C  CA  . ASP B 1 277 ? 20.384  10.289  51.038  1.00 15.37 ? 324 ASP B CA  1 
ATOM   4852 C  C   . ASP B 1 277 ? 20.390  9.148   50.019  1.00 14.37 ? 324 ASP B C   1 
ATOM   4853 O  O   . ASP B 1 277 ? 20.190  9.398   48.825  1.00 15.20 ? 324 ASP B O   1 
ATOM   4854 C  CB  . ASP B 1 277 ? 20.961  11.603  50.545  1.00 17.31 ? 324 ASP B CB  1 
ATOM   4855 C  CG  . ASP B 1 277 ? 20.609  12.803  51.413  1.00 20.92 ? 324 ASP B CG  1 
ATOM   4856 O  OD1 . ASP B 1 277 ? 19.449  12.913  51.848  1.00 21.70 ? 324 ASP B OD1 1 
ATOM   4857 O  OD2 . ASP B 1 277 ? 21.548  13.613  51.660  1.00 27.89 ? 324 ASP B OD2 1 
ATOM   4858 N  N   . ALA B 1 278 ? 20.557  7.905   50.464  1.00 14.34 ? 325 ALA B N   1 
ATOM   4859 C  CA  . ALA B 1 278 ? 20.423  6.771   49.564  1.00 13.73 ? 325 ALA B CA  1 
ATOM   4860 C  C   . ALA B 1 278 ? 18.970  6.652   49.129  1.00 13.73 ? 325 ALA B C   1 
ATOM   4861 O  O   . ALA B 1 278 ? 18.045  6.871   49.872  1.00 13.19 ? 325 ALA B O   1 
ATOM   4862 C  CB  . ALA B 1 278 ? 20.926  5.487   50.220  1.00 14.89 ? 325 ALA B CB  1 
ATOM   4863 N  N   . HIS B 1 279 ? 18.801  6.267   47.863  1.00 12.70 ? 326 HIS B N   1 
ATOM   4864 C  CA  . HIS B 1 279 ? 17.480  6.181   47.254  1.00 12.56 ? 326 HIS B CA  1 
ATOM   4865 C  C   . HIS B 1 279 ? 16.510  5.311   48.052  1.00 12.98 ? 326 HIS B C   1 
ATOM   4866 O  O   . HIS B 1 279 ? 15.386  5.709   48.286  1.00 12.88 ? 326 HIS B O   1 
ATOM   4867 C  CB  . HIS B 1 279 ? 17.640  5.636   45.831  1.00 11.40 ? 326 HIS B CB  1 
ATOM   4868 C  CG  . HIS B 1 279 ? 16.378  5.607   45.049  1.00 11.10 ? 326 HIS B CG  1 
ATOM   4869 N  ND1 . HIS B 1 279 ? 15.692  6.713   44.635  1.00 12.97 ? 326 HIS B ND1 1 
ATOM   4870 C  CD2 . HIS B 1 279 ? 15.633  4.514   44.709  1.00 11.84 ? 326 HIS B CD2 1 
ATOM   4871 C  CE1 . HIS B 1 279 ? 14.556  6.295   44.052  1.00 11.82 ? 326 HIS B CE1 1 
ATOM   4872 N  NE2 . HIS B 1 279 ? 14.509  4.984   44.056  1.00 10.92 ? 326 HIS B NE2 1 
ATOM   4873 N  N   . VAL B 1 280 ? 16.949  4.100   48.406  1.00 13.10 ? 327 VAL B N   1 
ATOM   4874 C  CA  . VAL B 1 280 ? 16.061  3.162   49.074  1.00 13.49 ? 327 VAL B CA  1 
ATOM   4875 C  C   . VAL B 1 280 ? 15.644  3.714   50.415  1.00 13.89 ? 327 VAL B C   1 
ATOM   4876 O  O   . VAL B 1 280 ? 14.482  3.613   50.764  1.00 15.75 ? 327 VAL B O   1 
ATOM   4877 C  CB  . VAL B 1 280 ? 16.686  1.780   49.220  1.00 14.71 ? 327 VAL B CB  1 
ATOM   4878 C  CG1 . VAL B 1 280 ? 15.859  0.895   50.128  1.00 16.06 ? 327 VAL B CG1 1 
ATOM   4879 C  CG2 . VAL B 1 280 ? 16.829  1.130   47.855  1.00 16.83 ? 327 VAL B CG2 1 
ATOM   4880 N  N   . ARG B 1 281 ? 16.583  4.345   51.142  1.00 13.39 ? 328 ARG B N   1 
ATOM   4881 C  CA  . ARG B 1 281 ? 16.246  4.898   52.444  1.00 14.44 ? 328 ARG B CA  1 
ATOM   4882 C  C   . ARG B 1 281 ? 15.214  6.016   52.325  1.00 14.01 ? 328 ARG B C   1 
ATOM   4883 O  O   . ARG B 1 281 ? 14.298  6.068   53.119  1.00 18.65 ? 328 ARG B O   1 
ATOM   4884 C  CB  . ARG B 1 281 ? 17.540  5.414   53.081  1.00 14.90 ? 328 ARG B CB  1 
ATOM   4885 C  CG  . ARG B 1 281 ? 17.315  6.043   54.450  1.00 17.70 ? 328 ARG B CG  1 
ATOM   4886 C  CD  . ARG B 1 281 ? 18.626  6.204   55.198  1.00 20.31 ? 328 ARG B CD  1 
ATOM   4887 N  NE  . ARG B 1 281 ? 18.338  6.810   56.506  1.00 24.12 ? 328 ARG B NE  1 
ATOM   4888 C  CZ  . ARG B 1 281 ? 19.274  6.963   57.412  1.00 25.74 ? 328 ARG B CZ  1 
ATOM   4889 N  NH1 . ARG B 1 281 ? 20.524  6.613   57.164  1.00 21.66 ? 328 ARG B NH1 1 
ATOM   4890 N  NH2 . ARG B 1 281 ? 18.974  7.579   58.528  1.00 29.70 ? 328 ARG B NH2 1 
ATOM   4891 N  N   . LEU B 1 282 ? 15.339  6.870   51.318  1.00 14.48 ? 329 LEU B N   1 
ATOM   4892 C  CA  . LEU B 1 282 ? 14.427  7.985   51.139  1.00 13.51 ? 329 LEU B CA  1 
ATOM   4893 C  C   . LEU B 1 282 ? 13.069  7.523   50.646  1.00 14.22 ? 329 LEU B C   1 
ATOM   4894 O  O   . LEU B 1 282 ? 12.070  8.151   50.924  1.00 14.28 ? 329 LEU B O   1 
ATOM   4895 C  CB  . LEU B 1 282 ? 14.977  9.052   50.206  1.00 13.47 ? 329 LEU B CB  1 
ATOM   4896 C  CG  . LEU B 1 282 ? 16.207  9.785   50.751  1.00 14.86 ? 329 LEU B CG  1 
ATOM   4897 C  CD1 . LEU B 1 282 ? 16.782  10.622  49.635  1.00 15.59 ? 329 LEU B CD1 1 
ATOM   4898 C  CD2 . LEU B 1 282 ? 15.886  10.645  51.967  1.00 16.05 ? 329 LEU B CD2 1 
ATOM   4899 N  N   . ALA B 1 283 ? 13.051  6.475   49.819  1.00 13.85 ? 330 ALA B N   1 
ATOM   4900 C  CA  . ALA B 1 283 ? 11.805  6.065   49.176  1.00 13.18 ? 330 ALA B CA  1 
ATOM   4901 C  C   . ALA B 1 283 ? 10.983  5.066   49.982  1.00 14.67 ? 330 ALA B C   1 
ATOM   4902 O  O   . ALA B 1 283 ? 9.821   4.803   49.679  1.00 15.20 ? 330 ALA B O   1 
ATOM   4903 C  CB  . ALA B 1 283 ? 12.147  5.474   47.830  1.00 14.05 ? 330 ALA B CB  1 
ATOM   4904 N  N   . HIS B 1 284 ? 11.595  4.468   50.978  1.00 13.39 ? 331 HIS B N   1 
ATOM   4905 C  CA  . HIS B 1 284 ? 10.969  3.411   51.761  1.00 14.40 ? 331 HIS B CA  1 
ATOM   4906 C  C   . HIS B 1 284 ? 9.741   3.928   52.478  1.00 15.35 ? 331 HIS B C   1 
ATOM   4907 O  O   . HIS B 1 284 ? 9.717   5.048   52.973  1.00 14.21 ? 331 HIS B O   1 
ATOM   4908 C  CB  . HIS B 1 284 ? 11.990  2.880   52.765  1.00 14.78 ? 331 HIS B CB  1 
ATOM   4909 C  CG  . HIS B 1 284 ? 11.609  1.597   53.419  1.00 17.15 ? 331 HIS B CG  1 
ATOM   4910 N  ND1 . HIS B 1 284 ? 10.791  1.569   54.528  1.00 19.41 ? 331 HIS B ND1 1 
ATOM   4911 C  CD2 . HIS B 1 284 ? 12.012  0.335   53.179  1.00 16.97 ? 331 HIS B CD2 1 
ATOM   4912 C  CE1 . HIS B 1 284 ? 10.703  0.303   54.921  1.00 19.50 ? 331 HIS B CE1 1 
ATOM   4913 N  NE2 . HIS B 1 284 ? 11.415  -0.478  54.111  1.00 18.76 ? 331 HIS B NE2 1 
ATOM   4914 N  N   . PRO B 1 285 ? 8.677   3.107   52.596  1.00 14.33 ? 332 PRO B N   1 
ATOM   4915 C  CA  . PRO B 1 285 ? 7.493   3.532   53.309  1.00 14.30 ? 332 PRO B CA  1 
ATOM   4916 C  C   . PRO B 1 285 ? 7.758   4.055   54.726  1.00 15.05 ? 332 PRO B C   1 
ATOM   4917 O  O   . PRO B 1 285 ? 7.100   5.029   55.110  1.00 16.65 ? 332 PRO B O   1 
ATOM   4918 C  CB  . PRO B 1 285 ? 6.580   2.297   53.284  1.00 15.88 ? 332 PRO B CB  1 
ATOM   4919 C  CG  . PRO B 1 285 ? 7.036   1.495   52.089  1.00 16.94 ? 332 PRO B CG  1 
ATOM   4920 C  CD  . PRO B 1 285 ? 8.503   1.816   51.893  1.00 15.91 ? 332 PRO B CD  1 
ATOM   4921 N  N   . ASP B 1 286 ? 8.779   3.499   55.401  1.00 17.10 ? 333 ASP B N   1 
ATOM   4922 C  CA  . ASP B 1 286 ? 9.032   3.881   56.793  1.00 18.83 ? 333 ASP B CA  1 
ATOM   4923 C  C   . ASP B 1 286 ? 9.512   5.325   56.854  1.00 19.93 ? 333 ASP B C   1 
ATOM   4924 O  O   . ASP B 1 286 ? 9.396   5.994   57.893  1.00 22.95 ? 333 ASP B O   1 
ATOM   4925 C  CB  . ASP B 1 286 ? 9.989   2.931   57.496  1.00 20.67 ? 333 ASP B CB  1 
ATOM   4926 C  CG  . ASP B 1 286 ? 9.417   1.557   57.816  1.00 23.53 ? 333 ASP B CG  1 
ATOM   4927 O  OD1 . ASP B 1 286 ? 8.211   1.359   57.591  1.00 26.86 ? 333 ASP B OD1 1 
ATOM   4928 O  OD2 . ASP B 1 286 ? 10.197  0.705   58.313  1.00 30.04 ? 333 ASP B OD2 1 
ATOM   4929 N  N   . SER B 1 287 ? 10.115  5.817   55.773  1.00 16.73 ? 334 SER B N   1 
ATOM   4930 C  CA  . SER B 1 287 ? 10.583  7.183   55.682  1.00 16.37 ? 334 SER B CA  1 
ATOM   4931 C  C   . SER B 1 287 ? 9.509   8.170   55.230  1.00 16.39 ? 334 SER B C   1 
ATOM   4932 O  O   . SER B 1 287 ? 9.761   9.365   55.131  1.00 19.98 ? 334 SER B O   1 
ATOM   4933 C  CB  . SER B 1 287 ? 11.775  7.291   54.754  1.00 17.49 ? 334 SER B CB  1 
ATOM   4934 O  OG  . SER B 1 287 ? 12.847  6.460   55.158  1.00 21.80 ? 334 SER B OG  1 
ATOM   4935 N  N   . ASN B 1 288 ? 8.341   7.673   54.853  1.00 16.12 ? 335 ASN B N   1 
ATOM   4936 C  CA  . ASN B 1 288 ? 7.303   8.451   54.235  1.00 16.77 ? 335 ASN B CA  1 
ATOM   4937 C  C   . ASN B 1 288 ? 5.957   8.196   54.910  1.00 18.16 ? 335 ASN B C   1 
ATOM   4938 O  O   . ASN B 1 288 ? 4.933   8.301   54.243  1.00 19.73 ? 335 ASN B O   1 
ATOM   4939 C  CB  . ASN B 1 288 ? 7.183   8.105   52.755  1.00 18.34 ? 335 ASN B CB  1 
ATOM   4940 C  CG  . ASN B 1 288 ? 8.409   8.557   52.011  1.00 18.37 ? 335 ASN B CG  1 
ATOM   4941 O  OD1 . ASN B 1 288 ? 8.575   9.749   51.744  1.00 19.14 ? 335 ASN B OD1 1 
ATOM   4942 N  ND2 . ASN B 1 288 ? 9.288   7.628   51.670  1.00 17.49 ? 335 ASN B ND2 1 
ATOM   4943 N  N   . GLY B 1 289 ? 5.949   7.920   56.219  1.00 19.60 ? 336 GLY B N   1 
ATOM   4944 C  CA  . GLY B 1 289 ? 4.690   7.813   56.938  1.00 22.76 ? 336 GLY B CA  1 
ATOM   4945 C  C   . GLY B 1 289 ? 3.865   6.615   56.494  1.00 22.17 ? 336 GLY B C   1 
ATOM   4946 O  O   . GLY B 1 289 ? 2.646   6.619   56.672  1.00 24.26 ? 336 GLY B O   1 
ATOM   4947 N  N   . GLY B 1 290 ? 4.520   5.626   55.856  1.00 19.38 ? 337 GLY B N   1 
ATOM   4948 C  CA  . GLY B 1 290 ? 3.817   4.436   55.419  1.00 18.90 ? 337 GLY B CA  1 
ATOM   4949 C  C   . GLY B 1 290 ? 3.409   4.479   53.945  1.00 17.28 ? 337 GLY B C   1 
ATOM   4950 O  O   . GLY B 1 290 ? 2.823   3.496   53.480  1.00 17.93 ? 337 GLY B O   1 
ATOM   4951 N  N   . ALA B 1 291 ? 3.689   5.561   53.227  1.00 16.50 ? 338 ALA B N   1 
ATOM   4952 C  CA  . ALA B 1 291 ? 3.249   5.711   51.847  1.00 16.91 ? 338 ALA B CA  1 
ATOM   4953 C  C   . ALA B 1 291 ? 3.895   4.618   51.007  1.00 15.80 ? 338 ALA B C   1 
ATOM   4954 O  O   . ALA B 1 291 ? 5.106   4.435   51.041  1.00 16.53 ? 338 ALA B O   1 
ATOM   4955 C  CB  . ALA B 1 291 ? 3.572   7.060   51.303  1.00 17.81 ? 338 ALA B CB  1 
ATOM   4956 N  N   . THR B 1 292 ? 3.070   3.896   50.235  1.00 16.30 ? 339 THR B N   1 
ATOM   4957 C  CA  . THR B 1 292 ? 3.500   2.696   49.532  1.00 16.01 ? 339 THR B CA  1 
ATOM   4958 C  C   . THR B 1 292 ? 2.879   2.744   48.138  1.00 15.88 ? 339 THR B C   1 
ATOM   4959 O  O   . THR B 1 292 ? 1.718   3.097   48.036  1.00 19.10 ? 339 THR B O   1 
ATOM   4960 C  CB  . THR B 1 292 ? 3.050   1.420   50.236  1.00 17.68 ? 339 THR B CB  1 
ATOM   4961 O  OG1 . THR B 1 292 ? 3.504   1.482   51.590  1.00 17.58 ? 339 THR B OG1 1 
ATOM   4962 C  CG2 . THR B 1 292 ? 3.655   0.185   49.607  1.00 17.70 ? 339 THR B CG2 1 
ATOM   4963 N  N   . LEU B 1 293 ? 3.665   2.388   47.106  1.00 15.42 ? 340 LEU B N   1 
ATOM   4964 C  CA  . LEU B 1 293 ? 3.297   2.529   45.698  1.00 16.69 ? 340 LEU B CA  1 
ATOM   4965 C  C   . LEU B 1 293 ? 3.317   1.180   45.005  1.00 13.42 ? 340 LEU B C   1 
ATOM   4966 O  O   . LEU B 1 293 ? 4.132   0.346   45.331  1.00 16.11 ? 340 LEU B O   1 
ATOM   4967 C  CB  . LEU B 1 293 ? 4.306   3.408   44.946  1.00 18.95 ? 340 LEU B CB  1 
ATOM   4968 C  CG  . LEU B 1 293 ? 4.532   4.799   45.514  1.00 22.78 ? 340 LEU B CG  1 
ATOM   4969 C  CD1 . LEU B 1 293 ? 5.631   5.547   44.773  1.00 24.90 ? 340 LEU B CD1 1 
ATOM   4970 C  CD2 . LEU B 1 293 ? 3.265   5.561   45.413  1.00 28.66 ? 340 LEU B CD2 1 
ATOM   4971 N  N   . LEU B 1 294 ? 2.496   1.013   43.956  1.00 13.36 ? 341 LEU B N   1 
ATOM   4972 C  CA  . LEU B 1 294 ? 2.677   -0.058  42.981  1.00 11.94 ? 341 LEU B CA  1 
ATOM   4973 C  C   . LEU B 1 294 ? 3.449   0.535   41.803  1.00 12.56 ? 341 LEU B C   1 
ATOM   4974 O  O   . LEU B 1 294 ? 2.912   1.344   41.057  1.00 13.76 ? 341 LEU B O   1 
ATOM   4975 C  CB  . LEU B 1 294 ? 1.338   -0.637  42.541  1.00 13.61 ? 341 LEU B CB  1 
ATOM   4976 C  CG  . LEU B 1 294 ? 1.429   -1.899  41.680  1.00 17.65 ? 341 LEU B CG  1 
ATOM   4977 C  CD1 . LEU B 1 294 ? 0.035   -2.530  41.649  1.00 20.94 ? 341 LEU B CD1 1 
ATOM   4978 C  CD2 . LEU B 1 294 ? 1.871   -1.626  40.302  1.00 22.66 ? 341 LEU B CD2 1 
ATOM   4979 N  N   . ARG B 1 295 ? 4.704   0.148   41.683  1.00 11.37 ? 342 ARG B N   1 
ATOM   4980 C  CA  . ARG B 1 295 ? 5.509   0.548   40.550  1.00 11.26 ? 342 ARG B CA  1 
ATOM   4981 C  C   . ARG B 1 295 ? 5.309   -0.477  39.444  1.00 12.21 ? 342 ARG B C   1 
ATOM   4982 O  O   . ARG B 1 295 ? 5.337   -1.685  39.672  1.00 13.28 ? 342 ARG B O   1 
ATOM   4983 C  CB  . ARG B 1 295 ? 6.969   0.621   40.973  1.00 11.53 ? 342 ARG B CB  1 
ATOM   4984 C  CG  . ARG B 1 295 ? 7.246   1.747   41.962  1.00 12.85 ? 342 ARG B CG  1 
ATOM   4985 C  CD  . ARG B 1 295 ? 8.715   1.791   42.407  1.00 13.60 ? 342 ARG B CD  1 
ATOM   4986 N  NE  . ARG B 1 295 ? 8.962   0.667   43.310  1.00 13.12 ? 342 ARG B NE  1 
ATOM   4987 C  CZ  . ARG B 1 295 ? 10.044  -0.067  43.385  1.00 13.34 ? 342 ARG B CZ  1 
ATOM   4988 N  NH1 . ARG B 1 295 ? 11.047  0.112   42.569  1.00 14.40 ? 342 ARG B NH1 1 
ATOM   4989 N  NH2 . ARG B 1 295 ? 10.175  -0.994  44.332  1.00 14.28 ? 342 ARG B NH2 1 
ATOM   4990 N  N   . ARG B 1 296 ? 5.139   0.039   38.243  1.00 10.90 ? 343 ARG B N   1 
ATOM   4991 C  CA  . ARG B 1 296 ? 4.929   -0.825  37.097  1.00 10.92 ? 343 ARG B CA  1 
ATOM   4992 C  C   . ARG B 1 296 ? 5.544   -0.185  35.880  1.00 11.67 ? 343 ARG B C   1 
ATOM   4993 O  O   . ARG B 1 296 ? 4.978   -0.233  34.790  1.00 11.94 ? 343 ARG B O   1 
ATOM   4994 C  CB  . ARG B 1 296 ? 3.428   -1.062  36.904  1.00 11.93 ? 343 ARG B CB  1 
ATOM   4995 C  CG  . ARG B 1 296 ? 3.111   -2.393  36.257  1.00 12.69 ? 343 ARG B CG  1 
ATOM   4996 C  CD  . ARG B 1 296 ? 1.626   -2.602  36.093  1.00 13.32 ? 343 ARG B CD  1 
ATOM   4997 N  NE  . ARG B 1 296 ? 1.274   -3.965  35.680  1.00 12.53 ? 343 ARG B NE  1 
ATOM   4998 C  CZ  . ARG B 1 296 ? 1.239   -4.415  34.429  1.00 12.22 ? 343 ARG B CZ  1 
ATOM   4999 N  NH1 . ARG B 1 296 ? 1.665   -3.629  33.465  1.00 12.33 ? 343 ARG B NH1 1 
ATOM   5000 N  NH2 . ARG B 1 296 ? 0.845   -5.638  34.144  1.00 12.13 ? 343 ARG B NH2 1 
ATOM   5001 N  N   . GLY B 1 297 ? 6.756   0.367   36.028  1.00 12.57 ? 344 GLY B N   1 
ATOM   5002 C  CA  . GLY B 1 297 ? 7.464   1.043   34.977  1.00 12.26 ? 344 GLY B CA  1 
ATOM   5003 C  C   . GLY B 1 297 ? 8.291   0.107   34.097  1.00 11.87 ? 344 GLY B C   1 
ATOM   5004 O  O   . GLY B 1 297 ? 8.430   -1.108  34.322  1.00 12.64 ? 344 GLY B O   1 
ATOM   5005 N  N   . TYR B 1 298 ? 8.804   0.736   33.051  1.00 11.39 ? 345 TYR B N   1 
ATOM   5006 C  CA  . TYR B 1 298 ? 9.495   0.041   31.996  1.00 12.38 ? 345 TYR B CA  1 
ATOM   5007 C  C   . TYR B 1 298 ? 10.717  0.835   31.637  1.00 12.72 ? 345 TYR B C   1 
ATOM   5008 O  O   . TYR B 1 298 ? 10.703  2.060   31.657  1.00 13.33 ? 345 TYR B O   1 
ATOM   5009 C  CB  . TYR B 1 298 ? 8.646   -0.109  30.735  1.00 12.49 ? 345 TYR B CB  1 
ATOM   5010 C  CG  . TYR B 1 298 ? 7.613   -1.190  30.891  1.00 11.78 ? 345 TYR B CG  1 
ATOM   5011 C  CD1 . TYR B 1 298 ? 6.446   -0.998  31.596  1.00 11.28 ? 345 TYR B CD1 1 
ATOM   5012 C  CD2 . TYR B 1 298 ? 7.778   -2.429  30.272  1.00 11.94 ? 345 TYR B CD2 1 
ATOM   5013 C  CE1 . TYR B 1 298 ? 5.506   -2.000  31.708  1.00 11.47 ? 345 TYR B CE1 1 
ATOM   5014 C  CE2 . TYR B 1 298 ? 6.863   -3.445  30.422  1.00 12.42 ? 345 TYR B CE2 1 
ATOM   5015 C  CZ  . TYR B 1 298 ? 5.708   -3.225  31.137  1.00 12.68 ? 345 TYR B CZ  1 
ATOM   5016 O  OH  . TYR B 1 298 ? 4.784   -4.228  31.274  1.00 13.99 ? 345 TYR B OH  1 
ATOM   5017 N  N   . SER B 1 299 ? 11.774  0.127   31.292  1.00 13.60 ? 346 SER B N   1 
ATOM   5018 C  CA  . SER B 1 299 ? 12.925  0.825   30.749  1.00 12.80 ? 346 SER B CA  1 
ATOM   5019 C  C   . SER B 1 299 ? 12.672  1.351   29.353  1.00 13.79 ? 346 SER B C   1 
ATOM   5020 O  O   . SER B 1 299 ? 11.841  0.805   28.618  1.00 13.85 ? 346 SER B O   1 
ATOM   5021 C  CB  . SER B 1 299 ? 14.114  -0.117  30.708  1.00 14.16 ? 346 SER B CB  1 
ATOM   5022 O  OG  . SER B 1 299 ? 14.476  -0.547  32.001  1.00 16.48 ? 346 SER B OG  1 
ATOM   5023 N  N   . PHE B 1 300 ? 13.392  2.389   28.930  1.00 13.30 ? 347 PHE B N   1 
ATOM   5024 C  CA  . PHE B 1 300 ? 13.300  2.843   27.575  1.00 13.61 ? 347 PHE B CA  1 
ATOM   5025 C  C   . PHE B 1 300 ? 14.678  3.136   27.063  1.00 14.55 ? 347 PHE B C   1 
ATOM   5026 O  O   . PHE B 1 300 ? 15.585  3.445   27.821  1.00 15.71 ? 347 PHE B O   1 
ATOM   5027 C  CB  . PHE B 1 300 ? 12.395  4.057   27.377  1.00 14.57 ? 347 PHE B CB  1 
ATOM   5028 C  CG  . PHE B 1 300 ? 12.909  5.365   27.956  1.00 14.98 ? 347 PHE B CG  1 
ATOM   5029 C  CD1 . PHE B 1 300 ? 13.752  6.191   27.224  1.00 17.12 ? 347 PHE B CD1 1 
ATOM   5030 C  CD2 . PHE B 1 300 ? 12.531  5.782   29.219  1.00 16.50 ? 347 PHE B CD2 1 
ATOM   5031 C  CE1 . PHE B 1 300 ? 14.197  7.408   27.743  1.00 17.17 ? 347 PHE B CE1 1 
ATOM   5032 C  CE2 . PHE B 1 300 ? 12.972  6.999   29.708  1.00 16.36 ? 347 PHE B CE2 1 
ATOM   5033 C  CZ  . PHE B 1 300 ? 13.792  7.795   28.977  1.00 16.48 ? 347 PHE B CZ  1 
ATOM   5034 N  N   . THR B 1 301 ? 14.824  2.963   25.770  1.00 15.13 ? 348 THR B N   1 
ATOM   5035 C  CA  . THR B 1 301 ? 16.007  3.414   25.082  1.00 15.27 ? 348 THR B CA  1 
ATOM   5036 C  C   . THR B 1 301 ? 15.504  3.872   23.731  1.00 16.85 ? 348 THR B C   1 
ATOM   5037 O  O   . THR B 1 301 ? 15.014  3.032   22.962  1.00 18.20 ? 348 THR B O   1 
ATOM   5038 C  CB  . THR B 1 301 ? 17.057  2.326   24.913  1.00 17.45 ? 348 THR B CB  1 
ATOM   5039 O  OG1 . THR B 1 301 ? 17.487  1.821   26.183  1.00 18.94 ? 348 THR B OG1 1 
ATOM   5040 C  CG2 . THR B 1 301 ? 18.273  2.888   24.200  1.00 20.69 ? 348 THR B CG2 1 
ATOM   5041 N  N   . ASP B 1 302 ? 15.575  5.174   23.483  1.00 15.77 ? 349 ASP B N   1 
ATOM   5042 C  CA  . ASP B 1 302 ? 14.945  5.775   22.330  1.00 18.63 ? 349 ASP B CA  1 
ATOM   5043 C  C   . ASP B 1 302 ? 15.952  5.976   21.201  1.00 21.03 ? 349 ASP B C   1 
ATOM   5044 O  O   . ASP B 1 302 ? 15.540  6.101   20.044  1.00 25.34 ? 349 ASP B O   1 
ATOM   5045 C  CB  . ASP B 1 302 ? 14.133  6.978   22.778  1.00 21.23 ? 349 ASP B CB  1 
ATOM   5046 C  CG  . ASP B 1 302 ? 12.838  6.588   23.482  1.00 22.87 ? 349 ASP B CG  1 
ATOM   5047 O  OD1 . ASP B 1 302 ? 12.460  5.408   23.411  1.00 24.32 ? 349 ASP B OD1 1 
ATOM   5048 O  OD2 . ASP B 1 302 ? 12.232  7.446   24.106  1.00 25.19 ? 349 ASP B OD2 1 
ATOM   5049 N  N   . GLY B 1 303 ? 17.239  5.972   21.529  1.00 18.28 ? 350 GLY B N   1 
ATOM   5050 C  CA  . GLY B 1 303 ? 18.258  6.333   20.551  1.00 18.18 ? 350 GLY B CA  1 
ATOM   5051 C  C   . GLY B 1 303 ? 19.353  7.167   21.189  1.00 17.65 ? 350 GLY B C   1 
ATOM   5052 O  O   . GLY B 1 303 ? 19.670  6.941   22.345  1.00 18.18 ? 350 GLY B O   1 
ATOM   5053 N  N   . THR B 1 304 ? 19.965  8.019   20.397  1.00 19.77 ? 351 THR B N   1 
ATOM   5054 C  CA  . THR B 1 304 ? 21.035  8.871   20.909  1.00 20.03 ? 351 THR B CA  1 
ATOM   5055 C  C   . THR B 1 304 ? 20.682  10.302  20.567  1.00 22.60 ? 351 THR B C   1 
ATOM   5056 O  O   . THR B 1 304 ? 20.061  10.574  19.540  1.00 24.63 ? 351 THR B O   1 
ATOM   5057 C  CB  . THR B 1 304 ? 22.404  8.460   20.387  1.00 26.01 ? 351 THR B CB  1 
ATOM   5058 O  OG1 . THR B 1 304 ? 22.355  8.168   19.003  1.00 23.51 ? 351 THR B OG1 1 
ATOM   5059 C  CG2 . THR B 1 304 ? 22.896  7.173   21.034  1.00 29.82 ? 351 THR B CG2 1 
ATOM   5060 N  N   . ASP B 1 305 ? 21.072  11.209  21.464  1.00 24.56 ? 352 ASP B N   1 
ATOM   5061 C  CA  . ASP B 1 305 ? 20.773  12.623  21.301  1.00 29.34 ? 352 ASP B CA  1 
ATOM   5062 C  C   . ASP B 1 305 ? 21.853  13.271  20.434  1.00 28.30 ? 352 ASP B C   1 
ATOM   5063 O  O   . ASP B 1 305 ? 22.721  12.604  19.873  1.00 30.68 ? 352 ASP B O   1 
ATOM   5064 C  CB  . ASP B 1 305 ? 20.590  13.296  22.651  1.00 29.59 ? 352 ASP B CB  1 
ATOM   5065 C  CG  . ASP B 1 305 ? 21.815  13.380  23.553  1.00 27.76 ? 352 ASP B CG  1 
ATOM   5066 O  OD1 . ASP B 1 305 ? 22.945  13.227  23.031  1.00 26.75 ? 352 ASP B OD1 1 
ATOM   5067 O  OD2 . ASP B 1 305 ? 21.591  13.530  24.772  1.00 31.29 ? 352 ASP B OD2 1 
ATOM   5068 N  N   . GLY B 1 306 ? 21.777  14.599  20.307  1.00 38.81 ? 353 GLY B N   1 
ATOM   5069 C  CA  . GLY B 1 306 ? 22.655  15.342  19.420  1.00 40.38 ? 353 GLY B CA  1 
ATOM   5070 C  C   . GLY B 1 306 ? 24.115  15.337  19.863  1.00 42.54 ? 353 GLY B C   1 
ATOM   5071 O  O   . GLY B 1 306 ? 24.991  15.608  19.046  1.00 44.56 ? 353 GLY B O   1 
ATOM   5072 N  N   . LEU B 1 307 ? 24.371  15.014  21.141  1.00 43.08 ? 354 LEU B N   1 
ATOM   5073 C  CA  . LEU B 1 307 ? 25.726  14.983  21.677  1.00 42.31 ? 354 LEU B CA  1 
ATOM   5074 C  C   . LEU B 1 307 ? 26.317  13.575  21.622  1.00 38.00 ? 354 LEU B C   1 
ATOM   5075 O  O   . LEU B 1 307 ? 27.455  13.376  22.021  1.00 37.92 ? 354 LEU B O   1 
ATOM   5076 C  CB  . LEU B 1 307 ? 25.721  15.555  23.097  1.00 48.75 ? 354 LEU B CB  1 
ATOM   5077 C  CG  . LEU B 1 307 ? 25.349  17.042  23.219  1.00 58.61 ? 354 LEU B CG  1 
ATOM   5078 C  CD1 . LEU B 1 307 ? 25.340  17.555  24.652  1.00 59.27 ? 354 LEU B CD1 1 
ATOM   5079 C  CD2 . LEU B 1 307 ? 26.293  17.901  22.384  1.00 60.73 ? 354 LEU B CD2 1 
ATOM   5080 N  N   . GLY B 1 308 ? 25.549  12.600  21.111  1.00 28.99 ? 355 GLY B N   1 
ATOM   5081 C  CA  . GLY B 1 308 ? 26.005  11.228  20.994  1.00 27.27 ? 355 GLY B CA  1 
ATOM   5082 C  C   . GLY B 1 308 ? 25.716  10.424  22.261  1.00 22.97 ? 355 GLY B C   1 
ATOM   5083 O  O   . GLY B 1 308 ? 26.209  9.311   22.395  1.00 28.83 ? 355 GLY B O   1 
ATOM   5084 N  N   . ARG B 1 309 ? 24.911  10.985  23.179  1.00 20.97 ? 356 ARG B N   1 
ATOM   5085 C  CA  . ARG B 1 309 ? 24.630  10.326  24.443  1.00 21.53 ? 356 ARG B CA  1 
ATOM   5086 C  C   . ARG B 1 309 ? 23.400  9.442   24.307  1.00 19.18 ? 356 ARG B C   1 
ATOM   5087 O  O   . ARG B 1 309 ? 22.511  9.754   23.522  1.00 20.99 ? 356 ARG B O   1 
ATOM   5088 C  CB  . ARG B 1 309 ? 24.344  11.386  25.511  1.00 25.46 ? 356 ARG B CB  1 
ATOM   5089 C  CG  . ARG B 1 309 ? 25.557  12.270  25.783  1.00 31.67 ? 356 ARG B CG  1 
ATOM   5090 C  CD  . ARG B 1 309 ? 25.246  13.279  26.865  1.00 38.60 ? 356 ARG B CD  1 
ATOM   5091 N  NE  . ARG B 1 309 ? 24.268  14.262  26.379  1.00 50.17 ? 356 ARG B NE  1 
ATOM   5092 C  CZ  . ARG B 1 309 ? 23.703  15.215  27.117  1.00 58.77 ? 356 ARG B CZ  1 
ATOM   5093 N  NH1 . ARG B 1 309 ? 23.960  15.297  28.415  1.00 62.59 ? 356 ARG B NH1 1 
ATOM   5094 N  NH2 . ARG B 1 309 ? 22.874  16.080  26.555  1.00 60.16 ? 356 ARG B NH2 1 
ATOM   5095 N  N   . LEU B 1 310 ? 23.323  8.394   25.123  1.00 17.50 ? 357 LEU B N   1 
ATOM   5096 C  CA  . LEU B 1 310 ? 22.205  7.463   25.044  1.00 18.60 ? 357 LEU B CA  1 
ATOM   5097 C  C   . LEU B 1 310 ? 20.965  8.096   25.637  1.00 19.68 ? 357 LEU B C   1 
ATOM   5098 O  O   . LEU B 1 310 ? 21.019  8.509   26.786  1.00 22.37 ? 357 LEU B O   1 
ATOM   5099 C  CB  . LEU B 1 310 ? 22.620  6.175   25.763  1.00 22.91 ? 357 LEU B CB  1 
ATOM   5100 C  CG  . LEU B 1 310 ? 21.882  4.894   25.366  1.00 29.70 ? 357 LEU B CG  1 
ATOM   5101 C  CD1 . LEU B 1 310 ? 22.178  4.474   23.947  1.00 30.73 ? 357 LEU B CD1 1 
ATOM   5102 C  CD2 . LEU B 1 310 ? 22.184  3.786   26.341  1.00 30.45 ? 357 LEU B CD2 1 
ATOM   5103 N  N   . ASP B 1 311 ? 19.866  8.163   24.859  1.00 15.77 ? 358 ASP B N   1 
ATOM   5104 C  CA  . ASP B 1 311 ? 18.579  8.651   25.337  1.00 16.19 ? 358 ASP B CA  1 
ATOM   5105 C  C   . ASP B 1 311 ? 17.852  7.463   25.923  1.00 17.03 ? 358 ASP B C   1 
ATOM   5106 O  O   . ASP B 1 311 ? 17.192  6.718   25.208  1.00 17.36 ? 358 ASP B O   1 
ATOM   5107 C  CB  . ASP B 1 311 ? 17.783  9.266   24.197  1.00 18.48 ? 358 ASP B CB  1 
ATOM   5108 C  CG  . ASP B 1 311 ? 16.486  9.933   24.605  1.00 23.20 ? 358 ASP B CG  1 
ATOM   5109 O  OD1 . ASP B 1 311 ? 16.173  9.905   25.806  1.00 22.29 ? 358 ASP B OD1 1 
ATOM   5110 O  OD2 . ASP B 1 311 ? 15.812  10.448  23.701  1.00 27.25 ? 358 ASP B OD2 1 
ATOM   5111 N  N   . ALA B 1 312 ? 18.044  7.269   27.217  1.00 14.95 ? 359 ALA B N   1 
ATOM   5112 C  CA  . ALA B 1 312 ? 17.619  6.050   27.851  1.00 15.19 ? 359 ALA B CA  1 
ATOM   5113 C  C   . ALA B 1 312 ? 17.219  6.421   29.257  1.00 14.90 ? 359 ALA B C   1 
ATOM   5114 O  O   . ALA B 1 312 ? 17.702  7.425   29.788  1.00 16.17 ? 359 ALA B O   1 
ATOM   5115 C  CB  . ALA B 1 312 ? 18.729  5.046   27.832  1.00 16.89 ? 359 ALA B CB  1 
ATOM   5116 N  N   . GLY B 1 313 ? 16.427  5.583   29.859  1.00 13.91 ? 360 GLY B N   1 
ATOM   5117 C  CA  . GLY B 1 313 ? 16.064  5.782   31.245  1.00 14.21 ? 360 GLY B CA  1 
ATOM   5118 C  C   . GLY B 1 313 ? 14.947  4.854   31.666  1.00 14.61 ? 360 GLY B C   1 
ATOM   5119 O  O   . GLY B 1 313 ? 14.858  3.705   31.230  1.00 14.70 ? 360 GLY B O   1 
ATOM   5120 N  N   . LEU B 1 314 ? 14.094  5.371   32.542  1.00 14.35 ? 361 LEU B N   1 
ATOM   5121 C  CA  . LEU B 1 314 ? 13.021  4.624   33.142  1.00 12.88 ? 361 LEU B CA  1 
ATOM   5122 C  C   . LEU B 1 314 ? 11.764  5.419   32.883  1.00 13.94 ? 361 LEU B C   1 
ATOM   5123 O  O   . LEU B 1 314 ? 11.692  6.593   33.189  1.00 13.22 ? 361 LEU B O   1 
ATOM   5124 C  CB  . LEU B 1 314 ? 13.252  4.400   34.632  1.00 15.72 ? 361 LEU B CB  1 
ATOM   5125 C  CG  . LEU B 1 314 ? 12.074  3.791   35.392  1.00 19.41 ? 361 LEU B CG  1 
ATOM   5126 C  CD1 . LEU B 1 314 ? 11.789  2.392   34.948  1.00 23.37 ? 361 LEU B CD1 1 
ATOM   5127 C  CD2 . LEU B 1 314 ? 12.365  3.848   36.881  1.00 21.95 ? 361 LEU B CD2 1 
ATOM   5128 N  N   . PHE B 1 315 ? 10.790  4.775   32.242  1.00 11.70 ? 362 PHE B N   1 
ATOM   5129 C  CA  . PHE B 1 315 ? 9.455   5.314   32.125  1.00 11.56 ? 362 PHE B CA  1 
ATOM   5130 C  C   . PHE B 1 315 ? 8.703   4.797   33.335  1.00 11.73 ? 362 PHE B C   1 
ATOM   5131 O  O   . PHE B 1 315 ? 8.222   3.675   33.415  1.00 12.15 ? 362 PHE B O   1 
ATOM   5132 C  CB  . PHE B 1 315 ? 8.791   4.882   30.810  1.00 10.90 ? 362 PHE B CB  1 
ATOM   5133 C  CG  . PHE B 1 315 ? 7.453   5.572   30.588  1.00 12.24 ? 362 PHE B CG  1 
ATOM   5134 C  CD1 . PHE B 1 315 ? 7.381   6.924   30.338  1.00 15.10 ? 362 PHE B CD1 1 
ATOM   5135 C  CD2 . PHE B 1 315 ? 6.279   4.845   30.560  1.00 13.07 ? 362 PHE B CD2 1 
ATOM   5136 C  CE1 . PHE B 1 315 ? 6.163   7.538   30.105  1.00 15.11 ? 362 PHE B CE1 1 
ATOM   5137 C  CE2 . PHE B 1 315 ? 5.061   5.476   30.341  1.00 14.27 ? 362 PHE B CE2 1 
ATOM   5138 C  CZ  . PHE B 1 315 ? 5.010   6.808   30.067  1.00 14.16 ? 362 PHE B CZ  1 
ATOM   5139 N  N   . PHE B 1 316 ? 8.680   5.643   34.359  1.00 11.25 ? 363 PHE B N   1 
ATOM   5140 C  CA  . PHE B 1 316 ? 8.181   5.309   35.675  1.00 11.74 ? 363 PHE B CA  1 
ATOM   5141 C  C   . PHE B 1 316 ? 6.668   5.419   35.671  1.00 11.99 ? 363 PHE B C   1 
ATOM   5142 O  O   . PHE B 1 316 ? 6.120   6.423   35.273  1.00 12.79 ? 363 PHE B O   1 
ATOM   5143 C  CB  . PHE B 1 316 ? 8.816   6.320   36.631  1.00 12.00 ? 363 PHE B CB  1 
ATOM   5144 C  CG  . PHE B 1 316 ? 8.441   6.078   38.069  1.00 13.41 ? 363 PHE B CG  1 
ATOM   5145 C  CD1 . PHE B 1 316 ? 9.214   5.227   38.857  1.00 14.20 ? 363 PHE B CD1 1 
ATOM   5146 C  CD2 . PHE B 1 316 ? 7.321   6.656   38.620  1.00 15.12 ? 363 PHE B CD2 1 
ATOM   5147 C  CE1 . PHE B 1 316 ? 8.828   4.969   40.172  1.00 14.16 ? 363 PHE B CE1 1 
ATOM   5148 C  CE2 . PHE B 1 316 ? 7.001   6.413   39.946  1.00 14.00 ? 363 PHE B CE2 1 
ATOM   5149 C  CZ  . PHE B 1 316 ? 7.731   5.569   40.667  1.00 13.85 ? 363 PHE B CZ  1 
ATOM   5150 N  N   . LEU B 1 317 ? 6.023   4.342   36.089  1.00 11.12 ? 364 LEU B N   1 
ATOM   5151 C  CA  . LEU B 1 317 ? 4.605   4.297   36.244  1.00 11.30 ? 364 LEU B CA  1 
ATOM   5152 C  C   . LEU B 1 317 ? 4.298   3.868   37.659  1.00 12.50 ? 364 LEU B C   1 
ATOM   5153 O  O   . LEU B 1 317 ? 4.779   2.827   38.140  1.00 14.13 ? 364 LEU B O   1 
ATOM   5154 C  CB  . LEU B 1 317 ? 3.985   3.330   35.228  1.00 11.37 ? 364 LEU B CB  1 
ATOM   5155 C  CG  . LEU B 1 317 ? 4.152   3.745   33.768  1.00 11.87 ? 364 LEU B CG  1 
ATOM   5156 C  CD1 . LEU B 1 317 ? 3.713   2.605   32.828  1.00 14.29 ? 364 LEU B CD1 1 
ATOM   5157 C  CD2 . LEU B 1 317 ? 3.369   5.024   33.485  1.00 13.53 ? 364 LEU B CD2 1 
ATOM   5158 N  N   . ALA B 1 318 ? 3.488   4.659   38.343  1.00 11.95 ? 365 ALA B N   1 
ATOM   5159 C  CA  . ALA B 1 318 ? 3.063   4.281   39.666  1.00 11.77 ? 365 ALA B CA  1 
ATOM   5160 C  C   . ALA B 1 318 ? 1.560   4.376   39.749  1.00 11.04 ? 365 ALA B C   1 
ATOM   5161 O  O   . ALA B 1 318 ? 0.985   5.377   39.345  1.00 11.84 ? 365 ALA B O   1 
ATOM   5162 C  CB  . ALA B 1 318 ? 3.653   5.151   40.733  1.00 14.39 ? 365 ALA B CB  1 
ATOM   5163 N  N   . TYR B 1 319 ? 0.977   3.354   40.342  1.00 11.23 ? 366 TYR B N   1 
ATOM   5164 C  CA  . TYR B 1 319 ? -0.428  3.290   40.627  1.00 11.03 ? 366 TYR B CA  1 
ATOM   5165 C  C   . TYR B 1 319 ? -0.614  3.427   42.122  1.00 11.16 ? 366 TYR B C   1 
ATOM   5166 O  O   . TYR B 1 319 ? 0.169   2.890   42.903  1.00 12.61 ? 366 TYR B O   1 
ATOM   5167 C  CB  . TYR B 1 319 ? -1.034  1.974   40.133  1.00 11.31 ? 366 TYR B CB  1 
ATOM   5168 C  CG  . TYR B 1 319 ? -1.145  1.861   38.635  1.00 11.41 ? 366 TYR B CG  1 
ATOM   5169 C  CD1 . TYR B 1 319 ? -2.251  2.352   37.967  1.00 11.39 ? 366 TYR B CD1 1 
ATOM   5170 C  CD2 . TYR B 1 319 ? -0.143  1.290   37.859  1.00 12.91 ? 366 TYR B CD2 1 
ATOM   5171 C  CE1 . TYR B 1 319 ? -2.367  2.264   36.608  1.00 12.19 ? 366 TYR B CE1 1 
ATOM   5172 C  CE2 . TYR B 1 319 ? -0.219  1.234   36.483  1.00 13.92 ? 366 TYR B CE2 1 
ATOM   5173 C  CZ  . TYR B 1 319 ? -1.349  1.688   35.864  1.00 13.51 ? 366 TYR B CZ  1 
ATOM   5174 O  OH  . TYR B 1 319 ? -1.535  1.647   34.505  1.00 14.68 ? 366 TYR B OH  1 
ATOM   5175 N  N   . GLN B 1 320 ? -1.669  4.130   42.484  1.00 10.78 ? 367 GLN B N   1 
ATOM   5176 C  CA  . GLN B 1 320 ? -1.941  4.407   43.873  1.00 11.62 ? 367 GLN B CA  1 
ATOM   5177 C  C   . GLN B 1 320 ? -3.407  4.805   44.037  1.00 11.40 ? 367 GLN B C   1 
ATOM   5178 O  O   . GLN B 1 320 ? -4.038  5.277   43.146  1.00 11.56 ? 367 GLN B O   1 
ATOM   5179 C  CB  . GLN B 1 320 ? -1.098  5.554   44.411  1.00 12.27 ? 367 GLN B CB  1 
ATOM   5180 C  CG  . GLN B 1 320 ? -1.274  6.861   43.655  1.00 12.99 ? 367 GLN B CG  1 
ATOM   5181 C  CD  . GLN B 1 320 ? -0.115  7.169   42.754  1.00 14.18 ? 367 GLN B CD  1 
ATOM   5182 O  OE1 . GLN B 1 320 ? -0.117  6.984   41.529  1.00 15.49 ? 367 GLN B OE1 1 
ATOM   5183 N  NE2 . GLN B 1 320 ? 0.943   7.617   43.349  1.00 16.13 ? 367 GLN B NE2 1 
ATOM   5184 N  N   . ARG B 1 321 ? -3.876  4.682   45.293  1.00 11.79 ? 368 ARG B N   1 
ATOM   5185 C  CA  . ARG B 1 321 ? -5.239  5.033   45.665  1.00 12.33 ? 368 ARG B CA  1 
ATOM   5186 C  C   . ARG B 1 321 ? -5.506  6.529   45.689  1.00 12.65 ? 368 ARG B C   1 
ATOM   5187 O  O   . ARG B 1 321 ? -6.644  6.963   45.488  1.00 13.78 ? 368 ARG B O   1 
ATOM   5188 C  CB  . ARG B 1 321 ? -5.457  4.399   47.041  1.00 13.54 ? 368 ARG B CB  1 
ATOM   5189 C  CG  . ARG B 1 321 ? -6.837  4.634   47.655  1.00 14.30 ? 368 ARG B CG  1 
ATOM   5190 C  CD  . ARG B 1 321 ? -6.983  3.687   48.788  1.00 16.23 ? 368 ARG B CD  1 
ATOM   5191 N  NE  . ARG B 1 321 ? -8.252  4.003   49.459  1.00 17.14 ? 368 ARG B NE  1 
ATOM   5192 C  CZ  . ARG B 1 321 ? -8.599  3.405   50.580  1.00 21.86 ? 368 ARG B CZ  1 
ATOM   5193 N  NH1 . ARG B 1 321 ? -7.771  2.527   51.113  1.00 25.06 ? 368 ARG B NH1 1 
ATOM   5194 N  NH2 . ARG B 1 321 ? -9.748  3.740   51.166  1.00 20.46 ? 368 ARG B NH2 1 
ATOM   5195 N  N   . ASP B 1 322 ? -4.440  7.309   45.889  1.00 12.12 ? 369 ASP B N   1 
ATOM   5196 C  CA  . ASP B 1 322 ? -4.559  8.770   45.930  1.00 12.87 ? 369 ASP B CA  1 
ATOM   5197 C  C   . ASP B 1 322 ? -3.190  9.353   45.620  1.00 13.09 ? 369 ASP B C   1 
ATOM   5198 O  O   . ASP B 1 322 ? -2.222  9.040   46.306  1.00 14.03 ? 369 ASP B O   1 
ATOM   5199 C  CB  . ASP B 1 322 ? -5.029  9.218   47.306  1.00 13.96 ? 369 ASP B CB  1 
ATOM   5200 C  CG  . ASP B 1 322 ? -5.463  10.677  47.412  1.00 15.08 ? 369 ASP B CG  1 
ATOM   5201 O  OD1 . ASP B 1 322 ? -4.840  11.544  46.776  1.00 14.84 ? 369 ASP B OD1 1 
ATOM   5202 O  OD2 . ASP B 1 322 ? -6.466  10.932  48.151  1.00 19.16 ? 369 ASP B OD2 1 
ATOM   5203 N  N   . ILE B 1 323 ? -3.110  10.204  44.604  1.00 12.45 ? 370 ILE B N   1 
ATOM   5204 C  CA  . ILE B 1 323 ? -1.827  10.808  44.258  1.00 13.25 ? 370 ILE B CA  1 
ATOM   5205 C  C   . ILE B 1 323 ? -1.244  11.573  45.439  1.00 13.78 ? 370 ILE B C   1 
ATOM   5206 O  O   . ILE B 1 323 ? -0.035  11.575  45.623  1.00 14.82 ? 370 ILE B O   1 
ATOM   5207 C  CB  . ILE B 1 323 ? -1.971  11.664  43.006  1.00 14.39 ? 370 ILE B CB  1 
ATOM   5208 C  CG1 . ILE B 1 323 ? -2.266  10.688  41.865  1.00 16.84 ? 370 ILE B CG1 1 
ATOM   5209 C  CG2 . ILE B 1 323 ? -0.746  12.542  42.713  1.00 16.70 ? 370 ILE B CG2 1 
ATOM   5210 C  CD1 . ILE B 1 323 ? -2.529  11.385  40.561  1.00 17.37 ? 370 ILE B CD1 1 
ATOM   5211 N  N   . ARG B 1 324 ? -2.090  12.201  46.236  1.00 13.89 ? 371 ARG B N   1 
ATOM   5212 C  CA  . ARG B 1 324 ? -1.606  13.045  47.322  1.00 14.54 ? 371 ARG B CA  1 
ATOM   5213 C  C   . ARG B 1 324 ? -0.951  12.246  48.444  1.00 16.12 ? 371 ARG B C   1 
ATOM   5214 O  O   . ARG B 1 324 ? -0.143  12.810  49.215  1.00 17.60 ? 371 ARG B O   1 
ATOM   5215 C  CB  . ARG B 1 324 ? -2.770  13.827  47.935  1.00 15.66 ? 371 ARG B CB  1 
ATOM   5216 C  CG  . ARG B 1 324 ? -3.451  14.716  46.902  1.00 17.26 ? 371 ARG B CG  1 
ATOM   5217 C  CD  . ARG B 1 324 ? -4.758  15.283  47.373  1.00 17.80 ? 371 ARG B CD  1 
ATOM   5218 N  NE  . ARG B 1 324 ? -5.771  14.256  47.600  1.00 18.55 ? 371 ARG B NE  1 
ATOM   5219 C  CZ  . ARG B 1 324 ? -6.976  14.445  48.049  1.00 22.02 ? 371 ARG B CZ  1 
ATOM   5220 N  NH1 . ARG B 1 324 ? -7.366  15.697  48.319  1.00 23.88 ? 371 ARG B NH1 1 
ATOM   5221 N  NH2 . ARG B 1 324 ? -7.768  13.426  48.172  1.00 22.62 ? 371 ARG B NH2 1 
ATOM   5222 N  N   . THR B 1 325 ? -1.248  10.947  48.568  1.00 15.41 ? 372 THR B N   1 
ATOM   5223 C  CA  . THR B 1 325 ? -0.679  10.110  49.615  1.00 15.85 ? 372 THR B CA  1 
ATOM   5224 C  C   . THR B 1 325 ? 0.218   9.005   49.083  1.00 15.45 ? 372 THR B C   1 
ATOM   5225 O  O   . THR B 1 325 ? 0.670   8.141   49.838  1.00 17.66 ? 372 THR B O   1 
ATOM   5226 C  CB  . THR B 1 325 ? -1.770  9.509   50.482  1.00 18.02 ? 372 THR B CB  1 
ATOM   5227 O  OG1 . THR B 1 325 ? -2.539  8.664   49.630  1.00 19.08 ? 372 THR B OG1 1 
ATOM   5228 C  CG2 . THR B 1 325 ? -2.631  10.587  51.133  1.00 21.84 ? 372 THR B CG2 1 
ATOM   5229 N  N   . GLY B 1 326 ? 0.467   8.990   47.785  1.00 15.59 ? 373 GLY B N   1 
ATOM   5230 C  CA  . GLY B 1 326 ? 1.333   7.987   47.200  1.00 14.91 ? 373 GLY B CA  1 
ATOM   5231 C  C   . GLY B 1 326 ? 2.534   8.699   46.605  1.00 14.05 ? 373 GLY B C   1 
ATOM   5232 O  O   . GLY B 1 326 ? 3.526   8.954   47.270  1.00 14.91 ? 373 GLY B O   1 
ATOM   5233 N  N   . PHE B 1 327 ? 2.474   8.974   45.312  1.00 13.64 ? 374 PHE B N   1 
ATOM   5234 C  CA  . PHE B 1 327 ? 3.642   9.542   44.648  1.00 13.49 ? 374 PHE B CA  1 
ATOM   5235 C  C   . PHE B 1 327 ? 4.138   10.841  45.272  1.00 13.49 ? 374 PHE B C   1 
ATOM   5236 O  O   . PHE B 1 327 ? 5.339   11.040  45.370  1.00 14.29 ? 374 PHE B O   1 
ATOM   5237 C  CB  . PHE B 1 327 ? 3.272   9.763   43.183  1.00 13.19 ? 374 PHE B CB  1 
ATOM   5238 C  CG  . PHE B 1 327 ? 4.424   10.347  42.402  1.00 13.16 ? 374 PHE B CG  1 
ATOM   5239 C  CD1 . PHE B 1 327 ? 5.421   9.534   41.883  1.00 13.92 ? 374 PHE B CD1 1 
ATOM   5240 C  CD2 . PHE B 1 327 ? 4.502   11.717  42.174  1.00 13.09 ? 374 PHE B CD2 1 
ATOM   5241 C  CE1 . PHE B 1 327 ? 6.463   10.057  41.173  1.00 14.19 ? 374 PHE B CE1 1 
ATOM   5242 C  CE2 . PHE B 1 327 ? 5.563   12.238  41.439  1.00 13.42 ? 374 PHE B CE2 1 
ATOM   5243 C  CZ  . PHE B 1 327 ? 6.523   11.398  40.944  1.00 13.10 ? 374 PHE B CZ  1 
ATOM   5244 N  N   . VAL B 1 328 ? 3.240   11.771  45.598  1.00 14.84 ? 375 VAL B N   1 
ATOM   5245 C  CA  . VAL B 1 328 ? 3.660   13.105  45.968  1.00 14.47 ? 375 VAL B CA  1 
ATOM   5246 C  C   . VAL B 1 328 ? 4.550   13.047  47.203  1.00 14.97 ? 375 VAL B C   1 
ATOM   5247 O  O   . VAL B 1 328 ? 5.668   13.575  47.135  1.00 13.58 ? 375 VAL B O   1 
ATOM   5248 C  CB  . VAL B 1 328 ? 2.510   14.092  46.128  1.00 14.78 ? 375 VAL B CB  1 
ATOM   5249 C  CG1 . VAL B 1 328 ? 2.974   15.367  46.819  1.00 16.20 ? 375 VAL B CG1 1 
ATOM   5250 C  CG2 . VAL B 1 328 ? 1.878   14.413  44.796  1.00 15.65 ? 375 VAL B CG2 1 
ATOM   5251 N  N   . PRO B 1 329 ? 4.172   12.427  48.334  1.00 14.29 ? 376 PRO B N   1 
ATOM   5252 C  CA  . PRO B 1 329 ? 5.075   12.421  49.490  1.00 13.82 ? 376 PRO B CA  1 
ATOM   5253 C  C   . PRO B 1 329 ? 6.395   11.733  49.195  1.00 14.95 ? 376 PRO B C   1 
ATOM   5254 O  O   . PRO B 1 329 ? 7.447   12.196  49.623  1.00 15.94 ? 376 PRO B O   1 
ATOM   5255 C  CB  . PRO B 1 329 ? 4.375   11.726  50.604  1.00 16.20 ? 376 PRO B CB  1 
ATOM   5256 C  CG  . PRO B 1 329 ? 3.096   11.244  50.005  1.00 18.46 ? 376 PRO B CG  1 
ATOM   5257 C  CD  . PRO B 1 329 ? 2.866   11.850  48.646  1.00 15.76 ? 376 PRO B CD  1 
ATOM   5258 N  N   . VAL B 1 330 ? 6.362   10.636  48.423  1.00 13.65 ? 377 VAL B N   1 
ATOM   5259 C  CA  . VAL B 1 330 ? 7.569   9.878   48.194  1.00 14.06 ? 377 VAL B CA  1 
ATOM   5260 C  C   . VAL B 1 330 ? 8.512   10.712  47.333  1.00 13.16 ? 377 VAL B C   1 
ATOM   5261 O  O   . VAL B 1 330 ? 9.687   10.859  47.640  1.00 15.15 ? 377 VAL B O   1 
ATOM   5262 C  CB  . VAL B 1 330 ? 7.307   8.475   47.607  1.00 14.75 ? 377 VAL B CB  1 
ATOM   5263 C  CG1 . VAL B 1 330 ? 8.625   7.748   47.344  1.00 15.79 ? 377 VAL B CG1 1 
ATOM   5264 C  CG2 . VAL B 1 330 ? 6.464   7.627   48.553  1.00 16.45 ? 377 VAL B CG2 1 
ATOM   5265 N  N   . GLN B 1 331 ? 8.015   11.259  46.212  1.00 12.27 ? 378 GLN B N   1 
ATOM   5266 C  CA  . GLN B 1 331 ? 8.841   12.070  45.344  1.00 12.64 ? 378 GLN B CA  1 
ATOM   5267 C  C   . GLN B 1 331 ? 9.346   13.325  46.064  1.00 13.61 ? 378 GLN B C   1 
ATOM   5268 O  O   . GLN B 1 331 ? 10.503  13.708  45.887  1.00 13.52 ? 378 GLN B O   1 
ATOM   5269 C  CB  . GLN B 1 331 ? 8.099   12.423  44.050  1.00 12.63 ? 378 GLN B CB  1 
ATOM   5270 C  CG  . GLN B 1 331 ? 8.870   13.345  43.111  1.00 13.15 ? 378 GLN B CG  1 
ATOM   5271 C  CD  . GLN B 1 331 ? 10.176  12.755  42.623  1.00 16.28 ? 378 GLN B CD  1 
ATOM   5272 O  OE1 . GLN B 1 331 ? 10.333  11.557  42.454  1.00 18.45 ? 378 GLN B OE1 1 
ATOM   5273 N  NE2 . GLN B 1 331 ? 11.172  13.607  42.418  1.00 19.55 ? 378 GLN B NE2 1 
ATOM   5274 N  N   . ARG B 1 332 ? 8.513   13.913  46.907  1.00 13.17 ? 379 ARG B N   1 
ATOM   5275 C  CA  . ARG B 1 332 ? 8.973   15.054  47.717  1.00 13.36 ? 379 ARG B CA  1 
ATOM   5276 C  C   . ARG B 1 332 ? 10.190  14.664  48.534  1.00 14.73 ? 379 ARG B C   1 
ATOM   5277 O  O   . ARG B 1 332 ? 11.146  15.439  48.614  1.00 14.84 ? 379 ARG B O   1 
ATOM   5278 C  CB  . ARG B 1 332 ? 7.816   15.553  48.585  1.00 15.87 ? 379 ARG B CB  1 
ATOM   5279 C  CG  . ARG B 1 332 ? 8.263   16.735  49.424  1.00 21.96 ? 379 ARG B CG  1 
ATOM   5280 C  CD  . ARG B 1 332 ? 7.128   17.291  50.238  1.00 30.58 ? 379 ARG B CD  1 
ATOM   5281 N  NE  . ARG B 1 332 ? 6.028   17.776  49.401  1.00 39.15 ? 379 ARG B NE  1 
ATOM   5282 C  CZ  . ARG B 1 332 ? 4.738   17.510  49.610  1.00 43.40 ? 379 ARG B CZ  1 
ATOM   5283 N  NH1 . ARG B 1 332 ? 4.367   16.711  50.596  1.00 45.50 ? 379 ARG B NH1 1 
ATOM   5284 N  NH2 . ARG B 1 332 ? 3.827   18.045  48.822  1.00 48.03 ? 379 ARG B NH2 1 
ATOM   5285 N  N   . ASN B 1 333 ? 10.149  13.468  49.113  1.00 13.32 ? 380 ASN B N   1 
ATOM   5286 C  CA  . ASN B 1 333 ? 11.230  12.982  49.961  1.00 13.93 ? 380 ASN B CA  1 
ATOM   5287 C  C   . ASN B 1 333 ? 12.522  12.739  49.177  1.00 14.67 ? 380 ASN B C   1 
ATOM   5288 O  O   . ASN B 1 333 ? 13.599  12.566  49.752  1.00 15.63 ? 380 ASN B O   1 
ATOM   5289 C  CB  . ASN B 1 333 ? 10.775  11.792  50.781  1.00 15.36 ? 380 ASN B CB  1 
ATOM   5290 C  CG  . ASN B 1 333 ? 11.443  11.742  52.121  1.00 19.26 ? 380 ASN B CG  1 
ATOM   5291 O  OD1 . ASN B 1 333 ? 11.448  12.771  52.795  1.00 19.76 ? 380 ASN B OD1 1 
ATOM   5292 N  ND2 . ASN B 1 333 ? 12.040  10.613  52.464  1.00 19.28 ? 380 ASN B ND2 1 
ATOM   5293 N  N   . LEU B 1 334 ? 12.451  12.609  47.860  1.00 13.81 ? 381 LEU B N   1 
ATOM   5294 C  CA  . LEU B 1 334 ? 13.630  12.366  47.052  1.00 13.69 ? 381 LEU B CA  1 
ATOM   5295 C  C   . LEU B 1 334 ? 14.307  13.684  46.674  1.00 14.27 ? 381 LEU B C   1 
ATOM   5296 O  O   . LEU B 1 334 ? 15.214  13.679  45.834  1.00 14.40 ? 381 LEU B O   1 
ATOM   5297 C  CB  . LEU B 1 334 ? 13.204  11.579  45.827  1.00 14.40 ? 381 LEU B CB  1 
ATOM   5298 C  CG  . LEU B 1 334 ? 12.642  10.182  46.104  1.00 13.65 ? 381 LEU B CG  1 
ATOM   5299 C  CD1 . LEU B 1 334 ? 12.373  9.543   44.770  1.00 14.87 ? 381 LEU B CD1 1 
ATOM   5300 C  CD2 . LEU B 1 334 ? 13.584  9.349   46.905  1.00 15.97 ? 381 LEU B CD2 1 
ATOM   5301 N  N   . ALA B 1 335 ? 13.937  14.797  47.333  1.00 14.23 ? 382 ALA B N   1 
ATOM   5302 C  CA  . ALA B 1 335 ? 14.577  16.064  47.036  1.00 14.46 ? 382 ALA B CA  1 
ATOM   5303 C  C   . ALA B 1 335 ? 16.093  15.984  47.159  1.00 14.78 ? 382 ALA B C   1 
ATOM   5304 O  O   . ALA B 1 335 ? 16.776  16.685  46.422  1.00 17.13 ? 382 ALA B O   1 
ATOM   5305 C  CB  . ALA B 1 335 ? 14.024  17.163  47.947  1.00 16.40 ? 382 ALA B CB  1 
ATOM   5306 N  N   . THR B 1 336 ? 16.603  15.204  48.114  1.00 14.37 ? 383 THR B N   1 
ATOM   5307 C  CA  . THR B 1 336 ? 18.046  15.176  48.352  1.00 14.74 ? 383 THR B CA  1 
ATOM   5308 C  C   . THR B 1 336 ? 18.668  13.831  47.950  1.00 15.66 ? 383 THR B C   1 
ATOM   5309 O  O   . THR B 1 336 ? 19.813  13.538  48.281  1.00 15.61 ? 383 THR B O   1 
ATOM   5310 C  CB  . THR B 1 336 ? 18.331  15.455  49.822  1.00 16.26 ? 383 THR B CB  1 
ATOM   5311 O  OG1 . THR B 1 336 ? 17.645  14.504  50.607  1.00 19.00 ? 383 THR B OG1 1 
ATOM   5312 C  CG2 . THR B 1 336 ? 17.914  16.857  50.216  1.00 18.04 ? 383 THR B CG2 1 
ATOM   5313 N  N   . ASP B 1 337 ? 17.924  13.021  47.168  1.00 12.88 ? 384 ASP B N   1 
ATOM   5314 C  CA  . ASP B 1 337 ? 18.350  11.709  46.738  1.00 13.21 ? 384 ASP B CA  1 
ATOM   5315 C  C   . ASP B 1 337 ? 19.688  11.803  46.028  1.00 13.42 ? 384 ASP B C   1 
ATOM   5316 O  O   . ASP B 1 337 ? 19.850  12.593  45.102  1.00 13.70 ? 384 ASP B O   1 
ATOM   5317 C  CB  . ASP B 1 337 ? 17.270  11.150  45.830  1.00 13.22 ? 384 ASP B CB  1 
ATOM   5318 C  CG  . ASP B 1 337 ? 17.384  9.691   45.430  1.00 13.84 ? 384 ASP B CG  1 
ATOM   5319 O  OD1 . ASP B 1 337 ? 18.383  9.036   45.724  1.00 13.33 ? 384 ASP B OD1 1 
ATOM   5320 O  OD2 . ASP B 1 337 ? 16.438  9.224   44.787  1.00 15.64 ? 384 ASP B OD2 1 
ATOM   5321 N  N   . ALA B 1 338 ? 20.626  10.946  46.437  1.00 12.91 ? 385 ALA B N   1 
ATOM   5322 C  CA  . ALA B 1 338 ? 21.904  10.821  45.756  1.00 13.66 ? 385 ALA B CA  1 
ATOM   5323 C  C   . ALA B 1 338 ? 21.727  10.451  44.286  1.00 13.74 ? 385 ALA B C   1 
ATOM   5324 O  O   . ALA B 1 338 ? 22.596  10.723  43.479  1.00 15.48 ? 385 ALA B O   1 
ATOM   5325 C  CB  . ALA B 1 338 ? 22.788  9.820   46.482  1.00 15.51 ? 385 ALA B CB  1 
ATOM   5326 N  N   . LEU B 1 339 ? 20.629  9.771   43.952  1.00 13.08 ? 386 LEU B N   1 
ATOM   5327 C  CA  . LEU B 1 339 ? 20.377  9.433   42.568  1.00 12.89 ? 386 LEU B CA  1 
ATOM   5328 C  C   . LEU B 1 339 ? 20.155  10.655  41.690  1.00 12.91 ? 386 LEU B C   1 
ATOM   5329 O  O   . LEU B 1 339 ? 20.318  10.558  40.469  1.00 13.36 ? 386 LEU B O   1 
ATOM   5330 C  CB  . LEU B 1 339 ? 19.137  8.529   42.571  1.00 13.42 ? 386 LEU B CB  1 
ATOM   5331 C  CG  . LEU B 1 339 ? 18.750  7.968   41.201  1.00 15.15 ? 386 LEU B CG  1 
ATOM   5332 C  CD1 . LEU B 1 339 ? 19.797  7.094   40.596  1.00 15.66 ? 386 LEU B CD1 1 
ATOM   5333 C  CD2 . LEU B 1 339 ? 17.428  7.202   41.293  1.00 16.41 ? 386 LEU B CD2 1 
ATOM   5334 N  N   . ASN B 1 340 ? 19.816  11.814  42.260  1.00 12.17 ? 387 ASN B N   1 
ATOM   5335 C  CA  . ASN B 1 340 ? 19.451  12.970  41.443  1.00 12.86 ? 387 ASN B CA  1 
ATOM   5336 C  C   . ASN B 1 340 ? 20.580  13.436  40.529  1.00 13.70 ? 387 ASN B C   1 
ATOM   5337 O  O   . ASN B 1 340 ? 20.303  14.025  39.509  1.00 15.11 ? 387 ASN B O   1 
ATOM   5338 C  CB  . ASN B 1 340 ? 18.953  14.123  42.283  1.00 13.57 ? 387 ASN B CB  1 
ATOM   5339 C  CG  . ASN B 1 340 ? 17.605  13.877  42.892  1.00 14.89 ? 387 ASN B CG  1 
ATOM   5340 O  OD1 . ASN B 1 340 ? 16.809  13.140  42.314  1.00 17.34 ? 387 ASN B OD1 1 
ATOM   5341 N  ND2 . ASN B 1 340 ? 17.289  14.565  43.984  1.00 15.68 ? 387 ASN B ND2 1 
ATOM   5342 N  N   . GLU B 1 341 ? 21.825  13.175  40.906  1.00 14.23 ? 388 GLU B N   1 
ATOM   5343 C  CA  . GLU B 1 341 ? 22.971  13.501  40.124  1.00 15.18 ? 388 GLU B CA  1 
ATOM   5344 C  C   . GLU B 1 341 ? 22.901  12.821  38.756  1.00 14.92 ? 388 GLU B C   1 
ATOM   5345 O  O   . GLU B 1 341 ? 23.421  13.361  37.788  1.00 16.14 ? 388 GLU B O   1 
ATOM   5346 C  CB  . GLU B 1 341 ? 24.215  13.106  40.928  1.00 18.20 ? 388 GLU B CB  1 
ATOM   5347 C  CG  . GLU B 1 341 ? 25.496  13.318  40.133  1.00 21.65 ? 388 GLU B CG  1 
ATOM   5348 C  CD  . GLU B 1 341 ? 26.786  13.144  40.911  1.00 28.69 ? 388 GLU B CD  1 
ATOM   5349 O  OE1 . GLU B 1 341 ? 26.739  12.778  42.094  1.00 35.40 ? 388 GLU B OE1 1 
ATOM   5350 O  OE2 . GLU B 1 341 ? 27.845  13.359  40.295  1.00 37.38 ? 388 GLU B OE2 1 
ATOM   5351 N  N   . PHE B 1 342 ? 22.188  11.687  38.671  1.00 13.27 ? 389 PHE B N   1 
ATOM   5352 C  CA  . PHE B 1 342 ? 22.294  10.868  37.470  1.00 14.08 ? 389 PHE B CA  1 
ATOM   5353 C  C   . PHE B 1 342 ? 20.989  10.728  36.706  1.00 14.49 ? 389 PHE B C   1 
ATOM   5354 O  O   . PHE B 1 342 ? 20.965  9.953   35.752  1.00 15.61 ? 389 PHE B O   1 
ATOM   5355 C  CB  . PHE B 1 342 ? 22.753  9.485   37.884  1.00 14.92 ? 389 PHE B CB  1 
ATOM   5356 C  CG  . PHE B 1 342 ? 24.067  9.492   38.636  1.00 15.22 ? 389 PHE B CG  1 
ATOM   5357 C  CD1 . PHE B 1 342 ? 25.253  9.612   37.963  1.00 17.36 ? 389 PHE B CD1 1 
ATOM   5358 C  CD2 . PHE B 1 342 ? 24.086  9.329   40.011  1.00 16.72 ? 389 PHE B CD2 1 
ATOM   5359 C  CE1 . PHE B 1 342 ? 26.468  9.630   38.650  1.00 16.77 ? 389 PHE B CE1 1 
ATOM   5360 C  CE2 . PHE B 1 342 ? 25.298  9.318   40.687  1.00 18.42 ? 389 PHE B CE2 1 
ATOM   5361 C  CZ  . PHE B 1 342 ? 26.470  9.473   40.001  1.00 15.60 ? 389 PHE B CZ  1 
ATOM   5362 N  N   . ILE B 1 343 ? 19.969  11.465  37.105  1.00 13.09 ? 390 ILE B N   1 
ATOM   5363 C  CA  . ILE B 1 343 ? 18.662  11.357  36.465  1.00 12.43 ? 390 ILE B CA  1 
ATOM   5364 C  C   . ILE B 1 343 ? 18.089  12.742  36.251  1.00 12.96 ? 390 ILE B C   1 
ATOM   5365 O  O   . ILE B 1 343 ? 18.477  13.708  36.876  1.00 15.42 ? 390 ILE B O   1 
ATOM   5366 C  CB  . ILE B 1 343 ? 17.670  10.488  37.252  1.00 14.32 ? 390 ILE B CB  1 
ATOM   5367 C  CG1 . ILE B 1 343 ? 17.306  11.113  38.610  1.00 15.48 ? 390 ILE B CG1 1 
ATOM   5368 C  CG2 . ILE B 1 343 ? 18.163  9.046   37.377  1.00 14.36 ? 390 ILE B CG2 1 
ATOM   5369 C  CD1 . ILE B 1 343 ? 16.121  10.467  39.267  1.00 18.76 ? 390 ILE B CD1 1 
ATOM   5370 N  N   . GLN B 1 344 ? 17.121  12.826  35.382  1.00 12.62 ? 391 GLN B N   1 
ATOM   5371 C  CA  . GLN B 1 344 ? 16.361  14.050  35.198  1.00 13.04 ? 391 GLN B CA  1 
ATOM   5372 C  C   . GLN B 1 344 ? 14.952  13.646  34.772  1.00 12.58 ? 391 GLN B C   1 
ATOM   5373 O  O   . GLN B 1 344 ? 14.783  12.907  33.808  1.00 12.65 ? 391 GLN B O   1 
ATOM   5374 C  CB  . GLN B 1 344 ? 16.964  14.915  34.100  1.00 17.12 ? 391 GLN B CB  1 
ATOM   5375 C  CG  . GLN B 1 344 ? 16.411  16.334  34.103  1.00 22.22 ? 391 GLN B CG  1 
ATOM   5376 C  CD  . GLN B 1 344 ? 17.157  17.239  33.155  1.00 26.86 ? 391 GLN B CD  1 
ATOM   5377 O  OE1 . GLN B 1 344 ? 17.127  17.036  31.943  1.00 29.61 ? 391 GLN B OE1 1 
ATOM   5378 N  NE2 . GLN B 1 344 ? 17.802  18.254  33.700  1.00 34.40 ? 391 GLN B NE2 1 
ATOM   5379 N  N   . HIS B 1 345 ? 13.940  14.196  35.446  1.00 12.05 ? 392 HIS B N   1 
ATOM   5380 C  CA  . HIS B 1 345 ? 12.558  13.961  35.053  1.00 11.31 ? 392 HIS B CA  1 
ATOM   5381 C  C   . HIS B 1 345 ? 12.229  14.932  33.932  1.00 12.46 ? 392 HIS B C   1 
ATOM   5382 O  O   . HIS B 1 345 ? 12.336  16.155  34.124  1.00 13.31 ? 392 HIS B O   1 
ATOM   5383 C  CB  . HIS B 1 345 ? 11.614  14.215  36.221  1.00 12.62 ? 392 HIS B CB  1 
ATOM   5384 C  CG  . HIS B 1 345 ? 11.750  13.289  37.343  1.00 11.23 ? 392 HIS B CG  1 
ATOM   5385 N  ND1 . HIS B 1 345 ? 10.639  12.624  37.772  1.00 13.81 ? 392 HIS B ND1 1 
ATOM   5386 C  CD2 . HIS B 1 345 ? 12.771  12.871  38.096  1.00 13.53 ? 392 HIS B CD2 1 
ATOM   5387 C  CE1 . HIS B 1 345 ? 11.000  11.845  38.771  1.00 13.27 ? 392 HIS B CE1 1 
ATOM   5388 N  NE2 . HIS B 1 345 ? 12.285  12.003  39.011  1.00 14.00 ? 392 HIS B NE2 1 
ATOM   5389 N  N   . VAL B 1 346 ? 11.865  14.377  32.767  1.00 12.44 ? 393 VAL B N   1 
ATOM   5390 C  CA  . VAL B 1 346 ? 11.682  15.179  31.567  1.00 13.38 ? 393 VAL B CA  1 
ATOM   5391 C  C   . VAL B 1 346 ? 10.279  15.071  31.001  1.00 13.50 ? 393 VAL B C   1 
ATOM   5392 O  O   . VAL B 1 346 ? 9.976   15.680  29.995  1.00 14.77 ? 393 VAL B O   1 
ATOM   5393 C  CB  . VAL B 1 346 ? 12.723  14.852  30.508  1.00 14.04 ? 393 VAL B CB  1 
ATOM   5394 C  CG1 . VAL B 1 346 ? 14.101  15.302  31.013  1.00 16.27 ? 393 VAL B CG1 1 
ATOM   5395 C  CG2 . VAL B 1 346 ? 12.677  13.405  30.076  1.00 15.92 ? 393 VAL B CG2 1 
ATOM   5396 N  N   . GLY B 1 347 ? 9.395   14.286  31.599  1.00 12.86 ? 394 GLY B N   1 
ATOM   5397 C  CA  . GLY B 1 347 ? 8.013   14.265  31.175  1.00 12.67 ? 394 GLY B CA  1 
ATOM   5398 C  C   . GLY B 1 347 ? 7.155   13.808  32.326  1.00 12.80 ? 394 GLY B C   1 
ATOM   5399 O  O   . GLY B 1 347 ? 7.647   13.045  33.157  1.00 12.92 ? 394 GLY B O   1 
ATOM   5400 N  N   . SER B 1 348 ? 5.909   14.238  32.345  1.00 11.63 ? 395 SER B N   1 
ATOM   5401 C  CA  . SER B 1 348 ? 5.057   13.946  33.474  1.00 12.19 ? 395 SER B CA  1 
ATOM   5402 C  C   . SER B 1 348 ? 3.604   13.967  33.043  1.00 12.46 ? 395 SER B C   1 
ATOM   5403 O  O   . SER B 1 348 ? 3.196   14.828  32.285  1.00 13.33 ? 395 SER B O   1 
ATOM   5404 C  CB  . SER B 1 348 ? 5.296   14.983  34.555  1.00 14.72 ? 395 SER B CB  1 
ATOM   5405 O  OG  . SER B 1 348 ? 4.526   14.696  35.718  1.00 14.65 ? 395 SER B OG  1 
ATOM   5406 N  N   . ALA B 1 349 ? 2.811   13.099  33.644  1.00 12.07 ? 396 ALA B N   1 
ATOM   5407 C  CA  . ALA B 1 349 ? 1.369   13.146  33.438  1.00 11.77 ? 396 ALA B CA  1 
ATOM   5408 C  C   . ALA B 1 349 ? 0.699   12.378  34.549  1.00 11.93 ? 396 ALA B C   1 
ATOM   5409 O  O   . ALA B 1 349 ? 1.261   11.431  35.071  1.00 13.80 ? 396 ALA B O   1 
ATOM   5410 C  CB  . ALA B 1 349 ? 1.013   12.536  32.122  1.00 12.84 ? 396 ALA B CB  1 
ATOM   5411 N  N   . VAL B 1 350 ? -0.525  12.769  34.865  1.00 11.32 ? 397 VAL B N   1 
ATOM   5412 C  CA  . VAL B 1 350 ? -1.326  12.053  35.835  1.00 11.65 ? 397 VAL B CA  1 
ATOM   5413 C  C   . VAL B 1 350 ? -2.658  11.680  35.221  1.00 11.54 ? 397 VAL B C   1 
ATOM   5414 O  O   . VAL B 1 350 ? -3.190  12.396  34.368  1.00 11.44 ? 397 VAL B O   1 
ATOM   5415 C  CB  . VAL B 1 350 ? -1.549  12.830  37.129  1.00 12.69 ? 397 VAL B CB  1 
ATOM   5416 C  CG1 . VAL B 1 350 ? -0.207  13.108  37.808  1.00 14.58 ? 397 VAL B CG1 1 
ATOM   5417 C  CG2 . VAL B 1 350 ? -2.314  14.121  36.946  1.00 14.09 ? 397 VAL B CG2 1 
ATOM   5418 N  N   . PHE B 1 351 ? -3.211  10.539  35.637  1.00 11.25 ? 398 PHE B N   1 
ATOM   5419 C  CA  . PHE B 1 351 ? -4.451  10.059  35.080  1.00 11.38 ? 398 PHE B CA  1 
ATOM   5420 C  C   . PHE B 1 351 ? -5.298  9.361   36.137  1.00 12.16 ? 398 PHE B C   1 
ATOM   5421 O  O   . PHE B 1 351 ? -4.751  8.687   37.001  1.00 12.56 ? 398 PHE B O   1 
ATOM   5422 C  CB  . PHE B 1 351 ? -4.231  9.017   33.984  1.00 11.42 ? 398 PHE B CB  1 
ATOM   5423 C  CG  . PHE B 1 351 ? -3.422  9.593   32.842  1.00 10.89 ? 398 PHE B CG  1 
ATOM   5424 C  CD1 . PHE B 1 351 ? -4.002  10.361  31.852  1.00 11.70 ? 398 PHE B CD1 1 
ATOM   5425 C  CD2 . PHE B 1 351 ? -2.058  9.362   32.806  1.00 12.38 ? 398 PHE B CD2 1 
ATOM   5426 C  CE1 . PHE B 1 351 ? -3.256  10.876  30.811  1.00 11.92 ? 398 PHE B CE1 1 
ATOM   5427 C  CE2 . PHE B 1 351 ? -1.300  9.903   31.787  1.00 12.79 ? 398 PHE B CE2 1 
ATOM   5428 C  CZ  . PHE B 1 351 ? -1.890  10.653  30.804  1.00 12.63 ? 398 PHE B CZ  1 
ATOM   5429 N  N   . ALA B 1 352 ? -6.603  9.495   36.061  1.00 11.46 ? 399 ALA B N   1 
ATOM   5430 C  CA  . ALA B 1 352 ? -7.565  8.689   36.783  1.00 11.57 ? 399 ALA B CA  1 
ATOM   5431 C  C   . ALA B 1 352 ? -7.916  7.498   35.911  1.00 10.76 ? 399 ALA B C   1 
ATOM   5432 O  O   . ALA B 1 352 ? -8.369  7.658   34.802  1.00 11.57 ? 399 ALA B O   1 
ATOM   5433 C  CB  . ALA B 1 352 ? -8.813  9.484   37.053  1.00 12.30 ? 399 ALA B CB  1 
ATOM   5434 N  N   . VAL B 1 353 ? -7.637  6.306   36.426  1.00 11.30 ? 400 VAL B N   1 
ATOM   5435 C  CA  . VAL B 1 353 ? -7.846  5.071   35.708  1.00 11.22 ? 400 VAL B CA  1 
ATOM   5436 C  C   . VAL B 1 353 ? -9.136  4.463   36.206  1.00 11.27 ? 400 VAL B C   1 
ATOM   5437 O  O   . VAL B 1 353 ? -9.216  4.060   37.359  1.00 11.69 ? 400 VAL B O   1 
ATOM   5438 C  CB  . VAL B 1 353 ? -6.646  4.148   35.911  1.00 13.41 ? 400 VAL B CB  1 
ATOM   5439 C  CG1 . VAL B 1 353 ? -6.853  2.746   35.355  1.00 15.01 ? 400 VAL B CG1 1 
ATOM   5440 C  CG2 . VAL B 1 353 ? -5.359  4.776   35.374  1.00 15.43 ? 400 VAL B CG2 1 
ATOM   5441 N  N   . PRO B 1 354 ? -10.190 4.445   35.379  1.00 10.96 ? 401 PRO B N   1 
ATOM   5442 C  CA  . PRO B 1 354 ? -11.486 4.053   35.911  1.00 12.43 ? 401 PRO B CA  1 
ATOM   5443 C  C   . PRO B 1 354 ? -11.558 2.586   36.244  1.00 13.07 ? 401 PRO B C   1 
ATOM   5444 O  O   . PRO B 1 354 ? -10.672 1.776   35.967  1.00 13.26 ? 401 PRO B O   1 
ATOM   5445 C  CB  . PRO B 1 354 ? -12.467 4.417   34.821  1.00 13.36 ? 401 PRO B CB  1 
ATOM   5446 C  CG  . PRO B 1 354 ? -11.659 4.565   33.599  1.00 14.50 ? 401 PRO B CG  1 
ATOM   5447 C  CD  . PRO B 1 354 ? -10.271 5.039   34.038  1.00 12.16 ? 401 PRO B CD  1 
ATOM   5448 N  N   . PRO B 1 355 ? -12.680 2.216   36.876  1.00 12.78 ? 402 PRO B N   1 
ATOM   5449 C  CA  . PRO B 1 355 ? -12.956 0.820   37.169  1.00 13.13 ? 402 PRO B CA  1 
ATOM   5450 C  C   . PRO B 1 355 ? -12.995 -0.013  35.904  1.00 12.22 ? 402 PRO B C   1 
ATOM   5451 O  O   . PRO B 1 355 ? -13.020 0.463   34.780  1.00 13.65 ? 402 PRO B O   1 
ATOM   5452 C  CB  . PRO B 1 355 ? -14.305 0.816   37.900  1.00 14.96 ? 402 PRO B CB  1 
ATOM   5453 C  CG  . PRO B 1 355 ? -14.817 2.179   37.758  1.00 16.70 ? 402 PRO B CG  1 
ATOM   5454 C  CD  . PRO B 1 355 ? -13.726 3.115   37.369  1.00 14.12 ? 402 PRO B CD  1 
ATOM   5455 N  N   . GLY B 1 356 ? -13.094 -1.314  36.155  1.00 12.99 ? 403 GLY B N   1 
ATOM   5456 C  CA  . GLY B 1 356 ? -13.082 -2.306  35.116  1.00 13.42 ? 403 GLY B CA  1 
ATOM   5457 C  C   . GLY B 1 356 ? -14.356 -2.331  34.286  1.00 13.96 ? 403 GLY B C   1 
ATOM   5458 O  O   . GLY B 1 356 ? -15.401 -1.771  34.650  1.00 15.61 ? 403 GLY B O   1 
ATOM   5459 N  N   . VAL B 1 357 ? -14.220 -2.969  33.123  1.00 14.42 ? 404 VAL B N   1 
ATOM   5460 C  CA  . VAL B 1 357 ? -15.333 -3.230  32.244  1.00 14.55 ? 404 VAL B CA  1 
ATOM   5461 C  C   . VAL B 1 357 ? -15.956 -4.526  32.729  1.00 15.30 ? 404 VAL B C   1 
ATOM   5462 O  O   . VAL B 1 357 ? -15.328 -5.584  32.664  1.00 16.30 ? 404 VAL B O   1 
ATOM   5463 C  CB  . VAL B 1 357 ? -14.835 -3.342  30.799  1.00 15.61 ? 404 VAL B CB  1 
ATOM   5464 C  CG1 . VAL B 1 357 ? -16.009 -3.535  29.866  1.00 16.97 ? 404 VAL B CG1 1 
ATOM   5465 C  CG2 . VAL B 1 357 ? -14.087 -2.068  30.407  1.00 17.68 ? 404 VAL B CG2 1 
ATOM   5466 N  N   . ARG B 1 358 ? -17.168 -4.424  33.290  1.00 16.53 ? 405 ARG B N   1 
ATOM   5467 C  CA  . ARG B 1 358 ? -17.712 -5.536  34.067  1.00 19.56 ? 405 ARG B CA  1 
ATOM   5468 C  C   . ARG B 1 358 ? -18.100 -6.745  33.206  1.00 20.19 ? 405 ARG B C   1 
ATOM   5469 O  O   . ARG B 1 358 ? -17.966 -7.887  33.677  1.00 23.29 ? 405 ARG B O   1 
ATOM   5470 C  CB  . ARG B 1 358 ? -18.938 -5.091  34.868  1.00 24.11 ? 405 ARG B CB  1 
ATOM   5471 C  CG  . ARG B 1 358 ? -18.638 -3.964  35.845  1.00 30.83 ? 405 ARG B CG  1 
ATOM   5472 C  CD  . ARG B 1 358 ? -17.426 -4.178  36.722  1.00 37.70 ? 405 ARG B CD  1 
ATOM   5473 N  NE  . ARG B 1 358 ? -17.486 -5.489  37.385  1.00 52.85 ? 405 ARG B NE  1 
ATOM   5474 C  CZ  . ARG B 1 358 ? -17.782 -5.704  38.666  1.00 55.16 ? 405 ARG B CZ  1 
ATOM   5475 N  NH1 . ARG B 1 358 ? -18.096 -4.683  39.440  1.00 52.71 ? 405 ARG B NH1 1 
ATOM   5476 N  NH2 . ARG B 1 358 ? -17.768 -6.939  39.152  1.00 56.16 ? 405 ARG B NH2 1 
ATOM   5477 N  N   . ASP B 1 359 ? -18.638 -6.512  32.013  1.00 19.11 ? 406 ASP B N   1 
ATOM   5478 C  CA  . ASP B 1 359 ? -19.104 -7.591  31.160  1.00 21.31 ? 406 ASP B CA  1 
ATOM   5479 C  C   . ASP B 1 359 ? -19.168 -7.086  29.733  1.00 21.95 ? 406 ASP B C   1 
ATOM   5480 O  O   . ASP B 1 359 ? -18.793 -5.946  29.434  1.00 19.29 ? 406 ASP B O   1 
ATOM   5481 C  CB  . ASP B 1 359 ? -20.453 -8.102  31.656  1.00 24.69 ? 406 ASP B CB  1 
ATOM   5482 C  CG  . ASP B 1 359 ? -21.578 -7.078  31.663  1.00 27.96 ? 406 ASP B CG  1 
ATOM   5483 O  OD1 . ASP B 1 359 ? -21.538 -6.109  30.850  1.00 25.23 ? 406 ASP B OD1 1 
ATOM   5484 O  OD2 . ASP B 1 359 ? -22.475 -7.241  32.512  1.00 36.53 ? 406 ASP B OD2 1 
ATOM   5485 N  N   . ALA B 1 360 ? -19.682 -7.926  28.827  1.00 21.16 ? 407 ALA B N   1 
ATOM   5486 C  CA  . ALA B 1 360 ? -19.721 -7.607  27.416  1.00 21.43 ? 407 ALA B CA  1 
ATOM   5487 C  C   . ALA B 1 360 ? -20.563 -6.387  27.035  1.00 20.32 ? 407 ALA B C   1 
ATOM   5488 O  O   . ALA B 1 360 ? -20.376 -5.859  25.953  1.00 26.79 ? 407 ALA B O   1 
ATOM   5489 C  CB  . ALA B 1 360 ? -20.166 -8.850  26.648  1.00 23.82 ? 407 ALA B CB  1 
ATOM   5490 N  N   . ASP B 1 361 ? -21.452 -5.901  27.898  1.00 22.26 ? 408 ASP B N   1 
ATOM   5491 C  CA  . ASP B 1 361 ? -22.299 -4.774  27.568  1.00 25.23 ? 408 ASP B CA  1 
ATOM   5492 C  C   . ASP B 1 361 ? -21.748 -3.460  28.137  1.00 23.06 ? 408 ASP B C   1 
ATOM   5493 O  O   . ASP B 1 361 ? -22.186 -2.398  27.735  1.00 26.41 ? 408 ASP B O   1 
ATOM   5494 C  CB  . ASP B 1 361 ? -23.717 -5.016  28.035  1.00 28.56 ? 408 ASP B CB  1 
ATOM   5495 C  CG  . ASP B 1 361 ? -24.413 -6.143  27.284  1.00 33.47 ? 408 ASP B CG  1 
ATOM   5496 O  OD1 . ASP B 1 361 ? -24.346 -6.160  26.037  1.00 40.39 ? 408 ASP B OD1 1 
ATOM   5497 O  OD2 . ASP B 1 361 ? -24.990 -6.989  27.952  1.00 39.94 ? 408 ASP B OD2 1 
ATOM   5498 N  N   . ASP B 1 362 ? -20.721 -3.551  28.993  1.00 18.97 ? 409 ASP B N   1 
ATOM   5499 C  CA  . ASP B 1 362 ? -20.136 -2.388  29.636  1.00 19.39 ? 409 ASP B CA  1 
ATOM   5500 C  C   . ASP B 1 362 ? -19.112 -1.744  28.700  1.00 16.63 ? 409 ASP B C   1 
ATOM   5501 O  O   . ASP B 1 362 ? -18.776 -2.272  27.649  1.00 18.09 ? 409 ASP B O   1 
ATOM   5502 C  CB  . ASP B 1 362 ? -19.545 -2.806  30.965  1.00 17.16 ? 409 ASP B CB  1 
ATOM   5503 C  CG  . ASP B 1 362 ? -19.317 -1.676  31.940  1.00 16.96 ? 409 ASP B CG  1 
ATOM   5504 O  OD1 . ASP B 1 362 ? -19.848 -0.583  31.639  1.00 17.85 ? 409 ASP B OD1 1 
ATOM   5505 O  OD2 . ASP B 1 362 ? -18.644 -1.909  32.948  1.00 18.60 ? 409 ASP B OD2 1 
ATOM   5506 N  N   . TRP B 1 363 ? -18.623 -0.565  29.094  1.00 14.99 ? 410 TRP B N   1 
ATOM   5507 C  CA  . TRP B 1 363 ? -17.731 0.172   28.227  1.00 14.30 ? 410 TRP B CA  1 
ATOM   5508 C  C   . TRP B 1 363 ? -16.866 1.075   29.093  1.00 13.74 ? 410 TRP B C   1 
ATOM   5509 O  O   . TRP B 1 363 ? -17.275 1.482   30.179  1.00 14.30 ? 410 TRP B O   1 
ATOM   5510 C  CB  . TRP B 1 363 ? -18.478 0.963   27.136  1.00 14.44 ? 410 TRP B CB  1 
ATOM   5511 C  CG  . TRP B 1 363 ? -19.712 1.663   27.617  1.00 16.92 ? 410 TRP B CG  1 
ATOM   5512 C  CD1 . TRP B 1 363 ? -20.955 1.116   27.762  1.00 19.82 ? 410 TRP B CD1 1 
ATOM   5513 C  CD2 . TRP B 1 363 ? -19.852 3.055   27.918  1.00 17.52 ? 410 TRP B CD2 1 
ATOM   5514 N  NE1 . TRP B 1 363 ? -21.836 2.065   28.192  1.00 20.15 ? 410 TRP B NE1 1 
ATOM   5515 C  CE2 . TRP B 1 363 ? -21.196 3.259   28.299  1.00 19.79 ? 410 TRP B CE2 1 
ATOM   5516 C  CE3 . TRP B 1 363 ? -18.980 4.141   27.929  1.00 18.11 ? 410 TRP B CE3 1 
ATOM   5517 C  CZ2 . TRP B 1 363 ? -21.687 4.503   28.664  1.00 18.64 ? 410 TRP B CZ2 1 
ATOM   5518 C  CZ3 . TRP B 1 363 ? -19.477 5.380   28.247  1.00 18.42 ? 410 TRP B CZ3 1 
ATOM   5519 C  CH2 . TRP B 1 363 ? -20.810 5.545   28.619  1.00 20.21 ? 410 TRP B CH2 1 
ATOM   5520 N  N   . TRP B 1 364 ? -15.654 1.336   28.616  1.00 12.70 ? 411 TRP B N   1 
ATOM   5521 C  CA  . TRP B 1 364 ? -14.723 2.224   29.297  1.00 12.58 ? 411 TRP B CA  1 
ATOM   5522 C  C   . TRP B 1 364 ? -15.381 3.550   29.640  1.00 13.00 ? 411 TRP B C   1 
ATOM   5523 O  O   . TRP B 1 364 ? -15.886 4.213   28.758  1.00 14.29 ? 411 TRP B O   1 
ATOM   5524 C  CB  . TRP B 1 364 ? -13.562 2.474   28.351  1.00 13.98 ? 411 TRP B CB  1 
ATOM   5525 C  CG  . TRP B 1 364 ? -12.531 1.398   28.322  1.00 12.48 ? 411 TRP B CG  1 
ATOM   5526 C  CD1 . TRP B 1 364 ? -12.236 0.517   29.313  1.00 13.59 ? 411 TRP B CD1 1 
ATOM   5527 C  CD2 . TRP B 1 364 ? -11.505 1.253   27.335  1.00 12.67 ? 411 TRP B CD2 1 
ATOM   5528 N  NE1 . TRP B 1 364 ? -11.120 -0.220  28.972  1.00 13.54 ? 411 TRP B NE1 1 
ATOM   5529 C  CE2 . TRP B 1 364 ? -10.636 0.221   27.783  1.00 12.72 ? 411 TRP B CE2 1 
ATOM   5530 C  CE3 . TRP B 1 364 ? -11.219 1.907   26.140  1.00 13.52 ? 411 TRP B CE3 1 
ATOM   5531 C  CZ2 . TRP B 1 364 ? -9.512  -0.177  27.055  1.00 12.73 ? 411 TRP B CZ2 1 
ATOM   5532 C  CZ3 . TRP B 1 364 ? -10.094 1.526   25.442  1.00 14.79 ? 411 TRP B CZ3 1 
ATOM   5533 C  CH2 . TRP B 1 364 ? -9.254  0.523   25.902  1.00 14.92 ? 411 TRP B CH2 1 
ATOM   5534 N  N   . GLY B 1 365 ? -15.275 3.956   30.896  1.00 13.56 ? 412 GLY B N   1 
ATOM   5535 C  CA  . GLY B 1 365 ? -15.789 5.255   31.292  1.00 14.70 ? 412 GLY B CA  1 
ATOM   5536 C  C   . GLY B 1 365 ? -17.280 5.256   31.607  1.00 14.77 ? 412 GLY B C   1 
ATOM   5537 O  O   . GLY B 1 365 ? -17.838 6.331   31.843  1.00 15.54 ? 412 GLY B O   1 
ATOM   5538 N  N   . SER B 1 366 ? -17.972 4.113   31.552  1.00 13.89 ? 413 SER B N   1 
ATOM   5539 C  CA  . SER B 1 366 ? -19.402 4.129   31.796  1.00 15.29 ? 413 SER B CA  1 
ATOM   5540 C  C   . SER B 1 366 ? -19.783 4.679   33.160  1.00 15.66 ? 413 SER B C   1 
ATOM   5541 O  O   . SER B 1 366 ? -20.889 5.251   33.256  1.00 18.01 ? 413 SER B O   1 
ATOM   5542 C  CB  . SER B 1 366 ? -19.991 2.749   31.644  1.00 14.24 ? 413 SER B CB  1 
ATOM   5543 O  OG  . SER B 1 366 ? -19.533 1.856   32.634  1.00 15.45 ? 413 SER B OG  1 
ATOM   5544 N  N   . THR B 1 367 ? -18.925 4.551   34.175  1.00 13.96 ? 414 THR B N   1 
ATOM   5545 C  CA  . THR B 1 367 ? -19.331 5.062   35.483  1.00 14.87 ? 414 THR B CA  1 
ATOM   5546 C  C   . THR B 1 367 ? -19.253 6.578   35.516  1.00 17.09 ? 414 THR B C   1 
ATOM   5547 O  O   . THR B 1 367 ? -19.932 7.204   36.333  1.00 19.61 ? 414 THR B O   1 
ATOM   5548 C  CB  . THR B 1 367 ? -18.529 4.481   36.634  1.00 15.17 ? 414 THR B CB  1 
ATOM   5549 O  OG1 . THR B 1 367 ? -17.171 4.829   36.479  1.00 15.71 ? 414 THR B OG1 1 
ATOM   5550 C  CG2 . THR B 1 367 ? -18.647 2.973   36.689  1.00 17.35 ? 414 THR B CG2 1 
ATOM   5551 N  N   . LEU B 1 368 ? -18.425 7.173   34.669  1.00 15.27 ? 415 LEU B N   1 
ATOM   5552 C  CA  . LEU B 1 368 ? -18.282 8.627   34.593  1.00 16.01 ? 415 LEU B CA  1 
ATOM   5553 C  C   . LEU B 1 368 ? -19.379 9.235   33.722  1.00 19.87 ? 415 LEU B C   1 
ATOM   5554 O  O   . LEU B 1 368 ? -20.032 10.222  34.105  1.00 22.99 ? 415 LEU B O   1 
ATOM   5555 C  CB  . LEU B 1 368 ? -16.889 8.979   34.103  1.00 15.36 ? 415 LEU B CB  1 
ATOM   5556 C  CG  . LEU B 1 368 ? -16.642 10.463  33.880  1.00 17.32 ? 415 LEU B CG  1 
ATOM   5557 C  CD1 . LEU B 1 368 ? -16.935 11.257  35.156  1.00 20.38 ? 415 LEU B CD1 1 
ATOM   5558 C  CD2 . LEU B 1 368 ? -15.229 10.642  33.416  1.00 18.40 ? 415 LEU B CD2 1 
ATOM   5559 N  N   . PHE B 1 369 ? -19.577 8.692   32.524  1.00 18.16 ? 416 PHE B N   1 
ATOM   5560 C  CA  . PHE B 1 369 ? -20.446 9.297   31.538  1.00 20.33 ? 416 PHE B CA  1 
ATOM   5561 C  C   . PHE B 1 369 ? -21.886 8.894   31.803  1.00 27.85 ? 416 PHE B C   1 
ATOM   5562 O  O   . PHE B 1 369 ? -22.778 9.679   31.536  1.00 32.89 ? 416 PHE B O   1 
ATOM   5563 C  CB  . PHE B 1 369 ? -19.900 8.980   30.150  1.00 20.12 ? 416 PHE B CB  1 
ATOM   5564 C  CG  . PHE B 1 369 ? -18.676 9.822   29.862  1.00 19.47 ? 416 PHE B CG  1 
ATOM   5565 C  CD1 . PHE B 1 369 ? -18.828 11.141  29.452  1.00 22.76 ? 416 PHE B CD1 1 
ATOM   5566 C  CD2 . PHE B 1 369 ? -17.392 9.341   30.029  1.00 19.34 ? 416 PHE B CD2 1 
ATOM   5567 C  CE1 . PHE B 1 369 ? -17.733 11.923  29.172  1.00 22.02 ? 416 PHE B CE1 1 
ATOM   5568 C  CE2 . PHE B 1 369 ? -16.304 10.138  29.783  1.00 21.54 ? 416 PHE B CE2 1 
ATOM   5569 C  CZ  . PHE B 1 369 ? -16.477 11.428  29.350  1.00 22.23 ? 416 PHE B CZ  1 
ATOM   5570 N  N   . GLY B 1 370 ? -22.116 7.687   32.322  1.00 28.91 ? 417 GLY B N   1 
ATOM   5571 C  CA  . GLY B 1 370 ? -23.416 7.329   32.879  1.00 35.45 ? 417 GLY B CA  1 
ATOM   5572 C  C   . GLY B 1 370 ? -24.214 6.501   31.896  1.00 39.41 ? 417 GLY B C   1 
ATOM   5573 O  O   . GLY B 1 370 ? -23.625 6.159   30.852  1.00 41.55 ? 417 GLY B O   1 
HETATM 5574 C  CHA . HEM C 2 .   ? 9.527   -7.564  -1.451  1.00 11.17 ? 501 HEM A CHA 1 
HETATM 5575 C  CHB . HEM C 2 .   ? 7.589   -4.234  1.432   1.00 11.63 ? 501 HEM A CHB 1 
HETATM 5576 C  CHC . HEM C 2 .   ? 11.332  -1.305  0.630   1.00 12.72 ? 501 HEM A CHC 1 
HETATM 5577 C  CHD . HEM C 2 .   ? 13.301  -4.714  -2.132  1.00 11.97 ? 501 HEM A CHD 1 
HETATM 5578 C  C1A . HEM C 2 .   ? 8.639   -6.918  -0.631  1.00 11.06 ? 501 HEM A C1A 1 
HETATM 5579 C  C2A . HEM C 2 .   ? 7.412   -7.462  -0.170  1.00 10.53 ? 501 HEM A C2A 1 
HETATM 5580 C  C3A . HEM C 2 .   ? 6.845   -6.512  0.641   1.00 10.96 ? 501 HEM A C3A 1 
HETATM 5581 C  C4A . HEM C 2 .   ? 7.750   -5.416  0.685   1.00 10.39 ? 501 HEM A C4A 1 
HETATM 5582 C  CMA . HEM C 2 .   ? 5.502   -6.560  1.348   1.00 12.16 ? 501 HEM A CMA 1 
HETATM 5583 C  CAA . HEM C 2 .   ? 6.815   -8.794  -0.569  1.00 11.05 ? 501 HEM A CAA 1 
HETATM 5584 C  CBA . HEM C 2 .   ? 7.258   -9.994  0.270   1.00 11.58 ? 501 HEM A CBA 1 
HETATM 5585 C  CGA . HEM C 2 .   ? 8.683   -10.320 0.144   1.00 12.34 ? 501 HEM A CGA 1 
HETATM 5586 O  O1A . HEM C 2 .   ? 9.528   -9.881  0.962   1.00 13.17 ? 501 HEM A O1A 1 
HETATM 5587 O  O2A . HEM C 2 .   ? 9.086   -11.072 -0.780  1.00 12.89 ? 501 HEM A O2A 1 
HETATM 5588 C  C1B . HEM C 2 .   ? 8.472   -3.158  1.486   1.00 11.69 ? 501 HEM A C1B 1 
HETATM 5589 C  C2B . HEM C 2 .   ? 8.214   -1.983  2.282   1.00 11.90 ? 501 HEM A C2B 1 
HETATM 5590 C  C3B . HEM C 2 .   ? 9.255   -1.162  2.035   1.00 12.27 ? 501 HEM A C3B 1 
HETATM 5591 C  C4B . HEM C 2 .   ? 10.154  -1.822  1.091   1.00 12.17 ? 501 HEM A C4B 1 
HETATM 5592 C  CMB . HEM C 2 .   ? 7.003   -1.728  3.160   1.00 12.31 ? 501 HEM A CMB 1 
HETATM 5593 C  CAB . HEM C 2 .   ? 9.616   0.166   2.592   1.00 14.54 ? 501 HEM A CAB 1 
HETATM 5594 C  CBB . HEM C 2 .   ? 9.115   0.691   3.655   1.00 16.25 ? 501 HEM A CBB 1 
HETATM 5595 C  C1C . HEM C 2 .   ? 12.208  -1.934  -0.225  1.00 11.69 ? 501 HEM A C1C 1 
HETATM 5596 C  C2C . HEM C 2 .   ? 13.421  -1.413  -0.740  1.00 11.72 ? 501 HEM A C2C 1 
HETATM 5597 C  C3C . HEM C 2 .   ? 13.991  -2.372  -1.520  1.00 12.06 ? 501 HEM A C3C 1 
HETATM 5598 C  C4C . HEM C 2 .   ? 13.090  -3.498  -1.532  1.00 12.06 ? 501 HEM A C4C 1 
HETATM 5599 C  CMC . HEM C 2 .   ? 13.935  -0.089  -0.373  1.00 13.64 ? 501 HEM A CMC 1 
HETATM 5600 C  CAC . HEM C 2 .   ? 15.223  -2.364  -2.318  1.00 13.44 ? 501 HEM A CAC 1 
HETATM 5601 C  CBC . HEM C 2 .   ? 15.853  -1.340  -2.725  1.00 17.47 ? 501 HEM A CBC 1 
HETATM 5602 C  C1D . HEM C 2 .   ? 12.435  -5.805  -2.105  1.00 11.76 ? 501 HEM A C1D 1 
HETATM 5603 C  C2D . HEM C 2 .   ? 12.742  -7.057  -2.795  1.00 11.78 ? 501 HEM A C2D 1 
HETATM 5604 C  C3D . HEM C 2 .   ? 11.678  -7.859  -2.668  1.00 10.86 ? 501 HEM A C3D 1 
HETATM 5605 C  C4D . HEM C 2 .   ? 10.734  -7.066  -1.843  1.00 10.80 ? 501 HEM A C4D 1 
HETATM 5606 C  CMD . HEM C 2 .   ? 14.036  -7.362  -3.540  1.00 13.34 ? 501 HEM A CMD 1 
HETATM 5607 C  CAD . HEM C 2 .   ? 11.482  -9.251  -3.130  1.00 12.59 ? 501 HEM A CAD 1 
HETATM 5608 C  CBD . HEM C 2 .   ? 10.945  -9.289  -4.584  1.00 12.62 ? 501 HEM A CBD 1 
HETATM 5609 C  CGD . HEM C 2 .   ? 10.927  -10.676 -5.114  1.00 12.44 ? 501 HEM A CGD 1 
HETATM 5610 O  O1D . HEM C 2 .   ? 9.832   -11.290 -5.143  1.00 13.37 ? 501 HEM A O1D 1 
HETATM 5611 O  O2D . HEM C 2 .   ? 12.018  -11.205 -5.444  1.00 14.55 ? 501 HEM A O2D 1 
HETATM 5612 N  NA  . HEM C 2 .   ? 8.843   -5.664  -0.076  1.00 10.81 ? 501 HEM A NA  1 
HETATM 5613 N  NB  . HEM C 2 .   ? 9.605   -3.020  0.830   1.00 11.65 ? 501 HEM A NB  1 
HETATM 5614 N  NC  . HEM C 2 .   ? 12.045  -3.211  -0.698  1.00 11.43 ? 501 HEM A NC  1 
HETATM 5615 N  ND  . HEM C 2 .   ? 11.232  -5.859  -1.545  1.00 11.04 ? 501 HEM A ND  1 
HETATM 5616 FE FE  . HEM C 2 .   ? 10.364  -4.416  -0.484  1.00 11.34 ? 501 HEM A FE  1 
HETATM 5617 C  CHA . HEM D 2 .   ? 13.328  1.211   45.062  1.00 11.56 ? 501 HEM B CHA 1 
HETATM 5618 C  CHB . HEM D 2 .   ? 15.734  2.523   41.157  1.00 12.93 ? 501 HEM B CHB 1 
HETATM 5619 C  CHC . HEM D 2 .   ? 12.885  6.351   40.627  1.00 10.96 ? 501 HEM B CHC 1 
HETATM 5620 C  CHD . HEM D 2 .   ? 10.322  4.874   44.398  1.00 11.62 ? 501 HEM B CHD 1 
HETATM 5621 C  C1A . HEM D 2 .   ? 14.257  1.252   44.070  1.00 11.88 ? 501 HEM B C1A 1 
HETATM 5622 C  C2A . HEM D 2 .   ? 15.344  0.337   43.911  1.00 11.76 ? 501 HEM B C2A 1 
HETATM 5623 C  C3A . HEM D 2 .   ? 16.027  0.697   42.756  1.00 12.94 ? 501 HEM B C3A 1 
HETATM 5624 C  C4A . HEM D 2 .   ? 15.362  1.857   42.243  1.00 11.94 ? 501 HEM B C4A 1 
HETATM 5625 C  CMA . HEM D 2 .   ? 17.285  0.083   42.175  1.00 14.74 ? 501 HEM B CMA 1 
HETATM 5626 C  CAA . HEM D 2 .   ? 15.630  -0.810  44.832  1.00 12.79 ? 501 HEM B CAA 1 
HETATM 5627 C  CBA . HEM D 2 .   ? 15.021  -2.153  44.538  1.00 12.74 ? 501 HEM B CBA 1 
HETATM 5628 C  CGA . HEM D 2 .   ? 13.561  -2.133  44.671  1.00 13.14 ? 501 HEM B CGA 1 
HETATM 5629 O  O1A . HEM D 2 .   ? 12.891  -1.903  43.631  1.00 14.58 ? 501 HEM B O1A 1 
HETATM 5630 O  O2A . HEM D 2 .   ? 13.039  -2.304  45.763  1.00 14.46 ? 501 HEM B O2A 1 
HETATM 5631 C  C1B . HEM D 2 .   ? 15.180  3.683   40.645  1.00 12.10 ? 501 HEM B C1B 1 
HETATM 5632 C  C2B . HEM D 2 .   ? 15.625  4.336   39.460  1.00 12.66 ? 501 HEM B C2B 1 
HETATM 5633 C  C3B . HEM D 2 .   ? 14.822  5.422   39.313  1.00 11.82 ? 501 HEM B C3B 1 
HETATM 5634 C  C4B . HEM D 2 .   ? 13.856  5.413   40.416  1.00 11.75 ? 501 HEM B C4B 1 
HETATM 5635 C  CMB . HEM D 2 .   ? 16.780  3.904   38.606  1.00 15.43 ? 501 HEM B CMB 1 
HETATM 5636 C  CAB . HEM D 2 .   ? 14.809  6.463   38.267  1.00 13.15 ? 501 HEM B CAB 1 
HETATM 5637 C  CBB . HEM D 2 .   ? 15.374  6.328   37.109  1.00 15.03 ? 501 HEM B CBB 1 
HETATM 5638 C  C1C . HEM D 2 .   ? 11.911  6.339   41.597  1.00 11.53 ? 501 HEM B C1C 1 
HETATM 5639 C  C2C . HEM D 2 .   ? 10.879  7.246   41.793  1.00 11.96 ? 501 HEM B C2C 1 
HETATM 5640 C  C3C . HEM D 2 .   ? 10.205  6.832   42.865  1.00 11.60 ? 501 HEM B C3C 1 
HETATM 5641 C  C4C . HEM D 2 .   ? 10.790  5.621   43.356  1.00 12.53 ? 501 HEM B C4C 1 
HETATM 5642 C  CMC . HEM D 2 .   ? 10.600  8.437   40.911  1.00 12.87 ? 501 HEM B CMC 1 
HETATM 5643 C  CAC . HEM D 2 .   ? 9.022   7.417   43.511  1.00 13.04 ? 501 HEM B CAC 1 
HETATM 5644 C  CBC . HEM D 2 .   ? 8.632   8.624   43.492  1.00 13.97 ? 501 HEM B CBC 1 
HETATM 5645 C  C1D . HEM D 2 .   ? 10.928  3.709   44.849  1.00 11.45 ? 501 HEM B C1D 1 
HETATM 5646 C  C2D . HEM D 2 .   ? 10.383  2.928   45.946  1.00 12.51 ? 501 HEM B C2D 1 
HETATM 5647 C  C3D . HEM D 2 .   ? 11.236  1.929   46.128  1.00 12.10 ? 501 HEM B C3D 1 
HETATM 5648 C  C4D . HEM D 2 .   ? 12.279  2.085   45.147  1.00 12.45 ? 501 HEM B C4D 1 
HETATM 5649 C  CMD . HEM D 2 .   ? 9.109   3.205   46.701  1.00 13.13 ? 501 HEM B CMD 1 
HETATM 5650 C  CAD . HEM D 2 .   ? 11.121  0.801   47.140  1.00 12.02 ? 501 HEM B CAD 1 
HETATM 5651 C  CBD . HEM D 2 .   ? 11.728  1.200   48.482  1.00 13.92 ? 501 HEM B CBD 1 
HETATM 5652 C  CGD . HEM D 2 .   ? 11.466  0.151   49.506  1.00 14.70 ? 501 HEM B CGD 1 
HETATM 5653 O  O1D . HEM D 2 .   ? 12.411  -0.556  49.810  1.00 14.53 ? 501 HEM B O1D 1 
HETATM 5654 O  O2D . HEM D 2 .   ? 10.327  0.008   49.972  1.00 15.85 ? 501 HEM B O2D 1 
HETATM 5655 N  NA  . HEM D 2 .   ? 14.333  2.169   43.016  1.00 11.72 ? 501 HEM B NA  1 
HETATM 5656 N  NB  . HEM D 2 .   ? 14.127  4.341   41.146  1.00 12.43 ? 501 HEM B NB  1 
HETATM 5657 N  NC  . HEM D 2 .   ? 11.860  5.346   42.567  1.00 11.51 ? 501 HEM B NC  1 
HETATM 5658 N  ND  . HEM D 2 .   ? 12.072  3.181   44.375  1.00 11.53 ? 501 HEM B ND  1 
HETATM 5659 FE FE  . HEM D 2 .   ? 13.202  3.847   42.925  1.00 11.51 ? 501 HEM B FE  1 
HETATM 5660 O  O   . HOH E 3 .   ? 1.296   -20.430 3.134   1.00 33.06 ? 601 HOH A O   1 
HETATM 5661 O  O   . HOH E 3 .   ? 12.020  -9.804  22.214  1.00 36.92 ? 602 HOH A O   1 
HETATM 5662 O  O   . HOH E 3 .   ? 13.252  -13.935 15.735  1.00 37.63 ? 603 HOH A O   1 
HETATM 5663 O  O   . HOH E 3 .   ? 11.995  -11.783 21.641  1.00 32.63 ? 604 HOH A O   1 
HETATM 5664 O  O   . HOH E 3 .   ? 18.059  -19.988 20.632  1.00 41.67 ? 605 HOH A O   1 
HETATM 5665 O  O   . HOH E 3 .   ? 14.794  -3.078  31.730  1.00 38.27 ? 606 HOH A O   1 
HETATM 5666 O  O   . HOH E 3 .   ? 0.677   10.674  5.820   1.00 43.12 ? 607 HOH A O   1 
HETATM 5667 O  O   . HOH E 3 .   ? 24.528  13.083  14.025  1.00 38.09 ? 608 HOH A O   1 
HETATM 5668 O  O   . HOH E 3 .   ? 32.813  8.872   -0.649  1.00 44.47 ? 609 HOH A O   1 
HETATM 5669 O  O   . HOH E 3 .   ? 23.666  -9.072  -4.730  1.00 24.89 ? 610 HOH A O   1 
HETATM 5670 O  O   . HOH E 3 .   ? 6.677   -2.965  -14.748 1.00 39.56 ? 611 HOH A O   1 
HETATM 5671 O  O   . HOH E 3 .   ? 38.444  -2.346  -5.178  1.00 36.02 ? 612 HOH A O   1 
HETATM 5672 O  O   . HOH E 3 .   ? -10.634 6.108   2.505   1.00 35.06 ? 613 HOH A O   1 
HETATM 5673 O  O   . HOH E 3 .   ? 8.465   -15.629 -11.093 1.00 39.39 ? 614 HOH A O   1 
HETATM 5674 O  O   . HOH E 3 .   ? 17.410  -2.836  -12.665 1.00 30.66 ? 615 HOH A O   1 
HETATM 5675 O  O   . HOH E 3 .   ? 28.435  7.355   1.071   1.00 36.37 ? 616 HOH A O   1 
HETATM 5676 O  O   . HOH E 3 .   ? 10.766  2.033   -12.469 1.00 28.54 ? 617 HOH A O   1 
HETATM 5677 O  O   . HOH E 3 .   ? 7.490   -5.170  12.066  1.00 27.91 ? 618 HOH A O   1 
HETATM 5678 O  O   . HOH E 3 .   ? 31.358  -14.960 -3.293  1.00 30.48 ? 619 HOH A O   1 
HETATM 5679 O  O   . HOH E 3 .   ? 39.124  -7.671  8.365   1.00 28.60 ? 620 HOH A O   1 
HETATM 5680 O  O   . HOH E 3 .   ? -5.091  0.286   -7.217  1.00 38.42 ? 621 HOH A O   1 
HETATM 5681 O  O   . HOH E 3 .   ? -5.555  -23.886 1.391   1.00 34.04 ? 622 HOH A O   1 
HETATM 5682 O  O   . HOH E 3 .   ? 30.142  12.868  14.697  1.00 43.05 ? 623 HOH A O   1 
HETATM 5683 O  O   . HOH E 3 .   ? 30.344  -4.433  -9.921  1.00 43.75 ? 624 HOH A O   1 
HETATM 5684 O  O   . HOH E 3 .   ? 49.649  4.892   20.061  1.00 25.44 ? 625 HOH A O   1 
HETATM 5685 O  O   . HOH E 3 .   ? -6.380  -10.321 1.384   1.00 33.12 ? 626 HOH A O   1 
HETATM 5686 O  O   . HOH E 3 .   ? 24.959  -13.223 33.990  1.00 37.28 ? 627 HOH A O   1 
HETATM 5687 O  O   . HOH E 3 .   ? 37.413  -20.695 14.975  1.00 40.91 ? 628 HOH A O   1 
HETATM 5688 O  O   . HOH E 3 .   ? 34.690  -6.513  -2.950  1.00 23.42 ? 629 HOH A O   1 
HETATM 5689 O  O   . HOH E 3 .   ? 35.931  -17.392 30.577  1.00 32.65 ? 630 HOH A O   1 
HETATM 5690 O  O   . HOH E 3 .   ? 39.701  6.072   -1.524  1.00 38.44 ? 631 HOH A O   1 
HETATM 5691 O  O   . HOH E 3 .   ? 8.230   -21.473 -4.642  1.00 35.73 ? 632 HOH A O   1 
HETATM 5692 O  O   . HOH E 3 .   ? 7.979   -8.237  13.618  1.00 31.45 ? 633 HOH A O   1 
HETATM 5693 O  O   . HOH E 3 .   ? 39.104  -12.826 8.451   1.00 39.82 ? 634 HOH A O   1 
HETATM 5694 O  O   . HOH E 3 .   ? 32.590  -7.574  -4.225  1.00 22.43 ? 635 HOH A O   1 
HETATM 5695 O  O   . HOH E 3 .   ? 28.243  -3.036  36.739  1.00 18.19 ? 636 HOH A O   1 
HETATM 5696 O  O   . HOH E 3 .   ? 15.312  -10.128 29.970  1.00 20.56 ? 637 HOH A O   1 
HETATM 5697 O  O   . HOH E 3 .   ? 4.813   -17.191 6.770   1.00 21.67 ? 638 HOH A O   1 
HETATM 5698 O  O   . HOH E 3 .   ? 16.790  -15.891 22.424  1.00 27.18 ? 639 HOH A O   1 
HETATM 5699 O  O   . HOH E 3 .   ? 7.568   -1.404  9.319   1.00 14.11 ? 640 HOH A O   1 
HETATM 5700 O  O   . HOH E 3 .   ? -6.625  10.836  6.619   1.00 20.97 ? 641 HOH A O   1 
HETATM 5701 O  O   . HOH E 3 .   ? -3.438  5.746   11.078  1.00 18.37 ? 642 HOH A O   1 
HETATM 5702 O  O   . HOH E 3 .   ? 14.202  8.139   -2.288  1.00 36.86 ? 643 HOH A O   1 
HETATM 5703 O  O   . HOH E 3 .   ? 24.531  -8.452  14.173  1.00 12.57 ? 644 HOH A O   1 
HETATM 5704 O  O   . HOH E 3 .   ? 32.689  -6.360  -6.626  1.00 33.93 ? 645 HOH A O   1 
HETATM 5705 O  O   . HOH E 3 .   ? -7.506  -10.167 -2.530  1.00 41.82 ? 646 HOH A O   1 
HETATM 5706 O  O   . HOH E 3 .   ? 32.155  -0.983  29.260  1.00 24.94 ? 647 HOH A O   1 
HETATM 5707 O  O   . HOH E 3 .   ? 3.011   9.682   11.042  1.00 28.57 ? 648 HOH A O   1 
HETATM 5708 O  O   . HOH E 3 .   ? 7.935   -11.052 -3.244  1.00 14.01 ? 649 HOH A O   1 
HETATM 5709 O  O   . HOH E 3 .   ? 36.708  9.788   9.051   1.00 40.25 ? 650 HOH A O   1 
HETATM 5710 O  O   . HOH E 3 .   ? 3.587   10.852  7.080   1.00 35.35 ? 651 HOH A O   1 
HETATM 5711 O  O   . HOH E 3 .   ? 31.346  -10.003 13.954  1.00 13.85 ? 652 HOH A O   1 
HETATM 5712 O  O   . HOH E 3 .   ? 25.657  0.745   35.070  1.00 30.67 ? 653 HOH A O   1 
HETATM 5713 O  O   . HOH E 3 .   ? 12.266  -7.997  4.317   1.00 14.11 ? 654 HOH A O   1 
HETATM 5714 O  O   . HOH E 3 .   ? 28.720  -16.832 20.867  1.00 26.31 ? 655 HOH A O   1 
HETATM 5715 O  O   . HOH E 3 .   ? 26.185  -14.269 8.874   1.00 15.12 ? 656 HOH A O   1 
HETATM 5716 O  O   . HOH E 3 .   ? 31.376  5.670   -5.051  1.00 45.71 ? 657 HOH A O   1 
HETATM 5717 O  O   . HOH E 3 .   ? 24.383  -11.899 30.208  1.00 30.77 ? 658 HOH A O   1 
HETATM 5718 O  O   . HOH E 3 .   ? 19.291  -18.315 8.480   1.00 23.33 ? 659 HOH A O   1 
HETATM 5719 O  O   . HOH E 3 .   ? 17.795  -14.666 -7.310  1.00 26.58 ? 660 HOH A O   1 
HETATM 5720 O  O   . HOH E 3 .   ? 25.003  0.307   -10.832 1.00 40.94 ? 661 HOH A O   1 
HETATM 5721 O  O   . HOH E 3 .   ? 10.989  -3.796  3.760   1.00 14.67 ? 662 HOH A O   1 
HETATM 5722 O  O   . HOH E 3 .   ? -4.649  -19.818 -8.267  1.00 43.12 ? 663 HOH A O   1 
HETATM 5723 O  O   . HOH E 3 .   ? -0.354  -16.584 6.739   1.00 43.04 ? 664 HOH A O   1 
HETATM 5724 O  O   . HOH E 3 .   ? 25.120  -7.595  25.792  1.00 15.70 ? 665 HOH A O   1 
HETATM 5725 O  O   . HOH E 3 .   ? 34.623  9.575   22.651  1.00 37.03 ? 666 HOH A O   1 
HETATM 5726 O  O   . HOH E 3 .   ? 32.543  -20.684 14.994  1.00 35.78 ? 667 HOH A O   1 
HETATM 5727 O  O   . HOH E 3 .   ? 10.131  -8.461  -15.201 1.00 32.86 ? 668 HOH A O   1 
HETATM 5728 O  O   . HOH E 3 .   ? -6.087  7.751   7.693   1.00 23.21 ? 669 HOH A O   1 
HETATM 5729 O  O   . HOH E 3 .   ? 33.051  -13.994 12.486  1.00 19.46 ? 670 HOH A O   1 
HETATM 5730 O  O   . HOH E 3 .   ? 0.162   -0.638  -8.205  1.00 26.50 ? 671 HOH A O   1 
HETATM 5731 O  O   . HOH E 3 .   ? -10.239 0.719   -4.534  1.00 32.75 ? 672 HOH A O   1 
HETATM 5732 O  O   . HOH E 3 .   ? 34.982  -2.085  40.326  1.00 24.93 ? 673 HOH A O   1 
HETATM 5733 O  O   . HOH E 3 .   ? 36.433  -15.217 4.903   1.00 35.93 ? 674 HOH A O   1 
HETATM 5734 O  O   . HOH E 3 .   ? 16.038  -8.015  -6.154  1.00 15.42 ? 675 HOH A O   1 
HETATM 5735 O  O   . HOH E 3 .   ? 36.167  0.021   34.446  1.00 44.64 ? 676 HOH A O   1 
HETATM 5736 O  O   . HOH E 3 .   ? 35.004  -1.974  29.752  1.00 34.97 ? 677 HOH A O   1 
HETATM 5737 O  O   . HOH E 3 .   ? 17.752  -14.337 29.677  1.00 33.11 ? 678 HOH A O   1 
HETATM 5738 O  O   . HOH E 3 .   ? 37.258  -8.891  10.525  1.00 25.64 ? 679 HOH A O   1 
HETATM 5739 O  O   . HOH E 3 .   ? 20.599  8.418   -1.966  1.00 23.36 ? 680 HOH A O   1 
HETATM 5740 O  O   . HOH E 3 .   ? -3.270  14.819  12.446  1.00 17.10 ? 681 HOH A O   1 
HETATM 5741 O  O   . HOH E 3 .   ? 37.234  -12.045 25.287  1.00 18.75 ? 682 HOH A O   1 
HETATM 5742 O  O   . HOH E 3 .   ? 14.271  -11.741 -3.974  1.00 16.25 ? 683 HOH A O   1 
HETATM 5743 O  O   . HOH E 3 .   ? 6.692   -16.258 -3.430  1.00 17.32 ? 684 HOH A O   1 
HETATM 5744 O  O   . HOH E 3 .   ? 10.924  -15.905 9.581   1.00 19.50 ? 685 HOH A O   1 
HETATM 5745 O  O   . HOH E 3 .   ? 25.306  -17.303 12.125  1.00 28.70 ? 686 HOH A O   1 
HETATM 5746 O  O   . HOH E 3 .   ? 5.269   8.047   10.150  1.00 22.99 ? 687 HOH A O   1 
HETATM 5747 O  O   . HOH E 3 .   ? 19.790  -8.053  33.609  1.00 22.00 ? 688 HOH A O   1 
HETATM 5748 O  O   . HOH E 3 .   ? 10.094  -16.007 -8.919  1.00 24.41 ? 689 HOH A O   1 
HETATM 5749 O  O   . HOH E 3 .   ? 9.876   2.154   -3.282  1.00 19.21 ? 690 HOH A O   1 
HETATM 5750 O  O   . HOH E 3 .   ? 24.965  -15.088 20.797  1.00 14.69 ? 691 HOH A O   1 
HETATM 5751 O  O   . HOH E 3 .   ? 7.147   -19.762 12.606  1.00 34.90 ? 692 HOH A O   1 
HETATM 5752 O  O   . HOH E 3 .   ? -4.001  -9.439  -13.298 1.00 39.31 ? 693 HOH A O   1 
HETATM 5753 O  O   . HOH E 3 .   ? -8.532  -6.881  -2.717  1.00 40.86 ? 694 HOH A O   1 
HETATM 5754 O  O   . HOH E 3 .   ? -4.469  7.056   0.423   1.00 24.93 ? 695 HOH A O   1 
HETATM 5755 O  O   . HOH E 3 .   ? 24.393  6.859   1.832   1.00 28.32 ? 696 HOH A O   1 
HETATM 5756 O  O   . HOH E 3 .   ? 14.771  4.404   -12.974 1.00 42.69 ? 697 HOH A O   1 
HETATM 5757 O  O   . HOH E 3 .   ? 17.725  -0.318  -12.546 1.00 28.27 ? 698 HOH A O   1 
HETATM 5758 O  O   . HOH E 3 .   ? 0.545   4.627   -5.343  1.00 23.18 ? 699 HOH A O   1 
HETATM 5759 O  O   . HOH E 3 .   ? -3.512  9.858   15.065  1.00 21.90 ? 700 HOH A O   1 
HETATM 5760 O  O   . HOH E 3 .   ? 12.217  2.503   -1.958  1.00 21.83 ? 701 HOH A O   1 
HETATM 5761 O  O   . HOH E 3 .   ? -2.777  -6.481  -7.835  1.00 23.88 ? 702 HOH A O   1 
HETATM 5762 O  O   . HOH E 3 .   ? 30.885  7.253   5.499   1.00 31.28 ? 703 HOH A O   1 
HETATM 5763 O  O   . HOH E 3 .   ? 34.928  3.048   -3.801  1.00 39.15 ? 704 HOH A O   1 
HETATM 5764 O  O   . HOH E 3 .   ? 12.016  8.682   -0.658  1.00 22.53 ? 705 HOH A O   1 
HETATM 5765 O  O   . HOH E 3 .   ? 14.838  -15.307 9.927   1.00 13.45 ? 706 HOH A O   1 
HETATM 5766 O  O   . HOH E 3 .   ? -1.848  -1.257  7.220   1.00 27.64 ? 707 HOH A O   1 
HETATM 5767 O  O   . HOH E 3 .   ? 27.619  -17.866 13.460  1.00 26.97 ? 708 HOH A O   1 
HETATM 5768 O  O   . HOH E 3 .   ? 27.133  -9.496  28.652  1.00 18.84 ? 709 HOH A O   1 
HETATM 5769 O  O   . HOH E 3 .   ? -4.351  10.491  -0.687  1.00 29.82 ? 710 HOH A O   1 
HETATM 5770 O  O   . HOH E 3 .   ? 9.878   -16.640 6.597   1.00 17.75 ? 711 HOH A O   1 
HETATM 5771 O  O   . HOH E 3 .   ? 11.657  -16.243 3.857   1.00 22.66 ? 712 HOH A O   1 
HETATM 5772 O  O   . HOH E 3 .   ? 12.516  -13.833 10.493  1.00 16.59 ? 713 HOH A O   1 
HETATM 5773 O  O   . HOH E 3 .   ? 23.064  -8.878  -7.571  1.00 29.66 ? 714 HOH A O   1 
HETATM 5774 O  O   . HOH E 3 .   ? 25.481  -10.211 26.431  1.00 16.61 ? 715 HOH A O   1 
HETATM 5775 O  O   . HOH E 3 .   ? 18.017  14.319  0.446   1.00 27.85 ? 716 HOH A O   1 
HETATM 5776 O  O   . HOH E 3 .   ? 11.172  -5.303  1.535   1.00 13.35 ? 717 HOH A O   1 
HETATM 5777 O  O   . HOH E 3 .   ? 36.799  -8.438  -2.928  1.00 28.41 ? 718 HOH A O   1 
HETATM 5778 O  O   . HOH E 3 .   ? 33.106  5.091   31.457  1.00 30.56 ? 719 HOH A O   1 
HETATM 5779 O  O   . HOH E 3 .   ? 32.054  6.095   22.073  1.00 29.81 ? 720 HOH A O   1 
HETATM 5780 O  O   . HOH E 3 .   ? 10.059  -2.376  23.113  1.00 34.04 ? 721 HOH A O   1 
HETATM 5781 O  O   . HOH E 3 .   ? 16.745  -13.416 -12.274 1.00 37.60 ? 722 HOH A O   1 
HETATM 5782 O  O   . HOH E 3 .   ? 25.926  -7.089  32.412  1.00 17.09 ? 723 HOH A O   1 
HETATM 5783 O  O   . HOH E 3 .   ? 4.322   -12.474 1.140   1.00 15.01 ? 724 HOH A O   1 
HETATM 5784 O  O   . HOH E 3 .   ? -3.186  -6.950  -10.600 1.00 29.55 ? 725 HOH A O   1 
HETATM 5785 O  O   . HOH E 3 .   ? 14.853  -14.544 -3.726  1.00 27.57 ? 726 HOH A O   1 
HETATM 5786 O  O   . HOH E 3 .   ? 19.794  12.640  -1.813  1.00 38.87 ? 727 HOH A O   1 
HETATM 5787 O  O   . HOH E 3 .   ? 48.105  -1.088  18.273  1.00 32.32 ? 728 HOH A O   1 
HETATM 5788 O  O   . HOH E 3 .   ? 27.341  -14.017 17.832  1.00 16.03 ? 729 HOH A O   1 
HETATM 5789 O  O   . HOH E 3 .   ? 15.579  -9.953  -1.187  1.00 14.98 ? 730 HOH A O   1 
HETATM 5790 O  O   . HOH E 3 .   ? 6.372   1.030   -13.543 1.00 36.33 ? 731 HOH A O   1 
HETATM 5791 O  O   . HOH E 3 .   ? 44.056  -15.617 13.699  1.00 37.19 ? 732 HOH A O   1 
HETATM 5792 O  O   . HOH E 3 .   ? 21.371  -5.493  -12.783 1.00 41.54 ? 733 HOH A O   1 
HETATM 5793 O  O   . HOH E 3 .   ? 3.463   -9.767  1.372   1.00 14.68 ? 734 HOH A O   1 
HETATM 5794 O  O   . HOH E 3 .   ? 25.722  -7.620  -5.535  1.00 24.10 ? 735 HOH A O   1 
HETATM 5795 O  O   . HOH E 3 .   ? 31.599  -11.199 6.939   1.00 16.52 ? 736 HOH A O   1 
HETATM 5796 O  O   . HOH E 3 .   ? 43.825  -3.575  22.738  1.00 35.72 ? 737 HOH A O   1 
HETATM 5797 O  O   . HOH E 3 .   ? 14.762  14.267  6.757   1.00 33.17 ? 738 HOH A O   1 
HETATM 5798 O  O   . HOH E 3 .   ? 9.479   11.676  -1.074  1.00 40.88 ? 739 HOH A O   1 
HETATM 5799 O  O   . HOH E 3 .   ? 30.605  1.201   34.581  1.00 27.60 ? 740 HOH A O   1 
HETATM 5800 O  O   . HOH E 3 .   ? 14.782  5.474   -7.581  1.00 25.57 ? 741 HOH A O   1 
HETATM 5801 O  O   . HOH E 3 .   ? 8.810   8.718   -1.906  1.00 31.94 ? 742 HOH A O   1 
HETATM 5802 O  O   . HOH E 3 .   ? 19.936  -7.077  10.382  1.00 13.91 ? 743 HOH A O   1 
HETATM 5803 O  O   . HOH E 3 .   ? 5.010   -12.889 -15.847 1.00 34.80 ? 744 HOH A O   1 
HETATM 5804 O  O   . HOH E 3 .   ? 33.263  -15.815 25.421  1.00 32.24 ? 745 HOH A O   1 
HETATM 5805 O  O   . HOH E 3 .   ? 37.420  -11.063 30.346  1.00 32.06 ? 746 HOH A O   1 
HETATM 5806 O  O   . HOH E 3 .   ? 15.970  -2.933  20.137  1.00 25.62 ? 747 HOH A O   1 
HETATM 5807 O  O   . HOH E 3 .   ? 36.830  7.578   1.021   1.00 32.64 ? 748 HOH A O   1 
HETATM 5808 O  O   . HOH E 3 .   ? 1.334   -13.466 -9.576  1.00 19.21 ? 749 HOH A O   1 
HETATM 5809 O  O   . HOH E 3 .   ? 16.401  10.432  9.477   1.00 33.31 ? 750 HOH A O   1 
HETATM 5810 O  O   . HOH E 3 .   ? -1.862  -21.097 -6.275  1.00 28.79 ? 751 HOH A O   1 
HETATM 5811 O  O   . HOH E 3 .   ? 31.230  -6.489  44.635  1.00 44.80 ? 752 HOH A O   1 
HETATM 5812 O  O   . HOH E 3 .   ? 13.253  -17.556 12.426  1.00 33.34 ? 753 HOH A O   1 
HETATM 5813 O  O   . HOH E 3 .   ? 4.783   -10.336 12.220  1.00 27.02 ? 754 HOH A O   1 
HETATM 5814 O  O   . HOH E 3 .   ? 33.480  -4.446  39.866  1.00 26.04 ? 755 HOH A O   1 
HETATM 5815 O  O   . HOH E 3 .   ? 14.937  -16.207 13.745  1.00 28.00 ? 756 HOH A O   1 
HETATM 5816 O  O   . HOH E 3 .   ? 29.137  9.244   21.753  1.00 38.60 ? 757 HOH A O   1 
HETATM 5817 O  O   . HOH E 3 .   ? 28.743  5.354   6.100   1.00 19.60 ? 758 HOH A O   1 
HETATM 5818 O  O   . HOH E 3 .   ? 30.353  -12.578 14.258  1.00 14.80 ? 759 HOH A O   1 
HETATM 5819 O  O   . HOH E 3 .   ? 1.595   19.369  18.600  1.00 41.08 ? 760 HOH A O   1 
HETATM 5820 O  O   . HOH E 3 .   ? 30.358  -12.917 33.113  1.00 32.22 ? 761 HOH A O   1 
HETATM 5821 O  O   . HOH E 3 .   ? 37.456  -5.858  25.972  1.00 29.17 ? 762 HOH A O   1 
HETATM 5822 O  O   . HOH E 3 .   ? 36.121  -8.016  27.482  1.00 22.57 ? 763 HOH A O   1 
HETATM 5823 O  O   . HOH E 3 .   ? -4.118  -0.121  6.722   1.00 22.06 ? 764 HOH A O   1 
HETATM 5824 O  O   . HOH E 3 .   ? 31.411  -15.863 21.754  1.00 24.77 ? 765 HOH A O   1 
HETATM 5825 O  O   . HOH E 3 .   ? -0.552  -14.450 8.958   1.00 38.16 ? 766 HOH A O   1 
HETATM 5826 O  O   . HOH E 3 .   ? 15.472  -4.658  4.915   1.00 16.83 ? 767 HOH A O   1 
HETATM 5827 O  O   . HOH E 3 .   ? 8.704   -10.257 19.957  1.00 47.80 ? 768 HOH A O   1 
HETATM 5828 O  O   . HOH E 3 .   ? 33.828  -15.946 32.766  1.00 35.57 ? 769 HOH A O   1 
HETATM 5829 O  O   . HOH E 3 .   ? 30.181  9.546   6.858   1.00 33.53 ? 770 HOH A O   1 
HETATM 5830 O  O   . HOH E 3 .   ? 1.178   -10.147 3.232   1.00 15.50 ? 771 HOH A O   1 
HETATM 5831 O  O   . HOH E 3 .   ? -2.939  0.917   -5.742  1.00 41.42 ? 772 HOH A O   1 
HETATM 5832 O  O   . HOH E 3 .   ? -0.212  -5.345  -8.483  1.00 18.00 ? 773 HOH A O   1 
HETATM 5833 O  O   . HOH E 3 .   ? 8.544   -18.279 -2.948  1.00 24.57 ? 774 HOH A O   1 
HETATM 5834 O  O   . HOH E 3 .   ? 43.817  -11.585 9.167   1.00 36.00 ? 775 HOH A O   1 
HETATM 5835 O  O   . HOH E 3 .   ? 28.355  -11.917 16.293  1.00 14.03 ? 776 HOH A O   1 
HETATM 5836 O  O   . HOH E 3 .   ? 35.880  -14.453 25.726  1.00 25.38 ? 777 HOH A O   1 
HETATM 5837 O  O   . HOH E 3 .   ? 6.983   11.787  0.777   1.00 33.67 ? 778 HOH A O   1 
HETATM 5838 O  O   . HOH E 3 .   ? 13.571  -16.566 1.128   1.00 26.61 ? 779 HOH A O   1 
HETATM 5839 O  O   . HOH E 3 .   ? 28.136  -19.313 26.730  1.00 44.04 ? 780 HOH A O   1 
HETATM 5840 O  O   . HOH E 3 .   ? 7.267   -18.924 5.599   1.00 25.56 ? 781 HOH A O   1 
HETATM 5841 O  O   . HOH E 3 .   ? 28.348  4.270   26.595  1.00 20.78 ? 782 HOH A O   1 
HETATM 5842 O  O   . HOH E 3 .   ? 5.485   -17.595 -12.512 1.00 28.08 ? 783 HOH A O   1 
HETATM 5843 O  O   . HOH E 3 .   ? 30.417  -20.010 27.843  1.00 28.66 ? 784 HOH A O   1 
HETATM 5844 O  O   . HOH E 3 .   ? 11.912  5.452   -3.728  1.00 37.90 ? 785 HOH A O   1 
HETATM 5845 O  O   . HOH E 3 .   ? 20.404  17.266  6.088   1.00 36.70 ? 786 HOH A O   1 
HETATM 5846 O  O   . HOH E 3 .   ? 16.298  -9.824  -3.998  1.00 15.44 ? 787 HOH A O   1 
HETATM 5847 O  O   . HOH E 3 .   ? -3.168  -13.489 -4.047  1.00 23.19 ? 788 HOH A O   1 
HETATM 5848 O  O   . HOH E 3 .   ? 40.756  -14.447 22.796  1.00 32.65 ? 789 HOH A O   1 
HETATM 5849 O  O   . HOH E 3 .   ? 45.687  2.945   22.432  1.00 37.41 ? 790 HOH A O   1 
HETATM 5850 O  O   . HOH E 3 .   ? 34.973  -4.615  37.053  1.00 28.07 ? 791 HOH A O   1 
HETATM 5851 O  O   . HOH E 3 .   ? -2.202  -7.986  -5.437  1.00 22.40 ? 792 HOH A O   1 
HETATM 5852 O  O   . HOH E 3 .   ? 23.576  -11.717 27.581  1.00 22.39 ? 793 HOH A O   1 
HETATM 5853 O  O   . HOH E 3 .   ? 29.205  -16.663 10.781  1.00 27.10 ? 794 HOH A O   1 
HETATM 5854 O  O   . HOH E 3 .   ? 25.943  12.479  6.277   1.00 37.59 ? 795 HOH A O   1 
HETATM 5855 O  O   . HOH E 3 .   ? 18.877  -17.459 -7.257  1.00 34.42 ? 796 HOH A O   1 
HETATM 5856 O  O   . HOH E 3 .   ? 30.404  -10.019 36.476  1.00 29.58 ? 797 HOH A O   1 
HETATM 5857 O  O   . HOH E 3 .   ? 26.318  6.989   -0.008  1.00 32.35 ? 798 HOH A O   1 
HETATM 5858 O  O   . HOH E 3 .   ? 11.156  -3.338  -14.552 1.00 34.75 ? 799 HOH A O   1 
HETATM 5859 O  O   . HOH E 3 .   ? 18.142  -2.406  22.023  1.00 31.52 ? 800 HOH A O   1 
HETATM 5860 O  O   . HOH E 3 .   ? 26.770  -12.116 32.506  1.00 34.73 ? 801 HOH A O   1 
HETATM 5861 O  O   . HOH E 3 .   ? 6.881   -14.095 -13.600 1.00 22.78 ? 802 HOH A O   1 
HETATM 5862 O  O   . HOH E 3 .   ? -4.541  -9.115  -4.659  1.00 28.19 ? 803 HOH A O   1 
HETATM 5863 O  O   . HOH E 3 .   ? 10.411  -9.250  15.931  1.00 23.74 ? 804 HOH A O   1 
HETATM 5864 O  O   . HOH E 3 .   ? 15.231  -21.952 11.355  1.00 54.20 ? 805 HOH A O   1 
HETATM 5865 O  O   . HOH E 3 .   ? 43.225  -5.806  -0.161  1.00 35.35 ? 806 HOH A O   1 
HETATM 5866 O  O   . HOH E 3 .   ? 11.008  4.499   20.614  1.00 45.73 ? 807 HOH A O   1 
HETATM 5867 O  O   . HOH E 3 .   ? 35.498  -4.141  -4.438  1.00 31.36 ? 808 HOH A O   1 
HETATM 5868 O  O   . HOH E 3 .   ? 39.363  -12.298 23.468  1.00 20.76 ? 809 HOH A O   1 
HETATM 5869 O  O   . HOH E 3 .   ? 1.330   9.349   8.879   1.00 24.13 ? 810 HOH A O   1 
HETATM 5870 O  O   . HOH E 3 .   ? 22.027  -22.018 -2.737  1.00 37.14 ? 811 HOH A O   1 
HETATM 5871 O  O   . HOH E 3 .   ? 27.473  -18.810 3.788   1.00 33.91 ? 812 HOH A O   1 
HETATM 5872 O  O   . HOH E 3 .   ? 13.014  6.587   -5.841  1.00 36.98 ? 813 HOH A O   1 
HETATM 5873 O  O   . HOH E 3 .   ? 14.731  -18.620 0.008   1.00 38.02 ? 814 HOH A O   1 
HETATM 5874 O  O   . HOH E 3 .   ? 13.837  -10.382 4.365   1.00 14.53 ? 815 HOH A O   1 
HETATM 5875 O  O   . HOH E 3 .   ? -1.596  7.815   14.443  1.00 21.16 ? 816 HOH A O   1 
HETATM 5876 O  O   . HOH E 3 .   ? 32.698  -19.245 17.514  1.00 32.83 ? 817 HOH A O   1 
HETATM 5877 O  O   . HOH E 3 .   ? 31.025  -18.133 8.835   1.00 29.91 ? 818 HOH A O   1 
HETATM 5878 O  O   . HOH E 3 .   ? 3.375   -20.854 1.400   1.00 22.17 ? 819 HOH A O   1 
HETATM 5879 O  O   . HOH E 3 .   ? 14.935  -15.226 -7.726  1.00 27.99 ? 820 HOH A O   1 
HETATM 5880 O  O   . HOH E 3 .   ? 14.349  -16.450 3.703   1.00 28.30 ? 821 HOH A O   1 
HETATM 5881 O  O   . HOH E 3 .   ? 7.925   12.026  19.863  1.00 39.06 ? 822 HOH A O   1 
HETATM 5882 O  O   . HOH E 3 .   ? 18.334  -19.832 15.748  1.00 38.14 ? 823 HOH A O   1 
HETATM 5883 O  O   . HOH E 3 .   ? 11.734  -0.142  22.670  1.00 33.02 ? 824 HOH A O   1 
HETATM 5884 O  O   . HOH E 3 .   ? 20.498  9.166   16.289  1.00 22.63 ? 825 HOH A O   1 
HETATM 5885 O  O   . HOH E 3 .   ? 27.520  6.379   3.830   1.00 26.63 ? 826 HOH A O   1 
HETATM 5886 O  O   . HOH E 3 .   ? 39.045  -10.568 10.493  1.00 35.98 ? 827 HOH A O   1 
HETATM 5887 O  O   . HOH E 3 .   ? 4.816   -19.858 3.872   1.00 36.17 ? 828 HOH A O   1 
HETATM 5888 O  O   . HOH E 3 .   ? 23.994  -21.947 23.405  1.00 41.65 ? 829 HOH A O   1 
HETATM 5889 O  O   . HOH E 3 .   ? 25.650  8.461   3.619   1.00 35.74 ? 830 HOH A O   1 
HETATM 5890 O  O   . HOH E 3 .   ? 16.323  6.520   -9.816  1.00 33.71 ? 831 HOH A O   1 
HETATM 5891 O  O   . HOH E 3 .   ? 11.689  1.452   17.368  1.00 24.48 ? 832 HOH A O   1 
HETATM 5892 O  O   . HOH E 3 .   ? 44.863  9.598   10.425  1.00 44.75 ? 833 HOH A O   1 
HETATM 5893 O  O   . HOH E 3 .   ? -4.339  -15.943 -1.475  1.00 31.99 ? 834 HOH A O   1 
HETATM 5894 O  O   . HOH E 3 .   ? 12.978  -5.252  5.136   1.00 26.90 ? 835 HOH A O   1 
HETATM 5895 O  O   . HOH E 3 .   ? 15.803  -7.503  31.416  1.00 29.29 ? 836 HOH A O   1 
HETATM 5896 O  O   . HOH E 3 .   ? 13.609  -16.698 -2.803  1.00 35.81 ? 837 HOH A O   1 
HETATM 5897 O  O   . HOH E 3 .   ? 22.657  -19.366 9.254   1.00 40.54 ? 838 HOH A O   1 
HETATM 5898 O  O   . HOH E 3 .   ? 33.484  -15.517 0.720   1.00 35.96 ? 839 HOH A O   1 
HETATM 5899 O  O   . HOH E 3 .   ? 26.432  -9.648  31.401  1.00 24.41 ? 840 HOH A O   1 
HETATM 5900 O  O   . HOH E 3 .   ? 42.273  -6.248  23.821  1.00 41.25 ? 841 HOH A O   1 
HETATM 5901 O  O   . HOH E 3 .   ? -1.755  8.186   11.404  1.00 26.06 ? 842 HOH A O   1 
HETATM 5902 O  O   . HOH E 3 .   ? 22.342  1.495   -11.987 1.00 49.85 ? 843 HOH A O   1 
HETATM 5903 O  O   . HOH E 3 .   ? 22.788  9.321   -0.857  1.00 34.46 ? 844 HOH A O   1 
HETATM 5904 O  O   . HOH E 3 .   ? 48.160  2.680   21.007  1.00 35.46 ? 845 HOH A O   1 
HETATM 5905 O  O   . HOH E 3 .   ? 37.898  -10.366 27.466  1.00 24.22 ? 846 HOH A O   1 
HETATM 5906 O  O   . HOH E 3 .   ? 6.787   -12.845 13.077  1.00 44.88 ? 847 HOH A O   1 
HETATM 5907 O  O   . HOH E 3 .   ? 26.761  -16.923 9.401   1.00 27.02 ? 848 HOH A O   1 
HETATM 5908 O  O   . HOH E 3 .   ? -1.681  1.101   -7.462  1.00 41.62 ? 849 HOH A O   1 
HETATM 5909 O  O   . HOH E 3 .   ? -3.939  9.617   11.740  1.00 34.32 ? 850 HOH A O   1 
HETATM 5910 O  O   . HOH E 3 .   ? 20.606  0.423   -13.009 1.00 41.15 ? 851 HOH A O   1 
HETATM 5911 O  O   . HOH E 3 .   ? 6.650   -16.426 -15.098 1.00 35.10 ? 852 HOH A O   1 
HETATM 5912 O  O   . HOH E 3 .   ? 41.824  -10.947 23.999  1.00 42.14 ? 853 HOH A O   1 
HETATM 5913 O  O   . HOH E 3 .   ? 5.860   -14.832 -17.446 1.00 45.43 ? 854 HOH A O   1 
HETATM 5914 O  O   . HOH E 3 .   ? 5.192   -0.587  -18.217 1.00 45.45 ? 855 HOH A O   1 
HETATM 5915 O  O   . HOH F 3 .   ? -16.167 6.824   17.309  1.00 36.89 ? 601 HOH B O   1 
HETATM 5916 O  O   . HOH F 3 .   ? 3.855   -13.221 22.345  1.00 31.48 ? 602 HOH B O   1 
HETATM 5917 O  O   . HOH F 3 .   ? 21.985  14.655  47.849  1.00 39.93 ? 603 HOH B O   1 
HETATM 5918 O  O   . HOH F 3 .   ? 13.152  -2.739  56.767  1.00 42.69 ? 604 HOH B O   1 
HETATM 5919 O  O   . HOH F 3 .   ? -20.995 17.317  35.623  1.00 38.67 ? 605 HOH B O   1 
HETATM 5920 O  O   . HOH F 3 .   ? -21.477 12.583  33.676  1.00 33.68 ? 606 HOH B O   1 
HETATM 5921 O  O   . HOH F 3 .   ? 5.691   5.562   19.199  1.00 29.69 ? 607 HOH B O   1 
HETATM 5922 O  O   . HOH F 3 .   ? 6.420   -10.911 16.726  1.00 36.16 ? 608 HOH B O   1 
HETATM 5923 O  O   . HOH F 3 .   ? 5.867   2.246   57.144  1.00 36.89 ? 609 HOH B O   1 
HETATM 5924 O  O   . HOH F 3 .   ? -19.873 22.530  21.105  1.00 35.18 ? 610 HOH B O   1 
HETATM 5925 O  O   . HOH F 3 .   ? 3.082   10.059  54.062  1.00 38.34 ? 611 HOH B O   1 
HETATM 5926 O  O   . HOH F 3 .   ? 22.553  12.335  29.547  1.00 37.25 ? 612 HOH B O   1 
HETATM 5927 O  O   . HOH F 3 .   ? -2.638  17.951  21.047  1.00 27.80 ? 613 HOH B O   1 
HETATM 5928 O  O   . HOH F 3 .   ? 6.504   -2.747  49.805  1.00 29.90 ? 614 HOH B O   1 
HETATM 5929 O  O   . HOH F 3 .   ? 14.105  -7.381  27.802  1.00 21.26 ? 615 HOH B O   1 
HETATM 5930 O  O   . HOH F 3 .   ? 28.455  -5.785  44.183  1.00 35.97 ? 616 HOH B O   1 
HETATM 5931 O  O   . HOH F 3 .   ? 1.283   -5.737  38.358  1.00 33.26 ? 617 HOH B O   1 
HETATM 5932 O  O   . HOH F 3 .   ? 26.911  6.248   25.177  1.00 28.53 ? 618 HOH B O   1 
HETATM 5933 O  O   . HOH F 3 .   ? 17.378  -12.692 27.627  1.00 27.00 ? 619 HOH B O   1 
HETATM 5934 O  O   . HOH F 3 .   ? -9.611  0.319   48.289  1.00 24.01 ? 620 HOH B O   1 
HETATM 5935 O  O   . HOH F 3 .   ? 9.185   -10.529 25.037  1.00 34.52 ? 621 HOH B O   1 
HETATM 5936 O  O   . HOH F 3 .   ? 2.006   19.760  37.579  1.00 34.62 ? 622 HOH B O   1 
HETATM 5937 O  O   . HOH F 3 .   ? 24.016  14.059  50.941  1.00 40.11 ? 623 HOH B O   1 
HETATM 5938 O  O   . HOH F 3 .   ? 7.420   -0.814  56.373  1.00 40.71 ? 624 HOH B O   1 
HETATM 5939 O  O   . HOH F 3 .   ? -9.238  -9.066  34.079  1.00 24.59 ? 625 HOH B O   1 
HETATM 5940 O  O   . HOH F 3 .   ? -9.067  7.394   46.378  1.00 18.73 ? 626 HOH B O   1 
HETATM 5941 O  O   . HOH F 3 .   ? -1.133  -8.528  32.772  1.00 16.89 ? 627 HOH B O   1 
HETATM 5942 O  O   . HOH F 3 .   ? -4.311  -7.877  55.772  1.00 27.30 ? 628 HOH B O   1 
HETATM 5943 O  O   . HOH F 3 .   ? 16.069  -11.858 41.486  1.00 30.97 ? 629 HOH B O   1 
HETATM 5944 O  O   . HOH F 3 .   ? -11.277 0.334   12.391  1.00 35.83 ? 630 HOH B O   1 
HETATM 5945 O  O   . HOH F 3 .   ? -8.550  9.360   48.450  1.00 27.37 ? 631 HOH B O   1 
HETATM 5946 O  O   . HOH F 3 .   ? 7.233   -3.020  35.670  1.00 30.30 ? 632 HOH B O   1 
HETATM 5947 O  O   . HOH F 3 .   ? -19.976 9.935   16.653  1.00 47.16 ? 633 HOH B O   1 
HETATM 5948 O  O   . HOH F 3 .   ? -0.591  4.367   47.848  1.00 22.30 ? 634 HOH B O   1 
HETATM 5949 O  O   . HOH F 3 .   ? 2.410   16.271  35.559  1.00 26.70 ? 635 HOH B O   1 
HETATM 5950 O  O   . HOH F 3 .   ? -6.255  21.969  38.433  1.00 36.18 ? 636 HOH B O   1 
HETATM 5951 O  O   . HOH F 3 .   ? 7.346   11.807  52.877  1.00 30.51 ? 637 HOH B O   1 
HETATM 5952 O  O   . HOH F 3 .   ? -6.854  17.700  44.762  1.00 35.44 ? 638 HOH B O   1 
HETATM 5953 O  O   . HOH F 3 .   ? 17.354  9.915   55.399  1.00 31.49 ? 639 HOH B O   1 
HETATM 5954 O  O   . HOH F 3 .   ? -7.577  18.879  24.301  1.00 32.89 ? 640 HOH B O   1 
HETATM 5955 O  O   . HOH F 3 .   ? -4.763  -9.443  41.836  1.00 34.09 ? 641 HOH B O   1 
HETATM 5956 O  O   . HOH F 3 .   ? 22.812  9.441   28.586  1.00 18.57 ? 642 HOH B O   1 
HETATM 5957 O  O   . HOH F 3 .   ? -18.111 25.866  20.894  1.00 23.19 ? 643 HOH B O   1 
HETATM 5958 O  O   . HOH F 3 .   ? 2.954   -14.276 25.735  1.00 28.31 ? 644 HOH B O   1 
HETATM 5959 O  O   . HOH F 3 .   ? 29.487  7.443   48.069  1.00 39.73 ? 645 HOH B O   1 
HETATM 5960 O  O   . HOH F 3 .   ? 28.833  4.827   29.200  1.00 21.03 ? 646 HOH B O   1 
HETATM 5961 O  O   . HOH F 3 .   ? -8.682  -6.392  51.584  1.00 37.78 ? 647 HOH B O   1 
HETATM 5962 O  O   . HOH F 3 .   ? 21.154  16.228  52.021  1.00 21.97 ? 648 HOH B O   1 
HETATM 5963 O  O   . HOH F 3 .   ? 13.632  14.115  53.542  1.00 24.69 ? 649 HOH B O   1 
HETATM 5964 O  O   . HOH F 3 .   ? -5.277  -4.758  6.929   1.00 16.33 ? 650 HOH B O   1 
HETATM 5965 O  O   . HOH F 3 .   ? -15.026 -2.170  40.441  1.00 32.25 ? 651 HOH B O   1 
HETATM 5966 O  O   . HOH F 3 .   ? -12.694 23.393  20.835  1.00 42.64 ? 652 HOH B O   1 
HETATM 5967 O  O   . HOH F 3 .   ? 7.687   -9.585  32.028  1.00 24.79 ? 653 HOH B O   1 
HETATM 5968 O  O   . HOH F 3 .   ? -9.260  -1.987  30.408  1.00 12.12 ? 654 HOH B O   1 
HETATM 5969 O  O   . HOH F 3 .   ? 14.999  14.492  51.051  1.00 19.16 ? 655 HOH B O   1 
HETATM 5970 O  O   . HOH F 3 .   ? -2.970  -5.648  19.012  1.00 13.63 ? 656 HOH B O   1 
HETATM 5971 O  O   . HOH F 3 .   ? -2.355  -2.340  30.123  1.00 10.13 ? 657 HOH B O   1 
HETATM 5972 O  O   . HOH F 3 .   ? -5.235  -5.117  37.060  1.00 14.70 ? 658 HOH B O   1 
HETATM 5973 O  O   . HOH F 3 .   ? -10.974 8.419   44.685  1.00 17.35 ? 659 HOH B O   1 
HETATM 5974 O  O   . HOH F 3 .   ? -19.430 -0.607  35.166  1.00 36.05 ? 660 HOH B O   1 
HETATM 5975 O  O   . HOH F 3 .   ? -7.821  13.210  14.918  1.00 37.16 ? 661 HOH B O   1 
HETATM 5976 O  O   . HOH F 3 .   ? 17.788  13.293  53.938  1.00 32.59 ? 662 HOH B O   1 
HETATM 5977 O  O   . HOH F 3 .   ? -22.855 -4.002  31.899  1.00 37.82 ? 663 HOH B O   1 
HETATM 5978 O  O   . HOH F 3 .   ? 20.510  15.479  36.952  1.00 39.69 ? 664 HOH B O   1 
HETATM 5979 O  O   . HOH F 3 .   ? -4.186  18.101  26.918  1.00 28.91 ? 665 HOH B O   1 
HETATM 5980 O  O   . HOH F 3 .   ? 34.663  5.303   45.329  1.00 35.75 ? 666 HOH B O   1 
HETATM 5981 O  O   . HOH F 3 .   ? 9.750   8.279   22.555  1.00 36.28 ? 667 HOH B O   1 
HETATM 5982 O  O   . HOH F 3 .   ? 14.283  -1.547  48.045  1.00 16.09 ? 668 HOH B O   1 
HETATM 5983 O  O   . HOH F 3 .   ? 25.533  11.219  30.398  1.00 29.15 ? 669 HOH B O   1 
HETATM 5984 O  O   . HOH F 3 .   ? -14.354 1.716   32.774  1.00 24.48 ? 670 HOH B O   1 
HETATM 5985 O  O   . HOH F 3 .   ? 17.324  -5.361  44.871  1.00 19.76 ? 671 HOH B O   1 
HETATM 5986 O  O   . HOH F 3 .   ? -25.121 5.669   26.406  1.00 46.12 ? 672 HOH B O   1 
HETATM 5987 O  O   . HOH F 3 .   ? 27.780  -1.522  49.030  1.00 42.01 ? 673 HOH B O   1 
HETATM 5988 O  O   . HOH F 3 .   ? -0.939  -10.885 39.327  1.00 31.12 ? 674 HOH B O   1 
HETATM 5989 O  O   . HOH F 3 .   ? 25.185  11.377  44.015  1.00 24.35 ? 675 HOH B O   1 
HETATM 5990 O  O   . HOH F 3 .   ? 0.538   15.428  49.545  1.00 42.10 ? 676 HOH B O   1 
HETATM 5991 O  O   . HOH F 3 .   ? 15.422  10.678  42.713  1.00 16.93 ? 677 HOH B O   1 
HETATM 5992 O  O   . HOH F 3 .   ? 6.351   17.939  38.599  1.00 17.58 ? 678 HOH B O   1 
HETATM 5993 O  O   . HOH F 3 .   ? 7.120   3.934   49.264  1.00 16.12 ? 679 HOH B O   1 
HETATM 5994 O  O   . HOH F 3 .   ? 14.544  -6.348  50.364  1.00 21.92 ? 680 HOH B O   1 
HETATM 5995 O  O   . HOH F 3 .   ? -11.802 -4.037  2.993   1.00 22.33 ? 681 HOH B O   1 
HETATM 5996 O  O   . HOH F 3 .   ? -4.612  7.250   50.716  1.00 38.37 ? 682 HOH B O   1 
HETATM 5997 O  O   . HOH F 3 .   ? 7.986   -0.594  48.690  1.00 18.59 ? 683 HOH B O   1 
HETATM 5998 O  O   . HOH F 3 .   ? 4.235   -5.844  41.101  1.00 33.46 ? 684 HOH B O   1 
HETATM 5999 O  O   . HOH F 3 .   ? 12.967  10.881  41.423  1.00 20.32 ? 685 HOH B O   1 
HETATM 6000 O  O   . HOH F 3 .   ? -10.265 15.138  48.892  1.00 42.94 ? 686 HOH B O   1 
HETATM 6001 O  O   . HOH F 3 .   ? -0.393  -15.394 23.776  1.00 28.84 ? 687 HOH B O   1 
HETATM 6002 O  O   . HOH F 3 .   ? -4.548  -10.800 26.489  1.00 12.39 ? 688 HOH B O   1 
HETATM 6003 O  O   . HOH F 3 .   ? -15.913 4.053   34.148  1.00 22.67 ? 689 HOH B O   1 
HETATM 6004 O  O   . HOH F 3 .   ? -8.326  -11.397 26.708  1.00 23.40 ? 690 HOH B O   1 
HETATM 6005 O  O   . HOH F 3 .   ? -22.240 19.729  33.924  1.00 37.34 ? 691 HOH B O   1 
HETATM 6006 O  O   . HOH F 3 .   ? 10.190  -1.135  39.758  1.00 28.13 ? 692 HOH B O   1 
HETATM 6007 O  O   . HOH F 3 .   ? 9.622   14.839  53.019  1.00 38.91 ? 693 HOH B O   1 
HETATM 6008 O  O   . HOH F 3 .   ? -4.153  -14.265 17.954  1.00 39.67 ? 694 HOH B O   1 
HETATM 6009 O  O   . HOH F 3 .   ? -11.780 -4.605  33.186  1.00 15.78 ? 695 HOH B O   1 
HETATM 6010 O  O   . HOH F 3 .   ? 4.243   -0.722  53.095  1.00 31.44 ? 696 HOH B O   1 
HETATM 6011 O  O   . HOH F 3 .   ? 12.934  16.203  39.757  1.00 26.74 ? 697 HOH B O   1 
HETATM 6012 O  O   . HOH F 3 .   ? -4.221  16.564  31.818  1.00 22.07 ? 698 HOH B O   1 
HETATM 6013 O  O   . HOH F 3 .   ? 13.151  18.455  28.801  1.00 30.45 ? 699 HOH B O   1 
HETATM 6014 O  O   . HOH F 3 .   ? -8.885  15.467  15.444  1.00 39.47 ? 700 HOH B O   1 
HETATM 6015 O  O   . HOH F 3 .   ? 8.095   -5.820  41.403  1.00 25.78 ? 701 HOH B O   1 
HETATM 6016 O  O   . HOH F 3 .   ? -8.989  17.438  41.756  1.00 31.34 ? 702 HOH B O   1 
HETATM 6017 O  O   A HOH F 3 .   ? 11.952  2.542   41.562  0.50 13.05 ? 703 HOH B O   1 
HETATM 6018 O  O   B HOH F 3 .   ? 11.969  1.848   40.298  0.50 14.58 ? 703 HOH B O   1 
HETATM 6019 O  O   . HOH F 3 .   ? -22.985 18.942  37.002  1.00 35.94 ? 704 HOH B O   1 
HETATM 6020 O  O   . HOH F 3 .   ? -3.960  -8.165  19.386  1.00 13.89 ? 705 HOH B O   1 
HETATM 6021 O  O   . HOH F 3 .   ? -21.398 1.652   34.690  1.00 38.64 ? 706 HOH B O   1 
HETATM 6022 O  O   . HOH F 3 .   ? 13.492  6.288   57.862  1.00 39.93 ? 707 HOH B O   1 
HETATM 6023 O  O   . HOH F 3 .   ? 18.751  -3.308  43.640  1.00 16.71 ? 708 HOH B O   1 
HETATM 6024 O  O   . HOH F 3 .   ? 7.859   8.283   58.312  1.00 31.62 ? 709 HOH B O   1 
HETATM 6025 O  O   . HOH F 3 .   ? -13.151 18.383  41.742  1.00 34.17 ? 710 HOH B O   1 
HETATM 6026 O  O   . HOH F 3 .   ? -6.002  9.638   16.603  1.00 21.46 ? 711 HOH B O   1 
HETATM 6027 O  O   . HOH F 3 .   ? 15.030  -10.019 56.288  1.00 43.90 ? 712 HOH B O   1 
HETATM 6028 O  O   . HOH F 3 .   ? -8.117  0.690   12.687  1.00 20.61 ? 713 HOH B O   1 
HETATM 6029 O  O   . HOH F 3 .   ? 20.331  -2.300  55.023  1.00 23.87 ? 714 HOH B O   1 
HETATM 6030 O  O   . HOH F 3 .   ? 9.249   -7.017  32.367  1.00 33.42 ? 715 HOH B O   1 
HETATM 6031 O  O   . HOH F 3 .   ? 26.291  2.411   53.739  1.00 36.83 ? 716 HOH B O   1 
HETATM 6032 O  O   . HOH F 3 .   ? -3.240  -11.265 16.483  1.00 21.26 ? 717 HOH B O   1 
HETATM 6033 O  O   . HOH F 3 .   ? 3.047   -12.643 19.406  1.00 27.83 ? 718 HOH B O   1 
HETATM 6034 O  O   . HOH F 3 .   ? -9.400  18.879  27.408  1.00 29.87 ? 719 HOH B O   1 
HETATM 6035 O  O   . HOH F 3 .   ? -23.315 8.691   22.366  1.00 25.06 ? 720 HOH B O   1 
HETATM 6036 O  O   . HOH F 3 .   ? -13.423 7.221   45.210  1.00 20.78 ? 721 HOH B O   1 
HETATM 6037 O  O   . HOH F 3 .   ? 7.015   0.323   45.305  1.00 17.04 ? 722 HOH B O   1 
HETATM 6038 O  O   . HOH F 3 .   ? 8.106   21.422  36.758  1.00 34.59 ? 723 HOH B O   1 
HETATM 6039 O  O   . HOH F 3 .   ? -13.353 8.828   15.362  1.00 41.74 ? 724 HOH B O   1 
HETATM 6040 O  O   . HOH F 3 .   ? 17.124  -9.931  35.593  1.00 35.67 ? 725 HOH B O   1 
HETATM 6041 O  O   . HOH F 3 .   ? 30.817  6.403   30.427  1.00 25.76 ? 726 HOH B O   1 
HETATM 6042 O  O   . HOH F 3 .   ? 2.541   -0.819  33.501  1.00 13.79 ? 727 HOH B O   1 
HETATM 6043 O  O   . HOH F 3 .   ? 15.910  1.584   33.162  1.00 16.67 ? 728 HOH B O   1 
HETATM 6044 O  O   . HOH F 3 .   ? 1.658   14.645  18.236  1.00 18.75 ? 729 HOH B O   1 
HETATM 6045 O  O   . HOH F 3 .   ? 2.788   16.910  22.059  1.00 29.42 ? 730 HOH B O   1 
HETATM 6046 O  O   . HOH F 3 .   ? -5.338  -7.999  16.882  1.00 16.29 ? 731 HOH B O   1 
HETATM 6047 O  O   . HOH F 3 .   ? -13.516 14.029  44.919  1.00 33.79 ? 732 HOH B O   1 
HETATM 6048 O  O   . HOH F 3 .   ? -8.749  -7.179  36.024  1.00 23.11 ? 733 HOH B O   1 
HETATM 6049 O  O   . HOH F 3 .   ? 27.482  7.671   45.975  1.00 33.77 ? 734 HOH B O   1 
HETATM 6050 O  O   . HOH F 3 .   ? 1.139   22.387  40.027  1.00 43.46 ? 735 HOH B O   1 
HETATM 6051 O  O   . HOH F 3 .   ? -23.498 5.987   22.518  1.00 27.94 ? 736 HOH B O   1 
HETATM 6052 O  O   . HOH F 3 .   ? -13.905 -2.070  5.978   1.00 42.63 ? 737 HOH B O   1 
HETATM 6053 O  O   . HOH F 3 .   ? 4.911   -11.832 33.925  1.00 30.19 ? 738 HOH B O   1 
HETATM 6054 O  O   . HOH F 3 .   ? 11.598  16.216  45.157  1.00 22.33 ? 739 HOH B O   1 
HETATM 6055 O  O   . HOH F 3 .   ? 30.539  10.217  37.382  1.00 33.36 ? 740 HOH B O   1 
HETATM 6056 O  O   . HOH F 3 .   ? 14.718  15.773  37.671  1.00 20.33 ? 741 HOH B O   1 
HETATM 6057 O  O   . HOH F 3 .   ? 13.674  16.277  43.371  1.00 32.40 ? 742 HOH B O   1 
HETATM 6058 O  O   . HOH F 3 .   ? 7.777   -8.133  17.427  1.00 30.44 ? 743 HOH B O   1 
HETATM 6059 O  O   . HOH F 3 .   ? -9.506  -0.368  37.425  1.00 13.23 ? 744 HOH B O   1 
HETATM 6060 O  O   . HOH F 3 .   ? -9.695  19.756  35.681  1.00 21.64 ? 745 HOH B O   1 
HETATM 6061 O  O   . HOH F 3 .   ? -6.573  -8.036  28.621  1.00 13.53 ? 746 HOH B O   1 
HETATM 6062 O  O   . HOH F 3 .   ? 4.663   -4.379  39.056  1.00 31.43 ? 747 HOH B O   1 
HETATM 6063 O  O   . HOH F 3 .   ? 17.087  -7.909  33.868  1.00 23.28 ? 748 HOH B O   1 
HETATM 6064 O  O   . HOH F 3 .   ? 9.555   5.436   22.557  1.00 25.46 ? 749 HOH B O   1 
HETATM 6065 O  O   . HOH F 3 .   ? -3.001  -14.152 46.078  1.00 22.15 ? 750 HOH B O   1 
HETATM 6066 O  O   . HOH F 3 .   ? -14.466 -1.232  17.396  1.00 25.63 ? 751 HOH B O   1 
HETATM 6067 O  O   . HOH F 3 .   ? 20.952  -4.846  42.229  1.00 19.31 ? 752 HOH B O   1 
HETATM 6068 O  O   . HOH F 3 .   ? 6.412   11.199  28.520  1.00 26.84 ? 753 HOH B O   1 
HETATM 6069 O  O   . HOH F 3 .   ? -7.694  -6.234  45.851  1.00 31.81 ? 754 HOH B O   1 
HETATM 6070 O  O   . HOH F 3 .   ? -3.186  17.820  29.308  1.00 25.69 ? 755 HOH B O   1 
HETATM 6071 O  O   . HOH F 3 .   ? 25.955  2.026   51.072  1.00 28.35 ? 756 HOH B O   1 
HETATM 6072 O  O   . HOH F 3 .   ? -11.942 -5.023  6.890   1.00 27.95 ? 757 HOH B O   1 
HETATM 6073 O  O   . HOH F 3 .   ? 2.422   -10.057 12.263  1.00 27.17 ? 758 HOH B O   1 
HETATM 6074 O  O   . HOH F 3 .   ? 12.202  -7.895  50.773  1.00 33.83 ? 759 HOH B O   1 
HETATM 6075 O  O   . HOH F 3 .   ? -8.940  -4.659  31.179  1.00 11.89 ? 760 HOH B O   1 
HETATM 6076 O  O   . HOH F 3 .   ? -11.117 -10.201 25.293  1.00 27.51 ? 761 HOH B O   1 
HETATM 6077 O  O   . HOH F 3 .   ? -13.956 -4.014  16.852  1.00 23.74 ? 762 HOH B O   1 
HETATM 6078 O  O   . HOH F 3 .   ? -2.593  14.034  32.071  1.00 15.81 ? 763 HOH B O   1 
HETATM 6079 O  O   . HOH F 3 .   ? -10.734 20.157  45.566  1.00 44.17 ? 764 HOH B O   1 
HETATM 6080 O  O   . HOH F 3 .   ? 2.030   19.755  29.012  1.00 41.22 ? 765 HOH B O   1 
HETATM 6081 O  O   . HOH F 3 .   ? 15.726  4.628   17.579  1.00 26.19 ? 766 HOH B O   1 
HETATM 6082 O  O   . HOH F 3 .   ? -11.205 11.304  45.075  1.00 22.75 ? 767 HOH B O   1 
HETATM 6083 O  O   . HOH F 3 .   ? 8.574   22.391  27.254  1.00 36.53 ? 768 HOH B O   1 
HETATM 6084 O  O   . HOH F 3 .   ? 11.273  -3.198  55.071  1.00 32.52 ? 769 HOH B O   1 
HETATM 6085 O  O   . HOH F 3 .   ? 19.859  -10.306 37.079  1.00 29.12 ? 770 HOH B O   1 
HETATM 6086 O  O   . HOH F 3 .   ? -8.759  19.197  46.667  1.00 41.61 ? 771 HOH B O   1 
HETATM 6087 O  O   . HOH F 3 .   ? 0.880   -13.485 9.546   1.00 32.72 ? 772 HOH B O   1 
HETATM 6088 O  O   . HOH F 3 .   ? -3.678  -7.408  12.631  1.00 15.33 ? 773 HOH B O   1 
HETATM 6089 O  O   . HOH F 3 .   ? 7.591   -1.955  23.499  1.00 30.97 ? 774 HOH B O   1 
HETATM 6090 O  O   . HOH F 3 .   ? -2.477  -10.350 18.893  1.00 18.13 ? 775 HOH B O   1 
HETATM 6091 O  O   . HOH F 3 .   ? -16.349 0.611   32.784  1.00 36.71 ? 776 HOH B O   1 
HETATM 6092 O  O   . HOH F 3 .   ? -12.025 0.888   7.516   1.00 40.42 ? 777 HOH B O   1 
HETATM 6093 O  O   . HOH F 3 .   ? 14.515  12.823  24.744  1.00 41.04 ? 778 HOH B O   1 
HETATM 6094 O  O   . HOH F 3 .   ? 14.135  14.045  41.647  1.00 29.74 ? 779 HOH B O   1 
HETATM 6095 O  O   . HOH F 3 .   ? -15.571 0.681   47.959  1.00 31.80 ? 780 HOH B O   1 
HETATM 6096 O  O   . HOH F 3 .   ? 12.276  2.337   24.279  1.00 17.59 ? 781 HOH B O   1 
HETATM 6097 O  O   . HOH F 3 .   ? 0.416   17.475  37.206  1.00 22.85 ? 782 HOH B O   1 
HETATM 6098 O  O   . HOH F 3 .   ? 7.266   14.215  51.716  1.00 36.64 ? 783 HOH B O   1 
HETATM 6099 O  O   . HOH F 3 .   ? 24.305  8.037   48.894  1.00 28.48 ? 784 HOH B O   1 
HETATM 6100 O  O   . HOH F 3 .   ? 6.366   1.649   47.927  1.00 15.72 ? 785 HOH B O   1 
HETATM 6101 O  O   . HOH F 3 .   ? -15.972 -6.608  20.286  1.00 25.51 ? 786 HOH B O   1 
HETATM 6102 O  O   . HOH F 3 .   ? 0.259   5.310   50.423  1.00 21.76 ? 787 HOH B O   1 
HETATM 6103 O  O   . HOH F 3 .   ? 15.188  -0.187  59.003  1.00 30.12 ? 788 HOH B O   1 
HETATM 6104 O  O   . HOH F 3 .   ? -2.324  6.324   47.882  1.00 20.65 ? 789 HOH B O   1 
HETATM 6105 O  O   . HOH F 3 .   ? -8.721  -10.432 9.839   1.00 26.55 ? 790 HOH B O   1 
HETATM 6106 O  O   . HOH F 3 .   ? -19.320 -7.550  23.799  1.00 42.87 ? 791 HOH B O   1 
HETATM 6107 O  O   . HOH F 3 .   ? 7.539   10.189  26.118  1.00 44.02 ? 792 HOH B O   1 
HETATM 6108 O  O   . HOH F 3 .   ? 23.859  3.796   51.061  1.00 20.38 ? 793 HOH B O   1 
HETATM 6109 O  O   . HOH F 3 .   ? 17.503  15.284  39.158  1.00 29.13 ? 794 HOH B O   1 
HETATM 6110 O  O   . HOH F 3 .   ? -4.151  -13.630 13.508  1.00 34.43 ? 795 HOH B O   1 
HETATM 6111 O  O   . HOH F 3 .   ? -7.934  5.721   8.289   1.00 24.47 ? 796 HOH B O   1 
HETATM 6112 O  O   . HOH F 3 .   ? -2.798  5.383   13.743  1.00 16.91 ? 797 HOH B O   1 
HETATM 6113 O  O   . HOH F 3 .   ? -4.555  19.422  42.540  1.00 33.27 ? 798 HOH B O   1 
HETATM 6114 O  O   . HOH F 3 .   ? 27.928  1.152   35.332  1.00 28.67 ? 799 HOH B O   1 
HETATM 6115 O  O   . HOH F 3 .   ? -6.918  -5.310  29.172  1.00 13.24 ? 800 HOH B O   1 
HETATM 6116 O  O   . HOH F 3 .   ? -15.645 2.351   50.528  1.00 41.42 ? 801 HOH B O   1 
HETATM 6117 O  O   . HOH F 3 .   ? 7.859   2.449   37.824  1.00 16.36 ? 802 HOH B O   1 
HETATM 6118 O  O   . HOH F 3 .   ? 29.481  -4.844  47.575  1.00 42.57 ? 803 HOH B O   1 
HETATM 6119 O  O   . HOH F 3 .   ? -17.891 -5.692  22.027  1.00 23.48 ? 804 HOH B O   1 
HETATM 6120 O  O   . HOH F 3 .   ? -20.824 9.885   37.229  1.00 37.46 ? 805 HOH B O   1 
HETATM 6121 O  O   . HOH F 3 .   ? 0.919   9.134   52.624  1.00 39.53 ? 806 HOH B O   1 
HETATM 6122 O  O   . HOH F 3 .   ? 31.633  -1.881  46.689  1.00 42.38 ? 807 HOH B O   1 
HETATM 6123 O  O   . HOH F 3 .   ? 24.739  -5.574  50.446  1.00 29.89 ? 808 HOH B O   1 
HETATM 6124 O  O   . HOH F 3 .   ? 9.830   21.628  34.480  1.00 25.15 ? 809 HOH B O   1 
HETATM 6125 O  O   . HOH F 3 .   ? 10.747  14.122  27.569  1.00 32.68 ? 810 HOH B O   1 
HETATM 6126 O  O   . HOH F 3 .   ? 25.140  -0.180  49.325  1.00 27.49 ? 811 HOH B O   1 
HETATM 6127 O  O   . HOH F 3 .   ? 18.615  8.029   17.721  1.00 28.01 ? 812 HOH B O   1 
HETATM 6128 O  O   . HOH F 3 .   ? -6.715  0.389   7.063   1.00 33.95 ? 813 HOH B O   1 
HETATM 6129 O  O   . HOH F 3 .   ? 25.693  14.543  33.828  1.00 37.41 ? 814 HOH B O   1 
HETATM 6130 O  O   . HOH F 3 .   ? 13.492  10.568  55.089  1.00 36.14 ? 815 HOH B O   1 
HETATM 6131 O  O   . HOH F 3 .   ? -17.124 21.622  30.112  1.00 22.88 ? 816 HOH B O   1 
HETATM 6132 O  O   . HOH F 3 .   ? -16.357 21.109  32.686  1.00 40.00 ? 817 HOH B O   1 
HETATM 6133 O  O   . HOH F 3 .   ? -19.254 9.951   41.107  1.00 29.26 ? 818 HOH B O   1 
HETATM 6134 O  O   . HOH F 3 .   ? -18.971 3.424   40.210  1.00 36.86 ? 819 HOH B O   1 
HETATM 6135 O  O   . HOH F 3 .   ? -8.926  -12.140 13.901  1.00 37.28 ? 820 HOH B O   1 
HETATM 6136 O  O   . HOH F 3 .   ? 5.585   -8.153  47.327  1.00 40.85 ? 821 HOH B O   1 
HETATM 6137 O  O   . HOH F 3 .   ? -10.723 -6.199  4.385   1.00 23.10 ? 822 HOH B O   1 
HETATM 6138 O  O   . HOH F 3 .   ? 6.728   -1.904  53.430  1.00 34.25 ? 823 HOH B O   1 
HETATM 6139 O  O   . HOH F 3 .   ? 35.891  7.298   35.860  1.00 37.36 ? 824 HOH B O   1 
HETATM 6140 O  O   . HOH F 3 .   ? -12.784 -11.247 29.934  1.00 35.53 ? 825 HOH B O   1 
HETATM 6141 O  O   . HOH F 3 .   ? -22.841 -0.209  31.920  1.00 41.35 ? 826 HOH B O   1 
HETATM 6142 O  O   . HOH F 3 .   ? 6.237   11.111  21.792  1.00 21.09 ? 827 HOH B O   1 
HETATM 6143 O  O   . HOH F 3 .   ? -10.569 -7.370  38.231  1.00 28.73 ? 828 HOH B O   1 
HETATM 6144 O  O   . HOH F 3 .   ? -5.856  -11.771 14.312  1.00 29.18 ? 829 HOH B O   1 
HETATM 6145 O  O   . HOH F 3 .   ? -20.542 3.718   19.422  1.00 21.90 ? 830 HOH B O   1 
HETATM 6146 O  O   . HOH F 3 .   ? -16.793 19.399  18.273  1.00 30.08 ? 831 HOH B O   1 
HETATM 6147 O  O   . HOH F 3 .   ? -12.668 -9.082  38.696  1.00 44.89 ? 832 HOH B O   1 
HETATM 6148 O  O   . HOH F 3 .   ? -20.144 4.331   16.867  1.00 42.06 ? 833 HOH B O   1 
HETATM 6149 O  O   . HOH F 3 .   ? -3.550  4.771   50.282  1.00 39.91 ? 834 HOH B O   1 
HETATM 6150 O  O   . HOH F 3 .   ? 7.070   -4.586  53.785  1.00 39.66 ? 835 HOH B O   1 
HETATM 6151 O  O   . HOH F 3 .   ? 10.994  -2.759  33.923  1.00 33.44 ? 836 HOH B O   1 
HETATM 6152 O  O   . HOH F 3 .   ? 23.634  9.866   50.664  1.00 31.01 ? 837 HOH B O   1 
HETATM 6153 O  O   . HOH F 3 .   ? 19.834  15.763  45.275  1.00 24.74 ? 838 HOH B O   1 
HETATM 6154 O  O   . HOH F 3 .   ? 16.719  -13.212 47.986  1.00 30.56 ? 839 HOH B O   1 
HETATM 6155 O  O   . HOH F 3 .   ? -1.916  17.805  35.920  1.00 39.40 ? 840 HOH B O   1 
HETATM 6156 O  O   . HOH F 3 .   ? -1.086  15.629  33.730  1.00 24.47 ? 841 HOH B O   1 
HETATM 6157 O  O   . HOH F 3 .   ? 9.731   -10.179 38.027  1.00 39.18 ? 842 HOH B O   1 
HETATM 6158 O  O   . HOH F 3 .   ? 6.612   -4.218  38.259  1.00 37.31 ? 843 HOH B O   1 
HETATM 6159 O  O   . HOH F 3 .   ? -16.231 -5.389  17.501  1.00 34.46 ? 844 HOH B O   1 
HETATM 6160 O  O   . HOH F 3 .   ? 11.439  -0.550  35.202  1.00 48.24 ? 845 HOH B O   1 
HETATM 6161 O  O   . HOH F 3 .   ? 2.547   -7.415  39.992  1.00 42.06 ? 846 HOH B O   1 
HETATM 6162 O  O   . HOH F 3 .   ? 15.005  -4.473  59.465  1.00 50.35 ? 847 HOH B O   1 
HETATM 6163 O  O   . HOH F 3 .   ? 10.722  18.198  47.017  1.00 29.80 ? 848 HOH B O   1 
HETATM 6164 O  O   . HOH F 3 .   ? 13.627  -1.144  35.077  1.00 43.10 ? 849 HOH B O   1 
HETATM 6165 O  O   . HOH F 3 .   ? 2.565   -2.729  53.609  1.00 35.93 ? 850 HOH B O   1 
HETATM 6166 O  O   . HOH F 3 .   ? -23.699 15.906  23.620  1.00 42.65 ? 851 HOH B O   1 
HETATM 6167 O  O   . HOH F 3 .   ? 1.071   17.283  33.065  1.00 33.20 ? 852 HOH B O   1 
HETATM 6168 O  O   . HOH F 3 .   ? -12.288 20.432  36.339  1.00 37.84 ? 853 HOH B O   1 
HETATM 6169 O  O   . HOH F 3 .   ? -11.945 -1.319  44.710  1.00 29.80 ? 854 HOH B O   1 
HETATM 6170 O  O   . HOH F 3 .   ? 25.500  -9.515  48.970  1.00 43.68 ? 855 HOH B O   1 
HETATM 6171 O  O   . HOH F 3 .   ? -10.127 5.065   6.364   1.00 35.42 ? 856 HOH B O   1 
HETATM 6172 O  O   . HOH F 3 .   ? 1.093   -17.774 30.754  1.00 41.14 ? 857 HOH B O   1 
HETATM 6173 O  O   . HOH F 3 .   ? -17.093 24.385  17.953  1.00 40.86 ? 858 HOH B O   1 
HETATM 6174 O  O   . HOH F 3 .   ? -21.881 15.199  34.349  1.00 36.87 ? 859 HOH B O   1 
HETATM 6175 O  O   . HOH F 3 .   ? 5.761   -8.988  37.317  1.00 38.27 ? 860 HOH B O   1 
HETATM 6176 O  O   . HOH F 3 .   ? -4.669  -9.257  14.511  1.00 20.60 ? 861 HOH B O   1 
HETATM 6177 O  O   . HOH F 3 .   ? 7.616   -5.133  49.724  1.00 36.75 ? 862 HOH B O   1 
HETATM 6178 O  O   . HOH F 3 .   ? 11.077  -1.673  37.186  1.00 41.08 ? 863 HOH B O   1 
HETATM 6179 O  O   . HOH F 3 .   ? -9.093  -14.634 28.898  1.00 38.92 ? 864 HOH B O   1 
HETATM 6180 O  O   . HOH F 3 .   ? -15.391 -9.333  20.836  1.00 37.20 ? 865 HOH B O   1 
HETATM 6181 O  O   . HOH F 3 .   ? 4.293   18.871  37.121  1.00 38.29 ? 866 HOH B O   1 
HETATM 6182 O  O   . HOH F 3 .   ? 10.153  1.275   38.299  1.00 31.84 ? 867 HOH B O   1 
HETATM 6183 O  O   . HOH F 3 .   ? -20.495 1.005   19.695  1.00 43.71 ? 868 HOH B O   1 
HETATM 6184 O  O   . HOH F 3 .   ? -1.107  -7.608  53.636  1.00 38.03 ? 869 HOH B O   1 
HETATM 6185 O  O   . HOH F 3 .   ? -1.171  5.558   52.468  1.00 39.84 ? 870 HOH B O   1 
HETATM 6186 O  O   . HOH F 3 .   ? -6.806  -7.190  38.136  1.00 25.37 ? 871 HOH B O   1 
HETATM 6187 O  O   . HOH F 3 .   ? 8.382   -8.508  36.309  1.00 37.37 ? 872 HOH B O   1 
HETATM 6188 O  O   . HOH F 3 .   ? 26.291  8.763   47.886  1.00 42.78 ? 873 HOH B O   1 
HETATM 6189 O  O   . HOH F 3 .   ? -24.500 9.689   24.563  1.00 41.35 ? 874 HOH B O   1 
HETATM 6190 O  O   . HOH F 3 .   ? -6.761  -7.688  41.295  1.00 41.95 ? 875 HOH B O   1 
HETATM 6191 O  O   . HOH F 3 .   ? 5.403   21.669  36.331  1.00 42.63 ? 876 HOH B O   1 
HETATM 6192 O  O   . HOH F 3 .   ? 6.560   -10.554 14.027  1.00 36.59 ? 877 HOH B O   1 
HETATM 6193 O  O   . HOH F 3 .   ? -5.656  7.412   10.553  1.00 25.75 ? 878 HOH B O   1 
HETATM 6194 O  O   . HOH F 3 .   ? 8.722   -5.765  36.994  1.00 37.78 ? 879 HOH B O   1 
HETATM 6195 O  O   . HOH F 3 .   ? 12.479  24.459  44.257  1.00 41.26 ? 880 HOH B O   1 
# 
