data_8ZOP
# 
_entry.id   8ZOP 
# 
_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   8ZOP         pdb_00008zop 10.2210/pdb8zop/pdb 
WWPDB D_1300048251 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_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                        8ZOP 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              mma@bjmu.edu.cn 
_pdbx_contact_author.name_first         Ming 
_pdbx_contact_author.name_last          Ma 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8311-3892 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ma, X.Y.'   1 ? 
'Chen, Q.Q.' 2 ? 
# 
_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                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Angew.Chem.Int.Ed.Engl. 
_citation.journal_id_ASTM           ACIEAY 
_citation.journal_id_CSD            0179 
_citation.journal_id_ISSN           1521-3773 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            64 
_citation.language                  ? 
_citation.page_first                e202418843 
_citation.page_last                 e202418843 
_citation.title                     
'Functional Characterization and Molecular Basis of a Multi-Site Halogenase in Naphthacemycin Biosynthesis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202418843 
_citation.pdbx_database_id_PubMed   39612320 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hu, Y.'     1  ?                   
primary 'Peng, S.Y.' 2  ?                   
primary 'Ma, X.'     3  ?                   
primary 'Chen, H.'   4  ?                   
primary 'Nie, Q.Y.'  5  ?                   
primary 'He, J.B.'   6  ?                   
primary 'Chen, Q.'   7  ?                   
primary 'Zhou, Q.'   8  ?                   
primary 'Lu, X.H.'   9  ?                   
primary 'Hua, Q.'    10 ?                   
primary 'Yang, D.'   11 ?                   
primary 'Liang, Y.'  12 ?                   
primary 'Ma, M.'     13 ?                   
primary 'Tang, G.L.' 14 0000-0003-3149-4683 
# 
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 Halogenase                    45895.258 1   ? ? ? 
;Sequence reference for Streptomyces sp. (1931) is not available in UniProt at the time of biocuration. Current sequence reference is from UniProt ID G3EGL7.
;
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   1   ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                35.453    1   ? ? ? ? 
4 water       nat water                         18.015    312 ? ? ? ? 
# 
_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       
;GSHMNNGHEEYDVIVVGGGPAGSSAAGLLALNGHSVLLLERDKFPRYHIGESLITGVLPTLARLGLTERMEQLGFQRKYG
GSLLWGKGHSKPWTFKFRETGNGKYEYAYQVRRADFDALLLDRARELGVTVLEGASVKEPLFDGDRMVGVRYSVRNEAET
VDVSGKITIDATGQQRWLGRHFDMVEWHEDLRNIAAWSYYQGGLRYEGETEGNILTENRPHGWLWYIPLSKDITSIGYVT
PSSRLAESGLTPEAMLDKQIAESSEVGRLTANARRVDIYRTARDWSYVCERFSGPGYALVGDAAAFIDPLLSTGVTLAMR
GGSTVSRAVHEALVDPAKERDTLQTYEDSYRDFLNSLLEFVRFFYDRTKGQKDYHVGAQAIIDPDKHFPANVDFVTLVSG
LARGDDAVDVPS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSHMNNGHEEYDVIVVGGGPAGSSAAGLLALNGHSVLLLERDKFPRYHIGESLITGVLPTLARLGLTERMEQLGFQRKYG
GSLLWGKGHSKPWTFKFRETGNGKYEYAYQVRRADFDALLLDRARELGVTVLEGASVKEPLFDGDRMVGVRYSVRNEAET
VDVSGKITIDATGQQRWLGRHFDMVEWHEDLRNIAAWSYYQGGLRYEGETEGNILTENRPHGWLWYIPLSKDITSIGYVT
PSSRLAESGLTPEAMLDKQIAESSEVGRLTANARRVDIYRTARDWSYVCERFSGPGYALVGDAAAFIDPLLSTGVTLAMR
GGSTVSRAVHEALVDPAKERDTLQTYEDSYRDFLNSLLEFVRFFYDRTKGQKDYHVGAQAIIDPDKHFPANVDFVTLVSG
LARGDDAVDVPS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'CHLORIDE ION'                CL  
4 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   HIS n 
1 4   MET n 
1 5   ASN n 
1 6   ASN n 
1 7   GLY n 
1 8   HIS n 
1 9   GLU n 
1 10  GLU n 
1 11  TYR n 
1 12  ASP n 
1 13  VAL n 
1 14  ILE n 
1 15  VAL n 
1 16  VAL n 
1 17  GLY n 
1 18  GLY n 
1 19  GLY n 
1 20  PRO n 
1 21  ALA n 
1 22  GLY n 
1 23  SER n 
1 24  SER n 
1 25  ALA n 
1 26  ALA n 
1 27  GLY n 
1 28  LEU n 
1 29  LEU n 
1 30  ALA n 
1 31  LEU n 
1 32  ASN n 
1 33  GLY n 
1 34  HIS n 
1 35  SER n 
1 36  VAL n 
1 37  LEU n 
1 38  LEU n 
1 39  LEU n 
1 40  GLU n 
1 41  ARG n 
1 42  ASP n 
1 43  LYS n 
1 44  PHE n 
1 45  PRO n 
1 46  ARG n 
1 47  TYR n 
1 48  HIS n 
1 49  ILE n 
1 50  GLY n 
1 51  GLU n 
1 52  SER n 
1 53  LEU n 
1 54  ILE n 
1 55  THR n 
1 56  GLY n 
1 57  VAL n 
1 58  LEU n 
1 59  PRO n 
1 60  THR n 
1 61  LEU n 
1 62  ALA n 
1 63  ARG n 
1 64  LEU n 
1 65  GLY n 
1 66  LEU n 
1 67  THR n 
1 68  GLU n 
1 69  ARG n 
1 70  MET n 
1 71  GLU n 
1 72  GLN n 
1 73  LEU n 
1 74  GLY n 
1 75  PHE n 
1 76  GLN n 
1 77  ARG n 
1 78  LYS n 
1 79  TYR n 
1 80  GLY n 
1 81  GLY n 
1 82  SER n 
1 83  LEU n 
1 84  LEU n 
1 85  TRP n 
1 86  GLY n 
1 87  LYS n 
1 88  GLY n 
1 89  HIS n 
1 90  SER n 
1 91  LYS n 
1 92  PRO n 
1 93  TRP n 
1 94  THR n 
1 95  PHE n 
1 96  LYS n 
1 97  PHE n 
1 98  ARG n 
1 99  GLU n 
1 100 THR n 
1 101 GLY n 
1 102 ASN n 
1 103 GLY n 
1 104 LYS n 
1 105 TYR n 
1 106 GLU n 
1 107 TYR n 
1 108 ALA n 
1 109 TYR n 
1 110 GLN n 
1 111 VAL n 
1 112 ARG n 
1 113 ARG n 
1 114 ALA n 
1 115 ASP n 
1 116 PHE n 
1 117 ASP n 
1 118 ALA n 
1 119 LEU n 
1 120 LEU n 
1 121 LEU n 
1 122 ASP n 
1 123 ARG n 
1 124 ALA n 
1 125 ARG n 
1 126 GLU n 
1 127 LEU n 
1 128 GLY n 
1 129 VAL n 
1 130 THR n 
1 131 VAL n 
1 132 LEU n 
1 133 GLU n 
1 134 GLY n 
1 135 ALA n 
1 136 SER n 
1 137 VAL n 
1 138 LYS n 
1 139 GLU n 
1 140 PRO n 
1 141 LEU n 
1 142 PHE n 
1 143 ASP n 
1 144 GLY n 
1 145 ASP n 
1 146 ARG n 
1 147 MET n 
1 148 VAL n 
1 149 GLY n 
1 150 VAL n 
1 151 ARG n 
1 152 TYR n 
1 153 SER n 
1 154 VAL n 
1 155 ARG n 
1 156 ASN n 
1 157 GLU n 
1 158 ALA n 
1 159 GLU n 
1 160 THR n 
1 161 VAL n 
1 162 ASP n 
1 163 VAL n 
1 164 SER n 
1 165 GLY n 
1 166 LYS n 
1 167 ILE n 
1 168 THR n 
1 169 ILE n 
1 170 ASP n 
1 171 ALA n 
1 172 THR n 
1 173 GLY n 
1 174 GLN n 
1 175 GLN n 
1 176 ARG n 
1 177 TRP n 
1 178 LEU n 
1 179 GLY n 
1 180 ARG n 
1 181 HIS n 
1 182 PHE n 
1 183 ASP n 
1 184 MET n 
1 185 VAL n 
1 186 GLU n 
1 187 TRP n 
1 188 HIS n 
1 189 GLU n 
1 190 ASP n 
1 191 LEU n 
1 192 ARG n 
1 193 ASN n 
1 194 ILE n 
1 195 ALA n 
1 196 ALA n 
1 197 TRP n 
1 198 SER n 
1 199 TYR n 
1 200 TYR n 
1 201 GLN n 
1 202 GLY n 
1 203 GLY n 
1 204 LEU n 
1 205 ARG n 
1 206 TYR n 
1 207 GLU n 
1 208 GLY n 
1 209 GLU n 
1 210 THR n 
1 211 GLU n 
1 212 GLY n 
1 213 ASN n 
1 214 ILE n 
1 215 LEU n 
1 216 THR n 
1 217 GLU n 
1 218 ASN n 
1 219 ARG n 
1 220 PRO n 
1 221 HIS n 
1 222 GLY n 
1 223 TRP n 
1 224 LEU n 
1 225 TRP n 
1 226 TYR n 
1 227 ILE n 
1 228 PRO n 
1 229 LEU n 
1 230 SER n 
1 231 LYS n 
1 232 ASP n 
1 233 ILE n 
1 234 THR n 
1 235 SER n 
1 236 ILE n 
1 237 GLY n 
1 238 TYR n 
1 239 VAL n 
1 240 THR n 
1 241 PRO n 
1 242 SER n 
1 243 SER n 
1 244 ARG n 
1 245 LEU n 
1 246 ALA n 
1 247 GLU n 
1 248 SER n 
1 249 GLY n 
1 250 LEU n 
1 251 THR n 
1 252 PRO n 
1 253 GLU n 
1 254 ALA n 
1 255 MET n 
1 256 LEU n 
1 257 ASP n 
1 258 LYS n 
1 259 GLN n 
1 260 ILE n 
1 261 ALA n 
1 262 GLU n 
1 263 SER n 
1 264 SER n 
1 265 GLU n 
1 266 VAL n 
1 267 GLY n 
1 268 ARG n 
1 269 LEU n 
1 270 THR n 
1 271 ALA n 
1 272 ASN n 
1 273 ALA n 
1 274 ARG n 
1 275 ARG n 
1 276 VAL n 
1 277 ASP n 
1 278 ILE n 
1 279 TYR n 
1 280 ARG n 
1 281 THR n 
1 282 ALA n 
1 283 ARG n 
1 284 ASP n 
1 285 TRP n 
1 286 SER n 
1 287 TYR n 
1 288 VAL n 
1 289 CYS n 
1 290 GLU n 
1 291 ARG n 
1 292 PHE n 
1 293 SER n 
1 294 GLY n 
1 295 PRO n 
1 296 GLY n 
1 297 TYR n 
1 298 ALA n 
1 299 LEU n 
1 300 VAL n 
1 301 GLY n 
1 302 ASP n 
1 303 ALA n 
1 304 ALA n 
1 305 ALA n 
1 306 PHE n 
1 307 ILE n 
1 308 ASP n 
1 309 PRO n 
1 310 LEU n 
1 311 LEU n 
1 312 SER n 
1 313 THR n 
1 314 GLY n 
1 315 VAL n 
1 316 THR n 
1 317 LEU n 
1 318 ALA n 
1 319 MET n 
1 320 ARG n 
1 321 GLY n 
1 322 GLY n 
1 323 SER n 
1 324 THR n 
1 325 VAL n 
1 326 SER n 
1 327 ARG n 
1 328 ALA n 
1 329 VAL n 
1 330 HIS n 
1 331 GLU n 
1 332 ALA n 
1 333 LEU n 
1 334 VAL n 
1 335 ASP n 
1 336 PRO n 
1 337 ALA n 
1 338 LYS n 
1 339 GLU n 
1 340 ARG n 
1 341 ASP n 
1 342 THR n 
1 343 LEU n 
1 344 GLN n 
1 345 THR n 
1 346 TYR n 
1 347 GLU n 
1 348 ASP n 
1 349 SER n 
1 350 TYR n 
1 351 ARG n 
1 352 ASP n 
1 353 PHE n 
1 354 LEU n 
1 355 ASN n 
1 356 SER n 
1 357 LEU n 
1 358 LEU n 
1 359 GLU n 
1 360 PHE n 
1 361 VAL n 
1 362 ARG n 
1 363 PHE n 
1 364 PHE n 
1 365 TYR n 
1 366 ASP n 
1 367 ARG n 
1 368 THR n 
1 369 LYS n 
1 370 GLY n 
1 371 GLN n 
1 372 LYS n 
1 373 ASP n 
1 374 TYR n 
1 375 HIS n 
1 376 VAL n 
1 377 GLY n 
1 378 ALA n 
1 379 GLN n 
1 380 ALA n 
1 381 ILE n 
1 382 ILE n 
1 383 ASP n 
1 384 PRO n 
1 385 ASP n 
1 386 LYS n 
1 387 HIS n 
1 388 PHE n 
1 389 PRO n 
1 390 ALA n 
1 391 ASN n 
1 392 VAL n 
1 393 ASP n 
1 394 PHE n 
1 395 VAL n 
1 396 THR n 
1 397 LEU n 
1 398 VAL n 
1 399 SER n 
1 400 GLY n 
1 401 LEU n 
1 402 ALA n 
1 403 ARG n 
1 404 GLY n 
1 405 ASP n 
1 406 ASP n 
1 407 ALA n 
1 408 VAL n 
1 409 ASP n 
1 410 VAL n 
1 411 PRO n 
1 412 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   412 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Streptomyces sp.' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1931 
_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-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                       ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                      ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                    ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'               ? 'C4 H7 N O4'        133.103 
CL  non-polymer         . 'CHLORIDE ION'                ? 'Cl -1'             35.453  
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                     ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ? 'C5 H11 N O2 S'     149.211 
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   GLY 1   -1  -1  GLY GLY A . n 
A 1 2   SER 2   0   0   SER SER A . n 
A 1 3   HIS 3   1   1   HIS HIS A . n 
A 1 4   MET 4   2   2   MET MET A . n 
A 1 5   ASN 5   3   3   ASN ASN A . n 
A 1 6   ASN 6   4   4   ASN ASN A . n 
A 1 7   GLY 7   5   5   GLY GLY A . n 
A 1 8   HIS 8   6   6   HIS HIS A . n 
A 1 9   GLU 9   7   7   GLU GLU A . n 
A 1 10  GLU 10  8   8   GLU GLU A . n 
A 1 11  TYR 11  9   9   TYR TYR A . n 
A 1 12  ASP 12  10  10  ASP ASP A . n 
A 1 13  VAL 13  11  11  VAL VAL A . n 
A 1 14  ILE 14  12  12  ILE ILE A . n 
A 1 15  VAL 15  13  13  VAL VAL A . n 
A 1 16  VAL 16  14  14  VAL VAL A . n 
A 1 17  GLY 17  15  15  GLY GLY A . n 
A 1 18  GLY 18  16  16  GLY GLY A . n 
A 1 19  GLY 19  17  17  GLY GLY A . n 
A 1 20  PRO 20  18  18  PRO PRO A . n 
A 1 21  ALA 21  19  19  ALA ALA A . n 
A 1 22  GLY 22  20  20  GLY GLY A . n 
A 1 23  SER 23  21  21  SER SER A . n 
A 1 24  SER 24  22  22  SER SER A . n 
A 1 25  ALA 25  23  23  ALA ALA A . n 
A 1 26  ALA 26  24  24  ALA ALA A . n 
A 1 27  GLY 27  25  25  GLY GLY A . n 
A 1 28  LEU 28  26  26  LEU LEU A . n 
A 1 29  LEU 29  27  27  LEU LEU A . n 
A 1 30  ALA 30  28  28  ALA ALA A . n 
A 1 31  LEU 31  29  29  LEU LEU A . n 
A 1 32  ASN 32  30  30  ASN ASN A . n 
A 1 33  GLY 33  31  31  GLY GLY A . n 
A 1 34  HIS 34  32  32  HIS HIS A . n 
A 1 35  SER 35  33  33  SER SER A . n 
A 1 36  VAL 36  34  34  VAL VAL A . n 
A 1 37  LEU 37  35  35  LEU LEU A . n 
A 1 38  LEU 38  36  36  LEU LEU A . n 
A 1 39  LEU 39  37  37  LEU LEU A . n 
A 1 40  GLU 40  38  38  GLU GLU A . n 
A 1 41  ARG 41  39  39  ARG ARG A . n 
A 1 42  ASP 42  40  40  ASP ASP A . n 
A 1 43  LYS 43  41  41  LYS LYS A . n 
A 1 44  PHE 44  42  42  PHE PHE A . n 
A 1 45  PRO 45  43  43  PRO PRO A . n 
A 1 46  ARG 46  44  44  ARG ARG A . n 
A 1 47  TYR 47  45  45  TYR TYR A . n 
A 1 48  HIS 48  46  46  HIS HIS A . n 
A 1 49  ILE 49  47  47  ILE ILE A . n 
A 1 50  GLY 50  48  48  GLY GLY A . n 
A 1 51  GLU 51  49  49  GLU GLU A . n 
A 1 52  SER 52  50  50  SER SER A . n 
A 1 53  LEU 53  51  51  LEU LEU A . n 
A 1 54  ILE 54  52  52  ILE ILE A . n 
A 1 55  THR 55  53  53  THR THR A . n 
A 1 56  GLY 56  54  54  GLY GLY A . n 
A 1 57  VAL 57  55  55  VAL VAL A . n 
A 1 58  LEU 58  56  56  LEU LEU A . n 
A 1 59  PRO 59  57  57  PRO PRO A . n 
A 1 60  THR 60  58  58  THR THR A . n 
A 1 61  LEU 61  59  59  LEU LEU A . n 
A 1 62  ALA 62  60  60  ALA ALA A . n 
A 1 63  ARG 63  61  61  ARG ARG A . n 
A 1 64  LEU 64  62  62  LEU LEU A . n 
A 1 65  GLY 65  63  63  GLY GLY A . n 
A 1 66  LEU 66  64  64  LEU LEU A . n 
A 1 67  THR 67  65  65  THR THR A . n 
A 1 68  GLU 68  66  66  GLU GLU A . n 
A 1 69  ARG 69  67  67  ARG ARG A . n 
A 1 70  MET 70  68  68  MET MET A . n 
A 1 71  GLU 71  69  69  GLU GLU A . n 
A 1 72  GLN 72  70  70  GLN GLN A . n 
A 1 73  LEU 73  71  71  LEU LEU A . n 
A 1 74  GLY 74  72  72  GLY GLY A . n 
A 1 75  PHE 75  73  73  PHE PHE A . n 
A 1 76  GLN 76  74  74  GLN GLN A . n 
A 1 77  ARG 77  75  75  ARG ARG A . n 
A 1 78  LYS 78  76  76  LYS LYS A . n 
A 1 79  TYR 79  77  77  TYR TYR A . n 
A 1 80  GLY 80  78  78  GLY GLY A . n 
A 1 81  GLY 81  79  79  GLY GLY A . n 
A 1 82  SER 82  80  80  SER SER A . n 
A 1 83  LEU 83  81  81  LEU LEU A . n 
A 1 84  LEU 84  82  82  LEU LEU A . n 
A 1 85  TRP 85  83  83  TRP TRP A . n 
A 1 86  GLY 86  84  84  GLY GLY A . n 
A 1 87  LYS 87  85  85  LYS LYS A . n 
A 1 88  GLY 88  86  ?   ?   ?   A . n 
A 1 89  HIS 89  87  ?   ?   ?   A . n 
A 1 90  SER 90  88  ?   ?   ?   A . n 
A 1 91  LYS 91  89  89  LYS LYS A . n 
A 1 92  PRO 92  90  90  PRO PRO A . n 
A 1 93  TRP 93  91  91  TRP TRP A . n 
A 1 94  THR 94  92  92  THR THR A . n 
A 1 95  PHE 95  93  93  PHE PHE A . n 
A 1 96  LYS 96  94  94  LYS LYS A . n 
A 1 97  PHE 97  95  95  PHE PHE A . n 
A 1 98  ARG 98  96  96  ARG ARG A . n 
A 1 99  GLU 99  97  97  GLU GLU A . n 
A 1 100 THR 100 98  98  THR THR A . n 
A 1 101 GLY 101 99  99  GLY GLY A . n 
A 1 102 ASN 102 100 100 ASN ASN A . n 
A 1 103 GLY 103 101 101 GLY GLY A . n 
A 1 104 LYS 104 102 102 LYS LYS A . n 
A 1 105 TYR 105 103 103 TYR TYR A . n 
A 1 106 GLU 106 104 104 GLU GLU A . n 
A 1 107 TYR 107 105 105 TYR TYR A . n 
A 1 108 ALA 108 106 106 ALA ALA A . n 
A 1 109 TYR 109 107 107 TYR TYR A . n 
A 1 110 GLN 110 108 108 GLN GLN A . n 
A 1 111 VAL 111 109 109 VAL VAL A . n 
A 1 112 ARG 112 110 110 ARG ARG A . n 
A 1 113 ARG 113 111 111 ARG ARG A . n 
A 1 114 ALA 114 112 112 ALA ALA A . n 
A 1 115 ASP 115 113 113 ASP ASP A . n 
A 1 116 PHE 116 114 114 PHE PHE A . n 
A 1 117 ASP 117 115 115 ASP ASP A . n 
A 1 118 ALA 118 116 116 ALA ALA A . n 
A 1 119 LEU 119 117 117 LEU LEU A . n 
A 1 120 LEU 120 118 118 LEU LEU A . n 
A 1 121 LEU 121 119 119 LEU LEU A . n 
A 1 122 ASP 122 120 120 ASP ASP A . n 
A 1 123 ARG 123 121 121 ARG ARG A . n 
A 1 124 ALA 124 122 122 ALA ALA A . n 
A 1 125 ARG 125 123 123 ARG ARG A . n 
A 1 126 GLU 126 124 124 GLU GLU A . n 
A 1 127 LEU 127 125 125 LEU LEU A . n 
A 1 128 GLY 128 126 126 GLY GLY A . n 
A 1 129 VAL 129 127 127 VAL VAL A . n 
A 1 130 THR 130 128 128 THR THR A . n 
A 1 131 VAL 131 129 129 VAL VAL A . n 
A 1 132 LEU 132 130 130 LEU LEU A . n 
A 1 133 GLU 133 131 131 GLU GLU A . n 
A 1 134 GLY 134 132 132 GLY GLY A . n 
A 1 135 ALA 135 133 133 ALA ALA A . n 
A 1 136 SER 136 134 134 SER SER A . n 
A 1 137 VAL 137 135 135 VAL VAL A . n 
A 1 138 LYS 138 136 136 LYS LYS A . n 
A 1 139 GLU 139 137 137 GLU GLU A . n 
A 1 140 PRO 140 138 138 PRO PRO A . n 
A 1 141 LEU 141 139 139 LEU LEU A . n 
A 1 142 PHE 142 140 140 PHE PHE A . n 
A 1 143 ASP 143 141 141 ASP ASP A . n 
A 1 144 GLY 144 142 142 GLY GLY A . n 
A 1 145 ASP 145 143 143 ASP ASP A . n 
A 1 146 ARG 146 144 144 ARG ARG A . n 
A 1 147 MET 147 145 145 MET MET A . n 
A 1 148 VAL 148 146 146 VAL VAL A . n 
A 1 149 GLY 149 147 147 GLY GLY A . n 
A 1 150 VAL 150 148 148 VAL VAL A . n 
A 1 151 ARG 151 149 149 ARG ARG A . n 
A 1 152 TYR 152 150 150 TYR TYR A . n 
A 1 153 SER 153 151 151 SER SER A . n 
A 1 154 VAL 154 152 152 VAL VAL A . n 
A 1 155 ARG 155 153 153 ARG ARG A . n 
A 1 156 ASN 156 154 154 ASN ASN A . n 
A 1 157 GLU 157 155 155 GLU GLU A . n 
A 1 158 ALA 158 156 156 ALA ALA A . n 
A 1 159 GLU 159 157 157 GLU GLU A . n 
A 1 160 THR 160 158 158 THR THR A . n 
A 1 161 VAL 161 159 159 VAL VAL A . n 
A 1 162 ASP 162 160 160 ASP ASP A . n 
A 1 163 VAL 163 161 161 VAL VAL A . n 
A 1 164 SER 164 162 162 SER SER A . n 
A 1 165 GLY 165 163 163 GLY GLY A . n 
A 1 166 LYS 166 164 164 LYS LYS A . n 
A 1 167 ILE 167 165 165 ILE ILE A . n 
A 1 168 THR 168 166 166 THR THR A . n 
A 1 169 ILE 169 167 167 ILE ILE A . n 
A 1 170 ASP 170 168 168 ASP ASP A . n 
A 1 171 ALA 171 169 169 ALA ALA A . n 
A 1 172 THR 172 170 170 THR THR A . n 
A 1 173 GLY 173 171 171 GLY GLY A . n 
A 1 174 GLN 174 172 172 GLN GLN A . n 
A 1 175 GLN 175 173 173 GLN GLN A . n 
A 1 176 ARG 176 174 174 ARG ARG A . n 
A 1 177 TRP 177 175 175 TRP TRP A . n 
A 1 178 LEU 178 176 176 LEU LEU A . n 
A 1 179 GLY 179 177 177 GLY GLY A . n 
A 1 180 ARG 180 178 178 ARG ARG A . n 
A 1 181 HIS 181 179 179 HIS HIS A . n 
A 1 182 PHE 182 180 180 PHE PHE A . n 
A 1 183 ASP 183 181 181 ASP ASP A . n 
A 1 184 MET 184 182 182 MET MET A . n 
A 1 185 VAL 185 183 183 VAL VAL A . n 
A 1 186 GLU 186 184 184 GLU GLU A . n 
A 1 187 TRP 187 185 185 TRP TRP A . n 
A 1 188 HIS 188 186 186 HIS HIS A . n 
A 1 189 GLU 189 187 187 GLU GLU A . n 
A 1 190 ASP 190 188 188 ASP ASP A . n 
A 1 191 LEU 191 189 189 LEU LEU A . n 
A 1 192 ARG 192 190 190 ARG ARG A . n 
A 1 193 ASN 193 191 191 ASN ASN A . n 
A 1 194 ILE 194 192 192 ILE ILE A . n 
A 1 195 ALA 195 193 193 ALA ALA A . n 
A 1 196 ALA 196 194 194 ALA ALA A . n 
A 1 197 TRP 197 195 195 TRP TRP A . n 
A 1 198 SER 198 196 196 SER SER A . n 
A 1 199 TYR 199 197 197 TYR TYR A . n 
A 1 200 TYR 200 198 198 TYR TYR A . n 
A 1 201 GLN 201 199 199 GLN GLN A . n 
A 1 202 GLY 202 200 200 GLY GLY A . n 
A 1 203 GLY 203 201 201 GLY GLY A . n 
A 1 204 LEU 204 202 202 LEU LEU A . n 
A 1 205 ARG 205 203 203 ARG ARG A . n 
A 1 206 TYR 206 204 204 TYR TYR A . n 
A 1 207 GLU 207 205 205 GLU GLU A . n 
A 1 208 GLY 208 206 206 GLY GLY A . n 
A 1 209 GLU 209 207 207 GLU GLU A . n 
A 1 210 THR 210 208 208 THR THR A . n 
A 1 211 GLU 211 209 209 GLU GLU A . n 
A 1 212 GLY 212 210 210 GLY GLY A . n 
A 1 213 ASN 213 211 211 ASN ASN A . n 
A 1 214 ILE 214 212 212 ILE ILE A . n 
A 1 215 LEU 215 213 213 LEU LEU A . n 
A 1 216 THR 216 214 214 THR THR A . n 
A 1 217 GLU 217 215 215 GLU GLU A . n 
A 1 218 ASN 218 216 216 ASN ASN A . n 
A 1 219 ARG 219 217 217 ARG ARG A . n 
A 1 220 PRO 220 218 218 PRO PRO A . n 
A 1 221 HIS 221 219 219 HIS HIS A . n 
A 1 222 GLY 222 220 220 GLY GLY A . n 
A 1 223 TRP 223 221 221 TRP TRP A . n 
A 1 224 LEU 224 222 222 LEU LEU A . n 
A 1 225 TRP 225 223 223 TRP TRP A . n 
A 1 226 TYR 226 224 224 TYR TYR A . n 
A 1 227 ILE 227 225 225 ILE ILE A . n 
A 1 228 PRO 228 226 226 PRO PRO A . n 
A 1 229 LEU 229 227 227 LEU LEU A . n 
A 1 230 SER 230 228 228 SER SER A . n 
A 1 231 LYS 231 229 229 LYS LYS A . n 
A 1 232 ASP 232 230 230 ASP ASP A . n 
A 1 233 ILE 233 231 231 ILE ILE A . n 
A 1 234 THR 234 232 232 THR THR A . n 
A 1 235 SER 235 233 233 SER SER A . n 
A 1 236 ILE 236 234 234 ILE ILE A . n 
A 1 237 GLY 237 235 235 GLY GLY A . n 
A 1 238 TYR 238 236 236 TYR TYR A . n 
A 1 239 VAL 239 237 237 VAL VAL A . n 
A 1 240 THR 240 238 238 THR THR A . n 
A 1 241 PRO 241 239 239 PRO PRO A . n 
A 1 242 SER 242 240 240 SER SER A . n 
A 1 243 SER 243 241 241 SER SER A . n 
A 1 244 ARG 244 242 242 ARG ARG A . n 
A 1 245 LEU 245 243 243 LEU LEU A . n 
A 1 246 ALA 246 244 244 ALA ALA A . n 
A 1 247 GLU 247 245 245 GLU GLU A . n 
A 1 248 SER 248 246 246 SER SER A . n 
A 1 249 GLY 249 247 247 GLY GLY A . n 
A 1 250 LEU 250 248 248 LEU LEU A . n 
A 1 251 THR 251 249 249 THR THR A . n 
A 1 252 PRO 252 250 250 PRO PRO A . n 
A 1 253 GLU 253 251 251 GLU GLU A . n 
A 1 254 ALA 254 252 252 ALA ALA A . n 
A 1 255 MET 255 253 253 MET MET A . n 
A 1 256 LEU 256 254 254 LEU LEU A . n 
A 1 257 ASP 257 255 255 ASP ASP A . n 
A 1 258 LYS 258 256 256 LYS LYS A . n 
A 1 259 GLN 259 257 257 GLN GLN A . n 
A 1 260 ILE 260 258 258 ILE ILE A . n 
A 1 261 ALA 261 259 259 ALA ALA A . n 
A 1 262 GLU 262 260 260 GLU GLU A . n 
A 1 263 SER 263 261 261 SER SER A . n 
A 1 264 SER 264 262 262 SER SER A . n 
A 1 265 GLU 265 263 263 GLU GLU A . n 
A 1 266 VAL 266 264 264 VAL VAL A . n 
A 1 267 GLY 267 265 265 GLY GLY A . n 
A 1 268 ARG 268 266 266 ARG ARG A . n 
A 1 269 LEU 269 267 267 LEU LEU A . n 
A 1 270 THR 270 268 268 THR THR A . n 
A 1 271 ALA 271 269 269 ALA ALA A . n 
A 1 272 ASN 272 270 270 ASN ASN A . n 
A 1 273 ALA 273 271 271 ALA ALA A . n 
A 1 274 ARG 274 272 272 ARG ARG A . n 
A 1 275 ARG 275 273 273 ARG ARG A . n 
A 1 276 VAL 276 274 274 VAL VAL A . n 
A 1 277 ASP 277 275 275 ASP ASP A . n 
A 1 278 ILE 278 276 276 ILE ILE A . n 
A 1 279 TYR 279 277 277 TYR TYR A . n 
A 1 280 ARG 280 278 278 ARG ARG A . n 
A 1 281 THR 281 279 279 THR THR A . n 
A 1 282 ALA 282 280 280 ALA ALA A . n 
A 1 283 ARG 283 281 281 ARG ARG A . n 
A 1 284 ASP 284 282 282 ASP ASP A . n 
A 1 285 TRP 285 283 283 TRP TRP A . n 
A 1 286 SER 286 284 284 SER SER A . n 
A 1 287 TYR 287 285 285 TYR TYR A . n 
A 1 288 VAL 288 286 286 VAL VAL A . n 
A 1 289 CYS 289 287 287 CYS CYS A . n 
A 1 290 GLU 290 288 288 GLU GLU A . n 
A 1 291 ARG 291 289 289 ARG ARG A . n 
A 1 292 PHE 292 290 290 PHE PHE A . n 
A 1 293 SER 293 291 291 SER SER A . n 
A 1 294 GLY 294 292 292 GLY GLY A . n 
A 1 295 PRO 295 293 293 PRO PRO A . n 
A 1 296 GLY 296 294 294 GLY GLY A . n 
A 1 297 TYR 297 295 295 TYR TYR A . n 
A 1 298 ALA 298 296 296 ALA ALA A . n 
A 1 299 LEU 299 297 297 LEU LEU A . n 
A 1 300 VAL 300 298 298 VAL VAL A . n 
A 1 301 GLY 301 299 299 GLY GLY A . n 
A 1 302 ASP 302 300 300 ASP ASP A . n 
A 1 303 ALA 303 301 301 ALA ALA A . n 
A 1 304 ALA 304 302 302 ALA ALA A . n 
A 1 305 ALA 305 303 303 ALA ALA A . n 
A 1 306 PHE 306 304 304 PHE PHE A . n 
A 1 307 ILE 307 305 305 ILE ILE A . n 
A 1 308 ASP 308 306 306 ASP ASP A . n 
A 1 309 PRO 309 307 307 PRO PRO A . n 
A 1 310 LEU 310 308 308 LEU LEU A . n 
A 1 311 LEU 311 309 309 LEU LEU A . n 
A 1 312 SER 312 310 310 SER SER A . n 
A 1 313 THR 313 311 311 THR THR A . n 
A 1 314 GLY 314 312 312 GLY GLY A . n 
A 1 315 VAL 315 313 313 VAL VAL A . n 
A 1 316 THR 316 314 314 THR THR A . n 
A 1 317 LEU 317 315 315 LEU LEU A . n 
A 1 318 ALA 318 316 316 ALA ALA A . n 
A 1 319 MET 319 317 317 MET MET A . n 
A 1 320 ARG 320 318 318 ARG ARG A . n 
A 1 321 GLY 321 319 319 GLY GLY A . n 
A 1 322 GLY 322 320 320 GLY GLY A . n 
A 1 323 SER 323 321 321 SER SER A . n 
A 1 324 THR 324 322 322 THR THR A . n 
A 1 325 VAL 325 323 323 VAL VAL A . n 
A 1 326 SER 326 324 324 SER SER A . n 
A 1 327 ARG 327 325 325 ARG ARG A . n 
A 1 328 ALA 328 326 326 ALA ALA A . n 
A 1 329 VAL 329 327 327 VAL VAL A . n 
A 1 330 HIS 330 328 328 HIS HIS A . n 
A 1 331 GLU 331 329 329 GLU GLU A . n 
A 1 332 ALA 332 330 330 ALA ALA A . n 
A 1 333 LEU 333 331 331 LEU LEU A . n 
A 1 334 VAL 334 332 332 VAL VAL A . n 
A 1 335 ASP 335 333 333 ASP ASP A . n 
A 1 336 PRO 336 334 334 PRO PRO A . n 
A 1 337 ALA 337 335 335 ALA ALA A . n 
A 1 338 LYS 338 336 336 LYS LYS A . n 
A 1 339 GLU 339 337 337 GLU GLU A . n 
A 1 340 ARG 340 338 338 ARG ARG A . n 
A 1 341 ASP 341 339 339 ASP ASP A . n 
A 1 342 THR 342 340 340 THR THR A . n 
A 1 343 LEU 343 341 341 LEU LEU A . n 
A 1 344 GLN 344 342 342 GLN GLN A . n 
A 1 345 THR 345 343 343 THR THR A . n 
A 1 346 TYR 346 344 344 TYR TYR A . n 
A 1 347 GLU 347 345 345 GLU GLU A . n 
A 1 348 ASP 348 346 346 ASP ASP A . n 
A 1 349 SER 349 347 347 SER SER A . n 
A 1 350 TYR 350 348 348 TYR TYR A . n 
A 1 351 ARG 351 349 349 ARG ARG A . n 
A 1 352 ASP 352 350 350 ASP ASP A . n 
A 1 353 PHE 353 351 351 PHE PHE A . n 
A 1 354 LEU 354 352 352 LEU LEU A . n 
A 1 355 ASN 355 353 353 ASN ASN A . n 
A 1 356 SER 356 354 354 SER SER A . n 
A 1 357 LEU 357 355 355 LEU LEU A . n 
A 1 358 LEU 358 356 356 LEU LEU A . n 
A 1 359 GLU 359 357 357 GLU GLU A . n 
A 1 360 PHE 360 358 358 PHE PHE A . n 
A 1 361 VAL 361 359 359 VAL VAL A . n 
A 1 362 ARG 362 360 360 ARG ARG A . n 
A 1 363 PHE 363 361 361 PHE PHE A . n 
A 1 364 PHE 364 362 362 PHE PHE A . n 
A 1 365 TYR 365 363 363 TYR TYR A . n 
A 1 366 ASP 366 364 364 ASP ASP A . n 
A 1 367 ARG 367 365 365 ARG ARG A . n 
A 1 368 THR 368 366 366 THR THR A . n 
A 1 369 LYS 369 367 367 LYS LYS A . n 
A 1 370 GLY 370 368 368 GLY GLY A . n 
A 1 371 GLN 371 369 369 GLN GLN A . n 
A 1 372 LYS 372 370 370 LYS LYS A . n 
A 1 373 ASP 373 371 371 ASP ASP A . n 
A 1 374 TYR 374 372 372 TYR TYR A . n 
A 1 375 HIS 375 373 373 HIS HIS A . n 
A 1 376 VAL 376 374 374 VAL VAL A . n 
A 1 377 GLY 377 375 375 GLY GLY A . n 
A 1 378 ALA 378 376 376 ALA ALA A . n 
A 1 379 GLN 379 377 377 GLN GLN A . n 
A 1 380 ALA 380 378 378 ALA ALA A . n 
A 1 381 ILE 381 379 379 ILE ILE A . n 
A 1 382 ILE 382 380 380 ILE ILE A . n 
A 1 383 ASP 383 381 381 ASP ASP A . n 
A 1 384 PRO 384 382 382 PRO PRO A . n 
A 1 385 ASP 385 383 383 ASP ASP A . n 
A 1 386 LYS 386 384 384 LYS LYS A . n 
A 1 387 HIS 387 385 385 HIS HIS A . n 
A 1 388 PHE 388 386 386 PHE PHE A . n 
A 1 389 PRO 389 387 387 PRO PRO A . n 
A 1 390 ALA 390 388 388 ALA ALA A . n 
A 1 391 ASN 391 389 389 ASN ASN A . n 
A 1 392 VAL 392 390 390 VAL VAL A . n 
A 1 393 ASP 393 391 391 ASP ASP A . n 
A 1 394 PHE 394 392 392 PHE PHE A . n 
A 1 395 VAL 395 393 393 VAL VAL A . n 
A 1 396 THR 396 394 394 THR THR A . n 
A 1 397 LEU 397 395 395 LEU LEU A . n 
A 1 398 VAL 398 396 396 VAL VAL A . n 
A 1 399 SER 399 397 397 SER SER A . n 
A 1 400 GLY 400 398 398 GLY GLY A . n 
A 1 401 LEU 401 399 399 LEU LEU A . n 
A 1 402 ALA 402 400 400 ALA ALA A . n 
A 1 403 ARG 403 401 401 ARG ARG A . n 
A 1 404 GLY 404 402 402 GLY GLY A . n 
A 1 405 ASP 405 403 403 ASP ASP A . n 
A 1 406 ASP 406 404 404 ASP ASP A . n 
A 1 407 ALA 407 405 405 ALA ALA A . n 
A 1 408 VAL 408 406 406 VAL VAL A . n 
A 1 409 ASP 409 407 407 ASP ASP A . n 
A 1 410 VAL 410 408 408 VAL VAL A . n 
A 1 411 PRO 411 409 409 PRO PRO A . n 
A 1 412 SER 412 410 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 FAD ? ? FAD ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CL  ? ? CL  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FAD 1   501 421 FAD FAD A . 
C 3 CL  1   502 422 CL  CL  A . 
D 4 HOH 1   601 133 HOH HOH A . 
D 4 HOH 2   602 347 HOH HOH A . 
D 4 HOH 3   603 188 HOH HOH A . 
D 4 HOH 4   604 308 HOH HOH A . 
D 4 HOH 5   605 144 HOH HOH A . 
D 4 HOH 6   606 134 HOH HOH A . 
D 4 HOH 7   607 105 HOH HOH A . 
D 4 HOH 8   608 320 HOH HOH A . 
D 4 HOH 9   609 137 HOH HOH A . 
D 4 HOH 10  610 87  HOH HOH A . 
D 4 HOH 11  611 22  HOH HOH A . 
D 4 HOH 12  612 220 HOH HOH A . 
D 4 HOH 13  613 409 HOH HOH A . 
D 4 HOH 14  614 145 HOH HOH A . 
D 4 HOH 15  615 228 HOH HOH A . 
D 4 HOH 16  616 167 HOH HOH A . 
D 4 HOH 17  617 416 HOH HOH A . 
D 4 HOH 18  618 46  HOH HOH A . 
D 4 HOH 19  619 57  HOH HOH A . 
D 4 HOH 20  620 66  HOH HOH A . 
D 4 HOH 21  621 31  HOH HOH A . 
D 4 HOH 22  622 117 HOH HOH A . 
D 4 HOH 23  623 160 HOH HOH A . 
D 4 HOH 24  624 269 HOH HOH A . 
D 4 HOH 25  625 186 HOH HOH A . 
D 4 HOH 26  626 214 HOH HOH A . 
D 4 HOH 27  627 219 HOH HOH A . 
D 4 HOH 28  628 24  HOH HOH A . 
D 4 HOH 29  629 32  HOH HOH A . 
D 4 HOH 30  630 284 HOH HOH A . 
D 4 HOH 31  631 264 HOH HOH A . 
D 4 HOH 32  632 231 HOH HOH A . 
D 4 HOH 33  633 28  HOH HOH A . 
D 4 HOH 34  634 341 HOH HOH A . 
D 4 HOH 35  635 244 HOH HOH A . 
D 4 HOH 36  636 8   HOH HOH A . 
D 4 HOH 37  637 51  HOH HOH A . 
D 4 HOH 38  638 143 HOH HOH A . 
D 4 HOH 39  639 360 HOH HOH A . 
D 4 HOH 40  640 97  HOH HOH A . 
D 4 HOH 41  641 131 HOH HOH A . 
D 4 HOH 42  642 37  HOH HOH A . 
D 4 HOH 43  643 115 HOH HOH A . 
D 4 HOH 44  644 441 HOH HOH A . 
D 4 HOH 45  645 41  HOH HOH A . 
D 4 HOH 46  646 39  HOH HOH A . 
D 4 HOH 47  647 260 HOH HOH A . 
D 4 HOH 48  648 303 HOH HOH A . 
D 4 HOH 49  649 141 HOH HOH A . 
D 4 HOH 50  650 3   HOH HOH A . 
D 4 HOH 51  651 292 HOH HOH A . 
D 4 HOH 52  652 77  HOH HOH A . 
D 4 HOH 53  653 110 HOH HOH A . 
D 4 HOH 54  654 1   HOH HOH A . 
D 4 HOH 55  655 73  HOH HOH A . 
D 4 HOH 56  656 88  HOH HOH A . 
D 4 HOH 57  657 80  HOH HOH A . 
D 4 HOH 58  658 104 HOH HOH A . 
D 4 HOH 59  659 265 HOH HOH A . 
D 4 HOH 60  660 10  HOH HOH A . 
D 4 HOH 61  661 121 HOH HOH A . 
D 4 HOH 62  662 290 HOH HOH A . 
D 4 HOH 63  663 40  HOH HOH A . 
D 4 HOH 64  664 262 HOH HOH A . 
D 4 HOH 65  665 47  HOH HOH A . 
D 4 HOH 66  666 29  HOH HOH A . 
D 4 HOH 67  667 9   HOH HOH A . 
D 4 HOH 68  668 13  HOH HOH A . 
D 4 HOH 69  669 204 HOH HOH A . 
D 4 HOH 70  670 16  HOH HOH A . 
D 4 HOH 71  671 299 HOH HOH A . 
D 4 HOH 72  672 18  HOH HOH A . 
D 4 HOH 73  673 171 HOH HOH A . 
D 4 HOH 74  674 286 HOH HOH A . 
D 4 HOH 75  675 56  HOH HOH A . 
D 4 HOH 76  676 229 HOH HOH A . 
D 4 HOH 77  677 54  HOH HOH A . 
D 4 HOH 78  678 50  HOH HOH A . 
D 4 HOH 79  679 14  HOH HOH A . 
D 4 HOH 80  680 332 HOH HOH A . 
D 4 HOH 81  681 193 HOH HOH A . 
D 4 HOH 82  682 85  HOH HOH A . 
D 4 HOH 83  683 158 HOH HOH A . 
D 4 HOH 84  684 226 HOH HOH A . 
D 4 HOH 85  685 90  HOH HOH A . 
D 4 HOH 86  686 277 HOH HOH A . 
D 4 HOH 87  687 239 HOH HOH A . 
D 4 HOH 88  688 69  HOH HOH A . 
D 4 HOH 89  689 155 HOH HOH A . 
D 4 HOH 90  690 21  HOH HOH A . 
D 4 HOH 91  691 79  HOH HOH A . 
D 4 HOH 92  692 201 HOH HOH A . 
D 4 HOH 93  693 63  HOH HOH A . 
D 4 HOH 94  694 4   HOH HOH A . 
D 4 HOH 95  695 11  HOH HOH A . 
D 4 HOH 96  696 82  HOH HOH A . 
D 4 HOH 97  697 281 HOH HOH A . 
D 4 HOH 98  698 348 HOH HOH A . 
D 4 HOH 99  699 116 HOH HOH A . 
D 4 HOH 100 700 68  HOH HOH A . 
D 4 HOH 101 701 208 HOH HOH A . 
D 4 HOH 102 702 53  HOH HOH A . 
D 4 HOH 103 703 221 HOH HOH A . 
D 4 HOH 104 704 30  HOH HOH A . 
D 4 HOH 105 705 385 HOH HOH A . 
D 4 HOH 106 706 61  HOH HOH A . 
D 4 HOH 107 707 72  HOH HOH A . 
D 4 HOH 108 708 296 HOH HOH A . 
D 4 HOH 109 709 55  HOH HOH A . 
D 4 HOH 110 710 163 HOH HOH A . 
D 4 HOH 111 711 58  HOH HOH A . 
D 4 HOH 112 712 216 HOH HOH A . 
D 4 HOH 113 713 5   HOH HOH A . 
D 4 HOH 114 714 107 HOH HOH A . 
D 4 HOH 115 715 282 HOH HOH A . 
D 4 HOH 116 716 438 HOH HOH A . 
D 4 HOH 117 717 197 HOH HOH A . 
D 4 HOH 118 718 410 HOH HOH A . 
D 4 HOH 119 719 15  HOH HOH A . 
D 4 HOH 120 720 377 HOH HOH A . 
D 4 HOH 121 721 238 HOH HOH A . 
D 4 HOH 122 722 184 HOH HOH A . 
D 4 HOH 123 723 267 HOH HOH A . 
D 4 HOH 124 724 157 HOH HOH A . 
D 4 HOH 125 725 91  HOH HOH A . 
D 4 HOH 126 726 309 HOH HOH A . 
D 4 HOH 127 727 130 HOH HOH A . 
D 4 HOH 128 728 289 HOH HOH A . 
D 4 HOH 129 729 103 HOH HOH A . 
D 4 HOH 130 730 159 HOH HOH A . 
D 4 HOH 131 731 12  HOH HOH A . 
D 4 HOH 132 732 149 HOH HOH A . 
D 4 HOH 133 733 245 HOH HOH A . 
D 4 HOH 134 734 266 HOH HOH A . 
D 4 HOH 135 735 146 HOH HOH A . 
D 4 HOH 136 736 52  HOH HOH A . 
D 4 HOH 137 737 148 HOH HOH A . 
D 4 HOH 138 738 36  HOH HOH A . 
D 4 HOH 139 739 120 HOH HOH A . 
D 4 HOH 140 740 42  HOH HOH A . 
D 4 HOH 141 741 67  HOH HOH A . 
D 4 HOH 142 742 300 HOH HOH A . 
D 4 HOH 143 743 382 HOH HOH A . 
D 4 HOH 144 744 26  HOH HOH A . 
D 4 HOH 145 745 301 HOH HOH A . 
D 4 HOH 146 746 128 HOH HOH A . 
D 4 HOH 147 747 192 HOH HOH A . 
D 4 HOH 148 748 45  HOH HOH A . 
D 4 HOH 149 749 414 HOH HOH A . 
D 4 HOH 150 750 224 HOH HOH A . 
D 4 HOH 151 751 6   HOH HOH A . 
D 4 HOH 152 752 2   HOH HOH A . 
D 4 HOH 153 753 84  HOH HOH A . 
D 4 HOH 154 754 95  HOH HOH A . 
D 4 HOH 155 755 271 HOH HOH A . 
D 4 HOH 156 756 75  HOH HOH A . 
D 4 HOH 157 757 169 HOH HOH A . 
D 4 HOH 158 758 33  HOH HOH A . 
D 4 HOH 159 759 100 HOH HOH A . 
D 4 HOH 160 760 196 HOH HOH A . 
D 4 HOH 161 761 240 HOH HOH A . 
D 4 HOH 162 762 261 HOH HOH A . 
D 4 HOH 163 763 27  HOH HOH A . 
D 4 HOH 164 764 354 HOH HOH A . 
D 4 HOH 165 765 232 HOH HOH A . 
D 4 HOH 166 766 122 HOH HOH A . 
D 4 HOH 167 767 263 HOH HOH A . 
D 4 HOH 168 768 304 HOH HOH A . 
D 4 HOH 169 769 161 HOH HOH A . 
D 4 HOH 170 770 172 HOH HOH A . 
D 4 HOH 171 771 183 HOH HOH A . 
D 4 HOH 172 772 222 HOH HOH A . 
D 4 HOH 173 773 102 HOH HOH A . 
D 4 HOH 174 774 124 HOH HOH A . 
D 4 HOH 175 775 64  HOH HOH A . 
D 4 HOH 176 776 19  HOH HOH A . 
D 4 HOH 177 777 83  HOH HOH A . 
D 4 HOH 178 778 153 HOH HOH A . 
D 4 HOH 179 779 140 HOH HOH A . 
D 4 HOH 180 780 126 HOH HOH A . 
D 4 HOH 181 781 345 HOH HOH A . 
D 4 HOH 182 782 89  HOH HOH A . 
D 4 HOH 183 783 109 HOH HOH A . 
D 4 HOH 184 784 60  HOH HOH A . 
D 4 HOH 185 785 253 HOH HOH A . 
D 4 HOH 186 786 351 HOH HOH A . 
D 4 HOH 187 787 35  HOH HOH A . 
D 4 HOH 188 788 210 HOH HOH A . 
D 4 HOH 189 789 176 HOH HOH A . 
D 4 HOH 190 790 285 HOH HOH A . 
D 4 HOH 191 791 166 HOH HOH A . 
D 4 HOH 192 792 113 HOH HOH A . 
D 4 HOH 193 793 175 HOH HOH A . 
D 4 HOH 194 794 185 HOH HOH A . 
D 4 HOH 195 795 23  HOH HOH A . 
D 4 HOH 196 796 25  HOH HOH A . 
D 4 HOH 197 797 132 HOH HOH A . 
D 4 HOH 198 798 98  HOH HOH A . 
D 4 HOH 199 799 179 HOH HOH A . 
D 4 HOH 200 800 371 HOH HOH A . 
D 4 HOH 201 801 327 HOH HOH A . 
D 4 HOH 202 802 306 HOH HOH A . 
D 4 HOH 203 803 217 HOH HOH A . 
D 4 HOH 204 804 174 HOH HOH A . 
D 4 HOH 205 805 361 HOH HOH A . 
D 4 HOH 206 806 94  HOH HOH A . 
D 4 HOH 207 807 287 HOH HOH A . 
D 4 HOH 208 808 170 HOH HOH A . 
D 4 HOH 209 809 7   HOH HOH A . 
D 4 HOH 210 810 112 HOH HOH A . 
D 4 HOH 211 811 249 HOH HOH A . 
D 4 HOH 212 812 20  HOH HOH A . 
D 4 HOH 213 813 96  HOH HOH A . 
D 4 HOH 214 814 59  HOH HOH A . 
D 4 HOH 215 815 49  HOH HOH A . 
D 4 HOH 216 816 373 HOH HOH A . 
D 4 HOH 217 817 38  HOH HOH A . 
D 4 HOH 218 818 218 HOH HOH A . 
D 4 HOH 219 819 78  HOH HOH A . 
D 4 HOH 220 820 48  HOH HOH A . 
D 4 HOH 221 821 93  HOH HOH A . 
D 4 HOH 222 822 147 HOH HOH A . 
D 4 HOH 223 823 259 HOH HOH A . 
D 4 HOH 224 824 181 HOH HOH A . 
D 4 HOH 225 825 349 HOH HOH A . 
D 4 HOH 226 826 86  HOH HOH A . 
D 4 HOH 227 827 156 HOH HOH A . 
D 4 HOH 228 828 195 HOH HOH A . 
D 4 HOH 229 829 164 HOH HOH A . 
D 4 HOH 230 830 366 HOH HOH A . 
D 4 HOH 231 831 17  HOH HOH A . 
D 4 HOH 232 832 135 HOH HOH A . 
D 4 HOH 233 833 191 HOH HOH A . 
D 4 HOH 234 834 215 HOH HOH A . 
D 4 HOH 235 835 70  HOH HOH A . 
D 4 HOH 236 836 355 HOH HOH A . 
D 4 HOH 237 837 375 HOH HOH A . 
D 4 HOH 238 838 71  HOH HOH A . 
D 4 HOH 239 839 251 HOH HOH A . 
D 4 HOH 240 840 412 HOH HOH A . 
D 4 HOH 241 841 92  HOH HOH A . 
D 4 HOH 242 842 162 HOH HOH A . 
D 4 HOH 243 843 233 HOH HOH A . 
D 4 HOH 244 844 125 HOH HOH A . 
D 4 HOH 245 845 252 HOH HOH A . 
D 4 HOH 246 846 288 HOH HOH A . 
D 4 HOH 247 847 340 HOH HOH A . 
D 4 HOH 248 848 106 HOH HOH A . 
D 4 HOH 249 849 43  HOH HOH A . 
D 4 HOH 250 850 294 HOH HOH A . 
D 4 HOH 251 851 209 HOH HOH A . 
D 4 HOH 252 852 227 HOH HOH A . 
D 4 HOH 253 853 101 HOH HOH A . 
D 4 HOH 254 854 74  HOH HOH A . 
D 4 HOH 255 855 34  HOH HOH A . 
D 4 HOH 256 856 353 HOH HOH A . 
D 4 HOH 257 857 62  HOH HOH A . 
D 4 HOH 258 858 237 HOH HOH A . 
D 4 HOH 259 859 65  HOH HOH A . 
D 4 HOH 260 860 119 HOH HOH A . 
D 4 HOH 261 861 329 HOH HOH A . 
D 4 HOH 262 862 151 HOH HOH A . 
D 4 HOH 263 863 376 HOH HOH A . 
D 4 HOH 264 864 177 HOH HOH A . 
D 4 HOH 265 865 297 HOH HOH A . 
D 4 HOH 266 866 205 HOH HOH A . 
D 4 HOH 267 867 374 HOH HOH A . 
D 4 HOH 268 868 316 HOH HOH A . 
D 4 HOH 269 869 99  HOH HOH A . 
D 4 HOH 270 870 357 HOH HOH A . 
D 4 HOH 271 871 212 HOH HOH A . 
D 4 HOH 272 872 278 HOH HOH A . 
D 4 HOH 273 873 364 HOH HOH A . 
D 4 HOH 274 874 44  HOH HOH A . 
D 4 HOH 275 875 118 HOH HOH A . 
D 4 HOH 276 876 236 HOH HOH A . 
D 4 HOH 277 877 76  HOH HOH A . 
D 4 HOH 278 878 321 HOH HOH A . 
D 4 HOH 279 879 213 HOH HOH A . 
D 4 HOH 280 880 273 HOH HOH A . 
D 4 HOH 281 881 182 HOH HOH A . 
D 4 HOH 282 882 123 HOH HOH A . 
D 4 HOH 283 883 274 HOH HOH A . 
D 4 HOH 284 884 310 HOH HOH A . 
D 4 HOH 285 885 370 HOH HOH A . 
D 4 HOH 286 886 334 HOH HOH A . 
D 4 HOH 287 887 270 HOH HOH A . 
D 4 HOH 288 888 367 HOH HOH A . 
D 4 HOH 289 889 139 HOH HOH A . 
D 4 HOH 290 890 136 HOH HOH A . 
D 4 HOH 291 891 256 HOH HOH A . 
D 4 HOH 292 892 324 HOH HOH A . 
D 4 HOH 293 893 225 HOH HOH A . 
D 4 HOH 294 894 198 HOH HOH A . 
D 4 HOH 295 895 279 HOH HOH A . 
D 4 HOH 296 896 202 HOH HOH A . 
D 4 HOH 297 897 272 HOH HOH A . 
D 4 HOH 298 898 199 HOH HOH A . 
D 4 HOH 299 899 150 HOH HOH A . 
D 4 HOH 300 900 315 HOH HOH A . 
D 4 HOH 301 901 317 HOH HOH A . 
D 4 HOH 302 902 254 HOH HOH A . 
D 4 HOH 303 903 248 HOH HOH A . 
D 4 HOH 304 904 81  HOH HOH A . 
D 4 HOH 305 905 194 HOH HOH A . 
D 4 HOH 306 906 129 HOH HOH A . 
D 4 HOH 307 907 108 HOH HOH A . 
D 4 HOH 308 908 114 HOH HOH A . 
D 4 HOH 309 909 426 HOH HOH A . 
D 4 HOH 310 910 323 HOH HOH A . 
D 4 HOH 311 911 234 HOH HOH A . 
D 4 HOH 312 912 396 HOH HOH A . 
# 
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   ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZOP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     117.607 
_cell.length_a_esd                 ? 
_cell.length_b                     117.607 
_cell.length_b_esd                 ? 
_cell.length_c                     63.829 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         8ZOP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZOP 
_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             2.78 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.70 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.8 M Ammonium citrate tribasic, pH 7.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-10-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZOP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.5 
_reflns.d_resolution_low                               58.8 
_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                                     81400 
_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                                19.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.8 
_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                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.090 
_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                                    1.50 
_reflns_shell.d_res_low                                     1.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4045 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.412 
_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]                            -0.09 
_refine.aniso_B[1][2]                            -0.04 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.09 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.28 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               13.750 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.971 
_refine.correlation_coeff_Fo_to_Fc_free          0.963 
_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                                 8ZOP 
_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                            1.50 
_refine.ls_d_res_low                             50.98 
_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                     79329 
_refine.ls_number_reflns_R_free                  1994 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 2.5 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14848 
_refine.ls_R_factor_R_free                       0.17145 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.14791 
_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                       0.053 
_refine.pdbx_overall_ESU_R_Free                  0.055 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             0.778 
_refine.overall_SU_ML                            0.030 
_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                       1.50 
_refine_hist.d_res_low                        50.98 
_refine_hist.number_atoms_solvent             312 
_refine_hist.number_atoms_total               3579 
_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        3213 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_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' ? 0.017  0.013  3344 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.015  3072 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.064  1.645  4542 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.611  1.582  7045 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.683  5.000  406  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 29.094 20.722 194  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.117 15.000 530  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.230 15.000 32   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.117  0.200  413  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  3818 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  819  ? 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' ? 1.414  1.235  1630 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.413  1.234  1629 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.075  1.851  2034 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.074  1.852  2035 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.883  1.504  1714 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.886  1.506  1711 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.289  2.140  2509 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.852  15.049 3853 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.813  14.743 3801 ? 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                       1.500 
_refine_ls_shell.d_res_low                        1.539 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             145 
_refine_ls_shell.number_reflns_R_work             5846 
_refine_ls_shell.percent_reflns_obs               99.98 
_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                  0.159 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.183 
# 
_struct.entry_id                     8ZOP 
_struct.title                        'Structure of FasV in complex with FAD' 
_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        8ZOP 
_struct_keywords.text            'Naphthacemycins, Flavin-dependent halogenases, FasV, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    G3EGL7_9BACT 
_struct_ref.pdbx_db_accession          G3EGL7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MNNGHEEYDVIVVGGGPAGSSAAGLLALNGHSVLLLERDKFPRYHIGESLITGVLPTLARLGLTERMEQLGFQRKYGGSL
LWGKGHSKPWTFKFRETGNGKYEYAYQVRRADFDALLLDRARELGVTVLEGASVKEPLFDGDRMVGVRYSVRNEAETVDV
SGKITIDATGQQRWLGRHFDMVEWHEDLRNIAAWSYYQGGLRYEGETEGNILTENRPHGWLWYIPLSKDITSIGYVTPSS
RLAESGLTPEAMLDKQIAESSEVGRLTANARRVDIYRTARDWSYVCERFSGPGYALVGDAAAFIDPLLSTGVTLAMRGGS
TVSRAVHEALVDPAKERDTLQTYEDSYRDFLNSLLEFVRFFYDRTKGQKDYHVGAQAIIDPDKHFPANVDFVTLVSGLAR
GDDAVDVPS
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8ZOP 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 412 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             G3EGL7 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  409 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       410 
# 
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 8ZOP GLY A 1 ? UNP G3EGL7 ? ? 'expression tag' -1 1 
1 8ZOP SER A 2 ? UNP G3EGL7 ? ? 'expression tag' 0  2 
1 8ZOP HIS A 3 ? UNP G3EGL7 ? ? 'expression tag' 1  3 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 1640  ? 
1 MORE         -19   ? 
1 'SSA (A^2)'  16770 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 GLY A 19  ? ASN A 32  ? GLY A 17  ASN A 30  1 ? 14 
HELX_P HELX_P2  AA2 ILE A 54  ? GLY A 56  ? ILE A 52  GLY A 54  5 ? 3  
HELX_P HELX_P3  AA3 VAL A 57  ? LEU A 64  ? VAL A 55  LEU A 62  1 ? 8  
HELX_P HELX_P4  AA4 LEU A 66  ? GLY A 74  ? LEU A 64  GLY A 72  1 ? 9  
HELX_P HELX_P5  AA5 ARG A 98  ? LYS A 104 ? ARG A 96  LYS A 102 5 ? 7  
HELX_P HELX_P6  AA6 ARG A 112 ? LEU A 127 ? ARG A 110 LEU A 125 1 ? 16 
HELX_P HELX_P7  AA7 THR A 172 ? GLN A 175 ? THR A 170 GLN A 173 5 ? 4  
HELX_P HELX_P8  AA8 ARG A 176 ? PHE A 182 ? ARG A 174 PHE A 180 1 ? 7  
HELX_P HELX_P9  AA9 GLU A 207 ? ASN A 213 ? GLU A 205 ASN A 211 5 ? 7  
HELX_P HELX_P10 AB1 SER A 242 ? GLY A 249 ? SER A 240 GLY A 247 1 ? 8  
HELX_P HELX_P11 AB2 THR A 251 ? SER A 263 ? THR A 249 SER A 261 1 ? 13 
HELX_P HELX_P12 AB3 SER A 264 ? THR A 270 ? SER A 262 THR A 268 1 ? 7  
HELX_P HELX_P13 AB4 GLY A 301 ? ALA A 303 ? GLY A 299 ALA A 301 5 ? 3  
HELX_P HELX_P14 AB5 THR A 313 ? ASP A 335 ? THR A 311 ASP A 333 1 ? 23 
HELX_P HELX_P15 AB6 LYS A 338 ? TYR A 365 ? LYS A 336 TYR A 363 1 ? 28 
HELX_P HELX_P16 AB7 GLY A 370 ? ASP A 383 ? GLY A 368 ASP A 381 1 ? 14 
HELX_P HELX_P17 AB8 PRO A 389 ? SER A 399 ? PRO A 387 SER A 397 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PHE 
_struct_mon_prot_cis.label_seq_id           44 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PHE 
_struct_mon_prot_cis.auth_seq_id            42 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    45 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     43 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.24 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 7 ? 
AA6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 130 ? GLU A 133 ? THR A 128 GLU A 131 
AA1 2 VAL A 36  ? GLU A 40  ? VAL A 34  GLU A 38  
AA1 3 GLU A 10  ? VAL A 16  ? GLU A 8   VAL A 14  
AA1 4 VAL A 161 ? ASP A 170 ? VAL A 159 ASP A 168 
AA1 5 ARG A 146 ? VAL A 154 ? ARG A 144 VAL A 152 
AA1 6 ALA A 135 ? ASP A 143 ? ALA A 133 ASP A 141 
AA2 1 THR A 130 ? GLU A 133 ? THR A 128 GLU A 131 
AA2 2 VAL A 36  ? GLU A 40  ? VAL A 34  GLU A 38  
AA2 3 GLU A 10  ? VAL A 16  ? GLU A 8   VAL A 14  
AA2 4 VAL A 161 ? ASP A 170 ? VAL A 159 ASP A 168 
AA2 5 TYR A 297 ? LEU A 299 ? TYR A 295 LEU A 297 
AA2 6 SER A 293 ? GLY A 294 ? SER A 291 GLY A 292 
AA3 1 GLN A 76  ? LYS A 78  ? GLN A 74  LYS A 76  
AA3 2 ALA A 108 ? GLN A 110 ? ALA A 106 GLN A 108 
AA4 1 TRP A 93  ? LYS A 96  ? TRP A 91  LYS A 94  
AA4 2 GLY A 80  ? LEU A 84  ? GLY A 78  LEU A 82  
AA4 3 ILE A 214 ? ARG A 219 ? ILE A 212 ARG A 217 
AA4 4 GLY A 222 ? PRO A 228 ? GLY A 220 PRO A 226 
AA4 5 ILE A 233 ? PRO A 241 ? ILE A 231 PRO A 239 
AA4 6 ASN A 193 ? GLN A 201 ? ASN A 191 GLN A 199 
AA4 7 ARG A 274 ? ARG A 275 ? ARG A 272 ARG A 273 
AA5 1 TRP A 93  ? LYS A 96  ? TRP A 91  LYS A 94  
AA5 2 GLY A 80  ? LEU A 84  ? GLY A 78  LEU A 82  
AA5 3 ILE A 214 ? ARG A 219 ? ILE A 212 ARG A 217 
AA5 4 GLY A 222 ? PRO A 228 ? GLY A 220 PRO A 226 
AA5 5 ILE A 233 ? PRO A 241 ? ILE A 231 PRO A 239 
AA5 6 ASN A 193 ? GLN A 201 ? ASN A 191 GLN A 199 
AA5 7 ARG A 280 ? ARG A 283 ? ARG A 278 ARG A 281 
AA6 1 VAL A 185 ? TRP A 187 ? VAL A 183 TRP A 185 
AA6 2 TYR A 287 ? CYS A 289 ? TYR A 285 CYS A 287 
AA6 3 ALA A 305 ? PHE A 306 ? ALA A 303 PHE A 304 
# 
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 O LEU A 132 ? O LEU A 130 N LEU A 38  ? N LEU A 36  
AA1 2 3 O LEU A 37  ? O LEU A 35  N VAL A 15  ? N VAL A 13  
AA1 3 4 N ILE A 14  ? N ILE A 12  O ILE A 169 ? O ILE A 167 
AA1 4 5 O VAL A 161 ? O VAL A 159 N TYR A 152 ? N TYR A 150 
AA1 5 6 O ARG A 151 ? O ARG A 149 N LYS A 138 ? N LYS A 136 
AA2 1 2 O LEU A 132 ? O LEU A 130 N LEU A 38  ? N LEU A 36  
AA2 2 3 O LEU A 37  ? O LEU A 35  N VAL A 15  ? N VAL A 13  
AA2 3 4 N ILE A 14  ? N ILE A 12  O ILE A 169 ? O ILE A 167 
AA2 4 5 N ASP A 170 ? N ASP A 168 O ALA A 298 ? O ALA A 296 
AA2 5 6 O TYR A 297 ? O TYR A 295 N GLY A 294 ? N GLY A 292 
AA3 1 2 N LYS A 78  ? N LYS A 76  O ALA A 108 ? O ALA A 106 
AA4 1 2 O TRP A 93  ? O TRP A 91  N LEU A 83  ? N LEU A 81  
AA4 2 3 N SER A 82  ? N SER A 80  O ILE A 214 ? O ILE A 212 
AA4 3 4 N ARG A 219 ? N ARG A 217 O GLY A 222 ? O GLY A 220 
AA4 4 5 N TRP A 223 ? N TRP A 221 O VAL A 239 ? O VAL A 237 
AA4 5 6 O THR A 240 ? O THR A 238 N ILE A 194 ? N ILE A 192 
AA4 6 7 N GLN A 201 ? N GLN A 199 O ARG A 274 ? O ARG A 272 
AA5 1 2 O TRP A 93  ? O TRP A 91  N LEU A 83  ? N LEU A 81  
AA5 2 3 N SER A 82  ? N SER A 80  O ILE A 214 ? O ILE A 212 
AA5 3 4 N ARG A 219 ? N ARG A 217 O GLY A 222 ? O GLY A 220 
AA5 4 5 N TRP A 223 ? N TRP A 221 O VAL A 239 ? O VAL A 237 
AA5 5 6 O THR A 240 ? O THR A 238 N ILE A 194 ? N ILE A 192 
AA5 6 7 N ALA A 195 ? N ALA A 193 O ALA A 282 ? O ALA A 280 
AA6 1 2 N GLU A 186 ? N GLU A 184 O VAL A 288 ? O VAL A 286 
AA6 2 3 N TYR A 287 ? N TYR A 285 O PHE A 306 ? O PHE A 304 
# 
_pdbx_entry_details.entry_id                   8ZOP 
_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_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 HIS A 1   ? ? -66.57  94.72   
2 1 ALA A 106 ? ? -115.62 -146.83 
3 1 ILE A 305 ? ? -96.18  -79.60  
4 1 ASP A 381 ? ? -147.22 55.90   
5 1 VAL A 406 ? ? -141.51 39.95   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     821 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       912 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.01 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 86  ? A GLY 88  
2 1 Y 1 A HIS 87  ? A HIS 89  
3 1 Y 1 A SER 88  ? A SER 90  
4 1 Y 1 A SER 410 ? A SER 412 
# 
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  
CL  CL     CL N N 74  
CYS N      N  N N 75  
CYS CA     C  N R 76  
CYS C      C  N N 77  
CYS O      O  N N 78  
CYS CB     C  N N 79  
CYS SG     S  N N 80  
CYS OXT    O  N N 81  
CYS H      H  N N 82  
CYS H2     H  N N 83  
CYS HA     H  N N 84  
CYS HB2    H  N N 85  
CYS HB3    H  N N 86  
CYS HG     H  N N 87  
CYS HXT    H  N N 88  
FAD PA     P  N R 89  
FAD O1A    O  N N 90  
FAD O2A    O  N N 91  
FAD O5B    O  N N 92  
FAD C5B    C  N N 93  
FAD C4B    C  N R 94  
FAD O4B    O  N N 95  
FAD C3B    C  N S 96  
FAD O3B    O  N N 97  
FAD C2B    C  N R 98  
FAD O2B    O  N N 99  
FAD C1B    C  N R 100 
FAD N9A    N  Y N 101 
FAD C8A    C  Y N 102 
FAD N7A    N  Y N 103 
FAD C5A    C  Y N 104 
FAD C6A    C  Y N 105 
FAD N6A    N  N N 106 
FAD N1A    N  Y N 107 
FAD C2A    C  Y N 108 
FAD N3A    N  Y N 109 
FAD C4A    C  Y N 110 
FAD N1     N  N N 111 
FAD C2     C  N N 112 
FAD O2     O  N N 113 
FAD N3     N  N N 114 
FAD C4     C  N N 115 
FAD O4     O  N N 116 
FAD C4X    C  N N 117 
FAD N5     N  N N 118 
FAD C5X    C  Y N 119 
FAD C6     C  Y N 120 
FAD C7     C  Y N 121 
FAD C7M    C  N N 122 
FAD C8     C  Y N 123 
FAD C8M    C  N N 124 
FAD C9     C  Y N 125 
FAD C9A    C  Y N 126 
FAD N10    N  N N 127 
FAD C10    C  N N 128 
FAD "C1'"  C  N N 129 
FAD "C2'"  C  N S 130 
FAD "O2'"  O  N N 131 
FAD "C3'"  C  N S 132 
FAD "O3'"  O  N N 133 
FAD "C4'"  C  N R 134 
FAD "O4'"  O  N N 135 
FAD "C5'"  C  N N 136 
FAD "O5'"  O  N N 137 
FAD P      P  N R 138 
FAD O1P    O  N N 139 
FAD O2P    O  N N 140 
FAD O3P    O  N N 141 
FAD HOA2   H  N N 142 
FAD H51A   H  N N 143 
FAD H52A   H  N N 144 
FAD H4B    H  N N 145 
FAD H3B    H  N N 146 
FAD HO3A   H  N N 147 
FAD H2B    H  N N 148 
FAD HO2A   H  N N 149 
FAD H1B    H  N N 150 
FAD H8A    H  N N 151 
FAD H61A   H  N N 152 
FAD H62A   H  N N 153 
FAD H2A    H  N N 154 
FAD HN3    H  N N 155 
FAD H6     H  N N 156 
FAD HM71   H  N N 157 
FAD HM72   H  N N 158 
FAD HM73   H  N N 159 
FAD HM81   H  N N 160 
FAD HM82   H  N N 161 
FAD HM83   H  N N 162 
FAD H9     H  N N 163 
FAD "H1'1" H  N N 164 
FAD "H1'2" H  N N 165 
FAD "H2'"  H  N N 166 
FAD "HO2'" H  N N 167 
FAD "H3'"  H  N N 168 
FAD "HO3'" H  N N 169 
FAD "H4'"  H  N N 170 
FAD "HO4'" H  N N 171 
FAD "H5'1" H  N N 172 
FAD "H5'2" H  N N 173 
FAD HOP2   H  N N 174 
GLN N      N  N N 175 
GLN CA     C  N S 176 
GLN C      C  N N 177 
GLN O      O  N N 178 
GLN CB     C  N N 179 
GLN CG     C  N N 180 
GLN CD     C  N N 181 
GLN OE1    O  N N 182 
GLN NE2    N  N N 183 
GLN OXT    O  N N 184 
GLN H      H  N N 185 
GLN H2     H  N N 186 
GLN HA     H  N N 187 
GLN HB2    H  N N 188 
GLN HB3    H  N N 189 
GLN HG2    H  N N 190 
GLN HG3    H  N N 191 
GLN HE21   H  N N 192 
GLN HE22   H  N N 193 
GLN HXT    H  N N 194 
GLU N      N  N N 195 
GLU CA     C  N S 196 
GLU C      C  N N 197 
GLU O      O  N N 198 
GLU CB     C  N N 199 
GLU CG     C  N N 200 
GLU CD     C  N N 201 
GLU OE1    O  N N 202 
GLU OE2    O  N N 203 
GLU OXT    O  N N 204 
GLU H      H  N N 205 
GLU H2     H  N N 206 
GLU HA     H  N N 207 
GLU HB2    H  N N 208 
GLU HB3    H  N N 209 
GLU HG2    H  N N 210 
GLU HG3    H  N N 211 
GLU HE2    H  N N 212 
GLU HXT    H  N N 213 
GLY N      N  N N 214 
GLY CA     C  N N 215 
GLY C      C  N N 216 
GLY O      O  N N 217 
GLY OXT    O  N N 218 
GLY H      H  N N 219 
GLY H2     H  N N 220 
GLY HA2    H  N N 221 
GLY HA3    H  N N 222 
GLY HXT    H  N N 223 
HIS N      N  N N 224 
HIS CA     C  N S 225 
HIS C      C  N N 226 
HIS O      O  N N 227 
HIS CB     C  N N 228 
HIS CG     C  Y N 229 
HIS ND1    N  Y N 230 
HIS CD2    C  Y N 231 
HIS CE1    C  Y N 232 
HIS NE2    N  Y N 233 
HIS OXT    O  N N 234 
HIS H      H  N N 235 
HIS H2     H  N N 236 
HIS HA     H  N N 237 
HIS HB2    H  N N 238 
HIS HB3    H  N N 239 
HIS HD1    H  N N 240 
HIS HD2    H  N N 241 
HIS HE1    H  N N 242 
HIS HE2    H  N N 243 
HIS HXT    H  N N 244 
HOH O      O  N N 245 
HOH H1     H  N N 246 
HOH H2     H  N N 247 
ILE N      N  N N 248 
ILE CA     C  N S 249 
ILE C      C  N N 250 
ILE O      O  N N 251 
ILE CB     C  N S 252 
ILE CG1    C  N N 253 
ILE CG2    C  N N 254 
ILE CD1    C  N N 255 
ILE OXT    O  N N 256 
ILE H      H  N N 257 
ILE H2     H  N N 258 
ILE HA     H  N N 259 
ILE HB     H  N N 260 
ILE HG12   H  N N 261 
ILE HG13   H  N N 262 
ILE HG21   H  N N 263 
ILE HG22   H  N N 264 
ILE HG23   H  N N 265 
ILE HD11   H  N N 266 
ILE HD12   H  N N 267 
ILE HD13   H  N N 268 
ILE HXT    H  N N 269 
LEU N      N  N N 270 
LEU CA     C  N S 271 
LEU C      C  N N 272 
LEU O      O  N N 273 
LEU CB     C  N N 274 
LEU CG     C  N N 275 
LEU CD1    C  N N 276 
LEU CD2    C  N N 277 
LEU OXT    O  N N 278 
LEU H      H  N N 279 
LEU H2     H  N N 280 
LEU HA     H  N N 281 
LEU HB2    H  N N 282 
LEU HB3    H  N N 283 
LEU HG     H  N N 284 
LEU HD11   H  N N 285 
LEU HD12   H  N N 286 
LEU HD13   H  N N 287 
LEU HD21   H  N N 288 
LEU HD22   H  N N 289 
LEU HD23   H  N N 290 
LEU HXT    H  N N 291 
LYS N      N  N N 292 
LYS CA     C  N S 293 
LYS C      C  N N 294 
LYS O      O  N N 295 
LYS CB     C  N N 296 
LYS CG     C  N N 297 
LYS CD     C  N N 298 
LYS CE     C  N N 299 
LYS NZ     N  N N 300 
LYS OXT    O  N N 301 
LYS H      H  N N 302 
LYS H2     H  N N 303 
LYS HA     H  N N 304 
LYS HB2    H  N N 305 
LYS HB3    H  N N 306 
LYS HG2    H  N N 307 
LYS HG3    H  N N 308 
LYS HD2    H  N N 309 
LYS HD3    H  N N 310 
LYS HE2    H  N N 311 
LYS HE3    H  N N 312 
LYS HZ1    H  N N 313 
LYS HZ2    H  N N 314 
LYS HZ3    H  N N 315 
LYS HXT    H  N N 316 
MET N      N  N N 317 
MET CA     C  N S 318 
MET C      C  N N 319 
MET O      O  N N 320 
MET CB     C  N N 321 
MET CG     C  N N 322 
MET SD     S  N N 323 
MET CE     C  N N 324 
MET OXT    O  N N 325 
MET H      H  N N 326 
MET H2     H  N N 327 
MET HA     H  N N 328 
MET HB2    H  N N 329 
MET HB3    H  N N 330 
MET HG2    H  N N 331 
MET HG3    H  N N 332 
MET HE1    H  N N 333 
MET HE2    H  N N 334 
MET HE3    H  N N 335 
MET HXT    H  N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
# 
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  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_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   3E1T 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZOP 
_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]   0.008503 
_atom_sites.fract_transf_matrix[1][2]   0.004909 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009818 
_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]   0.015667 
_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  
CL 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLY A 1 1   ? 67.415 16.149 -15.297 1.00 31.76 ?  -1  GLY A N     1 
ATOM   2    C  CA    . GLY A 1 1   ? 66.506 15.351 -14.398 1.00 27.92 ?  -1  GLY A CA    1 
ATOM   3    C  C     . GLY A 1 1   ? 65.863 16.191 -13.312 1.00 23.95 ?  -1  GLY A C     1 
ATOM   4    O  O     . GLY A 1 1   ? 66.072 17.454 -13.198 1.00 22.40 ?  -1  GLY A O     1 
ATOM   5    N  N     . SER A 1 2   ? 65.067 15.487 -12.510 1.00 24.97 ?  0   SER A N     1 
ATOM   6    C  CA    . SER A 1 2   ? 64.252 16.126 -11.459 1.00 25.34 ?  0   SER A CA    1 
ATOM   7    C  C     . SER A 1 2   ? 64.061 15.121 -10.323 1.00 26.25 ?  0   SER A C     1 
ATOM   8    O  O     . SER A 1 2   ? 64.036 13.892 -10.592 1.00 29.68 ?  0   SER A O     1 
ATOM   9    C  CB    . SER A 1 2   ? 62.944 16.605 -12.083 1.00 25.33 ?  0   SER A CB    1 
ATOM   10   O  OG    . SER A 1 2   ? 62.165 17.303 -11.141 1.00 27.94 ?  0   SER A OG    1 
ATOM   11   N  N     . HIS A 1 3   ? 63.902 15.627 -9.108  1.00 26.64 ?  1   HIS A N     1 
ATOM   12   C  CA    . HIS A 1 3   ? 63.359 14.807 -7.998  1.00 29.01 ?  1   HIS A CA    1 
ATOM   13   C  C     . HIS A 1 3   ? 61.886 14.485 -8.347  1.00 29.72 ?  1   HIS A C     1 
ATOM   14   O  O     . HIS A 1 3   ? 61.023 15.345 -8.182  1.00 31.19 ?  1   HIS A O     1 
ATOM   15   C  CB    . HIS A 1 3   ? 63.584 15.522 -6.654  1.00 35.20 ?  1   HIS A CB    1 
ATOM   16   C  CG    . HIS A 1 3   ? 63.185 14.689 -5.474  1.00 42.24 ?  1   HIS A CG    1 
ATOM   17   N  ND1   . HIS A 1 3   ? 63.650 14.950 -4.187  1.00 46.27 ?  1   HIS A ND1   1 
ATOM   18   C  CD2   . HIS A 1 3   ? 62.391 13.591 -5.379  1.00 45.25 ?  1   HIS A CD2   1 
ATOM   19   C  CE1   . HIS A 1 3   ? 63.127 14.066 -3.346  1.00 44.28 ?  1   HIS A CE1   1 
ATOM   20   N  NE2   . HIS A 1 3   ? 62.361 13.206 -4.057  1.00 41.01 ?  1   HIS A NE2   1 
ATOM   21   N  N     . MET A 1 4   ? 61.639 13.324 -8.959  1.00 34.58 ?  2   MET A N     1 
ATOM   22   C  CA    . MET A 1 4   ? 60.266 12.893 -9.350  1.00 34.17 ?  2   MET A CA    1 
ATOM   23   C  C     . MET A 1 4   ? 59.732 12.060 -8.177  1.00 35.31 ?  2   MET A C     1 
ATOM   24   O  O     . MET A 1 4   ? 60.533 11.437 -7.429  1.00 35.42 ?  2   MET A O     1 
ATOM   25   C  CB    . MET A 1 4   ? 60.246 12.068 -10.657 1.00 36.08 ?  2   MET A CB    1 
ATOM   26   C  CG    . MET A 1 4   ? 60.846 12.777 -11.898 1.00 40.45 ?  2   MET A CG    1 
ATOM   27   S  SD    . MET A 1 4   ? 60.066 14.404 -12.284 1.00 40.72 ?  2   MET A SD    1 
ATOM   28   C  CE    . MET A 1 4   ? 58.453 13.905 -12.889 1.00 41.75 ?  2   MET A CE    1 
ATOM   29   N  N     . ASN A 1 5   ? 58.424 12.122 -7.963  1.00 30.34 ?  3   ASN A N     1 
ATOM   30   C  CA    . ASN A 1 5   ? 57.740 11.458 -6.828  1.00 28.27 ?  3   ASN A CA    1 
ATOM   31   C  C     . ASN A 1 5   ? 56.870 10.346 -7.416  1.00 28.25 ?  3   ASN A C     1 
ATOM   32   O  O     . ASN A 1 5   ? 55.856 10.679 -8.084  1.00 26.99 ?  3   ASN A O     1 
ATOM   33   C  CB    . ASN A 1 5   ? 56.950 12.499 -6.036  1.00 27.45 ?  3   ASN A CB    1 
ATOM   34   C  CG    . ASN A 1 5   ? 57.871 13.404 -5.255  1.00 30.01 ?  3   ASN A CG    1 
ATOM   35   O  OD1   . ASN A 1 5   ? 58.494 12.964 -4.295  1.00 29.50 ?  3   ASN A OD1   1 
ATOM   36   N  ND2   . ASN A 1 5   ? 58.041 14.627 -5.725  1.00 32.64 ?  3   ASN A ND2   1 
ATOM   37   N  N     . ASN A 1 6   ? 57.256 9.087  -7.183  1.00 31.56 ?  4   ASN A N     1 
ATOM   38   C  CA    . ASN A 1 6   ? 56.464 7.911  -7.616  1.00 36.55 ?  4   ASN A CA    1 
ATOM   39   C  C     . ASN A 1 6   ? 55.120 7.965  -6.873  1.00 34.20 ?  4   ASN A C     1 
ATOM   40   O  O     . ASN A 1 6   ? 55.129 8.088  -5.625  1.00 32.67 ?  4   ASN A O     1 
ATOM   41   C  CB    . ASN A 1 6   ? 57.235 6.605  -7.381  1.00 42.08 ?  4   ASN A CB    1 
ATOM   42   C  CG    . ASN A 1 6   ? 56.804 5.524  -8.344  1.00 51.87 ?  4   ASN A CG    1 
ATOM   43   O  OD1   . ASN A 1 6   ? 55.615 5.340  -8.577  1.00 56.17 ?  4   ASN A OD1   1 
ATOM   44   N  ND2   . ASN A 1 6   ? 57.760 4.824  -8.930  1.00 61.46 ?  4   ASN A ND2   1 
ATOM   45   N  N     . GLY A 1 7   ? 54.012 7.889  -7.617  1.00 28.72 ?  5   GLY A N     1 
ATOM   46   C  CA    . GLY A 1 7   ? 52.624 7.920  -7.102  1.00 26.25 ?  5   GLY A CA    1 
ATOM   47   C  C     . GLY A 1 7   ? 52.362 9.255  -6.394  1.00 22.43 ?  5   GLY A C     1 
ATOM   48   O  O     . GLY A 1 7   ? 51.797 9.225  -5.294  1.00 23.04 ?  5   GLY A O     1 
ATOM   49   N  N     . HIS A 1 8   ? 52.805 10.385 -6.950  1.00 21.34 ?  6   HIS A N     1 
ATOM   50   C  CA    . HIS A 1 8   ? 52.680 11.694 -6.256  1.00 20.67 ?  6   HIS A CA    1 
ATOM   51   C  C     . HIS A 1 8   ? 51.194 11.976 -6.050  1.00 20.97 ?  6   HIS A C     1 
ATOM   52   O  O     . HIS A 1 8   ? 50.370 11.786 -7.004  1.00 20.83 ?  6   HIS A O     1 
ATOM   53   C  CB    . HIS A 1 8   ? 53.368 12.819 -7.041  1.00 19.93 ?  6   HIS A CB    1 
ATOM   54   C  CG    . HIS A 1 8   ? 53.393 14.108 -6.282  1.00 20.23 ?  6   HIS A CG    1 
ATOM   55   N  ND1   . HIS A 1 8   ? 54.125 14.314 -5.105  1.00 24.35 ?  6   HIS A ND1   1 
ATOM   56   C  CD2   . HIS A 1 8   ? 52.643 15.214 -6.482  1.00 21.07 ?  6   HIS A CD2   1 
ATOM   57   C  CE1   . HIS A 1 8   ? 53.845 15.529 -4.643  1.00 18.11 ?  6   HIS A CE1   1 
ATOM   58   N  NE2   . HIS A 1 8   ? 52.946 16.096 -5.461  1.00 25.57 ?  6   HIS A NE2   1 
ATOM   59   N  N     . GLU A 1 9   ? 50.840 12.483 -4.850  1.00 16.80 ?  7   GLU A N     1 
ATOM   60   C  CA    . GLU A 1 9   ? 49.477 12.830 -4.500  1.00 17.06 ?  7   GLU A CA    1 
ATOM   61   C  C     . GLU A 1 9   ? 49.424 14.309 -4.154  1.00 14.72 ?  7   GLU A C     1 
ATOM   62   O  O     . GLU A 1 9   ? 50.443 14.866 -3.690  1.00 15.90 ?  7   GLU A O     1 
ATOM   63   C  CB    . GLU A 1 9   ? 49.007 11.982 -3.340  1.00 15.97 ?  7   GLU A CB    1 
ATOM   64   C  CG    . GLU A 1 9   ? 48.920 10.515 -3.652  1.00 17.01 ?  7   GLU A CG    1 
ATOM   65   C  CD    . GLU A 1 9   ? 48.406 9.662  -2.490  1.00 19.45 ?  7   GLU A CD    1 
ATOM   66   O  OE1   . GLU A 1 9   ? 48.705 9.976  -1.302  1.00 18.49 ?  7   GLU A OE1   1 
ATOM   67   O  OE2   . GLU A 1 9   ? 47.724 8.617  -2.779  1.00 22.69 ?  7   GLU A OE2   1 
ATOM   68   N  N     . GLU A 1 10  ? 48.214 14.852 -4.351  1.00 15.32 ?  8   GLU A N     1 
ATOM   69   C  CA    . GLU A 1 10  ? 47.825 16.216 -3.964  1.00 16.18 ?  8   GLU A CA    1 
ATOM   70   C  C     . GLU A 1 10  ? 46.447 16.207 -3.306  1.00 14.59 ?  8   GLU A C     1 
ATOM   71   O  O     . GLU A 1 10  ? 45.510 15.562 -3.733  1.00 16.85 ?  8   GLU A O     1 
ATOM   72   C  CB    . GLU A 1 10  ? 47.854 17.129 -5.189  1.00 23.84 ?  8   GLU A CB    1 
ATOM   73   C  CG    . GLU A 1 10  ? 47.496 18.576 -4.920  1.00 34.05 ?  8   GLU A CG    1 
ATOM   74   C  CD    . GLU A 1 10  ? 47.277 19.444 -6.166  1.00 46.13 ?  8   GLU A CD    1 
ATOM   75   O  OE1   . GLU A 1 10  ? 46.839 20.605 -5.978  1.00 52.78 ?  8   GLU A OE1   1 
ATOM   76   O  OE2   . GLU A 1 10  ? 47.574 18.978 -7.318  1.00 50.87 ?  8   GLU A OE2   1 
ATOM   77   N  N     . TYR A 1 11  ? 46.358 16.889 -2.173  1.00 11.52 ?  9   TYR A N     1 
ATOM   78   C  CA    . TYR A 1 11  ? 45.154 17.032 -1.359  1.00 10.25 ?  9   TYR A CA    1 
ATOM   79   C  C     . TYR A 1 11  ? 44.830 18.498 -1.057  1.00 9.92  ?  9   TYR A C     1 
ATOM   80   O  O     . TYR A 1 11  ? 45.734 19.320 -1.057  1.00 12.25 ?  9   TYR A O     1 
ATOM   81   C  CB    . TYR A 1 11  ? 45.356 16.316 -0.002  1.00 10.28 ?  9   TYR A CB    1 
ATOM   82   C  CG    . TYR A 1 11  ? 45.507 14.823 -0.148  1.00 10.74 ?  9   TYR A CG    1 
ATOM   83   C  CD1   . TYR A 1 11  ? 46.749 14.271 -0.361  1.00 9.92  ?  9   TYR A CD1   1 
ATOM   84   C  CD2   . TYR A 1 11  ? 44.427 13.990 -0.012  1.00 10.91 ?  9   TYR A CD2   1 
ATOM   85   C  CE1   . TYR A 1 11  ? 46.911 12.904 -0.508  1.00 10.81 ?  9   TYR A CE1   1 
ATOM   86   C  CE2   . TYR A 1 11  ? 44.557 12.623 -0.147  1.00 11.45 ?  9   TYR A CE2   1 
ATOM   87   C  CZ    . TYR A 1 11  ? 45.796 12.103 -0.412  1.00 12.52 ?  9   TYR A CZ    1 
ATOM   88   O  OH    . TYR A 1 11  ? 46.009 10.733 -0.482  1.00 16.02 ?  9   TYR A OH    1 
ATOM   89   N  N     . ASP A 1 12  ? 43.591 18.754 -0.782  1.00 10.79 ?  10  ASP A N     1 
ATOM   90   C  CA    . ASP A 1 12  ? 43.213 20.086 -0.294  1.00 10.27 ?  10  ASP A CA    1 
ATOM   91   C  C     . ASP A 1 12  ? 43.896 20.343 1.057   1.00 10.21 ?  10  ASP A C     1 
ATOM   92   O  O     . ASP A 1 12  ? 44.432 21.453 1.294   1.00 10.16 ?  10  ASP A O     1 
ATOM   93   C  CB    . ASP A 1 12  ? 41.737 20.245 -0.105  1.00 11.30 ?  10  ASP A CB    1 
ATOM   94   C  CG    . ASP A 1 12  ? 40.941 20.246 -1.411  1.00 15.08 ?  10  ASP A CG    1 
ATOM   95   O  OD1   . ASP A 1 12  ? 41.515 20.707 -2.413  1.00 17.40 ?  10  ASP A OD1   1 
ATOM   96   O  OD2   . ASP A 1 12  ? 39.779 19.792 -1.355  1.00 16.74 ?  10  ASP A OD2   1 
ATOM   97   N  N     . VAL A 1 13  ? 43.846 19.376 1.954   1.00 9.68  ?  11  VAL A N     1 
ATOM   98   C  CA    . VAL A 1 13  ? 44.326 19.519 3.340   1.00 8.93  ?  11  VAL A CA    1 
ATOM   99   C  C     . VAL A 1 13  ? 45.115 18.290 3.713   1.00 8.12  ?  11  VAL A C     1 
ATOM   100  O  O     . VAL A 1 13  ? 44.689 17.144 3.444   1.00 8.94  ?  11  VAL A O     1 
ATOM   101  C  CB    . VAL A 1 13  ? 43.195 19.709 4.338   1.00 8.91  ?  11  VAL A CB    1 
ATOM   102  C  CG1   . VAL A 1 13  ? 43.727 19.929 5.743   1.00 10.92 ?  11  VAL A CG1   1 
ATOM   103  C  CG2   . VAL A 1 13  ? 42.273 20.842 3.909   1.00 9.77  ?  11  VAL A CG2   1 
ATOM   104  N  N     . ILE A 1 14  ? 46.260 18.516 4.338   1.00 8.32  ?  12  ILE A N     1 
ATOM   105  C  CA    . ILE A 1 14  ? 47.041 17.473 5.027   1.00 8.03  ?  12  ILE A CA    1 
ATOM   106  C  C     . ILE A 1 14  ? 46.918 17.746 6.515   1.00 8.15  ?  12  ILE A C     1 
ATOM   107  O  O     . ILE A 1 14  ? 47.178 18.882 6.945   1.00 8.61  ?  12  ILE A O     1 
ATOM   108  C  CB    . ILE A 1 14  ? 48.487 17.500 4.616   1.00 8.69  ?  12  ILE A CB    1 
ATOM   109  C  CG1   . ILE A 1 14  ? 48.663 17.229 3.121   1.00 9.13  ?  12  ILE A CG1   1 
ATOM   110  C  CG2   . ILE A 1 14  ? 49.262 16.527 5.490   1.00 9.91  ?  12  ILE A CG2   1 
ATOM   111  C  CD1   . ILE A 1 14  ? 50.020 17.566 2.602   1.00 10.00 ?  12  ILE A CD1   1 
ATOM   112  N  N     . VAL A 1 15  ? 46.490 16.770 7.298   1.00 7.00  ?  13  VAL A N     1 
ATOM   113  C  CA    . VAL A 1 15  ? 46.416 16.874 8.774   1.00 6.92  ?  13  VAL A CA    1 
ATOM   114  C  C     . VAL A 1 15  ? 47.512 15.985 9.325   1.00 7.21  ?  13  VAL A C     1 
ATOM   115  O  O     . VAL A 1 15  ? 47.544 14.768 8.952   1.00 7.81  ?  13  VAL A O     1 
ATOM   116  C  CB    . VAL A 1 15  ? 45.051 16.501 9.311   1.00 7.33  ?  13  VAL A CB    1 
ATOM   117  C  CG1   . VAL A 1 15  ? 45.058 16.567 10.833  1.00 8.13  ?  13  VAL A CG1   1 
ATOM   118  C  CG2   . VAL A 1 15  ? 43.989 17.416 8.716   1.00 8.01  ?  13  VAL A CG2   1 
ATOM   119  N  N     . VAL A 1 16  ? 48.372 16.500 10.171  1.00 6.63  ?  14  VAL A N     1 
ATOM   120  C  CA    . VAL A 1 16  ? 49.477 15.727 10.768  1.00 6.98  ?  14  VAL A CA    1 
ATOM   121  C  C     . VAL A 1 16  ? 49.069 15.451 12.201  1.00 6.75  ?  14  VAL A C     1 
ATOM   122  O  O     . VAL A 1 16  ? 49.029 16.375 13.044  1.00 7.32  ?  14  VAL A O     1 
ATOM   123  C  CB    . VAL A 1 16  ? 50.787 16.497 10.670  1.00 7.52  ?  14  VAL A CB    1 
ATOM   124  C  CG1   . VAL A 1 16  ? 51.883 15.628 11.208  1.00 8.54  ?  14  VAL A CG1   1 
ATOM   125  C  CG2   . VAL A 1 16  ? 51.067 16.907 9.227   1.00 8.33  ?  14  VAL A CG2   1 
ATOM   126  N  N     . GLY A 1 17  ? 48.784 14.197 12.479  1.00 6.82  ?  15  GLY A N     1 
ATOM   127  C  CA    . GLY A 1 17  ? 48.355 13.796 13.819  1.00 7.19  ?  15  GLY A CA    1 
ATOM   128  C  C     . GLY A 1 17  ? 46.898 13.414 13.841  1.00 7.52  ?  15  GLY A C     1 
ATOM   129  O  O     . GLY A 1 17  ? 46.056 14.142 13.306  1.00 8.25  ?  15  GLY A O     1 
ATOM   130  N  N     . GLY A 1 18  ? 46.532 12.285 14.458  1.00 7.17  ?  16  GLY A N     1 
ATOM   131  C  CA    . GLY A 1 18  ? 45.179 11.768 14.515  1.00 7.54  ?  16  GLY A CA    1 
ATOM   132  C  C     . GLY A 1 18  ? 44.584 11.650 15.879  1.00 7.33  ?  16  GLY A C     1 
ATOM   133  O  O     . GLY A 1 18  ? 43.676 10.836 16.041  1.00 8.19  ?  16  GLY A O     1 
ATOM   134  N  N     . GLY A 1 19  ? 45.031 12.420 16.866  1.00 7.77  ?  17  GLY A N     1 
ATOM   135  C  CA    . GLY A 1 19  ? 44.380 12.566 18.159  1.00 6.76  ?  17  GLY A CA    1 
ATOM   136  C  C     . GLY A 1 19  ? 43.106 13.384 17.946  1.00 7.19  ?  17  GLY A C     1 
ATOM   137  O  O     . GLY A 1 19  ? 42.742 13.697 16.809  1.00 7.64  ?  17  GLY A O     1 
ATOM   138  N  N     . PRO A 1 20  ? 42.420 13.760 19.007  1.00 6.79  ?  18  PRO A N     1 
ATOM   139  C  CA    . PRO A 1 20  ? 41.114 14.435 18.884  1.00 7.76  ?  18  PRO A CA    1 
ATOM   140  C  C     . PRO A 1 20  ? 41.177 15.712 18.067  1.00 8.30  ?  18  PRO A C     1 
ATOM   141  O  O     . PRO A 1 20  ? 40.224 15.998 17.359  1.00 8.79  ?  18  PRO A O     1 
ATOM   142  C  CB    . PRO A 1 20  ? 40.725 14.687 20.354  1.00 8.24  ?  18  PRO A CB    1 
ATOM   143  C  CG    . PRO A 1 20  ? 41.448 13.582 21.092  1.00 9.54  ?  18  PRO A CG    1 
ATOM   144  C  CD    . PRO A 1 20  ? 42.767 13.436 20.403  1.00 8.58  ?  18  PRO A CD    1 
ATOM   145  N  N     . ALA A 1 21  ? 42.263 16.455 18.127  1.00 8.21  ?  19  ALA A N     1 
ATOM   146  C  CA    . ALA A 1 21  ? 42.311 17.685 17.305  1.00 7.47  ?  19  ALA A CA    1 
ATOM   147  C  C     . ALA A 1 21  ? 42.364 17.350 15.844  1.00 7.84  ?  19  ALA A C     1 
ATOM   148  O  O     . ALA A 1 21  ? 41.632 17.917 15.052  1.00 8.79  ?  19  ALA A O     1 
ATOM   149  C  CB    . ALA A 1 21  ? 43.514 18.545 17.643  1.00 7.89  ?  19  ALA A CB    1 
ATOM   150  N  N     . GLY A 1 22  ? 43.264 16.457 15.445  1.00 6.96  ?  20  GLY A N     1 
ATOM   151  C  CA    . GLY A 1 22  ? 43.461 16.172 14.024  1.00 7.04  ?  20  GLY A CA    1 
ATOM   152  C  C     . GLY A 1 22  ? 42.287 15.412 13.466  1.00 8.42  ?  20  GLY A C     1 
ATOM   153  O  O     . GLY A 1 22  ? 41.865 15.693 12.313  1.00 7.93  ?  20  GLY A O     1 
ATOM   154  N  N     . SER A 1 23  ? 41.800 14.420 14.175  1.00 7.81  ?  21  SER A N     1 
ATOM   155  C  CA    . SER A 1 23  ? 40.681 13.611 13.637  1.00 8.38  ?  21  SER A CA    1 
ATOM   156  C  C     . SER A 1 23  ? 39.426 14.468 13.525  1.00 8.51  ?  21  SER A C     1 
ATOM   157  O  O     . SER A 1 23  ? 38.672 14.317 12.527  1.00 8.77  ?  21  SER A O     1 
ATOM   158  C  CB    . SER A 1 23  ? 40.424 12.392 14.455  1.00 8.99  ?  21  SER A CB    1 
ATOM   159  O  OG    . SER A 1 23  ? 40.026 12.758 15.753  1.00 9.61  ?  21  SER A OG    1 
ATOM   160  N  N     . SER A 1 24  ? 39.144 15.323 14.476  1.00 7.92  ?  22  SER A N     1 
ATOM   161  C  CA    . SER A 1 24  ? 37.961 16.194 14.403  1.00 8.89  ?  22  SER A CA    1 
ATOM   162  C  C     . SER A 1 24  ? 38.150 17.173 13.241  1.00 8.50  ?  22  SER A C     1 
ATOM   163  O  O     . SER A 1 24  ? 37.209 17.356 12.453  1.00 9.48  ?  22  SER A O     1 
ATOM   164  C  CB    . SER A 1 24  ? 37.616 16.833 15.712  1.00 10.12 ?  22  SER A CB    1 
ATOM   165  O  OG    . SER A 1 24  ? 38.600 17.787 16.092  1.00 12.46 ?  22  SER A OG    1 
ATOM   166  N  N     . ALA A 1 25  ? 39.307 17.808 13.120  1.00 8.62  ?  23  ALA A N     1 
ATOM   167  C  CA    . ALA A 1 25  ? 39.530 18.774 12.008  1.00 9.01  ?  23  ALA A CA    1 
ATOM   168  C  C     . ALA A 1 25  ? 39.357 18.059 10.669  1.00 9.57  ?  23  ALA A C     1 
ATOM   169  O  O     . ALA A 1 25  ? 38.666 18.541 9.761   1.00 9.23  ?  23  ALA A O     1 
ATOM   170  C  CB    . ALA A 1 25  ? 40.908 19.313 12.100  1.00 8.64  ?  23  ALA A CB    1 
ATOM   171  N  N     . ALA A 1 26  ? 39.970 16.881 10.539  1.00 8.26  ?  24  ALA A N     1 
ATOM   172  C  CA    . ALA A 1 26  ? 39.988 16.166 9.259   1.00 8.50  ?  24  ALA A CA    1 
ATOM   173  C  C     . ALA A 1 26  ? 38.570 15.714 8.913   1.00 9.37  ?  24  ALA A C     1 
ATOM   174  O  O     . ALA A 1 26  ? 38.155 15.858 7.767   1.00 9.13  ?  24  ALA A O     1 
ATOM   175  C  CB    . ALA A 1 26  ? 40.933 15.006 9.335   1.00 8.51  ?  24  ALA A CB    1 
ATOM   176  N  N     . GLY A 1 27  ? 37.873 15.118 9.848   1.00 8.49  ?  25  GLY A N     1 
ATOM   177  C  CA    . GLY A 1 27  ? 36.524 14.614 9.571   1.00 9.43  ?  25  GLY A CA    1 
ATOM   178  C  C     . GLY A 1 27  ? 35.622 15.738 9.197   1.00 10.07 ?  25  GLY A C     1 
ATOM   179  O  O     . GLY A 1 27  ? 34.843 15.564 8.251   1.00 11.93 ?  25  GLY A O     1 
ATOM   180  N  N     . LEU A 1 28  ? 35.694 16.874 9.873   1.00 9.87  ?  26  LEU A N     1 
ATOM   181  C  CA    . LEU A 1 28  ? 34.771 17.987 9.547   1.00 10.42 ?  26  LEU A CA    1 
ATOM   182  C  C     . LEU A 1 28  ? 35.165 18.555 8.190   1.00 11.35 ?  26  LEU A C     1 
ATOM   183  O  O     . LEU A 1 28  ? 34.230 18.970 7.441   1.00 12.63 ?  26  LEU A O     1 
ATOM   184  C  CB    . LEU A 1 28  ? 34.780 19.018 10.649  1.00 11.37 ?  26  LEU A CB    1 
ATOM   185  C  CG    . LEU A 1 28  ? 34.226 18.521 11.961  1.00 12.25 ?  26  LEU A CG    1 
ATOM   186  C  CD1   . LEU A 1 28  ? 34.462 19.479 13.100  1.00 12.31 ?  26  LEU A CD1   1 
ATOM   187  C  CD2   . LEU A 1 28  ? 32.735 18.185 11.850  1.00 13.19 ?  26  LEU A CD2   1 
ATOM   188  N  N     . LEU A 1 29  ? 36.422 18.633 7.807   1.00 9.72  ?  27  LEU A N     1 
ATOM   189  C  CA    . LEU A 1 29  ? 36.775 19.115 6.480   1.00 9.46  ?  27  LEU A CA    1 
ATOM   190  C  C     . LEU A 1 29  ? 36.296 18.134 5.427   1.00 11.85 ?  27  LEU A C     1 
ATOM   191  O  O     . LEU A 1 29  ? 35.824 18.572 4.352   1.00 11.59 ?  27  LEU A O     1 
ATOM   192  C  CB    . LEU A 1 29  ? 38.260 19.316 6.362   1.00 9.55  ?  27  LEU A CB    1 
ATOM   193  C  CG    . LEU A 1 29  ? 38.712 20.600 7.043   1.00 10.02 ?  27  LEU A CG    1 
ATOM   194  C  CD1   . LEU A 1 29  ? 40.164 20.511 7.440   1.00 11.17 ?  27  LEU A CD1   1 
ATOM   195  C  CD2   . LEU A 1 29  ? 38.456 21.825 6.162   1.00 11.02 ?  27  LEU A CD2   1 
ATOM   196  N  N     . ALA A 1 30  ? 36.376 16.833 5.645   1.00 10.90 ?  28  ALA A N     1 
ATOM   197  C  CA    . ALA A 1 30  ? 35.870 15.848 4.673   1.00 12.74 ?  28  ALA A CA    1 
ATOM   198  C  C     . ALA A 1 30  ? 34.359 15.974 4.569   1.00 13.31 ?  28  ALA A C     1 
ATOM   199  O  O     . ALA A 1 30  ? 33.848 15.861 3.426   1.00 14.41 ?  28  ALA A O     1 
ATOM   200  C  CB    . ALA A 1 30  ? 36.304 14.436 5.079   1.00 13.49 ?  28  ALA A CB    1 
ATOM   201  N  N     . LEU A 1 31  ? 33.667 16.279 5.618   1.00 13.89 ?  29  LEU A N     1 
ATOM   202  C  CA    . LEU A 1 31  ? 32.230 16.433 5.574   1.00 15.78 ?  29  LEU A CA    1 
ATOM   203  C  C     . LEU A 1 31  ? 31.861 17.621 4.681   1.00 19.09 ?  29  LEU A C     1 
ATOM   204  O  O     . LEU A 1 31  ? 30.834 17.655 4.076   1.00 22.10 ?  29  LEU A O     1 
ATOM   205  C  CB    . LEU A 1 31  ? 31.734 16.612 7.005   1.00 19.44 ?  29  LEU A CB    1 
ATOM   206  C  CG    . LEU A 1 31  ? 30.311 16.499 7.451   1.00 24.03 ?  29  LEU A CG    1 
ATOM   207  C  CD1   . LEU A 1 31  ? 29.639 15.232 6.952   1.00 21.42 ?  29  LEU A CD1   1 
ATOM   208  C  CD2   . LEU A 1 31  ? 30.252 16.572 8.957   1.00 27.01 ?  29  LEU A CD2   1 
ATOM   209  N  N     . ASN A 1 32  ? 32.725 18.607 4.628   1.00 17.44 ?  30  ASN A N     1 
ATOM   210  C  CA    . ASN A 1 32  ? 32.540 19.769 3.804   1.00 19.53 ?  30  ASN A CA    1 
ATOM   211  C  C     . ASN A 1 32  ? 32.967 19.577 2.360   1.00 16.62 ?  30  ASN A C     1 
ATOM   212  O  O     . ASN A 1 32  ? 33.063 20.521 1.640   1.00 22.38 ?  30  ASN A O     1 
ATOM   213  C  CB    . ASN A 1 32  ? 33.275 20.959 4.377   1.00 23.57 ?  30  ASN A CB    1 
ATOM   214  C  CG    . ASN A 1 32  ? 32.452 21.695 5.384   1.00 34.66 ?  30  ASN A CG    1 
ATOM   215  O  OD1   . ASN A 1 32  ? 32.460 22.874 5.464   1.00 34.63 ?  30  ASN A OD1   1 
ATOM   216  N  ND2   . ASN A 1 32  ? 31.743 20.962 6.145   1.00 35.82 ?  30  ASN A ND2   1 
ATOM   217  N  N     . GLY A 1 33  ? 33.370 18.379 2.014   1.00 15.44 ?  31  GLY A N     1 
ATOM   218  C  CA    . GLY A 1 33  ? 33.630 17.955 0.620   1.00 15.72 ?  31  GLY A CA    1 
ATOM   219  C  C     . GLY A 1 33  ? 35.081 18.125 0.195   1.00 16.87 ?  31  GLY A C     1 
ATOM   220  O  O     . GLY A 1 33  ? 35.436 17.860 -0.943  1.00 18.48 ?  31  GLY A O     1 
ATOM   221  N  N     . HIS A 1 34  ? 35.992 18.418 1.118   1.00 13.57 ?  32  HIS A N     1 
ATOM   222  C  CA    . HIS A 1 34  ? 37.403 18.556 0.732   1.00 12.60 ?  32  HIS A CA    1 
ATOM   223  C  C     . HIS A 1 34  ? 38.157 17.228 0.724   1.00 11.63 ?  32  HIS A C     1 
ATOM   224  O  O     . HIS A 1 34  ? 37.706 16.294 1.422   1.00 13.51 ?  32  HIS A O     1 
ATOM   225  C  CB    . HIS A 1 34  ? 38.109 19.520 1.703   1.00 13.99 ?  32  HIS A CB    1 
ATOM   226  C  CG    . HIS A 1 34  ? 37.522 20.884 1.709   1.00 13.50 ?  32  HIS A CG    1 
ATOM   227  N  ND1   . HIS A 1 34  ? 37.600 21.727 0.599   1.00 16.24 ?  32  HIS A ND1   1 
ATOM   228  C  CD2   . HIS A 1 34  ? 36.794 21.535 2.625   1.00 14.02 ?  32  HIS A CD2   1 
ATOM   229  C  CE1   . HIS A 1 34  ? 36.955 22.848 0.915   1.00 16.01 ?  32  HIS A CE1   1 
ATOM   230  N  NE2   . HIS A 1 34  ? 36.412 22.752 2.093   1.00 14.81 ?  32  HIS A NE2   1 
ATOM   231  N  N     . SER A 1 35  ? 39.232 17.148 -0.008  1.00 12.31 ?  33  SER A N     1 
ATOM   232  C  CA    . SER A 1 35  ? 40.139 15.988 -0.082  1.00 11.28 ?  33  SER A CA    1 
ATOM   233  C  C     . SER A 1 35  ? 41.137 16.172 1.054   1.00 11.54 ?  33  SER A C     1 
ATOM   234  O  O     . SER A 1 35  ? 41.869 17.152 1.104   1.00 12.49 ?  33  SER A O     1 
ATOM   235  C  CB    . SER A 1 35  ? 40.827 15.839 -1.410  1.00 13.82 ?  33  SER A CB    1 
ATOM   236  O  OG    . SER A 1 35  ? 41.557 16.992 -1.782  1.00 17.50 ?  33  SER A OG    1 
ATOM   237  N  N     . VAL A 1 36  ? 41.126 15.232 1.982   1.00 10.09 ?  34  VAL A N     1 
ATOM   238  C  CA    . VAL A 1 36  ? 41.910 15.330 3.227   1.00 9.05  ?  34  VAL A CA    1 
ATOM   239  C  C     . VAL A 1 36  ? 42.773 14.087 3.380   1.00 9.14  ?  34  VAL A C     1 
ATOM   240  O  O     . VAL A 1 36  ? 42.264 12.964 3.281   1.00 9.96  ?  34  VAL A O     1 
ATOM   241  C  CB    . VAL A 1 36  ? 41.051 15.528 4.472   1.00 9.52  ?  34  VAL A CB    1 
ATOM   242  C  CG1   . VAL A 1 36  ? 41.874 15.776 5.714   1.00 9.99  ?  34  VAL A CG1   1 
ATOM   243  C  CG2   . VAL A 1 36  ? 40.067 16.670 4.207   1.00 10.56 ?  34  VAL A CG2   1 
ATOM   244  N  N     . LEU A 1 37  ? 44.046 14.290 3.628   1.00 8.94  ?  35  LEU A N     1 
ATOM   245  C  CA    . LEU A 1 37  ? 45.044 13.287 4.014   1.00 8.37  ?  35  LEU A CA    1 
ATOM   246  C  C     . LEU A 1 37  ? 45.341 13.468 5.483   1.00 9.25  ?  35  LEU A C     1 
ATOM   247  O  O     . LEU A 1 37  ? 45.632 14.602 5.851   1.00 10.56 ?  35  LEU A O     1 
ATOM   248  C  CB    . LEU A 1 37  ? 46.322 13.435 3.226   1.00 9.56  ?  35  LEU A CB    1 
ATOM   249  C  CG    . LEU A 1 37  ? 47.411 12.421 3.539   1.00 9.88  ?  35  LEU A CG    1 
ATOM   250  C  CD1   . LEU A 1 37  ? 47.001 11.005 3.157   1.00 11.52 ?  35  LEU A CD1   1 
ATOM   251  C  CD2   . LEU A 1 37  ? 48.691 12.839 2.846   1.00 11.50 ?  35  LEU A CD2   1 
ATOM   252  N  N     . LEU A 1 38  ? 45.298 12.455 6.290   1.00 8.12  ?  36  LEU A N     1 
ATOM   253  C  CA    . LEU A 1 38  ? 45.704 12.529 7.708   1.00 7.99  ?  36  LEU A CA    1 
ATOM   254  C  C     . LEU A 1 38  ? 46.842 11.565 7.885   1.00 7.93  ?  36  LEU A C     1 
ATOM   255  O  O     . LEU A 1 38  ? 46.692 10.352 7.544   1.00 8.38  ?  36  LEU A O     1 
ATOM   256  C  CB    . LEU A 1 38  ? 44.558 12.262 8.653   1.00 7.34  ?  36  LEU A CB    1 
ATOM   257  C  CG    . LEU A 1 38  ? 44.856 12.502 10.154  1.00 8.07  ?  36  LEU A CG    1 
ATOM   258  C  CD1   . LEU A 1 38  ? 43.620 12.792 10.927  1.00 8.92  ?  36  LEU A CD1   1 
ATOM   259  C  CD2   . LEU A 1 38  ? 45.594 11.337 10.782  1.00 8.27  ?  36  LEU A CD2   1 
ATOM   260  N  N     . LEU A 1 39  ? 47.972 12.007 8.403   1.00 7.50  ?  37  LEU A N     1 
ATOM   261  C  CA    . LEU A 1 39  ? 49.170 11.203 8.662   1.00 7.34  ?  37  LEU A CA    1 
ATOM   262  C  C     . LEU A 1 39  ? 49.284 11.001 10.153  1.00 7.76  ?  37  LEU A C     1 
ATOM   263  O  O     . LEU A 1 39  ? 49.441 11.991 10.880  1.00 8.71  ?  37  LEU A O     1 
ATOM   264  C  CB    . LEU A 1 39  ? 50.386 11.926 8.065   1.00 8.72  ?  37  LEU A CB    1 
ATOM   265  C  CG    . LEU A 1 39  ? 50.292 12.209 6.556   1.00 10.37 ?  37  LEU A CG    1 
ATOM   266  C  CD1   . LEU A 1 39  ? 51.384 13.145 6.090   1.00 13.02 ?  37  LEU A CD1   1 
ATOM   267  C  CD2   . LEU A 1 39  ? 50.333 10.958 5.735   1.00 12.40 ?  37  LEU A CD2   1 
ATOM   268  N  N     . GLU A 1 40  ? 49.297 9.774  10.608  1.00 7.41  ?  38  GLU A N     1 
ATOM   269  C  CA    . GLU A 1 40  ? 49.414 9.424  12.032  1.00 6.80  ?  38  GLU A CA    1 
ATOM   270  C  C     . GLU A 1 40  ? 50.559 8.451  12.181  1.00 7.76  ?  38  GLU A C     1 
ATOM   271  O  O     . GLU A 1 40  ? 50.551 7.373  11.516  1.00 8.36  ?  38  GLU A O     1 
ATOM   272  C  CB    . GLU A 1 40  ? 48.094 8.869  12.524  1.00 8.31  ?  38  GLU A CB    1 
ATOM   273  C  CG    . GLU A 1 40  ? 48.191 8.208  13.889  1.00 8.36  ?  38  GLU A CG    1 
ATOM   274  C  CD    . GLU A 1 40  ? 48.738 9.032  15.036  1.00 9.03  ?  38  GLU A CD    1 
ATOM   275  O  OE1   . GLU A 1 40  ? 48.185 10.112 15.332  1.00 9.10  ?  38  GLU A OE1   1 
ATOM   276  O  OE2   . GLU A 1 40  ? 49.745 8.614  15.643  1.00 8.34  ?  38  GLU A OE2   1 
ATOM   277  N  N     . ARG A 1 41  ? 51.503 8.731  13.047  1.00 7.86  ?  39  ARG A N     1 
ATOM   278  C  CA    . ARG A 1 41  ? 52.709 7.898  13.180  1.00 9.30  ?  39  ARG A CA    1 
ATOM   279  C  C     . ARG A 1 41  ? 52.396 6.568  13.846  1.00 9.10  ?  39  ARG A C     1 
ATOM   280  O  O     . ARG A 1 41  ? 53.152 5.583  13.585  1.00 10.63 ?  39  ARG A O     1 
ATOM   281  C  CB    . ARG A 1 41  ? 53.782 8.665  13.918  1.00 9.94  ?  39  ARG A CB    1 
ATOM   282  C  CG    . ARG A 1 41  ? 53.468 8.986  15.343  1.00 11.57 ?  39  ARG A CG    1 
ATOM   283  C  CD    . ARG A 1 41  ? 54.534 9.844  16.070  1.00 13.54 ?  39  ARG A CD    1 
ATOM   284  N  NE    . ARG A 1 41  ? 54.069 9.930  17.445  1.00 15.67 ?  39  ARG A NE    1 
ATOM   285  C  CZ    . ARG A 1 41  ? 54.807 10.304 18.475  1.00 20.18 ?  39  ARG A CZ    1 
ATOM   286  N  NH1   . ARG A 1 41  ? 56.040 10.683 18.271  1.00 21.10 ?  39  ARG A NH1   1 
ATOM   287  N  NH2   . ARG A 1 41  ? 54.286 10.248 19.666  1.00 21.72 ?  39  ARG A NH2   1 
ATOM   288  N  N     . ASP A 1 42  ? 51.398 6.468  14.707  1.00 9.06  ?  40  ASP A N     1 
ATOM   289  C  CA    . ASP A 1 42  ? 51.109 5.264  15.500  1.00 10.57 ?  40  ASP A CA    1 
ATOM   290  C  C     . ASP A 1 42  ? 50.118 4.400  14.768  1.00 12.96 ?  40  ASP A C     1 
ATOM   291  O  O     . ASP A 1 42  ? 49.739 4.661  13.629  1.00 15.82 ?  40  ASP A O     1 
ATOM   292  C  CB    . ASP A 1 42  ? 50.631 5.693  16.876  1.00 12.58 ?  40  ASP A CB    1 
ATOM   293  C  CG    . ASP A 1 42  ? 51.684 5.852  17.908  1.00 24.46 ?  40  ASP A CG    1 
ATOM   294  O  OD1   . ASP A 1 42  ? 52.865 5.976  17.522  1.00 26.40 ?  40  ASP A OD1   1 
ATOM   295  O  OD2   . ASP A 1 42  ? 51.288 5.725  19.119  1.00 22.49 ?  40  ASP A OD2   1 
ATOM   296  N  N     . LYS A 1 43  ? 49.769 3.293  15.356  1.00 11.91 ?  41  LYS A N     1 
ATOM   297  C  CA    . LYS A 1 43  ? 48.682 2.383  15.019  1.00 10.39 ?  41  LYS A CA    1 
ATOM   298  C  C     . LYS A 1 43  ? 47.591 2.531  16.036  1.00 8.59  ?  41  LYS A C     1 
ATOM   299  O  O     . LYS A 1 43  ? 47.866 2.344  17.219  1.00 11.38 ?  41  LYS A O     1 
ATOM   300  C  CB    . LYS A 1 43  ? 49.137 0.936  14.982  1.00 10.06 ?  41  LYS A CB    1 
ATOM   301  C  CG    . LYS A 1 43  ? 48.042 -0.023 14.586  1.00 10.29 ?  41  LYS A CG    1 
ATOM   302  C  CD    . LYS A 1 43  ? 47.488 0.245  13.213  1.00 9.71  ?  41  LYS A CD    1 
ATOM   303  C  CE    . LYS A 1 43  ? 46.539 -0.856 12.750  1.00 12.11 ?  41  LYS A CE    1 
ATOM   304  N  NZ    . LYS A 1 43  ? 46.043 -0.524 11.388  1.00 12.43 ?  41  LYS A NZ    1 
ATOM   305  N  N     . PHE A 1 44  ? 46.392 2.872  15.621  1.00 8.29  ?  42  PHE A N     1 
ATOM   306  C  CA    . PHE A 1 44  ? 45.276 2.980  16.577  1.00 8.89  ?  42  PHE A CA    1 
ATOM   307  C  C     . PHE A 1 44  ? 44.541 1.668  16.733  1.00 9.92  ?  42  PHE A C     1 
ATOM   308  O  O     . PHE A 1 44  ? 44.418 0.897  15.770  1.00 10.64 ?  42  PHE A O     1 
ATOM   309  C  CB    . PHE A 1 44  ? 44.278 4.070  16.148  1.00 8.54  ?  42  PHE A CB    1 
ATOM   310  C  CG    . PHE A 1 44  ? 44.694 5.489  16.444  1.00 7.15  ?  42  PHE A CG    1 
ATOM   311  C  CD1   . PHE A 1 44  ? 46.015 5.893  16.556  1.00 7.91  ?  42  PHE A CD1   1 
ATOM   312  C  CD2   . PHE A 1 44  ? 43.727 6.447  16.605  1.00 8.34  ?  42  PHE A CD2   1 
ATOM   313  C  CE1   . PHE A 1 44  ? 46.323 7.227  16.870  1.00 7.86  ?  42  PHE A CE1   1 
ATOM   314  C  CE2   . PHE A 1 44  ? 44.022 7.757  16.891  1.00 7.82  ?  42  PHE A CE2   1 
ATOM   315  C  CZ    . PHE A 1 44  ? 45.341 8.146  17.002  1.00 7.49  ?  42  PHE A CZ    1 
ATOM   316  N  N     . PRO A 1 45  ? 43.968 1.372  17.899  1.00 8.52  ?  43  PRO A N     1 
ATOM   317  C  CA    . PRO A 1 45  ? 44.006 2.214  19.088  1.00 8.83  ?  43  PRO A CA    1 
ATOM   318  C  C     . PRO A 1 45  ? 45.357 2.209  19.767  1.00 9.16  ?  43  PRO A C     1 
ATOM   319  O  O     . PRO A 1 45  ? 46.030 1.177  19.840  1.00 11.03 ?  43  PRO A O     1 
ATOM   320  C  CB    . PRO A 1 45  ? 42.987 1.597  20.025  1.00 9.73  ?  43  PRO A CB    1 
ATOM   321  C  CG    . PRO A 1 45  ? 42.258 0.584  19.214  1.00 12.25 ?  43  PRO A CG    1 
ATOM   322  C  CD    . PRO A 1 45  ? 43.117 0.190  18.068  1.00 9.79  ?  43  PRO A CD    1 
ATOM   323  N  N     . ARG A 1 46  ? 45.744 3.345  20.362  1.00 8.29  ?  44  ARG A N     1 
ATOM   324  C  CA    . ARG A 1 46  ? 47.036 3.547  21.042  1.00 8.79  ?  44  ARG A CA    1 
ATOM   325  C  C     . ARG A 1 46  ? 46.798 4.296  22.358  1.00 8.44  ?  44  ARG A C     1 
ATOM   326  O  O     . ARG A 1 46  ? 45.965 5.227  22.454  1.00 8.49  ?  44  ARG A O     1 
ATOM   327  C  CB    . ARG A 1 46  ? 48.056 4.225  20.148  1.00 9.25  ?  44  ARG A CB    1 
ATOM   328  C  CG    . ARG A 1 46  ? 47.694 5.623  19.702  1.00 9.38  ?  44  ARG A CG    1 
ATOM   329  C  CD    . ARG A 1 46  ? 48.206 6.732  20.605  1.00 9.79  ?  44  ARG A CD    1 
ATOM   330  N  NE    . ARG A 1 46  ? 47.818 8.058  20.196  1.00 9.33  ?  44  ARG A NE    1 
ATOM   331  C  CZ    . ARG A 1 46  ? 46.642 8.600  20.461  1.00 8.42  ?  44  ARG A CZ    1 
ATOM   332  N  NH1   . ARG A 1 46  ? 45.747 7.953  21.206  1.00 9.02  ?  44  ARG A NH1   1 
ATOM   333  N  NH2   . ARG A 1 46  ? 46.385 9.834  20.054  1.00 8.98  ?  44  ARG A NH2   1 
ATOM   334  N  N     . TYR A 1 47  ? 47.565 3.921  23.392  1.00 8.63  ?  45  TYR A N     1 
ATOM   335  C  CA    . TYR A 1 47  ? 47.444 4.484  24.730  1.00 7.88  ?  45  TYR A CA    1 
ATOM   336  C  C     . TYR A 1 47  ? 47.652 5.993  24.681  1.00 8.09  ?  45  TYR A C     1 
ATOM   337  O  O     . TYR A 1 47  ? 48.567 6.474  24.031  1.00 8.70  ?  45  TYR A O     1 
ATOM   338  C  CB    . TYR A 1 47  ? 48.440 3.828  25.667  1.00 7.36  ?  45  TYR A CB    1 
ATOM   339  C  CG    . TYR A 1 47  ? 48.356 4.449  27.050  1.00 7.76  ?  45  TYR A CG    1 
ATOM   340  C  CD1   . TYR A 1 47  ? 47.350 4.083  27.924  1.00 8.05  ?  45  TYR A CD1   1 
ATOM   341  C  CD2   . TYR A 1 47  ? 49.189 5.502  27.392  1.00 8.27  ?  45  TYR A CD2   1 
ATOM   342  C  CE1   . TYR A 1 47  ? 47.165 4.750  29.135  1.00 7.67  ?  45  TYR A CE1   1 
ATOM   343  C  CE2   . TYR A 1 47  ? 49.023 6.178  28.595  1.00 8.04  ?  45  TYR A CE2   1 
ATOM   344  C  CZ    . TYR A 1 47  ? 48.004 5.799  29.441  1.00 7.86  ?  45  TYR A CZ    1 
ATOM   345  O  OH    . TYR A 1 47  ? 47.783 6.516  30.609  1.00 8.57  ?  45  TYR A OH    1 
ATOM   346  N  N     . HIS A 1 48  ? 46.883 6.695  25.506  1.00 7.38  ?  46  HIS A N     1 
ATOM   347  C  CA    . HIS A 1 48  ? 47.153 8.137  25.745  1.00 7.65  ?  46  HIS A CA    1 
ATOM   348  C  C     . HIS A 1 48  ? 46.559 8.511  27.097  1.00 7.50  ?  46  HIS A C     1 
ATOM   349  O  O     . HIS A 1 48  ? 45.482 8.035  27.454  1.00 7.76  ?  46  HIS A O     1 
ATOM   350  C  CB    . HIS A 1 48  ? 46.499 8.967  24.628  1.00 8.49  ?  46  HIS A CB    1 
ATOM   351  C  CG    . HIS A 1 48  ? 47.106 10.299 24.406  1.00 7.98  ?  46  HIS A CG    1 
ATOM   352  N  ND1   . HIS A 1 48  ? 46.932 11.369 25.270  1.00 8.16  ?  46  HIS A ND1   1 
ATOM   353  C  CD2   . HIS A 1 48  ? 47.703 10.796 23.303  1.00 8.53  ?  46  HIS A CD2   1 
ATOM   354  C  CE1   . HIS A 1 48  ? 47.518 12.436 24.709  1.00 8.58  ?  46  HIS A CE1   1 
ATOM   355  N  NE2   . HIS A 1 48  ? 47.982 12.135 23.502  1.00 8.49  ?  46  HIS A NE2   1 
ATOM   356  N  N     . ILE A 1 49  ? 47.194 9.438  27.770  1.00 8.21  ?  47  ILE A N     1 
ATOM   357  C  CA    . ILE A 1 49  ? 46.640 9.997  29.017  1.00 8.27  ?  47  ILE A CA    1 
ATOM   358  C  C     . ILE A 1 49  ? 45.669 11.099 28.677  1.00 9.10  ?  47  ILE A C     1 
ATOM   359  O  O     . ILE A 1 49  ? 45.706 11.655 27.566  1.00 12.08 ?  47  ILE A O     1 
ATOM   360  C  CB    . ILE A 1 49  ? 47.755 10.521 29.926  1.00 8.14  ?  47  ILE A CB    1 
ATOM   361  C  CG1   . ILE A 1 49  ? 47.306 10.731 31.383  1.00 8.59  ?  47  ILE A CG1   1 
ATOM   362  C  CG2   . ILE A 1 49  ? 48.444 11.729 29.373  1.00 9.87  ?  47  ILE A CG2   1 
ATOM   363  C  CD1   . ILE A 1 49  ? 46.505 9.647  32.025  1.00 9.00  ?  47  ILE A CD1   1 
ATOM   364  N  N     . GLY A 1 50  ? 44.826 11.485 29.568  1.00 8.31  ?  48  GLY A N     1 
ATOM   365  C  CA    . GLY A 1 50  ? 43.991 12.668 29.371  1.00 8.33  ?  48  GLY A CA    1 
ATOM   366  C  C     . GLY A 1 50  ? 42.546 12.316 29.179  1.00 7.59  ?  48  GLY A C     1 
ATOM   367  O  O     . GLY A 1 50  ? 42.045 12.394 28.058  1.00 8.47  ?  48  GLY A O     1 
ATOM   368  N  N     . GLU A 1 51  ? 41.907 11.823 30.230  1.00 7.56  ?  49  GLU A N     1 
ATOM   369  C  CA    . GLU A 1 51  ? 40.718 10.950 30.183  1.00 8.27  ?  49  GLU A CA    1 
ATOM   370  C  C     . GLU A 1 51  ? 39.426 11.644 30.567  1.00 7.78  ?  49  GLU A C     1 
ATOM   371  O  O     . GLU A 1 51  ? 38.357 11.101 30.248  1.00 8.36  ?  49  GLU A O     1 
ATOM   372  C  CB    . GLU A 1 51  ? 40.958 9.742  31.070  1.00 8.73  ?  49  GLU A CB    1 
ATOM   373  C  CG    . GLU A 1 51  ? 42.132 8.907  30.591  1.00 8.55  ?  49  GLU A CG    1 
ATOM   374  C  CD    . GLU A 1 51  ? 42.907 8.172  31.629  1.00 8.97  ?  49  GLU A CD    1 
ATOM   375  O  OE1   . GLU A 1 51  ? 43.100 8.688  32.749  1.00 9.90  ?  49  GLU A OE1   1 
ATOM   376  O  OE2   . GLU A 1 51  ? 43.395 7.051  31.286  1.00 9.82  ?  49  GLU A OE2   1 
ATOM   377  N  N     . SER A 1 52  ? 39.489 12.746 31.309  1.00 7.65  ?  50  SER A N     1 
ATOM   378  C  CA    . SER A 1 52  ? 38.247 13.336 31.829  1.00 7.87  ?  50  SER A CA    1 
ATOM   379  C  C     . SER A 1 52  ? 37.723 14.409 30.879  1.00 8.06  ?  50  SER A C     1 
ATOM   380  O  O     . SER A 1 52  ? 38.366 15.449 30.763  1.00 8.59  ?  50  SER A O     1 
ATOM   381  C  CB    . SER A 1 52  ? 38.495 13.858 33.182  1.00 9.04  ?  50  SER A CB    1 
ATOM   382  O  OG    . SER A 1 52  ? 37.229 14.017 33.891  1.00 9.41  ?  50  SER A OG    1 
ATOM   383  N  N     . LEU A 1 53  ? 36.586 14.213 30.241  1.00 8.59  ?  51  LEU A N     1 
ATOM   384  C  CA    . LEU A 1 53  ? 36.040 15.194 29.290  1.00 8.77  ?  51  LEU A CA    1 
ATOM   385  C  C     . LEU A 1 53  ? 35.068 16.121 29.994  1.00 8.93  ?  51  LEU A C     1 
ATOM   386  O  O     . LEU A 1 53  ? 34.600 15.853 31.109  1.00 9.96  ?  51  LEU A O     1 
ATOM   387  C  CB    . LEU A 1 53  ? 35.378 14.468 28.128  1.00 9.54  ?  51  LEU A CB    1 
ATOM   388  C  CG    . LEU A 1 53  ? 36.232 13.399 27.438  1.00 9.03  ?  51  LEU A CG    1 
ATOM   389  C  CD1   . LEU A 1 53  ? 35.525 12.894 26.218  1.00 9.78  ?  51  LEU A CD1   1 
ATOM   390  C  CD2   . LEU A 1 53  ? 37.613 13.968 27.034  1.00 9.41  ?  51  LEU A CD2   1 
ATOM   391  N  N     . ILE A 1 54  ? 34.820 17.255 29.380  1.00 9.50  ?  52  ILE A N     1 
ATOM   392  C  CA    . ILE A 1 54  ? 33.835 18.238 29.863  1.00 10.00 ?  52  ILE A CA    1 
ATOM   393  C  C     . ILE A 1 54  ? 32.877 18.475 28.725  1.00 9.64  ?  52  ILE A C     1 
ATOM   394  O  O     . ILE A 1 54  ? 33.084 18.018 27.580  1.00 10.19 ?  52  ILE A O     1 
ATOM   395  C  CB    . ILE A 1 54  ? 34.539 19.483 30.429  1.00 9.95  ?  52  ILE A CB    1 
ATOM   396  C  CG1   . ILE A 1 54  ? 35.435 20.153 29.392  1.00 10.63 ?  52  ILE A CG1   1 
ATOM   397  C  CG2   . ILE A 1 54  ? 35.323 19.107 31.674  1.00 9.87  ?  52  ILE A CG2   1 
ATOM   398  C  CD1   . ILE A 1 54  ? 36.262 21.268 29.827  1.00 10.84 ?  52  ILE A CD1   1 
ATOM   399  N  N     . THR A 1 55  ? 31.765 19.168 28.988  1.00 10.26 ?  53  THR A N     1 
ATOM   400  C  CA    . THR A 1 55  ? 30.643 19.159 28.024  1.00 10.23 ?  53  THR A CA    1 
ATOM   401  C  C     . THR A 1 55  ? 30.927 19.976 26.784  1.00 9.90  ?  53  THR A C     1 
ATOM   402  O  O     . THR A 1 55  ? 30.266 19.800 25.790  1.00 10.19 ?  53  THR A O     1 
ATOM   403  C  CB    . THR A 1 55  ? 29.344 19.592 28.700  1.00 11.23 ?  53  THR A CB    1 
ATOM   404  O  OG1   . THR A 1 55  ? 29.628 20.790 29.408  1.00 12.97 ?  53  THR A OG1   1 
ATOM   405  C  CG2   . THR A 1 55  ? 28.799 18.552 29.654  1.00 11.90 ?  53  THR A CG2   1 
ATOM   406  N  N     . GLY A 1 56  ? 31.995 20.770 26.777  1.00 10.48 ?  54  GLY A N     1 
ATOM   407  C  CA    . GLY A 1 56  ? 32.447 21.413 25.550  1.00 11.53 ?  54  GLY A CA    1 
ATOM   408  C  C     . GLY A 1 56  ? 32.802 20.459 24.410  1.00 11.26 ?  54  GLY A C     1 
ATOM   409  O  O     . GLY A 1 56  ? 32.847 20.880 23.235  1.00 12.38 ?  54  GLY A O     1 
ATOM   410  N  N     . VAL A 1 57  ? 33.038 19.182 24.678  1.00 10.59 ?  55  VAL A N     1 
ATOM   411  C  CA    . VAL A 1 57  ? 33.260 18.222 23.570  1.00 11.07 ?  55  VAL A CA    1 
ATOM   412  C  C     . VAL A 1 57  ? 31.968 17.918 22.834  1.00 10.80 ?  55  VAL A C     1 
ATOM   413  O  O     . VAL A 1 57  ? 32.051 17.456 21.706  1.00 10.95 ?  55  VAL A O     1 
ATOM   414  C  CB    . VAL A 1 57  ? 33.884 16.891 24.020  1.00 12.05 ?  55  VAL A CB    1 
ATOM   415  C  CG1   . VAL A 1 57  ? 35.266 17.139 24.573  1.00 13.44 ?  55  VAL A CG1   1 
ATOM   416  C  CG2   . VAL A 1 57  ? 33.046 16.063 24.960  1.00 11.62 ?  55  VAL A CG2   1 
ATOM   417  N  N     . LEU A 1 58  ? 30.831 18.079 23.504  1.00 11.53 ?  56  LEU A N     1 
ATOM   418  C  CA    . LEU A 1 58  ? 29.588 17.497 22.944  1.00 10.89 ?  56  LEU A CA    1 
ATOM   419  C  C     . LEU A 1 58  ? 29.183 18.099 21.607  1.00 10.08 ?  56  LEU A C     1 
ATOM   420  O  O     . LEU A 1 58  ? 28.768 17.356 20.712  1.00 10.92 ?  56  LEU A O     1 
ATOM   421  C  CB    . LEU A 1 58  ? 28.474 17.618 23.989  1.00 11.59 ?  56  LEU A CB    1 
ATOM   422  C  CG    . LEU A 1 58  ? 28.643 16.858 25.292  1.00 13.37 ?  56  LEU A CG    1 
ATOM   423  C  CD1   . LEU A 1 58  ? 27.486 17.225 26.224  1.00 14.40 ?  56  LEU A CD1   1 
ATOM   424  C  CD2   . LEU A 1 58  ? 28.714 15.344 25.057  1.00 15.83 ?  56  LEU A CD2   1 
ATOM   425  N  N     . PRO A 1 59  ? 29.281 19.421 21.382  1.00 10.99 ?  57  PRO A N     1 
ATOM   426  C  CA    . PRO A 1 59  ? 28.895 19.921 20.073  1.00 11.69 ?  57  PRO A CA    1 
ATOM   427  C  C     . PRO A 1 59  ? 29.728 19.377 18.915  1.00 11.13 ?  57  PRO A C     1 
ATOM   428  O  O     . PRO A 1 59  ? 29.207 19.117 17.867  1.00 12.72 ?  57  PRO A O     1 
ATOM   429  C  CB    . PRO A 1 59  ? 29.049 21.438 20.200  1.00 12.98 ?  57  PRO A CB    1 
ATOM   430  C  CG    . PRO A 1 59  ? 29.026 21.714 21.656  1.00 16.20 ?  57  PRO A CG    1 
ATOM   431  C  CD    . PRO A 1 59  ? 29.537 20.471 22.365  1.00 12.23 ?  57  PRO A CD    1 
ATOM   432  N  N     . THR A 1 60  ? 31.022 19.161 19.139  1.00 11.10 ?  58  THR A N     1 
ATOM   433  C  CA    . THR A 1 60  ? 31.883 18.608 18.066  1.00 11.58 ?  58  THR A CA    1 
ATOM   434  C  C     . THR A 1 60  ? 31.528 17.140 17.868  1.00 10.14 ?  58  THR A C     1 
ATOM   435  O  O     . THR A 1 60  ? 31.459 16.698 16.744  1.00 10.91 ?  58  THR A O     1 
ATOM   436  C  CB    . THR A 1 60  ? 33.350 18.825 18.390  1.00 12.53 ?  58  THR A CB    1 
ATOM   437  O  OG1   . THR A 1 60  ? 33.564 20.250 18.554  1.00 13.54 ?  58  THR A OG1   1 
ATOM   438  C  CG2   . THR A 1 60  ? 34.258 18.249 17.346  1.00 12.47 ?  58  THR A CG2   1 
ATOM   439  N  N     . LEU A 1 61  ? 31.332 16.405 18.953  1.00 10.21 ?  59  LEU A N     1 
ATOM   440  C  CA    . LEU A 1 61  ? 30.866 14.985 18.807  1.00 10.34 ?  59  LEU A CA    1 
ATOM   441  C  C     . LEU A 1 61  ? 29.554 14.914 18.015  1.00 10.52 ?  59  LEU A C     1 
ATOM   442  O  O     . LEU A 1 61  ? 29.384 14.024 17.171  1.00 11.76 ?  59  LEU A O     1 
ATOM   443  C  CB    . LEU A 1 61  ? 30.719 14.339 20.183  1.00 10.11 ?  59  LEU A CB    1 
ATOM   444  C  CG    . LEU A 1 61  ? 32.049 13.999 20.860  1.00 10.48 ?  59  LEU A CG    1 
ATOM   445  C  CD1   . LEU A 1 61  ? 31.876 13.589 22.288  1.00 11.39 ?  59  LEU A CD1   1 
ATOM   446  C  CD2   . LEU A 1 61  ? 32.824 12.903 20.098  1.00 11.84 ?  59  LEU A CD2   1 
ATOM   447  N  N     . ALA A 1 62  ? 28.698 15.897 18.210  1.00 10.97 ?  60  ALA A N     1 
ATOM   448  C  CA    . ALA A 1 62  ? 27.439 15.942 17.483  1.00 11.96 ?  60  ALA A CA    1 
ATOM   449  C  C     . ALA A 1 62  ? 27.634 16.238 15.991  1.00 11.82 ?  60  ALA A C     1 
ATOM   450  O  O     . ALA A 1 62  ? 27.054 15.588 15.154  1.00 13.87 ?  60  ALA A O     1 
ATOM   451  C  CB    . ALA A 1 62  ? 26.479 16.939 18.138  1.00 12.66 ?  60  ALA A CB    1 
ATOM   452  N  N     . ARG A 1 63  ? 28.489 17.191 15.707  1.00 11.50 ?  61  ARG A N     1 
ATOM   453  C  CA    . ARG A 1 63  ? 28.782 17.512 14.325  1.00 12.96 ?  61  ARG A CA    1 
ATOM   454  C  C     . ARG A 1 63  ? 29.407 16.303 13.629  1.00 12.53 ?  61  ARG A C     1 
ATOM   455  O  O     . ARG A 1 63  ? 29.197 16.109 12.456  1.00 14.00 ?  61  ARG A O     1 
ATOM   456  C  CB    . ARG A 1 63  ? 29.702 18.715 14.229  1.00 13.78 ?  61  ARG A CB    1 
ATOM   457  C  CG    . ARG A 1 63  ? 29.070 20.021 14.681  1.00 18.72 ?  61  ARG A CG    1 
ATOM   458  C  CD    . ARG A 1 63  ? 29.991 21.202 14.421  1.00 27.23 ?  61  ARG A CD    1 
ATOM   459  N  NE    . ARG A 1 63  ? 30.946 21.406 15.514  1.00 39.56 ?  61  ARG A NE    1 
ATOM   460  C  CZ    . ARG A 1 63  ? 30.756 22.232 16.542  1.00 35.45 ?  61  ARG A CZ    1 
ATOM   461  N  NH1   . ARG A 1 63  ? 29.640 22.943 16.627  1.00 32.26 ?  61  ARG A NH1   1 
ATOM   462  N  NH2   . ARG A 1 63  ? 31.683 22.346 17.483  1.00 20.37 ?  61  ARG A NH2   1 
ATOM   463  N  N     . LEU A 1 64  ? 30.192 15.508 14.349  1.00 11.09 ?  62  LEU A N     1 
ATOM   464  C  CA    . LEU A 1 64  ? 30.803 14.300 13.796  1.00 10.56 ?  62  LEU A CA    1 
ATOM   465  C  C     . LEU A 1 64  ? 29.841 13.124 13.791  1.00 12.20 ?  62  LEU A C     1 
ATOM   466  O  O     . LEU A 1 64  ? 30.282 12.058 13.358  1.00 13.18 ?  62  LEU A O     1 
ATOM   467  C  CB    . LEU A 1 64  ? 32.025 13.926 14.620  1.00 11.17 ?  62  LEU A CB    1 
ATOM   468  C  CG    . LEU A 1 64  ? 33.225 14.891 14.495  1.00 10.79 ?  62  LEU A CG    1 
ATOM   469  C  CD1   . LEU A 1 64  ? 34.276 14.604 15.567  1.00 12.60 ?  62  LEU A CD1   1 
ATOM   470  C  CD2   . LEU A 1 64  ? 33.830 14.795 13.106  1.00 12.09 ?  62  LEU A CD2   1 
ATOM   471  N  N     . GLY A 1 65  ? 28.628 13.252 14.283  1.00 12.32 ?  63  GLY A N     1 
ATOM   472  C  CA    . GLY A 1 65  ? 27.675 12.139 14.213  1.00 12.83 ?  63  GLY A CA    1 
ATOM   473  C  C     . GLY A 1 65  ? 27.995 11.039 15.196  1.00 12.34 ?  63  GLY A C     1 
ATOM   474  O  O     . GLY A 1 65  ? 27.626 9.882  14.950  1.00 13.13 ?  63  GLY A O     1 
ATOM   475  N  N     . LEU A 1 66  ? 28.577 11.398 16.327  1.00 10.81 ?  64  LEU A N     1 
ATOM   476  C  CA    . LEU A 1 66  ? 29.094 10.417 17.315  1.00 10.82 ?  64  LEU A CA    1 
ATOM   477  C  C     . LEU A 1 66  ? 28.325 10.397 18.631  1.00 11.45 ?  64  LEU A C     1 
ATOM   478  O  O     . LEU A 1 66  ? 28.704 9.608  19.524  1.00 12.16 ?  64  LEU A O     1 
ATOM   479  C  CB    . LEU A 1 66  ? 30.596 10.631 17.555  1.00 11.06 ?  64  LEU A CB    1 
ATOM   480  C  CG    . LEU A 1 66  ? 31.458 10.327 16.335  1.00 11.16 ?  64  LEU A CG    1 
ATOM   481  C  CD1   . LEU A 1 66  ? 32.932 10.639 16.625  1.00 12.26 ?  64  LEU A CD1   1 
ATOM   482  C  CD2   . LEU A 1 66  ? 31.305 8.876  15.907  1.00 12.02 ?  64  LEU A CD2   1 
ATOM   483  N  N     . THR A 1 67  ? 27.272 11.189 18.804  1.00 11.51 ?  65  THR A N     1 
ATOM   484  C  CA    . THR A 1 67  ? 26.575 11.269 20.098  1.00 12.71 ?  65  THR A CA    1 
ATOM   485  C  C     . THR A 1 67  ? 26.036 9.906  20.533  1.00 13.33 ?  65  THR A C     1 
ATOM   486  O  O     . THR A 1 67  ? 26.269 9.496  21.673  1.00 13.88 ?  65  THR A O     1 
ATOM   487  C  CB    . THR A 1 67  ? 25.437 12.273 19.966  1.00 13.98 ?  65  THR A CB    1 
ATOM   488  O  OG1   . THR A 1 67  ? 25.923 13.539 19.519  1.00 13.59 ?  65  THR A OG1   1 
ATOM   489  C  CG2   . THR A 1 67  ? 24.702 12.425 21.250  1.00 14.33 ?  65  THR A CG2   1 
ATOM   490  N  N     . GLU A 1 68  ? 25.432 9.159  19.640  1.00 14.27 ?  66  GLU A N     1 
ATOM   491  C  CA    . GLU A 1 68  ? 24.895 7.851  19.996  1.00 16.00 ?  66  GLU A CA    1 
ATOM   492  C  C     . GLU A 1 68  ? 26.002 6.794  20.133  1.00 15.19 ?  66  GLU A C     1 
ATOM   493  O  O     . GLU A 1 68  ? 25.938 5.961  20.926  1.00 13.94 ?  66  GLU A O     1 
ATOM   494  C  CB    . GLU A 1 68  ? 23.855 7.466  18.940  1.00 18.80 ?  66  GLU A CB    1 
ATOM   495  C  CG    . GLU A 1 68  ? 22.677 8.457  18.816  1.00 27.27 ?  66  GLU A CG    1 
ATOM   496  C  CD    . GLU A 1 68  ? 22.903 9.784  18.033  1.00 35.77 ?  66  GLU A CD    1 
ATOM   497  O  OE1   . GLU A 1 68  ? 23.790 9.936  17.162  1.00 33.63 ?  66  GLU A OE1   1 
ATOM   498  O  OE2   . GLU A 1 68  ? 22.131 10.710 18.340  1.00 44.46 ?  66  GLU A OE2   1 
ATOM   499  N  N     . ARG A 1 69  ? 27.033 6.903  19.329  1.00 13.29 ?  67  ARG A N     1 
ATOM   500  C  CA    . ARG A 1 69  ? 28.160 5.990  19.442  1.00 13.42 ?  67  ARG A CA    1 
ATOM   501  C  C     . ARG A 1 69  ? 28.813 6.063  20.821  1.00 13.19 ?  67  ARG A C     1 
ATOM   502  O  O     . ARG A 1 69  ? 29.266 5.036  21.328  1.00 13.12 ?  67  ARG A O     1 
ATOM   503  C  CB    . ARG A 1 69  ? 29.199 6.276  18.371  1.00 15.34 ?  67  ARG A CB    1 
ATOM   504  C  CG    . ARG A 1 69  ? 28.723 5.901  16.990  1.00 17.54 ?  67  ARG A CG    1 
ATOM   505  C  CD    . ARG A 1 69  ? 28.519 4.412  16.836  1.00 18.07 ?  67  ARG A CD    1 
ATOM   506  N  NE    . ARG A 1 69  ? 29.791 3.712  16.747  1.00 20.44 ?  67  ARG A NE    1 
ATOM   507  C  CZ    . ARG A 1 69  ? 29.983 2.481  17.212  1.00 23.04 ?  67  ARG A CZ    1 
ATOM   508  N  NH1   . ARG A 1 69  ? 28.987 1.827  17.793  1.00 18.49 ?  67  ARG A NH1   1 
ATOM   509  N  NH2   . ARG A 1 69  ? 31.171 1.904  17.096  1.00 22.75 ?  67  ARG A NH2   1 
ATOM   510  N  N     . MET A 1 70  ? 28.893 7.258  21.418  1.00 12.42 ?  68  MET A N     1 
ATOM   511  C  CA    . MET A 1 70  ? 29.489 7.363  22.758  1.00 12.03 ?  68  MET A CA    1 
ATOM   512  C  C     . MET A 1 70  ? 28.723 6.489  23.755  1.00 13.49 ?  68  MET A C     1 
ATOM   513  O  O     . MET A 1 70  ? 29.320 5.824  24.651  1.00 15.24 ?  68  MET A O     1 
ATOM   514  C  CB    . MET A 1 70  ? 29.502 8.821  23.243  1.00 13.25 ?  68  MET A CB    1 
ATOM   515  C  CG    . MET A 1 70  ? 30.425 9.662  22.451  1.00 12.26 ?  68  MET A CG    1 
ATOM   516  S  SD    . MET A 1 70  ? 32.185 9.252  22.634  1.00 12.19 ?  68  MET A SD    1 
ATOM   517  C  CE    . MET A 1 70  ? 32.459 9.792  24.306  1.00 12.64 ?  68  MET A CE    1 
ATOM   518  N  N     . GLU A 1 71  ? 27.401 6.470  23.615  1.00 14.43 ?  69  GLU A N     1 
ATOM   519  C  CA    . GLU A 1 71  ? 26.552 5.619  24.498  1.00 14.31 ?  69  GLU A CA    1 
ATOM   520  C  C     . GLU A 1 71  ? 26.662 4.133  24.143  1.00 15.38 ?  69  GLU A C     1 
ATOM   521  O  O     . GLU A 1 71  ? 26.739 3.296  25.054  1.00 16.54 ?  69  GLU A O     1 
ATOM   522  C  CB    . GLU A 1 71  ? 25.125 6.103  24.315  1.00 14.95 ?  69  GLU A CB    1 
ATOM   523  C  CG    . GLU A 1 71  ? 24.825 7.403  25.042  1.00 15.67 ?  69  GLU A CG    1 
ATOM   524  C  CD    . GLU A 1 71  ? 24.903 7.249  26.549  1.00 18.86 ?  69  GLU A CD    1 
ATOM   525  O  OE1   . GLU A 1 71  ? 24.104 6.425  27.092  1.00 19.32 ?  69  GLU A OE1   1 
ATOM   526  O  OE2   . GLU A 1 71  ? 25.780 7.886  27.237  1.00 17.91 ?  69  GLU A OE2   1 
ATOM   527  N  N     . GLN A 1 72  ? 26.745 3.808  22.873  1.00 14.92 ?  70  GLN A N     1 
ATOM   528  C  CA    . GLN A 1 72  ? 26.854 2.378  22.472  1.00 15.87 ?  70  GLN A CA    1 
ATOM   529  C  C     . GLN A 1 72  ? 28.142 1.802  23.002  1.00 17.21 ?  70  GLN A C     1 
ATOM   530  O  O     . GLN A 1 72  ? 28.161 0.619  23.385  1.00 18.08 ?  70  GLN A O     1 
ATOM   531  C  CB    . GLN A 1 72  ? 26.770 2.242  20.960  1.00 17.05 ?  70  GLN A CB    1 
ATOM   532  C  CG    . GLN A 1 72  ? 25.377 2.540  20.465  1.00 18.97 ?  70  GLN A CG    1 
ATOM   533  C  CD    . GLN A 1 72  ? 25.307 2.728  18.974  1.00 25.38 ?  70  GLN A CD    1 
ATOM   534  O  OE1   . GLN A 1 72  ? 26.281 2.622  18.245  1.00 23.56 ?  70  GLN A OE1   1 
ATOM   535  N  NE2   . GLN A 1 72  ? 24.129 3.120  18.497  1.00 32.49 ?  70  GLN A NE2   1 
ATOM   536  N  N     . LEU A 1 73  ? 29.234 2.539  22.925  1.00 15.83 ?  71  LEU A N     1 
ATOM   537  C  CA    . LEU A 1 73  ? 30.569 2.072  23.376  1.00 15.53 ?  71  LEU A CA    1 
ATOM   538  C  C     . LEU A 1 73  ? 30.541 1.918  24.889  1.00 16.57 ?  71  LEU A C     1 
ATOM   539  O  O     . LEU A 1 73  ? 31.343 1.148  25.361  1.00 19.32 ?  71  LEU A O     1 
ATOM   540  C  CB    . LEU A 1 73  ? 31.742 2.964  22.950  1.00 17.95 ?  71  LEU A CB    1 
ATOM   541  C  CG    . LEU A 1 73  ? 32.419 2.631  21.632  1.00 22.46 ?  71  LEU A CG    1 
ATOM   542  C  CD1   . LEU A 1 73  ? 31.441 2.605  20.563  1.00 23.04 ?  71  LEU A CD1   1 
ATOM   543  C  CD2   . LEU A 1 73  ? 33.575 3.544  21.275  1.00 23.18 ?  71  LEU A CD2   1 
ATOM   544  N  N     . GLY A 1 74  ? 29.706 2.681  25.604  1.00 14.67 ?  72  GLY A N     1 
ATOM   545  C  CA    . GLY A 1 74  ? 29.520 2.485  27.038  1.00 14.99 ?  72  GLY A CA    1 
ATOM   546  C  C     . GLY A 1 74  ? 30.559 3.193  27.888  1.00 15.58 ?  72  GLY A C     1 
ATOM   547  O  O     . GLY A 1 74  ? 30.861 2.781  29.016  1.00 16.87 ?  72  GLY A O     1 
ATOM   548  N  N     . PHE A 1 75  ? 31.061 4.297  27.402  1.00 13.11 ?  73  PHE A N     1 
ATOM   549  C  CA    . PHE A 1 75  ? 31.950 5.089  28.224  1.00 12.10 ?  73  PHE A CA    1 
ATOM   550  C  C     . PHE A 1 75  ? 31.210 5.569  29.488  1.00 12.39 ?  73  PHE A C     1 
ATOM   551  O  O     . PHE A 1 75  ? 30.061 5.839  29.454  1.00 13.57 ?  73  PHE A O     1 
ATOM   552  C  CB    . PHE A 1 75  ? 32.428 6.343  27.453  1.00 11.46 ?  73  PHE A CB    1 
ATOM   553  C  CG    . PHE A 1 75  ? 33.351 6.055  26.287  1.00 10.35 ?  73  PHE A CG    1 
ATOM   554  C  CD1   . PHE A 1 75  ? 34.635 5.628  26.479  1.00 11.58 ?  73  PHE A CD1   1 
ATOM   555  C  CD2   . PHE A 1 75  ? 32.961 6.315  25.033  1.00 10.95 ?  73  PHE A CD2   1 
ATOM   556  C  CE1   . PHE A 1 75  ? 35.477 5.383  25.433  1.00 10.74 ?  73  PHE A CE1   1 
ATOM   557  C  CE2   . PHE A 1 75  ? 33.793 6.059  23.964  1.00 13.60 ?  73  PHE A CE2   1 
ATOM   558  C  CZ    . PHE A 1 75  ? 35.076 5.623  24.173  1.00 10.85 ?  73  PHE A CZ    1 
ATOM   559  N  N     . GLN A 1 76  ? 31.928 5.707  30.568  1.00 10.19 ?  74  GLN A N     1 
ATOM   560  C  CA    . GLN A 1 76  ? 31.375 6.191  31.813  1.00 9.86  ?  74  GLN A CA    1 
ATOM   561  C  C     . GLN A 1 76  ? 30.870 7.628  31.733  1.00 10.11 ?  74  GLN A C     1 
ATOM   562  O  O     . GLN A 1 76  ? 31.585 8.487  31.454  1.00 10.20 ?  74  GLN A O     1 
ATOM   563  C  CB    . GLN A 1 76  ? 32.461 6.098  32.859  1.00 11.85 ?  74  GLN A CB    1 
ATOM   564  C  CG    . GLN A 1 76  ? 32.136 6.658  34.240  1.00 14.00 ?  74  GLN A CG    1 
ATOM   565  C  CD    . GLN A 1 76  ? 31.159 5.785  34.958  1.00 17.11 ?  74  GLN A CD    1 
ATOM   566  O  OE1   . GLN A 1 76  ? 31.424 4.660  35.198  1.00 19.76 ?  74  GLN A OE1   1 
ATOM   567  N  NE2   . GLN A 1 76  ? 30.000 6.335  35.244  1.00 19.75 ?  74  GLN A NE2   1 
ATOM   568  N  N     . ARG A 1 77  ? 29.590 7.818  31.980  1.00 9.85  ?  75  ARG A N     1 
ATOM   569  C  CA    . ARG A 1 77  ? 29.066 9.192  32.008  1.00 9.81  ?  75  ARG A CA    1 
ATOM   570  C  C     . ARG A 1 77  ? 29.578 9.968  33.206  1.00 10.90 ?  75  ARG A C     1 
ATOM   571  O  O     . ARG A 1 77  ? 29.682 9.425  34.319  1.00 12.44 ?  75  ARG A O     1 
ATOM   572  C  CB    . ARG A 1 77  ? 27.536 9.167  32.122  1.00 10.26 ?  75  ARG A CB    1 
ATOM   573  C  CG    . ARG A 1 77  ? 26.809 8.671  30.888  1.00 11.02 ?  75  ARG A CG    1 
ATOM   574  C  CD    . ARG A 1 77  ? 25.299 8.823  31.073  1.00 13.60 ?  75  ARG A CD    1 
ATOM   575  N  NE    . ARG A 1 77  ? 24.515 8.292  29.990  1.00 13.93 ?  75  ARG A NE    1 
ATOM   576  C  CZ    . ARG A 1 77  ? 23.190 8.214  30.034  1.00 16.90 ?  75  ARG A CZ    1 
ATOM   577  N  NH1   . ARG A 1 77  ? 22.540 8.701  31.067  1.00 17.78 ?  75  ARG A NH1   1 
ATOM   578  N  NH2   . ARG A 1 77  ? 22.540 7.642  29.055  1.00 15.99 ?  75  ARG A NH2   1 
ATOM   579  N  N     . LYS A 1 78  ? 29.826 11.238 32.985  1.00 10.04 ?  76  LYS A N     1 
ATOM   580  C  CA    . LYS A 1 78  ? 30.378 12.156 33.987  1.00 10.18 ?  76  LYS A CA    1 
ATOM   581  C  C     . LYS A 1 78  ? 29.411 13.340 34.112  1.00 10.65 ?  76  LYS A C     1 
ATOM   582  O  O     . LYS A 1 78  ? 29.304 14.129 33.198  1.00 11.71 ?  76  LYS A O     1 
ATOM   583  C  CB    . LYS A 1 78  ? 31.769 12.586 33.545  1.00 10.37 ?  76  LYS A CB    1 
ATOM   584  C  CG    . LYS A 1 78  ? 32.425 13.631 34.404  1.00 9.30  ?  76  LYS A CG    1 
ATOM   585  C  CD    . LYS A 1 78  ? 33.612 14.317 33.721  1.00 8.82  ?  76  LYS A CD    1 
ATOM   586  C  CE    . LYS A 1 78  ? 34.235 15.394 34.545  1.00 9.26  ?  76  LYS A CE    1 
ATOM   587  N  NZ    . LYS A 1 78  ? 35.368 16.066 33.840  1.00 9.66  ?  76  LYS A NZ    1 
ATOM   588  N  N     . TYR A 1 79  ? 28.727 13.427 35.242  1.00 10.18 ?  77  TYR A N     1 
ATOM   589  C  CA    . TYR A 1 79  ? 27.694 14.489 35.451  1.00 10.39 ?  77  TYR A CA    1 
ATOM   590  C  C     . TYR A 1 79  ? 28.252 15.739 36.055  1.00 11.34 ?  77  TYR A C     1 
ATOM   591  O  O     . TYR A 1 79  ? 27.551 16.773 36.183  1.00 11.57 ?  77  TYR A O     1 
ATOM   592  C  CB    . TYR A 1 79  ? 26.517 13.919 36.257  1.00 10.91 ?  77  TYR A CB    1 
ATOM   593  C  CG    . TYR A 1 79  ? 25.619 13.019 35.457  1.00 12.26 ?  77  TYR A CG    1 
ATOM   594  C  CD1   . TYR A 1 79  ? 24.409 13.488 34.980  1.00 13.15 ?  77  TYR A CD1   1 
ATOM   595  C  CD2   . TYR A 1 79  ? 25.907 11.677 35.311  1.00 12.80 ?  77  TYR A CD2   1 
ATOM   596  C  CE1   . TYR A 1 79  ? 23.577 12.631 34.302  1.00 12.74 ?  77  TYR A CE1   1 
ATOM   597  C  CE2   . TYR A 1 79  ? 25.094 10.811 34.601  1.00 12.84 ?  77  TYR A CE2   1 
ATOM   598  C  CZ    . TYR A 1 79  ? 23.922 11.312 34.077  1.00 12.87 ?  77  TYR A CZ    1 
ATOM   599  O  OH    . TYR A 1 79  ? 23.063 10.478 33.384  1.00 17.34 ?  77  TYR A OH    1 
ATOM   600  N  N     . GLY A 1 80  ? 29.488 15.718 36.531  1.00 10.76 ?  78  GLY A N     1 
ATOM   601  C  CA    . GLY A 1 80  ? 30.142 16.877 37.126  1.00 11.67 ?  78  GLY A CA    1 
ATOM   602  C  C     . GLY A 1 80  ? 31.429 16.465 37.778  1.00 11.07 ?  78  GLY A C     1 
ATOM   603  O  O     . GLY A 1 80  ? 32.074 15.493 37.353  1.00 11.12 ?  78  GLY A O     1 
ATOM   604  N  N     . GLY A 1 81  ? 31.875 17.274 38.706  1.00 11.40 ?  79  GLY A N     1 
ATOM   605  C  CA    . GLY A 1 81  ? 33.146 17.113 39.367  1.00 11.05 ?  79  GLY A CA    1 
ATOM   606  C  C     . GLY A 1 81  ? 33.071 17.265 40.855  1.00 11.43 ?  79  GLY A C     1 
ATOM   607  O  O     . GLY A 1 81  ? 32.166 18.059 41.299  1.00 12.02 ?  79  GLY A O     1 
ATOM   608  N  N     . SER A 1 82  ? 33.952 16.649 41.573  1.00 10.67 ?  80  SER A N     1 
ATOM   609  C  CA    . SER A 1 82  ? 34.112 16.752 43.022  1.00 11.07 ?  80  SER A CA    1 
ATOM   610  C  C     . SER A 1 82  ? 35.461 17.385 43.293  1.00 12.27 ?  80  SER A C     1 
ATOM   611  O  O     . SER A 1 82  ? 36.498 16.969 42.700  1.00 11.44 ?  80  SER A O     1 
ATOM   612  C  CB    . SER A 1 82  ? 34.009 15.414 43.648  1.00 11.61 ?  80  SER A CB    1 
ATOM   613  O  OG    . SER A 1 82  ? 32.734 14.842 43.384  1.00 12.41 ?  80  SER A OG    1 
ATOM   614  N  N     . LEU A 1 83  ? 35.542 18.389 44.142  1.00 12.59 ?  81  LEU A N     1 
ATOM   615  C  CA    . LEU A 1 83  ? 36.766 19.146 44.414  1.00 14.01 ?  81  LEU A CA    1 
ATOM   616  C  C     . LEU A 1 83  ? 37.018 19.155 45.895  1.00 14.24 ?  81  LEU A C     1 
ATOM   617  O  O     . LEU A 1 83  ? 36.238 19.793 46.626  1.00 15.19 ?  81  LEU A O     1 
ATOM   618  C  CB    . LEU A 1 83  ? 36.611 20.540 43.869  1.00 15.07 ?  81  LEU A CB    1 
ATOM   619  C  CG    . LEU A 1 83  ? 36.595 20.394 42.353  1.00 19.75 ?  81  LEU A CG    1 
ATOM   620  C  CD1   . LEU A 1 83  ? 35.268 20.689 41.725  1.00 19.74 ?  81  LEU A CD1   1 
ATOM   621  C  CD2   . LEU A 1 83  ? 37.848 20.911 41.710  1.00 21.85 ?  81  LEU A CD2   1 
ATOM   622  N  N     . LEU A 1 84  ? 38.046 18.532 46.374  1.00 11.76 ?  82  LEU A N     1 
ATOM   623  C  CA    . LEU A 1 84  ? 38.489 18.719 47.749  1.00 12.95 ?  82  LEU A CA    1 
ATOM   624  C  C     . LEU A 1 84  ? 39.586 19.757 47.601  1.00 11.83 ?  82  LEU A C     1 
ATOM   625  O  O     . LEU A 1 84  ? 40.716 19.465 47.268  1.00 12.60 ?  82  LEU A O     1 
ATOM   626  C  CB    . LEU A 1 84  ? 38.953 17.407 48.357  1.00 14.89 ?  82  LEU A CB    1 
ATOM   627  C  CG    . LEU A 1 84  ? 39.089 17.435 49.864  1.00 19.50 ?  82  LEU A CG    1 
ATOM   628  C  CD1   . LEU A 1 84  ? 39.393 16.038 50.359  1.00 20.61 ?  82  LEU A CD1   1 
ATOM   629  C  CD2   . LEU A 1 84  ? 40.153 18.397 50.292  1.00 23.41 ?  82  LEU A CD2   1 
ATOM   630  N  N     . TRP A 1 85  ? 39.219 21.017 47.738  1.00 12.83 ?  83  TRP A N     1 
ATOM   631  C  CA    . TRP A 1 85  ? 40.027 22.138 47.237  1.00 13.06 ?  83  TRP A CA    1 
ATOM   632  C  C     . TRP A 1 85  ? 39.671 23.418 47.994  1.00 13.42 ?  83  TRP A C     1 
ATOM   633  O  O     . TRP A 1 85  ? 38.534 23.866 47.944  1.00 15.04 ?  83  TRP A O     1 
ATOM   634  C  CB    . TRP A 1 85  ? 39.782 22.289 45.754  1.00 13.80 ?  83  TRP A CB    1 
ATOM   635  C  CG    . TRP A 1 85  ? 40.852 22.996 45.018  1.00 14.31 ?  83  TRP A CG    1 
ATOM   636  C  CD1   . TRP A 1 85  ? 40.950 24.344 44.848  1.00 14.71 ?  83  TRP A CD1   1 
ATOM   637  C  CD2   . TRP A 1 85  ? 42.003 22.427 44.391  1.00 13.56 ?  83  TRP A CD2   1 
ATOM   638  N  NE1   . TRP A 1 85  ? 42.089 24.645 44.150  1.00 16.49 ?  83  TRP A NE1   1 
ATOM   639  C  CE2   . TRP A 1 85  ? 42.754 23.486 43.842  1.00 14.29 ?  83  TRP A CE2   1 
ATOM   640  C  CE3   . TRP A 1 85  ? 42.407 21.125 44.112  1.00 13.43 ?  83  TRP A CE3   1 
ATOM   641  C  CZ2   . TRP A 1 85  ? 43.944 23.315 43.133  1.00 14.61 ?  83  TRP A CZ2   1 
ATOM   642  C  CZ3   . TRP A 1 85  ? 43.579 20.965 43.407  1.00 13.39 ?  83  TRP A CZ3   1 
ATOM   643  C  CH2   . TRP A 1 85  ? 44.329 22.015 42.931  1.00 13.11 ?  83  TRP A CH2   1 
ATOM   644  N  N     . GLY A 1 86  ? 40.702 23.957 48.575  1.00 15.44 ?  84  GLY A N     1 
ATOM   645  C  CA    . GLY A 1 86  ? 40.632 25.305 49.162  1.00 17.85 ?  84  GLY A CA    1 
ATOM   646  C  C     . GLY A 1 86  ? 40.483 25.198 50.656  1.00 25.59 ?  84  GLY A C     1 
ATOM   647  O  O     . GLY A 1 86  ? 40.836 24.182 51.207  1.00 24.88 ?  84  GLY A O     1 
ATOM   648  N  N     . LYS A 1 87  ? 39.937 26.238 51.276  1.00 32.41 ?  85  LYS A N     1 
ATOM   649  C  CA    . LYS A 1 87  ? 39.881 26.332 52.774  1.00 39.12 ?  85  LYS A CA    1 
ATOM   650  C  C     . LYS A 1 87  ? 39.260 25.079 53.409  1.00 45.60 ?  85  LYS A C     1 
ATOM   651  O  O     . LYS A 1 87  ? 38.004 24.992 53.402  1.00 52.80 ?  85  LYS A O     1 
ATOM   652  C  CB    . LYS A 1 87  ? 39.091 27.583 53.152  1.00 46.92 ?  85  LYS A CB    1 
ATOM   653  C  CG    . LYS A 1 87  ? 39.844 28.878 52.903  1.00 50.06 ?  85  LYS A CG    1 
ATOM   654  C  CD    . LYS A 1 87  ? 39.112 30.110 53.410  1.00 55.61 ?  85  LYS A CD    1 
ATOM   655  C  CE    . LYS A 1 87  ? 37.877 30.413 52.593  1.00 55.22 ?  85  LYS A CE    1 
ATOM   656  N  NZ    . LYS A 1 87  ? 37.375 31.775 52.872  1.00 64.27 ?  85  LYS A NZ    1 
ATOM   657  N  N     . LYS A 1 91  ? 35.803 17.914 53.241  1.00 31.95 ?  89  LYS A N     1 
ATOM   658  C  CA    . LYS A 1 91  ? 34.967 17.070 52.357  1.00 34.07 ?  89  LYS A CA    1 
ATOM   659  C  C     . LYS A 1 91  ? 34.770 17.781 51.016  1.00 25.29 ?  89  LYS A C     1 
ATOM   660  O  O     . LYS A 1 91  ? 34.817 19.021 50.939  1.00 25.81 ?  89  LYS A O     1 
ATOM   661  C  CB    . LYS A 1 91  ? 33.641 16.737 53.033  1.00 41.39 ?  89  LYS A CB    1 
ATOM   662  C  CG    . LYS A 1 91  ? 33.719 15.839 54.259  1.00 53.49 ?  89  LYS A CG    1 
ATOM   663  C  CD    . LYS A 1 91  ? 32.354 15.571 54.893  1.00 61.62 ?  89  LYS A CD    1 
ATOM   664  C  CE    . LYS A 1 91  ? 32.434 14.656 56.101  1.00 62.58 ?  89  LYS A CE    1 
ATOM   665  N  NZ    . LYS A 1 91  ? 31.098 14.437 56.705  1.00 59.76 ?  89  LYS A NZ    1 
ATOM   666  N  N     . PRO A 1 92  ? 34.675 17.036 49.900  1.00 22.55 ?  90  PRO A N     1 
ATOM   667  C  CA    . PRO A 1 92  ? 34.643 17.688 48.589  1.00 19.25 ?  90  PRO A CA    1 
ATOM   668  C  C     . PRO A 1 92  ? 33.401 18.550 48.389  1.00 19.74 ?  90  PRO A C     1 
ATOM   669  O  O     . PRO A 1 92  ? 32.349 18.208 48.846  1.00 23.66 ?  90  PRO A O     1 
ATOM   670  C  CB    . PRO A 1 92  ? 34.666 16.561 47.560  1.00 19.97 ?  90  PRO A CB    1 
ATOM   671  C  CG    . PRO A 1 92  ? 35.158 15.370 48.349  1.00 21.57 ?  90  PRO A CG    1 
ATOM   672  C  CD    . PRO A 1 92  ? 34.679 15.567 49.770  1.00 20.21 ?  90  PRO A CD    1 
ATOM   673  N  N     . TRP A 1 93  ? 33.536 19.661 47.679  1.00 14.86 ?  91  TRP A N     1 
ATOM   674  C  CA    . TRP A 1 93  ? 32.421 20.424 47.142  1.00 13.05 ?  91  TRP A CA    1 
ATOM   675  C  C     . TRP A 1 93  ? 32.268 20.007 45.693  1.00 15.00 ?  91  TRP A C     1 
ATOM   676  O  O     . TRP A 1 93  ? 33.174 19.307 45.163  1.00 15.48 ?  91  TRP A O     1 
ATOM   677  C  CB    . TRP A 1 93  ? 32.547 21.935 47.290  1.00 13.70 ?  91  TRP A CB    1 
ATOM   678  C  CG    . TRP A 1 93  ? 33.830 22.565 46.816  1.00 12.68 ?  91  TRP A CG    1 
ATOM   679  C  CD1   . TRP A 1 93  ? 34.959 22.733 47.537  1.00 13.32 ?  91  TRP A CD1   1 
ATOM   680  C  CD2   . TRP A 1 93  ? 34.066 23.190 45.548  1.00 13.10 ?  91  TRP A CD2   1 
ATOM   681  N  NE1   . TRP A 1 93  ? 35.905 23.388 46.803  1.00 15.00 ?  91  TRP A NE1   1 
ATOM   682  C  CE2   . TRP A 1 93  ? 35.381 23.684 45.583  1.00 12.91 ?  91  TRP A CE2   1 
ATOM   683  C  CE3   . TRP A 1 93  ? 33.298 23.329 44.397  1.00 14.46 ?  91  TRP A CE3   1 
ATOM   684  C  CZ2   . TRP A 1 93  ? 35.917 24.391 44.505  1.00 14.02 ?  91  TRP A CZ2   1 
ATOM   685  C  CZ3   . TRP A 1 93  ? 33.819 24.048 43.351  1.00 14.09 ?  91  TRP A CZ3   1 
ATOM   686  C  CH2   . TRP A 1 93  ? 35.139 24.536 43.399  1.00 14.49 ?  91  TRP A CH2   1 
ATOM   687  N  N     . THR A 1 94  ? 31.136 20.228 45.111  1.00 13.89 ?  92  THR A N     1 
ATOM   688  C  CA    . THR A 1 94  ? 30.802 19.645 43.816  1.00 13.53 ?  92  THR A CA    1 
ATOM   689  C  C     . THR A 1 94  ? 30.191 20.674 42.906  1.00 14.81 ?  92  THR A C     1 
ATOM   690  O  O     . THR A 1 94  ? 29.722 21.730 43.354  1.00 16.05 ?  92  THR A O     1 
ATOM   691  C  CB    . THR A 1 94  ? 29.887 18.416 43.921  1.00 15.31 ?  92  THR A CB    1 
ATOM   692  O  OG1   . THR A 1 94  ? 28.619 18.893 44.398  1.00 16.71 ?  92  THR A OG1   1 
ATOM   693  C  CG2   . THR A 1 94  ? 30.443 17.366 44.852  1.00 17.01 ?  92  THR A CG2   1 
ATOM   694  N  N     . PHE A 1 95  ? 30.162 20.366 41.616  1.00 12.81 ?  93  PHE A N     1 
ATOM   695  C  CA    . PHE A 1 95  ? 29.330 21.045 40.639  1.00 12.17 ?  93  PHE A CA    1 
ATOM   696  C  C     . PHE A 1 95  ? 28.738 20.059 39.692  1.00 12.94 ?  93  PHE A C     1 
ATOM   697  O  O     . PHE A 1 95  ? 29.223 18.893 39.596  1.00 12.83 ?  93  PHE A O     1 
ATOM   698  C  CB    . PHE A 1 95  ? 30.130 22.067 39.847  1.00 12.81 ?  93  PHE A CB    1 
ATOM   699  C  CG    . PHE A 1 95  ? 31.079 21.473 38.856  1.00 11.80 ?  93  PHE A CG    1 
ATOM   700  C  CD1   . PHE A 1 95  ? 32.363 21.117 39.255  1.00 13.81 ?  93  PHE A CD1   1 
ATOM   701  C  CD2   . PHE A 1 95  ? 30.672 21.293 37.556  1.00 13.27 ?  93  PHE A CD2   1 
ATOM   702  C  CE1   . PHE A 1 95  ? 33.216 20.521 38.346  1.00 13.85 ?  93  PHE A CE1   1 
ATOM   703  C  CE2   . PHE A 1 95  ? 31.515 20.637 36.656  1.00 13.55 ?  93  PHE A CE2   1 
ATOM   704  C  CZ    . PHE A 1 95  ? 32.792 20.334 37.047  1.00 12.27 ?  93  PHE A CZ    1 
ATOM   705  N  N     . LYS A 1 96  ? 27.677 20.436 39.038  1.00 12.86 ?  94  LYS A N     1 
ATOM   706  C  CA    . LYS A 1 96  ? 27.018 19.643 38.022  1.00 13.27 ?  94  LYS A CA    1 
ATOM   707  C  C     . LYS A 1 96  ? 27.046 20.347 36.687  1.00 12.66 ?  94  LYS A C     1 
ATOM   708  O  O     . LYS A 1 96  ? 26.831 21.575 36.604  1.00 12.51 ?  94  LYS A O     1 
ATOM   709  C  CB    . LYS A 1 96  ? 25.533 19.376 38.328  1.00 15.57 ?  94  LYS A CB    1 
ATOM   710  C  CG    . LYS A 1 96  ? 25.273 18.568 39.578  1.00 18.21 ?  94  LYS A CG    1 
ATOM   711  C  CD    . LYS A 1 96  ? 25.275 17.128 39.262  1.00 18.47 ?  94  LYS A CD    1 
ATOM   712  C  CE    . LYS A 1 96  ? 24.901 16.234 40.418  1.00 20.28 ?  94  LYS A CE    1 
ATOM   713  N  NZ    . LYS A 1 96  ? 25.024 14.816 40.054  1.00 21.23 ?  94  LYS A NZ    1 
ATOM   714  N  N     . PHE A 1 97  ? 27.338 19.650 35.595  1.00 12.61 ?  95  PHE A N     1 
ATOM   715  C  CA    . PHE A 1 97  ? 27.338 20.249 34.251  1.00 11.53 ?  95  PHE A CA    1 
ATOM   716  C  C     . PHE A 1 97  ? 25.978 20.876 33.925  1.00 13.35 ?  95  PHE A C     1 
ATOM   717  O  O     . PHE A 1 97  ? 25.914 21.844 33.180  1.00 14.94 ?  95  PHE A O     1 
ATOM   718  C  CB    . PHE A 1 97  ? 27.688 19.203 33.207  1.00 12.01 ?  95  PHE A CB    1 
ATOM   719  C  CG    . PHE A 1 97  ? 29.149 18.797 33.192  1.00 11.44 ?  95  PHE A CG    1 
ATOM   720  C  CD1   . PHE A 1 97  ? 30.151 19.738 33.104  1.00 10.98 ?  95  PHE A CD1   1 
ATOM   721  C  CD2   . PHE A 1 97  ? 29.483 17.458 33.313  1.00 10.99 ?  95  PHE A CD2   1 
ATOM   722  C  CE1   . PHE A 1 97  ? 31.489 19.372 33.088  1.00 11.07 ?  95  PHE A CE1   1 
ATOM   723  C  CE2   . PHE A 1 97  ? 30.820 17.081 33.264  1.00 11.71 ?  95  PHE A CE2   1 
ATOM   724  C  CZ    . PHE A 1 97  ? 31.807 18.027 33.151  1.00 11.00 ?  95  PHE A CZ    1 
ATOM   725  N  N     . ARG A 1 98  ? 24.885 20.330 34.493  1.00 12.29 ?  96  ARG A N     1 
ATOM   726  C  CA    . ARG A 1 98  ? 23.560 20.896 34.187  1.00 14.37 ?  96  ARG A CA    1 
ATOM   727  C  C     . ARG A 1 98  ? 23.341 22.253 34.821  1.00 16.31 ?  96  ARG A C     1 
ATOM   728  O  O     . ARG A 1 98  ? 22.257 22.808 34.493  1.00 17.29 ?  96  ARG A O     1 
ATOM   729  C  CB    . ARG A 1 98  ? 22.461 19.921 34.599  1.00 15.55 ?  96  ARG A CB    1 
ATOM   730  C  CG    . ARG A 1 98  ? 22.293 19.693 36.080  1.00 16.04 ?  96  ARG A CG    1 
ATOM   731  C  CD    . ARG A 1 98  ? 20.950 18.999 36.366  1.00 17.98 ?  96  ARG A CD    1 
ATOM   732  N  NE    . ARG A 1 98  ? 20.873 17.694 35.679  1.00 20.91 ?  96  ARG A NE    1 
ATOM   733  C  CZ    . ARG A 1 98  ? 21.334 16.537 36.216  1.00 19.33 ?  96  ARG A CZ    1 
ATOM   734  N  NH1   . ARG A 1 98  ? 21.847 16.536 37.435  1.00 20.29 ?  96  ARG A NH1   1 
ATOM   735  N  NH2   . ARG A 1 98  ? 21.235 15.410 35.530  1.00 18.82 ?  96  ARG A NH2   1 
ATOM   736  N  N     . GLU A 1 99  ? 24.231 22.789 35.630  1.00 15.07 ?  97  GLU A N     1 
ATOM   737  C  CA    . GLU A 1 99  ? 24.016 24.111 36.271  1.00 16.11 ?  97  GLU A CA    1 
ATOM   738  C  C     . GLU A 1 99  ? 24.112 25.221 35.245  1.00 18.82 ?  97  GLU A C     1 
ATOM   739  O  O     . GLU A 1 99  ? 23.668 26.336 35.587  1.00 22.22 ?  97  GLU A O     1 
ATOM   740  C  CB    . GLU A 1 99  ? 24.968 24.358 37.413  1.00 18.14 ?  97  GLU A CB    1 
ATOM   741  C  CG    . GLU A 1 99  ? 24.711 23.521 38.618  1.00 20.55 ?  97  GLU A CG    1 
ATOM   742  C  CD    . GLU A 1 99  ? 25.787 23.762 39.660  1.00 24.53 ?  97  GLU A CD    1 
ATOM   743  O  OE1   . GLU A 1 99  ? 26.477 22.840 40.063  1.00 18.76 ?  97  GLU A OE1   1 
ATOM   744  O  OE2   . GLU A 1 99  ? 25.986 24.950 40.077  1.00 32.55 ?  97  GLU A OE2   1 
ATOM   745  N  N     . THR A 1 100 ? 24.643 24.994 34.055  1.00 17.52 ?  98  THR A N     1 
ATOM   746  C  CA    . THR A 1 100 ? 24.689 26.024 33.022  1.00 18.55 ?  98  THR A CA    1 
ATOM   747  C  C     . THR A 1 100 ? 23.854 25.569 31.837  1.00 18.81 ?  98  THR A C     1 
ATOM   748  O  O     . THR A 1 100 ? 23.400 24.399 31.792  1.00 20.13 ?  98  THR A O     1 
ATOM   749  C  CB    . THR A 1 100 ? 26.136 26.367 32.655  1.00 17.60 ?  98  THR A CB    1 
ATOM   750  O  OG1   . THR A 1 100 ? 26.105 27.569 31.867  1.00 19.25 ?  98  THR A OG1   1 
ATOM   751  C  CG2   . THR A 1 100 ? 26.799 25.259 31.878  1.00 17.76 ?  98  THR A CG2   1 
ATOM   752  N  N     . GLY A 1 101 ? 23.621 26.469 30.876  1.00 23.46 ?  99  GLY A N     1 
ATOM   753  C  CA    . GLY A 1 101 ? 22.952 26.096 29.618  1.00 24.08 ?  99  GLY A CA    1 
ATOM   754  C  C     . GLY A 1 101 ? 21.544 25.552 29.817  1.00 25.43 ?  99  GLY A C     1 
ATOM   755  O  O     . GLY A 1 101 ? 21.131 24.757 28.949  1.00 23.00 ?  99  GLY A O     1 
ATOM   756  N  N     . ASN A 1 102 ? 20.839 25.955 30.883  1.00 25.18 ?  100 ASN A N     1 
ATOM   757  C  CA    . ASN A 1 102 ? 19.442 25.486 31.079  1.00 27.43 ?  100 ASN A CA    1 
ATOM   758  C  C     . ASN A 1 102 ? 19.413 23.965 31.157  1.00 27.20 ?  100 ASN A C     1 
ATOM   759  O  O     . ASN A 1 102 ? 18.386 23.341 30.855  1.00 24.89 ?  100 ASN A O     1 
ATOM   760  C  CB    . ASN A 1 102 ? 18.545 25.978 29.942  1.00 31.26 ?  100 ASN A CB    1 
ATOM   761  C  CG    . ASN A 1 102 ? 18.122 27.418 30.150  1.00 43.02 ?  100 ASN A CG    1 
ATOM   762  O  OD1   . ASN A 1 102 ? 18.076 27.894 31.282  1.00 50.91 ?  100 ASN A OD1   1 
ATOM   763  N  ND2   . ASN A 1 102 ? 17.826 28.122 29.068  1.00 49.09 ?  100 ASN A ND2   1 
ATOM   764  N  N     . GLY A 1 103 ? 20.508 23.359 31.611  1.00 24.36 ?  101 GLY A N     1 
ATOM   765  C  CA    . GLY A 1 103 ? 20.505 21.927 31.882  1.00 22.10 ?  101 GLY A CA    1 
ATOM   766  C  C     . GLY A 1 103 ? 20.587 21.059 30.656  1.00 22.97 ?  101 GLY A C     1 
ATOM   767  O  O     . GLY A 1 103 ? 20.451 19.842 30.844  1.00 25.17 ?  101 GLY A O     1 
ATOM   768  N  N     . LYS A 1 104 ? 20.843 21.573 29.461  1.00 19.18 ?  102 LYS A N     1 
ATOM   769  C  CA    . LYS A 1 104 ? 20.775 20.805 28.226  1.00 23.47 ?  102 LYS A CA    1 
ATOM   770  C  C     . LYS A 1 104 ? 21.992 19.874 28.066  1.00 20.73 ?  102 LYS A C     1 
ATOM   771  O  O     . LYS A 1 104 ? 21.825 18.789 27.498  1.00 22.63 ?  102 LYS A O     1 
ATOM   772  C  CB    . LYS A 1 104 ? 20.671 21.753 27.045  1.00 27.52 ?  102 LYS A CB    1 
ATOM   773  C  CG    . LYS A 1 104 ? 19.506 22.738 27.125  1.00 36.85 ?  102 LYS A CG    1 
ATOM   774  C  CD    . LYS A 1 104 ? 18.157 22.074 27.009  1.00 45.59 ?  102 LYS A CD    1 
ATOM   775  C  CE    . LYS A 1 104 ? 17.089 23.065 26.589  1.00 51.82 ?  102 LYS A CE    1 
ATOM   776  N  NZ    . LYS A 1 104 ? 16.000 22.402 25.834  1.00 55.87 ?  102 LYS A NZ    1 
ATOM   777  N  N     . TYR A 1 105 ? 23.142 20.244 28.616  1.00 18.36 ?  103 TYR A N     1 
ATOM   778  C  CA    . TYR A 1 105 ? 24.287 19.291 28.650  1.00 16.73 ?  103 TYR A CA    1 
ATOM   779  C  C     . TYR A 1 105 ? 24.447 18.774 30.070  1.00 14.59 ?  103 TYR A C     1 
ATOM   780  O  O     . TYR A 1 105 ? 25.049 19.413 30.921  1.00 17.62 ?  103 TYR A O     1 
ATOM   781  C  CB    . TYR A 1 105 ? 25.563 19.984 28.205  1.00 17.49 ?  103 TYR A CB    1 
ATOM   782  C  CG    . TYR A 1 105 ? 25.577 20.495 26.786  1.00 18.95 ?  103 TYR A CG    1 
ATOM   783  C  CD1   . TYR A 1 105 ? 24.747 19.989 25.809  1.00 20.00 ?  103 TYR A CD1   1 
ATOM   784  C  CD2   . TYR A 1 105 ? 26.484 21.458 26.405  1.00 16.27 ?  103 TYR A CD2   1 
ATOM   785  C  CE1   . TYR A 1 105 ? 24.827 20.409 24.483  1.00 19.16 ?  103 TYR A CE1   1 
ATOM   786  C  CE2   . TYR A 1 105 ? 26.587 21.875 25.091  1.00 18.13 ?  103 TYR A CE2   1 
ATOM   787  C  CZ    . TYR A 1 105 ? 25.768 21.337 24.123  1.00 20.54 ?  103 TYR A CZ    1 
ATOM   788  O  OH    . TYR A 1 105 ? 25.787 21.733 22.811  1.00 23.12 ?  103 TYR A OH    1 
ATOM   789  N  N     . GLU A 1 106 ? 23.871 17.603 30.319  1.00 14.97 ?  104 GLU A N     1 
ATOM   790  C  CA    . GLU A 1 106 ? 23.819 17.038 31.658  1.00 14.66 ?  104 GLU A CA    1 
ATOM   791  C  C     . GLU A 1 106 ? 25.113 16.263 31.976  1.00 12.46 ?  104 GLU A C     1 
ATOM   792  O  O     . GLU A 1 106 ? 25.450 16.117 33.144  1.00 13.94 ?  104 GLU A O     1 
ATOM   793  C  CB    . GLU A 1 106 ? 22.665 16.034 31.733  1.00 19.26 ?  104 GLU A CB    1 
ATOM   794  C  CG    . GLU A 1 106 ? 21.290 16.702 31.611  1.00 24.02 ?  104 GLU A CG    1 
ATOM   795  C  CD    . GLU A 1 106 ? 20.188 15.682 31.901  1.00 29.21 ?  104 GLU A CD    1 
ATOM   796  O  OE1   . GLU A 1 106 ? 19.729 14.998 30.943  1.00 42.93 ?  104 GLU A OE1   1 
ATOM   797  O  OE2   . GLU A 1 106 ? 19.958 15.418 33.087  1.00 34.93 ?  104 GLU A OE2   1 
ATOM   798  N  N     . TYR A 1 107 ? 25.724 15.685 30.973  1.00 12.45 ?  105 TYR A N     1 
ATOM   799  C  CA    . TYR A 1 107 ? 26.922 14.912 31.200  1.00 11.79 ?  105 TYR A CA    1 
ATOM   800  C  C     . TYR A 1 107 ? 27.886 14.859 30.030  1.00 10.95 ?  105 TYR A C     1 
ATOM   801  O  O     . TYR A 1 107 ? 27.524 15.011 28.863  1.00 11.15 ?  105 TYR A O     1 
ATOM   802  C  CB    . TYR A 1 107 ? 26.553 13.446 31.585  1.00 12.04 ?  105 TYR A CB    1 
ATOM   803  C  CG    . TYR A 1 107 ? 25.705 12.701 30.546  1.00 12.90 ?  105 TYR A CG    1 
ATOM   804  C  CD1   . TYR A 1 107 ? 26.284 12.085 29.468  1.00 13.92 ?  105 TYR A CD1   1 
ATOM   805  C  CD2   . TYR A 1 107 ? 24.350 12.682 30.654  1.00 13.71 ?  105 TYR A CD2   1 
ATOM   806  C  CE1   . TYR A 1 107 ? 25.510 11.443 28.542  1.00 15.04 ?  105 TYR A CE1   1 
ATOM   807  C  CE2   . TYR A 1 107 ? 23.558 12.054 29.717  1.00 16.00 ?  105 TYR A CE2   1 
ATOM   808  C  CZ    . TYR A 1 107 ? 24.162 11.434 28.656  1.00 16.27 ?  105 TYR A CZ    1 
ATOM   809  O  OH    . TYR A 1 107 ? 23.448 10.796 27.685  1.00 20.45 ?  105 TYR A OH    1 
ATOM   810  N  N     . ALA A 1 108 ? 29.135 14.630 30.407  1.00 10.50 ?  106 ALA A N     1 
ATOM   811  C  CA    . ALA A 1 108 ? 30.174 14.315 29.468  1.00 11.15 ?  106 ALA A CA    1 
ATOM   812  C  C     . ALA A 1 108 ? 30.616 12.857 29.823  1.00 10.79 ?  106 ALA A C     1 
ATOM   813  O  O     . ALA A 1 108 ? 29.811 12.087 30.256  1.00 10.49 ?  106 ALA A O     1 
ATOM   814  C  CB    . ALA A 1 108 ? 31.317 15.324 29.482  1.00 11.57 ?  106 ALA A CB    1 
ATOM   815  N  N     . TYR A 1 109 ? 31.893 12.551 29.640  1.00 9.02  ?  107 TYR A N     1 
ATOM   816  C  CA    . TYR A 1 109 ? 32.335 11.166 29.798  1.00 9.14  ?  107 TYR A CA    1 
ATOM   817  C  C     . TYR A 1 109 ? 33.729 11.172 30.411  1.00 9.43  ?  107 TYR A C     1 
ATOM   818  O  O     . TYR A 1 109 ? 34.510 12.106 30.203  1.00 9.40  ?  107 TYR A O     1 
ATOM   819  C  CB    . TYR A 1 109 ? 32.362 10.454 28.449  1.00 10.46 ?  107 TYR A CB    1 
ATOM   820  C  CG    . TYR A 1 109 ? 31.000 10.274 27.852  1.00 10.82 ?  107 TYR A CG    1 
ATOM   821  C  CD1   . TYR A 1 109 ? 30.247 9.180  28.201  1.00 11.96 ?  107 TYR A CD1   1 
ATOM   822  C  CD2   . TYR A 1 109 ? 30.514 11.156 26.911  1.00 13.14 ?  107 TYR A CD2   1 
ATOM   823  C  CE1   . TYR A 1 109 ? 28.997 8.973  27.649  1.00 11.33 ?  107 TYR A CE1   1 
ATOM   824  C  CE2   . TYR A 1 109 ? 29.255 10.965 26.359  1.00 12.29 ?  107 TYR A CE2   1 
ATOM   825  C  CZ    . TYR A 1 109 ? 28.524 9.863  26.710  1.00 12.08 ?  107 TYR A CZ    1 
ATOM   826  O  OH    . TYR A 1 109 ? 27.295 9.717  26.099  1.00 13.53 ?  107 TYR A OH    1 
ATOM   827  N  N     . GLN A 1 110 ? 34.065 10.057 31.020  1.00 9.09  ?  108 GLN A N     1 
ATOM   828  C  CA    . GLN A 1 110 ? 35.449 9.634  31.322  1.00 8.33  ?  108 GLN A CA    1 
ATOM   829  C  C     . GLN A 1 110 ? 35.750 8.607  30.249  1.00 8.74  ?  108 GLN A C     1 
ATOM   830  O  O     . GLN A 1 110 ? 34.970 7.687  30.070  1.00 9.31  ?  108 GLN A O     1 
ATOM   831  C  CB    . GLN A 1 110 ? 35.577 8.992  32.704  1.00 9.29  ?  108 GLN A CB    1 
ATOM   832  C  CG    . GLN A 1 110 ? 34.832 9.654  33.841  1.00 9.67  ?  108 GLN A CG    1 
ATOM   833  C  CD    . GLN A 1 110 ? 35.439 10.972 34.253  1.00 9.90  ?  108 GLN A CD    1 
ATOM   834  O  OE1   . GLN A 1 110 ? 36.318 11.509 33.593  1.00 10.07 ?  108 GLN A OE1   1 
ATOM   835  N  NE2   . GLN A 1 110 ? 35.080 11.466 35.439  1.00 10.18 ?  108 GLN A NE2   1 
ATOM   836  N  N     . VAL A 1 111 ? 36.900 8.753  29.589  1.00 8.85  ?  109 VAL A N     1 
ATOM   837  C  CA    . VAL A 1 111 ? 37.200 7.853  28.454  1.00 8.52  ?  109 VAL A CA    1 
ATOM   838  C  C     . VAL A 1 111 ? 38.604 7.282  28.576  1.00 8.15  ?  109 VAL A C     1 
ATOM   839  O  O     . VAL A 1 111 ? 39.568 7.979  28.852  1.00 8.61  ?  109 VAL A O     1 
ATOM   840  C  CB    . VAL A 1 111 ? 37.037 8.535  27.086  1.00 7.63  ?  109 VAL A CB    1 
ATOM   841  C  CG1   . VAL A 1 111 ? 35.631 9.089  26.930  1.00 8.98  ?  109 VAL A CG1   1 
ATOM   842  C  CG2   . VAL A 1 111 ? 38.051 9.658  26.869  1.00 8.91  ?  109 VAL A CG2   1 
ATOM   843  N  N     . ARG A 1 112 ? 38.748 5.978  28.273  1.00 8.14  ?  110 ARG A N     1 
ATOM   844  C  CA    . ARG A 1 112 ? 40.043 5.424  27.918  1.00 8.47  ?  110 ARG A CA    1 
ATOM   845  C  C     . ARG A 1 112 ? 40.381 5.971  26.531  1.00 7.96  ?  110 ARG A C     1 
ATOM   846  O  O     . ARG A 1 112 ? 39.632 5.798  25.554  1.00 8.73  ?  110 ARG A O     1 
ATOM   847  C  CB    . ARG A 1 112 ? 39.982 3.891  27.940  1.00 9.19  ?  110 ARG A CB    1 
ATOM   848  C  CG    . ARG A 1 112 ? 41.376 3.303  27.764  1.00 11.82 ?  110 ARG A CG    1 
ATOM   849  C  CD    . ARG A 1 112 ? 41.412 1.803  28.131  1.00 12.47 ?  110 ARG A CD    1 
ATOM   850  N  NE    . ARG A 1 112 ? 40.568 1.052  27.275  1.00 11.92 ?  110 ARG A NE    1 
ATOM   851  C  CZ    . ARG A 1 112 ? 40.030 -0.153 27.542  1.00 12.77 ?  110 ARG A CZ    1 
ATOM   852  N  NH1   . ARG A 1 112 ? 40.227 -0.700 28.716  1.00 10.86 ?  110 ARG A NH1   1 
ATOM   853  N  NH2   . ARG A 1 112 ? 39.267 -0.741 26.659  1.00 12.55 ?  110 ARG A NH2   1 
ATOM   854  N  N     . ARG A 1 113 ? 41.475 6.710  26.475  1.00 7.28  ?  111 ARG A N     1 
ATOM   855  C  CA    . ARG A 1 113 ? 41.778 7.482  25.278  1.00 7.34  ?  111 ARG A CA    1 
ATOM   856  C  C     . ARG A 1 113 ? 42.061 6.690  24.045  1.00 7.94  ?  111 ARG A C     1 
ATOM   857  O  O     . ARG A 1 113 ? 41.742 7.123  22.926  1.00 8.29  ?  111 ARG A O     1 
ATOM   858  C  CB    . ARG A 1 113 ? 42.857 8.520  25.550  1.00 7.44  ?  111 ARG A CB    1 
ATOM   859  C  CG    . ARG A 1 113 ? 42.353 9.738  26.298  1.00 7.30  ?  111 ARG A CG    1 
ATOM   860  C  CD    . ARG A 1 113 ? 41.523 10.746 25.475  1.00 7.99  ?  111 ARG A CD    1 
ATOM   861  N  NE    . ARG A 1 113 ? 42.282 11.227 24.328  1.00 8.63  ?  111 ARG A NE    1 
ATOM   862  C  CZ    . ARG A 1 113 ? 43.352 12.002 24.399  1.00 7.81  ?  111 ARG A CZ    1 
ATOM   863  N  NH1   . ARG A 1 113 ? 43.643 12.708 25.491  1.00 8.62  ?  111 ARG A NH1   1 
ATOM   864  N  NH2   . ARG A 1 113 ? 43.974 12.315 23.270  1.00 9.25  ?  111 ARG A NH2   1 
ATOM   865  N  N     . ALA A 1 114 ? 42.667 5.532  24.233  1.00 7.90  ?  112 ALA A N     1 
ATOM   866  C  CA    . ALA A 1 114 ? 42.916 4.703  23.033  1.00 7.65  ?  112 ALA A CA    1 
ATOM   867  C  C     . ALA A 1 114 ? 41.589 4.498  22.297  1.00 7.62  ?  112 ALA A C     1 
ATOM   868  O  O     . ALA A 1 114 ? 41.493 4.627  21.076  1.00 8.06  ?  112 ALA A O     1 
ATOM   869  C  CB    . ALA A 1 114 ? 43.518 3.379  23.453  1.00 8.58  ?  112 ALA A CB    1 
ATOM   870  N  N     . ASP A 1 115 ? 40.542 4.122  23.027  1.00 8.46  ?  113 ASP A N     1 
ATOM   871  C  CA    . ASP A 1 115 ? 39.235 3.799  22.465  1.00 9.06  ?  113 ASP A CA    1 
ATOM   872  C  C     . ASP A 1 115 ? 38.560 5.041  21.900  1.00 8.81  ?  113 ASP A C     1 
ATOM   873  O  O     . ASP A 1 115 ? 37.992 5.002  20.814  1.00 10.08 ?  113 ASP A O     1 
ATOM   874  C  CB    . ASP A 1 115 ? 38.396 3.150  23.577  1.00 9.94  ?  113 ASP A CB    1 
ATOM   875  C  CG    . ASP A 1 115 ? 39.085 2.002  24.311  1.00 12.35 ?  113 ASP A CG    1 
ATOM   876  O  OD1   . ASP A 1 115 ? 40.200 2.176  24.839  1.00 13.63 ?  113 ASP A OD1   1 
ATOM   877  O  OD2   . ASP A 1 115 ? 38.366 0.973  24.468  1.00 16.52 ?  113 ASP A OD2   1 
ATOM   878  N  N     . PHE A 1 116 ? 38.629 6.167  22.641  1.00 8.24  ?  114 PHE A N     1 
ATOM   879  C  CA    . PHE A 1 116 ? 37.984 7.416  22.204  1.00 7.94  ?  114 PHE A CA    1 
ATOM   880  C  C     . PHE A 1 116 ? 38.677 7.889  20.941  1.00 8.45  ?  114 PHE A C     1 
ATOM   881  O  O     . PHE A 1 116 ? 38.014 8.266  19.953  1.00 7.81  ?  114 PHE A O     1 
ATOM   882  C  CB    . PHE A 1 116 ? 38.095 8.438  23.339  1.00 8.19  ?  114 PHE A CB    1 
ATOM   883  C  CG    . PHE A 1 116 ? 37.461 9.754  23.001  1.00 8.04  ?  114 PHE A CG    1 
ATOM   884  C  CD1   . PHE A 1 116 ? 36.087 9.904  22.950  1.00 8.96  ?  114 PHE A CD1   1 
ATOM   885  C  CD2   . PHE A 1 116 ? 38.250 10.855 22.738  1.00 9.16  ?  114 PHE A CD2   1 
ATOM   886  C  CE1   . PHE A 1 116 ? 35.499 11.122 22.653  1.00 8.73  ?  114 PHE A CE1   1 
ATOM   887  C  CE2   . PHE A 1 116 ? 37.668 12.079 22.448  1.00 8.84  ?  114 PHE A CE2   1 
ATOM   888  C  CZ    . PHE A 1 116 ? 36.307 12.215 22.439  1.00 8.15  ?  114 PHE A CZ    1 
ATOM   889  N  N     . ASP A 1 117 ? 39.996 7.948  20.940  1.00 7.52  ?  115 ASP A N     1 
ATOM   890  C  CA    . ASP A 1 117 ? 40.715 8.522  19.804  1.00 7.58  ?  115 ASP A CA    1 
ATOM   891  C  C     . ASP A 1 117 ? 40.483 7.634  18.604  1.00 8.12  ?  115 ASP A C     1 
ATOM   892  O  O     . ASP A 1 117 ? 40.427 8.114  17.441  1.00 8.41  ?  115 ASP A O     1 
ATOM   893  C  CB    . ASP A 1 117 ? 42.206 8.682  20.095  1.00 7.29  ?  115 ASP A CB    1 
ATOM   894  C  CG    . ASP A 1 117 ? 42.495 9.712  21.188  1.00 8.75  ?  115 ASP A CG    1 
ATOM   895  O  OD1   . ASP A 1 117 ? 41.552 10.263 21.775  1.00 9.85  ?  115 ASP A OD1   1 
ATOM   896  O  OD2   . ASP A 1 117 ? 43.740 9.940  21.413  1.00 8.54  ?  115 ASP A OD2   1 
ATOM   897  N  N     . ALA A 1 118 ? 40.342 6.316  18.794  1.00 7.80  ?  116 ALA A N     1 
ATOM   898  C  CA    . ALA A 1 118 ? 40.084 5.412  17.650  1.00 8.41  ?  116 ALA A CA    1 
ATOM   899  C  C     . ALA A 1 118 ? 38.660 5.599  17.118  1.00 8.49  ?  116 ALA A C     1 
ATOM   900  O  O     . ALA A 1 118 ? 38.472 5.520  15.911  1.00 8.97  ?  116 ALA A O     1 
ATOM   901  C  CB    . ALA A 1 118 ? 40.324 3.968  18.044  1.00 8.50  ?  116 ALA A CB    1 
ATOM   902  N  N     . LEU A 1 119 ? 37.705 5.861  17.961  1.00 8.58  ?  117 LEU A N     1 
ATOM   903  C  CA    . LEU A 1 119 ? 36.339 6.179  17.495  1.00 8.69  ?  117 LEU A CA    1 
ATOM   904  C  C     . LEU A 1 119 ? 36.426 7.379  16.567  1.00 9.77  ?  117 LEU A C     1 
ATOM   905  O  O     . LEU A 1 119 ? 35.853 7.383  15.470  1.00 9.16  ?  117 LEU A O     1 
ATOM   906  C  CB    . LEU A 1 119 ? 35.451 6.467  18.693  1.00 9.68  ?  117 LEU A CB    1 
ATOM   907  C  CG    . LEU A 1 119 ? 34.022 6.873  18.330  1.00 11.05 ?  117 LEU A CG    1 
ATOM   908  C  CD1   . LEU A 1 119 ? 33.307 5.668  17.722  1.00 12.29 ?  117 LEU A CD1   1 
ATOM   909  C  CD2   . LEU A 1 119 ? 33.313 7.432  19.536  1.00 12.84 ?  117 LEU A CD2   1 
ATOM   910  N  N     . LEU A 1 120 ? 37.129 8.420  17.001  1.00 8.73  ?  118 LEU A N     1 
ATOM   911  C  CA    . LEU A 1 120 ? 37.161 9.661  16.179  1.00 9.21  ?  118 LEU A CA    1 
ATOM   912  C  C     . LEU A 1 120 ? 37.918 9.443  14.894  1.00 8.68  ?  118 LEU A C     1 
ATOM   913  O  O     . LEU A 1 120 ? 37.542 9.952  13.838  1.00 9.18  ?  118 LEU A O     1 
ATOM   914  C  CB    . LEU A 1 120 ? 37.769 10.791 16.994  1.00 9.97  ?  118 LEU A CB    1 
ATOM   915  C  CG    . LEU A 1 120 ? 36.841 11.542 17.951  1.00 13.76 ?  118 LEU A CG    1 
ATOM   916  C  CD1   . LEU A 1 120 ? 36.024 10.732 18.905  1.00 17.46 ?  118 LEU A CD1   1 
ATOM   917  C  CD2   . LEU A 1 120 ? 37.714 12.568 18.732  1.00 14.03 ?  118 LEU A CD2   1 
ATOM   918  N  N     . LEU A 1 121 ? 39.036 8.720  14.919  1.00 7.69  ?  119 LEU A N     1 
ATOM   919  C  CA    . LEU A 1 121 ? 39.841 8.510  13.700  1.00 8.46  ?  119 LEU A CA    1 
ATOM   920  C  C     . LEU A 1 121 ? 39.070 7.601  12.758  1.00 9.08  ?  119 LEU A C     1 
ATOM   921  O  O     . LEU A 1 121 ? 39.076 7.833  11.534  1.00 9.15  ?  119 LEU A O     1 
ATOM   922  C  CB    . LEU A 1 121 ? 41.213 7.945  14.041  1.00 9.31  ?  119 LEU A CB    1 
ATOM   923  C  CG    . LEU A 1 121 ? 42.183 7.967  12.875  1.00 10.08 ?  119 LEU A CG    1 
ATOM   924  C  CD1   . LEU A 1 121 ? 42.453 9.365  12.403  1.00 10.86 ?  119 LEU A CD1   1 
ATOM   925  C  CD2   . LEU A 1 121 ? 43.471 7.293  13.321  1.00 11.03 ?  119 LEU A CD2   1 
ATOM   926  N  N     . ASP A 1 122 ? 38.417 6.562  13.254  1.00 8.71  ?  120 ASP A N     1 
ATOM   927  C  CA    . ASP A 1 122 ? 37.653 5.675  12.402  1.00 9.63  ?  120 ASP A CA    1 
ATOM   928  C  C     . ASP A 1 122 ? 36.535 6.517  11.745  1.00 9.56  ?  120 ASP A C     1 
ATOM   929  O  O     . ASP A 1 122 ? 36.226 6.336  10.561  1.00 9.32  ?  120 ASP A O     1 
ATOM   930  C  CB    . ASP A 1 122 ? 37.019 4.542  13.225  1.00 10.14 ?  120 ASP A CB    1 
ATOM   931  C  CG    . ASP A 1 122 ? 37.976 3.417  13.611  1.00 11.89 ?  120 ASP A CG    1 
ATOM   932  O  OD1   . ASP A 1 122 ? 39.063 3.324  13.003  1.00 11.88 ?  120 ASP A OD1   1 
ATOM   933  O  OD2   . ASP A 1 122 ? 37.636 2.631  14.521  1.00 13.31 ?  120 ASP A OD2   1 
ATOM   934  N  N     . ARG A 1 123 ? 35.948 7.454  12.502  1.00 9.72  ?  121 ARG A N     1 
ATOM   935  C  CA    . ARG A 1 123 ? 34.837 8.287  11.966  1.00 9.20  ?  121 ARG A CA    1 
ATOM   936  C  C     . ARG A 1 123 ? 35.430 9.230  10.899  1.00 10.21 ?  121 ARG A C     1 
ATOM   937  O  O     . ARG A 1 123 ? 34.807 9.430  9.847   1.00 9.67  ?  121 ARG A O     1 
ATOM   938  C  CB    . ARG A 1 123 ? 34.186 9.119  13.052  1.00 9.59  ?  121 ARG A CB    1 
ATOM   939  C  CG    . ARG A 1 123 ? 33.067 9.976  12.510  1.00 10.34 ?  121 ARG A CG    1 
ATOM   940  C  CD    . ARG A 1 123 ? 31.963 9.229  11.832  1.00 11.00 ?  121 ARG A CD    1 
ATOM   941  N  NE    . ARG A 1 123 ? 30.857 10.139 11.568  1.00 11.63 ?  121 ARG A NE    1 
ATOM   942  C  CZ    . ARG A 1 123 ? 29.937 9.848  10.659  1.00 14.15 ?  121 ARG A CZ    1 
ATOM   943  N  NH1   . ARG A 1 123 ? 30.002 8.748  9.945   1.00 15.05 ?  121 ARG A NH1   1 
ATOM   944  N  NH2   . ARG A 1 123 ? 28.976 10.716 10.421  1.00 14.92 ?  121 ARG A NH2   1 
ATOM   945  N  N     . ALA A 1 124 ? 36.621 9.763  11.089  1.00 9.86  ?  122 ALA A N     1 
ATOM   946  C  CA    . ALA A 1 124 ? 37.219 10.616 10.063  1.00 10.35 ?  122 ALA A CA    1 
ATOM   947  C  C     . ALA A 1 124 ? 37.374 9.841  8.772   1.00 9.87  ?  122 ALA A C     1 
ATOM   948  O  O     . ALA A 1 124 ? 37.009 10.334 7.683   1.00 10.70 ?  122 ALA A O     1 
ATOM   949  C  CB    . ALA A 1 124 ? 38.546 11.146 10.498  1.00 11.19 ?  122 ALA A CB    1 
ATOM   950  N  N     . ARG A 1 125 ? 37.821 8.602  8.840   1.00 9.11  ?  123 ARG A N     1 
ATOM   951  C  CA    . ARG A 1 125 ? 37.944 7.760  7.665   1.00 10.45 ?  123 ARG A CA    1 
ATOM   952  C  C     . ARG A 1 125 ? 36.571 7.528  7.020   1.00 10.75 ?  123 ARG A C     1 
ATOM   953  O  O     . ARG A 1 125 ? 36.419 7.612  5.794   1.00 10.93 ?  123 ARG A O     1 
ATOM   954  C  CB    . ARG A 1 125 ? 38.571 6.427  8.045   1.00 11.81 ?  123 ARG A CB    1 
ATOM   955  C  CG    . ARG A 1 125 ? 38.984 5.655  6.834   1.00 13.88 ?  123 ARG A CG    1 
ATOM   956  C  CD    . ARG A 1 125 ? 39.540 4.274  7.212   1.00 13.24 ?  123 ARG A CD    1 
ATOM   957  N  NE    . ARG A 1 125 ? 40.710 4.354  8.093   1.00 12.11 ?  123 ARG A NE    1 
ATOM   958  C  CZ    . ARG A 1 125 ? 40.722 4.236  9.419   1.00 14.78 ?  123 ARG A CZ    1 
ATOM   959  N  NH1   . ARG A 1 125 ? 39.591 4.022  10.078  1.00 15.83 ?  123 ARG A NH1   1 
ATOM   960  N  NH2   . ARG A 1 125 ? 41.865 4.332  10.085  1.00 17.17 ?  123 ARG A NH2   1 
ATOM   961  N  N     . GLU A 1 126 ? 35.565 7.234  7.835   1.00 10.22 ?  124 GLU A N     1 
ATOM   962  C  CA    . GLU A 1 126 ? 34.228 7.002  7.303   1.00 11.22 ?  124 GLU A CA    1 
ATOM   963  C  C     . GLU A 1 126 ? 33.723 8.214  6.549   1.00 11.83 ?  124 GLU A C     1 
ATOM   964  O  O     . GLU A 1 126 ? 32.981 8.095  5.601   1.00 12.78 ?  124 GLU A O     1 
ATOM   965  C  CB    . GLU A 1 126 ? 33.238 6.758  8.419   1.00 12.06 ?  124 GLU A CB    1 
ATOM   966  C  CG    . GLU A 1 126 ? 33.418 5.536  9.211   1.00 19.43 ?  124 GLU A CG    1 
ATOM   967  C  CD    . GLU A 1 126 ? 32.574 5.520  10.506  1.00 24.19 ?  124 GLU A CD    1 
ATOM   968  O  OE1   . GLU A 1 126 ? 31.434 6.028  10.480  1.00 16.19 ?  124 GLU A OE1   1 
ATOM   969  O  OE2   . GLU A 1 126 ? 33.064 4.999  11.530  1.00 25.89 ?  124 GLU A OE2   1 
ATOM   970  N  N     . LEU A 1 127 ? 34.087 9.390  7.025   1.00 10.47 ?  125 LEU A N     1 
ATOM   971  C  CA    . LEU A 1 127 ? 33.661 10.680 6.390   1.00 10.56 ?  125 LEU A CA    1 
ATOM   972  C  C     . LEU A 1 127 ? 34.438 10.958 5.114   1.00 12.27 ?  125 LEU A C     1 
ATOM   973  O  O     . LEU A 1 127 ? 34.053 11.926 4.401   1.00 13.33 ?  125 LEU A O     1 
ATOM   974  C  CB    . LEU A 1 127 ? 33.775 11.815 7.397   1.00 11.85 ?  125 LEU A CB    1 
ATOM   975  C  CG    . LEU A 1 127 ? 32.747 11.757 8.519   1.00 12.03 ?  125 LEU A CG    1 
ATOM   976  C  CD1   . LEU A 1 127 ? 33.044 12.736 9.612   1.00 12.85 ?  125 LEU A CD1   1 
ATOM   977  C  CD2   . LEU A 1 127 ? 31.323 11.979 7.990   1.00 14.39 ?  125 LEU A CD2   1 
ATOM   978  N  N     . GLY A 1 128 ? 35.452 10.210 4.783   1.00 11.20 ?  126 GLY A N     1 
ATOM   979  C  CA    . GLY A 1 128 ? 36.229 10.314 3.547   1.00 10.92 ?  126 GLY A CA    1 
ATOM   980  C  C     . GLY A 1 128 ? 37.680 10.720 3.676   1.00 9.94  ?  126 GLY A C     1 
ATOM   981  O  O     . GLY A 1 128 ? 38.331 10.906 2.651   1.00 12.74 ?  126 GLY A O     1 
ATOM   982  N  N     . VAL A 1 129 ? 38.170 10.884 4.892   1.00 9.59  ?  127 VAL A N     1 
ATOM   983  C  CA    . VAL A 1 129 ? 39.591 11.185 5.056   1.00 8.65  ?  127 VAL A CA    1 
ATOM   984  C  C     . VAL A 1 129 ? 40.417 9.973  4.659   1.00 8.31  ?  127 VAL A C     1 
ATOM   985  O  O     . VAL A 1 129 ? 40.082 8.852  5.048   1.00 9.15  ?  127 VAL A O     1 
ATOM   986  C  CB    . VAL A 1 129 ? 39.875 11.587 6.517   1.00 8.40  ?  127 VAL A CB    1 
ATOM   987  C  CG1   . VAL A 1 129 ? 41.341 11.879 6.766   1.00 8.77  ?  127 VAL A CG1   1 
ATOM   988  C  CG2   . VAL A 1 129 ? 39.037 12.795 6.896   1.00 8.83  ?  127 VAL A CG2   1 
ATOM   989  N  N     . THR A 1 130 ? 41.501 10.187 3.960   1.00 9.01  ?  128 THR A N     1 
ATOM   990  C  CA    . THR A 1 130 ? 42.535 9.159  3.713   1.00 7.82  ?  128 THR A CA    1 
ATOM   991  C  C     . THR A 1 130 ? 43.427 9.196  4.932   1.00 9.05  ?  128 THR A C     1 
ATOM   992  O  O     . THR A 1 130 ? 44.246 10.096 5.059   1.00 9.09  ?  128 THR A O     1 
ATOM   993  C  CB    . THR A 1 130 ? 43.288 9.351  2.411   1.00 9.33  ?  128 THR A CB    1 
ATOM   994  O  OG1   . THR A 1 130 ? 42.355 9.282  1.311   1.00 11.10 ?  128 THR A OG1   1 
ATOM   995  C  CG2   . THR A 1 130 ? 44.381 8.326  2.254   1.00 10.12 ?  128 THR A CG2   1 
ATOM   996  N  N     . VAL A 1 131 ? 43.326 8.219  5.804   1.00 8.73  ?  129 VAL A N     1 
ATOM   997  C  CA    . VAL A 1 131 ? 44.107 8.126  7.058   1.00 8.38  ?  129 VAL A CA    1 
ATOM   998  C  C     . VAL A 1 131 ? 45.235 7.169  6.792   1.00 8.04  ?  129 VAL A C     1 
ATOM   999  O  O     . VAL A 1 131 ? 44.962 5.988  6.502   1.00 8.68  ?  129 VAL A O     1 
ATOM   1000 C  CB    . VAL A 1 131 ? 43.265 7.689  8.246   1.00 8.75  ?  129 VAL A CB    1 
ATOM   1001 C  CG1   . VAL A 1 131 ? 44.130 7.449  9.473   1.00 8.88  ?  129 VAL A CG1   1 
ATOM   1002 C  CG2   . VAL A 1 131 ? 42.133 8.659  8.512   1.00 9.67  ?  129 VAL A CG2   1 
ATOM   1003 N  N     . LEU A 1 132 ? 46.436 7.612  6.927   1.00 8.07  ?  130 LEU A N     1 
ATOM   1004 C  CA    . LEU A 1 132 ? 47.652 6.771  6.812   1.00 8.98  ?  130 LEU A CA    1 
ATOM   1005 C  C     . LEU A 1 132 ? 48.186 6.561  8.198   1.00 9.97  ?  130 LEU A C     1 
ATOM   1006 O  O     . LEU A 1 132 ? 48.591 7.531  8.833   1.00 11.97 ?  130 LEU A O     1 
ATOM   1007 C  CB    . LEU A 1 132 ? 48.740 7.359  5.919   1.00 10.13 ?  130 LEU A CB    1 
ATOM   1008 C  CG    . LEU A 1 132 ? 48.293 7.748  4.521   1.00 12.39 ?  130 LEU A CG    1 
ATOM   1009 C  CD1   . LEU A 1 132 ? 49.468 8.172  3.643   1.00 13.42 ?  130 LEU A CD1   1 
ATOM   1010 C  CD2   . LEU A 1 132 ? 47.500 6.693  3.813   1.00 12.54 ?  130 LEU A CD2   1 
ATOM   1011 N  N     . GLU A 1 133 ? 48.285 5.332  8.652   1.00 7.81  ?  131 GLU A N     1 
ATOM   1012 C  CA    . GLU A 1 133 ? 48.915 4.973  9.930   1.00 8.38  ?  131 GLU A CA    1 
ATOM   1013 C  C     . GLU A 1 133 ? 50.354 4.512  9.694   1.00 8.41  ?  131 GLU A C     1 
ATOM   1014 O  O     . GLU A 1 133 ? 50.735 4.075  8.563   1.00 10.11 ?  131 GLU A O     1 
ATOM   1015 C  CB    . GLU A 1 133 ? 48.115 3.878  10.635  1.00 9.16  ?  131 GLU A CB    1 
ATOM   1016 C  CG    . GLU A 1 133 ? 46.802 4.348  11.185  1.00 11.24 ?  131 GLU A CG    1 
ATOM   1017 C  CD    . GLU A 1 133 ? 45.942 3.233  11.720  1.00 12.50 ?  131 GLU A CD    1 
ATOM   1018 O  OE1   . GLU A 1 133 ? 45.645 3.257  12.918  1.00 13.41 ?  131 GLU A OE1   1 
ATOM   1019 O  OE2   . GLU A 1 133 ? 45.631 2.291  10.959  1.00 14.75 ?  131 GLU A OE2   1 
ATOM   1020 N  N     . GLY A 1 134 ? 51.179 4.653  10.699  1.00 8.25  ?  132 GLY A N     1 
ATOM   1021 C  CA    . GLY A 1 134 ? 52.605 4.399  10.577  1.00 8.78  ?  132 GLY A CA    1 
ATOM   1022 C  C     . GLY A 1 134 ? 53.369 5.416  9.778   1.00 9.17  ?  132 GLY A C     1 
ATOM   1023 O  O     . GLY A 1 134 ? 54.515 5.150  9.362   1.00 10.47 ?  132 GLY A O     1 
ATOM   1024 N  N     . ALA A 1 135 ? 52.792 6.594  9.573   1.00 9.17  ?  133 ALA A N     1 
ATOM   1025 C  CA    . ALA A 1 135 ? 53.345 7.648  8.712   1.00 9.78  ?  133 ALA A CA    1 
ATOM   1026 C  C     . ALA A 1 135 ? 53.813 8.791  9.608   1.00 9.83  ?  133 ALA A C     1 
ATOM   1027 O  O     . ALA A 1 135 ? 52.982 9.410  10.287  1.00 10.60 ?  133 ALA A O     1 
ATOM   1028 C  CB    . ALA A 1 135 ? 52.315 8.155  7.753   1.00 10.74 ?  133 ALA A CB    1 
ATOM   1029 N  N     . SER A 1 136 ? 55.114 9.011  9.668   1.00 9.73  ?  134 SER A N     1 
ATOM   1030 C  CA    . SER A 1 136 ? 55.707 10.033 10.557  1.00 10.94 ?  134 SER A CA    1 
ATOM   1031 C  C     . SER A 1 136 ? 56.103 11.205 9.690   1.00 10.52 ?  134 SER A C     1 
ATOM   1032 O  O     . SER A 1 136 ? 57.024 11.078 8.837   1.00 10.89 ?  134 SER A O     1 
ATOM   1033 C  CB    . SER A 1 136 ? 56.906 9.536  11.246  1.00 12.44 ?  134 SER A CB    1 
ATOM   1034 O  OG    . SER A 1 136 ? 56.599 8.481  12.147  1.00 21.00 ?  134 SER A OG    1 
ATOM   1035 N  N     . VAL A 1 137 ? 55.483 12.357 9.886   1.00 8.83  ?  135 VAL A N     1 
ATOM   1036 C  CA    . VAL A 1 137 ? 55.922 13.566 9.178   1.00 8.97  ?  135 VAL A CA    1 
ATOM   1037 C  C     . VAL A 1 137 ? 57.280 14.000 9.701   1.00 10.24 ?  135 VAL A C     1 
ATOM   1038 O  O     . VAL A 1 137 ? 57.452 14.135 10.905  1.00 11.29 ?  135 VAL A O     1 
ATOM   1039 C  CB    . VAL A 1 137 ? 54.836 14.636 9.230   1.00 9.77  ?  135 VAL A CB    1 
ATOM   1040 C  CG1   . VAL A 1 137 ? 55.354 15.935 8.725   1.00 10.60 ?  135 VAL A CG1   1 
ATOM   1041 C  CG2   . VAL A 1 137 ? 53.621 14.120 8.481   1.00 12.54 ?  135 VAL A CG2   1 
ATOM   1042 N  N     . LYS A 1 138 ? 58.184 14.261 8.788   1.00 9.81  ?  136 LYS A N     1 
ATOM   1043 C  CA    . LYS A 1 138 ? 59.567 14.645 9.101   1.00 12.23 ?  136 LYS A CA    1 
ATOM   1044 C  C     . LYS A 1 138 ? 59.791 16.144 8.940   1.00 13.88 ?  136 LYS A C     1 
ATOM   1045 O  O     . LYS A 1 138 ? 60.559 16.692 9.755   1.00 17.66 ?  136 LYS A O     1 
ATOM   1046 C  CB    . LYS A 1 138 ? 60.556 13.864 8.267   1.00 14.82 ?  136 LYS A CB    1 
ATOM   1047 C  CG    . LYS A 1 138 ? 60.497 12.333 8.386   1.00 19.58 ?  136 LYS A CG    1 
ATOM   1048 C  CD    . LYS A 1 138 ? 60.537 11.832 9.822   1.00 26.70 ?  136 LYS A CD    1 
ATOM   1049 C  CE    . LYS A 1 138 ? 61.828 12.104 10.555  1.00 33.19 ?  136 LYS A CE    1 
ATOM   1050 N  NZ    . LYS A 1 138 ? 61.801 11.502 11.911  1.00 42.50 ?  136 LYS A NZ    1 
ATOM   1051 N  N     . GLU A 1 139 ? 59.335 16.722 7.863   1.00 13.17 ?  137 GLU A N     1 
ATOM   1052 C  CA    . GLU A 1 139 ? 59.585 18.153 7.614   1.00 13.13 ?  137 GLU A CA    1 
ATOM   1053 C  C     . GLU A 1 139 ? 58.536 18.653 6.670   1.00 11.54 ?  137 GLU A C     1 
ATOM   1054 O  O     . GLU A 1 139 ? 57.950 17.941 5.848   1.00 11.60 ?  137 GLU A O     1 
ATOM   1055 C  CB    . GLU A 1 139 ? 60.956 18.433 7.093   1.00 18.71 ?  137 GLU A CB    1 
ATOM   1056 C  CG    . GLU A 1 139 ? 61.177 17.878 5.771   1.00 19.50 ?  137 GLU A CG    1 
ATOM   1057 C  CD    . GLU A 1 139 ? 62.688 17.893 5.487   1.00 30.23 ?  137 GLU A CD    1 
ATOM   1058 O  OE1   . GLU A 1 139 ? 63.145 17.149 4.578   1.00 34.29 ?  137 GLU A OE1   1 
ATOM   1059 O  OE2   . GLU A 1 139 ? 63.401 18.630 6.191   1.00 39.98 ?  137 GLU A OE2   1 
ATOM   1060 N  N     . PRO A 1 140 ? 58.218 19.938 6.774   1.00 9.79  ?  138 PRO A N     1 
ATOM   1061 C  CA    . PRO A 1 140 ? 57.358 20.577 5.813   1.00 10.44 ?  138 PRO A CA    1 
ATOM   1062 C  C     . PRO A 1 140 ? 58.045 20.861 4.488   1.00 11.07 ?  138 PRO A C     1 
ATOM   1063 O  O     . PRO A 1 140 ? 59.285 20.903 4.451   1.00 13.13 ?  138 PRO A O     1 
ATOM   1064 C  CB    . PRO A 1 140 ? 56.987 21.911 6.487   1.00 10.93 ?  138 PRO A CB    1 
ATOM   1065 C  CG    . PRO A 1 140 ? 57.727 21.944 7.774   1.00 12.01 ?  138 PRO A CG    1 
ATOM   1066 C  CD    . PRO A 1 140 ? 58.795 20.878 7.751   1.00 11.96 ?  138 PRO A CD    1 
ATOM   1067 N  N     . LEU A 1 141 ? 57.249 20.981 3.435   1.00 10.12 ?  139 LEU A N     1 
ATOM   1068 C  CA    . LEU A 1 141 ? 57.733 21.409 2.122   1.00 10.70 ?  139 LEU A CA    1 
ATOM   1069 C  C     . LEU A 1 141 ? 57.266 22.820 1.885   1.00 10.62 ?  139 LEU A C     1 
ATOM   1070 O  O     . LEU A 1 141 ? 56.105 23.109 2.159   1.00 10.98 ?  139 LEU A O     1 
ATOM   1071 C  CB    . LEU A 1 141 ? 57.248 20.475 1.018   1.00 12.34 ?  139 LEU A CB    1 
ATOM   1072 C  CG    . LEU A 1 141 ? 57.659 19.017 1.194   1.00 14.38 ?  139 LEU A CG    1 
ATOM   1073 C  CD1   . LEU A 1 141 ? 56.934 18.151 0.176   1.00 15.67 ?  139 LEU A CD1   1 
ATOM   1074 C  CD2   . LEU A 1 141 ? 59.151 18.861 1.164   1.00 17.24 ?  139 LEU A CD2   1 
ATOM   1075 N  N     . PHE A 1 142 ? 58.116 23.628 1.271   1.00 10.91 ?  140 PHE A N     1 
ATOM   1076 C  CA    . PHE A 1 142 ? 57.796 25.046 1.057   1.00 10.53 ?  140 PHE A CA    1 
ATOM   1077 C  C     . PHE A 1 142 ? 58.003 25.505 -0.381  1.00 12.07 ?  140 PHE A C     1 
ATOM   1078 O  O     . PHE A 1 142 ? 58.841 24.956 -1.119  1.00 15.20 ?  140 PHE A O     1 
ATOM   1079 C  CB    . PHE A 1 142 ? 58.728 25.879 1.914   1.00 11.17 ?  140 PHE A CB    1 
ATOM   1080 C  CG    . PHE A 1 142 ? 58.491 25.748 3.397   1.00 10.81 ?  140 PHE A CG    1 
ATOM   1081 C  CD1   . PHE A 1 142 ? 57.511 26.484 4.003   1.00 10.52 ?  140 PHE A CD1   1 
ATOM   1082 C  CD2   . PHE A 1 142 ? 59.246 24.923 4.197   1.00 11.37 ?  140 PHE A CD2   1 
ATOM   1083 C  CE1   . PHE A 1 142 ? 57.295 26.407 5.369   1.00 10.96 ?  140 PHE A CE1   1 
ATOM   1084 C  CE2   . PHE A 1 142 ? 59.016 24.815 5.538   1.00 11.80 ?  140 PHE A CE2   1 
ATOM   1085 C  CZ    . PHE A 1 142 ? 58.037 25.564 6.128   1.00 12.52 ?  140 PHE A CZ    1 
ATOM   1086 N  N     . ASP A 1 143 ? 57.206 26.478 -0.753  1.00 11.32 ?  141 ASP A N     1 
ATOM   1087 C  CA    . ASP A 1 143 ? 57.445 27.320 -1.980  1.00 13.41 ?  141 ASP A CA    1 
ATOM   1088 C  C     . ASP A 1 143 ? 57.622 28.744 -1.440  1.00 11.69 ?  141 ASP A C     1 
ATOM   1089 O  O     . ASP A 1 143 ? 56.618 29.371 -1.104  1.00 12.62 ?  141 ASP A O     1 
ATOM   1090 C  CB    . ASP A 1 143 ? 56.295 27.185 -2.980  1.00 14.97 ?  141 ASP A CB    1 
ATOM   1091 C  CG    . ASP A 1 143 ? 56.426 27.976 -4.280  1.00 20.05 ?  141 ASP A CG    1 
ATOM   1092 O  OD1   . ASP A 1 143 ? 57.408 28.686 -4.393  1.00 21.70 ?  141 ASP A OD1   1 
ATOM   1093 O  OD2   . ASP A 1 143 ? 55.509 27.842 -5.136  1.00 30.15 ?  141 ASP A OD2   1 
ATOM   1094 N  N     . GLY A 1 144 ? 58.849 29.177 -1.294  1.00 13.44 ?  142 GLY A N     1 
ATOM   1095 C  CA    . GLY A 1 144 ? 59.102 30.426 -0.555  1.00 13.28 ?  142 GLY A CA    1 
ATOM   1096 C  C     . GLY A 1 144 ? 58.666 30.231 0.873   1.00 12.95 ?  142 GLY A C     1 
ATOM   1097 O  O     . GLY A 1 144 ? 59.035 29.258 1.487   1.00 14.00 ?  142 GLY A O     1 
ATOM   1098 N  N     . ASP A 1 145 ? 57.876 31.160 1.387   1.00 11.81 ?  143 ASP A N     1 
ATOM   1099 C  CA    . ASP A 1 145 ? 57.390 31.022 2.781   1.00 12.85 ?  143 ASP A CA    1 
ATOM   1100 C  C     . ASP A 1 145 ? 56.200 30.093 2.833   1.00 11.34 ?  143 ASP A C     1 
ATOM   1101 O  O     . ASP A 1 145 ? 55.812 29.706 3.940   1.00 12.46 ?  143 ASP A O     1 
ATOM   1102 C  CB    . ASP A 1 145 ? 56.944 32.382 3.357   1.00 12.63 ?  143 ASP A CB    1 
ATOM   1103 C  CG    . ASP A 1 145 ? 58.060 33.339 3.669   1.00 14.55 ?  143 ASP A CG    1 
ATOM   1104 O  OD1   . ASP A 1 145 ? 59.251 32.912 3.704   1.00 17.50 ?  143 ASP A OD1   1 
ATOM   1105 O  OD2   . ASP A 1 145 ? 57.729 34.524 3.982   1.00 14.26 ?  143 ASP A OD2   1 
ATOM   1106 N  N     . ARG A 1 146 ? 55.491 29.799 1.750   1.00 10.48 ?  144 ARG A N     1 
ATOM   1107 C  CA    . ARG A 1 146 ? 54.219 29.070 1.818   1.00 9.74  ?  144 ARG A CA    1 
ATOM   1108 C  C     . ARG A 1 146 ? 54.500 27.583 2.003   1.00 10.10 ?  144 ARG A C     1 
ATOM   1109 O  O     . ARG A 1 146 ? 55.265 26.962 1.212   1.00 11.67 ?  144 ARG A O     1 
ATOM   1110 C  CB    . ARG A 1 146 ? 53.416 29.256 0.525   1.00 10.58 ?  144 ARG A CB    1 
ATOM   1111 C  CG    . ARG A 1 146 ? 52.050 28.643 0.591   1.00 12.23 ?  144 ARG A CG    1 
ATOM   1112 C  CD    . ARG A 1 146 ? 51.092 28.901 -0.577  1.00 13.14 ?  144 ARG A CD    1 
ATOM   1113 N  NE    . ARG A 1 146 ? 50.773 30.340 -0.619  1.00 13.51 ?  144 ARG A NE    1 
ATOM   1114 C  CZ    . ARG A 1 146 ? 49.944 30.963 0.174   1.00 14.78 ?  144 ARG A CZ    1 
ATOM   1115 N  NH1   . ARG A 1 146 ? 49.208 30.285 1.068   1.00 14.88 ?  144 ARG A NH1   1 
ATOM   1116 N  NH2   . ARG A 1 146 ? 49.887 32.294 0.108   1.00 15.53 ?  144 ARG A NH2   1 
ATOM   1117 N  N     . MET A 1 147 ? 53.887 26.983 3.003   1.00 9.04  ?  145 MET A N     1 
ATOM   1118 C  CA    . MET A 1 147 ? 53.909 25.521 3.139   1.00 8.68  ?  145 MET A CA    1 
ATOM   1119 C  C     . MET A 1 147 ? 53.058 24.975 2.002   1.00 9.04  ?  145 MET A C     1 
ATOM   1120 O  O     . MET A 1 147 ? 51.909 25.422 1.818   1.00 9.85  ?  145 MET A O     1 
ATOM   1121 C  CB    . MET A 1 147 ? 53.424 25.111 4.540   1.00 9.14  ?  145 MET A CB    1 
ATOM   1122 C  CG    . MET A 1 147 ? 53.787 23.628 4.797   1.00 8.96  ?  145 MET A CG    1 
ATOM   1123 S  SD    . MET A 1 147 ? 53.461 23.175 6.519   1.00 10.11 ?  145 MET A SD    1 
ATOM   1124 C  CE    . MET A 1 147 ? 54.536 24.305 7.378   1.00 10.94 ?  145 MET A CE    1 
ATOM   1125 N  N     . VAL A 1 148 ? 53.565 23.947 1.298   1.00 9.76  ?  146 VAL A N     1 
ATOM   1126 C  CA    . VAL A 1 148 ? 52.852 23.363 0.134   1.00 9.85  ?  146 VAL A CA    1 
ATOM   1127 C  C     . VAL A 1 148 ? 52.722 21.862 0.271   1.00 10.03 ?  146 VAL A C     1 
ATOM   1128 O  O     . VAL A 1 148 ? 52.245 21.214 -0.661  1.00 11.54 ?  146 VAL A O     1 
ATOM   1129 C  CB    . VAL A 1 148 ? 53.530 23.746 -1.192  1.00 10.55 ?  146 VAL A CB    1 
ATOM   1130 C  CG1   . VAL A 1 148 ? 53.412 25.262 -1.387  1.00 12.41 ?  146 VAL A CG1   1 
ATOM   1131 C  CG2   . VAL A 1 148 ? 54.983 23.334 -1.197  1.00 10.96 ?  146 VAL A CG2   1 
ATOM   1132 N  N     . GLY A 1 149 ? 53.176 21.284 1.374   1.00 9.97  ?  147 GLY A N     1 
ATOM   1133 C  CA    . GLY A 1 149 ? 53.046 19.837 1.578   1.00 11.40 ?  147 GLY A CA    1 
ATOM   1134 C  C     . GLY A 1 149 ? 53.980 19.416 2.688   1.00 10.22 ?  147 GLY A C     1 
ATOM   1135 O  O     . GLY A 1 149 ? 54.485 20.270 3.474   1.00 10.47 ?  147 GLY A O     1 
ATOM   1136 N  N     . VAL A 1 150 ? 54.210 18.113 2.800   1.00 10.14 ?  148 VAL A N     1 
ATOM   1137 C  CA    . VAL A 1 150 ? 55.077 17.534 3.834   1.00 9.79  ?  148 VAL A CA    1 
ATOM   1138 C  C     . VAL A 1 150 ? 55.863 16.383 3.229   1.00 9.57  ?  148 VAL A C     1 
ATOM   1139 O  O     . VAL A 1 150 ? 55.424 15.818 2.204   1.00 9.99  ?  148 VAL A O     1 
ATOM   1140 C  CB    . VAL A 1 150 ? 54.288 17.071 5.074   1.00 8.91  ?  148 VAL A CB    1 
ATOM   1141 C  CG1   . VAL A 1 150 ? 53.453 18.183 5.651   1.00 10.27 ?  148 VAL A CG1   1 
ATOM   1142 C  CG2   . VAL A 1 150 ? 53.413 15.883 4.783   1.00 10.23 ?  148 VAL A CG2   1 
ATOM   1143 N  N     . ARG A 1 151 ? 56.924 16.064 3.925   1.00 9.31  ?  149 ARG A N     1 
ATOM   1144 C  CA    . ARG A 1 151 ? 57.728 14.862 3.682   1.00 10.44 ?  149 ARG A CA    1 
ATOM   1145 C  C     . ARG A 1 151 ? 57.491 13.935 4.841   1.00 9.71  ?  149 ARG A C     1 
ATOM   1146 O  O     . ARG A 1 151 ? 57.679 14.344 6.008   1.00 10.29 ?  149 ARG A O     1 
ATOM   1147 C  CB    . ARG A 1 151 ? 59.202 15.218 3.541   1.00 11.01 ?  149 ARG A CB    1 
ATOM   1148 C  CG    . ARG A 1 151 ? 60.097 14.010 3.358   1.00 13.58 ?  149 ARG A CG    1 
ATOM   1149 C  CD    . ARG A 1 151 ? 61.485 14.470 2.929   1.00 16.12 ?  149 ARG A CD    1 
ATOM   1150 N  NE    . ARG A 1 151 ? 61.397 14.997 1.593   1.00 16.67 ?  149 ARG A NE    1 
ATOM   1151 C  CZ    . ARG A 1 151 ? 62.345 15.638 0.984   1.00 28.47 ?  149 ARG A CZ    1 
ATOM   1152 N  NH1   . ARG A 1 151 ? 63.521 15.770 1.577   1.00 33.04 ?  149 ARG A NH1   1 
ATOM   1153 N  NH2   . ARG A 1 151 ? 62.104 16.107 -0.226  1.00 29.86 ?  149 ARG A NH2   1 
ATOM   1154 N  N     . TYR A 1 152 ? 57.143 12.657 4.573   1.00 10.63 ?  150 TYR A N     1 
ATOM   1155 C  CA    . TYR A 1 152 ? 56.922 11.712 5.662   1.00 10.55 ?  150 TYR A CA    1 
ATOM   1156 C  C     . TYR A 1 152 ? 57.675 10.402 5.420   1.00 12.04 ?  150 TYR A C     1 
ATOM   1157 O  O     . TYR A 1 152 ? 58.048 10.124 4.296   1.00 12.65 ?  150 TYR A O     1 
ATOM   1158 C  CB    . TYR A 1 152 ? 55.432 11.459 5.882   1.00 10.64 ?  150 TYR A CB    1 
ATOM   1159 C  CG    . TYR A 1 152 ? 54.633 10.849 4.771   1.00 10.87 ?  150 TYR A CG    1 
ATOM   1160 C  CD1   . TYR A 1 152 ? 54.001 11.630 3.837   1.00 12.55 ?  150 TYR A CD1   1 
ATOM   1161 C  CD2   . TYR A 1 152 ? 54.418 9.470  4.686   1.00 12.44 ?  150 TYR A CD2   1 
ATOM   1162 C  CE1   . TYR A 1 152 ? 53.201 11.128 2.817   1.00 11.88 ?  150 TYR A CE1   1 
ATOM   1163 C  CE2   . TYR A 1 152 ? 53.607 8.924  3.684   1.00 12.13 ?  150 TYR A CE2   1 
ATOM   1164 C  CZ    . TYR A 1 152 ? 53.017 9.750  2.748   1.00 12.76 ?  150 TYR A CZ    1 
ATOM   1165 O  OH    . TYR A 1 152 ? 52.233 9.182  1.777   1.00 15.35 ?  150 TYR A OH    1 
ATOM   1166 N  N     . SER A 1 153 ? 57.868 9.664  6.489   1.00 12.47 ?  151 SER A N     1 
ATOM   1167 C  CA    . SER A 1 153 ? 58.545 8.354  6.485   1.00 14.44 ?  151 SER A CA    1 
ATOM   1168 C  C     . SER A 1 153 ? 57.485 7.359  6.921   1.00 13.86 ?  151 SER A C     1 
ATOM   1169 O  O     . SER A 1 153 ? 56.692 7.632  7.767   1.00 14.33 ?  151 SER A O     1 
ATOM   1170 C  CB    . SER A 1 153 ? 59.728 8.381  7.324   1.00 17.34 ?  151 SER A CB    1 
ATOM   1171 O  OG    . SER A 1 153 ? 59.382 8.453  8.675   1.00 28.53 ?  151 SER A OG    1 
ATOM   1172 N  N     . VAL A 1 154 ? 57.504 6.175  6.360   1.00 14.16 ?  152 VAL A N     1 
ATOM   1173 C  CA    . VAL A 1 154 ? 56.601 5.063  6.737   1.00 14.30 ?  152 VAL A CA    1 
ATOM   1174 C  C     . VAL A 1 154 ? 57.475 4.079  7.472   1.00 14.86 ?  152 VAL A C     1 
ATOM   1175 O  O     . VAL A 1 154 ? 58.576 3.751  7.004   1.00 16.06 ?  152 VAL A O     1 
ATOM   1176 C  CB    . VAL A 1 154 ? 55.878 4.428  5.558   1.00 15.22 ?  152 VAL A CB    1 
ATOM   1177 C  CG1   . VAL A 1 154 ? 55.015 3.245  5.978   1.00 17.40 ?  152 VAL A CG1   1 
ATOM   1178 C  CG2   . VAL A 1 154 ? 55.070 5.505  4.833   1.00 17.08 ?  152 VAL A CG2   1 
ATOM   1179 N  N     . ARG A 1 155 ? 57.015 3.619  8.608   1.00 14.43 ?  153 ARG A N     1 
ATOM   1180 C  CA    . ARG A 1 155 ? 57.821 2.742  9.425   1.00 16.42 ?  153 ARG A CA    1 
ATOM   1181 C  C     . ARG A 1 155 ? 58.331 1.527  8.646   1.00 18.76 ?  153 ARG A C     1 
ATOM   1182 O  O     . ARG A 1 155 ? 57.578 0.865  7.965   1.00 16.96 ?  153 ARG A O     1 
ATOM   1183 C  CB    . ARG A 1 155 ? 57.000 2.366  10.665  1.00 18.81 ?  153 ARG A CB    1 
ATOM   1184 C  CG    . ARG A 1 155 ? 57.671 1.540  11.721  1.00 25.57 ?  153 ARG A CG    1 
ATOM   1185 C  CD    . ARG A 1 155 ? 56.940 1.661  13.094  1.00 31.63 ?  153 ARG A CD    1 
ATOM   1186 N  NE    . ARG A 1 155 ? 55.554 1.166  13.082  1.00 46.78 ?  153 ARG A NE    1 
ATOM   1187 C  CZ    . ARG A 1 155 ? 54.464 1.721  13.662  1.00 51.65 ?  153 ARG A CZ    1 
ATOM   1188 N  NH1   . ARG A 1 155 ? 54.557 2.857  14.374  1.00 53.12 ?  153 ARG A NH1   1 
ATOM   1189 N  NH2   . ARG A 1 155 ? 53.266 1.109  13.554  1.00 36.29 ?  153 ARG A NH2   1 
ATOM   1190 N  N     . ASN A 1 156 ? 59.653 1.335  8.733   1.00 18.59 ?  154 ASN A N     1 
ATOM   1191 C  CA    . ASN A 1 156 ? 60.349 0.158  8.144   1.00 20.84 ?  154 ASN A CA    1 
ATOM   1192 C  C     . ASN A 1 156 ? 60.472 0.255  6.630   1.00 24.30 ?  154 ASN A C     1 
ATOM   1193 O  O     . ASN A 1 156 ? 60.832 -0.740 6.009   1.00 24.79 ?  154 ASN A O     1 
ATOM   1194 C  CB    . ASN A 1 156 ? 59.686 -1.187 8.491   1.00 22.59 ?  154 ASN A CB    1 
ATOM   1195 C  CG    . ASN A 1 156 ? 59.598 -1.414 9.977   1.00 28.85 ?  154 ASN A CG    1 
ATOM   1196 O  OD1   . ASN A 1 156 ? 58.624 -1.963 10.469  1.00 35.43 ?  154 ASN A OD1   1 
ATOM   1197 N  ND2   . ASN A 1 156 ? 60.614 -0.982 10.703  1.00 28.67 ?  154 ASN A ND2   1 
ATOM   1198 N  N     . GLU A 1 157 ? 60.154 1.398  6.020   1.00 18.85 ?  155 GLU A N     1 
ATOM   1199 C  CA    . GLU A 1 157 ? 60.313 1.611  4.576   1.00 17.51 ?  155 GLU A CA    1 
ATOM   1200 C  C     . GLU A 1 157 ? 61.426 2.620  4.382   1.00 20.80 ?  155 GLU A C     1 
ATOM   1201 O  O     . GLU A 1 157 ? 61.469 3.659  5.100   1.00 24.09 ?  155 GLU A O     1 
ATOM   1202 C  CB    . GLU A 1 157 ? 58.983 2.017  3.951   1.00 16.73 ?  155 GLU A CB    1 
ATOM   1203 C  CG    . GLU A 1 157 ? 57.968 0.887  4.051   1.00 19.08 ?  155 GLU A CG    1 
ATOM   1204 C  CD    . GLU A 1 157 ? 56.576 1.219  3.547   1.00 19.88 ?  155 GLU A CD    1 
ATOM   1205 O  OE1   . GLU A 1 157 ? 56.455 1.921  2.495   1.00 21.14 ?  155 GLU A OE1   1 
ATOM   1206 O  OE2   . GLU A 1 157 ? 55.637 0.700  4.142   1.00 15.91 ?  155 GLU A OE2   1 
ATOM   1207 N  N     . ALA A 1 158 ? 62.329 2.361  3.461   1.00 21.90 ?  156 ALA A N     1 
ATOM   1208 C  CA    . ALA A 1 158 ? 63.548 3.177  3.342   1.00 25.86 ?  156 ALA A CA    1 
ATOM   1209 C  C     . ALA A 1 158 ? 63.185 4.581  2.845   1.00 26.38 ?  156 ALA A C     1 
ATOM   1210 O  O     . ALA A 1 158 ? 63.722 5.570  3.372   1.00 34.57 ?  156 ALA A O     1 
ATOM   1211 C  CB    . ALA A 1 158 ? 64.497 2.457  2.438   1.00 27.32 ?  156 ALA A CB    1 
ATOM   1212 N  N     . GLU A 1 159 ? 62.269 4.666  1.919   1.00 23.70 ?  157 GLU A N     1 
ATOM   1213 C  CA    . GLU A 1 159 ? 62.144 5.895  1.095   1.00 25.10 ?  157 GLU A CA    1 
ATOM   1214 C  C     . GLU A 1 159 ? 61.074 6.777  1.702   1.00 22.14 ?  157 GLU A C     1 
ATOM   1215 O  O     . GLU A 1 159 ? 59.994 6.266  1.974   1.00 24.68 ?  157 GLU A O     1 
ATOM   1216 C  CB    . GLU A 1 159 ? 61.747 5.560  -0.329  1.00 32.84 ?  157 GLU A CB    1 
ATOM   1217 C  CG    . GLU A 1 159 ? 62.961 5.256  -1.186  1.00 48.39 ?  157 GLU A CG    1 
ATOM   1218 C  CD    . GLU A 1 159 ? 62.679 4.317  -2.335  1.00 58.14 ?  157 GLU A CD    1 
ATOM   1219 O  OE1   . GLU A 1 159 ? 63.450 3.355  -2.486  1.00 72.93 ?  157 GLU A OE1   1 
ATOM   1220 O  OE2   . GLU A 1 159 ? 61.677 4.538  -3.052  1.00 71.23 ?  157 GLU A OE2   1 
ATOM   1221 N  N     . THR A 1 160 ? 61.412 8.025  1.907   1.00 17.32 ?  158 THR A N     1 
ATOM   1222 C  CA    . THR A 1 160 ? 60.407 9.034  2.332   1.00 15.51 ?  158 THR A CA    1 
ATOM   1223 C  C     . THR A 1 160 ? 59.485 9.359  1.165   1.00 16.32 ?  158 THR A C     1 
ATOM   1224 O  O     . THR A 1 160 ? 59.705 8.998  0.002   1.00 17.59 ?  158 THR A O     1 
ATOM   1225 C  CB    . THR A 1 160 ? 61.054 10.324 2.810   1.00 17.12 ?  158 THR A CB    1 
ATOM   1226 O  OG1   . THR A 1 160 ? 61.862 10.892 1.806   1.00 19.57 ?  158 THR A OG1   1 
ATOM   1227 C  CG2   . THR A 1 160 ? 61.951 10.138 4.018   1.00 19.36 ?  158 THR A CG2   1 
ATOM   1228 N  N     . VAL A 1 161 ? 58.385 10.010 1.464   1.00 12.56 ?  159 VAL A N     1 
ATOM   1229 C  CA    . VAL A 1 161 ? 57.315 10.353 0.512   1.00 12.02 ?  159 VAL A CA    1 
ATOM   1230 C  C     . VAL A 1 161 ? 57.039 11.853 0.629   1.00 11.95 ?  159 VAL A C     1 
ATOM   1231 O  O     . VAL A 1 161 ? 56.909 12.330 1.763   1.00 11.91 ?  159 VAL A O     1 
ATOM   1232 C  CB    . VAL A 1 161 ? 56.022 9.585  0.806   1.00 12.19 ?  159 VAL A CB    1 
ATOM   1233 C  CG1   . VAL A 1 161 ? 54.948 9.952  -0.198  1.00 14.49 ?  159 VAL A CG1   1 
ATOM   1234 C  CG2   . VAL A 1 161 ? 56.278 8.084  0.763   1.00 15.50 ?  159 VAL A CG2   1 
ATOM   1235 N  N     . ASP A 1 162 ? 57.002 12.560 -0.465  1.00 11.72 ?  160 ASP A N     1 
ATOM   1236 C  CA    . ASP A 1 162 ? 56.558 13.958 -0.526  1.00 10.95 ?  160 ASP A CA    1 
ATOM   1237 C  C     . ASP A 1 162 ? 55.126 13.986 -0.991  1.00 12.41 ?  160 ASP A C     1 
ATOM   1238 O  O     . ASP A 1 162 ? 54.789 13.340 -2.017  1.00 13.34 ?  160 ASP A O     1 
ATOM   1239 C  CB    . ASP A 1 162 ? 57.430 14.784 -1.452  1.00 11.89 ?  160 ASP A CB    1 
ATOM   1240 C  CG    . ASP A 1 162 ? 58.818 14.946 -0.923  1.00 14.03 ?  160 ASP A CG    1 
ATOM   1241 O  OD1   . ASP A 1 162 ? 59.105 14.464 0.203   1.00 15.98 ?  160 ASP A OD1   1 
ATOM   1242 O  OD2   . ASP A 1 162 ? 59.633 15.647 -1.638  1.00 17.82 ?  160 ASP A OD2   1 
ATOM   1243 N  N     . VAL A 1 163 ? 54.291 14.771 -0.348  1.00 11.35 ?  161 VAL A N     1 
ATOM   1244 C  CA    . VAL A 1 163 ? 52.887 14.914 -0.685  1.00 11.12 ?  161 VAL A CA    1 
ATOM   1245 C  C     . VAL A 1 163 ? 52.517 16.394 -0.648  1.00 12.77 ?  161 VAL A C     1 
ATOM   1246 O  O     . VAL A 1 163 ? 52.956 17.111 0.225   1.00 11.72 ?  161 VAL A O     1 
ATOM   1247 C  CB    . VAL A 1 163 ? 52.002 14.037 0.210   1.00 10.74 ?  161 VAL A CB    1 
ATOM   1248 C  CG1   . VAL A 1 163 ? 52.137 14.436 1.694   1.00 11.12 ?  161 VAL A CG1   1 
ATOM   1249 C  CG2   . VAL A 1 163 ? 50.562 14.083 -0.271  1.00 11.01 ?  161 VAL A CG2   1 
ATOM   1250 N  N     . SER A 1 164 ? 51.696 16.812 -1.604  1.00 11.12 ?  162 SER A N     1 
ATOM   1251 C  CA    . SER A 1 164 ? 51.240 18.214 -1.727  1.00 10.93 ?  162 SER A CA    1 
ATOM   1252 C  C     . SER A 1 164 ? 49.912 18.396 -1.011  1.00 10.79 ?  162 SER A C     1 
ATOM   1253 O  O     . SER A 1 164 ? 49.011 17.575 -1.063  1.00 11.14 ?  162 SER A O     1 
ATOM   1254 C  CB    . SER A 1 164 ? 51.090 18.581 -3.177  1.00 13.21 ?  162 SER A CB    1 
ATOM   1255 O  OG    . SER A 1 164 ? 52.328 18.548 -3.808  1.00 18.79 ?  162 SER A OG    1 
ATOM   1256 N  N     . GLY A 1 165 ? 49.771 19.559 -0.376  1.00 10.86 ?  163 GLY A N     1 
ATOM   1257 C  CA    . GLY A 1 165 ? 48.512 19.981 0.226   1.00 11.25 ?  163 GLY A CA    1 
ATOM   1258 C  C     . GLY A 1 165 ? 48.372 21.493 0.179   1.00 10.50 ?  163 GLY A C     1 
ATOM   1259 O  O     . GLY A 1 165 ? 49.360 22.191 0.394   1.00 11.54 ?  163 GLY A O     1 
ATOM   1260 N  N     . LYS A 1 166 ? 47.168 21.941 -0.016  1.00 9.72  ?  164 LYS A N     1 
ATOM   1261 C  CA    . LYS A 1 166 ? 46.988 23.414 -0.133  1.00 10.36 ?  164 LYS A CA    1 
ATOM   1262 C  C     . LYS A 1 166 ? 47.123 24.055 1.243   1.00 10.75 ?  164 LYS A C     1 
ATOM   1263 O  O     . LYS A 1 166 ? 47.714 25.127 1.345   1.00 10.65 ?  164 LYS A O     1 
ATOM   1264 C  CB    . LYS A 1 166 ? 45.615 23.747 -0.678  1.00 12.63 ?  164 LYS A CB    1 
ATOM   1265 C  CG    . LYS A 1 166 ? 45.402 23.282 -2.113  1.00 15.75 ?  164 LYS A CG    1 
ATOM   1266 C  CD    . LYS A 1 166 ? 44.022 23.647 -2.637  1.00 20.55 ?  164 LYS A CD    1 
ATOM   1267 C  CE    . LYS A 1 166 ? 43.579 22.857 -3.853  1.00 31.51 ?  164 LYS A CE    1 
ATOM   1268 N  NZ    . LYS A 1 166 ? 44.354 23.297 -5.025  1.00 40.67 ?  164 LYS A NZ    1 
ATOM   1269 N  N     . ILE A 1 167 ? 46.623 23.400 2.300   1.00 9.49  ?  165 ILE A N     1 
ATOM   1270 C  CA    . ILE A 1 167 ? 46.857 23.848 3.696   1.00 9.28  ?  165 ILE A CA    1 
ATOM   1271 C  C     . ILE A 1 167 ? 47.248 22.586 4.467   1.00 9.14  ?  165 ILE A C     1 
ATOM   1272 O  O     . ILE A 1 167 ? 46.544 21.572 4.319   1.00 9.98  ?  165 ILE A O     1 
ATOM   1273 C  CB    . ILE A 1 167 ? 45.607 24.535 4.267   1.00 10.35 ?  165 ILE A CB    1 
ATOM   1274 C  CG1   . ILE A 1 167 ? 45.363 25.839 3.514   1.00 12.55 ?  165 ILE A CG1   1 
ATOM   1275 C  CG2   . ILE A 1 167 ? 45.794 24.759 5.749   1.00 10.94 ?  165 ILE A CG2   1 
ATOM   1276 C  CD1   . ILE A 1 167 ? 44.096 26.570 3.875   1.00 14.76 ?  165 ILE A CD1   1 
ATOM   1277 N  N     . THR A 1 168 ? 48.234 22.714 5.299   1.00 8.44  ?  166 THR A N     1 
ATOM   1278 C  CA    . THR A 1 168 ? 48.691 21.663 6.229   1.00 7.90  ?  166 THR A CA    1 
ATOM   1279 C  C     . THR A 1 168 ? 48.373 22.050 7.656   1.00 8.41  ?  166 THR A C     1 
ATOM   1280 O  O     . THR A 1 168 ? 48.690 23.165 8.055   1.00 8.71  ?  166 THR A O     1 
ATOM   1281 C  CB    . THR A 1 168 ? 50.168 21.388 6.060   1.00 8.86  ?  166 THR A CB    1 
ATOM   1282 O  OG1   . THR A 1 168 ? 50.427 20.934 4.725   1.00 10.04 ?  166 THR A OG1   1 
ATOM   1283 C  CG2   . THR A 1 168 ? 50.700 20.359 7.013   1.00 9.82  ?  166 THR A CG2   1 
ATOM   1284 N  N     . ILE A 1 169 ? 47.666 21.192 8.358   1.00 7.46  ?  167 ILE A N     1 
ATOM   1285 C  CA    . ILE A 1 169 ? 47.278 21.394 9.747   1.00 7.26  ?  167 ILE A CA    1 
ATOM   1286 C  C     . ILE A 1 169 ? 48.184 20.582 10.641  1.00 7.10  ?  167 ILE A C     1 
ATOM   1287 O  O     . ILE A 1 169 ? 48.166 19.330 10.554  1.00 7.76  ?  167 ILE A O     1 
ATOM   1288 C  CB    . ILE A 1 169 ? 45.816 21.062 9.963   1.00 7.89  ?  167 ILE A CB    1 
ATOM   1289 C  CG1   . ILE A 1 169 ? 44.886 21.918 9.071   1.00 8.45  ?  167 ILE A CG1   1 
ATOM   1290 C  CG2   . ILE A 1 169 ? 45.463 21.197 11.426  1.00 8.98  ?  167 ILE A CG2   1 
ATOM   1291 C  CD1   . ILE A 1 169 ? 43.441 21.578 9.141   1.00 8.77  ?  167 ILE A CD1   1 
ATOM   1292 N  N     . ASP A 1 170 ? 48.893 21.209 11.531  1.00 7.25  ?  168 ASP A N     1 
ATOM   1293 C  CA    . ASP A 1 170 ? 49.703 20.526 12.571  1.00 7.25  ?  168 ASP A CA    1 
ATOM   1294 C  C     . ASP A 1 170 ? 48.796 20.224 13.769  1.00 6.85  ?  168 ASP A C     1 
ATOM   1295 O  O     . ASP A 1 170 ? 48.354 21.142 14.481  1.00 7.32  ?  168 ASP A O     1 
ATOM   1296 C  CB    . ASP A 1 170 ? 50.835 21.452 13.001  1.00 7.49  ?  168 ASP A CB    1 
ATOM   1297 C  CG    . ASP A 1 170 ? 51.657 20.930 14.170  1.00 8.12  ?  168 ASP A CG    1 
ATOM   1298 O  OD1   . ASP A 1 170 ? 51.467 19.742 14.484  1.00 8.06  ?  168 ASP A OD1   1 
ATOM   1299 O  OD2   . ASP A 1 170 ? 52.514 21.697 14.657  1.00 8.36  ?  168 ASP A OD2   1 
ATOM   1300 N  N     . ALA A 1 171 ? 48.507 18.930 13.926  1.00 6.57  ?  169 ALA A N     1 
ATOM   1301 C  CA    . ALA A 1 171 ? 47.730 18.397 15.056  1.00 6.81  ?  169 ALA A CA    1 
ATOM   1302 C  C     . ALA A 1 171 ? 48.574 17.380 15.818  1.00 6.79  ?  169 ALA A C     1 
ATOM   1303 O  O     . ALA A 1 171 ? 48.058 16.332 16.251  1.00 7.22  ?  169 ALA A O     1 
ATOM   1304 C  CB    . ALA A 1 171 ? 46.430 17.831 14.572  1.00 7.06  ?  169 ALA A CB    1 
ATOM   1305 N  N     . THR A 1 172 ? 49.851 17.651 15.972  1.00 6.92  ?  170 THR A N     1 
ATOM   1306 C  CA    . THR A 1 172 ? 50.811 16.686 16.568  1.00 6.84  ?  170 THR A CA    1 
ATOM   1307 C  C     . THR A 1 172 ? 50.835 16.707 18.082  1.00 6.90  ?  170 THR A C     1 
ATOM   1308 O  O     . THR A 1 172 ? 51.715 16.045 18.665  1.00 7.77  ?  170 THR A O     1 
ATOM   1309 C  CB    . THR A 1 172 ? 52.202 16.863 15.990  1.00 7.23  ?  170 THR A CB    1 
ATOM   1310 O  OG1   . THR A 1 172 ? 52.678 18.200 16.270  1.00 7.93  ?  170 THR A OG1   1 
ATOM   1311 C  CG2   . THR A 1 172 ? 52.233 16.578 14.519  1.00 7.49  ?  170 THR A CG2   1 
ATOM   1312 N  N     . GLY A 1 173 ? 49.934 17.406 18.725  1.00 6.49  ?  171 GLY A N     1 
ATOM   1313 C  CA    . GLY A 1 173 ? 49.903 17.376 20.182  1.00 6.63  ?  171 GLY A CA    1 
ATOM   1314 C  C     . GLY A 1 173 ? 51.190 17.854 20.798  1.00 7.19  ?  171 GLY A C     1 
ATOM   1315 O  O     . GLY A 1 173 ? 51.831 18.815 20.295  1.00 7.72  ?  171 GLY A O     1 
ATOM   1316 N  N     . GLN A 1 174 ? 51.574 17.283 21.937  1.00 7.12  ?  172 GLN A N     1 
ATOM   1317 C  CA    . GLN A 1 174 ? 52.788 17.652 22.654  1.00 7.55  ?  172 GLN A CA    1 
ATOM   1318 C  C     . GLN A 1 174 ? 54.043 17.406 21.852  1.00 8.21  ?  172 GLN A C     1 
ATOM   1319 O  O     . GLN A 1 174 ? 55.125 17.862 22.244  1.00 9.18  ?  172 GLN A O     1 
ATOM   1320 C  CB    . GLN A 1 174 ? 52.845 16.925 24.002  1.00 7.25  ?  172 GLN A CB    1 
ATOM   1321 C  CG    . GLN A 1 174 ? 51.883 17.425 25.028  1.00 7.35  ?  172 GLN A CG    1 
ATOM   1322 C  CD    . GLN A 1 174 ? 52.259 18.701 25.720  1.00 8.46  ?  172 GLN A CD    1 
ATOM   1323 O  OE1   . GLN A 1 174 ? 53.438 18.968 25.940  1.00 10.00 ?  172 GLN A OE1   1 
ATOM   1324 N  NE2   . GLN A 1 174 ? 51.299 19.569 25.974  1.00 9.32  ?  172 GLN A NE2   1 
ATOM   1325 N  N     . GLN A 1 175 ? 54.000 16.728 20.733  1.00 7.53  ?  173 GLN A N     1 
ATOM   1326 C  CA    . GLN A 1 175 ? 55.200 16.647 19.845  1.00 8.49  ?  173 GLN A CA    1 
ATOM   1327 C  C     . GLN A 1 175 ? 55.518 17.985 19.206  1.00 8.32  ?  173 GLN A C     1 
ATOM   1328 O  O     . GLN A 1 175 ? 56.672 18.179 18.835  1.00 10.05 ?  173 GLN A O     1 
ATOM   1329 C  CB    . GLN A 1 175 ? 54.979 15.555 18.785  1.00 8.94  ?  173 GLN A CB    1 
ATOM   1330 C  CG    . GLN A 1 175 ? 55.189 14.127 19.311  1.00 11.67 ?  173 GLN A CG    1 
ATOM   1331 C  CD    . GLN A 1 175 ? 54.155 13.614 20.261  1.00 15.45 ?  173 GLN A CD    1 
ATOM   1332 O  OE1   . GLN A 1 175 ? 52.963 13.485 19.904  1.00 15.33 ?  173 GLN A OE1   1 
ATOM   1333 N  NE2   . GLN A 1 175 ? 54.587 13.416 21.494  1.00 18.55 ?  173 GLN A NE2   1 
ATOM   1334 N  N     . ARG A 1 176 ? 54.545 18.876 19.176  1.00 8.78  ?  174 ARG A N     1 
ATOM   1335 C  CA    . ARG A 1 176 ? 54.817 20.255 18.732  1.00 10.05 ?  174 ARG A CA    1 
ATOM   1336 C  C     . ARG A 1 176 ? 55.620 20.369 17.448  1.00 8.66  ?  174 ARG A C     1 
ATOM   1337 O  O     . ARG A 1 176 ? 56.557 21.080 17.375  1.00 9.54  ?  174 ARG A O     1 
ATOM   1338 C  CB    . ARG A 1 176 ? 55.618 20.991 19.834  1.00 14.30 ?  174 ARG A CB    1 
ATOM   1339 C  CG    . ARG A 1 176 ? 54.885 21.109 21.160  1.00 17.38 ?  174 ARG A CG    1 
ATOM   1340 C  CD    . ARG A 1 176 ? 55.665 21.962 22.148  1.00 16.37 ?  174 ARG A CD    1 
ATOM   1341 N  NE    . ARG A 1 176 ? 56.940 21.351 22.511  1.00 19.43 ?  174 ARG A NE    1 
ATOM   1342 C  CZ    . ARG A 1 176 ? 57.099 20.495 23.515  1.00 18.17 ?  174 ARG A CZ    1 
ATOM   1343 N  NH1   . ARG A 1 176 ? 56.060 20.145 24.262  1.00 21.92 ?  174 ARG A NH1   1 
ATOM   1344 N  NH2   . ARG A 1 176 ? 58.297 19.988 23.774  1.00 22.18 ?  174 ARG A NH2   1 
ATOM   1345 N  N     . TRP A 1 177 ? 55.210 19.712 16.403  1.00 7.90  ?  175 TRP A N     1 
ATOM   1346 C  CA    . TRP A 1 177 ? 55.946 19.693 15.132  1.00 8.07  ?  175 TRP A CA    1 
ATOM   1347 C  C     . TRP A 1 177 ? 56.273 21.085 14.603  1.00 8.00  ?  175 TRP A C     1 
ATOM   1348 O  O     . TRP A 1 177 ? 57.446 21.372 14.363  1.00 8.64  ?  175 TRP A O     1 
ATOM   1349 C  CB    . TRP A 1 177 ? 55.165 18.843 14.129  1.00 8.39  ?  175 TRP A CB    1 
ATOM   1350 C  CG    . TRP A 1 177 ? 55.668 18.877 12.722  1.00 8.58  ?  175 TRP A CG    1 
ATOM   1351 C  CD1   . TRP A 1 177 ? 56.950 18.635 12.338  1.00 10.75 ?  175 TRP A CD1   1 
ATOM   1352 C  CD2   . TRP A 1 177 ? 54.926 19.202 11.543  1.00 8.38  ?  175 TRP A CD2   1 
ATOM   1353 N  NE1   . TRP A 1 177 ? 57.026 18.798 10.958  1.00 10.79 ?  175 TRP A NE1   1 
ATOM   1354 C  CE2   . TRP A 1 177 ? 55.812 19.158 10.458  1.00 10.08 ?  175 TRP A CE2   1 
ATOM   1355 C  CE3   . TRP A 1 177 ? 53.580 19.470 11.335  1.00 8.32  ?  175 TRP A CE3   1 
ATOM   1356 C  CZ2   . TRP A 1 177 ? 55.345 19.442 9.173   1.00 9.36  ?  175 TRP A CZ2   1 
ATOM   1357 C  CZ3   . TRP A 1 177 ? 53.131 19.756 10.067  1.00 9.34  ?  175 TRP A CZ3   1 
ATOM   1358 C  CH2   . TRP A 1 177 ? 54.021 19.782 9.019   1.00 9.54  ?  175 TRP A CH2   1 
ATOM   1359 N  N     . LEU A 1 178 ? 55.280 21.929 14.393  1.00 8.43  ?  176 LEU A N     1 
ATOM   1360 C  CA    . LEU A 1 178 ? 55.590 23.246 13.825  1.00 8.11  ?  176 LEU A CA    1 
ATOM   1361 C  C     . LEU A 1 178 ? 56.086 24.218 14.880  1.00 8.18  ?  176 LEU A C     1 
ATOM   1362 O  O     . LEU A 1 178 ? 56.894 25.110 14.536  1.00 8.34  ?  176 LEU A O     1 
ATOM   1363 C  CB    . LEU A 1 178 ? 54.407 23.801 13.036  1.00 8.21  ?  176 LEU A CB    1 
ATOM   1364 C  CG    . LEU A 1 178 ? 54.087 23.020 11.765  1.00 8.39  ?  176 LEU A CG    1 
ATOM   1365 C  CD1   . LEU A 1 178 ? 52.969 23.719 10.998  1.00 8.46  ?  176 LEU A CD1   1 
ATOM   1366 C  CD2   . LEU A 1 178 ? 55.306 22.809 10.898  1.00 8.65  ?  176 LEU A CD2   1 
ATOM   1367 N  N     . GLY A 1 179 ? 55.724 24.077 16.118  1.00 7.80  ?  177 GLY A N     1 
ATOM   1368 C  CA    . GLY A 1 179 ? 56.320 24.902 17.157  1.00 8.41  ?  177 GLY A CA    1 
ATOM   1369 C  C     . GLY A 1 179 ? 57.811 24.683 17.177  1.00 7.94  ?  177 GLY A C     1 
ATOM   1370 O  O     . GLY A 1 179 ? 58.570 25.667 17.284  1.00 9.76  ?  177 GLY A O     1 
ATOM   1371 N  N     . ARG A 1 180 ? 58.256 23.458 17.048  1.00 8.31  ?  178 ARG A N     1 
ATOM   1372 C  CA    . ARG A 1 180 ? 59.704 23.136 16.986  1.00 8.36  ?  178 ARG A CA    1 
ATOM   1373 C  C     . ARG A 1 180 ? 60.246 23.606 15.665  1.00 9.63  ?  178 ARG A C     1 
ATOM   1374 O  O     . ARG A 1 180 ? 61.363 24.199 15.633  1.00 10.49 ?  178 ARG A O     1 
ATOM   1375 C  CB    . ARG A 1 180 ? 59.909 21.640 17.142  1.00 9.31  ?  178 ARG A CB    1 
ATOM   1376 C  CG    . ARG A 1 180 ? 59.629 21.145 18.549  1.00 9.59  ?  178 ARG A CG    1 
ATOM   1377 C  CD    . ARG A 1 180 ? 59.642 19.593 18.537  1.00 11.57 ?  178 ARG A CD    1 
ATOM   1378 N  NE    . ARG A 1 180 ? 59.516 19.012 19.859  1.00 12.81 ?  178 ARG A NE    1 
ATOM   1379 C  CZ    . ARG A 1 180 ? 60.515 18.922 20.730  1.00 12.79 ?  178 ARG A CZ    1 
ATOM   1380 N  NH1   . ARG A 1 180 ? 61.726 19.351 20.410  1.00 13.96 ?  178 ARG A NH1   1 
ATOM   1381 N  NH2   . ARG A 1 180 ? 60.284 18.404 21.927  1.00 15.85 ?  178 ARG A NH2   1 
ATOM   1382 N  N     . HIS A 1 181 ? 59.595 23.346 14.552  1.00 8.87  ?  179 HIS A N     1 
ATOM   1383 C  CA    . HIS A 1 181 ? 60.142 23.735 13.228  1.00 8.96  ?  179 HIS A CA    1 
ATOM   1384 C  C     . HIS A 1 181 ? 60.466 25.218 13.217  1.00 9.00  ?  179 HIS A C     1 
ATOM   1385 O  O     . HIS A 1 181 ? 61.552 25.591 12.687  1.00 11.43 ?  179 HIS A O     1 
ATOM   1386 C  CB    . HIS A 1 181 ? 59.179 23.356 12.108  1.00 9.34  ?  179 HIS A CB    1 
ATOM   1387 C  CG    . HIS A 1 181 ? 59.695 23.784 10.776  1.00 10.03 ?  179 HIS A CG    1 
ATOM   1388 N  ND1   . HIS A 1 181 ? 60.625 23.022 10.105  1.00 12.22 ?  179 HIS A ND1   1 
ATOM   1389 C  CD2   . HIS A 1 181 ? 59.479 24.905 10.066  1.00 11.42 ?  179 HIS A CD2   1 
ATOM   1390 C  CE1   . HIS A 1 181 ? 60.885 23.706 8.967   1.00 12.14 ?  179 HIS A CE1   1 
ATOM   1391 N  NE2   . HIS A 1 181 ? 60.250 24.848 8.927   1.00 12.32 ?  179 HIS A NE2   1 
ATOM   1392 N  N     . PHE A 1 182 ? 59.545 26.038 13.647  1.00 9.00  ?  180 PHE A N     1 
ATOM   1393 C  CA    . PHE A 1 182 ? 59.641 27.522 13.617  1.00 9.47  ?  180 PHE A CA    1 
ATOM   1394 C  C     . PHE A 1 182 ? 60.275 28.048 14.900  1.00 10.08 ?  180 PHE A C     1 
ATOM   1395 O  O     . PHE A 1 182 ? 60.407 29.280 14.954  1.00 11.98 ?  180 PHE A O     1 
ATOM   1396 C  CB    . PHE A 1 182 ? 58.289 28.134 13.312  1.00 9.46  ?  180 PHE A CB    1 
ATOM   1397 C  CG    . PHE A 1 182 ? 57.799 27.902 11.918  1.00 9.16  ?  180 PHE A CG    1 
ATOM   1398 C  CD1   . PHE A 1 182 ? 58.480 28.423 10.842  1.00 9.10  ?  180 PHE A CD1   1 
ATOM   1399 C  CD2   . PHE A 1 182 ? 56.674 27.142 11.680  1.00 8.62  ?  180 PHE A CD2   1 
ATOM   1400 C  CE1   . PHE A 1 182 ? 57.974 28.257 9.553   1.00 9.50  ?  180 PHE A CE1   1 
ATOM   1401 C  CE2   . PHE A 1 182 ? 56.199 26.936 10.406  1.00 9.43  ?  180 PHE A CE2   1 
ATOM   1402 C  CZ    . PHE A 1 182 ? 56.817 27.540 9.348   1.00 10.30 ?  180 PHE A CZ    1 
ATOM   1403 N  N     . ASP A 1 183 ? 60.705 27.221 15.824  1.00 9.32  ?  181 ASP A N     1 
ATOM   1404 C  CA    . ASP A 1 183 ? 61.264 27.661 17.130  1.00 9.34  ?  181 ASP A CA    1 
ATOM   1405 C  C     . ASP A 1 183 ? 60.394 28.745 17.708  1.00 10.38 ?  181 ASP A C     1 
ATOM   1406 O  O     . ASP A 1 183 ? 60.851 29.865 18.064  1.00 11.42 ?  181 ASP A O     1 
ATOM   1407 C  CB    . ASP A 1 183 ? 62.730 28.080 17.023  1.00 11.10 ?  181 ASP A CB    1 
ATOM   1408 C  CG    . ASP A 1 183 ? 63.302 28.413 18.378  1.00 13.80 ?  181 ASP A CG    1 
ATOM   1409 O  OD1   . ASP A 1 183 ? 62.827 27.929 19.432  1.00 13.84 ?  181 ASP A OD1   1 
ATOM   1410 O  OD2   . ASP A 1 183 ? 64.267 29.273 18.432  1.00 15.74 ?  181 ASP A OD2   1 
ATOM   1411 N  N     . MET A 1 184 ? 59.105 28.450 17.926  1.00 9.02  ?  182 MET A N     1 
ATOM   1412 C  CA    . MET A 1 184 ? 58.151 29.497 18.299  1.00 8.39  ?  182 MET A CA    1 
ATOM   1413 C  C     . MET A 1 184 ? 57.331 29.122 19.541  1.00 7.60  ?  182 MET A C     1 
ATOM   1414 O  O     . MET A 1 184 ? 56.253 29.647 19.753  1.00 9.91  ?  182 MET A O     1 
ATOM   1415 C  CB    . MET A 1 184 ? 57.241 29.872 17.143  1.00 8.15  ?  182 MET A CB    1 
ATOM   1416 C  CG    . MET A 1 184 ? 56.372 28.741 16.651  1.00 8.68  ?  182 MET A CG    1 
ATOM   1417 S  SD    . MET A 1 184 ? 55.170 29.428 15.476  1.00 10.59 ?  182 MET A SD    1 
ATOM   1418 C  CE    . MET A 1 184 ? 54.300 27.898 15.093  1.00 8.95  ?  182 MET A CE    1 
ATOM   1419 N  N     . VAL A 1 185 ? 57.827 28.184 20.334  1.00 8.96  ?  183 VAL A N     1 
ATOM   1420 C  CA    . VAL A 1 185 ? 57.100 27.739 21.539  1.00 9.00  ?  183 VAL A CA    1 
ATOM   1421 C  C     . VAL A 1 185 ? 57.339 28.760 22.678  1.00 9.55  ?  183 VAL A C     1 
ATOM   1422 O  O     . VAL A 1 185 ? 58.518 28.973 23.021  1.00 12.38 ?  183 VAL A O     1 
ATOM   1423 C  CB    . VAL A 1 185 ? 57.546 26.341 21.955  1.00 9.63  ?  183 VAL A CB    1 
ATOM   1424 C  CG1   . VAL A 1 185 ? 56.763 25.920 23.202  1.00 10.58 ?  183 VAL A CG1   1 
ATOM   1425 C  CG2   . VAL A 1 185 ? 57.356 25.352 20.842  1.00 11.43 ?  183 VAL A CG2   1 
ATOM   1426 N  N     . GLU A 1 186 ? 56.309 29.343 23.216  1.00 9.29  ?  184 GLU A N     1 
ATOM   1427 C  CA    . GLU A 1 186 ? 56.409 30.282 24.351  1.00 9.09  ?  184 GLU A CA    1 
ATOM   1428 C  C     . GLU A 1 186 ? 56.045 29.509 25.607  1.00 8.97  ?  184 GLU A C     1 
ATOM   1429 O  O     . GLU A 1 186 ? 54.846 29.235 25.824  1.00 10.19 ?  184 GLU A O     1 
ATOM   1430 C  CB    . GLU A 1 186 ? 55.575 31.528 24.171  1.00 10.03 ?  184 GLU A CB    1 
ATOM   1431 C  CG    . GLU A 1 186 ? 55.872 32.311 22.886  1.00 12.04 ?  184 GLU A CG    1 
ATOM   1432 C  CD    . GLU A 1 186 ? 54.943 33.509 22.680  1.00 15.09 ?  184 GLU A CD    1 
ATOM   1433 O  OE1   . GLU A 1 186 ? 53.878 33.646 23.372  1.00 18.82 ?  184 GLU A OE1   1 
ATOM   1434 O  OE2   . GLU A 1 186 ? 55.206 34.274 21.769  1.00 21.81 ?  184 GLU A OE2   1 
ATOM   1435 N  N     . TRP A 1 187 ? 57.020 29.145 26.395  1.00 8.48  ?  185 TRP A N     1 
ATOM   1436 C  CA    . TRP A 1 187 ? 56.763 28.353 27.570  1.00 8.44  ?  185 TRP A CA    1 
ATOM   1437 C  C     . TRP A 1 187 ? 56.165 29.144 28.734  1.00 8.39  ?  185 TRP A C     1 
ATOM   1438 O  O     . TRP A 1 187 ? 56.481 30.246 28.933  1.00 10.46 ?  185 TRP A O     1 
ATOM   1439 C  CB    . TRP A 1 187 ? 58.103 27.711 28.029  1.00 9.09  ?  185 TRP A CB    1 
ATOM   1440 C  CG    . TRP A 1 187 ? 58.568 26.678 27.093  1.00 9.37  ?  185 TRP A CG    1 
ATOM   1441 C  CD1   . TRP A 1 187 ? 59.477 26.820 26.087  1.00 9.72  ?  185 TRP A CD1   1 
ATOM   1442 C  CD2   . TRP A 1 187 ? 58.089 25.342 27.015  1.00 9.44  ?  185 TRP A CD2   1 
ATOM   1443 N  NE1   . TRP A 1 187 ? 59.569 25.653 25.396  1.00 10.39 ?  185 TRP A NE1   1 
ATOM   1444 C  CE2   . TRP A 1 187 ? 58.729 24.734 25.952  1.00 9.51  ?  185 TRP A CE2   1 
ATOM   1445 C  CE3   . TRP A 1 187 ? 57.203 24.604 27.769  1.00 9.75  ?  185 TRP A CE3   1 
ATOM   1446 C  CZ2   . TRP A 1 187 ? 58.493 23.419 25.611  1.00 10.85 ?  185 TRP A CZ2   1 
ATOM   1447 C  CZ3   . TRP A 1 187 ? 56.963 23.350 27.432  1.00 10.11 ?  185 TRP A CZ3   1 
ATOM   1448 C  CH2   . TRP A 1 187 ? 57.612 22.747 26.379  1.00 9.98  ?  185 TRP A CH2   1 
ATOM   1449 N  N     . HIS A 1 188 ? 55.258 28.513 29.455  1.00 8.43  ?  186 HIS A N     1 
ATOM   1450 C  CA    . HIS A 1 188 ? 54.735 29.066 30.699  1.00 8.11  ?  186 HIS A CA    1 
ATOM   1451 C  C     . HIS A 1 188 ? 55.695 28.569 31.802  1.00 9.78  ?  186 HIS A C     1 
ATOM   1452 O  O     . HIS A 1 188 ? 55.553 27.548 32.292  1.00 9.98  ?  186 HIS A O     1 
ATOM   1453 C  CB    . HIS A 1 188 ? 53.303 28.609 30.973  1.00 9.21  ?  186 HIS A CB    1 
ATOM   1454 C  CG    . HIS A 1 188 ? 52.338 29.079 29.945  1.00 9.88  ?  186 HIS A CG    1 
ATOM   1455 N  ND1   . HIS A 1 188 ? 51.365 28.280 29.397  1.00 12.87 ?  186 HIS A ND1   1 
ATOM   1456 C  CD2   . HIS A 1 188 ? 52.193 30.289 29.375  1.00 12.68 ?  186 HIS A CD2   1 
ATOM   1457 C  CE1   . HIS A 1 188 ? 50.687 28.971 28.503  1.00 12.69 ?  186 HIS A CE1   1 
ATOM   1458 N  NE2   . HIS A 1 188 ? 51.148 30.193 28.498  1.00 13.61 ?  186 HIS A NE2   1 
ATOM   1459 N  N     . GLU A 1 189 ? 56.661 29.393 32.129  1.00 9.76  ?  187 GLU A N     1 
ATOM   1460 C  CA    . GLU A 1 189 ? 57.736 28.973 33.056  1.00 10.10 ?  187 GLU A CA    1 
ATOM   1461 C  C     . GLU A 1 189 ? 57.191 28.876 34.481  1.00 8.97  ?  187 GLU A C     1 
ATOM   1462 O  O     . GLU A 1 189 ? 57.932 28.280 35.272  1.00 12.66 ?  187 GLU A O     1 
ATOM   1463 C  CB    . GLU A 1 189 ? 58.890 29.970 32.950  1.00 9.91  ?  187 GLU A CB    1 
ATOM   1464 C  CG    . GLU A 1 189 ? 59.562 30.005 31.620  1.00 10.12 ?  187 GLU A CG    1 
ATOM   1465 C  CD    . GLU A 1 189 ? 60.383 28.820 31.217  1.00 10.53 ?  187 GLU A CD    1 
ATOM   1466 O  OE1   . GLU A 1 189 ? 60.913 28.816 30.077  1.00 11.13 ?  187 GLU A OE1   1 
ATOM   1467 O  OE2   . GLU A 1 189 ? 60.525 27.911 32.051  1.00 10.92 ?  187 GLU A OE2   1 
ATOM   1468 N  N     . ASP A 1 190 ? 55.984 29.335 34.767  1.00 10.61 ?  188 ASP A N     1 
ATOM   1469 C  CA    . ASP A 1 190 ? 55.341 29.191 36.088  1.00 10.70 ?  188 ASP A CA    1 
ATOM   1470 C  C     . ASP A 1 190 ? 54.595 27.882 36.190  1.00 11.23 ?  188 ASP A C     1 
ATOM   1471 O  O     . ASP A 1 190 ? 54.154 27.528 37.282  1.00 13.44 ?  188 ASP A O     1 
ATOM   1472 C  CB    . ASP A 1 190 ? 54.351 30.328 36.357  1.00 12.78 ?  188 ASP A CB    1 
ATOM   1473 C  CG    . ASP A 1 190 ? 53.238 30.429 35.335  1.00 14.42 ?  188 ASP A CG    1 
ATOM   1474 O  OD1   . ASP A 1 190 ? 53.499 30.297 34.122  1.00 13.26 ?  188 ASP A OD1   1 
ATOM   1475 O  OD2   . ASP A 1 190 ? 52.012 30.509 35.773  1.00 15.44 ?  188 ASP A OD2   1 
ATOM   1476 N  N     . LEU A 1 191 ? 54.484 27.124 35.107  1.00 9.96  ?  189 LEU A N     1 
ATOM   1477 C  CA    . LEU A 1 191 ? 53.701 25.856 35.062  1.00 9.73  ?  189 LEU A CA    1 
ATOM   1478 C  C     . LEU A 1 191 ? 54.619 24.786 34.560  1.00 9.87  ?  189 LEU A C     1 
ATOM   1479 O  O     . LEU A 1 191 ? 54.387 24.179 33.482  1.00 10.63 ?  189 LEU A O     1 
ATOM   1480 C  CB    . LEU A 1 191 ? 52.451 26.018 34.185  1.00 10.10 ?  189 LEU A CB    1 
ATOM   1481 C  CG    . LEU A 1 191 ? 51.345 26.869 34.780  1.00 12.25 ?  189 LEU A CG    1 
ATOM   1482 C  CD1   . LEU A 1 191 ? 50.369 27.268 33.705  1.00 13.65 ?  189 LEU A CD1   1 
ATOM   1483 C  CD2   . LEU A 1 191 ? 50.604 26.158 35.901  1.00 14.94 ?  189 LEU A CD2   1 
ATOM   1484 N  N     . ARG A 1 192 ? 55.683 24.508 35.286  1.00 9.29  ?  190 ARG A N     1 
ATOM   1485 C  CA    . ARG A 1 192 ? 56.651 23.436 34.984  1.00 8.52  ?  190 ARG A CA    1 
ATOM   1486 C  C     . ARG A 1 192 ? 56.321 22.326 35.986  1.00 9.19  ?  190 ARG A C     1 
ATOM   1487 O  O     . ARG A 1 192 ? 56.882 22.227 37.093  1.00 9.63  ?  190 ARG A O     1 
ATOM   1488 C  CB    . ARG A 1 192 ? 58.095 23.923 35.123  1.00 9.04  ?  190 ARG A CB    1 
ATOM   1489 C  CG    . ARG A 1 192 ? 58.450 24.985 34.115  1.00 9.42  ?  190 ARG A CG    1 
ATOM   1490 C  CD    . ARG A 1 192 ? 59.898 25.449 34.214  1.00 10.68 ?  190 ARG A CD    1 
ATOM   1491 N  NE    . ARG A 1 192 ? 60.157 25.963 35.529  1.00 10.95 ?  190 ARG A NE    1 
ATOM   1492 C  CZ    . ARG A 1 192 ? 61.295 25.748 36.209  1.00 12.69 ?  190 ARG A CZ    1 
ATOM   1493 N  NH1   . ARG A 1 192 ? 62.265 25.022 35.670  1.00 13.22 ?  190 ARG A NH1   1 
ATOM   1494 N  NH2   . ARG A 1 192 ? 61.452 26.261 37.422  1.00 15.36 ?  190 ARG A NH2   1 
ATOM   1495 N  N     . ASN A 1 193 ? 55.423 21.454 35.558  1.00 9.07  ?  191 ASN A N     1 
ATOM   1496 C  CA    . ASN A 1 193 ? 54.862 20.435 36.455  1.00 9.10  ?  191 ASN A CA    1 
ATOM   1497 C  C     . ASN A 1 193 ? 55.205 19.054 35.922  1.00 8.43  ?  191 ASN A C     1 
ATOM   1498 O  O     . ASN A 1 193 ? 55.510 18.894 34.720  1.00 9.47  ?  191 ASN A O     1 
ATOM   1499 C  CB    . ASN A 1 193 ? 53.357 20.642 36.539  1.00 9.55  ?  191 ASN A CB    1 
ATOM   1500 C  CG    . ASN A 1 193 ? 52.993 21.938 37.181  1.00 13.59 ?  191 ASN A CG    1 
ATOM   1501 O  OD1   . ASN A 1 193 ? 53.685 22.373 38.105  1.00 14.79 ?  191 ASN A OD1   1 
ATOM   1502 N  ND2   . ASN A 1 193 ? 51.878 22.528 36.815  1.00 13.62 ?  191 ASN A ND2   1 
ATOM   1503 N  N     . ILE A 1 194 ? 55.126 18.087 36.815  1.00 8.41  ?  192 ILE A N     1 
ATOM   1504 C  CA    . ILE A 1 194 ? 55.295 16.664 36.506  1.00 8.66  ?  192 ILE A CA    1 
ATOM   1505 C  C     . ILE A 1 194 ? 54.047 15.962 37.012  1.00 8.49  ?  192 ILE A C     1 
ATOM   1506 O  O     . ILE A 1 194 ? 53.568 16.256 38.114  1.00 9.21  ?  192 ILE A O     1 
ATOM   1507 C  CB    . ILE A 1 194 ? 56.608 16.133 37.027  1.00 9.41  ?  192 ILE A CB    1 
ATOM   1508 C  CG1   . ILE A 1 194 ? 56.808 14.674 36.667  1.00 11.22 ?  192 ILE A CG1   1 
ATOM   1509 C  CG2   . ILE A 1 194 ? 56.768 16.379 38.516  1.00 9.95  ?  192 ILE A CG2   1 
ATOM   1510 C  CD1   . ILE A 1 194 ? 58.228 14.207 36.788  1.00 13.00 ?  192 ILE A CD1   1 
ATOM   1511 N  N     . ALA A 1 195 ? 53.608 14.975 36.266  1.00 7.71  ?  193 ALA A N     1 
ATOM   1512 C  CA    . ALA A 1 195 ? 52.509 14.084 36.618  1.00 7.30  ?  193 ALA A CA    1 
ATOM   1513 C  C     . ALA A 1 195 ? 53.054 12.673 36.679  1.00 7.49  ?  193 ALA A C     1 
ATOM   1514 O  O     . ALA A 1 195 ? 53.869 12.286 35.861  1.00 8.32  ?  193 ALA A O     1 
ATOM   1515 C  CB    . ALA A 1 195 ? 51.370 14.156 35.649  1.00 7.37  ?  193 ALA A CB    1 
ATOM   1516 N  N     . ALA A 1 196 ? 52.538 11.901 37.629  1.00 7.48  ?  194 ALA A N     1 
ATOM   1517 C  CA    . ALA A 1 196 ? 52.812 10.460 37.759  1.00 7.39  ?  194 ALA A CA    1 
ATOM   1518 C  C     . ALA A 1 196 ? 51.458 9.821  37.976  1.00 7.77  ?  194 ALA A C     1 
ATOM   1519 O  O     . ALA A 1 196 ? 50.716 10.285 38.844  1.00 7.78  ?  194 ALA A O     1 
ATOM   1520 C  CB    . ALA A 1 196 ? 53.760 10.187 38.914  1.00 8.78  ?  194 ALA A CB    1 
ATOM   1521 N  N     . TRP A 1 197 ? 51.187 8.715  37.284  1.00 6.83  ?  195 TRP A N     1 
ATOM   1522 C  CA    . TRP A 1 197 ? 49.865 8.088  37.406  1.00 7.00  ?  195 TRP A CA    1 
ATOM   1523 C  C     . TRP A 1 197 ? 49.940 6.611  37.145  1.00 6.84  ?  195 TRP A C     1 
ATOM   1524 O  O     . TRP A 1 197 ? 50.876 6.088  36.572  1.00 7.68  ?  195 TRP A O     1 
ATOM   1525 C  CB    . TRP A 1 197 ? 48.829 8.732  36.457  1.00 7.25  ?  195 TRP A CB    1 
ATOM   1526 C  CG    . TRP A 1 197 ? 49.089 8.504  35.015  1.00 6.84  ?  195 TRP A CG    1 
ATOM   1527 C  CD1   . TRP A 1 197 ? 48.623 7.483  34.244  1.00 7.17  ?  195 TRP A CD1   1 
ATOM   1528 C  CD2   . TRP A 1 197 ? 49.916 9.269  34.142  1.00 7.29  ?  195 TRP A CD2   1 
ATOM   1529 N  NE1   . TRP A 1 197 ? 49.120 7.555  32.981  1.00 7.42  ?  195 TRP A NE1   1 
ATOM   1530 C  CE2   . TRP A 1 197 ? 49.900 8.677  32.869  1.00 7.08  ?  195 TRP A CE2   1 
ATOM   1531 C  CE3   . TRP A 1 197 ? 50.662 10.432 34.287  1.00 7.44  ?  195 TRP A CE3   1 
ATOM   1532 C  CZ2   . TRP A 1 197 ? 50.593 9.163  31.775  1.00 7.45  ?  195 TRP A CZ2   1 
ATOM   1533 C  CZ3   . TRP A 1 197 ? 51.338 10.941 33.182  1.00 7.89  ?  195 TRP A CZ3   1 
ATOM   1534 C  CH2   . TRP A 1 197 ? 51.290 10.318 31.945  1.00 7.42  ?  195 TRP A CH2   1 
ATOM   1535 N  N     . SER A 1 198 ? 48.872 5.962  37.599  1.00 6.69  ?  196 SER A N     1 
ATOM   1536 C  CA    . SER A 1 198 ? 48.635 4.541  37.290  1.00 6.79  ?  196 SER A CA    1 
ATOM   1537 C  C     . SER A 1 198 ? 47.156 4.261  37.298  1.00 7.43  ?  196 SER A C     1 
ATOM   1538 O  O     . SER A 1 198 ? 46.314 5.173  37.416  1.00 7.42  ?  196 SER A O     1 
ATOM   1539 C  CB    . SER A 1 198 ? 49.471 3.652  38.189  1.00 7.80  ?  196 SER A CB    1 
ATOM   1540 O  OG    . SER A 1 198 ? 49.464 2.304  37.690  1.00 8.16  ?  196 SER A OG    1 
ATOM   1541 N  N     . TYR A 1 199 ? 46.832 2.987  37.159  1.00 6.76  ?  197 TYR A N     1 
ATOM   1542 C  CA    . TYR A 1 199 ? 45.457 2.471  37.115  1.00 6.90  ?  197 TYR A CA    1 
ATOM   1543 C  C     . TYR A 1 199 ? 45.272 1.505  38.271  1.00 7.41  ?  197 TYR A C     1 
ATOM   1544 O  O     . TYR A 1 199 ? 46.202 0.733  38.557  1.00 7.64  ?  197 TYR A O     1 
ATOM   1545 C  CB    . TYR A 1 199 ? 45.169 1.833  35.753  1.00 7.55  ?  197 TYR A CB    1 
ATOM   1546 C  CG    . TYR A 1 199 ? 45.216 2.863  34.645  1.00 7.05  ?  197 TYR A CG    1 
ATOM   1547 C  CD1   . TYR A 1 199 ? 44.111 3.635  34.311  1.00 7.67  ?  197 TYR A CD1   1 
ATOM   1548 C  CD2   . TYR A 1 199 ? 46.414 3.111  33.997  1.00 7.69  ?  197 TYR A CD2   1 
ATOM   1549 C  CE1   . TYR A 1 199 ? 44.210 4.686  33.384  1.00 8.19  ?  197 TYR A CE1   1 
ATOM   1550 C  CE2   . TYR A 1 199 ? 46.544 4.174  33.095  1.00 8.23  ?  197 TYR A CE2   1 
ATOM   1551 C  CZ    . TYR A 1 199 ? 45.450 4.953  32.806  1.00 8.07  ?  197 TYR A CZ    1 
ATOM   1552 O  OH    . TYR A 1 199 ? 45.545 5.977  31.913  1.00 9.01  ?  197 TYR A OH    1 
ATOM   1553 N  N     . TYR A 1 200 ? 44.077 1.531  38.823  1.00 7.79  ?  198 TYR A N     1 
ATOM   1554 C  CA    . TYR A 1 200 ? 43.760 0.846  40.102  1.00 7.53  ?  198 TYR A CA    1 
ATOM   1555 C  C     . TYR A 1 200 ? 42.459 0.146  39.977  1.00 8.65  ?  198 TYR A C     1 
ATOM   1556 O  O     . TYR A 1 200 ? 41.490 0.679  39.446  1.00 8.99  ?  198 TYR A O     1 
ATOM   1557 C  CB    . TYR A 1 200 ? 43.742 1.855  41.236  1.00 8.64  ?  198 TYR A CB    1 
ATOM   1558 C  CG    . TYR A 1 200 ? 45.074 2.506  41.441  1.00 8.17  ?  198 TYR A CG    1 
ATOM   1559 C  CD1   . TYR A 1 200 ? 45.522 3.556  40.648  1.00 8.42  ?  198 TYR A CD1   1 
ATOM   1560 C  CD2   . TYR A 1 200 ? 45.918 2.094  42.449  1.00 8.89  ?  198 TYR A CD2   1 
ATOM   1561 C  CE1   . TYR A 1 200 ? 46.792 4.087  40.826  1.00 8.30  ?  198 TYR A CE1   1 
ATOM   1562 C  CE2   . TYR A 1 200 ? 47.166 2.651  42.655  1.00 9.04  ?  198 TYR A CE2   1 
ATOM   1563 C  CZ    . TYR A 1 200 ? 47.634 3.635  41.806  1.00 8.83  ?  198 TYR A CZ    1 
ATOM   1564 O  OH    . TYR A 1 200 ? 48.907 4.156  41.905  1.00 10.63 ?  198 TYR A OH    1 
ATOM   1565 N  N     . GLN A 1 201 ? 42.433 -1.083 40.525  1.00 9.68  ?  199 GLN A N     1 
ATOM   1566 C  CA    . GLN A 1 201 ? 41.186 -1.867 40.659  1.00 10.13 ?  199 GLN A CA    1 
ATOM   1567 C  C     . GLN A 1 201 ? 40.712 -1.785 42.099  1.00 9.56  ?  199 GLN A C     1 
ATOM   1568 O  O     . GLN A 1 201 ? 41.511 -1.687 43.008  1.00 12.19 ?  199 GLN A O     1 
ATOM   1569 C  CB    . GLN A 1 201 ? 41.473 -3.307 40.275  1.00 12.44 ?  199 GLN A CB    1 
ATOM   1570 C  CG    . GLN A 1 201 ? 40.289 -4.240 40.210  1.00 17.12 ?  199 GLN A CG    1 
ATOM   1571 C  CD    . GLN A 1 201 ? 40.621 -5.521 39.460  1.00 27.04 ?  199 GLN A CD    1 
ATOM   1572 O  OE1   . GLN A 1 201 ? 41.762 -5.898 39.427  1.00 19.78 ?  199 GLN A OE1   1 
ATOM   1573 N  NE2   . GLN A 1 201 ? 39.609 -6.271 39.007  1.00 28.88 ?  199 GLN A NE2   1 
ATOM   1574 N  N     . GLY A 1 202 ? 39.392 -1.771 42.279  1.00 10.10 ?  200 GLY A N     1 
ATOM   1575 C  CA    . GLY A 1 202 ? 38.878 -1.849 43.642  1.00 10.68 ?  200 GLY A CA    1 
ATOM   1576 C  C     . GLY A 1 202 ? 38.636 -0.505 44.288  1.00 11.27 ?  200 GLY A C     1 
ATOM   1577 O  O     . GLY A 1 202 ? 38.256 -0.491 45.473  1.00 12.22 ?  200 GLY A O     1 
ATOM   1578 N  N     . GLY A 1 203 ? 38.856 0.630  43.593  1.00 10.41 ?  201 GLY A N     1 
ATOM   1579 C  CA    . GLY A 1 203 ? 38.502 1.921  44.159  1.00 9.72  ?  201 GLY A CA    1 
ATOM   1580 C  C     . GLY A 1 203 ? 37.007 2.028  44.396  1.00 10.31 ?  201 GLY A C     1 
ATOM   1581 O  O     . GLY A 1 203 ? 36.214 1.514  43.599  1.00 10.31 ?  201 GLY A O     1 
ATOM   1582 N  N     . LEU A 1 204 ? 36.650 2.801  45.418  1.00 10.19 ?  202 LEU A N     1 
ATOM   1583 C  CA    . LEU A 1 204 ? 35.219 3.037  45.685  1.00 10.86 ?  202 LEU A CA    1 
ATOM   1584 C  C     . LEU A 1 204 ? 34.593 3.976  44.669  1.00 11.53 ?  202 LEU A C     1 
ATOM   1585 O  O     . LEU A 1 204 ? 35.322 4.740  43.929  1.00 11.28 ?  202 LEU A O     1 
ATOM   1586 C  CB    . LEU A 1 204 ? 35.015 3.518  47.125  1.00 11.69 ?  202 LEU A CB    1 
ATOM   1587 C  CG    . LEU A 1 204 ? 35.470 2.584  48.225  1.00 14.28 ?  202 LEU A CG    1 
ATOM   1588 C  CD1   . LEU A 1 204 ? 35.186 3.217  49.570  1.00 14.62 ?  202 LEU A CD1   1 
ATOM   1589 C  CD2   . LEU A 1 204 ? 34.810 1.244  48.084  1.00 17.56 ?  202 LEU A CD2   1 
ATOM   1590 N  N     . ARG A 1 205 ? 33.272 4.028  44.679  1.00 14.19 ?  203 ARG A N     1 
ATOM   1591 C  CA    . ARG A 1 205 ? 32.515 4.909  43.777  1.00 14.83 ?  203 ARG A CA    1 
ATOM   1592 C  C     . ARG A 1 205 ? 31.519 5.711  44.590  1.00 16.99 ?  203 ARG A C     1 
ATOM   1593 O  O     . ARG A 1 205 ? 30.864 5.114  45.486  1.00 17.62 ?  203 ARG A O     1 
ATOM   1594 C  CB    . ARG A 1 205 ? 31.799 4.110  42.698  1.00 15.48 ?  203 ARG A CB    1 
ATOM   1595 C  CG    . ARG A 1 205 ? 32.703 3.365  41.721  1.00 13.52 ?  203 ARG A CG    1 
ATOM   1596 C  CD    . ARG A 1 205 ? 33.380 4.355  40.794  1.00 13.11 ?  203 ARG A CD    1 
ATOM   1597 N  NE    . ARG A 1 205 ? 34.285 3.752  39.869  1.00 11.50 ?  203 ARG A NE    1 
ATOM   1598 C  CZ    . ARG A 1 205 ? 35.611 3.778  40.015  1.00 10.26 ?  203 ARG A CZ    1 
ATOM   1599 N  NH1   . ARG A 1 205 ? 36.169 4.241  41.107  1.00 10.37 ?  203 ARG A NH1   1 
ATOM   1600 N  NH2   . ARG A 1 205 ? 36.385 3.343  39.043  1.00 10.51 ?  203 ARG A NH2   1 
ATOM   1601 N  N     . TYR A 1 206 ? 31.309 6.944  44.215  1.00 16.70 ?  204 TYR A N     1 
ATOM   1602 C  CA    . TYR A 1 206 ? 30.222 7.764  44.790  1.00 16.93 ?  204 TYR A CA    1 
ATOM   1603 C  C     . TYR A 1 206 ? 28.908 7.160  44.323  1.00 15.79 ?  204 TYR A C     1 
ATOM   1604 O  O     . TYR A 1 206 ? 28.791 6.424  43.341  1.00 15.67 ?  204 TYR A O     1 
ATOM   1605 C  CB    . TYR A 1 206 ? 30.393 9.219  44.411  1.00 17.59 ?  204 TYR A CB    1 
ATOM   1606 C  CG    . TYR A 1 206 ? 31.625 9.871  44.974  1.00 17.44 ?  204 TYR A CG    1 
ATOM   1607 C  CD1   . TYR A 1 206 ? 31.904 9.817  46.334  1.00 20.05 ?  204 TYR A CD1   1 
ATOM   1608 C  CD2   . TYR A 1 206 ? 32.569 10.531 44.187  1.00 19.66 ?  204 TYR A CD2   1 
ATOM   1609 C  CE1   . TYR A 1 206 ? 33.023 10.422 46.875  1.00 18.46 ?  204 TYR A CE1   1 
ATOM   1610 C  CE2   . TYR A 1 206 ? 33.699 11.127 44.722  1.00 18.93 ?  204 TYR A CE2   1 
ATOM   1611 C  CZ    . TYR A 1 206 ? 33.935 11.090 46.086  1.00 18.00 ?  204 TYR A CZ    1 
ATOM   1612 O  OH    . TYR A 1 206 ? 35.025 11.683 46.637  1.00 19.07 ?  204 TYR A OH    1 
ATOM   1613 N  N     . GLU A 1 207 ? 27.839 7.632  44.996  1.00 20.77 ?  205 GLU A N     1 
ATOM   1614 C  CA    . GLU A 1 207 ? 26.474 7.067  44.793  1.00 24.48 ?  205 GLU A CA    1 
ATOM   1615 C  C     . GLU A 1 207 ? 25.745 7.814  43.686  1.00 19.57 ?  205 GLU A C     1 
ATOM   1616 O  O     . GLU A 1 207 ? 26.030 9.012  43.429  1.00 20.98 ?  205 GLU A O     1 
ATOM   1617 C  CB    . GLU A 1 207 ? 25.706 7.158  46.119  1.00 27.79 ?  205 GLU A CB    1 
ATOM   1618 C  CG    . GLU A 1 207 ? 26.225 6.179  47.161  1.00 36.79 ?  205 GLU A CG    1 
ATOM   1619 C  CD    . GLU A 1 207 ? 25.683 4.748  47.046  1.00 51.33 ?  205 GLU A CD    1 
ATOM   1620 O  OE1   . GLU A 1 207 ? 25.770 4.138  45.938  1.00 58.10 ?  205 GLU A OE1   1 
ATOM   1621 O  OE2   . GLU A 1 207 ? 25.166 4.223  48.073  1.00 61.52 ?  205 GLU A OE2   1 
ATOM   1622 N  N     . GLY A 1 208 ? 24.883 7.141  42.969  1.00 20.18 ?  206 GLY A N     1 
ATOM   1623 C  CA    . GLY A 1 208 ? 23.962 7.797  42.016  1.00 21.59 ?  206 GLY A CA    1 
ATOM   1624 C  C     . GLY A 1 208 ? 24.697 8.428  40.852  1.00 19.53 ?  206 GLY A C     1 
ATOM   1625 O  O     . GLY A 1 208 ? 25.680 7.843  40.415  1.00 17.91 ?  206 GLY A O     1 
ATOM   1626 N  N     . GLU A 1 209 ? 24.248 9.595  40.383  1.00 17.46 ?  207 GLU A N     1 
ATOM   1627 C  CA    . GLU A 1 209 ? 24.829 10.303 39.234  1.00 18.22 ?  207 GLU A CA    1 
ATOM   1628 C  C     . GLU A 1 209 ? 26.276 10.616 39.544  1.00 17.51 ?  207 GLU A C     1 
ATOM   1629 O  O     . GLU A 1 209 ? 27.036 10.736 38.599  1.00 22.23 ?  207 GLU A O     1 
ATOM   1630 C  CB    . GLU A 1 209 ? 24.197 11.683 39.039  1.00 23.13 ?  207 GLU A CB    1 
ATOM   1631 C  CG    . GLU A 1 209 ? 23.224 11.707 37.967  1.00 23.06 ?  207 GLU A CG    1 
ATOM   1632 C  CD    . GLU A 1 209 ? 22.471 13.013 37.846  1.00 20.03 ?  207 GLU A CD    1 
ATOM   1633 O  OE1   . GLU A 1 209 ? 22.953 14.080 38.280  1.00 19.32 ?  207 GLU A OE1   1 
ATOM   1634 O  OE2   . GLU A 1 209 ? 21.448 12.922 37.220  1.00 20.99 ?  207 GLU A OE2   1 
ATOM   1635 N  N     . THR A 1 210 ? 26.664 10.810 40.805  1.00 14.80 ?  208 THR A N     1 
ATOM   1636 C  CA    . THR A 1 210 ? 28.044 11.246 41.150  1.00 14.61 ?  208 THR A CA    1 
ATOM   1637 C  C     . THR A 1 210 ? 29.056 10.105 40.978  1.00 13.89 ?  208 THR A C     1 
ATOM   1638 O  O     . THR A 1 210 ? 30.251 10.373 41.016  1.00 12.78 ?  208 THR A O     1 
ATOM   1639 C  CB    . THR A 1 210 ? 28.135 11.903 42.522  1.00 20.94 ?  208 THR A CB    1 
ATOM   1640 O  OG1   . THR A 1 210 ? 27.937 10.932 43.515  1.00 32.51 ?  208 THR A OG1   1 
ATOM   1641 C  CG2   . THR A 1 210 ? 26.983 12.855 42.704  1.00 18.45 ?  208 THR A CG2   1 
ATOM   1642 N  N     . GLU A 1 211 ? 28.648 8.889  40.717  1.00 12.57 ?  209 GLU A N     1 
ATOM   1643 C  CA    . GLU A 1 211 ? 29.529 7.755  40.454  1.00 12.07 ?  209 GLU A CA    1 
ATOM   1644 C  C     . GLU A 1 211 ? 30.602 8.130  39.413  1.00 12.01 ?  209 GLU A C     1 
ATOM   1645 O  O     . GLU A 1 211 ? 31.754 7.711  39.593  1.00 10.82 ?  209 GLU A O     1 
ATOM   1646 C  CB    . GLU A 1 211 ? 28.720 6.547  39.969  1.00 13.91 ?  209 GLU A CB    1 
ATOM   1647 C  CG    . GLU A 1 211 ? 29.579 5.366  39.580  1.00 15.32 ?  209 GLU A CG    1 
ATOM   1648 C  CD    . GLU A 1 211 ? 28.894 4.127  39.073  1.00 22.47 ?  209 GLU A CD    1 
ATOM   1649 O  OE1   . GLU A 1 211 ? 27.618 4.099  39.066  1.00 28.24 ?  209 GLU A OE1   1 
ATOM   1650 O  OE2   . GLU A 1 211 ? 29.576 3.165  38.688  1.00 21.96 ?  209 GLU A OE2   1 
ATOM   1651 N  N     . GLY A 1 212 ? 30.218 8.828  38.360  1.00 11.19 ?  210 GLY A N     1 
ATOM   1652 C  CA    . GLY A 1 212 ? 31.120 9.147  37.250  1.00 10.92 ?  210 GLY A CA    1 
ATOM   1653 C  C     . GLY A 1 212 ? 31.941 10.385 37.505  1.00 10.98 ?  210 GLY A C     1 
ATOM   1654 O  O     . GLY A 1 212 ? 32.610 10.785 36.566  1.00 11.09 ?  210 GLY A O     1 
ATOM   1655 N  N     . ASN A 1 213 ? 31.891 11.021 38.643  1.00 9.94  ?  211 ASN A N     1 
ATOM   1656 C  CA    . ASN A 1 213 ? 32.587 12.298 38.839  1.00 10.81 ?  211 ASN A CA    1 
ATOM   1657 C  C     . ASN A 1 213 ? 34.094 12.075 38.784  1.00 9.41  ?  211 ASN A C     1 
ATOM   1658 O  O     . ASN A 1 213 ? 34.628 11.079 39.297  1.00 10.89 ?  211 ASN A O     1 
ATOM   1659 C  CB    . ASN A 1 213 ? 32.262 12.923 40.190  1.00 10.96 ?  211 ASN A CB    1 
ATOM   1660 C  CG    . ASN A 1 213 ? 31.019 13.768 40.141  1.00 11.47 ?  211 ASN A CG    1 
ATOM   1661 O  OD1   . ASN A 1 213 ? 30.157 13.570 39.308  1.00 11.74 ?  211 ASN A OD1   1 
ATOM   1662 N  ND2   . ASN A 1 213 ? 30.985 14.720 41.075  1.00 12.30 ?  211 ASN A ND2   1 
ATOM   1663 N  N     . ILE A 1 214 ? 34.827 13.049 38.226  1.00 9.40  ?  212 ILE A N     1 
ATOM   1664 C  CA    . ILE A 1 214 ? 36.241 13.212 38.557  1.00 9.06  ?  212 ILE A CA    1 
ATOM   1665 C  C     . ILE A 1 214 ? 36.295 13.730 40.001  1.00 9.58  ?  212 ILE A C     1 
ATOM   1666 O  O     . ILE A 1 214 ? 35.455 14.627 40.343  1.00 10.42 ?  212 ILE A O     1 
ATOM   1667 C  CB    . ILE A 1 214 ? 37.003 14.124 37.564  1.00 9.29  ?  212 ILE A CB    1 
ATOM   1668 C  CG1   . ILE A 1 214 ? 38.476 14.162 37.939  1.00 9.17  ?  212 ILE A CG1   1 
ATOM   1669 C  CG2   . ILE A 1 214 ? 36.442 15.547 37.462  1.00 9.86  ?  212 ILE A CG2   1 
ATOM   1670 C  CD1   . ILE A 1 214 ? 39.367 14.755 36.852  1.00 9.46  ?  212 ILE A CD1   1 
ATOM   1671 N  N     . LEU A 1 215 ? 37.258 13.292 40.778  1.00 9.26  ?  213 LEU A N     1 
ATOM   1672 C  CA    . LEU A 1 215 ? 37.647 13.921 42.024  1.00 9.44  ?  213 LEU A CA    1 
ATOM   1673 C  C     . LEU A 1 215 ? 39.033 14.497 41.855  1.00 9.96  ?  213 LEU A C     1 
ATOM   1674 O  O     . LEU A 1 215 ? 39.946 13.833 41.379  1.00 9.59  ?  213 LEU A O     1 
ATOM   1675 C  CB    . LEU A 1 215 ? 37.652 12.939 43.198  1.00 10.23 ?  213 LEU A CB    1 
ATOM   1676 C  CG    . LEU A 1 215 ? 38.357 13.379 44.472  1.00 11.64 ?  213 LEU A CG    1 
ATOM   1677 C  CD1   . LEU A 1 215 ? 37.586 14.501 45.182  1.00 12.28 ?  213 LEU A CD1   1 
ATOM   1678 C  CD2   . LEU A 1 215 ? 38.540 12.159 45.333  1.00 12.95 ?  213 LEU A CD2   1 
ATOM   1679 N  N     . THR A 1 216 ? 39.157 15.755 42.219  1.00 9.44  ?  214 THR A N     1 
ATOM   1680 C  CA    . THR A 1 216 ? 40.425 16.454 42.228  1.00 9.59  ?  214 THR A CA    1 
ATOM   1681 C  C     . THR A 1 216 ? 40.678 16.830 43.704  1.00 10.64 ?  214 THR A C     1 
ATOM   1682 O  O     . THR A 1 216 ? 39.869 17.442 44.289  1.00 10.95 ?  214 THR A O     1 
ATOM   1683 C  CB    . THR A 1 216 ? 40.372 17.709 41.351  1.00 11.58 ?  214 THR A CB    1 
ATOM   1684 O  OG1   . THR A 1 216 ? 40.077 17.331 40.005  1.00 12.50 ?  214 THR A OG1   1 
ATOM   1685 C  CG2   . THR A 1 216 ? 41.677 18.416 41.369  1.00 13.62 ?  214 THR A CG2   1 
ATOM   1686 N  N     . GLU A 1 217 ? 41.810 16.415 44.242  1.00 9.15  ?  215 GLU A N     1 
ATOM   1687 C  CA    . GLU A 1 217 ? 42.091 16.631 45.660  1.00 9.66  ?  215 GLU A CA    1 
ATOM   1688 C  C     . GLU A 1 217 ? 43.383 17.372 45.902  1.00 10.02 ?  215 GLU A C     1 
ATOM   1689 O  O     . GLU A 1 217 ? 44.424 16.945 45.533  1.00 9.99  ?  215 GLU A O     1 
ATOM   1690 C  CB    . GLU A 1 217 ? 42.130 15.287 46.425  1.00 11.57 ?  215 GLU A CB    1 
ATOM   1691 C  CG    . GLU A 1 217 ? 42.463 15.423 47.911  1.00 12.16 ?  215 GLU A CG    1 
ATOM   1692 C  CD    . GLU A 1 217 ? 42.240 14.130 48.669  1.00 14.95 ?  215 GLU A CD    1 
ATOM   1693 O  OE1   . GLU A 1 217 ? 41.869 13.122 48.031  1.00 15.72 ?  215 GLU A OE1   1 
ATOM   1694 O  OE2   . GLU A 1 217 ? 42.435 14.120 49.902  1.00 17.05 ?  215 GLU A OE2   1 
ATOM   1695 N  N     . ASN A 1 218 ? 43.316 18.509 46.538  1.00 10.96 ?  216 ASN A N     1 
ATOM   1696 C  CA    . ASN A 1 218 ? 44.513 19.244 46.836  1.00 11.66 ?  216 ASN A CA    1 
ATOM   1697 C  C     . ASN A 1 218 ? 45.412 18.579 47.860  1.00 11.67 ?  216 ASN A C     1 
ATOM   1698 O  O     . ASN A 1 218 ? 44.921 17.979 48.724  1.00 12.16 ?  216 ASN A O     1 
ATOM   1699 C  CB    . ASN A 1 218 ? 44.253 20.751 47.219  1.00 13.72 ?  216 ASN A CB    1 
ATOM   1700 C  CG    . ASN A 1 218 ? 43.404 20.972 48.464  1.00 18.77 ?  216 ASN A CG    1 
ATOM   1701 O  OD1   . ASN A 1 218 ? 43.111 20.102 49.241  1.00 21.75 ?  216 ASN A OD1   1 
ATOM   1702 N  ND2   . ASN A 1 218 ? 43.054 22.210 48.648  1.00 21.94 ?  216 ASN A ND2   1 
ATOM   1703 N  N     . ARG A 1 219 ? 46.730 18.694 47.665  1.00 10.78 ?  217 ARG A N     1 
ATOM   1704 C  CA    . ARG A 1 219 ? 47.763 18.180 48.587  1.00 12.58 ?  217 ARG A CA    1 
ATOM   1705 C  C     . ARG A 1 219 ? 48.678 19.370 48.938  1.00 11.93 ?  217 ARG A C     1 
ATOM   1706 O  O     . ARG A 1 219 ? 48.568 20.430 48.315  1.00 13.42 ?  217 ARG A O     1 
ATOM   1707 C  CB    . ARG A 1 219 ? 48.479 17.004 47.894  1.00 13.54 ?  217 ARG A CB    1 
ATOM   1708 C  CG    . ARG A 1 219 ? 47.554 15.816 47.584  1.00 13.61 ?  217 ARG A CG    1 
ATOM   1709 C  CD    . ARG A 1 219 ? 46.951 15.135 48.792  1.00 14.96 ?  217 ARG A CD    1 
ATOM   1710 N  NE    . ARG A 1 219 ? 47.993 14.660 49.639  1.00 14.33 ?  217 ARG A NE    1 
ATOM   1711 C  CZ    . ARG A 1 219 ? 48.112 14.853 50.967  1.00 17.60 ?  217 ARG A CZ    1 
ATOM   1712 N  NH1   . ARG A 1 219 ? 47.108 15.304 51.684  1.00 17.35 ?  217 ARG A NH1   1 
ATOM   1713 N  NH2   . ARG A 1 219 ? 49.223 14.502 51.539  1.00 18.91 ?  217 ARG A NH2   1 
ATOM   1714 N  N     . PRO A 1 220 ? 49.572 19.177 49.931  1.00 13.63 ?  218 PRO A N     1 
ATOM   1715 C  CA    . PRO A 1 220 ? 50.395 20.319 50.377  1.00 14.64 ?  218 PRO A CA    1 
ATOM   1716 C  C     . PRO A 1 220 ? 51.126 21.010 49.235  1.00 15.23 ?  218 PRO A C     1 
ATOM   1717 O  O     . PRO A 1 220 ? 51.203 22.235 49.226  1.00 17.04 ?  218 PRO A O     1 
ATOM   1718 C  CB    . PRO A 1 220 ? 51.286 19.652 51.410  1.00 14.78 ?  218 PRO A CB    1 
ATOM   1719 C  CG    . PRO A 1 220 ? 50.405 18.582 52.008  1.00 15.28 ?  218 PRO A CG    1 
ATOM   1720 C  CD    . PRO A 1 220 ? 49.674 18.006 50.809  1.00 14.90 ?  218 PRO A CD    1 
ATOM   1721 N  N     . HIS A 1 221 ? 51.667 20.246 48.263  1.00 13.47 ?  219 HIS A N     1 
ATOM   1722 C  CA    . HIS A 1 221 ? 52.498 20.842 47.208  1.00 14.40 ?  219 HIS A CA    1 
ATOM   1723 C  C     . HIS A 1 221 ? 52.109 20.235 45.870  1.00 12.88 ?  219 HIS A C     1 
ATOM   1724 O  O     . HIS A 1 221 ? 52.936 20.225 44.967  1.00 13.63 ?  219 HIS A O     1 
ATOM   1725 C  CB    . HIS A 1 221 ? 53.969 20.576 47.496  1.00 16.30 ?  219 HIS A CB    1 
ATOM   1726 C  CG    . HIS A 1 221 ? 54.419 21.101 48.825  1.00 20.75 ?  219 HIS A CG    1 
ATOM   1727 N  ND1   . HIS A 1 221 ? 54.442 22.436 49.073  1.00 23.96 ?  219 HIS A ND1   1 
ATOM   1728 C  CD2   . HIS A 1 221 ? 54.829 20.458 49.949  1.00 23.93 ?  219 HIS A CD2   1 
ATOM   1729 C  CE1   . HIS A 1 221 ? 54.850 22.622 50.348  1.00 22.53 ?  219 HIS A CE1   1 
ATOM   1730 N  NE2   . HIS A 1 221 ? 55.121 21.441 50.873  1.00 25.97 ?  219 HIS A NE2   1 
ATOM   1731 N  N     . GLY A 1 222 ? 50.869 19.830 45.748  1.00 11.30 ?  220 GLY A N     1 
ATOM   1732 C  CA    . GLY A 1 222 ? 50.429 19.268 44.452  1.00 10.87 ?  220 GLY A CA    1 
ATOM   1733 C  C     . GLY A 1 222 ? 48.967 18.930 44.514  1.00 11.55 ?  220 GLY A C     1 
ATOM   1734 O  O     . GLY A 1 222 ? 48.202 19.458 45.331  1.00 12.06 ?  220 GLY A O     1 
ATOM   1735 N  N     . TRP A 1 223 ? 48.514 18.028 43.665  1.00 9.27  ?  221 TRP A N     1 
ATOM   1736 C  CA    . TRP A 1 223 ? 47.117 17.593 43.724  1.00 8.59  ?  221 TRP A CA    1 
ATOM   1737 C  C     . TRP A 1 223 ? 46.992 16.217 43.076  1.00 8.95  ?  221 TRP A C     1 
ATOM   1738 O  O     . TRP A 1 223 ? 47.839 15.805 42.277  1.00 9.37  ?  221 TRP A O     1 
ATOM   1739 C  CB    . TRP A 1 223 ? 46.195 18.605 43.071  1.00 8.92  ?  221 TRP A CB    1 
ATOM   1740 C  CG    . TRP A 1 223 ? 46.558 18.970 41.665  1.00 8.53  ?  221 TRP A CG    1 
ATOM   1741 C  CD1   . TRP A 1 223 ? 47.425 19.938 41.286  1.00 8.64  ?  221 TRP A CD1   1 
ATOM   1742 C  CD2   . TRP A 1 223 ? 46.032 18.405 40.451  1.00 8.67  ?  221 TRP A CD2   1 
ATOM   1743 N  NE1   . TRP A 1 223 ? 47.465 20.023 39.903  1.00 8.73  ?  221 TRP A NE1   1 
ATOM   1744 C  CE2   . TRP A 1 223 ? 46.614 19.097 39.369  1.00 8.32  ?  221 TRP A CE2   1 
ATOM   1745 C  CE3   . TRP A 1 223 ? 45.074 17.414 40.181  1.00 9.35  ?  221 TRP A CE3   1 
ATOM   1746 C  CZ2   . TRP A 1 223 ? 46.290 18.810 38.032  1.00 8.55  ?  221 TRP A CZ2   1 
ATOM   1747 C  CZ3   . TRP A 1 223 ? 44.757 17.155 38.876  1.00 9.68  ?  221 TRP A CZ3   1 
ATOM   1748 C  CH2   . TRP A 1 223 ? 45.357 17.835 37.822  1.00 10.27 ?  221 TRP A CH2   1 
ATOM   1749 N  N     . LEU A 1 224 ? 45.932 15.527 43.457  1.00 8.48  ?  222 LEU A N     1 
ATOM   1750 C  CA    . LEU A 1 224 ? 45.581 14.195 42.913  1.00 8.42  ?  222 LEU A CA    1 
ATOM   1751 C  C     . LEU A 1 224 ? 44.340 14.283 42.042  1.00 7.65  ?  222 LEU A C     1 
ATOM   1752 O  O     . LEU A 1 224 ? 43.398 15.065 42.327  1.00 8.79  ?  222 LEU A O     1 
ATOM   1753 C  CB    . LEU A 1 224 ? 45.256 13.226 44.042  1.00 8.54  ?  222 LEU A CB    1 
ATOM   1754 C  CG    . LEU A 1 224 ? 46.413 12.827 44.925  1.00 8.96  ?  222 LEU A CG    1 
ATOM   1755 C  CD1   . LEU A 1 224 ? 45.904 12.269 46.251  1.00 11.64 ?  222 LEU A CD1   1 
ATOM   1756 C  CD2   . LEU A 1 224 ? 47.294 11.801 44.250  1.00 9.15  ?  222 LEU A CD2   1 
ATOM   1757 N  N     . TRP A 1 225 ? 44.311 13.460 40.982  1.00 8.00  ?  223 TRP A N     1 
ATOM   1758 C  CA    . TRP A 1 225 ? 43.065 13.165 40.263  1.00 7.86  ?  223 TRP A CA    1 
ATOM   1759 C  C     . TRP A 1 225 ? 42.668 11.725 40.551  1.00 7.63  ?  223 TRP A C     1 
ATOM   1760 O  O     . TRP A 1 225 ? 43.513 10.858 40.789  1.00 8.21  ?  223 TRP A O     1 
ATOM   1761 C  CB    . TRP A 1 225 ? 43.154 13.386 38.745  1.00 7.86  ?  223 TRP A CB    1 
ATOM   1762 C  CG    . TRP A 1 225 ? 43.889 12.360 37.928  1.00 7.74  ?  223 TRP A CG    1 
ATOM   1763 C  CD1   . TRP A 1 225 ? 43.457 11.100 37.586  1.00 7.82  ?  223 TRP A CD1   1 
ATOM   1764 C  CD2   . TRP A 1 225 ? 45.144 12.526 37.240  1.00 7.73  ?  223 TRP A CD2   1 
ATOM   1765 N  NE1   . TRP A 1 225 ? 44.356 10.506 36.743  1.00 7.71  ?  223 TRP A NE1   1 
ATOM   1766 C  CE2   . TRP A 1 225 ? 45.414 11.328 36.527  1.00 7.12  ?  223 TRP A CE2   1 
ATOM   1767 C  CE3   . TRP A 1 225 ? 46.081 13.560 37.139  1.00 8.46  ?  223 TRP A CE3   1 
ATOM   1768 C  CZ2   . TRP A 1 225 ? 46.542 11.169 35.742  1.00 8.31  ?  223 TRP A CZ2   1 
ATOM   1769 C  CZ3   . TRP A 1 225 ? 47.171 13.395 36.327  1.00 8.79  ?  223 TRP A CZ3   1 
ATOM   1770 C  CH2   . TRP A 1 225 ? 47.417 12.214 35.649  1.00 8.06  ?  223 TRP A CH2   1 
ATOM   1771 N  N     . TYR A 1 226 ? 41.374 11.492 40.448  1.00 8.34  ?  224 TYR A N     1 
ATOM   1772 C  CA    . TYR A 1 226 ? 40.737 10.182 40.623  1.00 7.81  ?  224 TYR A CA    1 
ATOM   1773 C  C     . TYR A 1 226 ? 39.602 10.133 39.628  1.00 7.59  ?  224 TYR A C     1 
ATOM   1774 O  O     . TYR A 1 226 ? 38.590 10.856 39.748  1.00 9.11  ?  224 TYR A O     1 
ATOM   1775 C  CB    . TYR A 1 226 ? 40.223 10.075 42.065  1.00 8.89  ?  224 TYR A CB    1 
ATOM   1776 C  CG    . TYR A 1 226 ? 39.632 8.754  42.508  1.00 8.53  ?  224 TYR A CG    1 
ATOM   1777 C  CD1   . TYR A 1 226 ? 38.326 8.442  42.212  1.00 9.26  ?  224 TYR A CD1   1 
ATOM   1778 C  CD2   . TYR A 1 226 ? 40.388 7.834  43.206  1.00 8.89  ?  224 TYR A CD2   1 
ATOM   1779 C  CE1   . TYR A 1 226 ? 37.736 7.240  42.626  1.00 8.73  ?  224 TYR A CE1   1 
ATOM   1780 C  CE2   . TYR A 1 226 ? 39.835 6.655  43.644  1.00 8.28  ?  224 TYR A CE2   1 
ATOM   1781 C  CZ    . TYR A 1 226 ? 38.516 6.380  43.360  1.00 8.94  ?  224 TYR A CZ    1 
ATOM   1782 O  OH    . TYR A 1 226 ? 37.992 5.174  43.813  1.00 10.54 ?  224 TYR A OH    1 
ATOM   1783 N  N     . ILE A 1 227 ? 39.822 9.387  38.534  1.00 8.13  ?  225 ILE A N     1 
ATOM   1784 C  CA    . ILE A 1 227 ? 38.950 9.330  37.358  1.00 8.19  ?  225 ILE A CA    1 
ATOM   1785 C  C     . ILE A 1 227 ? 38.374 7.937  37.202  1.00 8.87  ?  225 ILE A C     1 
ATOM   1786 O  O     . ILE A 1 227 ? 39.122 6.979  36.917  1.00 9.06  ?  225 ILE A O     1 
ATOM   1787 C  CB    . ILE A 1 227 ? 39.688 9.763  36.072  1.00 9.37  ?  225 ILE A CB    1 
ATOM   1788 C  CG1   . ILE A 1 227 ? 40.073 11.238 36.131  1.00 8.73  ?  225 ILE A CG1   1 
ATOM   1789 C  CG2   . ILE A 1 227 ? 38.809 9.454  34.875  1.00 9.95  ?  225 ILE A CG2   1 
ATOM   1790 C  CD1   . ILE A 1 227 ? 41.062 11.644 35.099  1.00 10.04 ?  225 ILE A CD1   1 
ATOM   1791 N  N     . PRO A 1 228 ? 37.052 7.755  37.388  1.00 8.86  ?  226 PRO A N     1 
ATOM   1792 C  CA    . PRO A 1 228 ? 36.458 6.427  37.227  1.00 8.84  ?  226 PRO A CA    1 
ATOM   1793 C  C     . PRO A 1 228 ? 36.246 6.109  35.760  1.00 9.66  ?  226 PRO A C     1 
ATOM   1794 O  O     . PRO A 1 228 ? 35.342 6.679  35.111  1.00 11.81 ?  226 PRO A O     1 
ATOM   1795 C  CB    . PRO A 1 228 ? 35.168 6.592  38.003  1.00 10.77 ?  226 PRO A CB    1 
ATOM   1796 C  CG    . PRO A 1 228 ? 34.779 8.016  37.876  1.00 11.33 ?  226 PRO A CG    1 
ATOM   1797 C  CD    . PRO A 1 228 ? 36.085 8.758  37.869  1.00 9.79  ?  226 PRO A CD    1 
ATOM   1798 N  N     . LEU A 1 229 ? 37.035 5.256  35.175  1.00 9.85  ?  227 LEU A N     1 
ATOM   1799 C  CA    . LEU A 1 229 ? 36.871 4.854  33.760  1.00 9.87  ?  227 LEU A CA    1 
ATOM   1800 C  C     . LEU A 1 229 ? 35.752 3.814  33.616  1.00 10.26 ?  227 LEU A C     1 
ATOM   1801 O  O     . LEU A 1 229 ? 35.158 3.707  32.553  1.00 11.48 ?  227 LEU A O     1 
ATOM   1802 C  CB    . LEU A 1 229 ? 38.184 4.302  33.211  1.00 10.47 ?  227 LEU A CB    1 
ATOM   1803 C  CG    . LEU A 1 229 ? 39.308 5.338  33.016  1.00 11.24 ?  227 LEU A CG    1 
ATOM   1804 C  CD1   . LEU A 1 229 ? 40.508 4.661  32.445  1.00 13.71 ?  227 LEU A CD1   1 
ATOM   1805 C  CD2   . LEU A 1 229 ? 38.839 6.407  32.046  1.00 13.05 ?  227 LEU A CD2   1 
ATOM   1806 N  N     . SER A 1 230 ? 35.587 3.022  34.623  1.00 10.20 ?  228 SER A N     1 
ATOM   1807 C  CA    . SER A 1 230 ? 34.591 1.939  34.667  1.00 10.42 ?  228 SER A CA    1 
ATOM   1808 C  C     . SER A 1 230 ? 34.290 1.617  36.111  1.00 10.65 ?  228 SER A C     1 
ATOM   1809 O  O     . SER A 1 230 ? 34.902 2.203  37.019  1.00 11.87 ?  228 SER A O     1 
ATOM   1810 C  CB    . SER A 1 230 ? 35.126 0.742  33.936  1.00 10.68 ?  228 SER A CB    1 
ATOM   1811 O  OG    . SER A 1 230 ? 36.154 0.145  34.673  1.00 11.74 ?  228 SER A OG    1 
ATOM   1812 N  N     . LYS A 1 231 ? 33.401 0.668  36.353  1.00 12.42 ?  229 LYS A N     1 
ATOM   1813 C  CA    . LYS A 1 231 ? 33.155 0.263  37.745  1.00 12.97 ?  229 LYS A CA    1 
ATOM   1814 C  C     . LYS A 1 231 ? 34.424 -0.310 38.364  1.00 11.91 ?  229 LYS A C     1 
ATOM   1815 O  O     . LYS A 1 231 ? 34.527 -0.245 39.551  1.00 13.55 ?  229 LYS A O     1 
ATOM   1816 C  CB    . LYS A 1 231 ? 32.039 -0.789 37.776  1.00 17.10 ?  229 LYS A CB    1 
ATOM   1817 C  CG    . LYS A 1 231 ? 30.665 -0.166 37.565  1.00 25.54 ?  229 LYS A CG    1 
ATOM   1818 C  CD    . LYS A 1 231 ? 29.533 -1.153 37.872  1.00 34.56 ?  229 LYS A CD    1 
ATOM   1819 C  CE    . LYS A 1 231 ? 28.139 -0.658 37.517  1.00 40.73 ?  229 LYS A CE    1 
ATOM   1820 N  NZ    . LYS A 1 231 ? 28.047 0.825  37.541  1.00 46.23 ?  229 LYS A NZ    1 
ATOM   1821 N  N     . ASP A 1 232 ? 35.344 -0.879 37.583  1.00 11.99 ?  230 ASP A N     1 
ATOM   1822 C  CA    . ASP A 1 232 ? 36.488 -1.635 38.116  1.00 12.48 ?  230 ASP A CA    1 
ATOM   1823 C  C     . ASP A 1 232 ? 37.804 -0.864 38.025  1.00 12.25 ?  230 ASP A C     1 
ATOM   1824 O  O     . ASP A 1 232 ? 38.671 -1.184 38.813  1.00 13.14 ?  230 ASP A O     1 
ATOM   1825 C  CB    . ASP A 1 232 ? 36.597 -3.009 37.444  1.00 13.50 ?  230 ASP A CB    1 
ATOM   1826 C  CG    . ASP A 1 232 ? 35.432 -3.907 37.935  1.00 17.11 ?  230 ASP A CG    1 
ATOM   1827 O  OD1   . ASP A 1 232 ? 35.381 -4.186 39.205  1.00 23.57 ?  230 ASP A OD1   1 
ATOM   1828 O  OD2   . ASP A 1 232 ? 34.536 -4.065 37.165  1.00 20.71 ?  230 ASP A OD2   1 
ATOM   1829 N  N     . ILE A 1 233 ? 37.927 0.136  37.152  1.00 10.52 ?  231 ILE A N     1 
ATOM   1830 C  CA    . ILE A 1 233 ? 39.235 0.813  36.936  1.00 9.29  ?  231 ILE A CA    1 
ATOM   1831 C  C     . ILE A 1 233 ? 39.109 2.305  37.233  1.00 9.24  ?  231 ILE A C     1 
ATOM   1832 O  O     . ILE A 1 233 ? 38.220 2.974  36.701  1.00 8.72  ?  231 ILE A O     1 
ATOM   1833 C  CB    . ILE A 1 233 ? 39.746 0.579  35.527  1.00 10.34 ?  231 ILE A CB    1 
ATOM   1834 C  CG1   . ILE A 1 233 ? 40.160 -0.882 35.338  1.00 10.87 ?  231 ILE A CG1   1 
ATOM   1835 C  CG2   . ILE A 1 233 ? 40.912 1.525  35.170  1.00 11.28 ?  231 ILE A CG2   1 
ATOM   1836 C  CD1   . ILE A 1 233 ? 41.323 -1.304 36.158  1.00 12.19 ?  231 ILE A CD1   1 
ATOM   1837 N  N     . THR A 1 234 ? 40.072 2.759  37.999  1.00 8.40  ?  232 THR A N     1 
ATOM   1838 C  CA    . THR A 1 234 ? 40.270 4.176  38.302  1.00 7.30  ?  232 THR A CA    1 
ATOM   1839 C  C     . THR A 1 234 ? 41.653 4.613  37.840  1.00 7.90  ?  232 THR A C     1 
ATOM   1840 O  O     . THR A 1 234 ? 42.647 3.942  38.140  1.00 8.83  ?  232 THR A O     1 
ATOM   1841 C  CB    . THR A 1 234 ? 40.147 4.472  39.798  1.00 7.71  ?  232 THR A CB    1 
ATOM   1842 O  OG1   . THR A 1 234 ? 38.953 3.839  40.309  1.00 9.14  ?  232 THR A OG1   1 
ATOM   1843 C  CG2   . THR A 1 234 ? 40.037 5.945  40.071  1.00 8.80  ?  232 THR A CG2   1 
ATOM   1844 N  N     . SER A 1 235 ? 41.723 5.729  37.138  1.00 7.82  ?  233 SER A N     1 
ATOM   1845 C  CA    . SER A 1 235 ? 42.958 6.429  36.808  1.00 6.80  ?  233 SER A CA    1 
ATOM   1846 C  C     . SER A 1 235 ? 43.278 7.319  37.982  1.00 6.90  ?  233 SER A C     1 
ATOM   1847 O  O     . SER A 1 235 ? 42.405 8.121  38.307  1.00 7.95  ?  233 SER A O     1 
ATOM   1848 C  CB    . SER A 1 235 ? 42.758 7.178  35.529  1.00 7.22  ?  233 SER A CB    1 
ATOM   1849 O  OG    . SER A 1 235 ? 43.908 7.957  35.228  1.00 8.12  ?  233 SER A OG    1 
ATOM   1850 N  N     . ILE A 1 236 ? 44.449 7.215  38.550  1.00 6.76  ?  234 ILE A N     1 
ATOM   1851 C  CA    . ILE A 1 236 ? 44.831 8.073  39.690  1.00 7.43  ?  234 ILE A CA    1 
ATOM   1852 C  C     . ILE A 1 236 ? 46.206 8.645  39.404  1.00 7.70  ?  234 ILE A C     1 
ATOM   1853 O  O     . ILE A 1 236 ? 47.151 7.892  39.138  1.00 7.48  ?  234 ILE A O     1 
ATOM   1854 C  CB    . ILE A 1 236 ? 44.830 7.323  41.044  1.00 8.01  ?  234 ILE A CB    1 
ATOM   1855 C  CG1   . ILE A 1 236 ? 43.480 6.616  41.234  1.00 8.13  ?  234 ILE A CG1   1 
ATOM   1856 C  CG2   . ILE A 1 236 ? 45.235 8.264  42.154  1.00 8.82  ?  234 ILE A CG2   1 
ATOM   1857 C  CD1   . ILE A 1 236 ? 43.425 5.852  42.564  1.00 8.64  ?  234 ILE A CD1   1 
ATOM   1858 N  N     . GLY A 1 237 ? 46.323 9.964  39.473  1.00 7.23  ?  235 GLY A N     1 
ATOM   1859 C  CA    . GLY A 1 237 ? 47.597 10.662 39.229  1.00 7.55  ?  235 GLY A CA    1 
ATOM   1860 C  C     . GLY A 1 237 ? 47.862 11.760 40.249  1.00 8.40  ?  235 GLY A C     1 
ATOM   1861 O  O     . GLY A 1 237 ? 46.912 12.257 40.886  1.00 9.05  ?  235 GLY A O     1 
ATOM   1862 N  N     . TYR A 1 238 ? 49.125 12.087 40.361  1.00 7.32  ?  236 TYR A N     1 
ATOM   1863 C  CA    . TYR A 1 238 ? 49.588 13.196 41.232  1.00 7.87  ?  236 TYR A CA    1 
ATOM   1864 C  C     . TYR A 1 238 ? 50.363 14.166 40.356  1.00 7.76  ?  236 TYR A C     1 
ATOM   1865 O  O     . TYR A 1 238 ? 51.235 13.734 39.587  1.00 8.24  ?  236 TYR A O     1 
ATOM   1866 C  CB    . TYR A 1 238 ? 50.508 12.647 42.325  1.00 8.34  ?  236 TYR A CB    1 
ATOM   1867 C  CG    . TYR A 1 238 ? 51.055 13.723 43.234  1.00 8.96  ?  236 TYR A CG    1 
ATOM   1868 C  CD1   . TYR A 1 238 ? 50.193 14.447 44.031  1.00 9.28  ?  236 TYR A CD1   1 
ATOM   1869 C  CD2   . TYR A 1 238 ? 52.402 13.980 43.288  1.00 8.92  ?  236 TYR A CD2   1 
ATOM   1870 C  CE1   . TYR A 1 238 ? 50.681 15.460 44.860  1.00 10.08 ?  236 TYR A CE1   1 
ATOM   1871 C  CE2   . TYR A 1 238 ? 52.901 14.966 44.125  1.00 10.05 ?  236 TYR A CE2   1 
ATOM   1872 C  CZ    . TYR A 1 238 ? 52.042 15.679 44.901  1.00 10.20 ?  236 TYR A CZ    1 
ATOM   1873 O  OH    . TYR A 1 238 ? 52.527 16.677 45.767  1.00 11.95 ?  236 TYR A OH    1 
ATOM   1874 N  N     . VAL A 1 239 ? 50.040 15.448 40.509  1.00 7.98  ?  237 VAL A N     1 
ATOM   1875 C  CA    . VAL A 1 239 ? 50.674 16.533 39.745  1.00 8.17  ?  237 VAL A CA    1 
ATOM   1876 C  C     . VAL A 1 239 ? 51.313 17.503 40.724  1.00 8.45  ?  237 VAL A C     1 
ATOM   1877 O  O     . VAL A 1 239 ? 50.694 17.862 41.732  1.00 9.84  ?  237 VAL A O     1 
ATOM   1878 C  CB    . VAL A 1 239 ? 49.627 17.228 38.892  1.00 7.92  ?  237 VAL A CB    1 
ATOM   1879 C  CG1   . VAL A 1 239 ? 50.202 18.444 38.179  1.00 9.31  ?  237 VAL A CG1   1 
ATOM   1880 C  CG2   . VAL A 1 239 ? 48.939 16.277 37.943  1.00 8.63  ?  237 VAL A CG2   1 
ATOM   1881 N  N     . THR A 1 240 ? 52.540 17.899 40.461  1.00 8.12  ?  238 THR A N     1 
ATOM   1882 C  CA    . THR A 1 240 ? 53.291 18.763 41.375  1.00 9.21  ?  238 THR A CA    1 
ATOM   1883 C  C     . THR A 1 240 ? 54.292 19.531 40.551  1.00 9.87  ?  238 THR A C     1 
ATOM   1884 O  O     . THR A 1 240 ? 54.706 19.073 39.490  1.00 8.76  ?  238 THR A O     1 
ATOM   1885 C  CB    . THR A 1 240 ? 53.985 17.933 42.438  1.00 10.44 ?  238 THR A CB    1 
ATOM   1886 O  OG1   . THR A 1 240 ? 54.540 18.770 43.464  1.00 11.34 ?  238 THR A OG1   1 
ATOM   1887 C  CG2   . THR A 1 240 ? 55.088 17.047 41.925  1.00 9.60  ?  238 THR A CG2   1 
ATOM   1888 N  N     . PRO A 1 241 ? 54.712 20.731 40.960  1.00 8.45  ?  239 PRO A N     1 
ATOM   1889 C  CA    . PRO A 1 241 ? 55.828 21.350 40.280  1.00 8.56  ?  239 PRO A CA    1 
ATOM   1890 C  C     . PRO A 1 241 ? 57.054 20.443 40.279  1.00 8.56  ?  239 PRO A C     1 
ATOM   1891 O  O     . PRO A 1 241 ? 57.370 19.771 41.286  1.00 9.48  ?  239 PRO A O     1 
ATOM   1892 C  CB    . PRO A 1 241 ? 56.077 22.609 41.118  1.00 8.93  ?  239 PRO A CB    1 
ATOM   1893 C  CG    . PRO A 1 241 ? 54.784 22.887 41.739  1.00 9.01  ?  239 PRO A CG    1 
ATOM   1894 C  CD    . PRO A 1 241 ? 54.286 21.503 42.136  1.00 9.35  ?  239 PRO A CD    1 
ATOM   1895 N  N     . SER A 1 242 ? 57.800 20.395 39.159  1.00 8.54  ?  240 SER A N     1 
ATOM   1896 C  CA    . SER A 1 242 ? 59.027 19.613 39.100  1.00 9.29  ?  240 SER A CA    1 
ATOM   1897 C  C     . SER A 1 242 ? 59.985 20.024 40.220  1.00 10.06 ?  240 SER A C     1 
ATOM   1898 O  O     . SER A 1 242 ? 60.701 19.153 40.731  1.00 10.39 ?  240 SER A O     1 
ATOM   1899 C  CB    . SER A 1 242 ? 59.644 19.682 37.718  1.00 10.75 ?  240 SER A CB    1 
ATOM   1900 O  OG    . SER A 1 242 ? 59.870 21.018 37.379  1.00 13.51 ?  240 SER A OG    1 
ATOM   1901 N  N     . SER A 1 243 ? 60.009 21.287 40.604  1.00 9.46  ?  241 SER A N     1 
ATOM   1902 C  CA    . SER A 1 243 ? 60.891 21.726 41.726  1.00 10.55 ?  241 SER A CA    1 
ATOM   1903 C  C     . SER A 1 243 ? 60.509 21.057 43.023  1.00 10.77 ?  241 SER A C     1 
ATOM   1904 O  O     . SER A 1 243 ? 61.395 20.718 43.797  1.00 11.31 ?  241 SER A O     1 
ATOM   1905 C  CB    . SER A 1 243 ? 60.879 23.181 41.893  1.00 12.23 ?  241 SER A CB    1 
ATOM   1906 O  OG    . SER A 1 243 ? 59.609 23.631 42.218  1.00 16.34 ?  241 SER A OG    1 
ATOM   1907 N  N     . ARG A 1 244 ? 59.222 20.852 43.293  1.00 10.43 ?  242 ARG A N     1 
ATOM   1908 C  CA    . ARG A 1 244 ? 58.798 20.207 44.568  1.00 10.89 ?  242 ARG A CA    1 
ATOM   1909 C  C     . ARG A 1 244 ? 59.171 18.747 44.545  1.00 11.00 ?  242 ARG A C     1 
ATOM   1910 O  O     . ARG A 1 244 ? 59.647 18.194 45.558  1.00 12.45 ?  242 ARG A O     1 
ATOM   1911 C  CB    . ARG A 1 244 ? 57.306 20.402 44.775  1.00 11.13 ?  242 ARG A CB    1 
ATOM   1912 C  CG    . ARG A 1 244 ? 56.900 21.817 45.081  1.00 13.66 ?  242 ARG A CG    1 
ATOM   1913 C  CD    . ARG A 1 244 ? 57.391 22.215 46.484  1.00 16.84 ?  242 ARG A CD    1 
ATOM   1914 N  NE    . ARG A 1 244 ? 56.872 23.527 46.783  1.00 19.63 ?  242 ARG A NE    1 
ATOM   1915 C  CZ    . ARG A 1 244 ? 57.182 24.216 47.852  1.00 26.24 ?  242 ARG A CZ    1 
ATOM   1916 N  NH1   . ARG A 1 244 ? 58.019 23.707 48.730  1.00 28.42 ?  242 ARG A NH1   1 
ATOM   1917 N  NH2   . ARG A 1 244 ? 56.615 25.392 48.036  1.00 27.03 ?  242 ARG A NH2   1 
ATOM   1918 N  N     . LEU A 1 245 ? 58.948 18.042 43.449  1.00 10.09 ?  243 LEU A N     1 
ATOM   1919 C  CA    . LEU A 1 245 ? 59.392 16.660 43.412  1.00 10.15 ?  243 LEU A CA    1 
ATOM   1920 C  C     . LEU A 1 245 ? 60.895 16.570 43.606  1.00 10.38 ?  243 LEU A C     1 
ATOM   1921 O  O     . LEU A 1 245 ? 61.379 15.723 44.341  1.00 11.84 ?  243 LEU A O     1 
ATOM   1922 C  CB    . LEU A 1 245 ? 58.962 15.980 42.096  1.00 10.92 ?  243 LEU A CB    1 
ATOM   1923 C  CG    . LEU A 1 245 ? 59.327 14.519 42.025  1.00 11.52 ?  243 LEU A CG    1 
ATOM   1924 C  CD1   . LEU A 1 245 ? 58.588 13.702 43.074  1.00 12.66 ?  243 LEU A CD1   1 
ATOM   1925 C  CD2   . LEU A 1 245 ? 59.077 13.949 40.652  1.00 12.03 ?  243 LEU A CD2   1 
ATOM   1926 N  N     . ALA A 1 246 ? 61.656 17.426 42.914  1.00 10.28 ?  244 ALA A N     1 
ATOM   1927 C  CA    . ALA A 1 246 ? 63.135 17.358 42.984  1.00 12.13 ?  244 ALA A CA    1 
ATOM   1928 C  C     . ALA A 1 246 ? 63.592 17.559 44.423  1.00 12.24 ?  244 ALA A C     1 
ATOM   1929 O  O     . ALA A 1 246 ? 64.519 16.827 44.865  1.00 14.68 ?  244 ALA A O     1 
ATOM   1930 C  CB    . ALA A 1 246 ? 63.745 18.375 42.027  1.00 13.93 ?  244 ALA A CB    1 
ATOM   1931 N  N     . GLU A 1 247 ? 63.024 18.527 45.091  1.00 12.18 ?  245 GLU A N     1 
ATOM   1932 C  CA    . GLU A 1 247 ? 63.367 18.878 46.498  1.00 13.91 ?  245 GLU A CA    1 
ATOM   1933 C  C     . GLU A 1 247 ? 63.137 17.670 47.367  1.00 16.60 ?  245 GLU A C     1 
ATOM   1934 O  O     . GLU A 1 247 ? 64.003 17.418 48.274  1.00 18.51 ?  245 GLU A O     1 
ATOM   1935 C  CB    . GLU A 1 247 ? 62.625 20.075 47.003  1.00 15.53 ?  245 GLU A CB    1 
ATOM   1936 C  CG    . GLU A 1 247 ? 63.054 21.372 46.340  1.00 18.45 ?  245 GLU A CG    1 
ATOM   1937 C  CD    . GLU A 1 247 ? 62.007 22.478 46.536  1.00 19.53 ?  245 GLU A CD    1 
ATOM   1938 O  OE1   . GLU A 1 247 ? 60.975 22.212 47.241  1.00 27.07 ?  245 GLU A OE1   1 
ATOM   1939 O  OE2   . GLU A 1 247 ? 62.214 23.552 46.010  1.00 28.00 ?  245 GLU A OE2   1 
ATOM   1940 N  N     . SER A 1 248 ? 62.103 16.877 47.095  1.00 14.39 ?  246 SER A N     1 
ATOM   1941 C  CA    . SER A 1 248 ? 61.730 15.732 47.963  1.00 14.69 ?  246 SER A CA    1 
ATOM   1942 C  C     . SER A 1 248 ? 62.804 14.638 47.897  1.00 14.70 ?  246 SER A C     1 
ATOM   1943 O  O     . SER A 1 248 ? 62.863 13.819 48.873  1.00 18.75 ?  246 SER A O     1 
ATOM   1944 C  CB    . SER A 1 248 ? 60.388 15.192 47.589  1.00 13.42 ?  246 SER A CB    1 
ATOM   1945 O  OG    . SER A 1 248 ? 60.456 14.359 46.425  1.00 12.89 ?  246 SER A OG    1 
ATOM   1946 N  N     . GLY A 1 249 ? 63.550 14.502 46.803  1.00 14.31 ?  247 GLY A N     1 
ATOM   1947 C  CA    . GLY A 1 249 ? 64.471 13.399 46.518  1.00 16.22 ?  247 GLY A CA    1 
ATOM   1948 C  C     . GLY A 1 249 ? 63.738 12.112 46.150  1.00 17.51 ?  247 GLY A C     1 
ATOM   1949 O  O     . GLY A 1 249 ? 64.460 11.176 45.881  1.00 20.65 ?  247 GLY A O     1 
ATOM   1950 N  N     . LEU A 1 250 ? 62.392 12.076 46.149  1.00 14.69 ?  248 LEU A N     1 
ATOM   1951 C  CA    . LEU A 1 250 ? 61.635 10.847 45.803  1.00 14.11 ?  248 LEU A CA    1 
ATOM   1952 C  C     . LEU A 1 250 ? 61.512 10.726 44.289  1.00 13.31 ?  248 LEU A C     1 
ATOM   1953 O  O     . LEU A 1 250 ? 61.539 11.741 43.542  1.00 14.87 ?  248 LEU A O     1 
ATOM   1954 C  CB    . LEU A 1 250 ? 60.223 10.895 46.385  1.00 13.40 ?  248 LEU A CB    1 
ATOM   1955 C  CG    . LEU A 1 250 ? 60.118 10.989 47.904  1.00 16.59 ?  248 LEU A CG    1 
ATOM   1956 C  CD1   . LEU A 1 250 ? 58.674 10.910 48.328  1.00 17.49 ?  248 LEU A CD1   1 
ATOM   1957 C  CD2   . LEU A 1 250 ? 60.952 9.927  48.626  1.00 20.47 ?  248 LEU A CD2   1 
ATOM   1958 N  N     . THR A 1 251 ? 61.404 9.481  43.851  1.00 12.76 ?  249 THR A N     1 
ATOM   1959 C  CA    . THR A 1 251 ? 61.000 9.217  42.457  1.00 12.60 ?  249 THR A CA    1 
ATOM   1960 C  C     . THR A 1 251 ? 59.549 9.638  42.268  1.00 11.75 ?  249 THR A C     1 
ATOM   1961 O  O     . THR A 1 251 ? 58.749 9.736  43.184  1.00 12.51 ?  249 THR A O     1 
ATOM   1962 C  CB    . THR A 1 251 ? 61.141 7.749  42.107  1.00 12.86 ?  249 THR A CB    1 
ATOM   1963 O  OG1   . THR A 1 251 ? 60.264 6.993  42.938  1.00 13.57 ?  249 THR A OG1   1 
ATOM   1964 C  CG2   . THR A 1 251 ? 62.554 7.257  42.313  1.00 14.50 ?  249 THR A CG2   1 
ATOM   1965 N  N     . PRO A 1 252 ? 59.163 9.883  41.037  1.00 10.80 ?  250 PRO A N     1 
ATOM   1966 C  CA    . PRO A 1 252 ? 57.768 10.258 40.826  1.00 11.21 ?  250 PRO A CA    1 
ATOM   1967 C  C     . PRO A 1 252 ? 56.788 9.155  41.285  1.00 11.14 ?  250 PRO A C     1 
ATOM   1968 O  O     . PRO A 1 252 ? 55.756 9.462  41.751  1.00 10.05 ?  250 PRO A O     1 
ATOM   1969 C  CB    . PRO A 1 252 ? 57.681 10.436 39.297  1.00 13.04 ?  250 PRO A CB    1 
ATOM   1970 C  CG    . PRO A 1 252 ? 59.094 10.570 38.828  1.00 14.14 ?  250 PRO A CG    1 
ATOM   1971 C  CD    . PRO A 1 252 ? 59.983 9.934  39.824  1.00 12.58 ?  250 PRO A CD    1 
ATOM   1972 N  N     . GLU A 1 253 ? 57.176 7.906  41.086  1.00 11.75 ?  251 GLU A N     1 
ATOM   1973 C  CA    . GLU A 1 253 ? 56.378 6.762  41.460  1.00 12.20 ?  251 GLU A CA    1 
ATOM   1974 C  C     . GLU A 1 253 ? 56.261 6.656  42.960  1.00 11.61 ?  251 GLU A C     1 
ATOM   1975 O  O     . GLU A 1 253 ? 55.209 6.386  43.441  1.00 11.73 ?  251 GLU A O     1 
ATOM   1976 C  CB    . GLU A 1 253 ? 56.979 5.492  40.892  1.00 14.28 ?  251 GLU A CB    1 
ATOM   1977 C  CG    . GLU A 1 253 ? 57.174 5.548  39.382  1.00 17.07 ?  251 GLU A CG    1 
ATOM   1978 C  CD    . GLU A 1 253 ? 58.378 6.298  38.843  1.00 19.73 ?  251 GLU A CD    1 
ATOM   1979 O  OE1   . GLU A 1 253 ? 59.277 6.636  39.642  1.00 16.88 ?  251 GLU A OE1   1 
ATOM   1980 O  OE2   . GLU A 1 253 ? 58.424 6.550  37.621  1.00 25.29 ?  251 GLU A OE2   1 
ATOM   1981 N  N     . ALA A 1 254 ? 57.346 6.828  43.698  1.00 10.90 ?  252 ALA A N     1 
ATOM   1982 C  CA    . ALA A 1 254 ? 57.280 6.792  45.167  1.00 11.15 ?  252 ALA A CA    1 
ATOM   1983 C  C     . ALA A 1 254 ? 56.405 7.943  45.652  1.00 10.42 ?  252 ALA A C     1 
ATOM   1984 O  O     . ALA A 1 254 ? 55.693 7.819  46.669  1.00 10.86 ?  252 ALA A O     1 
ATOM   1985 C  CB    . ALA A 1 254 ? 58.681 6.855  45.732  1.00 11.89 ?  252 ALA A CB    1 
ATOM   1986 N  N     . MET A 1 255 ? 56.507 9.102  45.040  1.00 10.19 ?  253 MET A N     1 
ATOM   1987 C  CA    . MET A 1 255 ? 55.724 10.243 45.455  1.00 9.89  ?  253 MET A CA    1 
ATOM   1988 C  C     . MET A 1 255 ? 54.244 9.964  45.250  1.00 10.06 ?  253 MET A C     1 
ATOM   1989 O  O     . MET A 1 255 ? 53.397 10.317 46.060  1.00 10.64 ?  253 MET A O     1 
ATOM   1990 C  CB    . MET A 1 255 ? 56.210 11.516 44.778  1.00 10.69 ?  253 MET A CB    1 
ATOM   1991 C  CG    . MET A 1 255 ? 55.447 12.718 45.142  1.00 10.38 ?  253 MET A CG    1 
ATOM   1992 S  SD    . MET A 1 255 ? 55.583 13.190 46.889  1.00 13.11 ?  253 MET A SD    1 
ATOM   1993 C  CE    . MET A 1 255 ? 57.021 14.251 46.801  1.00 13.84 ?  253 MET A CE    1 
ATOM   1994 N  N     . LEU A 1 256 ? 53.846 9.405  44.075  1.00 8.92  ?  254 LEU A N     1 
ATOM   1995 C  CA    . LEU A 1 256 ? 52.446 9.037  43.847  1.00 9.13  ?  254 LEU A CA    1 
ATOM   1996 C  C     . LEU A 1 256 ? 51.976 8.104  44.981  1.00 9.52  ?  254 LEU A C     1 
ATOM   1997 O  O     . LEU A 1 256 ? 50.892 8.341  45.509  1.00 9.62  ?  254 LEU A O     1 
ATOM   1998 C  CB    . LEU A 1 256 ? 52.285 8.340  42.489  1.00 9.05  ?  254 LEU A CB    1 
ATOM   1999 C  CG    . LEU A 1 256 ? 50.908 7.795  42.181  1.00 8.99  ?  254 LEU A CG    1 
ATOM   2000 C  CD1   . LEU A 1 256 ? 49.870 8.877  42.172  1.00 9.29  ?  254 LEU A CD1   1 
ATOM   2001 C  CD2   . LEU A 1 256 ? 50.927 7.045  40.879  1.00 9.67  ?  254 LEU A CD2   1 
ATOM   2002 N  N     . ASP A 1 257 ? 52.722 7.075  45.269  1.00 9.90  ?  255 ASP A N     1 
ATOM   2003 C  CA    . ASP A 1 257 ? 52.302 6.146  46.290  1.00 10.33 ?  255 ASP A CA    1 
ATOM   2004 C  C     . ASP A 1 257 ? 52.105 6.879  47.635  1.00 10.56 ?  255 ASP A C     1 
ATOM   2005 O  O     . ASP A 1 257 ? 51.182 6.642  48.318  1.00 11.53 ?  255 ASP A O     1 
ATOM   2006 C  CB    . ASP A 1 257 ? 53.373 5.081  46.544  1.00 10.45 ?  255 ASP A CB    1 
ATOM   2007 C  CG    . ASP A 1 257 ? 53.540 4.042  45.436  1.00 13.72 ?  255 ASP A CG    1 
ATOM   2008 O  OD1   . ASP A 1 257 ? 52.796 4.012  44.500  1.00 12.27 ?  255 ASP A OD1   1 
ATOM   2009 O  OD2   . ASP A 1 257 ? 54.462 3.270  45.600  1.00 17.73 ?  255 ASP A OD2   1 
ATOM   2010 N  N     . LYS A 1 258 ? 53.039 7.742  47.971  1.00 10.12 ?  256 LYS A N     1 
ATOM   2011 C  CA    . LYS A 1 258 ? 52.973 8.500  49.269  1.00 10.76 ?  256 LYS A CA    1 
ATOM   2012 C  C     . LYS A 1 258 ? 51.724 9.381  49.284  1.00 12.01 ?  256 LYS A C     1 
ATOM   2013 O  O     . LYS A 1 258 ? 50.951 9.369  50.269  1.00 11.93 ?  256 LYS A O     1 
ATOM   2014 C  CB    . LYS A 1 258 ? 54.241 9.325  49.385  1.00 11.61 ?  256 LYS A CB    1 
ATOM   2015 C  CG    . LYS A 1 258 ? 54.199 10.273 50.544  1.00 13.40 ?  256 LYS A CG    1 
ATOM   2016 C  CD    . LYS A 1 258 ? 55.430 11.201 50.578  1.00 15.40 ?  256 LYS A CD    1 
ATOM   2017 C  CE    . LYS A 1 258 ? 55.314 12.337 51.603  1.00 21.02 ?  256 LYS A CE    1 
ATOM   2018 N  NZ    . LYS A 1 258 ? 55.554 11.720 52.945  1.00 24.11 ?  256 LYS A NZ    1 
ATOM   2019 N  N     . GLN A 1 259 ? 51.440 10.069 48.197  1.00 10.14 ?  257 GLN A N     1 
ATOM   2020 C  CA    . GLN A 1 259 ? 50.323 11.016 48.191  1.00 10.56 ?  257 GLN A CA    1 
ATOM   2021 C  C     . GLN A 1 259 ? 48.989 10.296 48.234  1.00 10.13 ?  257 GLN A C     1 
ATOM   2022 O  O     . GLN A 1 259 ? 48.053 10.776 48.882  1.00 11.02 ?  257 GLN A O     1 
ATOM   2023 C  CB    . GLN A 1 259 ? 50.443 11.975 46.996  1.00 10.90 ?  257 GLN A CB    1 
ATOM   2024 C  CG    . GLN A 1 259 ? 51.689 12.841 47.116  1.00 11.20 ?  257 GLN A CG    1 
ATOM   2025 C  CD    . GLN A 1 259 ? 51.668 13.777 48.302  1.00 13.62 ?  257 GLN A CD    1 
ATOM   2026 O  OE1   . GLN A 1 259 ? 50.629 14.053 48.911  1.00 14.03 ?  257 GLN A OE1   1 
ATOM   2027 N  NE2   . GLN A 1 259 ? 52.844 14.242 48.630  1.00 15.04 ?  257 GLN A NE2   1 
ATOM   2028 N  N     . ILE A 1 260 ? 48.859 9.179  47.501  1.00 9.88  ?  258 ILE A N     1 
ATOM   2029 C  CA    . ILE A 1 260 ? 47.605 8.396  47.605  1.00 10.46 ?  258 ILE A CA    1 
ATOM   2030 C  C     . ILE A 1 260 ? 47.444 8.018  49.100  1.00 11.90 ?  258 ILE A C     1 
ATOM   2031 O  O     . ILE A 1 260 ? 46.304 8.193  49.630  1.00 13.31 ?  258 ILE A O     1 
ATOM   2032 C  CB    . ILE A 1 260 ? 47.693 7.167  46.693  1.00 10.31 ?  258 ILE A CB    1 
ATOM   2033 C  CG1   . ILE A 1 260 ? 47.623 7.585  45.219  1.00 10.91 ?  258 ILE A CG1   1 
ATOM   2034 C  CG2   . ILE A 1 260 ? 46.586 6.165  47.043  1.00 10.81 ?  258 ILE A CG2   1 
ATOM   2035 C  CD1   . ILE A 1 260 ? 47.902 6.466  44.206  1.00 11.91 ?  258 ILE A CD1   1 
ATOM   2036 N  N     . ALA A 1 261 ? 48.466 7.445  49.701  1.00 11.75 ?  259 ALA A N     1 
ATOM   2037 C  CA    . ALA A 1 261 ? 48.313 6.936  51.086  1.00 13.90 ?  259 ALA A CA    1 
ATOM   2038 C  C     . ALA A 1 261 ? 47.976 8.054  52.031  1.00 15.59 ?  259 ALA A C     1 
ATOM   2039 O  O     . ALA A 1 261 ? 47.187 7.818  52.982  1.00 16.70 ?  259 ALA A O     1 
ATOM   2040 C  CB    . ALA A 1 261 ? 49.603 6.308  51.473  1.00 14.77 ?  259 ALA A CB    1 
ATOM   2041 N  N     . GLU A 1 262 ? 48.554 9.202  51.878  1.00 12.48 ?  260 GLU A N     1 
ATOM   2042 C  CA    . GLU A 1 262 ? 48.438 10.267 52.875  1.00 12.89 ?  260 GLU A CA    1 
ATOM   2043 C  C     . GLU A 1 262 ? 47.247 11.170 52.689  1.00 15.06 ?  260 GLU A C     1 
ATOM   2044 O  O     . GLU A 1 262 ? 46.841 11.900 53.590  1.00 16.90 ?  260 GLU A O     1 
ATOM   2045 C  CB    . GLU A 1 262 ? 49.754 11.065 52.952  1.00 13.32 ?  260 GLU A CB    1 
ATOM   2046 C  CG    . GLU A 1 262 ? 50.958 10.263 53.485  1.00 16.38 ?  260 GLU A CG    1 
ATOM   2047 C  CD    . GLU A 1 262 ? 52.285 11.040 53.559  1.00 16.58 ?  260 GLU A CD    1 
ATOM   2048 O  OE1   . GLU A 1 262 ? 52.282 12.253 53.263  1.00 20.12 ?  260 GLU A OE1   1 
ATOM   2049 O  OE2   . GLU A 1 262 ? 53.315 10.429 53.912  1.00 20.07 ?  260 GLU A OE2   1 
ATOM   2050 N  N     . SER A 1 263 ? 46.689 11.111 51.498  1.00 12.09 ?  261 SER A N     1 
ATOM   2051 C  CA    . SER A 1 263 ? 45.499 11.897 51.182  1.00 12.36 ?  261 SER A CA    1 
ATOM   2052 C  C     . SER A 1 263 ? 44.274 11.471 52.009  1.00 13.19 ?  261 SER A C     1 
ATOM   2053 O  O     . SER A 1 263 ? 44.170 10.317 52.430  1.00 15.47 ?  261 SER A O     1 
ATOM   2054 C  CB    . SER A 1 263 ? 45.205 11.835 49.706  1.00 11.66 ?  261 SER A CB    1 
ATOM   2055 O  OG    . SER A 1 263 ? 44.753 10.532 49.341  1.00 12.29 ?  261 SER A OG    1 
ATOM   2056 N  N     . SER A 1 264 ? 43.342 12.363 52.119  1.00 14.34 ?  262 SER A N     1 
ATOM   2057 C  CA    . SER A 1 264 ? 42.133 12.100 52.889  1.00 14.33 ?  262 SER A CA    1 
ATOM   2058 C  C     . SER A 1 264 ? 41.088 11.352 52.067  1.00 13.61 ?  262 SER A C     1 
ATOM   2059 O  O     . SER A 1 264 ? 40.695 10.280 52.411  1.00 15.82 ?  262 SER A O     1 
ATOM   2060 C  CB    . SER A 1 264 ? 41.574 13.444 53.331  1.00 18.29 ?  262 SER A CB    1 
ATOM   2061 O  OG    . SER A 1 264 ? 40.339 13.336 53.980  1.00 25.25 ?  262 SER A OG    1 
ATOM   2062 N  N     . GLU A 1 265 ? 40.696 11.921 50.945  1.00 13.96 ?  263 GLU A N     1 
ATOM   2063 C  CA    . GLU A 1 265 ? 39.635 11.310 50.179  1.00 13.96 ?  263 GLU A CA    1 
ATOM   2064 C  C     . GLU A 1 265 ? 40.132 10.233 49.250  1.00 12.01 ?  263 GLU A C     1 
ATOM   2065 O  O     . GLU A 1 265 ? 39.604 9.180  49.238  1.00 12.44 ?  263 GLU A O     1 
ATOM   2066 C  CB    . GLU A 1 265 ? 38.855 12.383 49.464  1.00 14.62 ?  263 GLU A CB    1 
ATOM   2067 C  CG    . GLU A 1 265 ? 37.585 11.970 48.778  1.00 16.96 ?  263 GLU A CG    1 
ATOM   2068 C  CD    . GLU A 1 265 ? 36.440 11.522 49.674  1.00 21.36 ?  263 GLU A CD    1 
ATOM   2069 O  OE1   . GLU A 1 265 ? 36.656 11.393 50.898  1.00 23.83 ?  263 GLU A OE1   1 
ATOM   2070 O  OE2   . GLU A 1 265 ? 35.326 11.300 49.153  1.00 22.86 ?  263 GLU A OE2   1 
ATOM   2071 N  N     . VAL A 1 266 ? 41.137 10.487 48.447  1.00 11.52 ?  264 VAL A N     1 
ATOM   2072 C  CA    . VAL A 1 266 ? 41.672 9.410  47.595  1.00 12.06 ?  264 VAL A CA    1 
ATOM   2073 C  C     . VAL A 1 266 ? 42.154 8.268  48.502  1.00 11.80 ?  264 VAL A C     1 
ATOM   2074 O  O     . VAL A 1 266 ? 41.923 7.089  48.142  1.00 12.17 ?  264 VAL A O     1 
ATOM   2075 C  CB    . VAL A 1 266 ? 42.749 9.954  46.656  1.00 11.72 ?  264 VAL A CB    1 
ATOM   2076 C  CG1   . VAL A 1 266 ? 43.469 8.800  46.009  1.00 11.75 ?  264 VAL A CG1   1 
ATOM   2077 C  CG2   . VAL A 1 266 ? 42.145 10.894 45.640  1.00 11.22 ?  264 VAL A CG2   1 
ATOM   2078 N  N     . GLY A 1 267 ? 42.738 8.543  49.658  1.00 12.44 ?  265 GLY A N     1 
ATOM   2079 C  CA    . GLY A 1 267 ? 43.206 7.474  50.559  1.00 12.53 ?  265 GLY A CA    1 
ATOM   2080 C  C     . GLY A 1 267 ? 42.028 6.627  51.005  1.00 12.84 ?  265 GLY A C     1 
ATOM   2081 O  O     . GLY A 1 267 ? 42.135 5.363  51.008  1.00 14.61 ?  265 GLY A O     1 
ATOM   2082 N  N     . ARG A 1 268 ? 40.934 7.245  51.333  1.00 12.34 ?  266 ARG A N     1 
ATOM   2083 C  CA    . ARG A 1 268 ? 39.716 6.492  51.760  1.00 12.53 ?  266 ARG A CA    1 
ATOM   2084 C  C     . ARG A 1 268 ? 39.207 5.658  50.584  1.00 13.03 ?  266 ARG A C     1 
ATOM   2085 O  O     . ARG A 1 268 ? 38.842 4.461  50.694  1.00 13.76 ?  266 ARG A O     1 
ATOM   2086 C  CB    . ARG A 1 268 ? 38.643 7.439  52.248  1.00 14.80 ?  266 ARG A CB    1 
ATOM   2087 C  CG    . ARG A 1 268 ? 37.397 6.743  52.754  1.00 17.85 ?  266 ARG A CG    1 
ATOM   2088 C  CD    . ARG A 1 268 ? 36.325 7.789  53.104  1.00 19.85 ?  266 ARG A CD    1 
ATOM   2089 N  NE    . ARG A 1 268 ? 35.658 8.469  51.996  1.00 21.98 ?  266 ARG A NE    1 
ATOM   2090 C  CZ    . ARG A 1 268 ? 34.679 7.967  51.297  1.00 23.31 ?  266 ARG A CZ    1 
ATOM   2091 N  NH1   . ARG A 1 268 ? 34.230 6.750  51.571  1.00 26.41 ?  266 ARG A NH1   1 
ATOM   2092 N  NH2   . ARG A 1 268 ? 34.175 8.642  50.278  1.00 25.66 ?  266 ARG A NH2   1 
ATOM   2093 N  N     . LEU A 1 269 ? 39.084 6.280  49.422  1.00 11.42 ?  267 LEU A N     1 
ATOM   2094 C  CA    . LEU A 1 269 ? 38.519 5.618  48.235  1.00 11.64 ?  267 LEU A CA    1 
ATOM   2095 C  C     . LEU A 1 269 ? 39.382 4.440  47.759  1.00 11.24 ?  267 LEU A C     1 
ATOM   2096 O  O     . LEU A 1 269 ? 38.830 3.519  47.113  1.00 11.46 ?  267 LEU A O     1 
ATOM   2097 C  CB    . LEU A 1 269 ? 38.358 6.604  47.083  1.00 11.67 ?  267 LEU A CB    1 
ATOM   2098 C  CG    . LEU A 1 269 ? 37.358 7.725  47.355  1.00 12.27 ?  267 LEU A CG    1 
ATOM   2099 C  CD1   . LEU A 1 269 ? 37.476 8.761  46.242  1.00 15.89 ?  267 LEU A CD1   1 
ATOM   2100 C  CD2   . LEU A 1 269 ? 35.933 7.263  47.395  1.00 15.25 ?  267 LEU A CD2   1 
ATOM   2101 N  N     . THR A 1 270 ? 40.650 4.452  48.114  1.00 10.63 ?  268 THR A N     1 
ATOM   2102 C  CA    . THR A 1 270 ? 41.599 3.408  47.680  1.00 10.48 ?  268 THR A CA    1 
ATOM   2103 C  C     . THR A 1 270 ? 41.935 2.396  48.796  1.00 11.73 ?  268 THR A C     1 
ATOM   2104 O  O     . THR A 1 270 ? 42.874 1.604  48.630  1.00 11.60 ?  268 THR A O     1 
ATOM   2105 C  CB    . THR A 1 270 ? 42.886 4.008  47.106  1.00 11.19 ?  268 THR A CB    1 
ATOM   2106 O  OG1   . THR A 1 270 ? 43.515 4.836  48.074  1.00 12.28 ?  268 THR A OG1   1 
ATOM   2107 C  CG2   . THR A 1 270 ? 42.594 4.768  45.828  1.00 12.45 ?  268 THR A CG2   1 
ATOM   2108 N  N     . ALA A 1 271 ? 41.170 2.389  49.884  1.00 11.47 ?  269 ALA A N     1 
ATOM   2109 C  CA    . ALA A 1 271 ? 41.562 1.527  51.017  1.00 12.63 ?  269 ALA A CA    1 
ATOM   2110 C  C     . ALA A 1 271 ? 41.628 0.055  50.591  1.00 12.11 ?  269 ALA A C     1 
ATOM   2111 O  O     . ALA A 1 271 ? 42.452 -0.659 51.201  1.00 14.28 ?  269 ALA A O     1 
ATOM   2112 C  CB    . ALA A 1 271 ? 40.545 1.723  52.117  1.00 14.12 ?  269 ALA A CB    1 
ATOM   2113 N  N     . ASN A 1 272 ? 40.847 -0.383 49.635  1.00 11.57 ?  270 ASN A N     1 
ATOM   2114 C  CA    . ASN A 1 272 ? 40.849 -1.803 49.221  1.00 13.07 ?  270 ASN A CA    1 
ATOM   2115 C  C     . ASN A 1 272 ? 41.294 -1.892 47.772  1.00 13.55 ?  270 ASN A C     1 
ATOM   2116 O  O     . ASN A 1 272 ? 41.037 -2.913 47.163  1.00 17.17 ?  270 ASN A O     1 
ATOM   2117 C  CB    . ASN A 1 272 ? 39.508 -2.475 49.405  1.00 15.66 ?  270 ASN A CB    1 
ATOM   2118 C  CG    . ASN A 1 272 ? 39.298 -2.885 50.868  1.00 18.62 ?  270 ASN A CG    1 
ATOM   2119 O  OD1   . ASN A 1 272 ? 38.464 -2.260 51.478  1.00 21.44 ?  270 ASN A OD1   1 
ATOM   2120 N  ND2   . ASN A 1 272 ? 40.113 -3.785 51.439  1.00 20.91 ?  270 ASN A ND2   1 
ATOM   2121 N  N     . ALA A 1 273 ? 41.962 -0.862 47.274  1.00 12.14 ?  271 ALA A N     1 
ATOM   2122 C  CA    . ALA A 1 273 ? 42.371 -0.831 45.846  1.00 12.02 ?  271 ALA A CA    1 
ATOM   2123 C  C     . ALA A 1 273 ? 43.729 -1.500 45.680  1.00 11.51 ?  271 ALA A C     1 
ATOM   2124 O  O     . ALA A 1 273 ? 44.504 -1.613 46.617  1.00 14.57 ?  271 ALA A O     1 
ATOM   2125 C  CB    . ALA A 1 273 ? 42.367 0.598  45.371  1.00 12.26 ?  271 ALA A CB    1 
ATOM   2126 N  N     . ARG A 1 274 ? 44.025 -1.837 44.420  1.00 10.69 ?  272 ARG A N     1 
ATOM   2127 C  CA    . ARG A 1 274 ? 45.307 -2.419 44.025  1.00 11.30 ?  272 ARG A CA    1 
ATOM   2128 C  C     . ARG A 1 274 ? 45.745 -1.776 42.703  1.00 8.79  ?  272 ARG A C     1 
ATOM   2129 O  O     . ARG A 1 274 ? 44.888 -1.624 41.831  1.00 9.29  ?  272 ARG A O     1 
ATOM   2130 C  CB    . ARG A 1 274 ? 45.174 -3.940 43.827  1.00 13.43 ?  272 ARG A CB    1 
ATOM   2131 C  CG    . ARG A 1 274 ? 46.531 -4.602 43.692  1.00 18.82 ?  272 ARG A CG    1 
ATOM   2132 C  CD    . ARG A 1 274 ? 46.411 -5.859 42.903  1.00 20.01 ?  272 ARG A CD    1 
ATOM   2133 N  NE    . ARG A 1 274 ? 47.561 -6.770 43.053  1.00 20.18 ?  272 ARG A NE    1 
ATOM   2134 C  CZ    . ARG A 1 274 ? 48.760 -6.555 42.519  1.00 21.87 ?  272 ARG A CZ    1 
ATOM   2135 N  NH1   . ARG A 1 274 ? 49.057 -5.443 41.851  1.00 22.48 ?  272 ARG A NH1   1 
ATOM   2136 N  NH2   . ARG A 1 274 ? 49.696 -7.476 42.657  1.00 21.64 ?  272 ARG A NH2   1 
ATOM   2137 N  N     . ARG A 1 275 ? 47.001 -1.440 42.588  1.00 8.87  ?  273 ARG A N     1 
ATOM   2138 C  CA    . ARG A 1 275 ? 47.544 -0.923 41.317  1.00 9.16  ?  273 ARG A CA    1 
ATOM   2139 C  C     . ARG A 1 275 ? 47.564 -2.089 40.366  1.00 9.34  ?  273 ARG A C     1 
ATOM   2140 O  O     . ARG A 1 275 ? 48.015 -3.200 40.718  1.00 10.58 ?  273 ARG A O     1 
ATOM   2141 C  CB    . ARG A 1 275 ? 48.918 -0.339 41.526  1.00 9.06  ?  273 ARG A CB    1 
ATOM   2142 C  CG    . ARG A 1 275 ? 49.527 0.213  40.266  1.00 9.94  ?  273 ARG A CG    1 
ATOM   2143 C  CD    . ARG A 1 275 ? 50.765 0.990  40.553  1.00 10.31 ?  273 ARG A CD    1 
ATOM   2144 N  NE    . ARG A 1 275 ? 51.841 0.251  41.182  1.00 11.33 ?  273 ARG A NE    1 
ATOM   2145 C  CZ    . ARG A 1 275 ? 52.861 -0.336 40.588  1.00 11.22 ?  273 ARG A CZ    1 
ATOM   2146 N  NH1   . ARG A 1 275 ? 52.962 -0.372 39.268  1.00 11.36 ?  273 ARG A NH1   1 
ATOM   2147 N  NH2   . ARG A 1 275 ? 53.872 -0.858 41.266  1.00 13.19 ?  273 ARG A NH2   1 
ATOM   2148 N  N     . VAL A 1 276 ? 47.157 -1.834 39.119  1.00 7.86  ?  274 VAL A N     1 
ATOM   2149 C  CA    . VAL A 1 276 ? 47.039 -2.903 38.105  1.00 8.25  ?  274 VAL A CA    1 
ATOM   2150 C  C     . VAL A 1 276 ? 47.704 -2.519 36.811  1.00 8.78  ?  274 VAL A C     1 
ATOM   2151 O  O     . VAL A 1 276 ? 47.437 -3.177 35.762  1.00 8.97  ?  274 VAL A O     1 
ATOM   2152 C  CB    . VAL A 1 276 ? 45.593 -3.321 37.893  1.00 8.11  ?  274 VAL A CB    1 
ATOM   2153 C  CG1   . VAL A 1 276 ? 45.020 -3.941 39.155  1.00 9.52  ?  274 VAL A CG1   1 
ATOM   2154 C  CG2   . VAL A 1 276 ? 44.699 -2.203 37.458  1.00 8.14  ?  274 VAL A CG2   1 
ATOM   2155 N  N     . ASP A 1 277 ? 48.554 -1.499 36.781  1.00 7.44  ?  275 ASP A N     1 
ATOM   2156 C  CA    . ASP A 1 277 ? 49.321 -1.177 35.580  1.00 7.54  ?  275 ASP A CA    1 
ATOM   2157 C  C     . ASP A 1 277 ? 50.652 -0.619 36.010  1.00 7.51  ?  275 ASP A C     1 
ATOM   2158 O  O     . ASP A 1 277 ? 50.882 -0.361 37.231  1.00 8.60  ?  275 ASP A O     1 
ATOM   2159 C  CB    . ASP A 1 277 ? 48.578 -0.196 34.669  1.00 7.95  ?  275 ASP A CB    1 
ATOM   2160 C  CG    . ASP A 1 277 ? 49.041 -0.134 33.226  1.00 10.08 ?  275 ASP A CG    1 
ATOM   2161 O  OD1   . ASP A 1 277 ? 49.955 -0.894 32.831  1.00 10.32 ?  275 ASP A OD1   1 
ATOM   2162 O  OD2   . ASP A 1 277 ? 48.441 0.700  32.495  1.00 11.41 ?  275 ASP A OD2   1 
ATOM   2163 N  N     . ILE A 1 278 ? 51.518 -0.375 35.062  1.00 8.48  ?  276 ILE A N     1 
ATOM   2164 C  CA    . ILE A 1 278 ? 52.782 0.344  35.289  1.00 8.41  ?  276 ILE A CA    1 
ATOM   2165 C  C     . ILE A 1 278 ? 52.479 1.777  35.754  1.00 8.03  ?  276 ILE A C     1 
ATOM   2166 O  O     . ILE A 1 278 ? 51.353 2.269  35.632  1.00 8.19  ?  276 ILE A O     1 
ATOM   2167 C  CB    . ILE A 1 278 ? 53.601 0.358  33.985  1.00 9.30  ?  276 ILE A CB    1 
ATOM   2168 C  CG1   . ILE A 1 278 ? 52.948 1.189  32.880  1.00 9.50  ?  276 ILE A CG1   1 
ATOM   2169 C  CG2   . ILE A 1 278 ? 53.869 -1.073 33.519  1.00 11.16 ?  276 ILE A CG2   1 
ATOM   2170 C  CD1   . ILE A 1 278 ? 53.890 1.455  31.694  1.00 10.84 ?  276 ILE A CD1   1 
ATOM   2171 N  N     . TYR A 1 279 ? 53.552 2.398  36.221  1.00 7.95  ?  277 TYR A N     1 
ATOM   2172 C  CA    . TYR A 1 279 ? 53.566 3.850  36.420  1.00 7.79  ?  277 TYR A CA    1 
ATOM   2173 C  C     . TYR A 1 279 ? 53.928 4.506  35.096  1.00 8.62  ?  277 TYR A C     1 
ATOM   2174 O  O     . TYR A 1 279 ? 54.722 3.999  34.331  1.00 9.00  ?  277 TYR A O     1 
ATOM   2175 C  CB    . TYR A 1 279 ? 54.563 4.260  37.476  1.00 8.89  ?  277 TYR A CB    1 
ATOM   2176 C  CG    . TYR A 1 279 ? 54.338 3.739  38.854  1.00 8.41  ?  277 TYR A CG    1 
ATOM   2177 C  CD1   . TYR A 1 279 ? 53.415 4.301  39.693  1.00 9.65  ?  277 TYR A CD1   1 
ATOM   2178 C  CD2   . TYR A 1 279 ? 55.078 2.677  39.323  1.00 10.01 ?  277 TYR A CD2   1 
ATOM   2179 C  CE1   . TYR A 1 279 ? 53.252 3.874  41.007  1.00 10.47 ?  277 TYR A CE1   1 
ATOM   2180 C  CE2   . TYR A 1 279 ? 54.943 2.246  40.621  1.00 9.95  ?  277 TYR A CE2   1 
ATOM   2181 C  CZ    . TYR A 1 279 ? 54.022 2.819  41.428  1.00 11.04 ?  277 TYR A CZ    1 
ATOM   2182 O  OH    . TYR A 1 279 ? 53.867 2.383  42.748  1.00 12.80 ?  277 TYR A OH    1 
ATOM   2183 N  N     . ARG A 1 280 ? 53.333 5.672  34.862  1.00 7.90  ?  278 ARG A N     1 
ATOM   2184 C  CA    . ARG A 1 280 ? 53.704 6.537  33.755  1.00 8.11  ?  278 ARG A CA    1 
ATOM   2185 C  C     . ARG A 1 280 ? 53.908 7.956  34.288  1.00 7.85  ?  278 ARG A C     1 
ATOM   2186 O  O     . ARG A 1 280 ? 53.330 8.312  35.319  1.00 7.69  ?  278 ARG A O     1 
ATOM   2187 C  CB    . ARG A 1 280 ? 52.678 6.521  32.634  1.00 8.23  ?  278 ARG A CB    1 
ATOM   2188 C  CG    . ARG A 1 280 ? 52.557 5.182  31.902  1.00 8.43  ?  278 ARG A CG    1 
ATOM   2189 C  CD    . ARG A 1 280 ? 51.430 5.227  30.918  1.00 8.97  ?  278 ARG A CD    1 
ATOM   2190 N  NE    . ARG A 1 280 ? 51.282 3.976  30.160  1.00 9.48  ?  278 ARG A NE    1 
ATOM   2191 C  CZ    . ARG A 1 280 ? 50.591 2.946  30.591  1.00 9.93  ?  278 ARG A CZ    1 
ATOM   2192 N  NH1   . ARG A 1 280 ? 49.938 2.959  31.724  1.00 10.26 ?  278 ARG A NH1   1 
ATOM   2193 N  NH2   . ARG A 1 280 ? 50.522 1.864  29.817  1.00 11.67 ?  278 ARG A NH2   1 
ATOM   2194 N  N     . THR A 1 281 ? 54.706 8.740  33.563  1.00 8.03  ?  279 THR A N     1 
ATOM   2195 C  CA    . THR A 1 281 ? 54.915 10.164 33.891  1.00 8.31  ?  279 THR A CA    1 
ATOM   2196 C  C     . THR A 1 281 ? 54.839 11.026 32.656  1.00 8.40  ?  279 THR A C     1 
ATOM   2197 O  O     . THR A 1 281 ? 54.994 10.557 31.534  1.00 9.43  ?  279 THR A O     1 
ATOM   2198 C  CB    . THR A 1 281 ? 56.234 10.427 34.606  1.00 9.65  ?  279 THR A CB    1 
ATOM   2199 O  OG1   . THR A 1 281 ? 57.309 10.134 33.703  1.00 12.78 ?  279 THR A OG1   1 
ATOM   2200 C  CG2   . THR A 1 281 ? 56.364 9.583  35.837  1.00 11.45 ?  279 THR A CG2   1 
ATOM   2201 N  N     . ALA A 1 282 ? 54.623 12.317 32.894  1.00 8.13  ?  280 ALA A N     1 
ATOM   2202 C  CA    . ALA A 1 282 ? 54.683 13.356 31.848  1.00 8.18  ?  280 ALA A CA    1 
ATOM   2203 C  C     . ALA A 1 282 ? 55.143 14.607 32.548  1.00 7.89  ?  280 ALA A C     1 
ATOM   2204 O  O     . ALA A 1 282 ? 54.955 14.755 33.768  1.00 8.08  ?  280 ALA A O     1 
ATOM   2205 C  CB    . ALA A 1 282 ? 53.302 13.602 31.300  1.00 9.47  ?  280 ALA A CB    1 
ATOM   2206 N  N     . ARG A 1 283 ? 55.749 15.524 31.824  1.00 7.73  ?  281 ARG A N     1 
ATOM   2207 C  CA    . ARG A 1 283 ? 56.143 16.829 32.394  1.00 8.76  ?  281 ARG A CA    1 
ATOM   2208 C  C     . ARG A 1 283 ? 56.251 17.865 31.305  1.00 8.35  ?  281 ARG A C     1 
ATOM   2209 O  O     . ARG A 1 283 ? 56.301 17.538 30.127  1.00 9.08  ?  281 ARG A O     1 
ATOM   2210 C  CB    . ARG A 1 283 ? 57.451 16.725 33.131  1.00 8.89  ?  281 ARG A CB    1 
ATOM   2211 C  CG    . ARG A 1 283 ? 58.617 16.308 32.251  1.00 9.95  ?  281 ARG A CG    1 
ATOM   2212 C  CD    . ARG A 1 283 ? 59.925 16.048 33.009  1.00 10.22 ?  281 ARG A CD    1 
ATOM   2213 N  NE    . ARG A 1 283 ? 60.374 17.242 33.675  1.00 10.37 ?  281 ARG A NE    1 
ATOM   2214 C  CZ    . ARG A 1 283 ? 61.242 17.250 34.673  1.00 11.20 ?  281 ARG A CZ    1 
ATOM   2215 N  NH1   . ARG A 1 283 ? 61.707 16.150 35.214  1.00 12.57 ?  281 ARG A NH1   1 
ATOM   2216 N  NH2   . ARG A 1 283 ? 61.640 18.404 35.193  1.00 10.42 ?  281 ARG A NH2   1 
ATOM   2217 N  N     . ASP A 1 284 ? 56.318 19.128 31.742  1.00 8.65  ?  282 ASP A N     1 
ATOM   2218 C  CA    . ASP A 1 284 ? 56.751 20.220 30.847  1.00 9.52  ?  282 ASP A CA    1 
ATOM   2219 C  C     . ASP A 1 284 ? 55.852 20.354 29.631  1.00 8.16  ?  282 ASP A C     1 
ATOM   2220 O  O     . ASP A 1 284 ? 56.269 20.168 28.483  1.00 9.53  ?  282 ASP A O     1 
ATOM   2221 C  CB    . ASP A 1 284 ? 58.232 20.093 30.527  1.00 9.57  ?  282 ASP A CB    1 
ATOM   2222 C  CG    . ASP A 1 284 ? 59.088 20.229 31.748  1.00 11.06 ?  282 ASP A CG    1 
ATOM   2223 O  OD1   . ASP A 1 284 ? 58.818 21.146 32.560  1.00 11.23 ?  282 ASP A OD1   1 
ATOM   2224 O  OD2   . ASP A 1 284 ? 60.056 19.426 31.872  1.00 11.53 ?  282 ASP A OD2   1 
ATOM   2225 N  N     . TRP A 1 285 ? 54.599 20.621 29.945  1.00 8.20  ?  283 TRP A N     1 
ATOM   2226 C  CA    . TRP A 1 285 ? 53.494 20.568 28.973  1.00 7.97  ?  283 TRP A CA    1 
ATOM   2227 C  C     . TRP A 1 285 ? 52.858 21.896 28.713  1.00 8.48  ?  283 TRP A C     1 
ATOM   2228 O  O     . TRP A 1 285 ? 51.955 21.941 27.857  1.00 8.83  ?  283 TRP A O     1 
ATOM   2229 C  CB    . TRP A 1 285 ? 52.428 19.561 29.458  1.00 7.88  ?  283 TRP A CB    1 
ATOM   2230 C  CG    . TRP A 1 285 ? 51.947 19.798 30.844  1.00 7.33  ?  283 TRP A CG    1 
ATOM   2231 C  CD1   . TRP A 1 285 ? 51.333 20.914 31.321  1.00 7.43  ?  283 TRP A CD1   1 
ATOM   2232 C  CD2   . TRP A 1 285 ? 52.024 18.881 31.944  1.00 7.26  ?  283 TRP A CD2   1 
ATOM   2233 N  NE1   . TRP A 1 285 ? 51.056 20.790 32.668  1.00 7.85  ?  283 TRP A NE1   1 
ATOM   2234 C  CE2   . TRP A 1 285 ? 51.437 19.530 33.046  1.00 7.60  ?  283 TRP A CE2   1 
ATOM   2235 C  CE3   . TRP A 1 285 ? 52.567 17.606 32.076  1.00 7.61  ?  283 TRP A CE3   1 
ATOM   2236 C  CZ2   . TRP A 1 285 ? 51.332 18.932 34.287  1.00 8.30  ?  283 TRP A CZ2   1 
ATOM   2237 C  CZ3   . TRP A 1 285 ? 52.429 17.015 33.318  1.00 8.47  ?  283 TRP A CZ3   1 
ATOM   2238 C  CH2   . TRP A 1 285 ? 51.846 17.670 34.398  1.00 8.03  ?  283 TRP A CH2   1 
ATOM   2239 N  N     . SER A 1 286 ? 53.237 22.983 29.400  1.00 7.93  ?  284 SER A N     1 
ATOM   2240 C  CA    . SER A 1 286 ? 52.444 24.240 29.408  1.00 7.71  ?  284 SER A CA    1 
ATOM   2241 C  C     . SER A 1 286 ? 53.087 25.319 28.569  1.00 8.24  ?  284 SER A C     1 
ATOM   2242 O  O     . SER A 1 286 ? 54.207 25.784 28.902  1.00 8.51  ?  284 SER A O     1 
ATOM   2243 C  CB    . SER A 1 286 ? 52.225 24.718 30.820  1.00 8.50  ?  284 SER A CB    1 
ATOM   2244 O  OG    . SER A 1 286 ? 51.256 25.746 30.834  1.00 8.66  ?  284 SER A OG    1 
ATOM   2245 N  N     . TYR A 1 287 ? 52.452 25.681 27.467  1.00 7.51  ?  285 TYR A N     1 
ATOM   2246 C  CA    . TYR A 1 287 ? 53.064 26.619 26.497  1.00 8.51  ?  285 TYR A CA    1 
ATOM   2247 C  C     . TYR A 1 287 ? 51.988 27.054 25.529  1.00 8.62  ?  285 TYR A C     1 
ATOM   2248 O  O     . TYR A 1 287 ? 50.887 26.505 25.481  1.00 8.79  ?  285 TYR A O     1 
ATOM   2249 C  CB    . TYR A 1 287 ? 54.156 25.917 25.689  1.00 8.45  ?  285 TYR A CB    1 
ATOM   2250 C  CG    . TYR A 1 287 ? 53.683 24.667 24.966  1.00 8.66  ?  285 TYR A CG    1 
ATOM   2251 C  CD1   . TYR A 1 287 ? 53.040 24.723 23.735  1.00 8.86  ?  285 TYR A CD1   1 
ATOM   2252 C  CD2   . TYR A 1 287 ? 53.896 23.425 25.514  1.00 8.81  ?  285 TYR A CD2   1 
ATOM   2253 C  CE1   . TYR A 1 287 ? 52.576 23.577 23.121  1.00 10.16 ?  285 TYR A CE1   1 
ATOM   2254 C  CE2   . TYR A 1 287 ? 53.398 22.269 24.939  1.00 9.31  ?  285 TYR A CE2   1 
ATOM   2255 C  CZ    . TYR A 1 287 ? 52.793 22.355 23.693  1.00 10.69 ?  285 TYR A CZ    1 
ATOM   2256 O  OH    . TYR A 1 287 ? 52.351 21.188 23.118  1.00 11.38 ?  285 TYR A OH    1 
ATOM   2257 N  N     . VAL A 1 288 ? 52.338 28.094 24.765  1.00 8.74  ?  286 VAL A N     1 
ATOM   2258 C  CA    . VAL A 1 288 ? 51.515 28.533 23.621  1.00 8.47  ?  286 VAL A CA    1 
ATOM   2259 C  C     . VAL A 1 288 ? 52.477 28.837 22.499  1.00 8.63  ?  286 VAL A C     1 
ATOM   2260 O  O     . VAL A 1 288 ? 53.544 29.467 22.752  1.00 9.72  ?  286 VAL A O     1 
ATOM   2261 C  CB    . VAL A 1 288 ? 50.637 29.718 23.968  1.00 10.26 ?  286 VAL A CB    1 
ATOM   2262 C  CG1   . VAL A 1 288 ? 51.474 30.893 24.401  1.00 13.85 ?  286 VAL A CG1   1 
ATOM   2263 C  CG2   . VAL A 1 288 ? 49.773 30.106 22.807  1.00 10.46 ?  286 VAL A CG2   1 
ATOM   2264 N  N     . CYS A 1 289 ? 52.167 28.504 21.252  1.00 7.62  ?  287 CYS A N     1 
ATOM   2265 C  CA    . CYS A 1 289 ? 53.005 28.898 20.111  1.00 8.73  ?  287 CYS A CA    1 
ATOM   2266 C  C     . CYS A 1 289 ? 52.764 30.381 19.837  1.00 8.27  ?  287 CYS A C     1 
ATOM   2267 O  O     . CYS A 1 289 ? 51.698 30.921 20.021  1.00 9.45  ?  287 CYS A O     1 
ATOM   2268 C  CB    . CYS A 1 289 ? 52.712 28.034 18.896  1.00 8.41  ?  287 CYS A CB    1 
ATOM   2269 S  SG    . CYS A 1 289 ? 53.460 26.396 19.030  1.00 10.11 ?  287 CYS A SG    1 
ATOM   2270 N  N     . GLU A 1 290 ? 53.797 31.007 19.262  1.00 8.49  ?  288 GLU A N     1 
ATOM   2271 C  CA    . GLU A 1 290 ? 53.730 32.431 18.920  1.00 9.13  ?  288 GLU A CA    1 
ATOM   2272 C  C     . GLU A 1 290 ? 52.630 32.727 17.902  1.00 8.36  ?  288 GLU A C     1 
ATOM   2273 O  O     . GLU A 1 290 ? 51.981 33.768 17.962  1.00 9.96  ?  288 GLU A O     1 
ATOM   2274 C  CB    . GLU A 1 290 ? 55.054 32.887 18.352  1.00 10.85 ?  288 GLU A CB    1 
ATOM   2275 C  CG    . GLU A 1 290 ? 55.193 34.377 18.176  1.00 17.48 ?  288 GLU A CG    1 
ATOM   2276 C  CD    . GLU A 1 290 ? 56.489 34.717 17.444  1.00 21.60 ?  288 GLU A CD    1 
ATOM   2277 O  OE1   . GLU A 1 290 ? 57.406 33.844 17.282  1.00 20.79 ?  288 GLU A OE1   1 
ATOM   2278 O  OE2   . GLU A 1 290 ? 56.505 35.889 16.931  1.00 35.13 ?  288 GLU A OE2   1 
ATOM   2279 N  N     . ARG A 1 291 ? 52.456 31.835 16.950  1.00 8.77  ?  289 ARG A N     1 
ATOM   2280 C  CA    . ARG A 1 291 ? 51.379 31.998 15.977  1.00 8.76  ?  289 ARG A CA    1 
ATOM   2281 C  C     . ARG A 1 291 ? 50.786 30.612 15.720  1.00 8.20  ?  289 ARG A C     1 
ATOM   2282 O  O     . ARG A 1 291 ? 51.423 29.650 15.896  1.00 8.33  ?  289 ARG A O     1 
ATOM   2283 C  CB    . ARG A 1 291 ? 51.880 32.603 14.648  1.00 9.50  ?  289 ARG A CB    1 
ATOM   2284 C  CG    . ARG A 1 291 ? 52.979 31.837 13.972  1.00 9.15  ?  289 ARG A CG    1 
ATOM   2285 C  CD    . ARG A 1 291 ? 53.424 32.541 12.691  1.00 10.92 ?  289 ARG A CD    1 
ATOM   2286 N  NE    . ARG A 1 291 ? 54.418 31.757 12.003  1.00 11.58 ?  289 ARG A NE    1 
ATOM   2287 C  CZ    . ARG A 1 291 ? 55.690 31.762 12.325  1.00 12.38 ?  289 ARG A CZ    1 
ATOM   2288 N  NH1   . ARG A 1 291 ? 56.144 32.535 13.261  1.00 12.74 ?  289 ARG A NH1   1 
ATOM   2289 N  NH2   . ARG A 1 291 ? 56.489 31.008 11.675  1.00 14.41 ?  289 ARG A NH2   1 
ATOM   2290 N  N     . PHE A 1 292 ? 49.539 30.585 15.296  1.00 7.66  ?  290 PHE A N     1 
ATOM   2291 C  CA    . PHE A 1 292 ? 48.821 29.335 15.018  1.00 7.44  ?  290 PHE A CA    1 
ATOM   2292 C  C     . PHE A 1 292 ? 48.557 29.142 13.500  1.00 8.33  ?  290 PHE A C     1 
ATOM   2293 O  O     . PHE A 1 292 ? 47.809 28.290 13.152  1.00 8.62  ?  290 PHE A O     1 
ATOM   2294 C  CB    . PHE A 1 292 ? 47.455 29.297 15.727  1.00 7.61  ?  290 PHE A CB    1 
ATOM   2295 C  CG    . PHE A 1 292 ? 47.470 29.340 17.242  1.00 7.84  ?  290 PHE A CG    1 
ATOM   2296 C  CD1   . PHE A 1 292 ? 48.605 29.349 17.973  1.00 8.28  ?  290 PHE A CD1   1 
ATOM   2297 C  CD2   . PHE A 1 292 ? 46.295 29.345 17.893  1.00 8.69  ?  290 PHE A CD2   1 
ATOM   2298 C  CE1   . PHE A 1 292 ? 48.573 29.399 19.340  1.00 9.06  ?  290 PHE A CE1   1 
ATOM   2299 C  CE2   . PHE A 1 292 ? 46.233 29.390 19.260  1.00 9.68  ?  290 PHE A CE2   1 
ATOM   2300 C  CZ    . PHE A 1 292 ? 47.382 29.427 19.983  1.00 8.69  ?  290 PHE A CZ    1 
ATOM   2301 N  N     . SER A 1 293 ? 49.197 29.958 12.670  1.00 8.40  ?  291 SER A N     1 
ATOM   2302 C  CA    . SER A 1 293 ? 49.044 29.813 11.221  1.00 8.60  ?  291 SER A CA    1 
ATOM   2303 C  C     . SER A 1 293 ? 50.134 30.604 10.543  1.00 8.92  ?  291 SER A C     1 
ATOM   2304 O  O     . SER A 1 293 ? 50.834 31.411 11.145  1.00 9.99  ?  291 SER A O     1 
ATOM   2305 C  CB    . SER A 1 293 ? 47.726 30.260 10.737  1.00 9.23  ?  291 SER A CB    1 
ATOM   2306 O  OG    . SER A 1 293 ? 47.681 31.710 10.647  1.00 10.19 ?  291 SER A OG    1 
ATOM   2307 N  N     . GLY A 1 294 ? 50.188 30.373 9.239   1.00 8.38  ?  292 GLY A N     1 
ATOM   2308 C  CA    . GLY A 1 294 ? 51.023 31.123 8.320   1.00 9.29  ?  292 GLY A CA    1 
ATOM   2309 C  C     . GLY A 1 294 ? 50.620 30.677 6.929   1.00 8.77  ?  292 GLY A C     1 
ATOM   2310 O  O     . GLY A 1 294 ? 49.644 29.961 6.752   1.00 9.63  ?  292 GLY A O     1 
ATOM   2311 N  N     . PRO A 1 295 ? 51.295 31.155 5.892   1.00 9.38  ?  293 PRO A N     1 
ATOM   2312 C  CA    . PRO A 1 295 ? 50.898 30.814 4.532   1.00 9.35  ?  293 PRO A CA    1 
ATOM   2313 C  C     . PRO A 1 295 ? 50.982 29.302 4.325   1.00 8.03  ?  293 PRO A C     1 
ATOM   2314 O  O     . PRO A 1 295 ? 52.027 28.718 4.409   1.00 9.22  ?  293 PRO A O     1 
ATOM   2315 C  CB    . PRO A 1 295 ? 51.883 31.586 3.670   1.00 10.35 ?  293 PRO A CB    1 
ATOM   2316 C  CG    . PRO A 1 295 ? 52.995 31.817 4.520   1.00 11.83 ?  293 PRO A CG    1 
ATOM   2317 C  CD    . PRO A 1 295 ? 52.503 31.994 5.939   1.00 11.11 ?  293 PRO A CD    1 
ATOM   2318 N  N     . GLY A 1 296 ? 49.827 28.704 4.064   1.00 8.25  ?  294 GLY A N     1 
ATOM   2319 C  CA    . GLY A 1 296 ? 49.739 27.265 3.800   1.00 8.79  ?  294 GLY A CA    1 
ATOM   2320 C  C     . GLY A 1 296 ? 49.652 26.406 5.047   1.00 8.40  ?  294 GLY A C     1 
ATOM   2321 O  O     . GLY A 1 296 ? 49.738 25.158 4.869   1.00 8.75  ?  294 GLY A O     1 
ATOM   2322 N  N     . TYR A 1 297 ? 49.537 26.928 6.255   1.00 8.83  ?  295 TYR A N     1 
ATOM   2323 C  CA    . TYR A 1 297 ? 49.534 26.045 7.442   1.00 8.65  ?  295 TYR A CA    1 
ATOM   2324 C  C     . TYR A 1 297 ? 48.735 26.626 8.590   1.00 8.57  ?  295 TYR A C     1 
ATOM   2325 O  O     . TYR A 1 297 ? 48.554 27.846 8.701   1.00 9.12  ?  295 TYR A O     1 
ATOM   2326 C  CB    . TYR A 1 297 ? 50.944 25.703 7.901   1.00 8.33  ?  295 TYR A CB    1 
ATOM   2327 C  CG    . TYR A 1 297 ? 51.799 26.844 8.386   1.00 8.29  ?  295 TYR A CG    1 
ATOM   2328 C  CD1   . TYR A 1 297 ? 52.570 27.581 7.497   1.00 9.33  ?  295 TYR A CD1   1 
ATOM   2329 C  CD2   . TYR A 1 297 ? 51.915 27.137 9.724   1.00 8.63  ?  295 TYR A CD2   1 
ATOM   2330 C  CE1   . TYR A 1 297 ? 53.374 28.627 7.941   1.00 8.76  ?  295 TYR A CE1   1 
ATOM   2331 C  CE2   . TYR A 1 297 ? 52.691 28.170 10.178  1.00 9.47  ?  295 TYR A CE2   1 
ATOM   2332 C  CZ    . TYR A 1 297 ? 53.471 28.891 9.287   1.00 8.98  ?  295 TYR A CZ    1 
ATOM   2333 O  OH    . TYR A 1 297 ? 54.272 29.930 9.780   1.00 10.62 ?  295 TYR A OH    1 
ATOM   2334 N  N     . ALA A 1 298 ? 48.313 25.732 9.491   1.00 7.79  ?  296 ALA A N     1 
ATOM   2335 C  CA    . ALA A 1 298 ? 47.628 26.077 10.732  1.00 8.00  ?  296 ALA A CA    1 
ATOM   2336 C  C     . ALA A 1 298 ? 48.056 25.086 11.783  1.00 8.85  ?  296 ALA A C     1 
ATOM   2337 O  O     . ALA A 1 298 ? 48.504 23.978 11.447  1.00 9.14  ?  296 ALA A O     1 
ATOM   2338 C  CB    . ALA A 1 298 ? 46.138 26.022 10.538  1.00 9.50  ?  296 ALA A CB    1 
ATOM   2339 N  N     . LEU A 1 299 ? 47.903 25.458 13.046  1.00 7.86  ?  297 LEU A N     1 
ATOM   2340 C  CA    . LEU A 1 299 ? 48.209 24.597 14.222  1.00 7.94  ?  297 LEU A CA    1 
ATOM   2341 C  C     . LEU A 1 299 ? 46.918 24.462 15.009  1.00 7.06  ?  297 LEU A C     1 
ATOM   2342 O  O     . LEU A 1 299 ? 46.149 25.438 15.105  1.00 7.70  ?  297 LEU A O     1 
ATOM   2343 C  CB    . LEU A 1 299 ? 49.278 25.208 15.120  1.00 8.39  ?  297 LEU A CB    1 
ATOM   2344 C  CG    . LEU A 1 299 ? 50.718 25.177 14.648  1.00 8.27  ?  297 LEU A CG    1 
ATOM   2345 C  CD1   . LEU A 1 299 ? 50.953 26.111 13.443  1.00 9.81  ?  297 LEU A CD1   1 
ATOM   2346 C  CD2   . LEU A 1 299 ? 51.647 25.556 15.760  1.00 8.54  ?  297 LEU A CD2   1 
ATOM   2347 N  N     . VAL A 1 300 ? 46.662 23.310 15.601  1.00 7.53  ?  298 VAL A N     1 
ATOM   2348 C  CA    . VAL A 1 300 ? 45.451 23.075 16.393  1.00 7.65  ?  298 VAL A CA    1 
ATOM   2349 C  C     . VAL A 1 300 ? 45.761 22.097 17.535  1.00 7.56  ?  298 VAL A C     1 
ATOM   2350 O  O     . VAL A 1 300 ? 46.600 21.222 17.352  1.00 7.95  ?  298 VAL A O     1 
ATOM   2351 C  CB    . VAL A 1 300 ? 44.343 22.517 15.476  1.00 7.21  ?  298 VAL A CB    1 
ATOM   2352 C  CG1   . VAL A 1 300 ? 44.676 21.159 14.882  1.00 7.76  ?  298 VAL A CG1   1 
ATOM   2353 C  CG2   . VAL A 1 300 ? 42.987 22.512 16.146  1.00 7.08  ?  298 VAL A CG2   1 
ATOM   2354 N  N     . GLY A 1 301 ? 45.021 22.175 18.633  1.00 7.27  ?  299 GLY A N     1 
ATOM   2355 C  CA    . GLY A 1 301 ? 45.198 21.264 19.769  1.00 7.00  ?  299 GLY A CA    1 
ATOM   2356 C  C     . GLY A 1 301 ? 46.478 21.549 20.486  1.00 7.37  ?  299 GLY A C     1 
ATOM   2357 O  O     . GLY A 1 301 ? 46.961 22.703 20.530  1.00 7.14  ?  299 GLY A O     1 
ATOM   2358 N  N     . ASP A 1 302 ? 47.050 20.563 21.166  1.00 7.44  ?  300 ASP A N     1 
ATOM   2359 C  CA    . ASP A 1 302 ? 48.230 20.802 21.994  1.00 7.62  ?  300 ASP A CA    1 
ATOM   2360 C  C     . ASP A 1 302 ? 49.391 21.303 21.126  1.00 7.07  ?  300 ASP A C     1 
ATOM   2361 O  O     . ASP A 1 302 ? 50.294 21.923 21.635  1.00 8.74  ?  300 ASP A O     1 
ATOM   2362 C  CB    . ASP A 1 302 ? 48.686 19.569 22.804  1.00 8.09  ?  300 ASP A CB    1 
ATOM   2363 C  CG    . ASP A 1 302 ? 47.868 19.228 23.993  1.00 9.97  ?  300 ASP A CG    1 
ATOM   2364 O  OD1   . ASP A 1 302 ? 46.724 19.720 24.090  1.00 8.97  ?  300 ASP A OD1   1 
ATOM   2365 O  OD2   . ASP A 1 302 ? 48.355 18.462 24.852  1.00 15.64 ?  300 ASP A OD2   1 
ATOM   2366 N  N     . ALA A 1 303 ? 49.408 20.993 19.832  1.00 6.64  ?  301 ALA A N     1 
ATOM   2367 C  CA    . ALA A 1 303 ? 50.468 21.520 18.960  1.00 7.21  ?  301 ALA A CA    1 
ATOM   2368 C  C     . ALA A 1 303 ? 50.440 23.053 18.982  1.00 7.36  ?  301 ALA A C     1 
ATOM   2369 O  O     . ALA A 1 303 ? 51.491 23.668 18.801  1.00 7.64  ?  301 ALA A O     1 
ATOM   2370 C  CB    . ALA A 1 303 ? 50.316 21.024 17.536  1.00 7.24  ?  301 ALA A CB    1 
ATOM   2371 N  N     . ALA A 1 304 ? 49.284 23.660 19.146  1.00 6.92  ?  302 ALA A N     1 
ATOM   2372 C  CA    . ALA A 1 304 ? 49.151 25.133 19.295  1.00 7.13  ?  302 ALA A CA    1 
ATOM   2373 C  C     . ALA A 1 304 ? 49.378 25.558 20.721  1.00 7.52  ?  302 ALA A C     1 
ATOM   2374 O  O     . ALA A 1 304 ? 50.075 26.569 20.915  1.00 7.95  ?  302 ALA A O     1 
ATOM   2375 C  CB    . ALA A 1 304 ? 47.781 25.574 18.843  1.00 7.81  ?  302 ALA A CB    1 
ATOM   2376 N  N     . ALA A 1 305 ? 48.766 24.921 21.687  1.00 7.56  ?  303 ALA A N     1 
ATOM   2377 C  CA    . ALA A 1 305 ? 48.821 25.394 23.089  1.00 7.73  ?  303 ALA A CA    1 
ATOM   2378 C  C     . ALA A 1 305 ? 48.316 24.301 24.016  1.00 8.38  ?  303 ALA A C     1 
ATOM   2379 O  O     . ALA A 1 305 ? 47.396 23.542 23.658  1.00 7.81  ?  303 ALA A O     1 
ATOM   2380 C  CB    . ALA A 1 305 ? 47.928 26.609 23.250  1.00 8.98  ?  303 ALA A CB    1 
ATOM   2381 N  N     . PHE A 1 306 ? 48.810 24.326 25.243  1.00 8.08  ?  304 PHE A N     1 
ATOM   2382 C  CA    . PHE A 1 306 ? 48.256 23.519 26.321  1.00 7.68  ?  304 PHE A CA    1 
ATOM   2383 C  C     . PHE A 1 306 ? 48.424 24.236 27.637  1.00 8.69  ?  304 PHE A C     1 
ATOM   2384 O  O     . PHE A 1 306 ? 49.449 24.906 27.787  1.00 9.00  ?  304 PHE A O     1 
ATOM   2385 C  CB    . PHE A 1 306 ? 48.890 22.115 26.353  1.00 8.04  ?  304 PHE A CB    1 
ATOM   2386 C  CG    . PHE A 1 306 ? 48.300 21.222 27.417  1.00 7.65  ?  304 PHE A CG    1 
ATOM   2387 C  CD1   . PHE A 1 306 ? 46.992 20.763 27.303  1.00 8.70  ?  304 PHE A CD1   1 
ATOM   2388 C  CD2   . PHE A 1 306 ? 49.025 20.880 28.549  1.00 8.04  ?  304 PHE A CD2   1 
ATOM   2389 C  CE1   . PHE A 1 306 ? 46.411 19.966 28.281  1.00 8.49  ?  304 PHE A CE1   1 
ATOM   2390 C  CE2   . PHE A 1 306 ? 48.436 20.070 29.530  1.00 7.97  ?  304 PHE A CE2   1 
ATOM   2391 C  CZ    . PHE A 1 306 ? 47.139 19.639 29.393  1.00 8.41  ?  304 PHE A CZ    1 
ATOM   2392 N  N     . ILE A 1 307 ? 47.477 24.095 28.531  1.00 8.63  ?  305 ILE A N     1 
ATOM   2393 C  CA    . ILE A 1 307 ? 47.562 24.781 29.841  1.00 8.77  ?  305 ILE A CA    1 
ATOM   2394 C  C     . ILE A 1 307 ? 48.150 23.803 30.889  1.00 8.50  ?  305 ILE A C     1 
ATOM   2395 O  O     . ILE A 1 307 ? 49.314 23.877 31.227  1.00 8.93  ?  305 ILE A O     1 
ATOM   2396 C  CB    . ILE A 1 307 ? 46.189 25.384 30.234  1.00 10.43 ?  305 ILE A CB    1 
ATOM   2397 C  CG1   . ILE A 1 307 ? 45.691 26.372 29.160  1.00 12.39 ?  305 ILE A CG1   1 
ATOM   2398 C  CG2   . ILE A 1 307 ? 46.332 26.061 31.590  1.00 10.86 ?  305 ILE A CG2   1 
ATOM   2399 C  CD1   . ILE A 1 307 ? 44.201 26.716 29.326  1.00 13.70 ?  305 ILE A CD1   1 
ATOM   2400 N  N     . ASP A 1 308 ? 47.330 22.918 31.400  1.00 8.56  ?  306 ASP A N     1 
ATOM   2401 C  CA    . ASP A 1 308 ? 47.709 22.043 32.525  1.00 8.71  ?  306 ASP A CA    1 
ATOM   2402 C  C     . ASP A 1 308 ? 46.528 21.118 32.766  1.00 8.43  ?  306 ASP A C     1 
ATOM   2403 O  O     . ASP A 1 308 ? 45.406 21.498 32.472  1.00 10.35 ?  306 ASP A O     1 
ATOM   2404 C  CB    . ASP A 1 308 ? 47.905 22.915 33.791  1.00 8.84  ?  306 ASP A CB    1 
ATOM   2405 C  CG    . ASP A 1 308 ? 48.601 22.200 34.908  1.00 8.82  ?  306 ASP A CG    1 
ATOM   2406 O  OD1   . ASP A 1 308 ? 49.823 21.968 34.797  1.00 8.76  ?  306 ASP A OD1   1 
ATOM   2407 O  OD2   . ASP A 1 308 ? 47.933 21.864 35.908  1.00 10.06 ?  306 ASP A OD2   1 
ATOM   2408 N  N     . PRO A 1 309 ? 46.760 19.916 33.326  1.00 8.31  ?  307 PRO A N     1 
ATOM   2409 C  CA    . PRO A 1 309 ? 45.629 19.026 33.531  1.00 8.89  ?  307 PRO A CA    1 
ATOM   2410 C  C     . PRO A 1 309 ? 44.614 19.457 34.582  1.00 9.25  ?  307 PRO A C     1 
ATOM   2411 O  O     . PRO A 1 309 ? 43.532 18.868 34.657  1.00 9.46  ?  307 PRO A O     1 
ATOM   2412 C  CB    . PRO A 1 309 ? 46.282 17.705 33.901  1.00 9.52  ?  307 PRO A CB    1 
ATOM   2413 C  CG    . PRO A 1 309 ? 47.701 17.823 33.588  1.00 11.15 ?  307 PRO A CG    1 
ATOM   2414 C  CD    . PRO A 1 309 ? 48.056 19.271 33.540  1.00 8.17  ?  307 PRO A CD    1 
ATOM   2415 N  N     . LEU A 1 310 ? 44.905 20.476 35.392  1.00 9.30  ?  308 LEU A N     1 
ATOM   2416 C  CA    . LEU A 1 310 ? 43.991 20.879 36.465  1.00 9.47  ?  308 LEU A CA    1 
ATOM   2417 C  C     . LEU A 1 310 ? 42.737 21.386 35.785  1.00 11.38 ?  308 LEU A C     1 
ATOM   2418 O  O     . LEU A 1 310 ? 42.861 22.324 34.921  1.00 13.49 ?  308 LEU A O     1 
ATOM   2419 C  CB    . LEU A 1 310 ? 44.652 21.957 37.333  1.00 10.56 ?  308 LEU A CB    1 
ATOM   2420 C  CG    . LEU A 1 310 ? 43.809 22.433 38.505  1.00 11.04 ?  308 LEU A CG    1 
ATOM   2421 C  CD1   . LEU A 1 310 ? 43.469 21.279 39.464  1.00 12.30 ?  308 LEU A CD1   1 
ATOM   2422 C  CD2   . LEU A 1 310 ? 44.608 23.486 39.270  1.00 12.81 ?  308 LEU A CD2   1 
ATOM   2423 N  N     . LEU A 1 311 ? 41.631 20.832 36.093  1.00 11.92 ?  309 LEU A N     1 
ATOM   2424 C  CA    . LEU A 1 311 ? 40.312 21.178 35.480  1.00 12.25 ?  309 LEU A CA    1 
ATOM   2425 C  C     . LEU A 1 311 ? 40.064 20.581 34.086  1.00 10.66 ?  309 LEU A C     1 
ATOM   2426 O  O     . LEU A 1 311 ? 39.000 20.788 33.483  1.00 9.97  ?  309 LEU A O     1 
ATOM   2427 C  CB    . LEU A 1 311 ? 39.994 22.682 35.469  1.00 14.45 ?  309 LEU A CB    1 
ATOM   2428 C  CG    . LEU A 1 311 ? 40.181 23.376 36.817  1.00 15.62 ?  309 LEU A CG    1 
ATOM   2429 C  CD1   . LEU A 1 311 ? 39.921 24.854 36.692  1.00 16.76 ?  309 LEU A CD1   1 
ATOM   2430 C  CD2   . LEU A 1 311 ? 39.307 22.775 37.840  1.00 17.12 ?  309 LEU A CD2   1 
ATOM   2431 N  N     . SER A 1 312 ? 40.907 19.636 33.652  1.00 9.67  ?  310 SER A N     1 
ATOM   2432 C  CA    . SER A 1 312 ? 40.604 18.679 32.557  1.00 9.39  ?  310 SER A CA    1 
ATOM   2433 C  C     . SER A 1 312 ? 39.973 19.326 31.311  1.00 8.65  ?  310 SER A C     1 
ATOM   2434 O  O     . SER A 1 312 ? 38.850 18.995 30.924  1.00 10.45 ?  310 SER A O     1 
ATOM   2435 C  CB    . SER A 1 312 ? 39.838 17.474 33.079  1.00 13.36 ?  310 SER A CB    1 
ATOM   2436 O  OG    . SER A 1 312 ? 38.558 17.827 33.499  1.00 15.45 ?  310 SER A OG    1 
ATOM   2437 N  N     . THR A 1 313 ? 40.715 20.210 30.668  1.00 8.89  ?  311 THR A N     1 
ATOM   2438 C  CA    . THR A 1 313 ? 40.259 20.960 29.470  1.00 9.58  ?  311 THR A CA    1 
ATOM   2439 C  C     . THR A 1 313 ? 40.900 20.569 28.150  1.00 8.61  ?  311 THR A C     1 
ATOM   2440 O  O     . THR A 1 313 ? 40.411 21.010 27.097  1.00 9.41  ?  311 THR A O     1 
ATOM   2441 C  CB    . THR A 1 313 ? 40.499 22.468 29.679  1.00 10.49 ?  311 THR A CB    1 
ATOM   2442 O  OG1   . THR A 1 313 ? 41.874 22.752 29.868  1.00 11.32 ?  311 THR A OG1   1 
ATOM   2443 C  CG2   . THR A 1 313 ? 39.684 22.973 30.865  1.00 11.60 ?  311 THR A CG2   1 
ATOM   2444 N  N     . GLY A 1 314 ? 41.972 19.786 28.132  1.00 7.77  ?  312 GLY A N     1 
ATOM   2445 C  CA    . GLY A 1 314 ? 42.774 19.654 26.919  1.00 8.25  ?  312 GLY A CA    1 
ATOM   2446 C  C     . GLY A 1 314 ? 42.063 19.074 25.736  1.00 7.73  ?  312 GLY A C     1 
ATOM   2447 O  O     . GLY A 1 314 ? 42.209 19.541 24.584  1.00 8.03  ?  312 GLY A O     1 
ATOM   2448 N  N     . VAL A 1 315 ? 41.308 17.990 25.928  1.00 7.29  ?  313 VAL A N     1 
ATOM   2449 C  CA    . VAL A 1 315 ? 40.634 17.345 24.782  1.00 8.11  ?  313 VAL A CA    1 
ATOM   2450 C  C     . VAL A 1 315 ? 39.523 18.271 24.296  1.00 8.04  ?  313 VAL A C     1 
ATOM   2451 O  O     . VAL A 1 315 ? 39.297 18.355 23.071  1.00 8.63  ?  313 VAL A O     1 
ATOM   2452 C  CB    . VAL A 1 315 ? 40.071 15.973 25.141  1.00 8.70  ?  313 VAL A CB    1 
ATOM   2453 C  CG1   . VAL A 1 315 ? 39.200 15.427 24.047  1.00 8.71  ?  313 VAL A CG1   1 
ATOM   2454 C  CG2   . VAL A 1 315 ? 41.182 14.997 25.497  1.00 9.43  ?  313 VAL A CG2   1 
ATOM   2455 N  N     . THR A 1 316 ? 38.940 19.095 25.162  1.00 8.94  ?  314 THR A N     1 
ATOM   2456 C  CA    . THR A 1 316 ? 37.909 20.065 24.745  1.00 9.02  ?  314 THR A CA    1 
ATOM   2457 C  C     . THR A 1 316 ? 38.553 21.228 23.962  1.00 9.07  ?  314 THR A C     1 
ATOM   2458 O  O     . THR A 1 316 ? 38.055 21.587 22.903  1.00 9.44  ?  314 THR A O     1 
ATOM   2459 C  CB    . THR A 1 316 ? 37.153 20.543 25.970  1.00 9.67  ?  314 THR A CB    1 
ATOM   2460 O  OG1   . THR A 1 316 ? 36.530 19.394 26.557  1.00 11.64 ?  314 THR A OG1   1 
ATOM   2461 C  CG2   . THR A 1 316 ? 36.142 21.596 25.533  1.00 11.34 ?  314 THR A CG2   1 
ATOM   2462 N  N     . LEU A 1 317 ? 39.709 21.708 24.396  1.00 8.65  ?  315 LEU A N     1 
ATOM   2463 C  CA    . LEU A 1 317 ? 40.496 22.686 23.626  1.00 8.78  ?  315 LEU A CA    1 
ATOM   2464 C  C     . LEU A 1 317 ? 40.787 22.099 22.268  1.00 8.53  ?  315 LEU A C     1 
ATOM   2465 O  O     . LEU A 1 317 ? 40.657 22.739 21.222  1.00 9.47  ?  315 LEU A O     1 
ATOM   2466 C  CB    . LEU A 1 317 ? 41.816 22.992 24.334  1.00 9.91  ?  315 LEU A CB    1 
ATOM   2467 C  CG    . LEU A 1 317 ? 41.690 24.000 25.456  1.00 11.48 ?  315 LEU A CG    1 
ATOM   2468 C  CD1   . LEU A 1 317 ? 42.874 23.884 26.371  1.00 11.80 ?  315 LEU A CD1   1 
ATOM   2469 C  CD2   . LEU A 1 317 ? 41.565 25.410 24.843  1.00 12.22 ?  315 LEU A CD2   1 
ATOM   2470 N  N     . ALA A 1 318 ? 41.182 20.814 22.210  1.00 7.65  ?  316 ALA A N     1 
ATOM   2471 C  CA    . ALA A 1 318 ? 41.566 20.165 20.955  1.00 8.23  ?  316 ALA A CA    1 
ATOM   2472 C  C     . ALA A 1 318 ? 40.387 20.047 20.019  1.00 8.01  ?  316 ALA A C     1 
ATOM   2473 O  O     . ALA A 1 318 ? 40.514 20.254 18.789  1.00 7.91  ?  316 ALA A O     1 
ATOM   2474 C  CB    . ALA A 1 318 ? 42.134 18.768 21.246  1.00 8.86  ?  316 ALA A CB    1 
ATOM   2475 N  N     . MET A 1 319 ? 39.233 19.622 20.493  1.00 8.48  ?  317 MET A N     1 
ATOM   2476 C  CA    . MET A 1 319 ? 38.055 19.401 19.633  1.00 8.51  ?  317 MET A CA    1 
ATOM   2477 C  C     . MET A 1 319 ? 37.358 20.709 19.292  1.00 8.45  ?  317 MET A C     1 
ATOM   2478 O  O     . MET A 1 319 ? 36.935 20.842 18.147  1.00 9.31  ?  317 MET A O     1 
ATOM   2479 C  CB    . MET A 1 319 ? 37.098 18.424 20.295  1.00 9.67  ?  317 MET A CB    1 
ATOM   2480 C  CG    . MET A 1 319 ? 37.752 17.069 20.468  1.00 9.07  ?  317 MET A CG    1 
ATOM   2481 S  SD    . MET A 1 319 ? 36.644 15.768 21.094  1.00 12.28 ?  317 MET A SD    1 
ATOM   2482 C  CE    . MET A 1 319 ? 35.521 15.577 19.725  1.00 13.17 ?  317 MET A CE    1 
ATOM   2483 N  N     . ARG A 1 320 ? 37.346 21.662 20.192  1.00 8.48  ?  318 ARG A N     1 
ATOM   2484 C  CA    . ARG A 1 320 ? 36.903 23.011 19.828  1.00 9.23  ?  318 ARG A CA    1 
ATOM   2485 C  C     . ARG A 1 320 ? 37.867 23.530 18.722  1.00 9.57  ?  318 ARG A C     1 
ATOM   2486 O  O     . ARG A 1 320 ? 37.438 24.188 17.748  1.00 10.35 ?  318 ARG A O     1 
ATOM   2487 C  CB    . ARG A 1 320 ? 36.984 23.957 21.021  1.00 10.30 ?  318 ARG A CB    1 
ATOM   2488 C  CG    . ARG A 1 320 ? 36.661 25.415 20.659  1.00 11.37 ?  318 ARG A CG    1 
ATOM   2489 C  CD    . ARG A 1 320 ? 37.056 26.411 21.713  1.00 11.41 ?  318 ARG A CD    1 
ATOM   2490 N  NE    . ARG A 1 320 ? 36.859 27.759 21.194  1.00 14.32 ?  318 ARG A NE    1 
ATOM   2491 C  CZ    . ARG A 1 320 ? 37.634 28.327 20.285  1.00 15.43 ?  318 ARG A CZ    1 
ATOM   2492 N  NH1   . ARG A 1 320 ? 38.668 27.665 19.785  1.00 14.20 ?  318 ARG A NH1   1 
ATOM   2493 N  NH2   . ARG A 1 320 ? 37.379 29.560 19.870  1.00 18.15 ?  318 ARG A NH2   1 
ATOM   2494 N  N     . GLY A 1 321 ? 39.174 23.283 18.901  1.00 8.55  ?  319 GLY A N     1 
ATOM   2495 C  CA    . GLY A 1 321 ? 40.161 23.658 17.888  1.00 8.65  ?  319 GLY A CA    1 
ATOM   2496 C  C     . GLY A 1 321 ? 39.858 22.978 16.578  1.00 9.01  ?  319 GLY A C     1 
ATOM   2497 O  O     . GLY A 1 321 ? 39.875 23.620 15.523  1.00 9.08  ?  319 GLY A O     1 
ATOM   2498 N  N     . GLY A 1 322 ? 39.560 21.684 16.582  1.00 8.78  ?  320 GLY A N     1 
ATOM   2499 C  CA    . GLY A 1 322 ? 39.276 21.042 15.323  1.00 9.18  ?  320 GLY A CA    1 
ATOM   2500 C  C     . GLY A 1 322 ? 38.046 21.591 14.600  1.00 8.61  ?  320 GLY A C     1 
ATOM   2501 O  O     . GLY A 1 322 ? 38.033 21.737 13.450  1.00 9.50  ?  320 GLY A O     1 
ATOM   2502 N  N     . SER A 1 323 ? 37.065 21.925 15.393  1.00 8.78  ?  321 SER A N     1 
ATOM   2503 C  CA    . SER A 1 323 ? 35.859 22.499 14.867  1.00 10.05 ?  321 SER A CA    1 
ATOM   2504 C  C     . SER A 1 323 ? 36.119 23.881 14.256  1.00 9.61  ?  321 SER A C     1 
ATOM   2505 O  O     . SER A 1 323 ? 35.716 24.125 13.147  1.00 10.98 ?  321 SER A O     1 
ATOM   2506 C  CB    . SER A 1 323 ? 34.829 22.605 15.974  1.00 12.60 ?  321 SER A CB    1 
ATOM   2507 O  OG    . SER A 1 323 ? 33.627 23.065 15.496  1.00 19.54 ?  321 SER A OG    1 
ATOM   2508 N  N     . THR A 1 324 ? 36.846 24.710 14.985  1.00 9.11  ?  322 THR A N     1 
ATOM   2509 C  CA    . THR A 1 324 ? 37.072 26.073 14.500  1.00 10.05 ?  322 THR A CA    1 
ATOM   2510 C  C     . THR A 1 324 ? 38.095 26.058 13.381  1.00 10.06 ?  322 THR A C     1 
ATOM   2511 O  O     . THR A 1 324 ? 37.962 26.871 12.437  1.00 11.01 ?  322 THR A O     1 
ATOM   2512 C  CB    . THR A 1 324 ? 37.400 27.031 15.622  1.00 10.44 ?  322 THR A CB    1 
ATOM   2513 O  OG1   . THR A 1 324 ? 38.609 26.570 16.254  1.00 10.75 ?  322 THR A OG1   1 
ATOM   2514 C  CG2   . THR A 1 324 ? 36.269 27.195 16.608  1.00 10.43 ?  322 THR A CG2   1 
ATOM   2515 N  N     . VAL A 1 325 ? 39.129 25.236 13.422  1.00 9.33  ?  323 VAL A N     1 
ATOM   2516 C  CA    . VAL A 1 325 ? 40.126 25.268 12.324  1.00 9.24  ?  323 VAL A CA    1 
ATOM   2517 C  C     . VAL A 1 325 ? 39.475 24.703 11.089  1.00 10.04 ?  323 VAL A C     1 
ATOM   2518 O  O     . VAL A 1 325 ? 39.852 25.093 9.986   1.00 9.58  ?  323 VAL A O     1 
ATOM   2519 C  CB    . VAL A 1 325 ? 41.407 24.519 12.723  1.00 9.52  ?  323 VAL A CB    1 
ATOM   2520 C  CG1   . VAL A 1 325 ? 41.339 22.992 12.558  1.00 9.66  ?  323 VAL A CG1   1 
ATOM   2521 C  CG2   . VAL A 1 325 ? 42.598 25.092 11.954  1.00 9.94  ?  323 VAL A CG2   1 
ATOM   2522 N  N     . SER A 1 326 ? 38.595 23.715 11.220  1.00 9.97  ?  324 SER A N     1 
ATOM   2523 C  CA    . SER A 1 326 ? 37.955 23.142 10.006  1.00 10.37 ?  324 SER A CA    1 
ATOM   2524 C  C     . SER A 1 326 ? 37.103 24.235 9.347   1.00 10.32 ?  324 SER A C     1 
ATOM   2525 O  O     . SER A 1 326 ? 37.148 24.335 8.092   1.00 10.83 ?  324 SER A O     1 
ATOM   2526 C  CB    . SER A 1 326 ? 37.136 21.906 10.338  1.00 10.99 ?  324 SER A CB    1 
ATOM   2527 O  OG    . SER A 1 326 ? 36.052 22.166 11.172  1.00 15.26 ?  324 SER A OG    1 
ATOM   2528 N  N     . ARG A 1 327 ? 36.410 25.046 10.127  1.00 11.33 ?  325 ARG A N     1 
ATOM   2529 C  CA    . ARG A 1 327 ? 35.586 26.134 9.519   1.00 12.97 ?  325 ARG A CA    1 
ATOM   2530 C  C     . ARG A 1 327 ? 36.520 27.136 8.848   1.00 12.12 ?  325 ARG A C     1 
ATOM   2531 O  O     . ARG A 1 327 ? 36.286 27.551 7.655   1.00 12.74 ?  325 ARG A O     1 
ATOM   2532 C  CB    . ARG A 1 327 ? 34.778 26.787 10.622  1.00 17.11 ?  325 ARG A CB    1 
ATOM   2533 C  CG    . ARG A 1 327 ? 33.910 27.924 10.091  1.00 25.02 ?  325 ARG A CG    1 
ATOM   2534 C  CD    . ARG A 1 327 ? 32.927 28.402 11.158  1.00 36.17 ?  325 ARG A CD    1 
ATOM   2535 N  NE    . ARG A 1 327 ? 33.326 29.665 11.782  1.00 50.33 ?  325 ARG A NE    1 
ATOM   2536 C  CZ    . ARG A 1 327 ? 32.987 30.890 11.347  1.00 58.62 ?  325 ARG A CZ    1 
ATOM   2537 N  NH1   . ARG A 1 327 ? 32.228 31.043 10.273  1.00 61.83 ?  325 ARG A NH1   1 
ATOM   2538 N  NH2   . ARG A 1 327 ? 33.414 31.964 11.995  1.00 58.28 ?  325 ARG A NH2   1 
ATOM   2539 N  N     . ALA A 1 328 ? 37.616 27.505 9.505   1.00 10.72 ?  326 ALA A N     1 
ATOM   2540 C  CA    . ALA A 1 328 ? 38.551 28.500 8.975   1.00 10.60 ?  326 ALA A CA    1 
ATOM   2541 C  C     . ALA A 1 328 ? 39.223 27.982 7.714   1.00 11.21 ?  326 ALA A C     1 
ATOM   2542 O  O     . ALA A 1 328 ? 39.355 28.680 6.696   1.00 10.75 ?  326 ALA A O     1 
ATOM   2543 C  CB    . ALA A 1 328 ? 39.605 28.880 9.971   1.00 10.84 ?  326 ALA A CB    1 
ATOM   2544 N  N     . VAL A 1 329 ? 39.697 26.751 7.757   1.00 9.94  ?  327 VAL A N     1 
ATOM   2545 C  CA    . VAL A 1 329 ? 40.358 26.180 6.591   1.00 10.55 ?  327 VAL A CA    1 
ATOM   2546 C  C     . VAL A 1 329 ? 39.398 26.034 5.398   1.00 10.32 ?  327 VAL A C     1 
ATOM   2547 O  O     . VAL A 1 329 ? 39.757 26.228 4.309   1.00 10.87 ?  327 VAL A O     1 
ATOM   2548 C  CB    . VAL A 1 329 ? 41.093 24.872 6.963   1.00 10.37 ?  327 VAL A CB    1 
ATOM   2549 C  CG1   . VAL A 1 329 ? 41.567 24.125 5.741   1.00 10.86 ?  327 VAL A CG1   1 
ATOM   2550 C  CG2   . VAL A 1 329 ? 42.289 25.180 7.840   1.00 10.09 ?  327 VAL A CG2   1 
ATOM   2551 N  N     . HIS A 1 330 ? 38.176 25.656 5.671   1.00 10.24 ?  328 HIS A N     1 
ATOM   2552 C  CA    . HIS A 1 330 ? 37.197 25.582 4.600   1.00 11.90 ?  328 HIS A CA    1 
ATOM   2553 C  C     . HIS A 1 330 ? 37.034 26.978 3.956   1.00 11.73 ?  328 HIS A C     1 
ATOM   2554 O  O     . HIS A 1 330 ? 37.044 27.076 2.789   1.00 11.37 ?  328 HIS A O     1 
ATOM   2555 C  CB    . HIS A 1 330 ? 35.865 25.116 5.170   1.00 12.16 ?  328 HIS A CB    1 
ATOM   2556 C  CG    . HIS A 1 330 ? 34.729 25.274 4.225   1.00 13.73 ?  328 HIS A CG    1 
ATOM   2557 N  ND1   . HIS A 1 330 ? 34.617 24.525 3.083   1.00 16.85 ?  328 HIS A ND1   1 
ATOM   2558 C  CD2   . HIS A 1 330 ? 33.664 26.103 4.250   1.00 17.11 ?  328 HIS A CD2   1 
ATOM   2559 C  CE1   . HIS A 1 330 ? 33.532 24.908 2.431   1.00 17.56 ?  328 HIS A CE1   1 
ATOM   2560 N  NE2   . HIS A 1 330 ? 32.924 25.836 3.134   1.00 18.38 ?  328 HIS A NE2   1 
ATOM   2561 N  N     . GLU A 1 331 ? 36.881 27.999 4.781   1.00 12.70 ?  329 GLU A N     1 
ATOM   2562 C  CA    . GLU A 1 331 ? 36.681 29.361 4.228   1.00 12.46 ?  329 GLU A CA    1 
ATOM   2563 C  C     . GLU A 1 331 ? 37.912 29.759 3.457   1.00 13.02 ?  329 GLU A C     1 
ATOM   2564 O  O     . GLU A 1 331 ? 37.812 30.370 2.318   1.00 14.14 ?  329 GLU A O     1 
ATOM   2565 C  CB    . GLU A 1 331 ? 36.422 30.316 5.360   1.00 13.94 ?  329 GLU A CB    1 
ATOM   2566 C  CG    . GLU A 1 331 ? 35.074 30.131 5.995   1.00 19.09 ?  329 GLU A CG    1 
ATOM   2567 C  CD    . GLU A 1 331 ? 34.829 31.053 7.184   1.00 28.22 ?  329 GLU A CD    1 
ATOM   2568 O  OE1   . GLU A 1 331 ? 35.715 31.931 7.441   1.00 34.48 ?  329 GLU A OE1   1 
ATOM   2569 O  OE2   . GLU A 1 331 ? 33.785 30.871 7.861   1.00 38.40 ?  329 GLU A OE2   1 
ATOM   2570 N  N     . ALA A 1 332 ? 39.101 29.424 3.896   1.00 10.59 ?  330 ALA A N     1 
ATOM   2571 C  CA    . ALA A 1 332 ? 40.353 29.725 3.190   1.00 11.90 ?  330 ALA A CA    1 
ATOM   2572 C  C     . ALA A 1 332 ? 40.462 28.985 1.865   1.00 12.96 ?  330 ALA A C     1 
ATOM   2573 O  O     . ALA A 1 332 ? 41.101 29.483 0.930   1.00 14.84 ?  330 ALA A O     1 
ATOM   2574 C  CB    . ALA A 1 332 ? 41.545 29.365 4.074   1.00 11.84 ?  330 ALA A CB    1 
ATOM   2575 N  N     . LEU A 1 333 ? 39.983 27.733 1.778   1.00 12.11 ?  331 LEU A N     1 
ATOM   2576 C  CA    . LEU A 1 333 ? 40.024 26.963 0.519   1.00 12.62 ?  331 LEU A CA    1 
ATOM   2577 C  C     . LEU A 1 333 ? 39.021 27.555 -0.481  1.00 13.06 ?  331 LEU A C     1 
ATOM   2578 O  O     . LEU A 1 333 ? 39.410 27.571 -1.685  1.00 15.43 ?  331 LEU A O     1 
ATOM   2579 C  CB    . LEU A 1 333 ? 39.748 25.488 0.816   1.00 12.77 ?  331 LEU A CB    1 
ATOM   2580 C  CG    . LEU A 1 333 ? 40.828 24.778 1.646   1.00 13.86 ?  331 LEU A CG    1 
ATOM   2581 C  CD1   . LEU A 1 333 ? 40.312 23.430 2.070   1.00 14.40 ?  331 LEU A CD1   1 
ATOM   2582 C  CD2   . LEU A 1 333 ? 42.088 24.652 0.805   1.00 16.68 ?  331 LEU A CD2   1 
ATOM   2583 N  N     . VAL A 1 334 ? 37.848 27.964 -0.023  1.00 14.07 ?  332 VAL A N     1 
ATOM   2584 C  CA    . VAL A 1 334 ? 36.800 28.527 -0.920  1.00 15.31 ?  332 VAL A CA    1 
ATOM   2585 C  C     . VAL A 1 334 ? 37.274 29.911 -1.383  1.00 17.34 ?  332 VAL A C     1 
ATOM   2586 O  O     . VAL A 1 334 ? 36.936 30.267 -2.536  1.00 17.35 ?  332 VAL A O     1 
ATOM   2587 C  CB    . VAL A 1 334 ? 35.463 28.552 -0.167  1.00 17.50 ?  332 VAL A CB    1 
ATOM   2588 C  CG1   . VAL A 1 334 ? 34.432 29.427 -0.892  1.00 20.45 ?  332 VAL A CG1   1 
ATOM   2589 C  CG2   . VAL A 1 334 ? 34.950 27.111 0.010   1.00 21.08 ?  332 VAL A CG2   1 
ATOM   2590 N  N     . ASP A 1 335 ? 37.944 30.721 -0.564  1.00 15.33 ?  333 ASP A N     1 
ATOM   2591 C  CA    . ASP A 1 335 ? 38.319 32.125 -0.903  1.00 15.59 ?  333 ASP A CA    1 
ATOM   2592 C  C     . ASP A 1 335 ? 39.772 32.280 -0.491  1.00 13.61 ?  333 ASP A C     1 
ATOM   2593 O  O     . ASP A 1 335 ? 40.079 32.859 0.544   1.00 14.98 ?  333 ASP A O     1 
ATOM   2594 C  CB    . ASP A 1 335 ? 37.413 33.117 -0.177  1.00 19.47 ?  333 ASP A CB    1 
ATOM   2595 C  CG    . ASP A 1 335 ? 37.621 34.575 -0.602  1.00 26.17 ?  333 ASP A CG    1 
ATOM   2596 O  OD1   . ASP A 1 335 ? 38.388 34.801 -1.592  1.00 31.01 ?  333 ASP A OD1   1 
ATOM   2597 O  OD2   . ASP A 1 335 ? 37.058 35.451 0.109   1.00 37.81 ?  333 ASP A OD2   1 
ATOM   2598 N  N     . PRO A 1 336 ? 40.693 31.749 -1.295  1.00 13.81 ?  334 PRO A N     1 
ATOM   2599 C  CA    . PRO A 1 336 ? 42.118 31.816 -0.980  1.00 13.33 ?  334 PRO A CA    1 
ATOM   2600 C  C     . PRO A 1 336 ? 42.663 33.224 -0.747  1.00 13.52 ?  334 PRO A C     1 
ATOM   2601 O  O     . PRO A 1 336 ? 43.613 33.406 -0.008  1.00 13.58 ?  334 PRO A O     1 
ATOM   2602 C  CB    . PRO A 1 336 ? 42.849 31.127 -2.117  1.00 17.89 ?  334 PRO A CB    1 
ATOM   2603 C  CG    . PRO A 1 336 ? 41.809 30.205 -2.665  1.00 19.74 ?  334 PRO A CG    1 
ATOM   2604 C  CD    . PRO A 1 336 ? 40.490 30.956 -2.537  1.00 14.57 ?  334 PRO A CD    1 
ATOM   2605 N  N     . ALA A 1 337 ? 42.010 34.247 -1.304  1.00 12.92 ?  335 ALA A N     1 
ATOM   2606 C  CA    . ALA A 1 337 ? 42.470 35.627 -1.098  1.00 12.79 ?  335 ALA A CA    1 
ATOM   2607 C  C     . ALA A 1 337 ? 42.307 36.017 0.361   1.00 13.10 ?  335 ALA A C     1 
ATOM   2608 O  O     . ALA A 1 337 ? 42.983 36.966 0.769   1.00 14.85 ?  335 ALA A O     1 
ATOM   2609 C  CB    . ALA A 1 337 ? 41.688 36.579 -1.986  1.00 14.15 ?  335 ALA A CB    1 
ATOM   2610 N  N     . LYS A 1 338 ? 41.447 35.343 1.092   1.00 12.50 ?  336 LYS A N     1 
ATOM   2611 C  CA    . LYS A 1 338 ? 41.204 35.653 2.503   1.00 14.97 ?  336 LYS A CA    1 
ATOM   2612 C  C     . LYS A 1 338 ? 41.830 34.618 3.403   1.00 13.21 ?  336 LYS A C     1 
ATOM   2613 O  O     . LYS A 1 338 ? 41.505 34.659 4.602   1.00 13.57 ?  336 LYS A O     1 
ATOM   2614 C  CB    . LYS A 1 338 ? 39.698 35.740 2.745   1.00 19.94 ?  336 LYS A CB    1 
ATOM   2615 C  CG    . LYS A 1 338 ? 39.122 36.974 2.073   1.00 27.14 ?  336 LYS A CG    1 
ATOM   2616 C  CD    . LYS A 1 338 ? 37.710 37.281 2.539   1.00 38.06 ?  336 LYS A CD    1 
ATOM   2617 C  CE    . LYS A 1 338 ? 37.063 38.400 1.748   1.00 42.93 ?  336 LYS A CE    1 
ATOM   2618 N  NZ    . LYS A 1 338 ? 37.554 39.719 2.201   1.00 48.64 ?  336 LYS A NZ    1 
ATOM   2619 N  N     . GLU A 1 339 ? 42.697 33.758 2.921   1.00 10.93 ?  337 GLU A N     1 
ATOM   2620 C  CA    . GLU A 1 339 ? 43.280 32.719 3.783   1.00 11.46 ?  337 GLU A CA    1 
ATOM   2621 C  C     . GLU A 1 339 ? 43.875 33.340 5.038   1.00 10.46 ?  337 GLU A C     1 
ATOM   2622 O  O     . GLU A 1 339 ? 43.598 32.861 6.176   1.00 11.10 ?  337 GLU A O     1 
ATOM   2623 C  CB    . GLU A 1 339 ? 44.340 31.957 3.024   1.00 11.51 ?  337 GLU A CB    1 
ATOM   2624 C  CG    . GLU A 1 339 ? 45.103 30.976 3.935   1.00 12.60 ?  337 GLU A CG    1 
ATOM   2625 C  CD    . GLU A 1 339 ? 46.183 30.235 3.196   1.00 18.56 ?  337 GLU A CD    1 
ATOM   2626 O  OE1   . GLU A 1 339 ? 45.881 29.655 2.094   1.00 16.48 ?  337 GLU A OE1   1 
ATOM   2627 O  OE2   . GLU A 1 339 ? 47.288 30.128 3.724   1.00 20.64 ?  337 GLU A OE2   1 
ATOM   2628 N  N     . ARG A 1 340 ? 44.751 34.341 4.892   1.00 10.07 ?  338 ARG A N     1 
ATOM   2629 C  CA    . ARG A 1 340 ? 45.446 34.856 6.098   1.00 10.04 ?  338 ARG A CA    1 
ATOM   2630 C  C     . ARG A 1 340 ? 44.442 35.465 7.047   1.00 10.01 ?  338 ARG A C     1 
ATOM   2631 O  O     . ARG A 1 340 ? 44.495 35.194 8.254   1.00 10.03 ?  338 ARG A O     1 
ATOM   2632 C  CB    . ARG A 1 340 ? 46.536 35.828 5.724   1.00 9.61  ?  338 ARG A CB    1 
ATOM   2633 C  CG    . ARG A 1 340 ? 47.330 36.260 6.940   1.00 10.81 ?  338 ARG A CG    1 
ATOM   2634 C  CD    . ARG A 1 340 ? 48.546 37.031 6.557   1.00 10.91 ?  338 ARG A CD    1 
ATOM   2635 N  NE    . ARG A 1 340 ? 49.330 37.407 7.680   1.00 11.35 ?  338 ARG A NE    1 
ATOM   2636 C  CZ    . ARG A 1 340 ? 50.328 36.688 8.217   1.00 10.51 ?  338 ARG A CZ    1 
ATOM   2637 N  NH1   . ARG A 1 340 ? 50.617 35.459 7.801   1.00 10.74 ?  338 ARG A NH1   1 
ATOM   2638 N  NH2   . ARG A 1 340 ? 51.021 37.204 9.212   1.00 10.72 ?  338 ARG A NH2   1 
ATOM   2639 N  N     . ASP A 1 341 ? 43.510 36.234 6.573   1.00 10.81 ?  339 ASP A N     1 
ATOM   2640 C  CA    . ASP A 1 341 ? 42.556 36.894 7.486   1.00 11.63 ?  339 ASP A CA    1 
ATOM   2641 C  C     . ASP A 1 341 ? 41.744 35.859 8.250   1.00 9.90  ?  339 ASP A C     1 
ATOM   2642 O  O     . ASP A 1 341 ? 41.546 35.987 9.462   1.00 10.13 ?  339 ASP A O     1 
ATOM   2643 C  CB    . ASP A 1 341 ? 41.622 37.824 6.723   1.00 14.36 ?  339 ASP A CB    1 
ATOM   2644 C  CG    . ASP A 1 341 ? 40.772 38.633 7.671   1.00 21.97 ?  339 ASP A CG    1 
ATOM   2645 O  OD1   . ASP A 1 341 ? 41.352 39.438 8.531   1.00 25.33 ?  339 ASP A OD1   1 
ATOM   2646 O  OD2   . ASP A 1 341 ? 39.532 38.411 7.646   1.00 28.28 ?  339 ASP A OD2   1 
ATOM   2647 N  N     . THR A 1 342 ? 41.299 34.822 7.562   1.00 9.87  ?  340 THR A N     1 
ATOM   2648 C  CA    . THR A 1 342 ? 40.453 33.799 8.192   1.00 10.54 ?  340 THR A CA    1 
ATOM   2649 C  C     . THR A 1 342 ? 41.273 33.048 9.246   1.00 9.59  ?  340 THR A C     1 
ATOM   2650 O  O     . THR A 1 342 ? 40.734 32.764 10.341  1.00 10.32 ?  340 THR A O     1 
ATOM   2651 C  CB    . THR A 1 342 ? 39.851 32.902 7.135   1.00 12.68 ?  340 THR A CB    1 
ATOM   2652 O  OG1   . THR A 1 342 ? 39.251 33.700 6.073   1.00 17.20 ?  340 THR A OG1   1 
ATOM   2653 C  CG2   . THR A 1 342 ? 38.901 31.997 7.862   1.00 14.40 ?  340 THR A CG2   1 
ATOM   2654 N  N     . LEU A 1 343 ? 42.513 32.748 8.968   1.00 9.11  ?  341 LEU A N     1 
ATOM   2655 C  CA    . LEU A 1 343 ? 43.333 32.034 9.929   1.00 10.05 ?  341 LEU A CA    1 
ATOM   2656 C  C     . LEU A 1 343 ? 43.769 32.923 11.073  1.00 8.77  ?  341 LEU A C     1 
ATOM   2657 O  O     . LEU A 1 343 ? 43.915 32.465 12.240  1.00 9.49  ?  341 LEU A O     1 
ATOM   2658 C  CB    . LEU A 1 343 ? 44.509 31.359 9.259   1.00 10.51 ?  341 LEU A CB    1 
ATOM   2659 C  CG    . LEU A 1 343 ? 44.152 30.132 8.414   1.00 13.56 ?  341 LEU A CG    1 
ATOM   2660 C  CD1   . LEU A 1 343 ? 45.322 29.759 7.566   1.00 14.63 ?  341 LEU A CD1   1 
ATOM   2661 C  CD2   . LEU A 1 343 ? 43.662 29.011 9.300   1.00 17.37 ?  341 LEU A CD2   1 
ATOM   2662 N  N     . GLN A 1 344 ? 43.907 34.232 10.866  1.00 9.15  ?  342 GLN A N     1 
ATOM   2663 C  CA    . GLN A 1 344 ? 44.202 35.136 12.009  1.00 8.83  ?  342 GLN A CA    1 
ATOM   2664 C  C     . GLN A 1 344 ? 42.966 35.227 12.901  1.00 8.92  ?  342 GLN A C     1 
ATOM   2665 O  O     . GLN A 1 344 ? 43.143 35.229 14.156  1.00 10.09 ?  342 GLN A O     1 
ATOM   2666 C  CB    . GLN A 1 344 ? 44.544 36.545 11.536  1.00 9.63  ?  342 GLN A CB    1 
ATOM   2667 C  CG    . GLN A 1 344 ? 45.819 36.640 10.709  1.00 10.44 ?  342 GLN A CG    1 
ATOM   2668 C  CD    . GLN A 1 344 ? 47.052 36.138 11.383  1.00 10.38 ?  342 GLN A CD    1 
ATOM   2669 O  OE1   . GLN A 1 344 ? 47.335 36.428 12.545  1.00 11.02 ?  342 GLN A OE1   1 
ATOM   2670 N  NE2   . GLN A 1 344 ? 47.820 35.315 10.666  1.00 12.78 ?  342 GLN A NE2   1 
ATOM   2671 N  N     . THR A 1 345 ? 41.766 35.202 12.372  1.00 9.26  ?  343 THR A N     1 
ATOM   2672 C  CA    . THR A 1 345 ? 40.561 35.225 13.182  1.00 10.31 ?  343 THR A CA    1 
ATOM   2673 C  C     . THR A 1 345 ? 40.417 33.925 14.002  1.00 10.50 ?  343 THR A C     1 
ATOM   2674 O  O     . THR A 1 345 ? 40.017 33.947 15.099  1.00 10.10 ?  343 THR A O     1 
ATOM   2675 C  CB    . THR A 1 345 ? 39.322 35.489 12.261  1.00 12.70 ?  343 THR A CB    1 
ATOM   2676 O  OG1   . THR A 1 345 ? 39.427 36.843 11.818  1.00 20.69 ?  343 THR A OG1   1 
ATOM   2677 C  CG2   . THR A 1 345 ? 38.022 35.350 13.016  1.00 17.37 ?  343 THR A CG2   1 
ATOM   2678 N  N     . TYR A 1 346 ? 40.779 32.825 13.388  1.00 9.80  ?  344 TYR A N     1 
ATOM   2679 C  CA    . TYR A 1 346 ? 40.782 31.506 14.058  1.00 9.90  ?  344 TYR A CA    1 
ATOM   2680 C  C     . TYR A 1 346 ? 41.646 31.594 15.292  1.00 9.28  ?  344 TYR A C     1 
ATOM   2681 O  O     . TYR A 1 346 ? 41.295 31.130 16.391  1.00 9.34  ?  344 TYR A O     1 
ATOM   2682 C  CB    . TYR A 1 346 ? 41.281 30.456 13.087  1.00 10.15 ?  344 TYR A CB    1 
ATOM   2683 C  CG    . TYR A 1 346 ? 41.890 29.217 13.709  1.00 9.17  ?  344 TYR A CG    1 
ATOM   2684 C  CD1   . TYR A 1 346 ? 41.093 28.280 14.356  1.00 8.45  ?  344 TYR A CD1   1 
ATOM   2685 C  CD2   . TYR A 1 346 ? 43.244 29.020 13.698  1.00 8.67  ?  344 TYR A CD2   1 
ATOM   2686 C  CE1   . TYR A 1 346 ? 41.646 27.157 14.922  1.00 9.12  ?  344 TYR A CE1   1 
ATOM   2687 C  CE2   . TYR A 1 346 ? 43.822 27.893 14.278  1.00 8.65  ?  344 TYR A CE2   1 
ATOM   2688 C  CZ    . TYR A 1 346 ? 43.003 26.972 14.902  1.00 8.93  ?  344 TYR A CZ    1 
ATOM   2689 O  OH    . TYR A 1 346 ? 43.521 25.831 15.450  1.00 8.66  ?  344 TYR A OH    1 
ATOM   2690 N  N     . GLU A 1 347 ? 42.830 32.181 15.158  1.00 8.24  ?  345 GLU A N     1 
ATOM   2691 C  CA    . GLU A 1 347 ? 43.777 32.279 16.262  1.00 8.47  ?  345 GLU A CA    1 
ATOM   2692 C  C     . GLU A 1 347 ? 43.271 33.219 17.339  1.00 9.11  ?  345 GLU A C     1 
ATOM   2693 O  O     . GLU A 1 347 ? 43.402 32.948 18.495  1.00 9.05  ?  345 GLU A O     1 
ATOM   2694 C  CB    . GLU A 1 347 ? 45.177 32.690 15.766  1.00 9.04  ?  345 GLU A CB    1 
ATOM   2695 C  CG    . GLU A 1 347 ? 46.172 33.058 16.876  1.00 8.66  ?  345 GLU A CG    1 
ATOM   2696 C  CD    . GLU A 1 347 ? 47.598 33.300 16.406  1.00 8.84  ?  345 GLU A CD    1 
ATOM   2697 O  OE1   . GLU A 1 347 ? 47.924 32.910 15.265  1.00 9.46  ?  345 GLU A OE1   1 
ATOM   2698 O  OE2   . GLU A 1 347 ? 48.390 33.879 17.179  1.00 10.51 ?  345 GLU A OE2   1 
ATOM   2699 N  N     . ASP A 1 348 ? 42.664 34.320 16.952  1.00 9.10  ?  346 ASP A N     1 
ATOM   2700 C  CA    . ASP A 1 348 ? 42.141 35.298 17.908  1.00 9.63  ?  346 ASP A CA    1 
ATOM   2701 C  C     . ASP A 1 348 ? 41.124 34.596 18.803  1.00 8.57  ?  346 ASP A C     1 
ATOM   2702 O  O     . ASP A 1 348 ? 41.132 34.714 19.982  1.00 9.53  ?  346 ASP A O     1 
ATOM   2703 C  CB    . ASP A 1 348 ? 41.368 36.429 17.227  1.00 10.69 ?  346 ASP A CB    1 
ATOM   2704 C  CG    . ASP A 1 348 ? 42.242 37.453 16.476  1.00 13.71 ?  346 ASP A CG    1 
ATOM   2705 O  OD1   . ASP A 1 348 ? 43.484 37.372 16.589  1.00 13.66 ?  346 ASP A OD1   1 
ATOM   2706 O  OD2   . ASP A 1 348 ? 41.677 38.324 15.783  1.00 18.14 ?  346 ASP A OD2   1 
ATOM   2707 N  N     . SER A 1 349 ? 40.202 33.881 18.206  1.00 9.02  ?  347 SER A N     1 
ATOM   2708 C  CA    . SER A 1 349 ? 39.161 33.189 18.918  1.00 10.45 ?  347 SER A CA    1 
ATOM   2709 C  C     . SER A 1 349 ? 39.706 32.103 19.855  1.00 10.27 ?  347 SER A C     1 
ATOM   2710 O  O     . SER A 1 349 ? 39.273 31.939 20.933  1.00 9.63  ?  347 SER A O     1 
ATOM   2711 C  CB    . SER A 1 349 ? 38.184 32.599 17.892  1.00 14.63 ?  347 SER A CB    1 
ATOM   2712 O  OG    . SER A 1 349 ? 37.183 31.856 18.452  1.00 20.97 ?  347 SER A OG    1 
ATOM   2713 N  N     . TYR A 1 350 ? 40.679 31.383 19.353  1.00 9.88  ?  348 TYR A N     1 
ATOM   2714 C  CA    . TYR A 1 350 ? 41.339 30.325 20.148  1.00 9.19  ?  348 TYR A CA    1 
ATOM   2715 C  C     . TYR A 1 350 ? 41.988 30.929 21.358  1.00 9.87  ?  348 TYR A C     1 
ATOM   2716 O  O     . TYR A 1 350 ? 41.897 30.464 22.494  1.00 9.14  ?  348 TYR A O     1 
ATOM   2717 C  CB    . TYR A 1 350 ? 42.353 29.622 19.253  1.00 9.61  ?  348 TYR A CB    1 
ATOM   2718 C  CG    . TYR A 1 350 ? 42.752 28.185 19.584  1.00 8.00  ?  348 TYR A CG    1 
ATOM   2719 C  CD1   . TYR A 1 350 ? 43.062 27.787 20.867  1.00 9.23  ?  348 TYR A CD1   1 
ATOM   2720 C  CD2   . TYR A 1 350 ? 42.805 27.240 18.579  1.00 8.99  ?  348 TYR A CD2   1 
ATOM   2721 C  CE1   . TYR A 1 350 ? 43.505 26.492 21.111  1.00 9.14  ?  348 TYR A CE1   1 
ATOM   2722 C  CE2   . TYR A 1 350 ? 43.217 25.937 18.816  1.00 8.69  ?  348 TYR A CE2   1 
ATOM   2723 C  CZ    . TYR A 1 350 ? 43.545 25.576 20.093  1.00 8.99  ?  348 TYR A CZ    1 
ATOM   2724 O  OH    . TYR A 1 350 ? 43.960 24.269 20.308  1.00 8.93  ?  348 TYR A OH    1 
ATOM   2725 N  N     . ARG A 1 351 ? 42.677 32.060 21.162  1.00 9.25  ?  349 ARG A N     1 
ATOM   2726 C  CA    . ARG A 1 351 ? 43.402 32.726 22.252  1.00 9.49  ?  349 ARG A CA    1 
ATOM   2727 C  C     . ARG A 1 351 ? 42.441 33.311 23.297  1.00 9.83  ?  349 ARG A C     1 
ATOM   2728 O  O     . ARG A 1 351 ? 42.805 33.299 24.481  1.00 10.25 ?  349 ARG A O     1 
ATOM   2729 C  CB    . ARG A 1 351 ? 44.354 33.807 21.773  1.00 9.25  ?  349 ARG A CB    1 
ATOM   2730 C  CG    . ARG A 1 351 ? 45.558 33.260 21.052  1.00 9.46  ?  349 ARG A CG    1 
ATOM   2731 C  CD    . ARG A 1 351 ? 46.512 34.388 20.681  1.00 10.10 ?  349 ARG A CD    1 
ATOM   2732 N  NE    . ARG A 1 351 ? 47.693 33.921 19.977  1.00 11.07 ?  349 ARG A NE    1 
ATOM   2733 C  CZ    . ARG A 1 351 ? 48.774 33.429 20.486  1.00 11.71 ?  349 ARG A CZ    1 
ATOM   2734 N  NH1   . ARG A 1 351 ? 48.905 33.349 21.800  1.00 13.65 ?  349 ARG A NH1   1 
ATOM   2735 N  NH2   . ARG A 1 351 ? 49.769 33.072 19.706  1.00 13.01 ?  349 ARG A NH2   1 
ATOM   2736 N  N     . ASP A 1 352 ? 41.303 33.813 22.881  1.00 9.61  ?  350 ASP A N     1 
ATOM   2737 C  CA    . ASP A 1 352 ? 40.305 34.315 23.814  1.00 11.00 ?  350 ASP A CA    1 
ATOM   2738 C  C     . ASP A 1 352 ? 39.839 33.152 24.711  1.00 10.40 ?  350 ASP A C     1 
ATOM   2739 O  O     . ASP A 1 352 ? 39.891 33.271 25.911  1.00 11.36 ?  350 ASP A O     1 
ATOM   2740 C  CB    . ASP A 1 352 ? 39.137 34.876 22.994  1.00 12.09 ?  350 ASP A CB    1 
ATOM   2741 C  CG    . ASP A 1 352 ? 38.076 35.599 23.800  1.00 17.55 ?  350 ASP A CG    1 
ATOM   2742 O  OD1   . ASP A 1 352 ? 38.178 35.706 24.950  1.00 20.87 ?  350 ASP A OD1   1 
ATOM   2743 O  OD2   . ASP A 1 352 ? 37.156 36.091 23.180  1.00 22.58 ?  350 ASP A OD2   1 
ATOM   2744 N  N     . PHE A 1 353 ? 39.465 32.032 24.102  1.00 9.98  ?  351 PHE A N     1 
ATOM   2745 C  CA    . PHE A 1 353 ? 38.986 30.872 24.855  1.00 10.17 ?  351 PHE A CA    1 
ATOM   2746 C  C     . PHE A 1 353 ? 40.092 30.337 25.755  1.00 11.05 ?  351 PHE A C     1 
ATOM   2747 O  O     . PHE A 1 353 ? 39.837 30.024 26.921  1.00 10.79 ?  351 PHE A O     1 
ATOM   2748 C  CB    . PHE A 1 353 ? 38.531 29.842 23.845  1.00 11.08 ?  351 PHE A CB    1 
ATOM   2749 C  CG    . PHE A 1 353 ? 37.940 28.616 24.491  1.00 11.18 ?  351 PHE A CG    1 
ATOM   2750 C  CD1   . PHE A 1 353 ? 36.601 28.571 24.828  1.00 12.89 ?  351 PHE A CD1   1 
ATOM   2751 C  CD2   . PHE A 1 353 ? 38.680 27.453 24.628  1.00 12.44 ?  351 PHE A CD2   1 
ATOM   2752 C  CE1   . PHE A 1 353 ? 36.052 27.445 25.442  1.00 12.92 ?  351 PHE A CE1   1 
ATOM   2753 C  CE2   . PHE A 1 353 ? 38.104 26.314 25.174  1.00 12.04 ?  351 PHE A CE2   1 
ATOM   2754 C  CZ    . PHE A 1 353 ? 36.796 26.307 25.577  1.00 12.40 ?  351 PHE A CZ    1 
ATOM   2755 N  N     . LEU A 1 354 ? 41.279 30.186 25.220  1.00 10.00 ?  352 LEU A N     1 
ATOM   2756 C  CA    . LEU A 1 354 ? 42.418 29.675 25.948  1.00 11.12 ?  352 LEU A CA    1 
ATOM   2757 C  C     . LEU A 1 354 ? 42.810 30.529 27.119  1.00 11.45 ?  352 LEU A C     1 
ATOM   2758 O  O     . LEU A 1 354 ? 43.092 30.060 28.125  1.00 11.61 ?  352 LEU A O     1 
ATOM   2759 C  CB    . LEU A 1 354 ? 43.596 29.533 24.959  1.00 13.72 ?  352 LEU A CB    1 
ATOM   2760 C  CG    . LEU A 1 354 ? 44.934 29.081 25.421  1.00 17.34 ?  352 LEU A CG    1 
ATOM   2761 C  CD1   . LEU A 1 354 ? 44.874 27.571 25.622  1.00 15.60 ?  352 LEU A CD1   1 
ATOM   2762 C  CD2   . LEU A 1 354 ? 45.919 29.357 24.299  1.00 20.41 ?  352 LEU A CD2   1 
ATOM   2763 N  N     . ASN A 1 355 ? 42.823 31.832 26.910  1.00 10.88 ?  353 ASN A N     1 
ATOM   2764 C  CA    . ASN A 1 355 ? 43.213 32.708 27.967  1.00 11.36 ?  353 ASN A CA    1 
ATOM   2765 C  C     . ASN A 1 355 ? 42.271 32.713 29.169  1.00 10.20 ?  353 ASN A C     1 
ATOM   2766 O  O     . ASN A 1 355 ? 42.711 32.878 30.235  1.00 11.15 ?  353 ASN A O     1 
ATOM   2767 C  CB    . ASN A 1 355 ? 43.448 34.156 27.461  1.00 12.69 ?  353 ASN A CB    1 
ATOM   2768 C  CG    . ASN A 1 355 ? 44.381 34.918 28.355  1.00 14.74 ?  353 ASN A CG    1 
ATOM   2769 O  OD1   . ASN A 1 355 ? 45.536 34.633 28.406  1.00 19.03 ?  353 ASN A OD1   1 
ATOM   2770 N  ND2   . ASN A 1 355 ? 43.853 35.827 29.054  1.00 14.93 ?  353 ASN A ND2   1 
ATOM   2771 N  N     . SER A 1 356 ? 40.971 32.567 28.937  1.00 10.91 ?  354 SER A N     1 
ATOM   2772 C  CA    . SER A 1 356 ? 40.046 32.521 30.087  1.00 12.23 ?  354 SER A CA    1 
ATOM   2773 C  C     . SER A 1 356 ? 40.415 31.340 30.992  1.00 10.92 ?  354 SER A C     1 
ATOM   2774 O  O     . SER A 1 356 ? 40.468 31.459 32.217  1.00 12.02 ?  354 SER A O     1 
ATOM   2775 C  CB    . SER A 1 356 ? 38.623 32.384 29.628  1.00 14.68 ?  354 SER A CB    1 
ATOM   2776 O  OG    . SER A 1 356 ? 38.260 33.524 28.893  1.00 17.92 ?  354 SER A OG    1 
ATOM   2777 N  N     . LEU A 1 357 ? 40.705 30.199 30.364  1.00 10.86 ?  355 LEU A N     1 
ATOM   2778 C  CA    . LEU A 1 357 ? 41.066 28.958 31.079  1.00 11.47 ?  355 LEU A CA    1 
ATOM   2779 C  C     . LEU A 1 357 ? 42.445 29.080 31.699  1.00 10.90 ?  355 LEU A C     1 
ATOM   2780 O  O     . LEU A 1 357 ? 42.635 28.637 32.820  1.00 11.56 ?  355 LEU A O     1 
ATOM   2781 C  CB    . LEU A 1 357 ? 40.956 27.766 30.140  1.00 11.60 ?  355 LEU A CB    1 
ATOM   2782 C  CG    . LEU A 1 357 ? 39.524 27.381 29.842  1.00 13.96 ?  355 LEU A CG    1 
ATOM   2783 C  CD1   . LEU A 1 357 ? 39.517 26.388 28.676  1.00 16.03 ?  355 LEU A CD1   1 
ATOM   2784 C  CD2   . LEU A 1 357 ? 38.808 26.891 31.066  1.00 15.42 ?  355 LEU A CD2   1 
ATOM   2785 N  N     . LEU A 1 358 ? 43.413 29.683 31.037  1.00 10.78 ?  356 LEU A N     1 
ATOM   2786 C  CA    . LEU A 1 358 ? 44.758 29.828 31.603  1.00 10.62 ?  356 LEU A CA    1 
ATOM   2787 C  C     . LEU A 1 358 ? 44.662 30.704 32.828  1.00 10.89 ?  356 LEU A C     1 
ATOM   2788 O  O     . LEU A 1 358 ? 45.322 30.387 33.865  1.00 11.23 ?  356 LEU A O     1 
ATOM   2789 C  CB    . LEU A 1 358 ? 45.678 30.437 30.540  1.00 11.22 ?  356 LEU A CB    1 
ATOM   2790 C  CG    . LEU A 1 358 ? 47.055 30.784 31.036  1.00 13.78 ?  356 LEU A CG    1 
ATOM   2791 C  CD1   . LEU A 1 358 ? 47.846 29.553 31.477  1.00 14.31 ?  356 LEU A CD1   1 
ATOM   2792 C  CD2   . LEU A 1 358 ? 47.816 31.474 29.929  1.00 16.49 ?  356 LEU A CD2   1 
ATOM   2793 N  N     . GLU A 1 359 ? 43.975 31.846 32.723  1.00 11.90 ?  357 GLU A N     1 
ATOM   2794 C  CA    . GLU A 1 359 ? 43.877 32.735 33.913  1.00 12.89 ?  357 GLU A CA    1 
ATOM   2795 C  C     . GLU A 1 359 ? 43.147 31.986 35.017  1.00 11.96 ?  357 GLU A C     1 
ATOM   2796 O  O     . GLU A 1 359 ? 43.557 32.118 36.180  1.00 14.03 ?  357 GLU A O     1 
ATOM   2797 C  CB    . GLU A 1 359 ? 43.060 34.005 33.588  1.00 14.99 ?  357 GLU A CB    1 
ATOM   2798 C  CG    . GLU A 1 359 ? 43.860 34.993 32.780  1.00 19.98 ?  357 GLU A CG    1 
ATOM   2799 C  CD    . GLU A 1 359 ? 43.332 36.411 32.802  1.00 24.18 ?  357 GLU A CD    1 
ATOM   2800 O  OE1   . GLU A 1 359 ? 42.458 36.696 33.674  1.00 24.89 ?  357 GLU A OE1   1 
ATOM   2801 O  OE2   . GLU A 1 359 ? 43.800 37.179 31.888  1.00 26.43 ?  357 GLU A OE2   1 
ATOM   2802 N  N     . PHE A 1 360 ? 42.122 31.218 34.717  1.00 11.86 ?  358 PHE A N     1 
ATOM   2803 C  CA    . PHE A 1 360 ? 41.363 30.547 35.792  1.00 12.23 ?  358 PHE A CA    1 
ATOM   2804 C  C     . PHE A 1 360 ? 42.185 29.426 36.400  1.00 12.40 ?  358 PHE A C     1 
ATOM   2805 O  O     . PHE A 1 360 ? 42.189 29.261 37.629  1.00 11.92 ?  358 PHE A O     1 
ATOM   2806 C  CB    . PHE A 1 360 ? 40.046 30.014 35.313  1.00 12.85 ?  358 PHE A CB    1 
ATOM   2807 C  CG    . PHE A 1 360 ? 39.200 29.596 36.470  1.00 13.43 ?  358 PHE A CG    1 
ATOM   2808 C  CD1   . PHE A 1 360 ? 38.715 30.574 37.355  1.00 14.68 ?  358 PHE A CD1   1 
ATOM   2809 C  CD2   . PHE A 1 360 ? 38.869 28.281 36.707  1.00 13.43 ?  358 PHE A CD2   1 
ATOM   2810 C  CE1   . PHE A 1 360 ? 37.968 30.202 38.459  1.00 14.41 ?  358 PHE A CE1   1 
ATOM   2811 C  CE2   . PHE A 1 360 ? 38.105 27.923 37.815  1.00 14.62 ?  358 PHE A CE2   1 
ATOM   2812 C  CZ    . PHE A 1 360 ? 37.646 28.890 38.677  1.00 14.58 ?  358 PHE A CZ    1 
ATOM   2813 N  N     . VAL A 1 361 ? 42.941 28.669 35.610  1.00 12.04 ?  359 VAL A N     1 
ATOM   2814 C  CA    . VAL A 1 361 ? 43.777 27.590 36.166  1.00 12.12 ?  359 VAL A CA    1 
ATOM   2815 C  C     . VAL A 1 361 ? 44.806 28.217 37.096  1.00 13.55 ?  359 VAL A C     1 
ATOM   2816 O  O     . VAL A 1 361 ? 45.074 27.727 38.204  1.00 12.67 ?  359 VAL A O     1 
ATOM   2817 C  CB    . VAL A 1 361 ? 44.408 26.756 35.034  1.00 12.68 ?  359 VAL A CB    1 
ATOM   2818 C  CG1   . VAL A 1 361 ? 45.557 25.918 35.578  1.00 15.16 ?  359 VAL A CG1   1 
ATOM   2819 C  CG2   . VAL A 1 361 ? 43.343 25.881 34.424  1.00 14.21 ?  359 VAL A CG2   1 
ATOM   2820 N  N     . ARG A 1 362 ? 45.438 29.330 36.703  1.00 12.73 ?  360 ARG A N     1 
ATOM   2821 C  CA    . ARG A 1 362 ? 46.438 29.971 37.543  1.00 12.89 ?  360 ARG A CA    1 
ATOM   2822 C  C     . ARG A 1 362 ? 45.779 30.458 38.836  1.00 13.08 ?  360 ARG A C     1 
ATOM   2823 O  O     . ARG A 1 362 ? 46.462 30.346 39.888  1.00 17.36 ?  360 ARG A O     1 
ATOM   2824 C  CB    . ARG A 1 362 ? 47.105 31.137 36.787  1.00 13.84 ?  360 ARG A CB    1 
ATOM   2825 C  CG    . ARG A 1 362 ? 48.170 30.698 35.805  1.00 14.04 ?  360 ARG A CG    1 
ATOM   2826 C  CD    . ARG A 1 362 ? 48.664 31.849 34.914  1.00 14.75 ?  360 ARG A CD    1 
ATOM   2827 N  NE    . ARG A 1 362 ? 49.876 31.488 34.252  1.00 15.59 ?  360 ARG A NE    1 
ATOM   2828 C  CZ    . ARG A 1 362 ? 50.359 32.114 33.158  1.00 17.58 ?  360 ARG A CZ    1 
ATOM   2829 N  NH1   . ARG A 1 362 ? 49.610 33.010 32.531  1.00 19.14 ?  360 ARG A NH1   1 
ATOM   2830 N  NH2   . ARG A 1 362 ? 51.502 31.734 32.648  1.00 18.30 ?  360 ARG A NH2   1 
ATOM   2831 N  N     . PHE A 1 363 ? 44.568 30.972 38.774  1.00 13.79 ?  361 PHE A N     1 
ATOM   2832 C  CA    . PHE A 1 363 ? 43.791 31.418 39.958  1.00 14.83 ?  361 PHE A CA    1 
ATOM   2833 C  C     . PHE A 1 363 ? 43.492 30.210 40.827  1.00 15.97 ?  361 PHE A C     1 
ATOM   2834 O  O     . PHE A 1 363 ? 43.707 30.269 42.080  1.00 16.49 ?  361 PHE A O     1 
ATOM   2835 C  CB    . PHE A 1 363 ? 42.547 32.151 39.497  1.00 16.37 ?  361 PHE A CB    1 
ATOM   2836 C  CG    . PHE A 1 363 ? 41.604 32.614 40.553  1.00 18.89 ?  361 PHE A CG    1 
ATOM   2837 C  CD1   . PHE A 1 363 ? 41.793 33.859 41.125  1.00 25.57 ?  361 PHE A CD1   1 
ATOM   2838 C  CD2   . PHE A 1 363 ? 40.499 31.880 40.902  1.00 21.92 ?  361 PHE A CD2   1 
ATOM   2839 C  CE1   . PHE A 1 363 ? 40.870 34.350 42.031  1.00 28.32 ?  361 PHE A CE1   1 
ATOM   2840 C  CE2   . PHE A 1 363 ? 39.640 32.332 41.889  1.00 23.74 ?  361 PHE A CE2   1 
ATOM   2841 C  CZ    . PHE A 1 363 ? 39.844 33.546 42.469  1.00 27.97 ?  361 PHE A CZ    1 
ATOM   2842 N  N     . PHE A 1 364 ? 43.024 29.127 40.228  1.00 14.48 ?  362 PHE A N     1 
ATOM   2843 C  CA    . PHE A 1 364 ? 42.501 27.961 40.960  1.00 14.94 ?  362 PHE A CA    1 
ATOM   2844 C  C     . PHE A 1 364 ? 43.635 27.271 41.682  1.00 14.93 ?  362 PHE A C     1 
ATOM   2845 O  O     . PHE A 1 364 ? 43.429 26.596 42.714  1.00 16.02 ?  362 PHE A O     1 
ATOM   2846 C  CB    . PHE A 1 364 ? 41.842 26.988 39.970  1.00 14.40 ?  362 PHE A CB    1 
ATOM   2847 C  CG    . PHE A 1 364 ? 40.890 26.035 40.618  1.00 14.74 ?  362 PHE A CG    1 
ATOM   2848 C  CD1   . PHE A 1 364 ? 39.623 26.475 41.004  1.00 15.92 ?  362 PHE A CD1   1 
ATOM   2849 C  CD2   . PHE A 1 364 ? 41.217 24.704 40.855  1.00 15.49 ?  362 PHE A CD2   1 
ATOM   2850 C  CE1   . PHE A 1 364 ? 38.737 25.644 41.652  1.00 15.91 ?  362 PHE A CE1   1 
ATOM   2851 C  CE2   . PHE A 1 364 ? 40.303 23.871 41.455  1.00 17.96 ?  362 PHE A CE2   1 
ATOM   2852 C  CZ    . PHE A 1 364 ? 39.076 24.328 41.861  1.00 17.18 ?  362 PHE A CZ    1 
ATOM   2853 N  N     . TYR A 1 365 ? 44.854 27.425 41.198  1.00 14.37 ?  363 TYR A N     1 
ATOM   2854 C  CA    . TYR A 1 365 ? 46.046 26.868 41.821  1.00 15.12 ?  363 TYR A CA    1 
ATOM   2855 C  C     . TYR A 1 365 ? 46.273 27.459 43.227  1.00 17.13 ?  363 TYR A C     1 
ATOM   2856 O  O     . TYR A 1 365 ? 47.026 26.835 44.002  1.00 17.98 ?  363 TYR A O     1 
ATOM   2857 C  CB    . TYR A 1 365 ? 47.292 27.000 40.947  1.00 13.36 ?  363 TYR A CB    1 
ATOM   2858 C  CG    . TYR A 1 365 ? 47.685 25.720 40.225  1.00 12.12 ?  363 TYR A CG    1 
ATOM   2859 C  CD1   . TYR A 1 365 ? 48.125 24.626 40.921  1.00 13.02 ?  363 TYR A CD1   1 
ATOM   2860 C  CD2   . TYR A 1 365 ? 47.634 25.610 38.834  1.00 11.97 ?  363 TYR A CD2   1 
ATOM   2861 C  CE1   . TYR A 1 365 ? 48.457 23.443 40.291  1.00 11.69 ?  363 TYR A CE1   1 
ATOM   2862 C  CE2   . TYR A 1 365 ? 47.976 24.427 38.186  1.00 10.77 ?  363 TYR A CE2   1 
ATOM   2863 C  CZ    . TYR A 1 365 ? 48.370 23.315 38.893  1.00 10.50 ?  363 TYR A CZ    1 
ATOM   2864 O  OH    . TYR A 1 365 ? 48.768 22.129 38.304  1.00 11.12 ?  363 TYR A OH    1 
ATOM   2865 N  N     . ASP A 1 366 ? 45.707 28.614 43.531  1.00 16.04 ?  364 ASP A N     1 
ATOM   2866 C  CA    . ASP A 1 366 ? 45.750 29.166 44.923  1.00 19.29 ?  364 ASP A CA    1 
ATOM   2867 C  C     . ASP A 1 366 ? 44.725 28.408 45.750  1.00 20.64 ?  364 ASP A C     1 
ATOM   2868 O  O     . ASP A 1 366 ? 43.504 28.687 45.575  1.00 19.89 ?  364 ASP A O     1 
ATOM   2869 C  CB    . ASP A 1 366 ? 45.462 30.656 44.855  1.00 19.70 ?  364 ASP A CB    1 
ATOM   2870 C  CG    . ASP A 1 366 ? 45.523 31.314 46.225  1.00 25.23 ?  364 ASP A CG    1 
ATOM   2871 O  OD1   . ASP A 1 366 ? 45.525 30.587 47.213  1.00 27.42 ?  364 ASP A OD1   1 
ATOM   2872 O  OD2   . ASP A 1 366 ? 45.560 32.542 46.244  1.00 30.63 ?  364 ASP A OD2   1 
ATOM   2873 N  N     . ARG A 1 367 ? 45.212 27.490 46.598  1.00 21.62 ?  365 ARG A N     1 
ATOM   2874 C  CA    . ARG A 1 367 ? 44.328 26.600 47.393  1.00 23.57 ?  365 ARG A CA    1 
ATOM   2875 C  C     . ARG A 1 367 ? 43.978 27.285 48.729  1.00 25.55 ?  365 ARG A C     1 
ATOM   2876 O  O     . ARG A 1 367 ? 43.525 26.559 49.613  1.00 30.87 ?  365 ARG A O     1 
ATOM   2877 C  CB    . ARG A 1 367 ? 44.982 25.217 47.540  1.00 24.16 ?  365 ARG A CB    1 
ATOM   2878 C  CG    . ARG A 1 367 ? 45.014 24.403 46.243  1.00 26.99 ?  365 ARG A CG    1 
ATOM   2879 C  CD    . ARG A 1 367 ? 46.245 23.523 46.052  1.00 32.83 ?  365 ARG A CD    1 
ATOM   2880 N  NE    . ARG A 1 367 ? 47.272 24.315 45.384  1.00 29.19 ?  365 ARG A NE    1 
ATOM   2881 C  CZ    . ARG A 1 367 ? 48.443 23.882 44.982  1.00 32.68 ?  365 ARG A CZ    1 
ATOM   2882 N  NH1   . ARG A 1 367 ? 48.766 22.602 45.111  1.00 38.00 ?  365 ARG A NH1   1 
ATOM   2883 N  NH2   . ARG A 1 367 ? 49.280 24.740 44.419  1.00 34.31 ?  365 ARG A NH2   1 
ATOM   2884 N  N     . THR A 1 368 ? 44.165 28.599 48.856  1.00 26.04 ?  366 THR A N     1 
ATOM   2885 C  CA    . THR A 1 368 ? 43.880 29.347 50.123  1.00 29.42 ?  366 THR A CA    1 
ATOM   2886 C  C     . THR A 1 368 ? 42.467 29.936 50.070  1.00 32.45 ?  366 THR A C     1 
ATOM   2887 O  O     . THR A 1 368 ? 41.992 30.422 51.108  1.00 33.94 ?  366 THR A O     1 
ATOM   2888 C  CB    . THR A 1 368 ? 44.940 30.410 50.430  1.00 28.85 ?  366 THR A CB    1 
ATOM   2889 O  OG1   . THR A 1 368 ? 44.833 31.518 49.540  1.00 32.60 ?  366 THR A OG1   1 
ATOM   2890 C  CG2   . THR A 1 368 ? 46.339 29.839 50.459  1.00 32.64 ?  366 THR A CG2   1 
ATOM   2891 N  N     . LYS A 1 369 ? 41.773 29.837 48.934  1.00 27.15 ?  367 LYS A N     1 
ATOM   2892 C  CA    . LYS A 1 369 ? 40.439 30.443 48.721  1.00 25.64 ?  367 LYS A CA    1 
ATOM   2893 C  C     . LYS A 1 369 ? 39.354 29.415 48.990  1.00 26.57 ?  367 LYS A C     1 
ATOM   2894 O  O     . LYS A 1 369 ? 39.664 28.227 49.104  1.00 30.71 ?  367 LYS A O     1 
ATOM   2895 C  CB    . LYS A 1 369 ? 40.298 30.947 47.291  1.00 25.33 ?  367 LYS A CB    1 
ATOM   2896 C  CG    . LYS A 1 369 ? 41.301 31.997 46.863  1.00 30.66 ?  367 LYS A CG    1 
ATOM   2897 C  CD    . LYS A 1 369 ? 41.292 32.154 45.369  1.00 36.14 ?  367 LYS A CD    1 
ATOM   2898 C  CE    . LYS A 1 369 ? 42.413 33.052 44.901  1.00 40.79 ?  367 LYS A CE    1 
ATOM   2899 N  NZ    . LYS A 1 369 ? 42.279 34.389 45.542  1.00 42.96 ?  367 LYS A NZ    1 
ATOM   2900 N  N     . GLY A 1 370 ? 38.107 29.832 48.965  1.00 24.67 ?  368 GLY A N     1 
ATOM   2901 C  CA    . GLY A 1 370 ? 36.967 28.925 49.164  1.00 25.63 ?  368 GLY A CA    1 
ATOM   2902 C  C     . GLY A 1 370 ? 36.178 28.761 47.882  1.00 23.66 ?  368 GLY A C     1 
ATOM   2903 O  O     . GLY A 1 370 ? 36.325 29.543 46.920  1.00 19.42 ?  368 GLY A O     1 
ATOM   2904 N  N     . GLN A 1 371 ? 35.249 27.813 47.888  1.00 21.81 ?  369 GLN A N     1 
ATOM   2905 C  CA    . GLN A 1 371 ? 34.362 27.530 46.739  1.00 20.70 ?  369 GLN A CA    1 
ATOM   2906 C  C     . GLN A 1 371 ? 33.749 28.823 46.180  1.00 21.43 ?  369 GLN A C     1 
ATOM   2907 O  O     . GLN A 1 371 ? 33.789 29.064 44.945  1.00 18.34 ?  369 GLN A O     1 
ATOM   2908 C  CB    . GLN A 1 371 ? 33.298 26.522 47.189  1.00 20.46 ?  369 GLN A CB    1 
ATOM   2909 C  CG    . GLN A 1 371 ? 32.267 26.279 46.140  1.00 18.54 ?  369 GLN A CG    1 
ATOM   2910 C  CD    . GLN A 1 371 ? 31.176 25.348 46.612  1.00 20.10 ?  369 GLN A CD    1 
ATOM   2911 O  OE1   . GLN A 1 371 ? 31.052 25.072 47.825  1.00 23.23 ?  369 GLN A OE1   1 
ATOM   2912 N  NE2   . GLN A 1 371 ? 30.425 24.849 45.665  1.00 21.87 ?  369 GLN A NE2   1 
ATOM   2913 N  N     . LYS A 1 372 ? 33.194 29.685 47.042  1.00 21.10 ?  370 LYS A N     1 
ATOM   2914 C  CA    . LYS A 1 372 ? 32.549 30.918 46.537  1.00 23.69 ?  370 LYS A CA    1 
ATOM   2915 C  C     . LYS A 1 372 ? 33.571 31.840 45.862  1.00 18.36 ?  370 LYS A C     1 
ATOM   2916 O  O     . LYS A 1 372 ? 33.188 32.474 44.844  1.00 20.91 ?  370 LYS A O     1 
ATOM   2917 C  CB    . LYS A 1 372 ? 31.858 31.612 47.712  1.00 27.74 ?  370 LYS A CB    1 
ATOM   2918 C  CG    . LYS A 1 372 ? 30.623 30.884 48.205  1.00 36.70 ?  370 LYS A CG    1 
ATOM   2919 C  CD    . LYS A 1 372 ? 29.712 31.819 48.994  1.00 45.93 ?  370 LYS A CD    1 
ATOM   2920 C  CE    . LYS A 1 372 ? 28.557 31.122 49.678  1.00 51.81 ?  370 LYS A CE    1 
ATOM   2921 N  NZ    . LYS A 1 372 ? 28.759 31.029 51.143  1.00 54.96 ?  370 LYS A NZ    1 
ATOM   2922 N  N     . ASP A 1 373 ? 34.769 31.908 46.417  1.00 19.09 ?  371 ASP A N     1 
ATOM   2923 C  CA    . ASP A 1 373 ? 35.867 32.719 45.833  1.00 19.42 ?  371 ASP A CA    1 
ATOM   2924 C  C     . ASP A 1 373 ? 36.161 32.185 44.427  1.00 17.83 ?  371 ASP A C     1 
ATOM   2925 O  O     . ASP A 1 373 ? 36.360 32.993 43.500  1.00 17.48 ?  371 ASP A O     1 
ATOM   2926 C  CB    . ASP A 1 373 ? 37.147 32.721 46.648  1.00 20.92 ?  371 ASP A CB    1 
ATOM   2927 C  CG    . ASP A 1 373 ? 36.976 33.295 48.055  1.00 26.43 ?  371 ASP A CG    1 
ATOM   2928 O  OD1   . ASP A 1 373 ? 36.347 34.372 48.132  1.00 27.12 ?  371 ASP A OD1   1 
ATOM   2929 O  OD2   . ASP A 1 373 ? 37.372 32.644 49.034  1.00 25.16 ?  371 ASP A OD2   1 
ATOM   2930 N  N     . TYR A 1 374 ? 36.225 30.857 44.281  1.00 17.95 ?  372 TYR A N     1 
ATOM   2931 C  CA    . TYR A 1 374 ? 36.505 30.323 42.920  1.00 16.04 ?  372 TYR A CA    1 
ATOM   2932 C  C     . TYR A 1 374 ? 35.398 30.650 41.947  1.00 16.25 ?  372 TYR A C     1 
ATOM   2933 O  O     . TYR A 1 374 ? 35.646 30.987 40.805  1.00 15.33 ?  372 TYR A O     1 
ATOM   2934 C  CB    . TYR A 1 374 ? 36.780 28.832 42.987  1.00 15.20 ?  372 TYR A CB    1 
ATOM   2935 C  CG    . TYR A 1 374 ? 37.988 28.475 43.809  1.00 15.49 ?  372 TYR A CG    1 
ATOM   2936 C  CD1   . TYR A 1 374 ? 39.271 28.938 43.515  1.00 16.09 ?  372 TYR A CD1   1 
ATOM   2937 C  CD2   . TYR A 1 374 ? 37.882 27.651 44.931  1.00 17.38 ?  372 TYR A CD2   1 
ATOM   2938 C  CE1   . TYR A 1 374 ? 40.360 28.625 44.306  1.00 17.56 ?  372 TYR A CE1   1 
ATOM   2939 C  CE2   . TYR A 1 374 ? 38.945 27.364 45.735  1.00 16.68 ?  372 TYR A CE2   1 
ATOM   2940 C  CZ    . TYR A 1 374 ? 40.223 27.831 45.436  1.00 17.18 ?  372 TYR A CZ    1 
ATOM   2941 O  OH    . TYR A 1 374 ? 41.309 27.518 46.195  1.00 20.00 ?  372 TYR A OH    1 
ATOM   2942 N  N     . HIS A 1 375 ? 34.166 30.612 42.383  1.00 15.21 ?  373 HIS A N     1 
ATOM   2943 C  CA    . HIS A 1 375 ? 33.087 30.971 41.527  1.00 15.82 ?  373 HIS A CA    1 
ATOM   2944 C  C     . HIS A 1 375 ? 33.175 32.448 41.081  1.00 15.54 ?  373 HIS A C     1 
ATOM   2945 O  O     . HIS A 1 375 ? 32.955 32.769 39.977  1.00 16.05 ?  373 HIS A O     1 
ATOM   2946 C  CB    . HIS A 1 375 ? 31.731 30.772 42.241  1.00 17.83 ?  373 HIS A CB    1 
ATOM   2947 C  CG    . HIS A 1 375 ? 31.347 29.352 42.504  1.00 17.87 ?  373 HIS A CG    1 
ATOM   2948 N  ND1   . HIS A 1 375 ? 30.199 29.027 43.184  1.00 20.26 ?  373 HIS A ND1   1 
ATOM   2949 C  CD2   . HIS A 1 375 ? 31.950 28.189 42.196  1.00 16.73 ?  373 HIS A CD2   1 
ATOM   2950 C  CE1   . HIS A 1 375 ? 30.101 27.719 43.260  1.00 21.93 ?  373 HIS A CE1   1 
ATOM   2951 N  NE2   . HIS A 1 375 ? 31.153 27.185 42.666  1.00 18.18 ?  373 HIS A NE2   1 
ATOM   2952 N  N     . VAL A 1 376 ? 33.436 33.319 42.041  1.00 18.53 ?  374 VAL A N     1 
ATOM   2953 C  CA    . VAL A 1 376 ? 33.526 34.767 41.747  1.00 19.26 ?  374 VAL A CA    1 
ATOM   2954 C  C     . VAL A 1 376 ? 34.752 35.009 40.842  1.00 17.72 ?  374 VAL A C     1 
ATOM   2955 O  O     . VAL A 1 376 ? 34.629 35.846 39.927  1.00 18.31 ?  374 VAL A O     1 
ATOM   2956 C  CB    . VAL A 1 376 ? 33.597 35.517 43.085  1.00 22.62 ?  374 VAL A CB    1 
ATOM   2957 C  CG1   . VAL A 1 376 ? 34.077 36.952 42.903  1.00 24.48 ?  374 VAL A CG1   1 
ATOM   2958 C  CG2   . VAL A 1 376 ? 32.237 35.456 43.786  1.00 22.43 ?  374 VAL A CG2   1 
ATOM   2959 N  N     . GLY A 1 377 ? 35.813 34.244 41.015  1.00 16.86 ?  375 GLY A N     1 
ATOM   2960 C  CA    . GLY A 1 377 ? 36.983 34.355 40.108  1.00 18.28 ?  375 GLY A CA    1 
ATOM   2961 C  C     . GLY A 1 377 ? 36.594 34.008 38.671  1.00 16.11 ?  375 GLY A C     1 
ATOM   2962 O  O     . GLY A 1 377 ? 36.983 34.696 37.704  1.00 16.95 ?  375 GLY A O     1 
ATOM   2963 N  N     . ALA A 1 378 ? 35.782 32.968 38.465  1.00 15.15 ?  376 ALA A N     1 
ATOM   2964 C  CA    . ALA A 1 378 ? 35.337 32.597 37.122  1.00 15.16 ?  376 ALA A CA    1 
ATOM   2965 C  C     . ALA A 1 378 ? 34.466 33.697 36.534  1.00 14.11 ?  376 ALA A C     1 
ATOM   2966 O  O     . ALA A 1 378 ? 34.585 34.067 35.370  1.00 14.98 ?  376 ALA A O     1 
ATOM   2967 C  CB    . ALA A 1 378 ? 34.577 31.285 37.180  1.00 15.13 ?  376 ALA A CB    1 
ATOM   2968 N  N     . GLN A 1 379 ? 33.512 34.186 37.342  1.00 16.29 ?  377 GLN A N     1 
ATOM   2969 C  CA    . GLN A 1 379 ? 32.657 35.318 36.909  1.00 17.05 ?  377 GLN A CA    1 
ATOM   2970 C  C     . GLN A 1 379 ? 33.471 36.570 36.513  1.00 15.19 ?  377 GLN A C     1 
ATOM   2971 O  O     . GLN A 1 379 ? 33.132 37.178 35.484  1.00 17.23 ?  377 GLN A O     1 
ATOM   2972 C  CB    . GLN A 1 379 ? 31.688 35.605 38.056  1.00 18.67 ?  377 GLN A CB    1 
ATOM   2973 C  CG    . GLN A 1 379 ? 30.730 36.769 37.752  1.00 22.20 ?  377 GLN A CG    1 
ATOM   2974 C  CD    . GLN A 1 379 ? 29.837 37.096 38.937  1.00 19.98 ?  377 GLN A CD    1 
ATOM   2975 O  OE1   . GLN A 1 379 ? 30.326 37.451 39.997  1.00 22.87 ?  377 GLN A OE1   1 
ATOM   2976 N  NE2   . GLN A 1 379 ? 28.557 36.803 38.784  1.00 22.96 ?  377 GLN A NE2   1 
ATOM   2977 N  N     . ALA A 1 380 ? 34.517 36.850 37.249  1.00 16.71 ?  378 ALA A N     1 
ATOM   2978 C  CA    . ALA A 1 380 ? 35.393 38.023 37.022  1.00 17.92 ?  378 ALA A CA    1 
ATOM   2979 C  C     . ALA A 1 380 ? 36.074 37.896 35.658  1.00 19.44 ?  378 ALA A C     1 
ATOM   2980 O  O     . ALA A 1 380 ? 36.290 38.916 34.956  1.00 21.09 ?  378 ALA A O     1 
ATOM   2981 C  CB    . ALA A 1 380 ? 36.356 38.195 38.115  1.00 18.24 ?  378 ALA A CB    1 
ATOM   2982 N  N     . ILE A 1 381 ? 36.337 36.674 35.201  1.00 17.40 ?  379 ILE A N     1 
ATOM   2983 C  CA    . ILE A 1 381 ? 36.958 36.481 33.863  1.00 16.25 ?  379 ILE A CA    1 
ATOM   2984 C  C     . ILE A 1 381 ? 35.943 36.506 32.737  1.00 17.73 ?  379 ILE A C     1 
ATOM   2985 O  O     . ILE A 1 381 ? 36.211 37.199 31.776  1.00 21.19 ?  379 ILE A O     1 
ATOM   2986 C  CB    . ILE A 1 381 ? 37.731 35.154 33.886  1.00 16.04 ?  379 ILE A CB    1 
ATOM   2987 C  CG1   . ILE A 1 381 ? 38.861 35.215 34.902  1.00 15.32 ?  379 ILE A CG1   1 
ATOM   2988 C  CG2   . ILE A 1 381 ? 38.229 34.793 32.487  1.00 15.62 ?  379 ILE A CG2   1 
ATOM   2989 C  CD1   . ILE A 1 381 ? 39.471 33.864 35.224  1.00 17.77 ?  379 ILE A CD1   1 
ATOM   2990 N  N     . ILE A 1 382 ? 34.863 35.703 32.771  1.00 16.69 ?  380 ILE A N     1 
ATOM   2991 C  CA    . ILE A 1 382 ? 33.998 35.488 31.598  1.00 17.76 ?  380 ILE A CA    1 
ATOM   2992 C  C     . ILE A 1 382 ? 32.722 36.349 31.649  1.00 17.42 ?  380 ILE A C     1 
ATOM   2993 O  O     . ILE A 1 382 ? 32.072 36.418 30.650  1.00 19.58 ?  380 ILE A O     1 
ATOM   2994 C  CB    . ILE A 1 382 ? 33.639 33.995 31.410  1.00 18.33 ?  380 ILE A CB    1 
ATOM   2995 C  CG1   . ILE A 1 382 ? 32.769 33.407 32.518  1.00 18.02 ?  380 ILE A CG1   1 
ATOM   2996 C  CG2   . ILE A 1 382 ? 34.914 33.212 31.183  1.00 19.42 ?  380 ILE A CG2   1 
ATOM   2997 C  CD1   . ILE A 1 382 ? 32.067 32.113 32.177  1.00 18.41 ?  380 ILE A CD1   1 
ATOM   2998 N  N     . ASP A 1 383 ? 32.415 36.966 32.793  1.00 19.88 ?  381 ASP A N     1 
ATOM   2999 C  CA    . ASP A 1 383 ? 31.098 37.658 32.977  1.00 21.38 ?  381 ASP A CA    1 
ATOM   3000 C  C     . ASP A 1 383 ? 31.300 38.862 33.889  1.00 21.33 ?  381 ASP A C     1 
ATOM   3001 O  O     . ASP A 1 383 ? 30.694 38.927 34.963  1.00 21.95 ?  381 ASP A O     1 
ATOM   3002 C  CB    . ASP A 1 383 ? 30.080 36.648 33.526  1.00 20.44 ?  381 ASP A CB    1 
ATOM   3003 C  CG    . ASP A 1 383 ? 28.695 37.229 33.812  1.00 22.07 ?  381 ASP A CG    1 
ATOM   3004 O  OD1   . ASP A 1 383 ? 28.318 38.180 33.070  1.00 25.44 ?  381 ASP A OD1   1 
ATOM   3005 O  OD2   . ASP A 1 383 ? 28.052 36.709 34.792  1.00 21.80 ?  381 ASP A OD2   1 
ATOM   3006 N  N     . PRO A 1 384 ? 32.220 39.800 33.550  1.00 23.70 ?  382 PRO A N     1 
ATOM   3007 C  CA    . PRO A 1 384 ? 32.563 40.908 34.456  1.00 27.25 ?  382 PRO A CA    1 
ATOM   3008 C  C     . PRO A 1 384 ? 31.338 41.814 34.765  1.00 26.14 ?  382 PRO A C     1 
ATOM   3009 O  O     . PRO A 1 384 ? 31.325 42.406 35.845  1.00 31.64 ?  382 PRO A O     1 
ATOM   3010 C  CB    . PRO A 1 384 ? 33.728 41.588 33.697  1.00 27.11 ?  382 PRO A CB    1 
ATOM   3011 C  CG    . PRO A 1 384 ? 33.384 41.338 32.259  1.00 24.95 ?  382 PRO A CG    1 
ATOM   3012 C  CD    . PRO A 1 384 ? 32.928 39.878 32.258  1.00 23.95 ?  382 PRO A CD    1 
ATOM   3013 N  N     . ASP A 1 385 ? 30.318 41.825 33.916  1.00 30.68 ?  383 ASP A N     1 
ATOM   3014 C  CA    . ASP A 1 385 ? 29.101 42.671 34.112  1.00 34.23 ?  383 ASP A CA    1 
ATOM   3015 C  C     . ASP A 1 385 ? 28.019 41.885 34.859  1.00 36.53 ?  383 ASP A C     1 
ATOM   3016 O  O     . ASP A 1 385 ? 26.907 42.428 35.066  1.00 34.56 ?  383 ASP A O     1 
ATOM   3017 C  CB    . ASP A 1 385 ? 28.658 43.239 32.768  1.00 36.29 ?  383 ASP A CB    1 
ATOM   3018 C  CG    . ASP A 1 385 ? 29.641 44.291 32.275  1.00 38.94 ?  383 ASP A CG    1 
ATOM   3019 O  OD1   . ASP A 1 385 ? 30.352 44.839 33.119  1.00 39.55 ?  383 ASP A OD1   1 
ATOM   3020 O  OD2   . ASP A 1 385 ? 29.688 44.540 31.062  1.00 47.39 ?  383 ASP A OD2   1 
ATOM   3021 N  N     . LYS A 1 386 ? 28.313 40.650 35.259  1.00 30.98 ?  384 LYS A N     1 
ATOM   3022 C  CA    . LYS A 1 386 ? 27.448 39.810 36.114  1.00 29.18 ?  384 LYS A CA    1 
ATOM   3023 C  C     . LYS A 1 386 ? 26.067 39.585 35.490  1.00 27.14 ?  384 LYS A C     1 
ATOM   3024 O  O     . LYS A 1 386 ? 25.058 39.717 36.228  1.00 35.82 ?  384 LYS A O     1 
ATOM   3025 C  CB    . LYS A 1 386 ? 27.345 40.359 37.533  1.00 33.94 ?  384 LYS A CB    1 
ATOM   3026 C  CG    . LYS A 1 386 ? 28.662 40.551 38.257  1.00 31.91 ?  384 LYS A CG    1 
ATOM   3027 C  CD    . LYS A 1 386 ? 28.409 40.822 39.726  1.00 41.39 ?  384 LYS A CD    1 
ATOM   3028 C  CE    . LYS A 1 386 ? 29.624 40.740 40.617  1.00 45.62 ?  384 LYS A CE    1 
ATOM   3029 N  NZ    . LYS A 1 386 ? 30.455 41.958 40.501  1.00 54.10 ?  384 LYS A NZ    1 
ATOM   3030 N  N     . HIS A 1 387 ? 25.984 39.268 34.209  1.00 27.12 ?  385 HIS A N     1 
ATOM   3031 C  CA    . HIS A 1 387 ? 24.733 38.810 33.543  1.00 27.21 ?  385 HIS A CA    1 
ATOM   3032 C  C     . HIS A 1 387 ? 24.208 37.552 34.221  1.00 31.95 ?  385 HIS A C     1 
ATOM   3033 O  O     . HIS A 1 387 ? 23.022 37.263 34.041  1.00 33.59 ?  385 HIS A O     1 
ATOM   3034 C  CB    . HIS A 1 387 ? 24.943 38.567 32.046  1.00 30.41 ?  385 HIS A CB    1 
ATOM   3035 C  CG    . HIS A 1 387 ? 25.209 39.825 31.299  1.00 31.24 ?  385 HIS A CG    1 
ATOM   3036 N  ND1   . HIS A 1 387 ? 25.602 41.007 31.949  1.00 38.47 ?  385 HIS A ND1   1 
ATOM   3037 C  CD2   . HIS A 1 387 ? 25.144 40.099 29.987  1.00 33.34 ?  385 HIS A CD2   1 
ATOM   3038 C  CE1   . HIS A 1 387 ? 25.785 41.945 31.042  1.00 34.87 ?  385 HIS A CE1   1 
ATOM   3039 N  NE2   . HIS A 1 387 ? 25.500 41.415 29.849  1.00 33.55 ?  385 HIS A NE2   1 
ATOM   3040 N  N     . PHE A 1 388 ? 25.079 36.766 34.878  1.00 28.69 ?  386 PHE A N     1 
ATOM   3041 C  CA    . PHE A 1 388 ? 24.703 35.424 35.390  1.00 26.47 ?  386 PHE A CA    1 
ATOM   3042 C  C     . PHE A 1 388 ? 25.186 35.217 36.810  1.00 21.58 ?  386 PHE A C     1 
ATOM   3043 O  O     . PHE A 1 388 ? 26.157 35.832 37.263  1.00 24.35 ?  386 PHE A O     1 
ATOM   3044 C  CB    . PHE A 1 388 ? 25.293 34.317 34.503  1.00 24.88 ?  386 PHE A CB    1 
ATOM   3045 C  CG    . PHE A 1 388 ? 24.893 34.441 33.065  1.00 26.49 ?  386 PHE A CG    1 
ATOM   3046 C  CD1   . PHE A 1 388 ? 25.695 35.142 32.182  1.00 27.88 ?  386 PHE A CD1   1 
ATOM   3047 C  CD2   . PHE A 1 388 ? 23.658 33.981 32.633  1.00 29.07 ?  386 PHE A CD2   1 
ATOM   3048 C  CE1   . PHE A 1 388 ? 25.289 35.327 30.870  1.00 29.45 ?  386 PHE A CE1   1 
ATOM   3049 C  CE2   . PHE A 1 388 ? 23.273 34.122 31.311  1.00 28.50 ?  386 PHE A CE2   1 
ATOM   3050 C  CZ    . PHE A 1 388 ? 24.067 34.830 30.442  1.00 29.75 ?  386 PHE A CZ    1 
ATOM   3051 N  N     . PRO A 1 389 ? 24.579 34.298 37.591  1.00 23.05 ?  387 PRO A N     1 
ATOM   3052 C  CA    . PRO A 1 389 ? 25.120 33.987 38.908  1.00 22.40 ?  387 PRO A CA    1 
ATOM   3053 C  C     . PRO A 1 389 ? 26.553 33.424 38.865  1.00 22.53 ?  387 PRO A C     1 
ATOM   3054 O  O     . PRO A 1 389 ? 26.851 32.773 37.883  1.00 22.67 ?  387 PRO A O     1 
ATOM   3055 C  CB    . PRO A 1 389 ? 24.163 32.929 39.459  1.00 26.04 ?  387 PRO A CB    1 
ATOM   3056 C  CG    . PRO A 1 389 ? 22.909 33.137 38.677  1.00 25.29 ?  387 PRO A CG    1 
ATOM   3057 C  CD    . PRO A 1 389 ? 23.319 33.575 37.302  1.00 25.45 ?  387 PRO A CD    1 
ATOM   3058 N  N     . ALA A 1 390 ? 27.368 33.691 39.866  1.00 20.80 ?  388 ALA A N     1 
ATOM   3059 C  CA    . ALA A 1 390 ? 28.802 33.275 39.890  1.00 19.61 ?  388 ALA A CA    1 
ATOM   3060 C  C     . ALA A 1 390 ? 28.871 31.744 39.721  1.00 22.38 ?  388 ALA A C     1 
ATOM   3061 O  O     . ALA A 1 390 ? 29.775 31.256 39.006  1.00 19.46 ?  388 ALA A O     1 
ATOM   3062 C  CB    . ALA A 1 390 ? 29.518 33.685 41.124  1.00 20.40 ?  388 ALA A CB    1 
ATOM   3063 N  N     . ASN A 1 391 ? 27.956 30.978 40.286  1.00 20.17 ?  389 ASN A N     1 
ATOM   3064 C  CA    . ASN A 1 391 ? 28.081 29.479 40.220  1.00 21.78 ?  389 ASN A CA    1 
ATOM   3065 C  C     . ASN A 1 391 ? 27.809 29.045 38.763  1.00 21.54 ?  389 ASN A C     1 
ATOM   3066 O  O     . ASN A 1 391 ? 28.484 28.079 38.290  1.00 19.90 ?  389 ASN A O     1 
ATOM   3067 C  CB    . ASN A 1 391 ? 27.172 28.740 41.218  1.00 23.83 ?  389 ASN A CB    1 
ATOM   3068 C  CG    . ASN A 1 391 ? 25.764 28.644 40.702  1.00 30.33 ?  389 ASN A CG    1 
ATOM   3069 O  OD1   . ASN A 1 391 ? 25.319 27.584 40.251  1.00 29.26 ?  389 ASN A OD1   1 
ATOM   3070 N  ND2   . ASN A 1 391 ? 25.099 29.793 40.660  1.00 27.96 ?  389 ASN A ND2   1 
ATOM   3071 N  N     . VAL A 1 392 ? 26.928 29.701 38.039  1.00 19.64 ?  390 VAL A N     1 
ATOM   3072 C  CA    . VAL A 1 392 ? 26.646 29.441 36.612  1.00 18.34 ?  390 VAL A CA    1 
ATOM   3073 C  C     . VAL A 1 392 ? 27.898 29.773 35.798  1.00 18.32 ?  390 VAL A C     1 
ATOM   3074 O  O     . VAL A 1 392 ? 28.306 28.961 34.931  1.00 18.90 ?  390 VAL A O     1 
ATOM   3075 C  CB    . VAL A 1 392 ? 25.423 30.225 36.105  1.00 19.85 ?  390 VAL A CB    1 
ATOM   3076 C  CG1   . VAL A 1 392 ? 25.274 30.163 34.615  1.00 20.76 ?  390 VAL A CG1   1 
ATOM   3077 C  CG2   . VAL A 1 392 ? 24.185 29.698 36.821  1.00 22.47 ?  390 VAL A CG2   1 
ATOM   3078 N  N     . ASP A 1 393 ? 28.526 30.908 36.055  1.00 17.54 ?  391 ASP A N     1 
ATOM   3079 C  CA    . ASP A 1 393 ? 29.749 31.274 35.361  1.00 17.87 ?  391 ASP A CA    1 
ATOM   3080 C  C     . ASP A 1 393 ? 30.862 30.250 35.608  1.00 16.10 ?  391 ASP A C     1 
ATOM   3081 O  O     . ASP A 1 393 ? 31.562 29.869 34.670  1.00 14.67 ?  391 ASP A O     1 
ATOM   3082 C  CB    . ASP A 1 393 ? 30.136 32.703 35.725  1.00 16.37 ?  391 ASP A CB    1 
ATOM   3083 C  CG    . ASP A 1 393 ? 29.118 33.703 35.188  1.00 17.81 ?  391 ASP A CG    1 
ATOM   3084 O  OD1   . ASP A 1 393 ? 28.513 33.428 34.130  1.00 19.55 ?  391 ASP A OD1   1 
ATOM   3085 O  OD2   . ASP A 1 393 ? 28.927 34.760 35.826  1.00 20.84 ?  391 ASP A OD2   1 
ATOM   3086 N  N     . PHE A 1 394 ? 31.014 29.804 36.857  1.00 14.45 ?  392 PHE A N     1 
ATOM   3087 C  CA    . PHE A 1 394 ? 32.011 28.759 37.199  1.00 13.61 ?  392 PHE A CA    1 
ATOM   3088 C  C     . PHE A 1 394 ? 31.739 27.570 36.307  1.00 14.16 ?  392 PHE A C     1 
ATOM   3089 O  O     . PHE A 1 394 ? 32.660 27.030 35.639  1.00 13.33 ?  392 PHE A O     1 
ATOM   3090 C  CB    . PHE A 1 394 ? 31.939 28.405 38.693  1.00 13.48 ?  392 PHE A CB    1 
ATOM   3091 C  CG    . PHE A 1 394 ? 32.835 27.279 39.059  1.00 13.28 ?  392 PHE A CG    1 
ATOM   3092 C  CD1   . PHE A 1 394 ? 34.183 27.467 39.257  1.00 13.70 ?  392 PHE A CD1   1 
ATOM   3093 C  CD2   . PHE A 1 394 ? 32.332 25.984 39.148  1.00 15.13 ?  392 PHE A CD2   1 
ATOM   3094 C  CE1   . PHE A 1 394 ? 35.013 26.396 39.558  1.00 13.60 ?  392 PHE A CE1   1 
ATOM   3095 C  CE2   . PHE A 1 394 ? 33.156 24.928 39.513  1.00 14.23 ?  392 PHE A CE2   1 
ATOM   3096 C  CZ    . PHE A 1 394 ? 34.489 25.125 39.700  1.00 14.46 ?  392 PHE A CZ    1 
ATOM   3097 N  N     . VAL A 1 395 ? 30.514 27.075 36.270  1.00 13.51 ?  393 VAL A N     1 
ATOM   3098 C  CA    . VAL A 1 395 ? 30.231 25.841 35.510  1.00 12.72 ?  393 VAL A CA    1 
ATOM   3099 C  C     . VAL A 1 395 ? 30.399 26.091 34.010  1.00 13.15 ?  393 VAL A C     1 
ATOM   3100 O  O     . VAL A 1 395 ? 30.984 25.249 33.292  1.00 13.55 ?  393 VAL A O     1 
ATOM   3101 C  CB    . VAL A 1 395 ? 28.888 25.240 35.874  1.00 13.62 ?  393 VAL A CB    1 
ATOM   3102 C  CG1   . VAL A 1 395 ? 28.622 24.022 35.040  1.00 14.59 ?  393 VAL A CG1   1 
ATOM   3103 C  CG2   . VAL A 1 395 ? 28.890 24.875 37.336  1.00 15.17 ?  393 VAL A CG2   1 
ATOM   3104 N  N     . THR A 1 396 ? 30.001 27.245 33.463  1.00 12.79 ?  394 THR A N     1 
ATOM   3105 C  CA    . THR A 1 396 ? 30.252 27.583 32.057  1.00 11.99 ?  394 THR A CA    1 
ATOM   3106 C  C     . THR A 1 396 ? 31.768 27.437 31.796  1.00 11.86 ?  394 THR A C     1 
ATOM   3107 O  O     . THR A 1 396 ? 32.164 26.747 30.794  1.00 11.98 ?  394 THR A O     1 
ATOM   3108 C  CB    . THR A 1 396 ? 29.831 29.008 31.716  1.00 13.06 ?  394 THR A CB    1 
ATOM   3109 O  OG1   . THR A 1 396 ? 28.396 29.065 31.902  1.00 15.83 ?  394 THR A OG1   1 
ATOM   3110 C  CG2   . THR A 1 396 ? 30.134 29.341 30.289  1.00 14.11 ?  394 THR A CG2   1 
ATOM   3111 N  N     . LEU A 1 397 ? 32.579 28.071 32.589  1.00 11.90 ?  395 LEU A N     1 
ATOM   3112 C  CA    . LEU A 1 397 ? 34.038 28.115 32.319  1.00 11.10 ?  395 LEU A CA    1 
ATOM   3113 C  C     . LEU A 1 397 ? 34.611 26.689 32.408  1.00 11.12 ?  395 LEU A C     1 
ATOM   3114 O  O     . LEU A 1 397 ? 35.324 26.280 31.469  1.00 10.98 ?  395 LEU A O     1 
ATOM   3115 C  CB    . LEU A 1 397 ? 34.646 29.117 33.295  1.00 11.78 ?  395 LEU A CB    1 
ATOM   3116 C  CG    . LEU A 1 397 ? 36.135 29.390 33.119  1.00 12.56 ?  395 LEU A CG    1 
ATOM   3117 C  CD1   . LEU A 1 397 ? 36.535 29.773 31.703  1.00 15.51 ?  395 LEU A CD1   1 
ATOM   3118 C  CD2   . LEU A 1 397 ? 36.554 30.453 34.106  1.00 14.05 ?  395 LEU A CD2   1 
ATOM   3119 N  N     . VAL A 1 398 ? 34.377 25.989 33.511  1.00 11.46 ?  396 VAL A N     1 
ATOM   3120 C  CA    . VAL A 1 398 ? 35.027 24.658 33.707  1.00 10.61 ?  396 VAL A CA    1 
ATOM   3121 C  C     . VAL A 1 398 ? 34.349 23.611 32.870  1.00 11.88 ?  396 VAL A C     1 
ATOM   3122 O  O     . VAL A 1 398 ? 34.885 22.510 32.820  1.00 11.95 ?  396 VAL A O     1 
ATOM   3123 C  CB    . VAL A 1 398 ? 35.124 24.281 35.191  1.00 10.99 ?  396 VAL A CB    1 
ATOM   3124 C  CG1   . VAL A 1 398 ? 35.802 25.366 36.001  1.00 12.31 ?  396 VAL A CG1   1 
ATOM   3125 C  CG2   . VAL A 1 398 ? 33.820 23.823 35.805  1.00 12.20 ?  396 VAL A CG2   1 
ATOM   3126 N  N     . SER A 1 399 ? 33.252 23.868 32.210  1.00 10.49 ?  397 SER A N     1 
ATOM   3127 C  CA    . SER A 1 399 ? 32.663 22.980 31.210  1.00 10.34 ?  397 SER A CA    1 
ATOM   3128 C  C     . SER A 1 399 ? 33.325 23.112 29.852  1.00 9.24  ?  397 SER A C     1 
ATOM   3129 O  O     . SER A 1 399 ? 33.022 22.319 28.957  1.00 10.88 ?  397 SER A O     1 
ATOM   3130 C  CB    . SER A 1 399 ? 31.180 23.196 31.002  1.00 11.30 ?  397 SER A CB    1 
ATOM   3131 O  OG    . SER A 1 399 ? 30.417 22.913 32.204  1.00 12.97 ?  397 SER A OG    1 
ATOM   3132 N  N     . GLY A 1 400 ? 34.197 24.100 29.663  1.00 9.62  ?  398 GLY A N     1 
ATOM   3133 C  CA    . GLY A 1 400 ? 34.786 24.387 28.361  1.00 11.06 ?  398 GLY A CA    1 
ATOM   3134 C  C     . GLY A 1 400 ? 33.769 24.882 27.368  1.00 10.29 ?  398 GLY A C     1 
ATOM   3135 O  O     . GLY A 1 400 ? 33.881 24.635 26.173  1.00 10.76 ?  398 GLY A O     1 
ATOM   3136 N  N     . LEU A 1 401 ? 32.818 25.662 27.875  1.00 11.42 ?  399 LEU A N     1 
ATOM   3137 C  CA    . LEU A 1 401 ? 31.843 26.321 27.014  1.00 11.78 ?  399 LEU A CA    1 
ATOM   3138 C  C     . LEU A 1 401 ? 32.161 27.808 27.029  1.00 12.99 ?  399 LEU A C     1 
ATOM   3139 O  O     . LEU A 1 401 ? 32.889 28.310 27.861  1.00 13.09 ?  399 LEU A O     1 
ATOM   3140 C  CB    . LEU A 1 401 ? 30.455 26.068 27.570  1.00 13.57 ?  399 LEU A CB    1 
ATOM   3141 C  CG    . LEU A 1 401 ? 30.042 24.601 27.634  1.00 13.75 ?  399 LEU A CG    1 
ATOM   3142 C  CD1   . LEU A 1 401 ? 28.722 24.490 28.422  1.00 15.57 ?  399 LEU A CD1   1 
ATOM   3143 C  CD2   . LEU A 1 401 ? 29.904 24.055 26.228  1.00 14.67 ?  399 LEU A CD2   1 
ATOM   3144 N  N     . ALA A 1 402 ? 31.664 28.521 26.040  1.00 15.65 ?  400 ALA A N     1 
ATOM   3145 C  CA    . ALA A 1 402 ? 31.835 29.959 25.963  1.00 15.95 ?  400 ALA A CA    1 
ATOM   3146 C  C     . ALA A 1 402 ? 30.648 30.529 25.214  1.00 17.82 ?  400 ALA A C     1 
ATOM   3147 O  O     . ALA A 1 402 ? 30.359 30.133 24.127  1.00 18.50 ?  400 ALA A O     1 
ATOM   3148 C  CB    . ALA A 1 402 ? 33.101 30.327 25.250  1.00 17.78 ?  400 ALA A CB    1 
ATOM   3149 N  N     . ARG A 1 403 ? 29.989 31.476 25.854  1.00 18.82 ?  401 ARG A N     1 
ATOM   3150 C  CA    . ARG A 1 403 ? 28.820 32.078 25.250  1.00 23.13 ?  401 ARG A CA    1 
ATOM   3151 C  C     . ARG A 1 403 ? 29.162 32.807 24.005  1.00 22.45 ?  401 ARG A C     1 
ATOM   3152 O  O     . ARG A 1 403 ? 30.024 33.620 23.993  1.00 22.55 ?  401 ARG A O     1 
ATOM   3153 C  CB    . ARG A 1 403 ? 28.212 33.074 26.186  1.00 24.93 ?  401 ARG A CB    1 
ATOM   3154 C  CG    . ARG A 1 403 ? 27.578 32.385 27.315  1.00 29.40 ?  401 ARG A CG    1 
ATOM   3155 C  CD    . ARG A 1 403 ? 26.614 33.275 28.050  1.00 30.22 ?  401 ARG A CD    1 
ATOM   3156 N  NE    . ARG A 1 403 ? 26.413 32.602 29.303  1.00 30.49 ?  401 ARG A NE    1 
ATOM   3157 C  CZ    . ARG A 1 403 ? 25.407 31.823 29.592  1.00 30.58 ?  401 ARG A CZ    1 
ATOM   3158 N  NH1   . ARG A 1 403 ? 24.460 31.598 28.692  1.00 29.22 ?  401 ARG A NH1   1 
ATOM   3159 N  NH2   . ARG A 1 403 ? 25.327 31.255 30.787  1.00 28.46 ?  401 ARG A NH2   1 
ATOM   3160 N  N     . GLY A 1 404 ? 28.427 32.539 22.959  1.00 23.24 ?  402 GLY A N     1 
ATOM   3161 C  CA    . GLY A 1 404 ? 28.647 33.178 21.687  1.00 24.64 ?  402 GLY A CA    1 
ATOM   3162 C  C     . GLY A 1 404 ? 29.673 32.523 20.803  1.00 28.91 ?  402 GLY A C     1 
ATOM   3163 O  O     . GLY A 1 404 ? 29.906 32.946 19.719  1.00 28.60 ?  402 GLY A O     1 
ATOM   3164 N  N     . ASP A 1 405 ? 30.310 31.480 21.323  1.00 25.28 ?  403 ASP A N     1 
ATOM   3165 C  CA    . ASP A 1 405 ? 31.316 30.721 20.546  1.00 23.70 ?  403 ASP A CA    1 
ATOM   3166 C  C     . ASP A 1 405 ? 30.534 29.627 19.818  1.00 24.75 ?  403 ASP A C     1 
ATOM   3167 O  O     . ASP A 1 405 ? 29.984 28.753 20.483  1.00 27.16 ?  403 ASP A O     1 
ATOM   3168 C  CB    . ASP A 1 405 ? 32.385 30.221 21.508  1.00 23.52 ?  403 ASP A CB    1 
ATOM   3169 C  CG    . ASP A 1 405 ? 33.532 29.486 20.830  1.00 26.29 ?  403 ASP A CG    1 
ATOM   3170 O  OD1   . ASP A 1 405 ? 33.274 28.807 19.807  1.00 27.49 ?  403 ASP A OD1   1 
ATOM   3171 O  OD2   . ASP A 1 405 ? 34.683 29.673 21.261  1.00 21.58 ?  403 ASP A OD2   1 
ATOM   3172 N  N     . ASP A 1 406 ? 30.518 29.665 18.499  1.00 25.76 ?  404 ASP A N     1 
ATOM   3173 C  CA    . ASP A 1 406 ? 29.742 28.727 17.659  1.00 31.46 ?  404 ASP A CA    1 
ATOM   3174 C  C     . ASP A 1 406 ? 30.251 27.295 17.850  1.00 28.78 ?  404 ASP A C     1 
ATOM   3175 O  O     . ASP A 1 406 ? 29.499 26.394 17.483  1.00 29.66 ?  404 ASP A O     1 
ATOM   3176 C  CB    . ASP A 1 406 ? 29.844 29.085 16.172  1.00 36.95 ?  404 ASP A CB    1 
ATOM   3177 C  CG    . ASP A 1 406 ? 28.898 30.183 15.716  1.00 45.95 ?  404 ASP A CG    1 
ATOM   3178 O  OD1   . ASP A 1 406 ? 28.185 30.767 16.569  1.00 47.82 ?  404 ASP A OD1   1 
ATOM   3179 O  OD2   . ASP A 1 406 ? 28.884 30.440 14.513  1.00 50.43 ?  404 ASP A OD2   1 
ATOM   3180 N  N     . ALA A 1 407 ? 31.469 27.068 18.377  1.00 21.09 ?  405 ALA A N     1 
ATOM   3181 C  CA    . ALA A 1 407 ? 31.976 25.676 18.471  1.00 17.77 ?  405 ALA A CA    1 
ATOM   3182 C  C     . ALA A 1 407 ? 31.624 25.074 19.828  1.00 17.08 ?  405 ALA A C     1 
ATOM   3183 O  O     . ALA A 1 407 ? 31.628 23.823 19.942  1.00 19.33 ?  405 ALA A O     1 
ATOM   3184 C  CB    . ALA A 1 407 ? 33.476 25.614 18.259  1.00 20.18 ?  405 ALA A CB    1 
ATOM   3185 N  N     . VAL A 1 408 ? 31.474 25.899 20.857  1.00 17.22 ?  406 VAL A N     1 
ATOM   3186 C  CA    . VAL A 1 408 ? 31.284 25.444 22.268  1.00 16.40 ?  406 VAL A CA    1 
ATOM   3187 C  C     . VAL A 1 408 ? 30.278 26.339 22.985  1.00 15.88 ?  406 VAL A C     1 
ATOM   3188 O  O     . VAL A 1 408 ? 30.466 26.702 24.135  1.00 14.87 ?  406 VAL A O     1 
ATOM   3189 C  CB    . VAL A 1 408 ? 32.597 25.388 23.061  1.00 14.78 ?  406 VAL A CB    1 
ATOM   3190 C  CG1   . VAL A 1 408 ? 33.533 24.268 22.605  1.00 16.07 ?  406 VAL A CG1   1 
ATOM   3191 C  CG2   . VAL A 1 408 ? 33.326 26.728 22.975  1.00 16.09 ?  406 VAL A CG2   1 
ATOM   3192 N  N     . ASP A 1 409 ? 29.221 26.716 22.264  1.00 18.67 ?  407 ASP A N     1 
ATOM   3193 C  CA    . ASP A 1 409 ? 28.250 27.669 22.817  1.00 19.62 ?  407 ASP A CA    1 
ATOM   3194 C  C     . ASP A 1 409 ? 27.555 27.049 24.026  1.00 19.27 ?  407 ASP A C     1 
ATOM   3195 O  O     . ASP A 1 409 ? 27.352 25.832 24.109  1.00 19.83 ?  407 ASP A O     1 
ATOM   3196 C  CB    . ASP A 1 409 ? 27.259 28.099 21.739  1.00 20.45 ?  407 ASP A CB    1 
ATOM   3197 C  CG    . ASP A 1 409 ? 26.667 29.478 21.978  1.00 25.32 ?  407 ASP A CG    1 
ATOM   3198 O  OD1   . ASP A 1 409 ? 26.914 30.125 23.056  1.00 21.42 ?  407 ASP A OD1   1 
ATOM   3199 O  OD2   . ASP A 1 409 ? 26.039 29.938 21.025  1.00 31.60 ?  407 ASP A OD2   1 
ATOM   3200 N  N     . VAL A 1 410 ? 27.116 27.919 24.921  1.00 20.94 ?  408 VAL A N     1 
ATOM   3201 C  CA    . VAL A 1 410 ? 26.252 27.516 26.056  1.00 20.74 ?  408 VAL A CA    1 
ATOM   3202 C  C     . VAL A 1 410 ? 24.881 27.227 25.460  1.00 23.47 ?  408 VAL A C     1 
ATOM   3203 O  O     . VAL A 1 410 ? 24.324 28.081 24.766  1.00 26.32 ?  408 VAL A O     1 
ATOM   3204 C  CB    . VAL A 1 410 ? 26.221 28.628 27.107  1.00 20.37 ?  408 VAL A CB    1 
ATOM   3205 C  CG1   . VAL A 1 410 ? 25.318 28.274 28.286  1.00 21.74 ?  408 VAL A CG1   1 
ATOM   3206 C  CG2   . VAL A 1 410 ? 27.634 28.965 27.603  1.00 20.84 ?  408 VAL A CG2   1 
ATOM   3207 N  N     . PRO A 1 411 ? 24.297 26.041 25.689  1.00 26.98 ?  409 PRO A N     1 
ATOM   3208 C  CA    . PRO A 1 411 ? 23.013 25.729 25.060  1.00 29.46 ?  409 PRO A CA    1 
ATOM   3209 C  C     . PRO A 1 411 ? 21.837 26.397 25.794  1.00 29.16 ?  409 PRO A C     1 
ATOM   3210 O  O     . PRO A 1 411 ? 22.041 27.087 26.770  1.00 26.99 ?  409 PRO A O     1 
ATOM   3211 C  CB    . PRO A 1 411 ? 23.035 24.195 25.092  1.00 31.99 ?  409 PRO A CB    1 
ATOM   3212 C  CG    . PRO A 1 411 ? 23.812 23.849 26.338  1.00 30.81 ?  409 PRO A CG    1 
ATOM   3213 C  CD    . PRO A 1 411 ? 24.891 24.905 26.432  1.00 25.71 ?  409 PRO A CD    1 
HETATM 3214 P  PA    . FAD B 2 .   ? 47.187 14.151 20.903  1.00 7.26  ?  501 FAD A PA    1 
HETATM 3215 O  O1A   . FAD B 2 .   ? 45.847 13.687 21.424  1.00 7.10  -1 501 FAD A O1A   1 
HETATM 3216 O  O2A   . FAD B 2 .   ? 48.435 13.912 21.718  1.00 7.79  ?  501 FAD A O2A   1 
HETATM 3217 O  O5B   . FAD B 2 .   ? 47.408 13.509 19.443  1.00 6.57  ?  501 FAD A O5B   1 
HETATM 3218 C  C5B   . FAD B 2 .   ? 48.482 13.944 18.613  1.00 6.99  ?  501 FAD A C5B   1 
HETATM 3219 C  C4B   . FAD B 2 .   ? 48.839 12.833 17.616  1.00 6.93  ?  501 FAD A C4B   1 
HETATM 3220 O  O4B   . FAD B 2 .   ? 49.887 13.239 16.713  1.00 7.46  ?  501 FAD A O4B   1 
HETATM 3221 C  C3B   . FAD B 2 .   ? 49.319 11.540 18.287  1.00 7.53  ?  501 FAD A C3B   1 
HETATM 3222 O  O3B   . FAD B 2 .   ? 48.428 10.438 17.998  1.00 7.68  ?  501 FAD A O3B   1 
HETATM 3223 C  C2B   . FAD B 2 .   ? 50.714 11.326 17.708  1.00 7.15  ?  501 FAD A C2B   1 
HETATM 3224 O  O2B   . FAD B 2 .   ? 51.043 9.957  17.467  1.00 9.14  ?  501 FAD A O2B   1 
HETATM 3225 C  C1B   . FAD B 2 .   ? 50.636 12.078 16.397  1.00 7.75  ?  501 FAD A C1B   1 
HETATM 3226 N  N9A   . FAD B 2 .   ? 51.908 12.606 15.899  1.00 7.32  ?  501 FAD A N9A   1 
HETATM 3227 C  C8A   . FAD B 2 .   ? 52.789 13.332 16.574  1.00 8.04  ?  501 FAD A C8A   1 
HETATM 3228 N  N7A   . FAD B 2 .   ? 53.851 13.705 15.830  1.00 8.50  ?  501 FAD A N7A   1 
HETATM 3229 C  C5A   . FAD B 2 .   ? 53.612 13.200 14.618  1.00 7.17  ?  501 FAD A C5A   1 
HETATM 3230 C  C6A   . FAD B 2 .   ? 54.276 13.181 13.323  1.00 8.37  ?  501 FAD A C6A   1 
HETATM 3231 N  N6A   . FAD B 2 .   ? 55.434 13.799 13.194  1.00 10.18 ?  501 FAD A N6A   1 
HETATM 3232 N  N1A   . FAD B 2 .   ? 53.708 12.554 12.291  1.00 7.88  ?  501 FAD A N1A   1 
HETATM 3233 C  C2A   . FAD B 2 .   ? 52.546 11.922 12.402  1.00 7.44  ?  501 FAD A C2A   1 
HETATM 3234 N  N3A   . FAD B 2 .   ? 51.901 11.900 13.565  1.00 7.25  ?  501 FAD A N3A   1 
HETATM 3235 C  C4A   . FAD B 2 .   ? 52.344 12.499 14.667  1.00 7.44  ?  501 FAD A C4A   1 
HETATM 3236 N  N1    . FAD B 2 .   ? 42.753 16.496 28.729  1.00 7.00  ?  501 FAD A N1    1 
HETATM 3237 C  C2    . FAD B 2 .   ? 41.449 16.325 29.066  1.00 7.89  ?  501 FAD A C2    1 
HETATM 3238 O  O2    . FAD B 2 .   ? 40.569 16.769 28.298  1.00 8.68  ?  501 FAD A O2    1 
HETATM 3239 N  N3    . FAD B 2 .   ? 41.066 15.698 30.192  1.00 7.34  ?  501 FAD A N3    1 
HETATM 3240 C  C4    . FAD B 2 .   ? 41.947 15.195 31.066  1.00 7.87  ?  501 FAD A C4    1 
HETATM 3241 O  O4    . FAD B 2 .   ? 41.559 14.617 32.104  1.00 9.57  ?  501 FAD A O4    1 
HETATM 3242 C  C4X   . FAD B 2 .   ? 43.393 15.340 30.773  1.00 7.17  ?  501 FAD A C4X   1 
HETATM 3243 N  N5    . FAD B 2 .   ? 44.346 14.860 31.603  1.00 7.94  ?  501 FAD A N5    1 
HETATM 3244 C  C5X   . FAD B 2 .   ? 45.658 15.008 31.308  1.00 6.97  ?  501 FAD A C5X   1 
HETATM 3245 C  C6    . FAD B 2 .   ? 46.621 14.506 32.176  1.00 7.40  ?  501 FAD A C6    1 
HETATM 3246 C  C7    . FAD B 2 .   ? 47.971 14.653 31.881  1.00 8.14  ?  501 FAD A C7    1 
HETATM 3247 C  C7M   . FAD B 2 .   ? 49.011 14.109 32.824  1.00 9.10  ?  501 FAD A C7M   1 
HETATM 3248 C  C8    . FAD B 2 .   ? 48.390 15.348 30.634  1.00 8.10  ?  501 FAD A C8    1 
HETATM 3249 C  C8M   . FAD B 2 .   ? 49.854 15.506 30.316  1.00 9.25  ?  501 FAD A C8M   1 
HETATM 3250 C  C9    . FAD B 2 .   ? 47.431 15.850 29.763  1.00 7.57  ?  501 FAD A C9    1 
HETATM 3251 C  C9A   . FAD B 2 .   ? 46.081 15.703 30.058  1.00 6.73  ?  501 FAD A C9A   1 
HETATM 3252 N  N10   . FAD B 2 .   ? 45.103 16.210 29.181  1.00 7.15  ?  501 FAD A N10   1 
HETATM 3253 C  C10   . FAD B 2 .   ? 43.748 16.039 29.518  1.00 7.10  ?  501 FAD A C10   1 
HETATM 3254 C  "C1'" . FAD B 2 .   ? 45.487 16.898 27.946  1.00 7.45  ?  501 FAD A "C1'" 1 
HETATM 3255 C  "C2'" . FAD B 2 .   ? 45.155 16.014 26.749  1.00 6.96  ?  501 FAD A "C2'" 1 
HETATM 3256 O  "O2'" . FAD B 2 .   ? 45.792 14.741 26.906  1.00 9.04  ?  501 FAD A "O2'" 1 
HETATM 3257 C  "C3'" . FAD B 2 .   ? 45.621 16.660 25.450  1.00 7.26  ?  501 FAD A "C3'" 1 
HETATM 3258 O  "O3'" . FAD B 2 .   ? 45.286 18.052 25.463  1.00 7.75  ?  501 FAD A "O3'" 1 
HETATM 3259 C  "C4'" . FAD B 2 .   ? 44.971 15.991 24.244  1.00 8.22  ?  501 FAD A "C4'" 1 
HETATM 3260 O  "O4'" . FAD B 2 .   ? 45.585 14.718 24.015  1.00 8.42  ?  501 FAD A "O4'" 1 
HETATM 3261 C  "C5'" . FAD B 2 .   ? 45.113 16.857 22.997  1.00 8.56  ?  501 FAD A "C5'" 1 
HETATM 3262 O  "O5'" . FAD B 2 .   ? 44.928 16.053 21.835  1.00 7.05  ?  501 FAD A "O5'" 1 
HETATM 3263 P  P     . FAD B 2 .   ? 45.649 16.441 20.448  1.00 7.35  ?  501 FAD A P     1 
HETATM 3264 O  O1P   . FAD B 2 .   ? 44.896 15.775 19.321  1.00 7.51  -1 501 FAD A O1P   1 
HETATM 3265 O  O2P   . FAD B 2 .   ? 45.865 17.935 20.431  1.00 7.30  ?  501 FAD A O2P   1 
HETATM 3266 O  O3P   . FAD B 2 .   ? 47.085 15.726 20.585  1.00 7.07  ?  501 FAD A O3P   1 
HETATM 3267 CL CL    . CL  C 3 .   ? 43.810 19.177 30.558  1.00 11.49 ?  502 CL  A CL    1 
HETATM 3268 O  O     . HOH D 4 .   ? 58.787 32.794 18.983  1.00 19.67 ?  601 HOH A O     1 
HETATM 3269 O  O     . HOH D 4 .   ? 38.193 13.621 52.869  1.00 35.20 ?  602 HOH A O     1 
HETATM 3270 O  O     . HOH D 4 .   ? 54.343 36.485 21.228  1.00 29.79 ?  603 HOH A O     1 
HETATM 3271 O  O     . HOH D 4 .   ? 31.970 20.336 8.495   1.00 27.17 ?  604 HOH A O     1 
HETATM 3272 O  O     . HOH D 4 .   ? 45.446 1.969  8.520   1.00 19.62 ?  605 HOH A O     1 
HETATM 3273 O  O     . HOH D 4 .   ? 61.019 32.324 18.249  1.00 17.82 ?  606 HOH A O     1 
HETATM 3274 O  O     . HOH D 4 .   ? 43.751 40.069 8.672   1.00 19.68 ?  607 HOH A O     1 
HETATM 3275 O  O     . HOH D 4 .   ? 59.172 6.190  9.786   1.00 29.77 ?  608 HOH A O     1 
HETATM 3276 O  O     . HOH D 4 .   ? 64.605 24.000 45.299  1.00 23.83 ?  609 HOH A O     1 
HETATM 3277 O  O     . HOH D 4 .   ? 60.987 28.956 23.607  1.00 16.16 ?  610 HOH A O     1 
HETATM 3278 O  O     . HOH D 4 .   ? 48.888 17.626 27.193  1.00 11.38 ?  611 HOH A O     1 
HETATM 3279 O  O     . HOH D 4 .   ? 57.450 34.694 20.649  1.00 23.67 ?  612 HOH A O     1 
HETATM 3280 O  O     . HOH D 4 .   ? 35.891 0.773  23.893  1.00 33.96 ?  613 HOH A O     1 
HETATM 3281 O  O     . HOH D 4 .   ? 52.138 6.676  1.300   1.00 21.44 ?  614 HOH A O     1 
HETATM 3282 O  O     . HOH D 4 .   ? 32.729 38.339 39.939  1.00 31.95 ?  615 HOH A O     1 
HETATM 3283 O  O     . HOH D 4 .   ? 55.297 37.540 18.486  1.00 31.00 ?  616 HOH A O     1 
HETATM 3284 O  O     . HOH D 4 .   ? 61.337 28.188 1.017   1.00 32.74 ?  617 HOH A O     1 
HETATM 3285 O  O     . HOH D 4 .   ? 55.663 31.230 8.020   1.00 13.34 ?  618 HOH A O     1 
HETATM 3286 O  O     . HOH D 4 .   ? 45.295 36.569 18.262  1.00 15.44 ?  619 HOH A O     1 
HETATM 3287 O  O     . HOH D 4 .   ? 42.771 22.139 32.224  1.00 16.27 ?  620 HOH A O     1 
HETATM 3288 O  O     . HOH D 4 .   ? 46.664 32.644 12.855  1.00 13.44 ?  621 HOH A O     1 
HETATM 3289 O  O     . HOH D 4 .   ? 57.330 11.014 -3.011  1.00 18.56 ?  622 HOH A O     1 
HETATM 3290 O  O     . HOH D 4 .   ? 50.706 8.345  19.491  1.00 21.58 ?  623 HOH A O     1 
HETATM 3291 O  O     . HOH D 4 .   ? 61.960 20.796 10.380  1.00 29.87 ?  624 HOH A O     1 
HETATM 3292 O  O     . HOH D 4 .   ? 32.534 -5.461 38.102  1.00 25.96 ?  625 HOH A O     1 
HETATM 3293 O  O     . HOH D 4 .   ? 34.551 -2.656 34.962  1.00 25.96 ?  626 HOH A O     1 
HETATM 3294 O  O     . HOH D 4 .   ? 63.255 13.708 43.372  1.00 25.47 ?  627 HOH A O     1 
HETATM 3295 O  O     . HOH D 4 .   ? 34.850 5.078  30.250  1.00 11.66 ?  628 HOH A O     1 
HETATM 3296 O  O     . HOH D 4 .   ? 60.660 30.908 28.520  1.00 12.29 ?  629 HOH A O     1 
HETATM 3297 O  O     . HOH D 4 .   ? 38.269 36.404 6.528   1.00 32.14 ?  630 HOH A O     1 
HETATM 3298 O  O     . HOH D 4 .   ? 25.552 5.176  40.277  1.00 28.66 ?  631 HOH A O     1 
HETATM 3299 O  O     . HOH D 4 .   ? 35.286 37.639 24.190  1.00 31.83 ?  632 HOH A O     1 
HETATM 3300 O  O     . HOH D 4 .   ? 29.162 11.779 37.454  1.00 12.43 ?  633 HOH A O     1 
HETATM 3301 O  O     . HOH D 4 .   ? 58.569 33.355 14.973  1.00 32.42 ?  634 HOH A O     1 
HETATM 3302 O  O     . HOH D 4 .   ? 57.051 5.949  35.458  1.00 25.09 ?  635 HOH A O     1 
HETATM 3303 O  O     . HOH D 4 .   ? 44.791 23.554 22.702  1.00 9.22  ?  636 HOH A O     1 
HETATM 3304 O  O     . HOH D 4 .   ? 42.276 -5.334 36.906  1.00 15.16 ?  637 HOH A O     1 
HETATM 3305 O  O     . HOH D 4 .   ? 31.744 13.846 45.617  1.00 22.88 ?  638 HOH A O     1 
HETATM 3306 O  O     . HOH D 4 .   ? 56.563 4.445  1.729   1.00 31.38 ?  639 HOH A O     1 
HETATM 3307 O  O     . HOH D 4 .   ? 47.986 33.184 8.475   1.00 21.31 ?  640 HOH A O     1 
HETATM 3308 O  O     . HOH D 4 .   ? 23.961 22.047 30.723  1.00 20.94 ?  641 HOH A O     1 
HETATM 3309 O  O     . HOH D 4 .   ? 56.084 -0.867 6.225   1.00 13.48 ?  642 HOH A O     1 
HETATM 3310 O  O     . HOH D 4 .   ? 43.896 28.770 0.583   1.00 19.48 ?  643 HOH A O     1 
HETATM 3311 O  O     . HOH D 4 .   ? 64.486 11.216 1.961   1.00 36.26 ?  644 HOH A O     1 
HETATM 3312 O  O     . HOH D 4 .   ? 55.139 17.076 45.570  1.00 13.81 ?  645 HOH A O     1 
HETATM 3313 O  O     . HOH D 4 .   ? 55.201 34.978 4.633   1.00 11.45 ?  646 HOH A O     1 
HETATM 3314 O  O     . HOH D 4 .   ? 51.157 30.148 38.256  1.00 33.10 ?  647 HOH A O     1 
HETATM 3315 O  O     . HOH D 4 .   ? 20.803 10.745 27.871  1.00 31.46 ?  648 HOH A O     1 
HETATM 3316 O  O     . HOH D 4 .   ? 23.865 14.683 18.298  1.00 25.20 ?  649 HOH A O     1 
HETATM 3317 O  O     . HOH D 4 .   ? 45.618 15.232 16.827  1.00 8.08  ?  650 HOH A O     1 
HETATM 3318 O  O     . HOH D 4 .   ? 27.935 3.971  42.801  1.00 30.55 ?  651 HOH A O     1 
HETATM 3319 O  O     . HOH D 4 .   ? 50.316 3.181  44.034  1.00 14.92 ?  652 HOH A O     1 
HETATM 3320 O  O     . HOH D 4 .   ? 50.965 -1.510 30.440  1.00 18.08 ?  653 HOH A O     1 
HETATM 3321 O  O     . HOH D 4 .   ? 47.650 18.996 18.384  1.00 7.12  ?  654 HOH A O     1 
HETATM 3322 O  O     . HOH D 4 .   ? 58.109 18.889 27.033  1.00 17.26 ?  655 HOH A O     1 
HETATM 3323 O  O     . HOH D 4 .   ? 47.612 27.966 0.964   1.00 16.46 ?  656 HOH A O     1 
HETATM 3324 O  O     . HOH D 4 .   ? 50.912 12.651 21.396  1.00 17.32 ?  657 HOH A O     1 
HETATM 3325 O  O     . HOH D 4 .   ? 43.513 1.682  13.282  1.00 14.70 ?  658 HOH A O     1 
HETATM 3326 O  O     . HOH D 4 .   ? 54.758 28.583 39.669  1.00 27.23 ?  659 HOH A O     1 
HETATM 3327 O  O     . HOH D 4 .   ? 38.232 18.085 28.311  1.00 10.54 ?  660 HOH A O     1 
HETATM 3328 O  O     . HOH D 4 .   ? 44.712 34.317 37.197  1.00 23.48 ?  661 HOH A O     1 
HETATM 3329 O  O     . HOH D 4 .   ? 55.780 5.297  13.103  1.00 28.45 ?  662 HOH A O     1 
HETATM 3330 O  O     . HOH D 4 .   ? 49.914 25.752 -0.075  1.00 13.48 ?  663 HOH A O     1 
HETATM 3331 O  O     . HOH D 4 .   ? 48.067 12.820 -7.942  1.00 27.02 ?  664 HOH A O     1 
HETATM 3332 O  O     . HOH D 4 .   ? 26.381 11.049 23.942  1.00 16.14 ?  665 HOH A O     1 
HETATM 3333 O  O     . HOH D 4 .   ? 24.865 17.470 35.401  1.00 13.87 ?  666 HOH A O     1 
HETATM 3334 O  O     . HOH D 4 .   ? 39.177 1.201  40.818  1.00 9.79  ?  667 HOH A O     1 
HETATM 3335 O  O     . HOH D 4 .   ? 44.430 20.836 23.212  1.00 10.26 ?  668 HOH A O     1 
HETATM 3336 O  O     . HOH D 4 .   ? 41.668 26.506 -2.711  1.00 26.86 ?  669 HOH A O     1 
HETATM 3337 O  O     . HOH D 4 .   ? 60.450 21.016 34.708  1.00 11.17 ?  670 HOH A O     1 
HETATM 3338 O  O     . HOH D 4 .   ? 36.873 -2.598 46.448  1.00 27.90 ?  671 HOH A O     1 
HETATM 3339 O  O     . HOH D 4 .   ? 60.562 26.926 20.517  1.00 12.69 ?  672 HOH A O     1 
HETATM 3340 O  O     . HOH D 4 .   ? 56.794 6.177  10.743  1.00 20.68 ?  673 HOH A O     1 
HETATM 3341 O  O     . HOH D 4 .   ? 28.162 5.445  27.568  1.00 28.68 ?  674 HOH A O     1 
HETATM 3342 O  O     . HOH D 4 .   ? 37.381 17.555 40.028  1.00 13.14 ?  675 HOH A O     1 
HETATM 3343 O  O     . HOH D 4 .   ? 58.591 36.031 6.061   1.00 26.31 ?  676 HOH A O     1 
HETATM 3344 O  O     . HOH D 4 .   ? 32.985 7.617  42.006  1.00 14.44 ?  677 HOH A O     1 
HETATM 3345 O  O     . HOH D 4 .   ? 32.137 3.537  37.876  1.00 14.65 ?  678 HOH A O     1 
HETATM 3346 O  O     . HOH D 4 .   ? 41.317 10.866 17.381  1.00 9.85  ?  679 HOH A O     1 
HETATM 3347 O  O     . HOH D 4 .   ? 54.958 10.307 -4.073  1.00 27.29 ?  680 HOH A O     1 
HETATM 3348 O  O     . HOH D 4 .   ? 52.961 33.606 25.926  1.00 25.39 ?  681 HOH A O     1 
HETATM 3349 O  O     . HOH D 4 .   ? 56.378 6.147  48.698  1.00 19.01 ?  682 HOH A O     1 
HETATM 3350 O  O     . HOH D 4 .   ? 60.500 12.158 -0.179  1.00 22.52 ?  683 HOH A O     1 
HETATM 3351 O  O     . HOH D 4 .   ? 56.418 3.495  47.477  1.00 29.40 ?  684 HOH A O     1 
HETATM 3352 O  O     . HOH D 4 .   ? 57.758 17.178 22.239  1.00 18.04 ?  685 HOH A O     1 
HETATM 3353 O  O     . HOH D 4 .   ? 29.281 37.950 42.462  1.00 33.28 ?  686 HOH A O     1 
HETATM 3354 O  O     . HOH D 4 .   ? 23.223 29.552 31.094  1.00 31.67 ?  687 HOH A O     1 
HETATM 3355 O  O     . HOH D 4 .   ? 37.332 3.099  52.508  1.00 18.35 ?  688 HOH A O     1 
HETATM 3356 O  O     . HOH D 4 .   ? 28.156 8.035  13.016  1.00 27.96 ?  689 HOH A O     1 
HETATM 3357 O  O     . HOH D 4 .   ? 49.490 15.795 23.392  1.00 11.56 ?  690 HOH A O     1 
HETATM 3358 O  O     . HOH D 4 .   ? 51.775 35.771 19.811  1.00 19.35 ?  691 HOH A O     1 
HETATM 3359 O  O     . HOH D 4 .   ? 43.657 9.280  -1.098  1.00 28.45 ?  692 HOH A O     1 
HETATM 3360 O  O     . HOH D 4 .   ? 27.902 22.055 31.117  1.00 14.96 ?  693 HOH A O     1 
HETATM 3361 O  O     . HOH D 4 .   ? 43.520 6.500  28.593  1.00 8.34  ?  694 HOH A O     1 
HETATM 3362 O  O     . HOH D 4 .   ? 36.467 21.000 34.508  1.00 10.91 ?  695 HOH A O     1 
HETATM 3363 O  O     . HOH D 4 .   ? 52.671 11.734 -2.688  1.00 16.43 ?  696 HOH A O     1 
HETATM 3364 O  O     . HOH D 4 .   ? 45.039 8.746  54.504  1.00 30.13 ?  697 HOH A O     1 
HETATM 3365 O  O     . HOH D 4 .   ? 35.111 -6.916 39.226  1.00 36.71 ?  698 HOH A O     1 
HETATM 3366 O  O     . HOH D 4 .   ? 44.403 15.556 51.302  1.00 24.57 ?  699 HOH A O     1 
HETATM 3367 O  O     . HOH D 4 .   ? 46.547 -0.937 18.169  1.00 14.98 ?  700 HOH A O     1 
HETATM 3368 O  O     . HOH D 4 .   ? 50.952 5.355  23.255  1.00 26.06 ?  701 HOH A O     1 
HETATM 3369 O  O     . HOH D 4 .   ? 57.123 29.787 6.352   1.00 15.81 ?  702 HOH A O     1 
HETATM 3370 O  O     . HOH D 4 .   ? 54.469 24.954 38.625  1.00 26.85 ?  703 HOH A O     1 
HETATM 3371 O  O     . HOH D 4 .   ? 58.302 23.332 30.978  1.00 11.12 ?  704 HOH A O     1 
HETATM 3372 O  O     . HOH D 4 .   ? 61.036 4.669  7.813   1.00 33.32 ?  705 HOH A O     1 
HETATM 3373 O  O     . HOH D 4 .   ? 62.801 26.523 32.719  1.00 15.31 ?  706 HOH A O     1 
HETATM 3374 O  O     . HOH D 4 .   ? 27.676 14.786 39.329  1.00 15.65 ?  707 HOH A O     1 
HETATM 3375 O  O     . HOH D 4 .   ? 38.937 38.249 15.562  1.00 27.62 ?  708 HOH A O     1 
HETATM 3376 O  O     . HOH D 4 .   ? 27.203 15.048 21.430  1.00 15.03 ?  709 HOH A O     1 
HETATM 3377 O  O     . HOH D 4 .   ? 37.202 35.551 44.067  1.00 23.94 ?  710 HOH A O     1 
HETATM 3378 O  O     . HOH D 4 .   ? 51.934 17.507 48.365  1.00 15.32 ?  711 HOH A O     1 
HETATM 3379 O  O     . HOH D 4 .   ? 36.952 -3.319 41.295  1.00 28.86 ?  712 HOH A O     1 
HETATM 3380 O  O     . HOH D 4 .   ? 53.448 22.631 17.076  1.00 8.03  ?  713 HOH A O     1 
HETATM 3381 O  O     . HOH D 4 .   ? 36.932 2.753  19.617  1.00 18.00 ?  714 HOH A O     1 
HETATM 3382 O  O     . HOH D 4 .   ? 27.918 18.020 10.930  1.00 27.31 ?  715 HOH A O     1 
HETATM 3383 O  O     . HOH D 4 .   ? 22.285 26.870 37.915  1.00 33.04 ?  716 HOH A O     1 
HETATM 3384 O  O     . HOH D 4 .   ? 31.555 13.084 4.195   1.00 25.41 ?  717 HOH A O     1 
HETATM 3385 O  O     . HOH D 4 .   ? 63.696 24.161 11.693  1.00 35.86 ?  718 HOH A O     1 
HETATM 3386 O  O     . HOH D 4 .   ? 54.222 21.498 32.834  1.00 11.11 ?  719 HOH A O     1 
HETATM 3387 O  O     . HOH D 4 .   ? 58.108 7.497  33.480  1.00 31.31 ?  720 HOH A O     1 
HETATM 3388 O  O     . HOH D 4 .   ? 54.268 20.086 -2.576  1.00 30.22 ?  721 HOH A O     1 
HETATM 3389 O  O     . HOH D 4 .   ? 32.573 -0.212 41.508  1.00 24.41 ?  722 HOH A O     1 
HETATM 3390 O  O     . HOH D 4 .   ? 29.547 40.200 31.632  1.00 29.82 ?  723 HOH A O     1 
HETATM 3391 O  O     . HOH D 4 .   ? 37.263 -0.248 50.001  1.00 28.74 ?  724 HOH A O     1 
HETATM 3392 O  O     . HOH D 4 .   ? 35.031 9.645  41.633  1.00 16.19 ?  725 HOH A O     1 
HETATM 3393 O  O     . HOH D 4 .   ? 38.132 36.698 9.317   1.00 30.71 ?  726 HOH A O     1 
HETATM 3394 O  O     . HOH D 4 .   ? 25.390 12.126 16.573  1.00 23.14 ?  727 HOH A O     1 
HETATM 3395 O  O     . HOH D 4 .   ? 39.677 35.351 45.427  1.00 30.84 ?  728 HOH A O     1 
HETATM 3396 O  O     . HOH D 4 .   ? 41.058 11.721 1.031   1.00 18.73 ?  729 HOH A O     1 
HETATM 3397 O  O     . HOH D 4 .   ? 41.767 3.956  13.017  1.00 21.08 ?  730 HOH A O     1 
HETATM 3398 O  O     . HOH D 4 .   ? 50.490 22.995 2.864   1.00 11.61 ?  731 HOH A O     1 
HETATM 3399 O  O     . HOH D 4 .   ? 51.400 10.485 -0.534  1.00 19.24 ?  732 HOH A O     1 
HETATM 3400 O  O     . HOH D 4 .   ? 35.653 36.389 46.345  1.00 33.34 ?  733 HOH A O     1 
HETATM 3401 O  O     . HOH D 4 .   ? 56.262 4.369  32.043  1.00 30.50 ?  734 HOH A O     1 
HETATM 3402 O  O     . HOH D 4 .   ? 61.082 26.985 7.349   1.00 21.99 ?  735 HOH A O     1 
HETATM 3403 O  O     . HOH D 4 .   ? 26.269 8.363  16.849  1.00 15.86 ?  736 HOH A O     1 
HETATM 3404 O  O     . HOH D 4 .   ? 53.720 10.564 29.054  1.00 20.83 ?  737 HOH A O     1 
HETATM 3405 O  O     . HOH D 4 .   ? 38.862 0.831  47.855  1.00 13.44 ?  738 HOH A O     1 
HETATM 3406 O  O     . HOH D 4 .   ? 49.876 4.178  48.349  1.00 20.70 ?  739 HOH A O     1 
HETATM 3407 O  O     . HOH D 4 .   ? 36.740 0.163  41.199  1.00 13.03 ?  740 HOH A O     1 
HETATM 3408 O  O     . HOH D 4 .   ? 59.752 19.919 13.769  1.00 14.72 ?  741 HOH A O     1 
HETATM 3409 O  O     . HOH D 4 .   ? 28.538 30.990 44.280  1.00 29.74 ?  742 HOH A O     1 
HETATM 3410 O  O     . HOH D 4 .   ? 47.213 35.433 30.495  1.00 31.55 ?  743 HOH A O     1 
HETATM 3411 O  O     . HOH D 4 .   ? 35.466 18.491 35.230  1.00 12.36 ?  744 HOH A O     1 
HETATM 3412 O  O     . HOH D 4 .   ? 41.795 8.758  54.484  1.00 29.31 ?  745 HOH A O     1 
HETATM 3413 O  O     . HOH D 4 .   ? 36.264 29.089 12.610  1.00 24.27 ?  746 HOH A O     1 
HETATM 3414 O  O     . HOH D 4 .   ? 52.954 4.000  27.915  1.00 26.93 ?  747 HOH A O     1 
HETATM 3415 O  O     . HOH D 4 .   ? 28.647 16.606 41.114  1.00 14.83 ?  748 HOH A O     1 
HETATM 3416 O  O     . HOH D 4 .   ? 61.529 22.135 5.617   1.00 36.59 ?  749 HOH A O     1 
HETATM 3417 O  O     . HOH D 4 .   ? 34.351 2.579  10.895  1.00 29.58 ?  750 HOH A O     1 
HETATM 3418 O  O     . HOH D 4 .   ? 43.831 5.493  19.770  1.00 8.93  ?  751 HOH A O     1 
HETATM 3419 O  O     . HOH D 4 .   ? 50.190 4.378  34.171  1.00 8.69  ?  752 HOH A O     1 
HETATM 3420 O  O     . HOH D 4 .   ? 44.026 4.006  8.306   1.00 18.61 ?  753 HOH A O     1 
HETATM 3421 O  O     . HOH D 4 .   ? 54.030 13.953 39.888  1.00 15.12 ?  754 HOH A O     1 
HETATM 3422 O  O     . HOH D 4 .   ? 33.749 0.151  43.744  1.00 29.55 ?  755 HOH A O     1 
HETATM 3423 O  O     . HOH D 4 .   ? 54.931 17.250 27.608  1.00 17.17 ?  756 HOH A O     1 
HETATM 3424 O  O     . HOH D 4 .   ? 45.173 4.054  50.223  1.00 27.27 ?  757 HOH A O     1 
HETATM 3425 O  O     . HOH D 4 .   ? 46.014 36.070 15.016  1.00 14.06 ?  758 HOH A O     1 
HETATM 3426 O  O     . HOH D 4 .   ? 38.008 32.355 10.965  1.00 20.27 ?  759 HOH A O     1 
HETATM 3427 O  O     . HOH D 4 .   ? 36.617 3.771  9.436   1.00 26.01 ?  760 HOH A O     1 
HETATM 3428 O  O     . HOH D 4 .   ? 37.395 -1.451 32.694  1.00 28.72 ?  761 HOH A O     1 
HETATM 3429 O  O     . HOH D 4 .   ? 39.430 36.039 38.169  1.00 30.89 ?  762 HOH A O     1 
HETATM 3430 O  O     . HOH D 4 .   ? 35.407 27.527 28.929  1.00 12.51 ?  763 HOH A O     1 
HETATM 3431 O  O     . HOH D 4 .   ? 37.041 24.480 50.273  1.00 34.23 ?  764 HOH A O     1 
HETATM 3432 O  O     . HOH D 4 .   ? 58.696 18.915 48.129  1.00 25.72 ?  765 HOH A O     1 
HETATM 3433 O  O     . HOH D 4 .   ? 60.784 22.758 0.850   1.00 22.36 ?  766 HOH A O     1 
HETATM 3434 O  O     . HOH D 4 .   ? 60.300 8.065  36.124  1.00 32.15 ?  767 HOH A O     1 
HETATM 3435 O  O     . HOH D 4 .   ? 58.607 27.520 37.922  1.00 31.59 ?  768 HOH A O     1 
HETATM 3436 O  O     . HOH D 4 .   ? 33.242 2.146  31.157  1.00 21.99 ?  769 HOH A O     1 
HETATM 3437 O  O     . HOH D 4 .   ? 30.035 6.053  12.953  1.00 26.85 ?  770 HOH A O     1 
HETATM 3438 O  O     . HOH D 4 .   ? 50.109 32.540 27.277  1.00 29.32 ?  771 HOH A O     1 
HETATM 3439 O  O     . HOH D 4 .   ? 35.262 14.867 1.103   1.00 30.17 ?  772 HOH A O     1 
HETATM 3440 O  O     . HOH D 4 .   ? 38.716 13.708 2.288   1.00 19.63 ?  773 HOH A O     1 
HETATM 3441 O  O     . HOH D 4 .   ? 58.463 12.694 33.198  1.00 23.35 ?  774 HOH A O     1 
HETATM 3442 O  O     . HOH D 4 .   ? 38.662 18.362 36.300  1.00 13.81 ?  775 HOH A O     1 
HETATM 3443 O  O     . HOH D 4 .   ? 55.556 24.098 30.880  1.00 10.88 ?  776 HOH A O     1 
HETATM 3444 O  O     . HOH D 4 .   ? 42.653 16.437 35.867  1.00 18.02 ?  777 HOH A O     1 
HETATM 3445 O  O     . HOH D 4 .   ? 58.581 25.681 40.517  1.00 22.47 ?  778 HOH A O     1 
HETATM 3446 O  O     . HOH D 4 .   ? 31.224 5.010  14.641  1.00 22.63 ?  779 HOH A O     1 
HETATM 3447 O  O     . HOH D 4 .   ? 30.272 24.465 42.647  1.00 20.48 ?  780 HOH A O     1 
HETATM 3448 O  O     . HOH D 4 .   ? 61.109 27.517 -1.856  1.00 33.52 ?  781 HOH A O     1 
HETATM 3449 O  O     . HOH D 4 .   ? 33.419 30.915 28.916  1.00 17.53 ?  782 HOH A O     1 
HETATM 3450 O  O     . HOH D 4 .   ? 61.307 16.785 39.243  1.00 17.22 ?  783 HOH A O     1 
HETATM 3451 O  O     . HOH D 4 .   ? 41.167 18.185 37.500  1.00 15.07 ?  784 HOH A O     1 
HETATM 3452 O  O     . HOH D 4 .   ? 50.417 22.268 -2.597  1.00 27.38 ?  785 HOH A O     1 
HETATM 3453 O  O     . HOH D 4 .   ? 44.931 13.704 54.731  1.00 35.07 ?  786 HOH A O     1 
HETATM 3454 O  O     . HOH D 4 .   ? 39.470 29.079 17.342  1.00 12.93 ?  787 HOH A O     1 
HETATM 3455 O  O     . HOH D 4 .   ? 29.115 33.148 30.092  1.00 26.02 ?  788 HOH A O     1 
HETATM 3456 O  O     . HOH D 4 .   ? 33.378 2.905  15.561  1.00 28.79 ?  789 HOH A O     1 
HETATM 3457 O  O     . HOH D 4 .   ? 23.845 13.591 42.365  1.00 35.46 ?  790 HOH A O     1 
HETATM 3458 O  O     . HOH D 4 .   ? 56.598 14.545 15.863  1.00 21.76 ?  791 HOH A O     1 
HETATM 3459 O  O     . HOH D 4 .   ? 54.908 30.941 -2.797  1.00 21.03 ?  792 HOH A O     1 
HETATM 3460 O  O     . HOH D 4 .   ? 47.051 34.245 32.964  1.00 27.11 ?  793 HOH A O     1 
HETATM 3461 O  O     . HOH D 4 .   ? 54.918 34.568 14.931  1.00 21.81 ?  794 HOH A O     1 
HETATM 3462 O  O     . HOH D 4 .   ? 43.720 11.489 32.524  1.00 10.11 ?  795 HOH A O     1 
HETATM 3463 O  O     . HOH D 4 .   ? 40.307 25.594 21.110  1.00 12.38 ?  796 HOH A O     1 
HETATM 3464 O  O     . HOH D 4 .   ? 31.902 1.772  45.836  1.00 20.96 ?  797 HOH A O     1 
HETATM 3465 O  O     . HOH D 4 .   ? 50.415 8.689  24.051  1.00 17.78 ?  798 HOH A O     1 
HETATM 3466 O  O     . HOH D 4 .   ? 49.640 2.033  22.720  1.00 22.67 ?  799 HOH A O     1 
HETATM 3467 O  O     . HOH D 4 .   ? 51.691 1.755  27.180  1.00 33.39 ?  800 HOH A O     1 
HETATM 3468 O  O     . HOH D 4 .   ? 29.829 1.326  40.900  1.00 33.43 ?  801 HOH A O     1 
HETATM 3469 O  O     . HOH D 4 .   ? 31.588 -0.068 34.224  1.00 28.20 ?  802 HOH A O     1 
HETATM 3470 O  O     . HOH D 4 .   ? 33.877 5.494  14.518  1.00 24.16 ?  803 HOH A O     1 
HETATM 3471 O  O     . HOH D 4 .   ? 60.591 31.993 15.947  1.00 23.30 ?  804 HOH A O     1 
HETATM 3472 O  O     . HOH D 4 .   ? 59.630 22.299 22.005  1.00 18.93 ?  805 HOH A O     1 
HETATM 3473 O  O     . HOH D 4 .   ? 36.363 12.476 13.037  1.00 16.30 ?  806 HOH A O     1 
HETATM 3474 O  O     . HOH D 4 .   ? 45.958 31.702 -0.102  1.00 25.51 ?  807 HOH A O     1 
HETATM 3475 O  O     . HOH D 4 .   ? 63.118 20.462 18.114  1.00 21.70 ?  808 HOH A O     1 
HETATM 3476 O  O     . HOH D 4 .   ? 44.325 4.772  26.496  1.00 8.56  ?  809 HOH A O     1 
HETATM 3477 O  O     . HOH D 4 .   ? 31.159 32.554 28.290  1.00 19.29 ?  810 HOH A O     1 
HETATM 3478 O  O     . HOH D 4 .   ? 35.248 31.739 2.181   1.00 27.46 ?  811 HOH A O     1 
HETATM 3479 O  O     . HOH D 4 .   ? 44.952 -1.947 16.108  1.00 10.15 ?  812 HOH A O     1 
HETATM 3480 O  O     . HOH D 4 .   ? 43.672 -2.217 11.345  1.00 19.81 ?  813 HOH A O     1 
HETATM 3481 O  O     . HOH D 4 .   ? 27.767 5.669  32.726  1.00 18.61 ?  814 HOH A O     1 
HETATM 3482 O  O     . HOH D 4 .   ? 56.658 32.215 31.397  1.00 15.57 ?  815 HOH A O     1 
HETATM 3483 O  O     . HOH D 4 .   ? 48.987 9.245  -7.365  1.00 30.72 ?  816 HOH A O     1 
HETATM 3484 O  O     . HOH D 4 .   ? 37.211 29.616 28.125  1.00 13.37 ?  817 HOH A O     1 
HETATM 3485 O  O     . HOH D 4 .   ? 48.064 27.428 47.212  1.00 27.03 ?  818 HOH A O     1 
HETATM 3486 O  O     . HOH D 4 .   ? 43.666 13.790 34.234  1.00 16.60 ?  819 HOH A O     1 
HETATM 3487 O  O     . HOH D 4 .   ? 44.740 22.432 29.376  1.00 12.45 ?  820 HOH A O     1 
HETATM 3488 O  O     . HOH D 4 .   ? 48.292 -0.000 21.276  0.50 17.51 ?  821 HOH A O     1 
HETATM 3489 O  O     . HOH D 4 .   ? 45.448 35.780 2.439   1.00 23.93 ?  822 HOH A O     1 
HETATM 3490 O  O     . HOH D 4 .   ? 21.567 27.467 33.286  1.00 30.90 ?  823 HOH A O     1 
HETATM 3491 O  O     . HOH D 4 .   ? 57.623 9.838  30.454  1.00 26.31 ?  824 HOH A O     1 
HETATM 3492 O  O     . HOH D 4 .   ? 33.262 29.383 49.964  1.00 29.84 ?  825 HOH A O     1 
HETATM 3493 O  O     . HOH D 4 .   ? 48.902 -1.604 44.824  1.00 21.03 ?  826 HOH A O     1 
HETATM 3494 O  O     . HOH D 4 .   ? 35.107 4.553  53.316  1.00 25.79 ?  827 HOH A O     1 
HETATM 3495 O  O     . HOH D 4 .   ? 41.486 -4.711 44.880  1.00 33.84 ?  828 HOH A O     1 
HETATM 3496 O  O     . HOH D 4 .   ? 51.177 0.419  44.042  1.00 20.95 ?  829 HOH A O     1 
HETATM 3497 O  O     . HOH D 4 .   ? 56.666 25.427 37.902  1.00 34.26 ?  830 HOH A O     1 
HETATM 3498 O  O     . HOH D 4 .   ? 59.007 23.468 38.761  1.00 11.84 ?  831 HOH A O     1 
HETATM 3499 O  O     . HOH D 4 .   ? 38.958 -0.938 22.304  1.00 19.34 ?  832 HOH A O     1 
HETATM 3500 O  O     . HOH D 4 .   ? 21.412 18.376 39.700  1.00 27.69 ?  833 HOH A O     1 
HETATM 3501 O  O     . HOH D 4 .   ? 33.006 25.798 14.552  1.00 29.14 ?  834 HOH A O     1 
HETATM 3502 O  O     . HOH D 4 .   ? 49.739 34.028 5.364   1.00 17.40 ?  835 HOH A O     1 
HETATM 3503 O  O     . HOH D 4 .   ? 19.242 18.776 33.327  1.00 30.45 ?  836 HOH A O     1 
HETATM 3504 O  O     . HOH D 4 .   ? 27.002 16.720 43.201  1.00 30.18 ?  837 HOH A O     1 
HETATM 3505 O  O     . HOH D 4 .   ? 36.697 3.858  28.550  1.00 13.43 ?  838 HOH A O     1 
HETATM 3506 O  O     . HOH D 4 .   ? 23.913 11.159 24.780  1.00 27.83 ?  839 HOH A O     1 
HETATM 3507 O  O     . HOH D 4 .   ? 26.709 20.488 17.046  1.00 31.31 ?  840 HOH A O     1 
HETATM 3508 O  O     . HOH D 4 .   ? 61.798 23.052 38.351  1.00 16.25 ?  841 HOH A O     1 
HETATM 3509 O  O     . HOH D 4 .   ? 55.191 12.374 41.768  1.00 18.96 ?  842 HOH A O     1 
HETATM 3510 O  O     . HOH D 4 .   ? 29.097 21.171 47.060  1.00 26.17 ?  843 HOH A O     1 
HETATM 3511 O  O     . HOH D 4 .   ? 28.499 13.640 10.944  1.00 21.66 ?  844 HOH A O     1 
HETATM 3512 O  O     . HOH D 4 .   ? 58.039 31.493 -3.615  1.00 28.36 ?  845 HOH A O     1 
HETATM 3513 O  O     . HOH D 4 .   ? 26.393 31.860 42.669  1.00 33.11 ?  846 HOH A O     1 
HETATM 3514 O  O     . HOH D 4 .   ? 52.355 8.311  -2.505  1.00 33.80 ?  847 HOH A O     1 
HETATM 3515 O  O     . HOH D 4 .   ? 56.672 14.412 29.206  1.00 17.15 ?  848 HOH A O     1 
HETATM 3516 O  O     . HOH D 4 .   ? 48.733 15.015 26.378  1.00 13.42 ?  849 HOH A O     1 
HETATM 3517 O  O     . HOH D 4 .   ? 21.850 10.802 41.725  1.00 35.05 ?  850 HOH A O     1 
HETATM 3518 O  O     . HOH D 4 .   ? 37.101 21.149 49.864  1.00 23.01 ?  851 HOH A O     1 
HETATM 3519 O  O     . HOH D 4 .   ? 33.594 22.689 9.521   1.00 29.79 ?  852 HOH A O     1 
HETATM 3520 O  O     . HOH D 4 .   ? 47.783 32.187 5.860   1.00 18.88 ?  853 HOH A O     1 
HETATM 3521 O  O     . HOH D 4 .   ? 62.449 30.058 21.523  1.00 18.37 ?  854 HOH A O     1 
HETATM 3522 O  O     . HOH D 4 .   ? 49.914 10.017 26.612  1.00 11.72 ?  855 HOH A O     1 
HETATM 3523 O  O     . HOH D 4 .   ? 32.750 24.758 50.303  1.00 37.37 ?  856 HOH A O     1 
HETATM 3524 O  O     . HOH D 4 .   ? 62.048 7.362  45.910  1.00 16.83 ?  857 HOH A O     1 
HETATM 3525 O  O     . HOH D 4 .   ? 59.279 31.504 12.733  1.00 30.70 ?  858 HOH A O     1 
HETATM 3526 O  O     . HOH D 4 .   ? 56.022 7.226  31.295  1.00 15.90 ?  859 HOH A O     1 
HETATM 3527 O  O     . HOH D 4 .   ? 56.209 33.003 -0.346  1.00 21.13 ?  860 HOH A O     1 
HETATM 3528 O  O     . HOH D 4 .   ? 53.987 31.749 27.306  1.00 28.88 ?  861 HOH A O     1 
HETATM 3529 O  O     . HOH D 4 .   ? 60.003 19.501 10.961  1.00 24.44 ?  862 HOH A O     1 
HETATM 3530 O  O     . HOH D 4 .   ? 36.584 0.263  12.893  1.00 35.02 ?  863 HOH A O     1 
HETATM 3531 O  O     . HOH D 4 .   ? 53.251 16.333 50.833  1.00 26.20 ?  864 HOH A O     1 
HETATM 3532 O  O     . HOH D 4 .   ? 51.331 21.662 39.939  1.00 29.81 ?  865 HOH A O     1 
HETATM 3533 O  O     . HOH D 4 .   ? 34.884 25.901 50.267  1.00 31.48 ?  866 HOH A O     1 
HETATM 3534 O  O     . HOH D 4 .   ? 47.955 32.945 2.643   1.00 29.65 ?  867 HOH A O     1 
HETATM 3535 O  O     . HOH D 4 .   ? 43.859 37.905 3.982   1.00 27.82 ?  868 HOH A O     1 
HETATM 3536 O  O     . HOH D 4 .   ? 35.872 31.895 27.709  1.00 19.11 ?  869 HOH A O     1 
HETATM 3537 O  O     . HOH D 4 .   ? 58.604 16.430 28.317  1.00 25.24 ?  870 HOH A O     1 
HETATM 3538 O  O     . HOH D 4 .   ? 55.074 17.267 -2.904  1.00 25.60 ?  871 HOH A O     1 
HETATM 3539 O  O     . HOH D 4 .   ? 36.148 30.578 10.276  1.00 32.08 ?  872 HOH A O     1 
HETATM 3540 O  O     . HOH D 4 .   ? 41.947 0.000  31.291  1.00 22.98 ?  873 HOH A O     1 
HETATM 3541 O  O     . HOH D 4 .   ? 62.032 26.036 23.403  1.00 13.95 ?  874 HOH A O     1 
HETATM 3542 O  O     . HOH D 4 .   ? 58.714 32.728 29.553  1.00 20.98 ?  875 HOH A O     1 
HETATM 3543 O  O     . HOH D 4 .   ? 46.872 0.919  46.111  1.00 37.20 ?  876 HOH A O     1 
HETATM 3544 O  O     . HOH D 4 .   ? 50.470 9.932  21.600  1.00 18.47 ?  877 HOH A O     1 
HETATM 3545 O  O     . HOH D 4 .   ? 36.693 34.577 9.610   1.00 35.09 ?  878 HOH A O     1 
HETATM 3546 O  O     . HOH D 4 .   ? 37.915 1.672  30.017  1.00 24.64 ?  879 HOH A O     1 
HETATM 3547 O  O     . HOH D 4 .   ? 37.521 31.345 13.328  1.00 28.85 ?  880 HOH A O     1 
HETATM 3548 O  O     . HOH D 4 .   ? 54.092 32.650 30.318  1.00 25.67 ?  881 HOH A O     1 
HETATM 3549 O  O     . HOH D 4 .   ? 62.266 20.932 14.336  1.00 20.98 ?  882 HOH A O     1 
HETATM 3550 O  O     . HOH D 4 .   ? 35.929 32.712 25.062  1.00 27.31 ?  883 HOH A O     1 
HETATM 3551 O  O     . HOH D 4 .   ? 36.224 0.669  52.119  1.00 24.86 ?  884 HOH A O     1 
HETATM 3552 O  O     . HOH D 4 .   ? 45.559 39.373 6.305   1.00 23.84 ?  885 HOH A O     1 
HETATM 3553 O  O     . HOH D 4 .   ? 38.937 0.425  32.151  1.00 37.39 ?  886 HOH A O     1 
HETATM 3554 O  O     . HOH D 4 .   ? 47.744 3.719  49.945  1.00 26.76 ?  887 HOH A O     1 
HETATM 3555 O  O     . HOH D 4 .   ? 37.890 37.326 41.959  1.00 28.06 ?  888 HOH A O     1 
HETATM 3556 O  O     . HOH D 4 .   ? 50.491 12.795 26.392  1.00 19.23 ?  889 HOH A O     1 
HETATM 3557 O  O     . HOH D 4 .   ? 51.660 13.369 24.073  1.00 26.19 ?  890 HOH A O     1 
HETATM 3558 O  O     . HOH D 4 .   ? 62.843 14.761 40.317  1.00 28.09 ?  891 HOH A O     1 
HETATM 3559 O  O     . HOH D 4 .   ? 39.550 -5.392 43.800  1.00 34.67 ?  892 HOH A O     1 
HETATM 3560 O  O     . HOH D 4 .   ? 60.820 24.103 20.117  1.00 24.02 ?  893 HOH A O     1 
HETATM 3561 O  O     . HOH D 4 .   ? 49.899 24.782 -2.572  1.00 26.33 ?  894 HOH A O     1 
HETATM 3562 O  O     . HOH D 4 .   ? 47.282 28.249 -1.788  1.00 34.91 ?  895 HOH A O     1 
HETATM 3563 O  O     . HOH D 4 .   ? 28.502 12.704 22.677  1.00 21.03 ?  896 HOH A O     1 
HETATM 3564 O  O     . HOH D 4 .   ? 58.428 12.622 30.712  1.00 34.19 ?  897 HOH A O     1 
HETATM 3565 O  O     . HOH D 4 .   ? 25.068 6.234  15.563  1.00 29.92 ?  898 HOH A O     1 
HETATM 3566 O  O     . HOH D 4 .   ? 56.178 17.915 47.972  1.00 22.94 ?  899 HOH A O     1 
HETATM 3567 O  O     . HOH D 4 .   ? 25.010 15.990 22.949  1.00 31.54 ?  900 HOH A O     1 
HETATM 3568 O  O     . HOH D 4 .   ? 40.280 12.503 -1.341  1.00 31.09 ?  901 HOH A O     1 
HETATM 3569 O  O     . HOH D 4 .   ? 44.201 27.289 -1.526  1.00 29.63 ?  902 HOH A O     1 
HETATM 3570 O  O     . HOH D 4 .   ? 58.862 6.873  49.765  1.00 29.94 ?  903 HOH A O     1 
HETATM 3571 O  O     . HOH D 4 .   ? 36.433 18.968 37.854  1.00 14.52 ?  904 HOH A O     1 
HETATM 3572 O  O     . HOH D 4 .   ? 48.675 2.966  46.281  1.00 26.32 ?  905 HOH A O     1 
HETATM 3573 O  O     . HOH D 4 .   ? 59.798 17.550 15.244  1.00 23.18 ?  906 HOH A O     1 
HETATM 3574 O  O     . HOH D 4 .   ? 51.666 8.660  28.363  1.00 16.40 ?  907 HOH A O     1 
HETATM 3575 O  O     . HOH D 4 .   ? 36.199 21.632 37.268  1.00 17.66 ?  908 HOH A O     1 
HETATM 3576 O  O     . HOH D 4 .   ? 22.080 21.056 39.463  1.00 36.70 ?  909 HOH A O     1 
HETATM 3577 O  O     . HOH D 4 .   ? 51.279 -0.947 17.564  1.00 32.46 ?  910 HOH A O     1 
HETATM 3578 O  O     . HOH D 4 .   ? 61.048 6.389  48.512  1.00 30.10 ?  911 HOH A O     1 
HETATM 3579 O  O     . HOH D 4 .   ? 33.240 0.833  51.989  1.00 35.63 ?  912 HOH A O     1 
# 
