data_8YLY
# 
_entry.id   8YLY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8YLY         pdb_00008yly 10.2210/pdb8yly/pdb 
WWPDB D_1300045914 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-19 
_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                        8YLY 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-07 
_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              mahonglei@qibebt.ac.cn 
_pdbx_contact_author.name_first         Honglei 
_pdbx_contact_author.name_last          Ma 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3571-8867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cheng, C.' 1 0009-0005-5230-2419 
'Ma, H.'    2 0000-0003-3571-8867 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural basis of Elongation factor Tu in regulating photoinhibition in Synechococcus sp. PCC 7942' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, C.' 1 0009-0005-5230-2419 
primary 'Ma, H.'   2 0000-0003-3571-8867 
# 
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 'Elongation factor Tu'     44113.094 1   ? ? ? 
;The sequence reference for (strain ATCC 33912 / PCC 7942 / FACHB-805) is not available in Uniprot at the time of biocuration. Current sequence reference is from Uniprot id P18668.
;
2 non-polymer syn GLYCEROL                   92.094    6   ? ? ? ? 
3 non-polymer nat BETA-MERCAPTOETHANOL       78.133    4   ? ? ? ? 
4 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE" 443.201   1   ? ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'            24.305    1   ? ? ? ? 
6 water       nat water                      18.015    501 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        EF-Tu 
# 
_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       
;ARAKFERTKPHANIGTIGHVDHGKTTLTAAITTVLAKAGMAKARAYADIDAAPEEKARGITINTAHVEYETGNRHYAHVD
CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPNIVVFLNKEDMVDDAELLELVELEVRELLSSY
DFPGDDIPIVAGSALQALEAIQGGASGQKGDNPWVDKILKLMEEVDAYIPTPEREVDRPFLMAVEDVFTITGRGTVATGR
IERGSVKVGETIEIVGLRDTRSTTVTGVEMFQKTLDEGLAGDNVGLLLRGIQKTDIERGMVLAKPGSITPHTKFESEVYV
LKKEEGGRHTPFFPGYRPQFYVRTTDVTGAISDFTADDGSAAEMVIPGDRIKMTVELINPIAIEQGMRFAIREGGRTIGA
GVVSKILQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ARAKFERTKPHANIGTIGHVDHGKTTLTAAITTVLAKAGMAKARAYADIDAAPEEKARGITINTAHVEYETGNRHYAHVD
CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPNIVVFLNKEDMVDDAELLELVELEVRELLSSY
DFPGDDIPIVAGSALQALEAIQGGASGQKGDNPWVDKILKLMEEVDAYIPTPEREVDRPFLMAVEDVFTITGRGTVATGR
IERGSVKVGETIEIVGLRDTRSTTVTGVEMFQKTLDEGLAGDNVGLLLRGIQKTDIERGMVLAKPGSITPHTKFESEVYV
LKKEEGGRHTPFFPGYRPQFYVRTTDVTGAISDFTADDGSAAEMVIPGDRIKMTVELINPIAIEQGMRFAIREGGRTIGA
GVVSKILQ
;
_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 GLYCEROL                   GOL 
3 BETA-MERCAPTOETHANOL       BME 
4 "GUANOSINE-5'-DIPHOSPHATE" GDP 
5 'MAGNESIUM ION'            MG  
6 water                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ARG n 
1 3   ALA n 
1 4   LYS n 
1 5   PHE n 
1 6   GLU n 
1 7   ARG n 
1 8   THR n 
1 9   LYS n 
1 10  PRO n 
1 11  HIS n 
1 12  ALA n 
1 13  ASN n 
1 14  ILE n 
1 15  GLY n 
1 16  THR n 
1 17  ILE n 
1 18  GLY n 
1 19  HIS n 
1 20  VAL n 
1 21  ASP n 
1 22  HIS n 
1 23  GLY n 
1 24  LYS n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  THR n 
1 29  ALA n 
1 30  ALA n 
1 31  ILE n 
1 32  THR n 
1 33  THR n 
1 34  VAL n 
1 35  LEU n 
1 36  ALA n 
1 37  LYS n 
1 38  ALA n 
1 39  GLY n 
1 40  MET n 
1 41  ALA n 
1 42  LYS n 
1 43  ALA n 
1 44  ARG n 
1 45  ALA n 
1 46  TYR n 
1 47  ALA n 
1 48  ASP n 
1 49  ILE n 
1 50  ASP n 
1 51  ALA n 
1 52  ALA n 
1 53  PRO n 
1 54  GLU n 
1 55  GLU n 
1 56  LYS n 
1 57  ALA n 
1 58  ARG n 
1 59  GLY n 
1 60  ILE n 
1 61  THR n 
1 62  ILE n 
1 63  ASN n 
1 64  THR n 
1 65  ALA n 
1 66  HIS n 
1 67  VAL n 
1 68  GLU n 
1 69  TYR n 
1 70  GLU n 
1 71  THR n 
1 72  GLY n 
1 73  ASN n 
1 74  ARG n 
1 75  HIS n 
1 76  TYR n 
1 77  ALA n 
1 78  HIS n 
1 79  VAL n 
1 80  ASP n 
1 81  CYS n 
1 82  PRO n 
1 83  GLY n 
1 84  HIS n 
1 85  ALA n 
1 86  ASP n 
1 87  TYR n 
1 88  VAL n 
1 89  LYS n 
1 90  ASN n 
1 91  MET n 
1 92  ILE n 
1 93  THR n 
1 94  GLY n 
1 95  ALA n 
1 96  ALA n 
1 97  GLN n 
1 98  MET n 
1 99  ASP n 
1 100 GLY n 
1 101 ALA n 
1 102 ILE n 
1 103 LEU n 
1 104 VAL n 
1 105 VAL n 
1 106 SER n 
1 107 ALA n 
1 108 ALA n 
1 109 ASP n 
1 110 GLY n 
1 111 PRO n 
1 112 MET n 
1 113 PRO n 
1 114 GLN n 
1 115 THR n 
1 116 ARG n 
1 117 GLU n 
1 118 HIS n 
1 119 ILE n 
1 120 LEU n 
1 121 LEU n 
1 122 ALA n 
1 123 LYS n 
1 124 GLN n 
1 125 VAL n 
1 126 GLY n 
1 127 VAL n 
1 128 PRO n 
1 129 ASN n 
1 130 ILE n 
1 131 VAL n 
1 132 VAL n 
1 133 PHE n 
1 134 LEU n 
1 135 ASN n 
1 136 LYS n 
1 137 GLU n 
1 138 ASP n 
1 139 MET n 
1 140 VAL n 
1 141 ASP n 
1 142 ASP n 
1 143 ALA n 
1 144 GLU n 
1 145 LEU n 
1 146 LEU n 
1 147 GLU n 
1 148 LEU n 
1 149 VAL n 
1 150 GLU n 
1 151 LEU n 
1 152 GLU n 
1 153 VAL n 
1 154 ARG n 
1 155 GLU n 
1 156 LEU n 
1 157 LEU n 
1 158 SER n 
1 159 SER n 
1 160 TYR n 
1 161 ASP n 
1 162 PHE n 
1 163 PRO n 
1 164 GLY n 
1 165 ASP n 
1 166 ASP n 
1 167 ILE n 
1 168 PRO n 
1 169 ILE n 
1 170 VAL n 
1 171 ALA n 
1 172 GLY n 
1 173 SER n 
1 174 ALA n 
1 175 LEU n 
1 176 GLN n 
1 177 ALA n 
1 178 LEU n 
1 179 GLU n 
1 180 ALA n 
1 181 ILE n 
1 182 GLN n 
1 183 GLY n 
1 184 GLY n 
1 185 ALA n 
1 186 SER n 
1 187 GLY n 
1 188 GLN n 
1 189 LYS n 
1 190 GLY n 
1 191 ASP n 
1 192 ASN n 
1 193 PRO n 
1 194 TRP n 
1 195 VAL n 
1 196 ASP n 
1 197 LYS n 
1 198 ILE n 
1 199 LEU n 
1 200 LYS n 
1 201 LEU n 
1 202 MET n 
1 203 GLU n 
1 204 GLU n 
1 205 VAL n 
1 206 ASP n 
1 207 ALA n 
1 208 TYR n 
1 209 ILE n 
1 210 PRO n 
1 211 THR n 
1 212 PRO n 
1 213 GLU n 
1 214 ARG n 
1 215 GLU n 
1 216 VAL n 
1 217 ASP n 
1 218 ARG n 
1 219 PRO n 
1 220 PHE n 
1 221 LEU n 
1 222 MET n 
1 223 ALA n 
1 224 VAL n 
1 225 GLU n 
1 226 ASP n 
1 227 VAL n 
1 228 PHE n 
1 229 THR n 
1 230 ILE n 
1 231 THR n 
1 232 GLY n 
1 233 ARG n 
1 234 GLY n 
1 235 THR n 
1 236 VAL n 
1 237 ALA n 
1 238 THR n 
1 239 GLY n 
1 240 ARG n 
1 241 ILE n 
1 242 GLU n 
1 243 ARG n 
1 244 GLY n 
1 245 SER n 
1 246 VAL n 
1 247 LYS n 
1 248 VAL n 
1 249 GLY n 
1 250 GLU n 
1 251 THR n 
1 252 ILE n 
1 253 GLU n 
1 254 ILE n 
1 255 VAL n 
1 256 GLY n 
1 257 LEU n 
1 258 ARG n 
1 259 ASP n 
1 260 THR n 
1 261 ARG n 
1 262 SER n 
1 263 THR n 
1 264 THR n 
1 265 VAL n 
1 266 THR n 
1 267 GLY n 
1 268 VAL n 
1 269 GLU n 
1 270 MET n 
1 271 PHE n 
1 272 GLN n 
1 273 LYS n 
1 274 THR n 
1 275 LEU n 
1 276 ASP n 
1 277 GLU n 
1 278 GLY n 
1 279 LEU n 
1 280 ALA n 
1 281 GLY n 
1 282 ASP n 
1 283 ASN n 
1 284 VAL n 
1 285 GLY n 
1 286 LEU n 
1 287 LEU n 
1 288 LEU n 
1 289 ARG n 
1 290 GLY n 
1 291 ILE n 
1 292 GLN n 
1 293 LYS n 
1 294 THR n 
1 295 ASP n 
1 296 ILE n 
1 297 GLU n 
1 298 ARG n 
1 299 GLY n 
1 300 MET n 
1 301 VAL n 
1 302 LEU n 
1 303 ALA n 
1 304 LYS n 
1 305 PRO n 
1 306 GLY n 
1 307 SER n 
1 308 ILE n 
1 309 THR n 
1 310 PRO n 
1 311 HIS n 
1 312 THR n 
1 313 LYS n 
1 314 PHE n 
1 315 GLU n 
1 316 SER n 
1 317 GLU n 
1 318 VAL n 
1 319 TYR n 
1 320 VAL n 
1 321 LEU n 
1 322 LYS n 
1 323 LYS n 
1 324 GLU n 
1 325 GLU n 
1 326 GLY n 
1 327 GLY n 
1 328 ARG n 
1 329 HIS n 
1 330 THR n 
1 331 PRO n 
1 332 PHE n 
1 333 PHE n 
1 334 PRO n 
1 335 GLY n 
1 336 TYR n 
1 337 ARG n 
1 338 PRO n 
1 339 GLN n 
1 340 PHE n 
1 341 TYR n 
1 342 VAL n 
1 343 ARG n 
1 344 THR n 
1 345 THR n 
1 346 ASP n 
1 347 VAL n 
1 348 THR n 
1 349 GLY n 
1 350 ALA n 
1 351 ILE n 
1 352 SER n 
1 353 ASP n 
1 354 PHE n 
1 355 THR n 
1 356 ALA n 
1 357 ASP n 
1 358 ASP n 
1 359 GLY n 
1 360 SER n 
1 361 ALA n 
1 362 ALA n 
1 363 GLU n 
1 364 MET n 
1 365 VAL n 
1 366 ILE n 
1 367 PRO n 
1 368 GLY n 
1 369 ASP n 
1 370 ARG n 
1 371 ILE n 
1 372 LYS n 
1 373 MET n 
1 374 THR n 
1 375 VAL n 
1 376 GLU n 
1 377 LEU n 
1 378 ILE n 
1 379 ASN n 
1 380 PRO n 
1 381 ILE n 
1 382 ALA n 
1 383 ILE n 
1 384 GLU n 
1 385 GLN n 
1 386 GLY n 
1 387 MET n 
1 388 ARG n 
1 389 PHE n 
1 390 ALA n 
1 391 ILE n 
1 392 ARG n 
1 393 GLU n 
1 394 GLY n 
1 395 GLY n 
1 396 ARG n 
1 397 THR n 
1 398 ILE n 
1 399 GLY n 
1 400 ALA n 
1 401 GLY n 
1 402 VAL n 
1 403 VAL n 
1 404 SER n 
1 405 LYS n 
1 406 ILE n 
1 407 LEU n 
1 408 GLN 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                   408 
_entity_src_gen.gene_src_common_name               'Anacystis nidulans R2' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'tuf, tufA, syc0656_d' 
_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      'Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1140 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
BME non-polymer         . BETA-MERCAPTOETHANOL       ?                               'C2 H6 O S'         78.133  
CYS 'L-peptide linking' y CYSTEINE                   ?                               'C3 H7 N O2 S'      121.158 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE" ?                               'C10 H15 N5 O11 P2' 443.201 
GLN 'L-peptide linking' y GLUTAMINE                  ?                               'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ?                               'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                    ?                               'C2 H5 N O2'        75.067  
GOL non-polymer         . GLYCEROL                   'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
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 
MG  non-polymer         . 'MAGNESIUM ION'            ?                               'Mg 2'              24.305  
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   ALA 1   2   ?   ?   ?   A . n 
A 1 2   ARG 2   3   ?   ?   ?   A . n 
A 1 3   ALA 3   4   ?   ?   ?   A . n 
A 1 4   LYS 4   5   ?   ?   ?   A . n 
A 1 5   PHE 5   6   6   PHE PHE A . n 
A 1 6   GLU 6   7   7   GLU GLU A . n 
A 1 7   ARG 7   8   8   ARG ARG A . n 
A 1 8   THR 8   9   9   THR THR A . n 
A 1 9   LYS 9   10  10  LYS LYS A . n 
A 1 10  PRO 10  11  11  PRO PRO A . n 
A 1 11  HIS 11  12  12  HIS HIS A . n 
A 1 12  ALA 12  13  13  ALA ALA A . n 
A 1 13  ASN 13  14  14  ASN ASN A . n 
A 1 14  ILE 14  15  15  ILE ILE A . n 
A 1 15  GLY 15  16  16  GLY GLY A . n 
A 1 16  THR 16  17  17  THR THR A . n 
A 1 17  ILE 17  18  18  ILE ILE A . n 
A 1 18  GLY 18  19  19  GLY GLY A . n 
A 1 19  HIS 19  20  20  HIS HIS A . n 
A 1 20  VAL 20  21  21  VAL VAL A . n 
A 1 21  ASP 21  22  22  ASP ASP A . n 
A 1 22  HIS 22  23  23  HIS HIS A . n 
A 1 23  GLY 23  24  24  GLY GLY A . n 
A 1 24  LYS 24  25  25  LYS LYS A . n 
A 1 25  THR 25  26  26  THR THR A . n 
A 1 26  THR 26  27  27  THR THR A . n 
A 1 27  LEU 27  28  28  LEU LEU A . n 
A 1 28  THR 28  29  29  THR THR A . n 
A 1 29  ALA 29  30  30  ALA ALA A . n 
A 1 30  ALA 30  31  31  ALA ALA A . n 
A 1 31  ILE 31  32  32  ILE ILE A . n 
A 1 32  THR 32  33  33  THR THR A . n 
A 1 33  THR 33  34  34  THR THR A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  LEU 35  36  36  LEU LEU A . n 
A 1 36  ALA 36  37  37  ALA ALA A . n 
A 1 37  LYS 37  38  38  LYS LYS A . n 
A 1 38  ALA 38  39  39  ALA ALA A . n 
A 1 39  GLY 39  40  40  GLY GLY A . n 
A 1 40  MET 40  41  41  MET MET A . n 
A 1 41  ALA 41  42  42  ALA ALA A . n 
A 1 42  LYS 42  43  43  LYS LYS A . n 
A 1 43  ALA 43  44  44  ALA ALA A . n 
A 1 44  ARG 44  45  45  ARG ARG A . n 
A 1 45  ALA 45  46  46  ALA ALA A . n 
A 1 46  TYR 46  47  47  TYR TYR A . n 
A 1 47  ALA 47  48  48  ALA ALA A . n 
A 1 48  ASP 48  49  49  ASP ASP A . n 
A 1 49  ILE 49  50  50  ILE ILE A . n 
A 1 50  ASP 50  51  51  ASP ASP A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  ALA 52  53  53  ALA ALA A . n 
A 1 53  PRO 53  54  54  PRO PRO A . n 
A 1 54  GLU 54  55  55  GLU GLU A . n 
A 1 55  GLU 55  56  56  GLU GLU A . n 
A 1 56  LYS 56  57  57  LYS LYS A . n 
A 1 57  ALA 57  58  58  ALA ALA A . n 
A 1 58  ARG 58  59  59  ARG ARG A . n 
A 1 59  GLY 59  60  60  GLY GLY A . n 
A 1 60  ILE 60  61  61  ILE ILE A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  ILE 62  63  63  ILE ILE A . n 
A 1 63  ASN 63  64  64  ASN ASN A . n 
A 1 64  THR 64  65  65  THR THR A . n 
A 1 65  ALA 65  66  66  ALA ALA A . n 
A 1 66  HIS 66  67  67  HIS HIS A . n 
A 1 67  VAL 67  68  68  VAL VAL A . n 
A 1 68  GLU 68  69  69  GLU GLU A . n 
A 1 69  TYR 69  70  70  TYR TYR A . n 
A 1 70  GLU 70  71  71  GLU GLU A . n 
A 1 71  THR 71  72  72  THR THR A . n 
A 1 72  GLY 72  73  73  GLY GLY A . n 
A 1 73  ASN 73  74  74  ASN ASN A . n 
A 1 74  ARG 74  75  75  ARG ARG A . n 
A 1 75  HIS 75  76  76  HIS HIS A . n 
A 1 76  TYR 76  77  77  TYR TYR A . n 
A 1 77  ALA 77  78  78  ALA ALA A . n 
A 1 78  HIS 78  79  79  HIS HIS A . n 
A 1 79  VAL 79  80  80  VAL VAL A . n 
A 1 80  ASP 80  81  81  ASP ASP A . n 
A 1 81  CYS 81  82  82  CYS CYS A . n 
A 1 82  PRO 82  83  83  PRO PRO A . n 
A 1 83  GLY 83  84  84  GLY GLY A . n 
A 1 84  HIS 84  85  85  HIS HIS A . n 
A 1 85  ALA 85  86  86  ALA ALA A . n 
A 1 86  ASP 86  87  87  ASP ASP A . n 
A 1 87  TYR 87  88  88  TYR TYR A . n 
A 1 88  VAL 88  89  89  VAL VAL A . n 
A 1 89  LYS 89  90  90  LYS LYS A . n 
A 1 90  ASN 90  91  91  ASN ASN A . n 
A 1 91  MET 91  92  92  MET MET A . n 
A 1 92  ILE 92  93  93  ILE ILE A . n 
A 1 93  THR 93  94  94  THR THR A . n 
A 1 94  GLY 94  95  95  GLY GLY A . n 
A 1 95  ALA 95  96  96  ALA ALA A . n 
A 1 96  ALA 96  97  97  ALA ALA A . n 
A 1 97  GLN 97  98  98  GLN GLN A . n 
A 1 98  MET 98  99  99  MET MET A . n 
A 1 99  ASP 99  100 100 ASP ASP A . n 
A 1 100 GLY 100 101 101 GLY GLY A . n 
A 1 101 ALA 101 102 102 ALA ALA A . n 
A 1 102 ILE 102 103 103 ILE ILE A . n 
A 1 103 LEU 103 104 104 LEU LEU A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 VAL 105 106 106 VAL VAL A . n 
A 1 106 SER 106 107 107 SER SER A . n 
A 1 107 ALA 107 108 108 ALA ALA A . n 
A 1 108 ALA 108 109 109 ALA ALA A . n 
A 1 109 ASP 109 110 110 ASP ASP A . n 
A 1 110 GLY 110 111 111 GLY GLY A . n 
A 1 111 PRO 111 112 112 PRO PRO A . n 
A 1 112 MET 112 113 113 MET MET A . n 
A 1 113 PRO 113 114 114 PRO PRO A . n 
A 1 114 GLN 114 115 115 GLN GLN A . n 
A 1 115 THR 115 116 116 THR THR A . n 
A 1 116 ARG 116 117 117 ARG ARG A . n 
A 1 117 GLU 117 118 118 GLU GLU A . n 
A 1 118 HIS 118 119 119 HIS HIS A . n 
A 1 119 ILE 119 120 120 ILE ILE A . n 
A 1 120 LEU 120 121 121 LEU LEU A . n 
A 1 121 LEU 121 122 122 LEU LEU A . n 
A 1 122 ALA 122 123 123 ALA ALA A . n 
A 1 123 LYS 123 124 124 LYS LYS A . n 
A 1 124 GLN 124 125 125 GLN GLN A . n 
A 1 125 VAL 125 126 126 VAL VAL A . n 
A 1 126 GLY 126 127 127 GLY GLY A . n 
A 1 127 VAL 127 128 128 VAL VAL A . n 
A 1 128 PRO 128 129 129 PRO PRO A . n 
A 1 129 ASN 129 130 130 ASN ASN A . n 
A 1 130 ILE 130 131 131 ILE ILE A . n 
A 1 131 VAL 131 132 132 VAL VAL A . n 
A 1 132 VAL 132 133 133 VAL VAL A . n 
A 1 133 PHE 133 134 134 PHE PHE A . n 
A 1 134 LEU 134 135 135 LEU LEU A . n 
A 1 135 ASN 135 136 136 ASN ASN A . n 
A 1 136 LYS 136 137 137 LYS LYS A . n 
A 1 137 GLU 137 138 138 GLU GLU A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 MET 139 140 140 MET MET A . n 
A 1 140 VAL 140 141 141 VAL VAL A . n 
A 1 141 ASP 141 142 142 ASP ASP A . n 
A 1 142 ASP 142 143 143 ASP ASP A . n 
A 1 143 ALA 143 144 144 ALA ALA A . n 
A 1 144 GLU 144 145 145 GLU GLU A . n 
A 1 145 LEU 145 146 146 LEU LEU A . n 
A 1 146 LEU 146 147 147 LEU LEU A . n 
A 1 147 GLU 147 148 148 GLU GLU A . n 
A 1 148 LEU 148 149 149 LEU LEU A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLU 150 151 151 GLU GLU A . n 
A 1 151 LEU 151 152 152 LEU LEU A . n 
A 1 152 GLU 152 153 153 GLU GLU A . n 
A 1 153 VAL 153 154 154 VAL VAL A . n 
A 1 154 ARG 154 155 155 ARG ARG A . n 
A 1 155 GLU 155 156 156 GLU GLU A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 LEU 157 158 158 LEU LEU A . n 
A 1 158 SER 158 159 159 SER SER A . n 
A 1 159 SER 159 160 160 SER SER A . n 
A 1 160 TYR 160 161 161 TYR TYR A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 PHE 162 163 163 PHE PHE A . n 
A 1 163 PRO 163 164 164 PRO PRO A . n 
A 1 164 GLY 164 165 165 GLY GLY A . n 
A 1 165 ASP 165 166 166 ASP ASP A . n 
A 1 166 ASP 166 167 167 ASP ASP A . n 
A 1 167 ILE 167 168 168 ILE ILE A . n 
A 1 168 PRO 168 169 169 PRO PRO A . n 
A 1 169 ILE 169 170 170 ILE ILE A . n 
A 1 170 VAL 170 171 171 VAL VAL A . n 
A 1 171 ALA 171 172 172 ALA ALA A . n 
A 1 172 GLY 172 173 173 GLY GLY A . n 
A 1 173 SER 173 174 174 SER SER A . n 
A 1 174 ALA 174 175 175 ALA ALA A . n 
A 1 175 LEU 175 176 176 LEU LEU A . n 
A 1 176 GLN 176 177 177 GLN GLN A . n 
A 1 177 ALA 177 178 178 ALA ALA A . n 
A 1 178 LEU 178 179 179 LEU LEU A . n 
A 1 179 GLU 179 180 180 GLU GLU A . n 
A 1 180 ALA 180 181 181 ALA ALA A . n 
A 1 181 ILE 181 182 182 ILE ILE A . n 
A 1 182 GLN 182 183 183 GLN GLN A . n 
A 1 183 GLY 183 184 184 GLY GLY A . n 
A 1 184 GLY 184 185 185 GLY GLY A . n 
A 1 185 ALA 185 186 186 ALA ALA A . n 
A 1 186 SER 186 187 187 SER SER A . n 
A 1 187 GLY 187 188 188 GLY GLY A . n 
A 1 188 GLN 188 189 189 GLN GLN A . n 
A 1 189 LYS 189 190 190 LYS LYS A . n 
A 1 190 GLY 190 191 191 GLY GLY A . n 
A 1 191 ASP 191 192 192 ASP ASP A . n 
A 1 192 ASN 192 193 193 ASN ASN A . n 
A 1 193 PRO 193 194 194 PRO PRO A . n 
A 1 194 TRP 194 195 195 TRP TRP A . n 
A 1 195 VAL 195 196 196 VAL VAL A . n 
A 1 196 ASP 196 197 197 ASP ASP A . n 
A 1 197 LYS 197 198 198 LYS LYS A . n 
A 1 198 ILE 198 199 199 ILE ILE A . n 
A 1 199 LEU 199 200 200 LEU LEU A . n 
A 1 200 LYS 200 201 201 LYS LYS A . n 
A 1 201 LEU 201 202 202 LEU LEU A . n 
A 1 202 MET 202 203 203 MET MET A . n 
A 1 203 GLU 203 204 204 GLU GLU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 VAL 205 206 206 VAL VAL A . n 
A 1 206 ASP 206 207 207 ASP ASP A . n 
A 1 207 ALA 207 208 208 ALA ALA A . n 
A 1 208 TYR 208 209 209 TYR TYR A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 PRO 210 211 211 PRO PRO A . n 
A 1 211 THR 211 212 212 THR THR A . n 
A 1 212 PRO 212 213 213 PRO PRO A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 ARG 214 215 215 ARG ARG A . n 
A 1 215 GLU 215 216 216 GLU GLU A . n 
A 1 216 VAL 216 217 217 VAL VAL A . n 
A 1 217 ASP 217 218 218 ASP ASP A . n 
A 1 218 ARG 218 219 219 ARG ARG A . n 
A 1 219 PRO 219 220 220 PRO PRO A . n 
A 1 220 PHE 220 221 221 PHE PHE A . n 
A 1 221 LEU 221 222 222 LEU LEU A . n 
A 1 222 MET 222 223 223 MET MET A . n 
A 1 223 ALA 223 224 224 ALA ALA A . n 
A 1 224 VAL 224 225 225 VAL VAL A . n 
A 1 225 GLU 225 226 226 GLU GLU A . n 
A 1 226 ASP 226 227 227 ASP ASP A . n 
A 1 227 VAL 227 228 228 VAL VAL A . n 
A 1 228 PHE 228 229 229 PHE PHE A . n 
A 1 229 THR 229 230 230 THR THR A . n 
A 1 230 ILE 230 231 231 ILE ILE A . n 
A 1 231 THR 231 232 232 THR THR A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 ARG 233 234 234 ARG ARG A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 THR 235 236 236 THR THR A . n 
A 1 236 VAL 236 237 237 VAL VAL A . n 
A 1 237 ALA 237 238 238 ALA ALA A . n 
A 1 238 THR 238 239 239 THR THR A . n 
A 1 239 GLY 239 240 240 GLY GLY A . n 
A 1 240 ARG 240 241 241 ARG ARG A . n 
A 1 241 ILE 241 242 242 ILE ILE A . n 
A 1 242 GLU 242 243 243 GLU GLU A . n 
A 1 243 ARG 243 244 244 ARG ARG A . n 
A 1 244 GLY 244 245 245 GLY GLY A . n 
A 1 245 SER 245 246 246 SER SER A . n 
A 1 246 VAL 246 247 247 VAL VAL A . n 
A 1 247 LYS 247 248 248 LYS LYS A . n 
A 1 248 VAL 248 249 249 VAL VAL A . n 
A 1 249 GLY 249 250 250 GLY GLY A . n 
A 1 250 GLU 250 251 251 GLU GLU A . n 
A 1 251 THR 251 252 252 THR THR A . n 
A 1 252 ILE 252 253 253 ILE ILE A . n 
A 1 253 GLU 253 254 254 GLU GLU A . n 
A 1 254 ILE 254 255 255 ILE ILE A . n 
A 1 255 VAL 255 256 256 VAL VAL A . n 
A 1 256 GLY 256 257 257 GLY GLY A . n 
A 1 257 LEU 257 258 258 LEU LEU A . n 
A 1 258 ARG 258 259 259 ARG ARG A . n 
A 1 259 ASP 259 260 260 ASP ASP A . n 
A 1 260 THR 260 261 261 THR THR A . n 
A 1 261 ARG 261 262 262 ARG ARG A . n 
A 1 262 SER 262 263 263 SER SER A . n 
A 1 263 THR 263 264 264 THR THR A . n 
A 1 264 THR 264 265 265 THR THR A . n 
A 1 265 VAL 265 266 266 VAL VAL A . n 
A 1 266 THR 266 267 267 THR THR A . n 
A 1 267 GLY 267 268 268 GLY GLY A . n 
A 1 268 VAL 268 269 269 VAL VAL A . n 
A 1 269 GLU 269 270 270 GLU GLU A . n 
A 1 270 MET 270 271 271 MET MET A . n 
A 1 271 PHE 271 272 272 PHE PHE A . n 
A 1 272 GLN 272 273 273 GLN GLN A . n 
A 1 273 LYS 273 274 274 LYS LYS A . n 
A 1 274 THR 274 275 275 THR THR A . n 
A 1 275 LEU 275 276 276 LEU LEU A . n 
A 1 276 ASP 276 277 277 ASP ASP A . n 
A 1 277 GLU 277 278 278 GLU GLU A . n 
A 1 278 GLY 278 279 279 GLY GLY A . n 
A 1 279 LEU 279 280 280 LEU LEU A . n 
A 1 280 ALA 280 281 281 ALA ALA A . n 
A 1 281 GLY 281 282 282 GLY GLY A . n 
A 1 282 ASP 282 283 283 ASP ASP A . n 
A 1 283 ASN 283 284 284 ASN ASN A . n 
A 1 284 VAL 284 285 285 VAL VAL A . n 
A 1 285 GLY 285 286 286 GLY GLY A . n 
A 1 286 LEU 286 287 287 LEU LEU A . n 
A 1 287 LEU 287 288 288 LEU LEU A . n 
A 1 288 LEU 288 289 289 LEU LEU A . n 
A 1 289 ARG 289 290 290 ARG ARG A . n 
A 1 290 GLY 290 291 291 GLY GLY A . n 
A 1 291 ILE 291 292 292 ILE ILE A . n 
A 1 292 GLN 292 293 293 GLN GLN A . n 
A 1 293 LYS 293 294 294 LYS LYS A . n 
A 1 294 THR 294 295 295 THR THR A . n 
A 1 295 ASP 295 296 296 ASP ASP A . n 
A 1 296 ILE 296 297 297 ILE ILE A . n 
A 1 297 GLU 297 298 298 GLU GLU A . n 
A 1 298 ARG 298 299 299 ARG ARG A . n 
A 1 299 GLY 299 300 300 GLY GLY A . n 
A 1 300 MET 300 301 301 MET MET A . n 
A 1 301 VAL 301 302 302 VAL VAL A . n 
A 1 302 LEU 302 303 303 LEU LEU A . n 
A 1 303 ALA 303 304 304 ALA ALA A . n 
A 1 304 LYS 304 305 305 LYS LYS A . n 
A 1 305 PRO 305 306 306 PRO PRO A . n 
A 1 306 GLY 306 307 307 GLY GLY A . n 
A 1 307 SER 307 308 308 SER SER A . n 
A 1 308 ILE 308 309 309 ILE ILE A . n 
A 1 309 THR 309 310 310 THR THR A . n 
A 1 310 PRO 310 311 311 PRO PRO A . n 
A 1 311 HIS 311 312 312 HIS HIS A . n 
A 1 312 THR 312 313 313 THR THR A . n 
A 1 313 LYS 313 314 314 LYS LYS A . n 
A 1 314 PHE 314 315 315 PHE PHE A . n 
A 1 315 GLU 315 316 316 GLU GLU A . n 
A 1 316 SER 316 317 317 SER SER A . n 
A 1 317 GLU 317 318 318 GLU GLU A . n 
A 1 318 VAL 318 319 319 VAL VAL A . n 
A 1 319 TYR 319 320 320 TYR TYR A . n 
A 1 320 VAL 320 321 321 VAL VAL A . n 
A 1 321 LEU 321 322 322 LEU LEU A . n 
A 1 322 LYS 322 323 323 LYS LYS A . n 
A 1 323 LYS 323 324 324 LYS LYS A . n 
A 1 324 GLU 324 325 325 GLU GLU A . n 
A 1 325 GLU 325 326 326 GLU GLU A . n 
A 1 326 GLY 326 327 327 GLY GLY A . n 
A 1 327 GLY 327 328 328 GLY GLY A . n 
A 1 328 ARG 328 329 329 ARG ARG A . n 
A 1 329 HIS 329 330 330 HIS HIS A . n 
A 1 330 THR 330 331 331 THR THR A . n 
A 1 331 PRO 331 332 332 PRO PRO A . n 
A 1 332 PHE 332 333 333 PHE PHE A . n 
A 1 333 PHE 333 334 334 PHE PHE A . n 
A 1 334 PRO 334 335 335 PRO PRO A . n 
A 1 335 GLY 335 336 336 GLY GLY A . n 
A 1 336 TYR 336 337 337 TYR TYR A . n 
A 1 337 ARG 337 338 338 ARG ARG A . n 
A 1 338 PRO 338 339 339 PRO PRO A . n 
A 1 339 GLN 339 340 340 GLN GLN A . n 
A 1 340 PHE 340 341 341 PHE PHE A . n 
A 1 341 TYR 341 342 342 TYR TYR A . n 
A 1 342 VAL 342 343 343 VAL VAL A . n 
A 1 343 ARG 343 344 344 ARG ARG A . n 
A 1 344 THR 344 345 345 THR THR A . n 
A 1 345 THR 345 346 346 THR THR A . n 
A 1 346 ASP 346 347 347 ASP ASP A . n 
A 1 347 VAL 347 348 348 VAL VAL A . n 
A 1 348 THR 348 349 349 THR THR A . n 
A 1 349 GLY 349 350 350 GLY GLY A . n 
A 1 350 ALA 350 351 351 ALA ALA A . n 
A 1 351 ILE 351 352 352 ILE ILE A . n 
A 1 352 SER 352 353 353 SER SER A . n 
A 1 353 ASP 353 354 354 ASP ASP A . n 
A 1 354 PHE 354 355 355 PHE PHE A . n 
A 1 355 THR 355 356 356 THR THR A . n 
A 1 356 ALA 356 357 357 ALA ALA A . n 
A 1 357 ASP 357 358 358 ASP ASP A . n 
A 1 358 ASP 358 359 359 ASP ASP A . n 
A 1 359 GLY 359 360 360 GLY GLY A . n 
A 1 360 SER 360 361 361 SER SER A . n 
A 1 361 ALA 361 362 362 ALA ALA A . n 
A 1 362 ALA 362 363 363 ALA ALA A . n 
A 1 363 GLU 363 364 364 GLU GLU A . n 
A 1 364 MET 364 365 365 MET MET A . n 
A 1 365 VAL 365 366 366 VAL VAL A . n 
A 1 366 ILE 366 367 367 ILE ILE A . n 
A 1 367 PRO 367 368 368 PRO PRO A . n 
A 1 368 GLY 368 369 369 GLY GLY A . n 
A 1 369 ASP 369 370 370 ASP ASP A . n 
A 1 370 ARG 370 371 371 ARG ARG A . n 
A 1 371 ILE 371 372 372 ILE ILE A . n 
A 1 372 LYS 372 373 373 LYS LYS A . n 
A 1 373 MET 373 374 374 MET MET A . n 
A 1 374 THR 374 375 375 THR THR A . n 
A 1 375 VAL 375 376 376 VAL VAL A . n 
A 1 376 GLU 376 377 377 GLU GLU A . n 
A 1 377 LEU 377 378 378 LEU LEU A . n 
A 1 378 ILE 378 379 379 ILE ILE A . n 
A 1 379 ASN 379 380 380 ASN ASN A . n 
A 1 380 PRO 380 381 381 PRO PRO A . n 
A 1 381 ILE 381 382 382 ILE ILE A . n 
A 1 382 ALA 382 383 383 ALA ALA A . n 
A 1 383 ILE 383 384 384 ILE ILE A . n 
A 1 384 GLU 384 385 385 GLU GLU A . n 
A 1 385 GLN 385 386 386 GLN GLN A . n 
A 1 386 GLY 386 387 387 GLY GLY A . n 
A 1 387 MET 387 388 388 MET MET A . n 
A 1 388 ARG 388 389 389 ARG ARG A . n 
A 1 389 PHE 389 390 390 PHE PHE A . n 
A 1 390 ALA 390 391 391 ALA ALA A . n 
A 1 391 ILE 391 392 392 ILE ILE A . n 
A 1 392 ARG 392 393 393 ARG ARG A . n 
A 1 393 GLU 393 394 394 GLU GLU A . n 
A 1 394 GLY 394 395 395 GLY GLY A . n 
A 1 395 GLY 395 396 396 GLY GLY A . n 
A 1 396 ARG 396 397 397 ARG ARG A . n 
A 1 397 THR 397 398 398 THR THR A . n 
A 1 398 ILE 398 399 399 ILE ILE A . n 
A 1 399 GLY 399 400 400 GLY GLY A . n 
A 1 400 ALA 400 401 401 ALA ALA A . n 
A 1 401 GLY 401 402 402 GLY GLY A . n 
A 1 402 VAL 402 403 403 VAL VAL A . n 
A 1 403 VAL 403 404 404 VAL VAL A . n 
A 1 404 SER 404 405 405 SER SER A . n 
A 1 405 LYS 405 406 406 LYS LYS A . n 
A 1 406 ILE 406 407 407 ILE ILE A . n 
A 1 407 LEU 407 408 408 LEU LEU A . n 
A 1 408 GLN 408 409 409 GLN GLN 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 BME ? ? BME ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GDP ? ? GDP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 GOL ? ? GOL ? ? 'SUBJECT OF INVESTIGATION' ? 
4 MG  ? ? MG  ? ? '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 GOL 1   501  510 GOL GOL A . 
C 3 BME 1   502  511 BME BME A . 
D 4 GDP 1   503  501 GDP GDP A . 
E 3 BME 1   504  502 BME BME A . 
F 2 GOL 1   505  503 GOL GOL A . 
G 2 GOL 1   506  504 GOL GOL A . 
H 2 GOL 1   507  505 GOL GOL A . 
I 3 BME 1   508  506 BME BME A . 
J 3 BME 1   509  507 BME BME A . 
K 2 GOL 1   510  508 GOL GOL A . 
L 2 GOL 1   511  509 GOL GOL A . 
M 5 MG  1   512  2   MG  MG  A . 
N 6 HOH 1   601  66  HOH HOH A . 
N 6 HOH 2   602  489 HOH HOH A . 
N 6 HOH 3   603  242 HOH HOH A . 
N 6 HOH 4   604  314 HOH HOH A . 
N 6 HOH 5   605  448 HOH HOH A . 
N 6 HOH 6   606  277 HOH HOH A . 
N 6 HOH 7   607  102 HOH HOH A . 
N 6 HOH 8   608  50  HOH HOH A . 
N 6 HOH 9   609  349 HOH HOH A . 
N 6 HOH 10  610  319 HOH HOH A . 
N 6 HOH 11  611  281 HOH HOH A . 
N 6 HOH 12  612  426 HOH HOH A . 
N 6 HOH 13  613  183 HOH HOH A . 
N 6 HOH 14  614  269 HOH HOH A . 
N 6 HOH 15  615  272 HOH HOH A . 
N 6 HOH 16  616  370 HOH HOH A . 
N 6 HOH 17  617  267 HOH HOH A . 
N 6 HOH 18  618  229 HOH HOH A . 
N 6 HOH 19  619  410 HOH HOH A . 
N 6 HOH 20  620  80  HOH HOH A . 
N 6 HOH 21  621  251 HOH HOH A . 
N 6 HOH 22  622  165 HOH HOH A . 
N 6 HOH 23  623  185 HOH HOH A . 
N 6 HOH 24  624  86  HOH HOH A . 
N 6 HOH 25  625  81  HOH HOH A . 
N 6 HOH 26  626  173 HOH HOH A . 
N 6 HOH 27  627  204 HOH HOH A . 
N 6 HOH 28  628  274 HOH HOH A . 
N 6 HOH 29  629  257 HOH HOH A . 
N 6 HOH 30  630  248 HOH HOH A . 
N 6 HOH 31  631  123 HOH HOH A . 
N 6 HOH 32  632  88  HOH HOH A . 
N 6 HOH 33  633  163 HOH HOH A . 
N 6 HOH 34  634  316 HOH HOH A . 
N 6 HOH 35  635  358 HOH HOH A . 
N 6 HOH 36  636  268 HOH HOH A . 
N 6 HOH 37  637  146 HOH HOH A . 
N 6 HOH 38  638  315 HOH HOH A . 
N 6 HOH 39  639  120 HOH HOH A . 
N 6 HOH 40  640  297 HOH HOH A . 
N 6 HOH 41  641  431 HOH HOH A . 
N 6 HOH 42  642  430 HOH HOH A . 
N 6 HOH 43  643  342 HOH HOH A . 
N 6 HOH 44  644  409 HOH HOH A . 
N 6 HOH 45  645  68  HOH HOH A . 
N 6 HOH 46  646  72  HOH HOH A . 
N 6 HOH 47  647  45  HOH HOH A . 
N 6 HOH 48  648  23  HOH HOH A . 
N 6 HOH 49  649  273 HOH HOH A . 
N 6 HOH 50  650  402 HOH HOH A . 
N 6 HOH 51  651  83  HOH HOH A . 
N 6 HOH 52  652  199 HOH HOH A . 
N 6 HOH 53  653  470 HOH HOH A . 
N 6 HOH 54  654  396 HOH HOH A . 
N 6 HOH 55  655  482 HOH HOH A . 
N 6 HOH 56  656  250 HOH HOH A . 
N 6 HOH 57  657  231 HOH HOH A . 
N 6 HOH 58  658  139 HOH HOH A . 
N 6 HOH 59  659  37  HOH HOH A . 
N 6 HOH 60  660  289 HOH HOH A . 
N 6 HOH 61  661  34  HOH HOH A . 
N 6 HOH 62  662  44  HOH HOH A . 
N 6 HOH 63  663  361 HOH HOH A . 
N 6 HOH 64  664  245 HOH HOH A . 
N 6 HOH 65  665  221 HOH HOH A . 
N 6 HOH 66  666  256 HOH HOH A . 
N 6 HOH 67  667  25  HOH HOH A . 
N 6 HOH 68  668  131 HOH HOH A . 
N 6 HOH 69  669  62  HOH HOH A . 
N 6 HOH 70  670  236 HOH HOH A . 
N 6 HOH 71  671  348 HOH HOH A . 
N 6 HOH 72  672  388 HOH HOH A . 
N 6 HOH 73  673  61  HOH HOH A . 
N 6 HOH 74  674  271 HOH HOH A . 
N 6 HOH 75  675  149 HOH HOH A . 
N 6 HOH 76  676  151 HOH HOH A . 
N 6 HOH 77  677  79  HOH HOH A . 
N 6 HOH 78  678  429 HOH HOH A . 
N 6 HOH 79  679  91  HOH HOH A . 
N 6 HOH 80  680  92  HOH HOH A . 
N 6 HOH 81  681  137 HOH HOH A . 
N 6 HOH 82  682  436 HOH HOH A . 
N 6 HOH 83  683  49  HOH HOH A . 
N 6 HOH 84  684  177 HOH HOH A . 
N 6 HOH 85  685  452 HOH HOH A . 
N 6 HOH 86  686  9   HOH HOH A . 
N 6 HOH 87  687  141 HOH HOH A . 
N 6 HOH 88  688  205 HOH HOH A . 
N 6 HOH 89  689  38  HOH HOH A . 
N 6 HOH 90  690  76  HOH HOH A . 
N 6 HOH 91  691  119 HOH HOH A . 
N 6 HOH 92  692  175 HOH HOH A . 
N 6 HOH 93  693  11  HOH HOH A . 
N 6 HOH 94  694  117 HOH HOH A . 
N 6 HOH 95  695  17  HOH HOH A . 
N 6 HOH 96  696  208 HOH HOH A . 
N 6 HOH 97  697  122 HOH HOH A . 
N 6 HOH 98  698  148 HOH HOH A . 
N 6 HOH 99  699  207 HOH HOH A . 
N 6 HOH 100 700  99  HOH HOH A . 
N 6 HOH 101 701  29  HOH HOH A . 
N 6 HOH 102 702  82  HOH HOH A . 
N 6 HOH 103 703  247 HOH HOH A . 
N 6 HOH 104 704  143 HOH HOH A . 
N 6 HOH 105 705  270 HOH HOH A . 
N 6 HOH 106 706  127 HOH HOH A . 
N 6 HOH 107 707  21  HOH HOH A . 
N 6 HOH 108 708  365 HOH HOH A . 
N 6 HOH 109 709  133 HOH HOH A . 
N 6 HOH 110 710  216 HOH HOH A . 
N 6 HOH 111 711  395 HOH HOH A . 
N 6 HOH 112 712  422 HOH HOH A . 
N 6 HOH 113 713  237 HOH HOH A . 
N 6 HOH 114 714  232 HOH HOH A . 
N 6 HOH 115 715  15  HOH HOH A . 
N 6 HOH 116 716  283 HOH HOH A . 
N 6 HOH 117 717  32  HOH HOH A . 
N 6 HOH 118 718  70  HOH HOH A . 
N 6 HOH 119 719  421 HOH HOH A . 
N 6 HOH 120 720  1   HOH HOH A . 
N 6 HOH 121 721  157 HOH HOH A . 
N 6 HOH 122 722  69  HOH HOH A . 
N 6 HOH 123 723  295 HOH HOH A . 
N 6 HOH 124 724  428 HOH HOH A . 
N 6 HOH 125 725  404 HOH HOH A . 
N 6 HOH 126 726  136 HOH HOH A . 
N 6 HOH 127 727  290 HOH HOH A . 
N 6 HOH 128 728  155 HOH HOH A . 
N 6 HOH 129 729  159 HOH HOH A . 
N 6 HOH 130 730  41  HOH HOH A . 
N 6 HOH 131 731  347 HOH HOH A . 
N 6 HOH 132 732  14  HOH HOH A . 
N 6 HOH 133 733  65  HOH HOH A . 
N 6 HOH 134 734  129 HOH HOH A . 
N 6 HOH 135 735  130 HOH HOH A . 
N 6 HOH 136 736  241 HOH HOH A . 
N 6 HOH 137 737  98  HOH HOH A . 
N 6 HOH 138 738  30  HOH HOH A . 
N 6 HOH 139 739  28  HOH HOH A . 
N 6 HOH 140 740  215 HOH HOH A . 
N 6 HOH 141 741  235 HOH HOH A . 
N 6 HOH 142 742  18  HOH HOH A . 
N 6 HOH 143 743  307 HOH HOH A . 
N 6 HOH 144 744  94  HOH HOH A . 
N 6 HOH 145 745  467 HOH HOH A . 
N 6 HOH 146 746  213 HOH HOH A . 
N 6 HOH 147 747  457 HOH HOH A . 
N 6 HOH 148 748  496 HOH HOH A . 
N 6 HOH 149 749  135 HOH HOH A . 
N 6 HOH 150 750  12  HOH HOH A . 
N 6 HOH 151 751  309 HOH HOH A . 
N 6 HOH 152 752  304 HOH HOH A . 
N 6 HOH 153 753  186 HOH HOH A . 
N 6 HOH 154 754  115 HOH HOH A . 
N 6 HOH 155 755  31  HOH HOH A . 
N 6 HOH 156 756  209 HOH HOH A . 
N 6 HOH 157 757  368 HOH HOH A . 
N 6 HOH 158 758  56  HOH HOH A . 
N 6 HOH 159 759  225 HOH HOH A . 
N 6 HOH 160 760  7   HOH HOH A . 
N 6 HOH 161 761  103 HOH HOH A . 
N 6 HOH 162 762  100 HOH HOH A . 
N 6 HOH 163 763  26  HOH HOH A . 
N 6 HOH 164 764  212 HOH HOH A . 
N 6 HOH 165 765  203 HOH HOH A . 
N 6 HOH 166 766  217 HOH HOH A . 
N 6 HOH 167 767  33  HOH HOH A . 
N 6 HOH 168 768  214 HOH HOH A . 
N 6 HOH 169 769  218 HOH HOH A . 
N 6 HOH 170 770  8   HOH HOH A . 
N 6 HOH 171 771  71  HOH HOH A . 
N 6 HOH 172 772  182 HOH HOH A . 
N 6 HOH 173 773  252 HOH HOH A . 
N 6 HOH 174 774  188 HOH HOH A . 
N 6 HOH 175 775  67  HOH HOH A . 
N 6 HOH 176 776  97  HOH HOH A . 
N 6 HOH 177 777  417 HOH HOH A . 
N 6 HOH 178 778  398 HOH HOH A . 
N 6 HOH 179 779  51  HOH HOH A . 
N 6 HOH 180 780  24  HOH HOH A . 
N 6 HOH 181 781  22  HOH HOH A . 
N 6 HOH 182 782  197 HOH HOH A . 
N 6 HOH 183 783  158 HOH HOH A . 
N 6 HOH 184 784  341 HOH HOH A . 
N 6 HOH 185 785  464 HOH HOH A . 
N 6 HOH 186 786  301 HOH HOH A . 
N 6 HOH 187 787  458 HOH HOH A . 
N 6 HOH 188 788  419 HOH HOH A . 
N 6 HOH 189 789  308 HOH HOH A . 
N 6 HOH 190 790  414 HOH HOH A . 
N 6 HOH 191 791  392 HOH HOH A . 
N 6 HOH 192 792  285 HOH HOH A . 
N 6 HOH 193 793  306 HOH HOH A . 
N 6 HOH 194 794  48  HOH HOH A . 
N 6 HOH 195 795  276 HOH HOH A . 
N 6 HOH 196 796  74  HOH HOH A . 
N 6 HOH 197 797  3   HOH HOH A . 
N 6 HOH 198 798  75  HOH HOH A . 
N 6 HOH 199 799  353 HOH HOH A . 
N 6 HOH 200 800  233 HOH HOH A . 
N 6 HOH 201 801  58  HOH HOH A . 
N 6 HOH 202 802  13  HOH HOH A . 
N 6 HOH 203 803  219 HOH HOH A . 
N 6 HOH 204 804  311 HOH HOH A . 
N 6 HOH 205 805  294 HOH HOH A . 
N 6 HOH 206 806  36  HOH HOH A . 
N 6 HOH 207 807  166 HOH HOH A . 
N 6 HOH 208 808  303 HOH HOH A . 
N 6 HOH 209 809  4   HOH HOH A . 
N 6 HOH 210 810  128 HOH HOH A . 
N 6 HOH 211 811  313 HOH HOH A . 
N 6 HOH 212 812  462 HOH HOH A . 
N 6 HOH 213 813  327 HOH HOH A . 
N 6 HOH 214 814  497 HOH HOH A . 
N 6 HOH 215 815  172 HOH HOH A . 
N 6 HOH 216 816  16  HOH HOH A . 
N 6 HOH 217 817  60  HOH HOH A . 
N 6 HOH 218 818  234 HOH HOH A . 
N 6 HOH 219 819  95  HOH HOH A . 
N 6 HOH 220 820  52  HOH HOH A . 
N 6 HOH 221 821  168 HOH HOH A . 
N 6 HOH 222 822  220 HOH HOH A . 
N 6 HOH 223 823  40  HOH HOH A . 
N 6 HOH 224 824  2   HOH HOH A . 
N 6 HOH 225 825  55  HOH HOH A . 
N 6 HOH 226 826  264 HOH HOH A . 
N 6 HOH 227 827  27  HOH HOH A . 
N 6 HOH 228 828  339 HOH HOH A . 
N 6 HOH 229 829  39  HOH HOH A . 
N 6 HOH 230 830  206 HOH HOH A . 
N 6 HOH 231 831  6   HOH HOH A . 
N 6 HOH 232 832  85  HOH HOH A . 
N 6 HOH 233 833  317 HOH HOH A . 
N 6 HOH 234 834  292 HOH HOH A . 
N 6 HOH 235 835  384 HOH HOH A . 
N 6 HOH 236 836  93  HOH HOH A . 
N 6 HOH 237 837  184 HOH HOH A . 
N 6 HOH 238 838  138 HOH HOH A . 
N 6 HOH 239 839  35  HOH HOH A . 
N 6 HOH 240 840  42  HOH HOH A . 
N 6 HOH 241 841  20  HOH HOH A . 
N 6 HOH 242 842  160 HOH HOH A . 
N 6 HOH 243 843  193 HOH HOH A . 
N 6 HOH 244 844  174 HOH HOH A . 
N 6 HOH 245 845  198 HOH HOH A . 
N 6 HOH 246 846  46  HOH HOH A . 
N 6 HOH 247 847  310 HOH HOH A . 
N 6 HOH 248 848  399 HOH HOH A . 
N 6 HOH 249 849  336 HOH HOH A . 
N 6 HOH 250 850  196 HOH HOH A . 
N 6 HOH 251 851  387 HOH HOH A . 
N 6 HOH 252 852  5   HOH HOH A . 
N 6 HOH 253 853  57  HOH HOH A . 
N 6 HOH 254 854  43  HOH HOH A . 
N 6 HOH 255 855  299 HOH HOH A . 
N 6 HOH 256 856  53  HOH HOH A . 
N 6 HOH 257 857  469 HOH HOH A . 
N 6 HOH 258 858  239 HOH HOH A . 
N 6 HOH 259 859  366 HOH HOH A . 
N 6 HOH 260 860  78  HOH HOH A . 
N 6 HOH 261 861  59  HOH HOH A . 
N 6 HOH 262 862  411 HOH HOH A . 
N 6 HOH 263 863  401 HOH HOH A . 
N 6 HOH 264 864  121 HOH HOH A . 
N 6 HOH 265 865  230 HOH HOH A . 
N 6 HOH 266 866  147 HOH HOH A . 
N 6 HOH 267 867  443 HOH HOH A . 
N 6 HOH 268 868  124 HOH HOH A . 
N 6 HOH 269 869  96  HOH HOH A . 
N 6 HOH 270 870  63  HOH HOH A . 
N 6 HOH 271 871  244 HOH HOH A . 
N 6 HOH 272 872  54  HOH HOH A . 
N 6 HOH 273 873  47  HOH HOH A . 
N 6 HOH 274 874  142 HOH HOH A . 
N 6 HOH 275 875  194 HOH HOH A . 
N 6 HOH 276 876  19  HOH HOH A . 
N 6 HOH 277 877  126 HOH HOH A . 
N 6 HOH 278 878  360 HOH HOH A . 
N 6 HOH 279 879  474 HOH HOH A . 
N 6 HOH 280 880  227 HOH HOH A . 
N 6 HOH 281 881  318 HOH HOH A . 
N 6 HOH 282 882  238 HOH HOH A . 
N 6 HOH 283 883  144 HOH HOH A . 
N 6 HOH 284 884  10  HOH HOH A . 
N 6 HOH 285 885  490 HOH HOH A . 
N 6 HOH 286 886  211 HOH HOH A . 
N 6 HOH 287 887  300 HOH HOH A . 
N 6 HOH 288 888  187 HOH HOH A . 
N 6 HOH 289 889  132 HOH HOH A . 
N 6 HOH 290 890  450 HOH HOH A . 
N 6 HOH 291 891  343 HOH HOH A . 
N 6 HOH 292 892  302 HOH HOH A . 
N 6 HOH 293 893  84  HOH HOH A . 
N 6 HOH 294 894  140 HOH HOH A . 
N 6 HOH 295 895  334 HOH HOH A . 
N 6 HOH 296 896  249 HOH HOH A . 
N 6 HOH 297 897  161 HOH HOH A . 
N 6 HOH 298 898  278 HOH HOH A . 
N 6 HOH 299 899  189 HOH HOH A . 
N 6 HOH 300 900  180 HOH HOH A . 
N 6 HOH 301 901  222 HOH HOH A . 
N 6 HOH 302 902  280 HOH HOH A . 
N 6 HOH 303 903  385 HOH HOH A . 
N 6 HOH 304 904  355 HOH HOH A . 
N 6 HOH 305 905  73  HOH HOH A . 
N 6 HOH 306 906  377 HOH HOH A . 
N 6 HOH 307 907  369 HOH HOH A . 
N 6 HOH 308 908  420 HOH HOH A . 
N 6 HOH 309 909  298 HOH HOH A . 
N 6 HOH 310 910  389 HOH HOH A . 
N 6 HOH 311 911  104 HOH HOH A . 
N 6 HOH 312 912  153 HOH HOH A . 
N 6 HOH 313 913  162 HOH HOH A . 
N 6 HOH 314 914  105 HOH HOH A . 
N 6 HOH 315 915  156 HOH HOH A . 
N 6 HOH 316 916  337 HOH HOH A . 
N 6 HOH 317 917  118 HOH HOH A . 
N 6 HOH 318 918  432 HOH HOH A . 
N 6 HOH 319 919  77  HOH HOH A . 
N 6 HOH 320 920  125 HOH HOH A . 
N 6 HOH 321 921  407 HOH HOH A . 
N 6 HOH 322 922  284 HOH HOH A . 
N 6 HOH 323 923  379 HOH HOH A . 
N 6 HOH 324 924  228 HOH HOH A . 
N 6 HOH 325 925  330 HOH HOH A . 
N 6 HOH 326 926  265 HOH HOH A . 
N 6 HOH 327 927  415 HOH HOH A . 
N 6 HOH 328 928  416 HOH HOH A . 
N 6 HOH 329 929  291 HOH HOH A . 
N 6 HOH 330 930  210 HOH HOH A . 
N 6 HOH 331 931  367 HOH HOH A . 
N 6 HOH 332 932  170 HOH HOH A . 
N 6 HOH 333 933  380 HOH HOH A . 
N 6 HOH 334 934  403 HOH HOH A . 
N 6 HOH 335 935  359 HOH HOH A . 
N 6 HOH 336 936  391 HOH HOH A . 
N 6 HOH 337 937  487 HOH HOH A . 
N 6 HOH 338 938  305 HOH HOH A . 
N 6 HOH 339 939  397 HOH HOH A . 
N 6 HOH 340 940  171 HOH HOH A . 
N 6 HOH 341 941  435 HOH HOH A . 
N 6 HOH 342 942  179 HOH HOH A . 
N 6 HOH 343 943  106 HOH HOH A . 
N 6 HOH 344 944  201 HOH HOH A . 
N 6 HOH 345 945  134 HOH HOH A . 
N 6 HOH 346 946  393 HOH HOH A . 
N 6 HOH 347 947  178 HOH HOH A . 
N 6 HOH 348 948  491 HOH HOH A . 
N 6 HOH 349 949  465 HOH HOH A . 
N 6 HOH 350 950  483 HOH HOH A . 
N 6 HOH 351 951  351 HOH HOH A . 
N 6 HOH 352 952  279 HOH HOH A . 
N 6 HOH 353 953  374 HOH HOH A . 
N 6 HOH 354 954  495 HOH HOH A . 
N 6 HOH 355 955  113 HOH HOH A . 
N 6 HOH 356 956  356 HOH HOH A . 
N 6 HOH 357 957  390 HOH HOH A . 
N 6 HOH 358 958  321 HOH HOH A . 
N 6 HOH 359 959  224 HOH HOH A . 
N 6 HOH 360 960  418 HOH HOH A . 
N 6 HOH 361 961  446 HOH HOH A . 
N 6 HOH 362 962  164 HOH HOH A . 
N 6 HOH 363 963  386 HOH HOH A . 
N 6 HOH 364 964  494 HOH HOH A . 
N 6 HOH 365 965  191 HOH HOH A . 
N 6 HOH 366 966  195 HOH HOH A . 
N 6 HOH 367 967  442 HOH HOH A . 
N 6 HOH 368 968  261 HOH HOH A . 
N 6 HOH 369 969  260 HOH HOH A . 
N 6 HOH 370 970  372 HOH HOH A . 
N 6 HOH 371 971  473 HOH HOH A . 
N 6 HOH 372 972  226 HOH HOH A . 
N 6 HOH 373 973  346 HOH HOH A . 
N 6 HOH 374 974  451 HOH HOH A . 
N 6 HOH 375 975  463 HOH HOH A . 
N 6 HOH 376 976  109 HOH HOH A . 
N 6 HOH 377 977  468 HOH HOH A . 
N 6 HOH 378 978  223 HOH HOH A . 
N 6 HOH 379 979  154 HOH HOH A . 
N 6 HOH 380 980  350 HOH HOH A . 
N 6 HOH 381 981  108 HOH HOH A . 
N 6 HOH 382 982  240 HOH HOH A . 
N 6 HOH 383 983  488 HOH HOH A . 
N 6 HOH 384 984  167 HOH HOH A . 
N 6 HOH 385 985  434 HOH HOH A . 
N 6 HOH 386 986  425 HOH HOH A . 
N 6 HOH 387 987  454 HOH HOH A . 
N 6 HOH 388 988  150 HOH HOH A . 
N 6 HOH 389 989  455 HOH HOH A . 
N 6 HOH 390 990  90  HOH HOH A . 
N 6 HOH 391 991  322 HOH HOH A . 
N 6 HOH 392 992  499 HOH HOH A . 
N 6 HOH 393 993  255 HOH HOH A . 
N 6 HOH 394 994  202 HOH HOH A . 
N 6 HOH 395 995  373 HOH HOH A . 
N 6 HOH 396 996  253 HOH HOH A . 
N 6 HOH 397 997  112 HOH HOH A . 
N 6 HOH 398 998  312 HOH HOH A . 
N 6 HOH 399 999  287 HOH HOH A . 
N 6 HOH 400 1000 344 HOH HOH A . 
N 6 HOH 401 1001 363 HOH HOH A . 
N 6 HOH 402 1002 378 HOH HOH A . 
N 6 HOH 403 1003 412 HOH HOH A . 
N 6 HOH 404 1004 479 HOH HOH A . 
N 6 HOH 405 1005 362 HOH HOH A . 
N 6 HOH 406 1006 481 HOH HOH A . 
N 6 HOH 407 1007 254 HOH HOH A . 
N 6 HOH 408 1008 394 HOH HOH A . 
N 6 HOH 409 1009 477 HOH HOH A . 
N 6 HOH 410 1010 492 HOH HOH A . 
N 6 HOH 411 1011 500 HOH HOH A . 
N 6 HOH 412 1012 275 HOH HOH A . 
N 6 HOH 413 1013 371 HOH HOH A . 
N 6 HOH 414 1014 376 HOH HOH A . 
N 6 HOH 415 1015 453 HOH HOH A . 
N 6 HOH 416 1016 493 HOH HOH A . 
N 6 HOH 417 1017 87  HOH HOH A . 
N 6 HOH 418 1018 331 HOH HOH A . 
N 6 HOH 419 1019 110 HOH HOH A . 
N 6 HOH 420 1020 408 HOH HOH A . 
N 6 HOH 421 1021 266 HOH HOH A . 
N 6 HOH 422 1022 444 HOH HOH A . 
N 6 HOH 423 1023 192 HOH HOH A . 
N 6 HOH 424 1024 335 HOH HOH A . 
N 6 HOH 425 1025 383 HOH HOH A . 
N 6 HOH 426 1026 333 HOH HOH A . 
N 6 HOH 427 1027 364 HOH HOH A . 
N 6 HOH 428 1028 152 HOH HOH A . 
N 6 HOH 429 1029 423 HOH HOH A . 
N 6 HOH 430 1030 332 HOH HOH A . 
N 6 HOH 431 1031 484 HOH HOH A . 
N 6 HOH 432 1032 354 HOH HOH A . 
N 6 HOH 433 1033 107 HOH HOH A . 
N 6 HOH 434 1034 200 HOH HOH A . 
N 6 HOH 435 1035 427 HOH HOH A . 
N 6 HOH 436 1036 114 HOH HOH A . 
N 6 HOH 437 1037 486 HOH HOH A . 
N 6 HOH 438 1038 381 HOH HOH A . 
N 6 HOH 439 1039 476 HOH HOH A . 
N 6 HOH 440 1040 475 HOH HOH A . 
N 6 HOH 441 1041 501 HOH HOH A . 
N 6 HOH 442 1042 424 HOH HOH A . 
N 6 HOH 443 1043 461 HOH HOH A . 
N 6 HOH 444 1044 282 HOH HOH A . 
N 6 HOH 445 1045 169 HOH HOH A . 
N 6 HOH 446 1046 345 HOH HOH A . 
N 6 HOH 447 1047 329 HOH HOH A . 
N 6 HOH 448 1048 263 HOH HOH A . 
N 6 HOH 449 1049 460 HOH HOH A . 
N 6 HOH 450 1050 246 HOH HOH A . 
N 6 HOH 451 1051 111 HOH HOH A . 
N 6 HOH 452 1052 472 HOH HOH A . 
N 6 HOH 453 1053 400 HOH HOH A . 
N 6 HOH 454 1054 375 HOH HOH A . 
N 6 HOH 455 1055 406 HOH HOH A . 
N 6 HOH 456 1056 459 HOH HOH A . 
N 6 HOH 457 1057 433 HOH HOH A . 
N 6 HOH 458 1058 323 HOH HOH A . 
N 6 HOH 459 1059 471 HOH HOH A . 
N 6 HOH 460 1060 259 HOH HOH A . 
N 6 HOH 461 1061 338 HOH HOH A . 
N 6 HOH 462 1062 405 HOH HOH A . 
N 6 HOH 463 1063 296 HOH HOH A . 
N 6 HOH 464 1064 357 HOH HOH A . 
N 6 HOH 465 1065 438 HOH HOH A . 
N 6 HOH 466 1066 440 HOH HOH A . 
N 6 HOH 467 1067 243 HOH HOH A . 
N 6 HOH 468 1068 466 HOH HOH A . 
N 6 HOH 469 1069 288 HOH HOH A . 
N 6 HOH 470 1070 324 HOH HOH A . 
N 6 HOH 471 1071 413 HOH HOH A . 
N 6 HOH 472 1072 145 HOH HOH A . 
N 6 HOH 473 1073 89  HOH HOH A . 
N 6 HOH 474 1074 447 HOH HOH A . 
N 6 HOH 475 1075 340 HOH HOH A . 
N 6 HOH 476 1076 286 HOH HOH A . 
N 6 HOH 477 1077 176 HOH HOH A . 
N 6 HOH 478 1078 326 HOH HOH A . 
N 6 HOH 479 1079 480 HOH HOH A . 
N 6 HOH 480 1080 116 HOH HOH A . 
N 6 HOH 481 1081 439 HOH HOH A . 
N 6 HOH 482 1082 478 HOH HOH A . 
N 6 HOH 483 1083 449 HOH HOH A . 
N 6 HOH 484 1084 320 HOH HOH A . 
N 6 HOH 485 1085 258 HOH HOH A . 
N 6 HOH 486 1086 441 HOH HOH A . 
N 6 HOH 487 1087 190 HOH HOH A . 
N 6 HOH 488 1088 64  HOH HOH A . 
N 6 HOH 489 1089 325 HOH HOH A . 
N 6 HOH 490 1090 437 HOH HOH A . 
N 6 HOH 491 1091 293 HOH HOH A . 
N 6 HOH 492 1092 382 HOH HOH A . 
N 6 HOH 493 1093 498 HOH HOH A . 
N 6 HOH 494 1094 328 HOH HOH A . 
N 6 HOH 495 1095 181 HOH HOH A . 
N 6 HOH 496 1096 262 HOH HOH A . 
N 6 HOH 497 1097 101 HOH HOH A . 
N 6 HOH 498 1098 445 HOH HOH A . 
N 6 HOH 499 1099 352 HOH HOH A . 
N 6 HOH 500 1100 485 HOH HOH A . 
N 6 HOH 501 1101 456 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        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(1.18.2_3874: ???)' 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? 7.21                 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? 7.21                 3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? 2.7.0                4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27                 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.87 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YLY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.244 
_cell.length_a_esd                 ? 
_cell.length_b                     86.938 
_cell.length_b_esd                 ? 
_cell.length_c                     61.255 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8YLY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YLY 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.34 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.18 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.8 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.085 M  HEPES sodium pH 7.5, 1.7% v/v Polyethylene glycol 400, 1.7 M Ammonium sulfate, 15% v/v Glycerol' 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_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                        'NFPSS BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       NFPSS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YLY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.49 
_reflns.d_resolution_low                               60.93 
_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                                     90042 
_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                           95.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.85 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.052 
_reflns.pdbx_Rpim_I_all                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       403107 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.046 
_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                                    1.49 
_reflns_shell.d_res_low                                     1.57 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           47566 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             13636 
_reflns_shell.percent_possible_obs                          99.1 
_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                               3.5 
_reflns_shell.pdbx_chi_squared                              0.58 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.7 
_reflns_shell.pdbx_Rrim_I_all                               0.525 
_reflns_shell.pdbx_Rpim_I_all                               0.275 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.786 
_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                                  0.442 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8YLY 
_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                            1.49 
_refine.ls_d_res_low                             30.47 
_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                     89999 
_refine.ls_number_reflns_R_free                  4455 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.35 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1771 
_refine.ls_R_factor_R_free                       0.1927 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1763 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.96 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.49 
_refine_hist.d_res_low                        30.47 
_refine_hist.number_atoms_solvent             501 
_refine_hist.number_atoms_total               3646 
_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        3134 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         11 
_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' ? 0.016  ? 3187 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.623  ? 4307 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.006 ? 1185 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.109  ? 494  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.012  ? 556  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.49 1.50  . . 151 2909 98.00  . . . . 0.2772 . . . . . . . . . . . 0.2901 
'X-RAY DIFFRACTION' 1.50 1.52  . . 133 2994 99.00  . . . . 0.2466 . . . . . . . . . . . 0.2692 
'X-RAY DIFFRACTION' 1.52 1.54  . . 146 2990 99.00  . . . . 0.2342 . . . . . . . . . . . 0.2418 
'X-RAY DIFFRACTION' 1.54 1.56  . . 138 2948 99.00  . . . . 0.2279 . . . . . . . . . . . 0.2555 
'X-RAY DIFFRACTION' 1.56 1.58  . . 161 2990 100.00 . . . . 0.2287 . . . . . . . . . . . 0.2269 
'X-RAY DIFFRACTION' 1.58 1.60  . . 170 2941 100.00 . . . . 0.2189 . . . . . . . . . . . 0.2444 
'X-RAY DIFFRACTION' 1.60 1.62  . . 146 2985 100.00 . . . . 0.2113 . . . . . . . . . . . 0.2251 
'X-RAY DIFFRACTION' 1.62 1.65  . . 144 2963 100.00 . . . . 0.2047 . . . . . . . . . . . 0.2204 
'X-RAY DIFFRACTION' 1.65 1.67  . . 145 3027 100.00 . . . . 0.2034 . . . . . . . . . . . 0.2038 
'X-RAY DIFFRACTION' 1.67 1.70  . . 131 2999 100.00 . . . . 0.2011 . . . . . . . . . . . 0.2296 
'X-RAY DIFFRACTION' 1.70 1.73  . . 160 2959 100.00 . . . . 0.1982 . . . . . . . . . . . 0.2258 
'X-RAY DIFFRACTION' 1.73 1.76  . . 143 2963 100.00 . . . . 0.2012 . . . . . . . . . . . 0.1984 
'X-RAY DIFFRACTION' 1.76 1.80  . . 155 2997 100.00 . . . . 0.1958 . . . . . . . . . . . 0.2611 
'X-RAY DIFFRACTION' 1.80 1.83  . . 162 2990 100.00 . . . . 0.2004 . . . . . . . . . . . 0.2006 
'X-RAY DIFFRACTION' 1.83 1.87  . . 154 2972 100.00 . . . . 0.1924 . . . . . . . . . . . 0.2256 
'X-RAY DIFFRACTION' 1.87 1.91  . . 140 2397 95.00  . . . . 0.1871 . . . . . . . . . . . 0.1921 
'X-RAY DIFFRACTION' 1.92 1.97  . . 139 2526 100.00 . . . . 0.1851 . . . . . . . . . . . 0.2077 
'X-RAY DIFFRACTION' 1.97 2.02  . . 169 2965 100.00 . . . . 0.1866 . . . . . . . . . . . 0.1976 
'X-RAY DIFFRACTION' 2.02 2.06  . . 115 1967 97.00  . . . . 0.1839 . . . . . . . . . . . 0.1913 
'X-RAY DIFFRACTION' 2.08 2.14  . . 150 2625 100.00 . . . . 0.1799 . . . . . . . . . . . 0.1813 
'X-RAY DIFFRACTION' 2.14 2.22  . . 161 2999 100.00 . . . . 0.1817 . . . . . . . . . . . 0.1940 
'X-RAY DIFFRACTION' 2.22 2.31  . . 107 1972 66.00  . . . . 0.1759 . . . . . . . . . . . 0.2020 
'X-RAY DIFFRACTION' 2.31 2.42  . . 141 2993 100.00 . . . . 0.1785 . . . . . . . . . . . 0.1864 
'X-RAY DIFFRACTION' 2.42 2.54  . . 153 3003 100.00 . . . . 0.1874 . . . . . . . . . . . 0.2161 
'X-RAY DIFFRACTION' 2.54 2.70  . . 165 2975 100.00 . . . . 0.1825 . . . . . . . . . . . 0.2026 
'X-RAY DIFFRACTION' 2.70 2.91  . . 160 2993 100.00 . . . . 0.1750 . . . . . . . . . . . 0.1966 
'X-RAY DIFFRACTION' 2.91 3.20  . . 176 2961 99.00  . . . . 0.1697 . . . . . . . . . . . 0.1790 
'X-RAY DIFFRACTION' 3.20 3.64  . . 154 2814 98.00  . . . . 0.1562 . . . . . . . . . . . 0.1795 
'X-RAY DIFFRACTION' 3.69 4.61  . . 137 2691 92.00  . . . . 0.1386 . . . . . . . . . . . 0.1502 
'X-RAY DIFFRACTION' 4.62 30.47 . . 149 3036 99.00  . . . . 0.1659 . . . . . . . . . . . 0.1844 
# 
_struct.entry_id                     8YLY 
_struct.title                        
'Structural basis of Elongation factor Tu in regulating photoinhibition in Synechococcus sp. PCC 7942.' 
_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        8YLY 
_struct_keywords.text            'Elongation factor, Synechococcus PCC 7942, photosystem 2, photoremediation, PHOTOSYNTHESIS' 
_struct_keywords.pdbx_keywords   PHOTOSYNTHESIS 
# 
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 ? 
E N N 3 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
K N N 2 ? 
L N N 2 ? 
M N N 5 ? 
N N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    EFTU_SYNP6 
_struct_ref.pdbx_db_accession          P18668 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ARAKFERTKPHANIGTIGHVDHGKTTLTAAITTVLAKAGMAKARAYADIDAAPEEKARGITINTAHVEYETGNRHYAHVD
CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPNIVVFLNKEDMVDDAELLELVELEVRELLSSY
DFPGDDIPIVAGSALQALEAIQGGASGQKGDNPWVDKILKLMEEVDAYIPTPEREVDRPFLMAVEDVFTITGRGTVATGR
IERGSVKVGETIEIVGLRDTRSTTVTGVEMFQKTLDEGLAGDNVGLLLRGIQKTDIERGMVLAKPGSITPHTKFESEVYV
LKKEEGGRHTPFFPGYRPQFYVRTTDVTGAISDFTADDGSAAEMVIPGDRIKMTVELINPIAIEQGMRFAIREGGRTIGA
GVVSKILQ
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YLY 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 408 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P18668 
_struct_ref_seq.db_align_beg                  2 
_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       409 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_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 23  ? ALA A 38  ? GLY A 24  ALA A 39  1 ? 16 
HELX_P HELX_P2  AA2 ALA A 45  ? ALA A 51  ? ALA A 46  ALA A 52  1 ? 7  
HELX_P HELX_P3  AA3 GLY A 83  ? GLY A 94  ? GLY A 84  GLY A 95  1 ? 12 
HELX_P HELX_P4  AA4 MET A 112 ? GLY A 126 ? MET A 113 GLY A 127 1 ? 15 
HELX_P HELX_P5  AA5 LYS A 136 ? VAL A 140 ? LYS A 137 VAL A 141 5 ? 5  
HELX_P HELX_P6  AA6 ASP A 142 ? TYR A 160 ? ASP A 143 TYR A 161 1 ? 19 
HELX_P HELX_P7  AA7 SER A 173 ? GLY A 183 ? SER A 174 GLY A 184 1 ? 11 
HELX_P HELX_P8  AA8 ASN A 192 ? ILE A 209 ? ASN A 193 ILE A 210 1 ? 18 
HELX_P HELX_P9  AA9 ARG A 214 ? ARG A 218 ? ARG A 215 ARG A 219 5 ? 5  
HELX_P HELX_P10 AB1 GLN A 292 ? ILE A 296 ? GLN A 293 ILE A 297 5 ? 5  
HELX_P HELX_P11 AB2 LYS A 322 ? GLY A 326 ? LYS A 323 GLY A 327 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A THR 25 OG1 ? ? ? 1_555 M MG  . MG ? ? A THR 26  A MG  512 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc2 metalc ? ? D GDP .  O3B ? ? ? 1_555 M MG  . MG ? ? A GDP 503 A MG  512 1_555 ? ? ? ? ? ? ? 2.090 ? ? 
metalc3 metalc ? ? M MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? A MG  512 A HOH 688 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc4 metalc ? ? M MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? A MG  512 A HOH 696 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
metalc5 metalc ? ? M MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? A MG  512 A HOH 699 1_555 ? ? ? ? ? ? ? 2.110 ? ? 
metalc6 metalc ? ? M MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? A MG  512 A HOH 830 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG1 ? A THR 25 ? A THR 26  ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O3B ? D GDP . ? A GDP 503 ? 1_555 93.5  ? 
2  OG1 ? A THR 25 ? A THR 26  ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 688 ? 1_555 174.1 ? 
3  O3B ? D GDP .  ? A GDP 503 ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 688 ? 1_555 89.9  ? 
4  OG1 ? A THR 25 ? A THR 26  ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 696 ? 1_555 84.0  ? 
5  O3B ? D GDP .  ? A GDP 503 ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 696 ? 1_555 92.5  ? 
6  O   ? N HOH .  ? A HOH 688 ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 696 ? 1_555 91.1  ? 
7  OG1 ? A THR 25 ? A THR 26  ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 699 ? 1_555 91.7  ? 
8  O3B ? D GDP .  ? A GDP 503 ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 699 ? 1_555 88.6  ? 
9  O   ? N HOH .  ? A HOH 688 ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 699 ? 1_555 93.2  ? 
10 O   ? N HOH .  ? A HOH 696 ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 699 ? 1_555 175.6 ? 
11 OG1 ? A THR 25 ? A THR 26  ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 830 ? 1_555 86.8  ? 
12 O3B ? D GDP .  ? A GDP 503 ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 830 ? 1_555 173.8 ? 
13 O   ? N HOH .  ? A HOH 688 ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 830 ? 1_555 90.2  ? 
14 O   ? N HOH .  ? A HOH 696 ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 830 ? 1_555 93.6  ? 
15 O   ? N HOH .  ? A HOH 699 ? 1_555 MG ? M MG . ? A MG 512 ? 1_555 O   ? N HOH . ? A HOH 830 ? 1_555 85.2  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? 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 ALA A 65  ? GLU A 70  ? ALA A 66  GLU A 71  
AA1 2 HIS A 75  ? ASP A 80  ? HIS A 76  ASP A 81  
AA1 3 HIS A 11  ? ILE A 17  ? HIS A 12  ILE A 18  
AA1 4 ALA A 101 ? SER A 106 ? ALA A 102 SER A 107 
AA1 5 ILE A 130 ? ASN A 135 ? ILE A 131 ASN A 136 
AA1 6 ILE A 169 ? ALA A 171 ? ILE A 170 ALA A 172 
AA2 1 GLU A 54  ? ALA A 57  ? GLU A 55  ALA A 58  
AA2 2 ILE A 60  ? ASN A 63  ? ILE A 61  ASN A 64  
AA3 1 ASP A 226 ? PHE A 228 ? ASP A 227 PHE A 229 
AA3 2 GLY A 234 ? ARG A 243 ? GLY A 235 ARG A 244 
AA3 3 LEU A 221 ? ALA A 223 ? LEU A 222 ALA A 224 
AA3 4 VAL A 301 ? ALA A 303 ? VAL A 302 ALA A 304 
AA3 5 THR A 251 ? VAL A 255 ? THR A 252 VAL A 256 
AA3 6 ARG A 261 ? MET A 270 ? ARG A 262 MET A 271 
AA3 7 LYS A 273 ? LEU A 275 ? LYS A 274 LEU A 276 
AA4 1 ASP A 226 ? PHE A 228 ? ASP A 227 PHE A 229 
AA4 2 GLY A 234 ? ARG A 243 ? GLY A 235 ARG A 244 
AA4 3 ASN A 283 ? ARG A 289 ? ASN A 284 ARG A 290 
AA4 4 ARG A 261 ? MET A 270 ? ARG A 262 MET A 271 
AA4 5 LYS A 273 ? LEU A 275 ? LYS A 274 LEU A 276 
AA5 1 SER A 245 ? LYS A 247 ? SER A 246 LYS A 248 
AA5 2 GLU A 277 ? LEU A 279 ? GLU A 278 LEU A 280 
AA6 1 THR A 309 ? VAL A 320 ? THR A 310 VAL A 321 
AA6 2 ARG A 370 ? ILE A 383 ? ARG A 371 ILE A 384 
AA6 3 THR A 345 ? THR A 355 ? THR A 346 THR A 356 
AA6 4 GLN A 339 ? VAL A 342 ? GLN A 340 VAL A 343 
AA6 5 ARG A 388 ? GLU A 393 ? ARG A 389 GLU A 394 
AA6 6 ARG A 396 ? GLN A 408 ? ARG A 397 GLN A 409 
AA6 7 THR A 309 ? VAL A 320 ? THR A 310 VAL A 321 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TYR A 69  ? N TYR A 70  O TYR A 76  ? O TYR A 77  
AA1 2 3 O ALA A 77  ? O ALA A 78  N ILE A 14  ? N ILE A 15  
AA1 3 4 N GLY A 15  ? N GLY A 16  O ILE A 102 ? O ILE A 103 
AA1 4 5 N LEU A 103 ? N LEU A 104 O VAL A 131 ? O VAL A 132 
AA1 5 6 N VAL A 132 ? N VAL A 133 O VAL A 170 ? O VAL A 171 
AA2 1 2 N GLU A 55  ? N GLU A 56  O ILE A 62  ? O ILE A 63  
AA3 1 2 N PHE A 228 ? N PHE A 229 O VAL A 236 ? O VAL A 237 
AA3 2 3 O GLU A 242 ? O GLU A 243 N LEU A 221 ? N LEU A 222 
AA3 3 4 N MET A 222 ? N MET A 223 O LEU A 302 ? O LEU A 303 
AA3 4 5 O ALA A 303 ? O ALA A 304 N GLU A 253 ? N GLU A 254 
AA3 5 6 N ILE A 254 ? N ILE A 255 O ARG A 261 ? O ARG A 262 
AA3 6 7 N VAL A 268 ? N VAL A 269 O LEU A 275 ? O LEU A 276 
AA4 1 2 N PHE A 228 ? N PHE A 229 O VAL A 236 ? O VAL A 237 
AA4 2 3 N ALA A 237 ? N ALA A 238 O LEU A 286 ? O LEU A 287 
AA4 3 4 O ARG A 289 ? O ARG A 290 N THR A 264 ? N THR A 265 
AA4 4 5 N VAL A 268 ? N VAL A 269 O LEU A 275 ? O LEU A 276 
AA5 1 2 N VAL A 246 ? N VAL A 247 O GLY A 278 ? O GLY A 279 
AA6 1 2 N THR A 312 ? N THR A 313 O LEU A 377 ? O LEU A 378 
AA6 2 3 O THR A 374 ? O THR A 375 N SER A 352 ? N SER A 353 
AA6 3 4 O VAL A 347 ? O VAL A 348 N PHE A 340 ? N PHE A 341 
AA6 4 5 N GLN A 339 ? N GLN A 340 O ARG A 392 ? O ARG A 393 
AA6 5 6 N ILE A 391 ? N ILE A 392 O ILE A 398 ? O ILE A 399 
AA6 6 7 O LYS A 405 ? O LYS A 406 N GLU A 315 ? N GLU A 316 
# 
_pdbx_entry_details.entry_id                   8YLY 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 C2  A GOL 510  ? ? O  A HOH 602  ? ? 0.45 
2  1 O3  A GOL 510  ? ? O  A HOH 601  ? ? 0.85 
3  1 C1  A GOL 510  ? ? O  A HOH 602  ? ? 1.26 
4  1 O   A HOH 1003 ? ? O  A HOH 1041 ? ? 1.31 
5  1 O2  A GOL 510  ? ? O  A HOH 602  ? ? 1.39 
6  1 O   A HOH 954  ? ? O  A HOH 964  ? ? 1.60 
7  1 CB  A ALA 58   ? ? S2 A BME 502  ? ? 1.77 
8  1 O   A HOH 992  ? ? O  A HOH 1093 ? ? 1.84 
9  1 O   A HOH 849  ? ? O  A HOH 1002 ? ? 1.84 
10 1 O   A HOH 641  ? ? O  A HOH 963  ? ? 1.85 
11 1 O   A HOH 759  ? ? O  A HOH 838  ? ? 1.85 
12 1 O   A HOH 708  ? ? O  A HOH 980  ? ? 1.90 
13 1 O   A HOH 1032 ? ? O  A HOH 1055 ? ? 1.92 
14 1 O   A HOH 759  ? ? O  A HOH 1002 ? ? 1.94 
15 1 N   A GLY 300  ? ? O  A HOH 603  ? ? 1.95 
16 1 C3  A GOL 510  ? ? O  A HOH 602  ? ? 1.95 
17 1 OE1 A GLU 151  ? ? O  A HOH 604  ? ? 1.98 
18 1 O   A HOH 990  ? ? O  A HOH 1001 ? ? 2.00 
19 1 O   A HOH 879  ? ? O  A HOH 1049 ? ? 2.02 
20 1 O   A HOH 995  ? ? O  A HOH 1054 ? ? 2.02 
21 1 OE1 A GLU 55   ? ? O  A HOH 605  ? ? 2.03 
22 1 O   A HOH 848  ? ? O  A HOH 863  ? ? 2.04 
23 1 O   A HOH 601  ? ? O  A HOH 774  ? ? 2.05 
24 1 O1  A GOL 510  ? ? O  A HOH 602  ? ? 2.11 
25 1 O   A HOH 792  ? ? O  A HOH 1072 ? ? 2.11 
26 1 O   A HOH 629  ? ? O  A HOH 891  ? ? 2.11 
27 1 O   A HOH 611  ? ? O  A HOH 795  ? ? 2.12 
28 1 O   A HOH 885  ? ? O  A HOH 948  ? ? 2.12 
29 1 C3  A GOL 510  ? ? O  A HOH 601  ? ? 2.13 
30 1 O   A HOH 883  ? ? O  A HOH 1024 ? ? 2.13 
31 1 OE1 A GLU 205  ? ? O  A HOH 606  ? ? 2.13 
32 1 O   A HOH 944  ? ? O  A HOH 1081 ? ? 2.14 
33 1 O   A HOH 719  ? ? O  A HOH 939  ? ? 2.14 
34 1 O   A HOH 1035 ? ? O  A HOH 1036 ? ? 2.14 
35 1 O   A HOH 684  ? ? O  A HOH 1051 ? ? 2.15 
36 1 O   A HOH 950  ? ? O  A HOH 1079 ? ? 2.15 
37 1 O   A HOH 921  ? ? O  A HOH 957  ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 1079 ? ? 1_555 O A HOH 1082 ? ? 1_655 2.17 
2 1 O A HOH 753  ? ? 1_555 O A HOH 809  ? ? 2_546 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CB A TYR 70  ? ? CG A TYR 70  ? ? CD2 A TYR 70  ? ? 116.26 121.00 -4.74  0.60 N 
2  1 CB A LEU 149 ? ? CG A LEU 149 ? ? CD2 A LEU 149 ? ? 122.65 111.00 11.65  1.70 N 
3  1 NE A ARG 155 ? ? CZ A ARG 155 ? ? NH2 A ARG 155 ? ? 115.70 120.30 -4.60  0.50 N 
4  1 CB A ASP 207 ? ? CG A ASP 207 ? ? OD1 A ASP 207 ? ? 124.21 118.30 5.91   0.90 N 
5  1 CB A PHE 315 ? ? CG A PHE 315 ? ? CD2 A PHE 315 ? ? 115.53 120.80 -5.27  0.70 N 
6  1 CB A PHE 334 ? ? CG A PHE 334 ? ? CD2 A PHE 334 ? ? 113.39 120.80 -7.41  0.70 N 
7  1 CB A PHE 334 ? ? CG A PHE 334 ? ? CD1 A PHE 334 ? ? 127.17 120.80 6.37   0.70 N 
8  1 NE A ARG 344 ? ? CZ A ARG 344 ? ? NH1 A ARG 344 ? ? 123.88 120.30 3.58   0.50 N 
9  1 NE A ARG 344 ? ? CZ A ARG 344 ? ? NH2 A ARG 344 ? ? 116.78 120.30 -3.52  0.50 N 
10 1 CG A MET 365 ? ? SD A MET 365 ? ? CE  A MET 365 ? ? 115.71 100.20 15.51  1.60 N 
11 1 CG A ARG 371 ? ? CD A ARG 371 ? ? NE  A ARG 371 ? ? 98.55  111.80 -13.25 2.10 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 ALA A 58  ? ? -160.08 119.00 
2 1 LEU A 258 ? ? 68.29   -36.43 
3 1 ARG A 344 ? ? 66.89   -48.24 
4 1 THR A 345 ? ? -142.57 -11.52 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
_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                       1101 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.34 
_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 ALA 2 ? A ALA 1 
2 1 Y 1 A ARG 3 ? A ARG 2 
3 1 Y 1 A ALA 4 ? A ALA 3 
4 1 Y 1 A LYS 5 ? A LYS 4 
# 
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  
BME C1     C  N N 74  
BME C2     C  N N 75  
BME O1     O  N N 76  
BME S2     S  N N 77  
BME H11    H  N N 78  
BME H12    H  N N 79  
BME H21    H  N N 80  
BME H22    H  N N 81  
BME HO1    H  N N 82  
BME HS2    H  N N 83  
CYS N      N  N N 84  
CYS CA     C  N R 85  
CYS C      C  N N 86  
CYS O      O  N N 87  
CYS CB     C  N N 88  
CYS SG     S  N N 89  
CYS OXT    O  N N 90  
CYS H      H  N N 91  
CYS H2     H  N N 92  
CYS HA     H  N N 93  
CYS HB2    H  N N 94  
CYS HB3    H  N N 95  
CYS HG     H  N N 96  
CYS HXT    H  N N 97  
GDP PB     P  N N 98  
GDP O1B    O  N N 99  
GDP O2B    O  N N 100 
GDP O3B    O  N N 101 
GDP O3A    O  N N 102 
GDP PA     P  N N 103 
GDP O1A    O  N N 104 
GDP O2A    O  N N 105 
GDP "O5'"  O  N N 106 
GDP "C5'"  C  N N 107 
GDP "C4'"  C  N R 108 
GDP "O4'"  O  N N 109 
GDP "C3'"  C  N S 110 
GDP "O3'"  O  N N 111 
GDP "C2'"  C  N R 112 
GDP "O2'"  O  N N 113 
GDP "C1'"  C  N R 114 
GDP N9     N  Y N 115 
GDP C8     C  Y N 116 
GDP N7     N  Y N 117 
GDP C5     C  Y N 118 
GDP C6     C  N N 119 
GDP O6     O  N N 120 
GDP N1     N  N N 121 
GDP C2     C  N N 122 
GDP N2     N  N N 123 
GDP N3     N  N N 124 
GDP C4     C  Y N 125 
GDP HOB2   H  N N 126 
GDP HOB3   H  N N 127 
GDP HOA2   H  N N 128 
GDP "H5'"  H  N N 129 
GDP "H5''" H  N N 130 
GDP "H4'"  H  N N 131 
GDP "H3'"  H  N N 132 
GDP "HO3'" H  N N 133 
GDP "H2'"  H  N N 134 
GDP "HO2'" H  N N 135 
GDP "H1'"  H  N N 136 
GDP H8     H  N N 137 
GDP HN1    H  N N 138 
GDP HN21   H  N N 139 
GDP HN22   H  N N 140 
GLN N      N  N N 141 
GLN CA     C  N S 142 
GLN C      C  N N 143 
GLN O      O  N N 144 
GLN CB     C  N N 145 
GLN CG     C  N N 146 
GLN CD     C  N N 147 
GLN OE1    O  N N 148 
GLN NE2    N  N N 149 
GLN OXT    O  N N 150 
GLN H      H  N N 151 
GLN H2     H  N N 152 
GLN HA     H  N N 153 
GLN HB2    H  N N 154 
GLN HB3    H  N N 155 
GLN HG2    H  N N 156 
GLN HG3    H  N N 157 
GLN HE21   H  N N 158 
GLN HE22   H  N N 159 
GLN HXT    H  N N 160 
GLU N      N  N N 161 
GLU CA     C  N S 162 
GLU C      C  N N 163 
GLU O      O  N N 164 
GLU CB     C  N N 165 
GLU CG     C  N N 166 
GLU CD     C  N N 167 
GLU OE1    O  N N 168 
GLU OE2    O  N N 169 
GLU OXT    O  N N 170 
GLU H      H  N N 171 
GLU H2     H  N N 172 
GLU HA     H  N N 173 
GLU HB2    H  N N 174 
GLU HB3    H  N N 175 
GLU HG2    H  N N 176 
GLU HG3    H  N N 177 
GLU HE2    H  N N 178 
GLU HXT    H  N N 179 
GLY N      N  N N 180 
GLY CA     C  N N 181 
GLY C      C  N N 182 
GLY O      O  N N 183 
GLY OXT    O  N N 184 
GLY H      H  N N 185 
GLY H2     H  N N 186 
GLY HA2    H  N N 187 
GLY HA3    H  N N 188 
GLY HXT    H  N N 189 
GOL C1     C  N N 190 
GOL O1     O  N N 191 
GOL C2     C  N N 192 
GOL O2     O  N N 193 
GOL C3     C  N N 194 
GOL O3     O  N N 195 
GOL H11    H  N N 196 
GOL H12    H  N N 197 
GOL HO1    H  N N 198 
GOL H2     H  N N 199 
GOL HO2    H  N N 200 
GOL H31    H  N N 201 
GOL H32    H  N N 202 
GOL HO3    H  N N 203 
HIS N      N  N N 204 
HIS CA     C  N S 205 
HIS C      C  N N 206 
HIS O      O  N N 207 
HIS CB     C  N N 208 
HIS CG     C  Y N 209 
HIS ND1    N  Y N 210 
HIS CD2    C  Y N 211 
HIS CE1    C  Y N 212 
HIS NE2    N  Y N 213 
HIS OXT    O  N N 214 
HIS H      H  N N 215 
HIS H2     H  N N 216 
HIS HA     H  N N 217 
HIS HB2    H  N N 218 
HIS HB3    H  N N 219 
HIS HD1    H  N N 220 
HIS HD2    H  N N 221 
HIS HE1    H  N N 222 
HIS HE2    H  N N 223 
HIS HXT    H  N N 224 
HOH O      O  N N 225 
HOH H1     H  N N 226 
HOH H2     H  N N 227 
ILE N      N  N N 228 
ILE CA     C  N S 229 
ILE C      C  N N 230 
ILE O      O  N N 231 
ILE CB     C  N S 232 
ILE CG1    C  N N 233 
ILE CG2    C  N N 234 
ILE CD1    C  N N 235 
ILE OXT    O  N N 236 
ILE H      H  N N 237 
ILE H2     H  N N 238 
ILE HA     H  N N 239 
ILE HB     H  N N 240 
ILE HG12   H  N N 241 
ILE HG13   H  N N 242 
ILE HG21   H  N N 243 
ILE HG22   H  N N 244 
ILE HG23   H  N N 245 
ILE HD11   H  N N 246 
ILE HD12   H  N N 247 
ILE HD13   H  N N 248 
ILE HXT    H  N N 249 
LEU N      N  N N 250 
LEU CA     C  N S 251 
LEU C      C  N N 252 
LEU O      O  N N 253 
LEU CB     C  N N 254 
LEU CG     C  N N 255 
LEU CD1    C  N N 256 
LEU CD2    C  N N 257 
LEU OXT    O  N N 258 
LEU H      H  N N 259 
LEU H2     H  N N 260 
LEU HA     H  N N 261 
LEU HB2    H  N N 262 
LEU HB3    H  N N 263 
LEU HG     H  N N 264 
LEU HD11   H  N N 265 
LEU HD12   H  N N 266 
LEU HD13   H  N N 267 
LEU HD21   H  N N 268 
LEU HD22   H  N N 269 
LEU HD23   H  N N 270 
LEU HXT    H  N N 271 
LYS N      N  N N 272 
LYS CA     C  N S 273 
LYS C      C  N N 274 
LYS O      O  N N 275 
LYS CB     C  N N 276 
LYS CG     C  N N 277 
LYS CD     C  N N 278 
LYS CE     C  N N 279 
LYS NZ     N  N N 280 
LYS OXT    O  N N 281 
LYS H      H  N N 282 
LYS H2     H  N N 283 
LYS HA     H  N N 284 
LYS HB2    H  N N 285 
LYS HB3    H  N N 286 
LYS HG2    H  N N 287 
LYS HG3    H  N N 288 
LYS HD2    H  N N 289 
LYS HD3    H  N N 290 
LYS HE2    H  N N 291 
LYS HE3    H  N N 292 
LYS HZ1    H  N N 293 
LYS HZ2    H  N N 294 
LYS HZ3    H  N N 295 
LYS HXT    H  N N 296 
MET N      N  N N 297 
MET CA     C  N S 298 
MET C      C  N N 299 
MET O      O  N N 300 
MET CB     C  N N 301 
MET CG     C  N N 302 
MET SD     S  N N 303 
MET CE     C  N N 304 
MET OXT    O  N N 305 
MET H      H  N N 306 
MET H2     H  N N 307 
MET HA     H  N N 308 
MET HB2    H  N N 309 
MET HB3    H  N N 310 
MET HG2    H  N N 311 
MET HG3    H  N N 312 
MET HE1    H  N N 313 
MET HE2    H  N N 314 
MET HE3    H  N N 315 
MET HXT    H  N N 316 
MG  MG     MG N N 317 
PHE N      N  N N 318 
PHE CA     C  N S 319 
PHE C      C  N N 320 
PHE O      O  N N 321 
PHE CB     C  N N 322 
PHE CG     C  Y N 323 
PHE CD1    C  Y N 324 
PHE CD2    C  Y N 325 
PHE CE1    C  Y N 326 
PHE CE2    C  Y N 327 
PHE CZ     C  Y N 328 
PHE OXT    O  N N 329 
PHE H      H  N N 330 
PHE H2     H  N N 331 
PHE HA     H  N N 332 
PHE HB2    H  N N 333 
PHE HB3    H  N N 334 
PHE HD1    H  N N 335 
PHE HD2    H  N N 336 
PHE HE1    H  N N 337 
PHE HE2    H  N N 338 
PHE HZ     H  N N 339 
PHE HXT    H  N N 340 
PRO N      N  N N 341 
PRO CA     C  N S 342 
PRO C      C  N N 343 
PRO O      O  N N 344 
PRO CB     C  N N 345 
PRO CG     C  N N 346 
PRO CD     C  N N 347 
PRO OXT    O  N N 348 
PRO H      H  N N 349 
PRO HA     H  N N 350 
PRO HB2    H  N N 351 
PRO HB3    H  N N 352 
PRO HG2    H  N N 353 
PRO HG3    H  N N 354 
PRO HD2    H  N N 355 
PRO HD3    H  N N 356 
PRO HXT    H  N N 357 
SER N      N  N N 358 
SER CA     C  N S 359 
SER C      C  N N 360 
SER O      O  N N 361 
SER CB     C  N N 362 
SER OG     O  N N 363 
SER OXT    O  N N 364 
SER H      H  N N 365 
SER H2     H  N N 366 
SER HA     H  N N 367 
SER HB2    H  N N 368 
SER HB3    H  N N 369 
SER HG     H  N N 370 
SER HXT    H  N N 371 
THR N      N  N N 372 
THR CA     C  N S 373 
THR C      C  N N 374 
THR O      O  N N 375 
THR CB     C  N R 376 
THR OG1    O  N N 377 
THR CG2    C  N N 378 
THR OXT    O  N N 379 
THR H      H  N N 380 
THR H2     H  N N 381 
THR HA     H  N N 382 
THR HB     H  N N 383 
THR HG1    H  N N 384 
THR HG21   H  N N 385 
THR HG22   H  N N 386 
THR HG23   H  N N 387 
THR HXT    H  N N 388 
TRP N      N  N N 389 
TRP CA     C  N S 390 
TRP C      C  N N 391 
TRP O      O  N N 392 
TRP CB     C  N N 393 
TRP CG     C  Y N 394 
TRP CD1    C  Y N 395 
TRP CD2    C  Y N 396 
TRP NE1    N  Y N 397 
TRP CE2    C  Y N 398 
TRP CE3    C  Y N 399 
TRP CZ2    C  Y N 400 
TRP CZ3    C  Y N 401 
TRP CH2    C  Y N 402 
TRP OXT    O  N N 403 
TRP H      H  N N 404 
TRP H2     H  N N 405 
TRP HA     H  N N 406 
TRP HB2    H  N N 407 
TRP HB3    H  N N 408 
TRP HD1    H  N N 409 
TRP HE1    H  N N 410 
TRP HE3    H  N N 411 
TRP HZ2    H  N N 412 
TRP HZ3    H  N N 413 
TRP HH2    H  N N 414 
TRP HXT    H  N N 415 
TYR N      N  N N 416 
TYR CA     C  N S 417 
TYR C      C  N N 418 
TYR O      O  N N 419 
TYR CB     C  N N 420 
TYR CG     C  Y N 421 
TYR CD1    C  Y N 422 
TYR CD2    C  Y N 423 
TYR CE1    C  Y N 424 
TYR CE2    C  Y N 425 
TYR CZ     C  Y N 426 
TYR OH     O  N N 427 
TYR OXT    O  N N 428 
TYR H      H  N N 429 
TYR H2     H  N N 430 
TYR HA     H  N N 431 
TYR HB2    H  N N 432 
TYR HB3    H  N N 433 
TYR HD1    H  N N 434 
TYR HD2    H  N N 435 
TYR HE1    H  N N 436 
TYR HE2    H  N N 437 
TYR HH     H  N N 438 
TYR HXT    H  N N 439 
VAL N      N  N N 440 
VAL CA     C  N S 441 
VAL C      C  N N 442 
VAL O      O  N N 443 
VAL CB     C  N N 444 
VAL CG1    C  N N 445 
VAL CG2    C  N N 446 
VAL OXT    O  N N 447 
VAL H      H  N N 448 
VAL H2     H  N N 449 
VAL HA     H  N N 450 
VAL HB     H  N N 451 
VAL HG11   H  N N 452 
VAL HG12   H  N N 453 
VAL HG13   H  N N 454 
VAL HG21   H  N N 455 
VAL HG22   H  N N 456 
VAL HG23   H  N N 457 
VAL HXT    H  N N 458 
# 
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  
BME C1    C2     sing N N 70  
BME C1    O1     sing N N 71  
BME C1    H11    sing N N 72  
BME C1    H12    sing N N 73  
BME C2    S2     sing N N 74  
BME C2    H21    sing N N 75  
BME C2    H22    sing N N 76  
BME O1    HO1    sing N N 77  
BME S2    HS2    sing N N 78  
CYS N     CA     sing N N 79  
CYS N     H      sing N N 80  
CYS N     H2     sing N N 81  
CYS CA    C      sing N N 82  
CYS CA    CB     sing N N 83  
CYS CA    HA     sing N N 84  
CYS C     O      doub N N 85  
CYS C     OXT    sing N N 86  
CYS CB    SG     sing N N 87  
CYS CB    HB2    sing N N 88  
CYS CB    HB3    sing N N 89  
CYS SG    HG     sing N N 90  
CYS OXT   HXT    sing N N 91  
GDP PB    O1B    doub N N 92  
GDP PB    O2B    sing N N 93  
GDP PB    O3B    sing N N 94  
GDP PB    O3A    sing N N 95  
GDP O2B   HOB2   sing N N 96  
GDP O3B   HOB3   sing N N 97  
GDP O3A   PA     sing N N 98  
GDP PA    O1A    doub N N 99  
GDP PA    O2A    sing N N 100 
GDP PA    "O5'"  sing N N 101 
GDP O2A   HOA2   sing N N 102 
GDP "O5'" "C5'"  sing N N 103 
GDP "C5'" "C4'"  sing N N 104 
GDP "C5'" "H5'"  sing N N 105 
GDP "C5'" "H5''" sing N N 106 
GDP "C4'" "O4'"  sing N N 107 
GDP "C4'" "C3'"  sing N N 108 
GDP "C4'" "H4'"  sing N N 109 
GDP "O4'" "C1'"  sing N N 110 
GDP "C3'" "O3'"  sing N N 111 
GDP "C3'" "C2'"  sing N N 112 
GDP "C3'" "H3'"  sing N N 113 
GDP "O3'" "HO3'" sing N N 114 
GDP "C2'" "O2'"  sing N N 115 
GDP "C2'" "C1'"  sing N N 116 
GDP "C2'" "H2'"  sing N N 117 
GDP "O2'" "HO2'" sing N N 118 
GDP "C1'" N9     sing N N 119 
GDP "C1'" "H1'"  sing N N 120 
GDP N9    C8     sing Y N 121 
GDP N9    C4     sing Y N 122 
GDP C8    N7     doub Y N 123 
GDP C8    H8     sing N N 124 
GDP N7    C5     sing Y N 125 
GDP C5    C6     sing N N 126 
GDP C5    C4     doub Y N 127 
GDP C6    O6     doub N N 128 
GDP C6    N1     sing N N 129 
GDP N1    C2     sing N N 130 
GDP N1    HN1    sing N N 131 
GDP C2    N2     sing N N 132 
GDP C2    N3     doub N N 133 
GDP N2    HN21   sing N N 134 
GDP N2    HN22   sing N N 135 
GDP N3    C4     sing N N 136 
GLN N     CA     sing N N 137 
GLN N     H      sing N N 138 
GLN N     H2     sing N N 139 
GLN CA    C      sing N N 140 
GLN CA    CB     sing N N 141 
GLN CA    HA     sing N N 142 
GLN C     O      doub N N 143 
GLN C     OXT    sing N N 144 
GLN CB    CG     sing N N 145 
GLN CB    HB2    sing N N 146 
GLN CB    HB3    sing N N 147 
GLN CG    CD     sing N N 148 
GLN CG    HG2    sing N N 149 
GLN CG    HG3    sing N N 150 
GLN CD    OE1    doub N N 151 
GLN CD    NE2    sing N N 152 
GLN NE2   HE21   sing N N 153 
GLN NE2   HE22   sing N N 154 
GLN OXT   HXT    sing N N 155 
GLU N     CA     sing N N 156 
GLU N     H      sing N N 157 
GLU N     H2     sing N N 158 
GLU CA    C      sing N N 159 
GLU CA    CB     sing N N 160 
GLU CA    HA     sing N N 161 
GLU C     O      doub N N 162 
GLU C     OXT    sing N N 163 
GLU CB    CG     sing N N 164 
GLU CB    HB2    sing N N 165 
GLU CB    HB3    sing N N 166 
GLU CG    CD     sing N N 167 
GLU CG    HG2    sing N N 168 
GLU CG    HG3    sing N N 169 
GLU CD    OE1    doub N N 170 
GLU CD    OE2    sing N N 171 
GLU OE2   HE2    sing N N 172 
GLU OXT   HXT    sing N N 173 
GLY N     CA     sing N N 174 
GLY N     H      sing N N 175 
GLY N     H2     sing N N 176 
GLY CA    C      sing N N 177 
GLY CA    HA2    sing N N 178 
GLY CA    HA3    sing N N 179 
GLY C     O      doub N N 180 
GLY C     OXT    sing N N 181 
GLY OXT   HXT    sing N N 182 
GOL C1    O1     sing N N 183 
GOL C1    C2     sing N N 184 
GOL C1    H11    sing N N 185 
GOL C1    H12    sing N N 186 
GOL O1    HO1    sing N N 187 
GOL C2    O2     sing N N 188 
GOL C2    C3     sing N N 189 
GOL C2    H2     sing N N 190 
GOL O2    HO2    sing N N 191 
GOL C3    O3     sing N N 192 
GOL C3    H31    sing N N 193 
GOL C3    H32    sing N N 194 
GOL O3    HO3    sing N N 195 
HIS N     CA     sing N N 196 
HIS N     H      sing N N 197 
HIS N     H2     sing N N 198 
HIS CA    C      sing N N 199 
HIS CA    CB     sing N N 200 
HIS CA    HA     sing N N 201 
HIS C     O      doub N N 202 
HIS C     OXT    sing N N 203 
HIS CB    CG     sing N N 204 
HIS CB    HB2    sing N N 205 
HIS CB    HB3    sing N N 206 
HIS CG    ND1    sing Y N 207 
HIS CG    CD2    doub Y N 208 
HIS ND1   CE1    doub Y N 209 
HIS ND1   HD1    sing N N 210 
HIS CD2   NE2    sing Y N 211 
HIS CD2   HD2    sing N N 212 
HIS CE1   NE2    sing Y N 213 
HIS CE1   HE1    sing N N 214 
HIS NE2   HE2    sing N N 215 
HIS OXT   HXT    sing N N 216 
HOH O     H1     sing N N 217 
HOH O     H2     sing N N 218 
ILE N     CA     sing N N 219 
ILE N     H      sing N N 220 
ILE N     H2     sing N N 221 
ILE CA    C      sing N N 222 
ILE CA    CB     sing N N 223 
ILE CA    HA     sing N N 224 
ILE C     O      doub N N 225 
ILE C     OXT    sing N N 226 
ILE CB    CG1    sing N N 227 
ILE CB    CG2    sing N N 228 
ILE CB    HB     sing N N 229 
ILE CG1   CD1    sing N N 230 
ILE CG1   HG12   sing N N 231 
ILE CG1   HG13   sing N N 232 
ILE CG2   HG21   sing N N 233 
ILE CG2   HG22   sing N N 234 
ILE CG2   HG23   sing N N 235 
ILE CD1   HD11   sing N N 236 
ILE CD1   HD12   sing N N 237 
ILE CD1   HD13   sing N N 238 
ILE OXT   HXT    sing N N 239 
LEU N     CA     sing N N 240 
LEU N     H      sing N N 241 
LEU N     H2     sing N N 242 
LEU CA    C      sing N N 243 
LEU CA    CB     sing N N 244 
LEU CA    HA     sing N N 245 
LEU C     O      doub N N 246 
LEU C     OXT    sing N N 247 
LEU CB    CG     sing N N 248 
LEU CB    HB2    sing N N 249 
LEU CB    HB3    sing N N 250 
LEU CG    CD1    sing N N 251 
LEU CG    CD2    sing N N 252 
LEU CG    HG     sing N N 253 
LEU CD1   HD11   sing N N 254 
LEU CD1   HD12   sing N N 255 
LEU CD1   HD13   sing N N 256 
LEU CD2   HD21   sing N N 257 
LEU CD2   HD22   sing N N 258 
LEU CD2   HD23   sing N N 259 
LEU OXT   HXT    sing N N 260 
LYS N     CA     sing N N 261 
LYS N     H      sing N N 262 
LYS N     H2     sing N N 263 
LYS CA    C      sing N N 264 
LYS CA    CB     sing N N 265 
LYS CA    HA     sing N N 266 
LYS C     O      doub N N 267 
LYS C     OXT    sing N N 268 
LYS CB    CG     sing N N 269 
LYS CB    HB2    sing N N 270 
LYS CB    HB3    sing N N 271 
LYS CG    CD     sing N N 272 
LYS CG    HG2    sing N N 273 
LYS CG    HG3    sing N N 274 
LYS CD    CE     sing N N 275 
LYS CD    HD2    sing N N 276 
LYS CD    HD3    sing N N 277 
LYS CE    NZ     sing N N 278 
LYS CE    HE2    sing N N 279 
LYS CE    HE3    sing N N 280 
LYS NZ    HZ1    sing N N 281 
LYS NZ    HZ2    sing N N 282 
LYS NZ    HZ3    sing N N 283 
LYS OXT   HXT    sing N N 284 
MET N     CA     sing N N 285 
MET N     H      sing N N 286 
MET N     H2     sing N N 287 
MET CA    C      sing N N 288 
MET CA    CB     sing N N 289 
MET CA    HA     sing N N 290 
MET C     O      doub N N 291 
MET C     OXT    sing N N 292 
MET CB    CG     sing N N 293 
MET CB    HB2    sing N N 294 
MET CB    HB3    sing N N 295 
MET CG    SD     sing N N 296 
MET CG    HG2    sing N N 297 
MET CG    HG3    sing N N 298 
MET SD    CE     sing N N 299 
MET CE    HE1    sing N N 300 
MET CE    HE2    sing N N 301 
MET CE    HE3    sing N N 302 
MET OXT   HXT    sing N N 303 
PHE N     CA     sing N N 304 
PHE N     H      sing N N 305 
PHE N     H2     sing N N 306 
PHE CA    C      sing N N 307 
PHE CA    CB     sing N N 308 
PHE CA    HA     sing N N 309 
PHE C     O      doub N N 310 
PHE C     OXT    sing N N 311 
PHE CB    CG     sing N N 312 
PHE CB    HB2    sing N N 313 
PHE CB    HB3    sing N N 314 
PHE CG    CD1    doub Y N 315 
PHE CG    CD2    sing Y N 316 
PHE CD1   CE1    sing Y N 317 
PHE CD1   HD1    sing N N 318 
PHE CD2   CE2    doub Y N 319 
PHE CD2   HD2    sing N N 320 
PHE CE1   CZ     doub Y N 321 
PHE CE1   HE1    sing N N 322 
PHE CE2   CZ     sing Y N 323 
PHE CE2   HE2    sing N N 324 
PHE CZ    HZ     sing N N 325 
PHE OXT   HXT    sing N N 326 
PRO N     CA     sing N N 327 
PRO N     CD     sing N N 328 
PRO N     H      sing N N 329 
PRO CA    C      sing N N 330 
PRO CA    CB     sing N N 331 
PRO CA    HA     sing N N 332 
PRO C     O      doub N N 333 
PRO C     OXT    sing N N 334 
PRO CB    CG     sing N N 335 
PRO CB    HB2    sing N N 336 
PRO CB    HB3    sing N N 337 
PRO CG    CD     sing N N 338 
PRO CG    HG2    sing N N 339 
PRO CG    HG3    sing N N 340 
PRO CD    HD2    sing N N 341 
PRO CD    HD3    sing N N 342 
PRO OXT   HXT    sing N N 343 
SER N     CA     sing N N 344 
SER N     H      sing N N 345 
SER N     H2     sing N N 346 
SER CA    C      sing N N 347 
SER CA    CB     sing N N 348 
SER CA    HA     sing N N 349 
SER C     O      doub N N 350 
SER C     OXT    sing N N 351 
SER CB    OG     sing N N 352 
SER CB    HB2    sing N N 353 
SER CB    HB3    sing N N 354 
SER OG    HG     sing N N 355 
SER OXT   HXT    sing N N 356 
THR N     CA     sing N N 357 
THR N     H      sing N N 358 
THR N     H2     sing N N 359 
THR CA    C      sing N N 360 
THR CA    CB     sing N N 361 
THR CA    HA     sing N N 362 
THR C     O      doub N N 363 
THR C     OXT    sing N N 364 
THR CB    OG1    sing N N 365 
THR CB    CG2    sing N N 366 
THR CB    HB     sing N N 367 
THR OG1   HG1    sing N N 368 
THR CG2   HG21   sing N N 369 
THR CG2   HG22   sing N N 370 
THR CG2   HG23   sing N N 371 
THR OXT   HXT    sing N N 372 
TRP N     CA     sing N N 373 
TRP N     H      sing N N 374 
TRP N     H2     sing N N 375 
TRP CA    C      sing N N 376 
TRP CA    CB     sing N N 377 
TRP CA    HA     sing N N 378 
TRP C     O      doub N N 379 
TRP C     OXT    sing N N 380 
TRP CB    CG     sing N N 381 
TRP CB    HB2    sing N N 382 
TRP CB    HB3    sing N N 383 
TRP CG    CD1    doub Y N 384 
TRP CG    CD2    sing Y N 385 
TRP CD1   NE1    sing Y N 386 
TRP CD1   HD1    sing N N 387 
TRP CD2   CE2    doub Y N 388 
TRP CD2   CE3    sing Y N 389 
TRP NE1   CE2    sing Y N 390 
TRP NE1   HE1    sing N N 391 
TRP CE2   CZ2    sing Y N 392 
TRP CE3   CZ3    doub Y N 393 
TRP CE3   HE3    sing N N 394 
TRP CZ2   CH2    doub Y N 395 
TRP CZ2   HZ2    sing N N 396 
TRP CZ3   CH2    sing Y N 397 
TRP CZ3   HZ3    sing N N 398 
TRP CH2   HH2    sing N N 399 
TRP OXT   HXT    sing N N 400 
TYR N     CA     sing N N 401 
TYR N     H      sing N N 402 
TYR N     H2     sing N N 403 
TYR CA    C      sing N N 404 
TYR CA    CB     sing N N 405 
TYR CA    HA     sing N N 406 
TYR C     O      doub N N 407 
TYR C     OXT    sing N N 408 
TYR CB    CG     sing N N 409 
TYR CB    HB2    sing N N 410 
TYR CB    HB3    sing N N 411 
TYR CG    CD1    doub Y N 412 
TYR CG    CD2    sing Y N 413 
TYR CD1   CE1    sing Y N 414 
TYR CD1   HD1    sing N N 415 
TYR CD2   CE2    doub Y N 416 
TYR CD2   HD2    sing N N 417 
TYR CE1   CZ     doub Y N 418 
TYR CE1   HE1    sing N N 419 
TYR CE2   CZ     sing Y N 420 
TYR CE2   HE2    sing N N 421 
TYR CZ    OH     sing N N 422 
TYR OH    HH     sing N N 423 
TYR OXT   HXT    sing N N 424 
VAL N     CA     sing N N 425 
VAL N     H      sing N N 426 
VAL N     H2     sing N N 427 
VAL CA    C      sing N N 428 
VAL CA    CB     sing N N 429 
VAL CA    HA     sing N N 430 
VAL C     O      doub N N 431 
VAL C     OXT    sing N N 432 
VAL CB    CG1    sing N N 433 
VAL CB    CG2    sing N N 434 
VAL CB    HB     sing N N 435 
VAL CG1   HG11   sing N N 436 
VAL CG1   HG12   sing N N 437 
VAL CG1   HG13   sing N N 438 
VAL CG2   HG21   sing N N 439 
VAL CG2   HG22   sing N N 440 
VAL CG2   HG23   sing N N 441 
VAL OXT   HXT    sing N N 442 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32271358 
_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   2C78 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.crystal_system   monoclinic 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.IT_number        4 
_space_group.name_Hall        'P 2yb' 
_space_group.id               1 
# 
_atom_sites.entry_id                    8YLY 
_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]   0.018102 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001860 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011502 
_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]   0.016411 
_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  
H  
MG 
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     . PHE A 1 5   ? 20.241  13.981  39.694 1.00 66.62  ? 6    PHE A N     1 
ATOM   2    C  CA    . PHE A 1 5   ? 20.385  12.550  39.458 1.00 53.17  ? 6    PHE A CA    1 
ATOM   3    C  C     . PHE A 1 5   ? 19.041  11.822  39.638 1.00 44.73  ? 6    PHE A C     1 
ATOM   4    O  O     . PHE A 1 5   ? 18.393  11.935  40.675 1.00 44.49  ? 6    PHE A O     1 
ATOM   5    C  CB    . PHE A 1 5   ? 21.441  11.949  40.400 1.00 50.11  ? 6    PHE A CB    1 
ATOM   6    C  CG    . PHE A 1 5   ? 21.702  10.488  40.153 1.00 38.69  ? 6    PHE A CG    1 
ATOM   7    C  CD1   . PHE A 1 5   ? 22.562  10.081  39.127 1.00 41.78  ? 6    PHE A CD1   1 
ATOM   8    C  CD2   . PHE A 1 5   ? 21.076  9.512   40.926 1.00 33.12  ? 6    PHE A CD2   1 
ATOM   9    C  CE1   . PHE A 1 5   ? 22.798  8.731   38.895 1.00 41.96  ? 6    PHE A CE1   1 
ATOM   10   C  CE2   . PHE A 1 5   ? 21.303  8.158   40.707 1.00 36.81  ? 6    PHE A CE2   1 
ATOM   11   C  CZ    . PHE A 1 5   ? 22.157  7.761   39.661 1.00 43.10  ? 6    PHE A CZ    1 
ATOM   12   N  N     . GLU A 1 6   ? 18.600  11.070  38.638 1.00 35.78  ? 7    GLU A N     1 
ATOM   13   C  CA    . GLU A 1 6   ? 17.375  10.296  38.791 1.00 36.84  ? 7    GLU A CA    1 
ATOM   14   C  C     . GLU A 1 6   ? 17.733  8.910   39.306 1.00 35.94  ? 7    GLU A C     1 
ATOM   15   O  O     . GLU A 1 6   ? 18.370  8.121   38.602 1.00 33.50  ? 7    GLU A O     1 
ATOM   16   C  CB    . GLU A 1 6   ? 16.608  10.191  37.474 1.00 42.06  ? 7    GLU A CB    1 
ATOM   17   C  CG    . GLU A 1 6   ? 16.019  11.506  37.004 1.00 57.88  ? 7    GLU A CG    1 
ATOM   18   C  CD    . GLU A 1 6   ? 15.192  11.351  35.736 1.00 72.55  ? 7    GLU A CD    1 
ATOM   19   O  OE1   . GLU A 1 6   ? 15.138  10.229  35.178 1.00 62.61  ? 7    GLU A OE1   1 
ATOM   20   O  OE2   . GLU A 1 6   ? 14.593  12.359  35.303 1.00 83.61  ? 7    GLU A OE2   1 
ATOM   21   N  N     . ARG A 1 7   ? 17.322  8.606   40.533 1.00 33.88  ? 8    ARG A N     1 
ATOM   22   C  CA    . ARG A 1 7   ? 17.597  7.294   41.109 1.00 31.81  ? 8    ARG A CA    1 
ATOM   23   C  C     . ARG A 1 7   ? 16.974  6.167   40.310 1.00 33.11  ? 8    ARG A C     1 
ATOM   24   O  O     . ARG A 1 7   ? 17.516  5.060   40.296 1.00 30.10  ? 8    ARG A O     1 
ATOM   25   C  CB    . ARG A 1 7   ? 17.109  7.252   42.560 1.00 33.88  ? 8    ARG A CB    1 
ATOM   26   C  CG    . ARG A 1 7   ? 18.018  8.049   43.451 1.00 43.27  ? 8    ARG A CG    1 
ATOM   27   C  CD    . ARG A 1 7   ? 17.636  7.996   44.913 1.00 57.68  ? 8    ARG A CD    1 
ATOM   28   N  NE    . ARG A 1 7   ? 18.619  8.776   45.667 1.00 69.81  ? 8    ARG A NE    1 
ATOM   29   C  CZ    . ARG A 1 7   ? 18.619  8.946   46.983 1.00 84.82  ? 8    ARG A CZ    1 
ATOM   30   N  NH1   . ARG A 1 7   ? 17.681  8.375   47.728 1.00 95.24  ? 8    ARG A NH1   1 
ATOM   31   N  NH2   . ARG A 1 7   ? 19.568  9.682   47.553 1.00 81.51  ? 8    ARG A NH2   1 
ATOM   32   N  N     . THR A 1 8   ? 15.823  6.402   39.670 1.00 28.12  ? 9    THR A N     1 
ATOM   33   C  CA    . THR A 1 8   ? 15.176  5.360   38.887 1.00 29.38  ? 9    THR A CA    1 
ATOM   34   C  C     . THR A 1 8   ? 14.783  5.871   37.503 1.00 27.32  ? 9    THR A C     1 
ATOM   35   O  O     . THR A 1 8   ? 14.383  7.033   37.317 1.00 28.44  ? 9    THR A O     1 
ATOM   36   C  CB    . THR A 1 8   ? 13.928  4.831   39.608 1.00 39.16  ? 9    THR A CB    1 
ATOM   37   O  OG1   . THR A 1 8   ? 12.981  5.888   39.677 1.00 56.55  ? 9    THR A OG1   1 
ATOM   38   C  CG2   . THR A 1 8   ? 14.272  4.419   41.034 1.00 35.20  ? 9    THR A CG2   1 
ATOM   39   N  N     . LYS A 1 9   ? 14.875  4.983   36.536 1.00 26.25  ? 10   LYS A N     1 
ATOM   40   C  CA    . LYS A 1 9   ? 14.423  5.341   35.213 1.00 26.15  ? 10   LYS A CA    1 
ATOM   41   C  C     . LYS A 1 9   ? 12.917  5.686   35.267 1.00 24.28  ? 10   LYS A C     1 
ATOM   42   O  O     . LYS A 1 9   ? 12.204  5.237   36.177 1.00 27.01  ? 10   LYS A O     1 
ATOM   43   C  CB    . LYS A 1 9   ? 14.791  4.144   34.323 1.00 32.40  ? 10   LYS A CB    1 
ATOM   44   C  CG    . LYS A 1 9   ? 14.788  4.301   32.881 1.00 35.63  ? 10   LYS A CG    1 
ATOM   45   C  CD    . LYS A 1 9   ? 15.322  2.992   32.234 1.00 23.79  ? 10   LYS A CD    1 
ATOM   46   C  CE    . LYS A 1 9   ? 16.849  2.956   31.988 1.00 19.72  ? 10   LYS A CE    1 
ATOM   47   N  NZ    . LYS A 1 9   ? 17.139  1.737   31.175 1.00 20.23  ? 10   LYS A NZ    1 
ATOM   48   N  N     . PRO A 1 10  ? 12.414  6.585   34.397 1.00 28.65  ? 11   PRO A N     1 
ATOM   49   C  CA    . PRO A 1 10  ? 10.965  6.866   34.363 1.00 26.35  ? 11   PRO A CA    1 
ATOM   50   C  C     . PRO A 1 10  ? 10.201  5.580   34.052 1.00 22.27  ? 11   PRO A C     1 
ATOM   51   O  O     . PRO A 1 10  ? 10.782  4.625   33.539 1.00 23.64  ? 11   PRO A O     1 
ATOM   52   C  CB    . PRO A 1 10  ? 10.821  7.873   33.207 1.00 31.98  ? 11   PRO A CB    1 
ATOM   53   C  CG    . PRO A 1 10  ? 12.237  8.438   33.030 1.00 37.90  ? 11   PRO A CG    1 
ATOM   54   C  CD    . PRO A 1 10  ? 13.179  7.400   33.434 1.00 33.16  ? 11   PRO A CD    1 
ATOM   55   N  N     . HIS A 1 11  ? 8.905   5.576   34.368 1.00 24.09  ? 12   HIS A N     1 
ATOM   56   C  CA    . HIS A 1 11  ? 8.064   4.399   34.198 1.00 24.37  ? 12   HIS A CA    1 
ATOM   57   C  C     . HIS A 1 11  ? 6.797   4.744   33.431 1.00 21.17  ? 12   HIS A C     1 
ATOM   58   O  O     . HIS A 1 11  ? 6.164   5.771   33.702 1.00 22.97  ? 12   HIS A O     1 
ATOM   59   C  CB    . HIS A 1 11  ? 7.691   3.808   35.577 1.00 24.27  ? 12   HIS A CB    1 
ATOM   60   C  CG    . HIS A 1 11  ? 6.755   2.655   35.460 1.00 23.63  ? 12   HIS A CG    1 
ATOM   61   N  ND1   . HIS A 1 11  ? 7.164   1.395   35.054 1.00 28.98  ? 12   HIS A ND1   1 
ATOM   62   C  CD2   . HIS A 1 11  ? 5.400   2.618   35.502 1.00 28.83  ? 12   HIS A CD2   1 
ATOM   63   C  CE1   . HIS A 1 11  ? 6.106   0.611   34.963 1.00 25.66  ? 12   HIS A CE1   1 
ATOM   64   N  NE2   . HIS A 1 11  ? 5.023   1.341   35.177 1.00 28.32  ? 12   HIS A NE2   1 
ATOM   65   N  N     . ALA A 1 12  ? 6.402   3.871   32.497 1.00 18.04  ? 13   ALA A N     1 
ATOM   66   C  CA    . ALA A 1 12  ? 5.088   4.029   31.889 1.00 18.00  ? 13   ALA A CA    1 
ATOM   67   C  C     . ALA A 1 12  ? 4.413   2.681   31.806 1.00 21.15  ? 13   ALA A C     1 
ATOM   68   O  O     . ALA A 1 12  ? 5.057   1.633   31.716 1.00 19.02  ? 13   ALA A O     1 
ATOM   69   C  CB    . ALA A 1 12  ? 5.220   4.656   30.474 1.00 21.70  ? 13   ALA A CB    1 
ATOM   70   N  N     . ASN A 1 13  ? 3.088   2.734   31.692 1.00 18.74  ? 14   ASN A N     1 
ATOM   71   C  CA    . ASN A 1 13  ? 2.229   1.563   31.550 1.00 18.47  ? 14   ASN A CA    1 
ATOM   72   C  C     . ASN A 1 13  ? 1.612   1.551   30.167 1.00 18.12  ? 14   ASN A C     1 
ATOM   73   O  O     . ASN A 1 13  ? 0.950   2.520   29.779 1.00 19.10  ? 14   ASN A O     1 
ATOM   74   C  CB    . ASN A 1 13  ? 1.144   1.663   32.624 1.00 18.81  ? 14   ASN A CB    1 
ATOM   75   C  CG    . ASN A 1 13  ? 1.722   1.702   34.035 1.00 30.92  ? 14   ASN A CG    1 
ATOM   76   O  OD1   . ASN A 1 13  ? 2.327   0.747   34.508 1.00 25.59  ? 14   ASN A OD1   1 
ATOM   77   N  ND2   . ASN A 1 13  ? 1.723   2.907   34.613 1.00 33.70  ? 14   ASN A ND2   1 
ATOM   78   N  N     . ILE A 1 14  ? 1.869   0.504   29.391 1.00 15.95  ? 15   ILE A N     1 
ATOM   79   C  CA    . ILE A 1 14  ? 1.277   0.449   28.065 1.00 15.60  ? 15   ILE A CA    1 
ATOM   80   C  C     . ILE A 1 14  ? 0.664   -0.909  27.767 1.00 16.10  ? 15   ILE A C     1 
ATOM   81   O  O     . ILE A 1 14  ? 0.643   -1.793  28.624 1.00 16.29  ? 15   ILE A O     1 
ATOM   82   C  CB    . ILE A 1 14  ? 2.314   0.788   26.973 1.00 16.38  ? 15   ILE A CB    1 
ATOM   83   C  CG1   . ILE A 1 14  ? 3.469   -0.213  26.944 1.00 18.75  ? 15   ILE A CG1   1 
ATOM   84   C  CG2   . ILE A 1 14  ? 2.899   2.243   27.182 1.00 20.33  ? 15   ILE A CG2   1 
ATOM   85   C  CD1   . ILE A 1 14  ? 4.469   0.028   25.768 1.00 20.88  ? 15   ILE A CD1   1 
ATOM   86   N  N     . GLY A 1 15  ? 0.210   -1.129  26.544 1.00 18.43  ? 16   GLY A N     1 
ATOM   87   C  CA    . GLY A 1 15  ? -0.326  -2.454  26.221 1.00 18.12  ? 16   GLY A CA    1 
ATOM   88   C  C     . GLY A 1 15  ? -0.523  -2.520  24.730 1.00 15.99  ? 16   GLY A C     1 
ATOM   89   O  O     . GLY A 1 15  ? -0.474  -1.484  24.055 1.00 18.82  ? 16   GLY A O     1 
ATOM   90   N  N     . THR A 1 16  ? -0.625  -3.750  24.217 1.00 16.12  ? 17   THR A N     1 
ATOM   91   C  CA    . THR A 1 16  ? -0.914  -3.992  22.794 1.00 13.65  ? 17   THR A CA    1 
ATOM   92   C  C     . THR A 1 16  ? -2.411  -4.167  22.626 1.00 15.47  ? 17   THR A C     1 
ATOM   93   O  O     . THR A 1 16  ? -3.003  -5.003  23.313 1.00 18.31  ? 17   THR A O     1 
ATOM   94   C  CB    . THR A 1 16  ? -0.117  -5.228  22.277 1.00 14.79  ? 17   THR A CB    1 
ATOM   95   O  OG1   . THR A 1 16  ? 0.008   -6.224  23.330 1.00 19.66  ? 17   THR A OG1   1 
ATOM   96   C  CG2   . THR A 1 16  ? 1.274   -4.821  21.795 1.00 19.83  ? 17   THR A CG2   1 
ATOM   97   N  N     . ILE A 1 17  ? -3.015  -3.380  21.720 1.00 14.25  ? 18   ILE A N     1 
ATOM   98   C  CA    . ILE A 1 17  ? -4.437  -3.469  21.403 1.00 13.79  ? 18   ILE A CA    1 
ATOM   99   C  C     . ILE A 1 17  ? -4.584  -3.712  19.919 1.00 15.83  ? 18   ILE A C     1 
ATOM   100  O  O     . ILE A 1 17  ? -3.619  -3.645  19.173 1.00 15.02  ? 18   ILE A O     1 
ATOM   101  C  CB    . ILE A 1 17  ? -5.196  -2.211  21.821 1.00 15.23  ? 18   ILE A CB    1 
ATOM   102  C  CG1   . ILE A 1 17  ? -4.701  -0.946  21.050 1.00 16.04  ? 18   ILE A CG1   1 
ATOM   103  C  CG2   . ILE A 1 17  ? -5.100  -1.983  23.411 1.00 18.61  ? 18   ILE A CG2   1 
ATOM   104  C  CD1   . ILE A 1 17  ? -5.445  0.377   21.414 1.00 16.73  ? 18   ILE A CD1   1 
ATOM   105  N  N     . GLY A 1 18  ? -5.802  -4.051  19.488 1.00 14.56  ? 19   GLY A N     1 
ATOM   106  C  CA    . GLY A 1 18  ? -6.022  -4.387  18.083 1.00 15.71  ? 19   GLY A CA    1 
ATOM   107  C  C     . GLY A 1 18  ? -6.766  -5.700  17.885 1.00 14.53  ? 19   GLY A C     1 
ATOM   108  O  O     . GLY A 1 18  ? -7.038  -6.454  18.827 1.00 16.03  ? 19   GLY A O     1 
ATOM   109  N  N     . HIS A 1 19  ? -7.151  -5.930  16.622 1.00 13.88  ? 20   HIS A N     1 
ATOM   110  C  CA    . HIS A 1 19  ? -8.026  -7.046  16.270 1.00 14.48  ? 20   HIS A CA    1 
ATOM   111  C  C     . HIS A 1 19  ? -7.334  -8.395  16.515 1.00 15.56  ? 20   HIS A C     1 
ATOM   112  O  O     . HIS A 1 19  ? -6.111  -8.534  16.444 1.00 15.22  ? 20   HIS A O     1 
ATOM   113  C  CB    . HIS A 1 19  ? -8.401  -6.890  14.792 1.00 14.98  ? 20   HIS A CB    1 
ATOM   114  C  CG    . HIS A 1 19  ? -9.542  -7.739  14.378 1.00 15.48  ? 20   HIS A CG    1 
ATOM   115  N  ND1   . HIS A 1 19  ? -10.850 -7.326  14.519 1.00 16.45  ? 20   HIS A ND1   1 
ATOM   116  C  CD2   . HIS A 1 19  ? -9.572  -8.976  13.837 1.00 16.84  ? 20   HIS A CD2   1 
ATOM   117  C  CE1   . HIS A 1 19  ? -11.647 -8.270  14.060 1.00 18.74  ? 20   HIS A CE1   1 
ATOM   118  N  NE2   . HIS A 1 19  ? -10.902 -9.287  13.642 1.00 18.87  ? 20   HIS A NE2   1 
ATOM   119  N  N     . VAL A 1 20  ? -8.155  -9.406  16.756 1.00 16.09  ? 21   VAL A N     1 
ATOM   120  C  CA    . VAL A 1 20  ? -7.644  -10.753 16.992 1.00 18.04  ? 21   VAL A CA    1 
ATOM   121  C  C     . VAL A 1 20  ? -6.836  -11.257 15.789 1.00 17.91  ? 21   VAL A C     1 
ATOM   122  O  O     . VAL A 1 20  ? -7.150  -10.993 14.625 1.00 17.72  ? 21   VAL A O     1 
ATOM   123  C  CB    . VAL A 1 20  ? -8.807  -11.699 17.366 1.00 18.94  ? 21   VAL A CB    1 
ATOM   124  C  CG1   . VAL A 1 20  ? -9.774  -11.898 16.156 1.00 18.70  ? 21   VAL A CG1   1 
ATOM   125  C  CG2   . VAL A 1 20  ? -8.197  -13.010 17.919 1.00 20.44  ? 21   VAL A CG2   1 
ATOM   126  N  N     . ASP A 1 21  ? -5.714  -11.939 16.118 1.00 16.21  ? 22   ASP A N     1 
ATOM   127  C  CA    . ASP A 1 21  ? -4.790  -12.561 15.169 1.00 17.56  ? 22   ASP A CA    1 
ATOM   128  C  C     . ASP A 1 21  ? -3.967  -11.537 14.396 1.00 16.10  ? 22   ASP A C     1 
ATOM   129  O  O     . ASP A 1 21  ? -3.246  -11.949 13.472 1.00 16.85  ? 22   ASP A O     1 
ATOM   130  C  CB    . ASP A 1 21  ? -5.481  -13.547 14.195 1.00 16.42  ? 22   ASP A CB    1 
ATOM   131  C  CG    . ASP A 1 21  ? -5.832  -14.844 14.888 1.00 30.13  ? 22   ASP A CG    1 
ATOM   132  O  OD1   . ASP A 1 21  ? -5.063  -15.321 15.733 1.00 31.90  ? 22   ASP A OD1   1 
ATOM   133  O  OD2   . ASP A 1 21  ? -6.921  -15.381 14.620 1.00 39.38  ? 22   ASP A OD2   1 
ATOM   134  N  N     . HIS A 1 22  ? -3.995  -10.248 14.763 1.00 14.54  ? 23   HIS A N     1 
ATOM   135  C  CA    . HIS A 1 22  ? -3.178  -9.272  14.022 1.00 13.57  ? 23   HIS A CA    1 
ATOM   136  C  C     . HIS A 1 22  ? -1.739  -9.278  14.482 1.00 14.28  ? 23   HIS A C     1 
ATOM   137  O  O     . HIS A 1 22  ? -0.894  -8.749  13.762 1.00 14.71  ? 23   HIS A O     1 
ATOM   138  C  CB    . HIS A 1 22  ? -3.808  -7.864  14.040 1.00 13.70  ? 23   HIS A CB    1 
ATOM   139  C  CG    . HIS A 1 22  ? -4.934  -7.758  13.103 1.00 14.03  ? 23   HIS A CG    1 
ATOM   140  N  ND1   . HIS A 1 22  ? -5.312  -6.571  12.518 1.00 14.72  ? 23   HIS A ND1   1 
ATOM   141  C  CD2   . HIS A 1 22  ? -5.744  -8.724  12.616 1.00 15.30  ? 23   HIS A CD2   1 
ATOM   142  C  CE1   . HIS A 1 22  ? -6.314  -6.825  11.671 1.00 14.76  ? 23   HIS A CE1   1 
ATOM   143  N  NE2   . HIS A 1 22  ? -6.574  -8.113  11.694 1.00 17.48  ? 23   HIS A NE2   1 
ATOM   144  N  N     . GLY A 1 23  ? -1.458  -9.831  15.652 1.00 14.05  ? 24   GLY A N     1 
ATOM   145  C  CA    . GLY A 1 23  ? -0.076  -10.062 16.065 1.00 14.64  ? 24   GLY A CA    1 
ATOM   146  C  C     . GLY A 1 23  ? 0.307   -9.432  17.373 1.00 15.93  ? 24   GLY A C     1 
ATOM   147  O  O     . GLY A 1 23  ? 1.515   -9.250  17.618 1.00 13.98  ? 24   GLY A O     1 
ATOM   148  N  N     . LYS A 1 24  ? -0.658  -9.138  18.242 1.00 13.78  ? 25   LYS A N     1 
ATOM   149  C  CA    . LYS A 1 24  ? -0.362  -8.445  19.500 1.00 13.60  ? 25   LYS A CA    1 
ATOM   150  C  C     . LYS A 1 24  ? 0.590   -9.264  20.365 1.00 13.69  ? 25   LYS A C     1 
ATOM   151  O  O     . LYS A 1 24  ? 1.571   -8.716  20.914 1.00 14.38  ? 25   LYS A O     1 
ATOM   152  C  CB    . LYS A 1 24  ? -1.670  -8.206  20.246 1.00 13.87  ? 25   LYS A CB    1 
ATOM   153  C  CG    . LYS A 1 24  ? -2.551  -7.258  19.449 1.00 14.97  ? 25   LYS A CG    1 
ATOM   154  C  CD    . LYS A 1 24  ? -3.857  -6.960  20.236 1.00 16.41  ? 25   LYS A CD    1 
ATOM   155  C  CE    . LYS A 1 24  ? -4.749  -8.178  20.533 1.00 16.00  ? 25   LYS A CE    1 
ATOM   156  N  NZ    . LYS A 1 24  ? -5.219  -8.892  19.259 1.00 15.81  ? 25   LYS A NZ    1 
ATOM   157  N  N     . THR A 1 25  ? 0.297   -10.572 20.556 1.00 13.77  ? 26   THR A N     1 
ATOM   158  C  CA    . THR A 1 25  ? 1.149   -11.364 21.446 1.00 13.66  ? 26   THR A CA    1 
ATOM   159  C  C     . THR A 1 25  ? 2.490   -11.655 20.814 1.00 15.26  ? 26   THR A C     1 
ATOM   160  O  O     . THR A 1 25  ? 3.525   -11.615 21.496 1.00 14.89  ? 26   THR A O     1 
ATOM   161  C  CB    . THR A 1 25  ? 0.404   -12.651 21.758 1.00 15.84  ? 26   THR A CB    1 
ATOM   162  O  OG1   . THR A 1 25  ? -0.844  -12.278 22.359 1.00 16.59  ? 26   THR A OG1   1 
ATOM   163  C  CG2   . THR A 1 25  ? 1.167   -13.572 22.689 1.00 17.02  ? 26   THR A CG2   1 
ATOM   164  N  N     . THR A 1 26  ? 2.532   -11.871 19.498 1.00 14.18  ? 27   THR A N     1 
ATOM   165  C  CA    . THR A 1 26  ? 3.826   -12.067 18.877 1.00 12.70  ? 27   THR A CA    1 
ATOM   166  C  C     . THR A 1 26  ? 4.683   -10.799 18.968 1.00 15.45  ? 27   THR A C     1 
ATOM   167  O  O     . THR A 1 26  ? 5.906   -10.879 19.225 1.00 15.37  ? 27   THR A O     1 
ATOM   168  C  CB    . THR A 1 26  ? 3.630   -12.427 17.388 1.00 12.86  ? 27   THR A CB    1 
ATOM   169  O  OG1   . THR A 1 26  ? 2.789   -13.585 17.282 1.00 14.70  ? 27   THR A OG1   1 
ATOM   170  C  CG2   . THR A 1 26  ? 4.940   -12.822 16.729 1.00 16.91  ? 27   THR A CG2   1 
ATOM   171  N  N     . LEU A 1 27  ? 4.082   -9.615  18.816 1.00 13.09  ? 28   LEU A N     1 
ATOM   172  C  CA    . LEU A 1 27  ? 4.846   -8.368  18.984 1.00 12.51  ? 28   LEU A CA    1 
ATOM   173  C  C     . LEU A 1 27  ? 5.330   -8.240  20.422 1.00 13.84  ? 28   LEU A C     1 
ATOM   174  O  O     . LEU A 1 27  ? 6.483   -7.836  20.636 1.00 14.46  ? 28   LEU A O     1 
ATOM   175  C  CB    . LEU A 1 27  ? 3.976   -7.170  18.592 1.00 12.83  ? 28   LEU A CB    1 
ATOM   176  C  CG    . LEU A 1 27  ? 4.710   -5.828  18.778 1.00 12.59  ? 28   LEU A CG    1 
ATOM   177  C  CD1   . LEU A 1 27  ? 5.944   -5.768  17.857 1.00 14.59  ? 28   LEU A CD1   1 
ATOM   178  C  CD2   . LEU A 1 27  ? 3.714   -4.697  18.452 1.00 14.13  ? 28   LEU A CD2   1 
ATOM   179  N  N     . THR A 1 28  ? 4.473   -8.562  21.412 1.00 13.19  ? 29   THR A N     1 
ATOM   180  C  CA    . THR A 1 28  ? 4.900   -8.485  22.813 1.00 13.61  ? 29   THR A CA    1 
ATOM   181  C  C     . THR A 1 28  ? 6.101   -9.383  23.035 1.00 15.12  ? 29   THR A C     1 
ATOM   182  O  O     . THR A 1 28  ? 7.097   -8.980  23.672 1.00 15.87  ? 29   THR A O     1 
ATOM   183  C  CB    . THR A 1 28  ? 3.744   -8.881  23.705 1.00 15.07  ? 29   THR A CB    1 
ATOM   184  O  OG1   . THR A 1 28  ? 2.666   -7.987  23.455 1.00 16.83  ? 29   THR A OG1   1 
ATOM   185  C  CG2   . THR A 1 28  ? 4.141   -8.761  25.207 1.00 16.57  ? 29   THR A CG2   1 
ATOM   186  N  N     . ALA A 1 29  ? 6.049   -10.605 22.512 1.00 14.52  ? 30   ALA A N     1 
ATOM   187  C  CA    . ALA A 1 29  ? 7.187   -11.507 22.662 1.00 14.36  ? 30   ALA A CA    1 
ATOM   188  C  C     . ALA A 1 29  ? 8.405   -10.948 21.975 1.00 17.38  ? 30   ALA A C     1 
ATOM   189  O  O     . ALA A 1 29  ? 9.522   -11.013 22.523 1.00 16.62  ? 30   ALA A O     1 
ATOM   190  C  CB    . ALA A 1 29  ? 6.873   -12.877 22.074 1.00 17.67  ? 30   ALA A CB    1 
ATOM   191  N  N     . ALA A 1 30  ? 8.246   -10.436 20.761 1.00 15.14  ? 31   ALA A N     1 
ATOM   192  C  CA    . ALA A 1 30  ? 9.391   -9.877  20.057 1.00 14.13  ? 31   ALA A CA    1 
ATOM   193  C  C     . ALA A 1 30  ? 10.014  -8.706  20.801 1.00 15.19  ? 31   ALA A C     1 
ATOM   194  O  O     . ALA A 1 30  ? 11.252  -8.593  20.828 1.00 16.21  ? 31   ALA A O     1 
ATOM   195  C  CB    . ALA A 1 30  ? 8.950   -9.453  18.634 1.00 15.00  ? 31   ALA A CB    1 
ATOM   196  N  N     . ILE A 1 31  ? 9.219   -7.806  21.372 1.00 14.74  ? 32   ILE A N     1 
ATOM   197  C  CA    . ILE A 1 31  ? 9.798   -6.689  22.138 1.00 13.90  ? 32   ILE A CA    1 
ATOM   198  C  C     . ILE A 1 31  ? 10.641  -7.243  23.289 1.00 15.39  ? 32   ILE A C     1 
ATOM   199  O  O     . ILE A 1 31  ? 11.806  -6.837  23.491 1.00 16.06  ? 32   ILE A O     1 
ATOM   200  C  CB    . ILE A 1 31  ? 8.680   -5.765  22.637 1.00 14.30  ? 32   ILE A CB    1 
ATOM   201  C  CG1   . ILE A 1 31  ? 7.982   -5.048  21.470 1.00 12.38  ? 32   ILE A CG1   1 
ATOM   202  C  CG2   . ILE A 1 31  ? 9.237   -4.738  23.650 1.00 15.36  ? 32   ILE A CG2   1 
ATOM   203  C  CD1   . ILE A 1 31  ? 6.675   -4.363  21.973 1.00 14.93  ? 32   ILE A CD1   1 
ATOM   204  N  N     . THR A 1 32  ? 10.111  -8.210  24.029 1.00 15.39  ? 33   THR A N     1 
ATOM   205  C  CA    . THR A 1 32  ? 10.893  -8.667  25.195 1.00 14.26  ? 33   THR A CA    1 
ATOM   206  C  C     . THR A 1 32  ? 12.155  -9.392  24.754 1.00 17.57  ? 33   THR A C     1 
ATOM   207  O  O     . THR A 1 32  ? 13.195  -9.325  25.459 1.00 16.85  ? 33   THR A O     1 
ATOM   208  C  CB    . THR A 1 32  ? 10.071  -9.588  26.106 1.00 17.90  ? 33   THR A CB    1 
ATOM   209  O  OG1   . THR A 1 32  ? 9.839   -10.867 25.484 1.00 18.58  ? 33   THR A OG1   1 
ATOM   210  C  CG2   . THR A 1 32  ? 8.779   -8.927  26.601 1.00 18.23  ? 33   THR A CG2   1 
ATOM   211  N  N     . THR A 1 33  ? 12.105  -10.097 23.627 1.00 16.73  ? 34   THR A N     1 
ATOM   212  C  CA    . THR A 1 33  ? 13.238  -10.883 23.146 1.00 16.15  ? 34   THR A CA    1 
ATOM   213  C  C     . THR A 1 33  ? 14.326  -9.964  22.599 1.00 16.64  ? 34   THR A C     1 
ATOM   214  O  O     . THR A 1 33  ? 15.526  -10.194 22.828 1.00 19.77  ? 34   THR A O     1 
ATOM   215  C  CB    . THR A 1 33  ? 12.695  -11.845 22.100 1.00 19.44  ? 34   THR A CB    1 
ATOM   216  O  OG1   . THR A 1 33  ? 11.788  -12.735 22.755 1.00 21.47  ? 34   THR A OG1   1 
ATOM   217  C  CG2   . THR A 1 33  ? 13.783  -12.628 21.529 1.00 20.88  ? 34   THR A CG2   1 
ATOM   218  N  N     . VAL A 1 34  ? 13.944  -8.925  21.857 1.00 15.75  ? 35   VAL A N     1 
ATOM   219  C  CA    . VAL A 1 34  ? 14.921  -7.966  21.343 1.00 14.98  ? 35   VAL A CA    1 
ATOM   220  C  C     . VAL A 1 34  ? 15.585  -7.209  22.496 1.00 17.63  ? 35   VAL A C     1 
ATOM   221  O  O     . VAL A 1 34  ? 16.819  -7.060  22.534 1.00 17.36  ? 35   VAL A O     1 
ATOM   222  C  CB    . VAL A 1 34  ? 14.253  -6.998  20.359 1.00 14.44  ? 35   VAL A CB    1 
ATOM   223  C  CG1   . VAL A 1 34  ? 15.180  -5.846  20.016 1.00 16.60  ? 35   VAL A CG1   1 
ATOM   224  C  CG2   . VAL A 1 34  ? 13.886  -7.784  19.054 1.00 15.20  ? 35   VAL A CG2   1 
ATOM   225  N  N     . LEU A 1 35  ? 14.782  -6.728  23.460 1.00 15.62  ? 36   LEU A N     1 
ATOM   226  C  CA    . LEU A 1 35  ? 15.367  -5.957  24.554 1.00 14.66  ? 36   LEU A CA    1 
ATOM   227  C  C     . LEU A 1 35  ? 16.161  -6.862  25.493 1.00 17.63  ? 36   LEU A C     1 
ATOM   228  O  O     . LEU A 1 35  ? 17.130  -6.367  26.116 1.00 17.62  ? 36   LEU A O     1 
ATOM   229  C  CB    . LEU A 1 35  ? 14.259  -5.209  25.334 1.00 16.32  ? 36   LEU A CB    1 
ATOM   230  C  CG    . LEU A 1 35  ? 13.554  -4.169  24.472 1.00 18.27  ? 36   LEU A CG    1 
ATOM   231  C  CD1   . LEU A 1 35  ? 12.391  -3.555  25.285 1.00 20.63  ? 36   LEU A CD1   1 
ATOM   232  C  CD2   . LEU A 1 35  ? 14.483  -3.062  23.981 1.00 20.50  ? 36   LEU A CD2   1 
ATOM   233  N  N     . ALA A 1 36  ? 15.827  -8.165  25.581 1.00 16.79  ? 37   ALA A N     1 
ATOM   234  C  CA    . ALA A 1 36  ? 16.623  -9.081  26.413 1.00 16.75  ? 37   ALA A CA    1 
ATOM   235  C  C     . ALA A 1 36  ? 18.060  -9.204  25.898 1.00 17.49  ? 37   ALA A C     1 
ATOM   236  O  O     . ALA A 1 36  ? 18.988  -9.444  26.687 1.00 20.11  ? 37   ALA A O     1 
ATOM   237  C  CB    . ALA A 1 36  ? 15.991  -10.480 26.494 1.00 19.42  ? 37   ALA A CB    1 
ATOM   238  N  N     . LYS A 1 37  ? 18.284  -9.014  24.574 1.00 16.57  ? 38   LYS A N     1 
ATOM   239  C  CA    . LYS A 1 37  ? 19.641  -9.091  24.064 1.00 18.31  ? 38   LYS A CA    1 
ATOM   240  C  C     . LYS A 1 37  ? 20.499  -7.988  24.662 1.00 20.49  ? 38   LYS A C     1 
ATOM   241  O  O     . LYS A 1 37  ? 21.713  -8.171  24.805 1.00 20.73  ? 38   LYS A O     1 
ATOM   242  C  CB    . LYS A 1 37  ? 19.691  -8.967  22.529 1.00 19.86  ? 38   LYS A CB    1 
ATOM   243  C  CG    . LYS A 1 37  ? 18.972  -10.052 21.764 1.00 19.04  ? 38   LYS A CG    1 
ATOM   244  C  CD    . LYS A 1 37  ? 19.502  -11.404 22.089 1.00 28.34  ? 38   LYS A CD    1 
ATOM   245  C  CE    . LYS A 1 37  ? 20.878  -11.612 21.536 1.00 30.90  ? 38   LYS A CE    1 
ATOM   246  N  NZ    . LYS A 1 37  ? 21.277  -13.099 21.598 1.00 31.48  ? 38   LYS A NZ    1 
ATOM   247  N  N     . ALA A 1 38  ? 19.896  -6.863  25.040 1.00 17.54  ? 39   ALA A N     1 
ATOM   248  C  CA    . ALA A 1 38  ? 20.609  -5.758  25.684 1.00 20.51  ? 39   ALA A CA    1 
ATOM   249  C  C     . ALA A 1 38  ? 20.672  -5.893  27.189 1.00 20.81  ? 39   ALA A C     1 
ATOM   250  O  O     . ALA A 1 38  ? 21.293  -5.043  27.830 1.00 24.06  ? 39   ALA A O     1 
ATOM   251  C  CB    . ALA A 1 38  ? 19.956  -4.438  25.312 1.00 21.26  ? 39   ALA A CB    1 
ATOM   252  N  N     . GLY A 1 39  ? 20.148  -6.967  27.760 1.00 19.14  ? 40   GLY A N     1 
ATOM   253  C  CA    . GLY A 1 39  ? 20.048  -7.056  29.204 1.00 19.55  ? 40   GLY A CA    1 
ATOM   254  C  C     . GLY A 1 39  ? 18.920  -6.262  29.817 1.00 22.68  ? 40   GLY A C     1 
ATOM   255  O  O     . GLY A 1 39  ? 18.864  -6.125  31.047 1.00 24.39  ? 40   GLY A O     1 
ATOM   256  N  N     . MET A 1 40  ? 17.955  -5.816  29.016 1.00 18.59  ? 41   MET A N     1 
ATOM   257  C  CA    . MET A 1 40  ? 16.922  -4.918  29.496 1.00 19.04  ? 41   MET A CA    1 
ATOM   258  C  C     . MET A 1 40  ? 15.577  -5.602  29.677 1.00 20.97  ? 41   MET A C     1 
ATOM   259  O  O     . MET A 1 40  ? 14.577  -4.916  29.936 1.00 21.96  ? 41   MET A O     1 
ATOM   260  C  CB    . MET A 1 40  ? 16.774  -3.727  28.548 1.00 19.10  ? 41   MET A CB    1 
ATOM   261  C  CG    . MET A 1 40  ? 18.068  -2.878  28.583 1.00 20.62  ? 41   MET A CG    1 
ATOM   262  S  SD    . MET A 1 40  ? 17.868  -1.229  27.967 1.00 22.54  ? 41   MET A SD    1 
ATOM   263  C  CE    . MET A 1 40  ? 17.472  -1.652  26.291 1.00 24.89  ? 41   MET A CE    1 
ATOM   264  N  N     . ALA A 1 41  ? 15.511  -6.923  29.567 1.00 20.67  ? 42   ALA A N     1 
ATOM   265  C  CA    . ALA A 1 41  ? 14.260  -7.646  29.774 1.00 18.63  ? 42   ALA A CA    1 
ATOM   266  C  C     . ALA A 1 41  ? 14.618  -9.099  29.993 1.00 18.38  ? 42   ALA A C     1 
ATOM   267  O  O     . ALA A 1 41  ? 15.674  -9.571  29.559 1.00 23.03  ? 42   ALA A O     1 
ATOM   268  C  CB    . ALA A 1 41  ? 13.319  -7.547  28.573 1.00 18.68  ? 42   ALA A CB    1 
ATOM   269  N  N     . LYS A 1 42  ? 13.712  -9.816  30.638 1.00 20.10  ? 43   LYS A N     1 
ATOM   270  C  CA    . LYS A 1 42  ? 13.665  -11.261 30.516 1.00 23.32  ? 43   LYS A CA    1 
ATOM   271  C  C     . LYS A 1 42  ? 12.900  -11.614 29.254 1.00 20.20  ? 43   LYS A C     1 
ATOM   272  O  O     . LYS A 1 42  ? 11.793  -11.108 29.029 1.00 22.33  ? 43   LYS A O     1 
ATOM   273  C  CB    . LYS A 1 42  ? 12.969  -11.851 31.737 1.00 27.94  ? 43   LYS A CB    1 
ATOM   274  C  CG    . LYS A 1 42  ? 12.839  -13.363 31.738 1.00 44.82  ? 43   LYS A CG    1 
ATOM   275  C  CD    . LYS A 1 42  ? 12.345  -13.876 33.102 1.00 59.65  ? 43   LYS A CD    1 
ATOM   276  C  CE    . LYS A 1 42  ? 10.851  -13.656 33.318 1.00 65.24  ? 43   LYS A CE    1 
ATOM   277  N  NZ    . LYS A 1 42  ? 10.043  -14.618 32.524 1.00 67.91  ? 43   LYS A NZ    1 
ATOM   278  N  N     . ALA A 1 43  ? 13.526  -12.380 28.374 1.00 20.67  ? 44   ALA A N     1 
ATOM   279  C  CA    . ALA A 1 43  ? 12.819  -12.775 27.160 1.00 21.19  ? 44   ALA A CA    1 
ATOM   280  C  C     . ALA A 1 43  ? 11.611  -13.646 27.522 1.00 20.50  ? 44   ALA A C     1 
ATOM   281  O  O     . ALA A 1 43  ? 11.731  -14.585 28.332 1.00 23.68  ? 44   ALA A O     1 
ATOM   282  C  CB    . ALA A 1 43  ? 13.756  -13.576 26.281 1.00 22.89  ? 44   ALA A CB    1 
ATOM   283  N  N     . ARG A 1 44  ? 10.457  -13.355 26.897 1.00 20.97  ? 45   ARG A N     1 
ATOM   284  C  CA    . ARG A 1 44  ? 9.209   -14.082 27.164 1.00 20.87  ? 45   ARG A CA    1 
ATOM   285  C  C     . ARG A 1 44  ? 8.782   -14.732 25.858 1.00 20.40  ? 45   ARG A C     1 
ATOM   286  O  O     . ARG A 1 44  ? 8.723   -14.043 24.822 1.00 25.29  ? 45   ARG A O     1 
ATOM   287  C  CB    . ARG A 1 44  ? 8.118   -13.135 27.695 1.00 22.18  ? 45   ARG A CB    1 
ATOM   288  C  CG    . ARG A 1 44  ? 8.423   -12.417 29.073 1.00 27.91  ? 45   ARG A CG    1 
ATOM   289  C  CD    . ARG A 1 44  ? 8.276   -13.317 30.280 1.00 29.07  ? 45   ARG A CD    1 
ATOM   290  N  NE    . ARG A 1 44  ? 6.912   -13.876 30.431 1.00 30.31  ? 45   ARG A NE    1 
ATOM   291  C  CZ    . ARG A 1 44  ? 5.840   -13.255 30.951 1.00 29.04  ? 45   ARG A CZ    1 
ATOM   292  N  NH1   . ARG A 1 44  ? 5.921   -12.019 31.441 1.00 29.56  ? 45   ARG A NH1   1 
ATOM   293  N  NH2   . ARG A 1 44  ? 4.652   -13.873 30.972 1.00 29.77  ? 45   ARG A NH2   1 
ATOM   294  N  N     . ALA A 1 45  ? 8.570   -16.038 25.896 1.00 22.40  ? 46   ALA A N     1 
ATOM   295  C  CA    . ALA A 1 45  ? 8.191   -16.801 24.701 1.00 21.15  ? 46   ALA A CA    1 
ATOM   296  C  C     . ALA A 1 45  ? 6.742   -16.508 24.340 1.00 25.14  ? 46   ALA A C     1 
ATOM   297  O  O     . ALA A 1 45  ? 5.888   -16.287 25.209 1.00 21.69  ? 46   ALA A O     1 
ATOM   298  C  CB    . ALA A 1 45  ? 8.357   -18.279 24.953 1.00 29.27  ? 46   ALA A CB    1 
ATOM   299  N  N     . TYR A 1 46  ? 6.461   -16.549 23.035 1.00 19.94  ? 47   TYR A N     1 
ATOM   300  C  CA    . TYR A 1 46  ? 5.084   -16.418 22.600 1.00 17.92  ? 47   TYR A CA    1 
ATOM   301  C  C     . TYR A 1 46  ? 4.153   -17.325 23.359 1.00 20.20  ? 47   TYR A C     1 
ATOM   302  O  O     . TYR A 1 46  ? 3.069   -16.895 23.771 1.00 20.81  ? 47   TYR A O     1 
ATOM   303  C  CB    . TYR A 1 46  ? 5.024   -16.751 21.100 1.00 19.85  ? 47   TYR A CB    1 
ATOM   304  C  CG    . TYR A 1 46  ? 3.624   -16.785 20.540 1.00 17.73  ? 47   TYR A CG    1 
ATOM   305  C  CD1   . TYR A 1 46  ? 2.970   -15.613 20.165 1.00 16.07  ? 47   TYR A CD1   1 
ATOM   306  C  CD2   . TYR A 1 46  ? 2.923   -17.977 20.469 1.00 18.02  ? 47   TYR A CD2   1 
ATOM   307  C  CE1   . TYR A 1 46  ? 1.646   -15.653 19.675 1.00 17.32  ? 47   TYR A CE1   1 
ATOM   308  C  CE2   . TYR A 1 46  ? 1.582   -18.028 20.000 1.00 17.46  ? 47   TYR A CE2   1 
ATOM   309  C  CZ    . TYR A 1 46  ? 0.983   -16.864 19.604 1.00 17.31  ? 47   TYR A CZ    1 
ATOM   310  O  OH    . TYR A 1 46  ? -0.299  -16.929 19.102 1.00 19.71  ? 47   TYR A OH    1 
ATOM   311  N  N     . ALA A 1 47  ? 4.513   -18.609 23.480 1.00 18.30  ? 48   ALA A N     1 
ATOM   312  C  CA    . ALA A 1 47  ? 3.569   -19.558 24.048 1.00 20.05  ? 48   ALA A CA    1 
ATOM   313  C  C     . ALA A 1 47  ? 3.220   -19.177 25.493 1.00 27.68  ? 48   ALA A C     1 
ATOM   314  O  O     . ALA A 1 47  ? 2.069   -19.382 25.933 1.00 27.12  ? 48   ALA A O     1 
ATOM   315  C  CB    . ALA A 1 47  ? 4.175   -20.957 23.949 1.00 25.26  ? 48   ALA A CB    1 
ATOM   316  N  N     . ASP A 1 48  ? 4.180   -18.567 26.202 1.00 25.25  ? 49   ASP A N     1 
ATOM   317  C  CA    . ASP A 1 48  ? 3.989   -18.140 27.597 1.00 25.44  ? 49   ASP A CA    1 
ATOM   318  C  C     . ASP A 1 48  ? 3.000   -16.978 27.661 1.00 26.40  ? 49   ASP A C     1 
ATOM   319  O  O     . ASP A 1 48  ? 1.958   -17.060 28.332 1.00 28.19  ? 49   ASP A O     1 
ATOM   320  C  CB    . ASP A 1 48  ? 5.375   -17.758 28.139 1.00 23.78  ? 49   ASP A CB    1 
ATOM   321  C  CG    . ASP A 1 48  ? 5.379   -17.058 29.497 1.00 46.31  ? 49   ASP A CG    1 
ATOM   322  O  OD1   . ASP A 1 48  ? 4.330   -16.869 30.142 1.00 44.30  ? 49   ASP A OD1   1 
ATOM   323  O  OD2   . ASP A 1 48  ? 6.510   -16.641 29.889 1.00 37.18  ? 49   ASP A OD2   1 
ATOM   324  N  N     . ILE A 1 49  ? 3.271   -15.918 26.885 1.00 19.75  ? 50   ILE A N     1 
ATOM   325  C  CA    . ILE A 1 49  ? 2.424   -14.730 26.904 1.00 21.47  ? 50   ILE A CA    1 
ATOM   326  C  C     . ILE A 1 49  ? 1.023   -15.069 26.385 1.00 23.66  ? 50   ILE A C     1 
ATOM   327  O  O     . ILE A 1 49  ? 0.021   -14.530 26.877 1.00 21.71  ? 50   ILE A O     1 
ATOM   328  C  CB    . ILE A 1 49  ? 3.062   -13.612 26.061 1.00 18.56  ? 50   ILE A CB    1 
ATOM   329  C  CG1   . ILE A 1 49  ? 4.458   -13.233 26.552 1.00 21.88  ? 50   ILE A CG1   1 
ATOM   330  C  CG2   . ILE A 1 49  ? 2.206   -12.349 26.040 1.00 22.03  ? 50   ILE A CG2   1 
ATOM   331  C  CD1   . ILE A 1 49  ? 5.222   -12.366 25.571 1.00 24.98  ? 50   ILE A CD1   1 
ATOM   332  N  N     . ASP A 1 50  ? 0.943   -15.924 25.338 1.00 19.29  ? 51   ASP A N     1 
ATOM   333  C  CA    . ASP A 1 50  ? -0.340  -16.316 24.747 1.00 21.32  ? 51   ASP A CA    1 
ATOM   334  C  C     . ASP A 1 50  ? -1.241  -17.018 25.755 1.00 25.03  ? 51   ASP A C     1 
ATOM   335  O  O     . ASP A 1 50  ? -2.466  -16.863 25.706 1.00 26.63  ? 51   ASP A O     1 
ATOM   336  C  CB    . ASP A 1 50  ? -0.067  -17.209 23.516 1.00 21.94  ? 51   ASP A CB    1 
ATOM   337  C  CG    . ASP A 1 50  ? -1.335  -17.637 22.800 1.00 25.23  ? 51   ASP A CG    1 
ATOM   338  O  OD1   . ASP A 1 50  ? -2.064  -16.786 22.270 1.00 27.11  ? 51   ASP A OD1   1 
ATOM   339  O  OD2   . ASP A 1 50  ? -1.597  -18.853 22.768 1.00 29.74  ? 51   ASP A OD2   1 
ATOM   340  N  N     . ALA A 1 51  ? -0.657  -17.780 26.671 1.00 22.79  ? 52   ALA A N     1 
ATOM   341  C  CA    . ALA A 1 51  ? -1.412  -18.504 27.701 1.00 24.25  ? 52   ALA A CA    1 
ATOM   342  C  C     . ALA A 1 51  ? -1.613  -17.584 28.911 1.00 26.89  ? 52   ALA A C     1 
ATOM   343  O  O     . ALA A 1 51  ? -1.123  -17.838 30.002 1.00 31.55  ? 52   ALA A O     1 
ATOM   344  C  CB    . ALA A 1 51  ? -0.665  -19.774 28.091 1.00 29.74  ? 52   ALA A CB    1 
ATOM   345  N  N     . ALA A 1 52  ? -2.323  -16.478 28.690 1.00 27.98  ? 53   ALA A N     1 
ATOM   346  C  CA    . ALA A 1 52  ? -2.501  -15.475 29.739 1.00 24.35  ? 53   ALA A CA    1 
ATOM   347  C  C     . ALA A 1 52  ? -3.322  -16.030 30.898 1.00 30.29  ? 53   ALA A C     1 
ATOM   348  O  O     . ALA A 1 52  ? -4.367  -16.645 30.676 1.00 33.07  ? 53   ALA A O     1 
ATOM   349  C  CB    . ALA A 1 52  ? -3.208  -14.231 29.195 1.00 26.14  ? 53   ALA A CB    1 
ATOM   350  N  N     . PRO A 1 53  ? -2.933  -15.737 32.135 1.00 28.63  ? 54   PRO A N     1 
ATOM   351  C  CA    . PRO A 1 53  ? -3.696  -16.204 33.298 1.00 31.26  ? 54   PRO A CA    1 
ATOM   352  C  C     . PRO A 1 53  ? -4.951  -15.376 33.576 1.00 30.83  ? 54   PRO A C     1 
ATOM   353  O  O     . PRO A 1 53  ? -5.077  -14.216 33.171 1.00 29.48  ? 54   PRO A O     1 
ATOM   354  C  CB    . PRO A 1 53  ? -2.678  -16.063 34.432 1.00 33.61  ? 54   PRO A CB    1 
ATOM   355  C  CG    . PRO A 1 53  ? -1.783  -14.976 34.024 1.00 33.33  ? 54   PRO A CG    1 
ATOM   356  C  CD    . PRO A 1 53  ? -1.704  -15.013 32.514 1.00 30.59  ? 54   PRO A CD    1 
ATOM   357  N  N     . GLU A 1 54  ? -5.903  -16.009 34.277 1.00 33.51  ? 55   GLU A N     1 
ATOM   358  C  CA    . GLU A 1 54  ? -7.063  -15.278 34.784 1.00 38.63  ? 55   GLU A CA    1 
ATOM   359  C  C     . GLU A 1 54  ? -6.702  -14.432 35.991 1.00 45.41  ? 55   GLU A C     1 
ATOM   360  O  O     . GLU A 1 54  ? -5.932  -14.843 36.868 1.00 44.18  ? 55   GLU A O     1 
ATOM   361  C  CB    . GLU A 1 54  ? -8.211  -16.196 35.213 1.00 52.49  ? 55   GLU A CB    1 
ATOM   362  C  CG    . GLU A 1 54  ? -9.101  -16.745 34.142 1.00 66.36  ? 55   GLU A CG    1 
ATOM   363  C  CD    . GLU A 1 54  ? -10.390 -17.313 34.725 1.00 76.94  ? 55   GLU A CD    1 
ATOM   364  O  OE1   . GLU A 1 54  ? -10.534 -17.301 35.968 1.00 80.62  ? 55   GLU A OE1   1 
ATOM   365  O  OE2   . GLU A 1 54  ? -11.257 -17.762 33.948 1.00 79.69  ? 55   GLU A OE2   1 
ATOM   366  N  N     . GLU A 1 55  ? -7.314  -13.264 36.058 1.00 34.96  ? 56   GLU A N     1 
ATOM   367  C  CA    . GLU A 1 55  ? -7.190  -12.354 37.185 1.00 34.46  ? 56   GLU A CA    1 
ATOM   368  C  C     . GLU A 1 55  ? -8.585  -11.875 37.535 1.00 40.42  ? 56   GLU A C     1 
ATOM   369  O  O     . GLU A 1 55  ? -9.395  -11.618 36.639 1.00 36.83  ? 56   GLU A O     1 
ATOM   370  C  CB    . GLU A 1 55  ? -6.276  -11.196 36.816 1.00 49.08  ? 56   GLU A CB    1 
ATOM   371  C  CG    . GLU A 1 55  ? -4.909  -11.711 36.444 1.00 61.57  ? 56   GLU A CG    1 
ATOM   372  C  CD    . GLU A 1 55  ? -4.007  -10.664 35.836 1.00 67.63  ? 56   GLU A CD    1 
ATOM   373  O  OE1   . GLU A 1 55  ? -4.441  -9.497  35.680 1.00 65.69  ? 56   GLU A OE1   1 
ATOM   374  O  OE2   . GLU A 1 55  ? -2.873  -11.043 35.472 1.00 72.42  ? 56   GLU A OE2   1 
ATOM   375  N  N     . LYS A 1 56  ? -8.876  -11.811 38.830 1.00 43.27  ? 57   LYS A N     1 
ATOM   376  C  CA    . LYS A 1 56  ? -10.168 -11.401 39.363 1.00 61.06  ? 57   LYS A CA    1 
ATOM   377  C  C     . LYS A 1 56  ? -9.965  -10.230 40.309 1.00 77.59  ? 57   LYS A C     1 
ATOM   378  O  O     . LYS A 1 56  ? -9.013  -10.218 41.098 1.00 84.67  ? 57   LYS A O     1 
ATOM   379  C  CB    . LYS A 1 56  ? -10.846 -12.529 40.125 1.00 61.63  ? 57   LYS A CB    1 
ATOM   380  C  CG    . LYS A 1 56  ? -11.203 -13.730 39.301 1.00 67.78  ? 57   LYS A CG    1 
ATOM   381  C  CD    . LYS A 1 56  ? -11.906 -14.749 40.178 1.00 72.49  ? 57   LYS A CD    1 
ATOM   382  C  CE    . LYS A 1 56  ? -12.212 -16.017 39.410 1.00 80.70  ? 57   LYS A CE    1 
ATOM   383  N  NZ    . LYS A 1 56  ? -13.225 -15.778 38.343 1.00 82.97  ? 57   LYS A NZ    1 
ATOM   384  N  N     . ALA A 1 57  ? -10.867 -9.253  40.241 1.00 83.37  ? 58   ALA A N     1 
ATOM   385  C  CA    . ALA A 1 57  ? -10.691 -8.006  40.982 1.00 89.54  ? 58   ALA A CA    1 
ATOM   386  C  C     . ALA A 1 57  ? -12.040 -7.317  41.118 1.00 81.21  ? 58   ALA A C     1 
ATOM   387  O  O     . ALA A 1 57  ? -12.665 -6.981  40.106 1.00 69.28  ? 58   ALA A O     1 
ATOM   388  C  CB    . ALA A 1 57  ? -9.680  -7.101  40.266 1.00 102.92 ? 58   ALA A CB    1 
ATOM   389  N  N     . ARG A 1 58  ? -12.494 -7.120  42.356 1.00 80.86  ? 59   ARG A N     1 
ATOM   390  C  CA    . ARG A 1 58  ? -13.731 -6.382  42.628 1.00 87.99  ? 59   ARG A CA    1 
ATOM   391  C  C     . ARG A 1 58  ? -14.898 -6.952  41.820 1.00 91.95  ? 59   ARG A C     1 
ATOM   392  O  O     . ARG A 1 58  ? -15.743 -6.219  41.300 1.00 95.06  ? 59   ARG A O     1 
ATOM   393  C  CB    . ARG A 1 58  ? -13.538 -4.889  42.345 1.00 86.86  ? 59   ARG A CB    1 
ATOM   394  C  CG    . ARG A 1 58  ? -12.502 -4.233  43.247 1.00 86.74  ? 59   ARG A CG    1 
ATOM   395  C  CD    . ARG A 1 58  ? -12.300 -2.766  42.915 1.00 88.07  ? 59   ARG A CD    1 
ATOM   396  N  NE    . ARG A 1 58  ? -11.896 -2.606  41.518 1.00 94.24  ? 59   ARG A NE    1 
ATOM   397  C  CZ    . ARG A 1 58  ? -10.661 -2.797  41.058 1.00 95.89  ? 59   ARG A CZ    1 
ATOM   398  N  NH1   . ARG A 1 58  ? -9.696  -3.178  41.883 1.00 99.66  ? 59   ARG A NH1   1 
ATOM   399  N  NH2   . ARG A 1 58  ? -10.393 -2.628  39.766 1.00 92.52  ? 59   ARG A NH2   1 
ATOM   400  N  N     . GLY A 1 59  ? -14.915 -8.277  41.680 1.00 87.25  ? 60   GLY A N     1 
ATOM   401  C  CA    . GLY A 1 59  ? -15.996 -8.966  41.003 1.00 79.10  ? 60   GLY A CA    1 
ATOM   402  C  C     . GLY A 1 59  ? -15.887 -9.082  39.497 1.00 67.48  ? 60   GLY A C     1 
ATOM   403  O  O     . GLY A 1 59  ? -16.892 -9.394  38.848 1.00 62.09  ? 60   GLY A O     1 
ATOM   404  N  N     . ILE A 1 60  ? -14.708 -8.861  38.908 1.00 50.42  ? 61   ILE A N     1 
ATOM   405  C  CA    . ILE A 1 60  ? -14.593 -8.862  37.452 1.00 42.65  ? 61   ILE A CA    1 
ATOM   406  C  C     . ILE A 1 60  ? -13.370 -9.674  37.041 1.00 48.27  ? 61   ILE A C     1 
ATOM   407  O  O     . ILE A 1 60  ? -12.253 -9.402  37.495 1.00 52.01  ? 61   ILE A O     1 
ATOM   408  C  CB    . ILE A 1 60  ? -14.535 -7.432  36.885 1.00 50.75  ? 61   ILE A CB    1 
ATOM   409  C  CG1   . ILE A 1 60  ? -15.923 -6.789  37.011 1.00 55.43  ? 61   ILE A CG1   1 
ATOM   410  C  CG2   . ILE A 1 60  ? -14.028 -7.436  35.432 1.00 48.15  ? 61   ILE A CG2   1 
ATOM   411  C  CD1   . ILE A 1 60  ? -15.930 -5.301  36.944 1.00 57.05  ? 61   ILE A CD1   1 
ATOM   412  N  N     . THR A 1 61  ? -13.582 -10.658 36.175 1.00 33.04  ? 62   THR A N     1 
ATOM   413  C  CA    . THR A 1 61  ? -12.567 -11.614 35.762 1.00 35.19  ? 62   THR A CA    1 
ATOM   414  C  C     . THR A 1 61  ? -12.072 -11.277 34.355 1.00 31.77  ? 62   THR A C     1 
ATOM   415  O  O     . THR A 1 61  ? -12.879 -11.064 33.440 1.00 32.87  ? 62   THR A O     1 
ATOM   416  C  CB    . THR A 1 61  ? -13.139 -13.029 35.791 1.00 40.27  ? 62   THR A CB    1 
ATOM   417  O  OG1   . THR A 1 61  ? -13.583 -13.331 37.127 1.00 53.43  ? 62   THR A OG1   1 
ATOM   418  C  CG2   . THR A 1 61  ? -12.084 -14.024 35.379 1.00 39.49  ? 62   THR A CG2   1 
ATOM   419  N  N     . ILE A 1 62  ? -10.747 -11.196 34.191 1.00 28.89  ? 63   ILE A N     1 
ATOM   420  C  CA    . ILE A 1 62  ? -10.126 -10.835 32.932 1.00 25.96  ? 63   ILE A CA    1 
ATOM   421  C  C     . ILE A 1 62  ? -8.924  -11.745 32.735 1.00 29.82  ? 63   ILE A C     1 
ATOM   422  O  O     . ILE A 1 62  ? -8.217  -12.053 33.699 1.00 32.15  ? 63   ILE A O     1 
ATOM   423  C  CB    . ILE A 1 62  ? -9.661  -9.362  32.937 1.00 26.82  ? 63   ILE A CB    1 
ATOM   424  C  CG1   . ILE A 1 62  ? -10.792 -8.450  33.440 1.00 35.72  ? 63   ILE A CG1   1 
ATOM   425  C  CG2   . ILE A 1 62  ? -9.298  -8.917  31.539 1.00 26.40  ? 63   ILE A CG2   1 
ATOM   426  C  CD1   . ILE A 1 62  ? -10.354 -6.976  33.502 1.00 35.33  ? 63   ILE A CD1   1 
ATOM   427  N  N     . ASN A 1 63  ? -8.669  -12.155 31.507 1.00 25.50  ? 64   ASN A N     1 
ATOM   428  C  CA    . ASN A 1 63  ? -7.418  -12.853 31.170 1.00 22.87  ? 64   ASN A CA    1 
ATOM   429  C  C     . ASN A 1 63  ? -6.422  -11.827 30.637 1.00 23.13  ? 64   ASN A C     1 
ATOM   430  O  O     . ASN A 1 63  ? -6.695  -11.156 29.636 1.00 22.98  ? 64   ASN A O     1 
ATOM   431  C  CB    . ASN A 1 63  ? -7.683  -13.919 30.110 1.00 24.35  ? 64   ASN A CB    1 
ATOM   432  C  CG    . ASN A 1 63  ? -8.729  -14.919 30.520 1.00 34.07  ? 64   ASN A CG    1 
ATOM   433  O  OD1   . ASN A 1 63  ? -8.593  -15.551 31.524 1.00 40.06  ? 64   ASN A OD1   1 
ATOM   434  N  ND2   . ASN A 1 63  ? -9.817  -15.005 29.764 1.00 42.71  ? 64   ASN A ND2   1 
ATOM   435  N  N     . THR A 1 64  ? -5.263  -11.687 31.303 1.00 23.92  ? 65   THR A N     1 
ATOM   436  C  CA    . THR A 1 64  ? -4.294  -10.632 30.980 1.00 22.99  ? 65   THR A CA    1 
ATOM   437  C  C     . THR A 1 64  ? -2.886  -11.184 31.211 1.00 21.60  ? 65   THR A C     1 
ATOM   438  O  O     . THR A 1 64  ? -2.620  -11.790 32.270 1.00 25.61  ? 65   THR A O     1 
ATOM   439  C  CB    . THR A 1 64  ? -4.485  -9.368  31.857 1.00 25.88  ? 65   THR A CB    1 
ATOM   440  O  OG1   . THR A 1 64  ? -5.850  -8.911  31.778 1.00 37.40  ? 65   THR A OG1   1 
ATOM   441  C  CG2   . THR A 1 64  ? -3.587  -8.184  31.424 1.00 26.63  ? 65   THR A CG2   1 
ATOM   442  N  N     . ALA A 1 65  ? -2.029  -11.018 30.219 1.00 20.79  ? 66   ALA A N     1 
ATOM   443  C  CA    . ALA A 1 65  ? -0.606  -11.231 30.391 1.00 20.58  ? 66   ALA A CA    1 
ATOM   444  C  C     . ALA A 1 65  ? 0.049   -9.917  30.798 1.00 21.19  ? 66   ALA A C     1 
ATOM   445  O  O     . ALA A 1 65  ? -0.321  -8.844  30.316 1.00 21.78  ? 66   ALA A O     1 
ATOM   446  C  CB    . ALA A 1 65  ? 0.016   -11.751 29.090 1.00 23.78  ? 66   ALA A CB    1 
ATOM   447  N  N     . HIS A 1 66  ? 1.039   -10.011 31.686 1.00 22.37  ? 67   HIS A N     1 
ATOM   448  C  CA    . HIS A 1 66  ? 1.828   -8.866  32.127 1.00 22.18  ? 67   HIS A CA    1 
ATOM   449  C  C     . HIS A 1 66  ? 3.294   -9.120  31.802 1.00 24.87  ? 67   HIS A C     1 
ATOM   450  O  O     . HIS A 1 66  ? 3.859   -10.124 32.247 1.00 27.31  ? 67   HIS A O     1 
ATOM   451  C  CB    . HIS A 1 66  ? 1.658   -8.679  33.632 1.00 24.65  ? 67   HIS A CB    1 
ATOM   452  C  CG    . HIS A 1 66  ? 0.244   -8.375  34.052 1.00 28.57  ? 67   HIS A CG    1 
ATOM   453  N  ND1   . HIS A 1 66  ? -0.289  -7.106  34.023 1.00 34.35  ? 67   HIS A ND1   1 
ATOM   454  C  CD2   . HIS A 1 66  ? -0.762  -9.190  34.448 1.00 31.75  ? 67   HIS A CD2   1 
ATOM   455  C  CE1   . HIS A 1 66  ? -1.553  -7.142  34.404 1.00 33.53  ? 67   HIS A CE1   1 
ATOM   456  N  NE2   . HIS A 1 66  ? -1.865  -8.394  34.682 1.00 32.40  ? 67   HIS A NE2   1 
ATOM   457  N  N     . VAL A 1 67  ? 3.921   -8.214  31.090 1.00 19.74  ? 68   VAL A N     1 
ATOM   458  C  CA    . VAL A 1 67  ? 5.367   -8.324  30.896 1.00 19.85  ? 68   VAL A CA    1 
ATOM   459  C  C     . VAL A 1 67  ? 5.984   -6.999  31.319 1.00 19.94  ? 68   VAL A C     1 
ATOM   460  O  O     . VAL A 1 67  ? 5.327   -5.959  31.392 1.00 19.68  ? 68   VAL A O     1 
ATOM   461  C  CB    . VAL A 1 67  ? 5.847   -8.726  29.438 1.00 22.53  ? 68   VAL A CB    1 
ATOM   462  C  CG1   . VAL A 1 67  ? 5.183   -10.042 28.956 1.00 27.55  ? 68   VAL A CG1   1 
ATOM   463  C  CG2   . VAL A 1 67  ? 5.741   -7.637  28.454 1.00 25.17  ? 68   VAL A CG2   1 
ATOM   464  N  N     . GLU A 1 68  ? 7.243   -7.075  31.728 1.00 18.76  ? 69   GLU A N     1 
ATOM   465  C  CA    . GLU A 1 68  ? 8.004   -5.892  32.064 1.00 21.77  ? 69   GLU A CA    1 
ATOM   466  C  C     . GLU A 1 68  ? 9.290   -5.878  31.275 1.00 21.85  ? 69   GLU A C     1 
ATOM   467  O  O     . GLU A 1 68  ? 9.906   -6.922  31.033 1.00 21.78  ? 69   GLU A O     1 
ATOM   468  C  CB    . GLU A 1 68  ? 8.329   -5.880  33.574 1.00 27.16  ? 69   GLU A CB    1 
ATOM   469  C  CG    . GLU A 1 68  ? 7.095   -5.575  34.401 1.00 46.63  ? 69   GLU A CG    1 
ATOM   470  C  CD    . GLU A 1 68  ? 7.401   -5.485  35.884 1.00 65.09  ? 69   GLU A CD    1 
ATOM   471  O  OE1   . GLU A 1 68  ? 8.550   -5.792  36.273 1.00 69.10  ? 69   GLU A OE1   1 
ATOM   472  O  OE2   . GLU A 1 68  ? 6.495   -5.101  36.653 1.00 71.08  ? 69   GLU A OE2   1 
ATOM   473  N  N     . TYR A 1 69  ? 9.712   -4.669  30.904 1.00 20.27  ? 70   TYR A N     1 
ATOM   474  C  CA    . TYR A 1 69  ? 10.961  -4.503  30.195 1.00 20.50  ? 70   TYR A CA    1 
ATOM   475  C  C     . TYR A 1 69  ? 11.314  -3.040  30.280 1.00 20.52  ? 70   TYR A C     1 
ATOM   476  O  O     . TYR A 1 69  ? 10.543  -2.232  30.797 1.00 21.00  ? 70   TYR A O     1 
ATOM   477  C  CB    . TYR A 1 69  ? 10.756  -5.095  28.813 1.00 19.83  ? 70   TYR A CB    1 
ATOM   478  C  CG    . TYR A 1 69  ? 9.731   -4.418  27.907 1.00 19.82  ? 70   TYR A CG    1 
ATOM   479  C  CD1   . TYR A 1 69  ? 9.733   -3.062  27.587 1.00 19.09  ? 70   TYR A CD1   1 
ATOM   480  C  CD2   . TYR A 1 69  ? 8.520   -5.097  27.726 1.00 18.15  ? 70   TYR A CD2   1 
ATOM   481  C  CE1   . TYR A 1 69  ? 8.702   -2.490  26.848 1.00 17.42  ? 70   TYR A CE1   1 
ATOM   482  C  CE2   . TYR A 1 69  ? 7.479   -4.545  26.987 1.00 17.85  ? 70   TYR A CE2   1 
ATOM   483  C  CZ    . TYR A 1 69  ? 7.557   -3.255  26.566 1.00 18.10  ? 70   TYR A CZ    1 
ATOM   484  O  OH    . TYR A 1 69  ? 6.524   -2.676  25.877 1.00 19.07  ? 70   TYR A OH    1 
ATOM   485  N  N     . GLU A 1 70  ? 12.537  -2.713  29.877 1.00 19.98  ? 71   GLU A N     1 
ATOM   486  C  CA    . GLU A 1 70  ? 12.899  -1.303  29.747 1.00 18.41  ? 71   GLU A CA    1 
ATOM   487  C  C     . GLU A 1 70  ? 13.646  -1.101  28.453 1.00 17.00  ? 71   GLU A C     1 
ATOM   488  O  O     . GLU A 1 70  ? 14.244  -2.025  27.894 1.00 19.19  ? 71   GLU A O     1 
ATOM   489  C  CB    . GLU A 1 70  ? 13.755  -0.742  30.908 1.00 17.85  ? 71   GLU A CB    1 
ATOM   490  C  CG    . GLU A 1 70  ? 15.095  -1.568  31.154 1.00 21.02  ? 71   GLU A CG    1 
ATOM   491  C  CD    . GLU A 1 70  ? 15.753  -1.284  32.483 1.00 20.88  ? 71   GLU A CD    1 
ATOM   492  O  OE1   . GLU A 1 70  ? 16.327  -0.201  32.752 1.00 26.01  ? 71   GLU A OE1   1 
ATOM   493  O  OE2   . GLU A 1 70  ? 15.423  -2.099  33.366 1.00 31.35  ? 71   GLU A OE2   1 
ATOM   494  N  N     . THR A 1 71  ? 13.581  0.140   27.981 1.00 19.35  ? 72   THR A N     1 
ATOM   495  C  CA    . THR A 1 71  ? 14.473  0.633   26.962 1.00 19.67  ? 72   THR A CA    1 
ATOM   496  C  C     . THR A 1 71  ? 15.568  1.425   27.655 1.00 18.28  ? 72   THR A C     1 
ATOM   497  O  O     . THR A 1 71  ? 15.578  1.571   28.896 1.00 18.73  ? 72   THR A O     1 
ATOM   498  C  CB    . THR A 1 71  ? 13.769  1.591   26.003 1.00 19.52  ? 72   THR A CB    1 
ATOM   499  O  OG1   . THR A 1 71  ? 13.264  2.716   26.767 1.00 21.99  ? 72   THR A OG1   1 
ATOM   500  C  CG2   . THR A 1 71  ? 12.569  0.918   25.293 1.00 21.83  ? 72   THR A CG2   1 
ATOM   501  N  N     . GLY A 1 72  ? 16.483  2.037   26.885 1.00 20.82  ? 73   GLY A N     1 
ATOM   502  C  CA    . GLY A 1 72  ? 17.478  2.909   27.494 1.00 21.50  ? 73   GLY A CA    1 
ATOM   503  C  C     . GLY A 1 72  ? 16.866  4.122   28.165 1.00 20.90  ? 73   GLY A C     1 
ATOM   504  O  O     . GLY A 1 72  ? 17.493  4.751   29.041 1.00 24.52  ? 73   GLY A O     1 
ATOM   505  N  N     . ASN A 1 73  ? 15.627  4.466   27.795 1.00 20.31  ? 74   ASN A N     1 
ATOM   506  C  CA    . ASN A 1 73  ? 14.979  5.666   28.287 1.00 21.76  ? 74   ASN A CA    1 
ATOM   507  C  C     . ASN A 1 73  ? 13.970  5.415   29.389 1.00 22.74  ? 74   ASN A C     1 
ATOM   508  O  O     . ASN A 1 73  ? 13.756  6.315   30.203 1.00 24.88  ? 74   ASN A O     1 
ATOM   509  C  CB    . ASN A 1 73  ? 14.271  6.376   27.136 1.00 20.81  ? 74   ASN A CB    1 
ATOM   510  C  CG    . ASN A 1 73  ? 15.246  6.840   26.102 1.00 25.42  ? 74   ASN A CG    1 
ATOM   511  O  OD1   . ASN A 1 73  ? 16.239  7.536   26.434 1.00 28.57  ? 74   ASN A OD1   1 
ATOM   512  N  ND2   . ASN A 1 73  ? 15.048  6.408   24.870 1.00 22.78  ? 74   ASN A ND2   1 
ATOM   513  N  N     . ARG A 1 74  ? 13.307  4.265   29.426 1.00 21.19  ? 75   ARG A N     1 
ATOM   514  C  CA    . ARG A 1 74  ? 12.112  4.195   30.260 1.00 21.04  ? 75   ARG A CA    1 
ATOM   515  C  C     . ARG A 1 74  ? 11.825  2.736   30.567 1.00 17.87  ? 75   ARG A C     1 
ATOM   516  O  O     . ARG A 1 74  ? 12.043  1.874   29.720 1.00 19.91  ? 75   ARG A O     1 
ATOM   517  C  CB    . ARG A 1 74  ? 10.910  4.891   29.535 1.00 18.31  ? 75   ARG A CB    1 
ATOM   518  C  CG    . ARG A 1 74  ? 9.645   4.966   30.411 1.00 22.33  ? 75   ARG A CG    1 
ATOM   519  C  CD    . ARG A 1 74  ? 8.778   6.136   29.975 1.00 19.53  ? 75   ARG A CD    1 
ATOM   520  N  NE    . ARG A 1 74  ? 8.289   5.901   28.600 1.00 17.56  ? 75   ARG A NE    1 
ATOM   521  C  CZ    . ARG A 1 74  ? 7.478   6.745   27.964 1.00 18.30  ? 75   ARG A CZ    1 
ATOM   522  N  NH1   . ARG A 1 74  ? 7.049   7.868   28.565 1.00 21.35  ? 75   ARG A NH1   1 
ATOM   523  N  NH2   . ARG A 1 74  ? 7.042   6.417   26.731 1.00 16.91  ? 75   ARG A NH2   1 
ATOM   524  N  N     . HIS A 1 75  ? 11.281  2.497   31.751 1.00 19.41  ? 76   HIS A N     1 
ATOM   525  C  CA    . HIS A 1 75  ? 10.800  1.194   32.179 1.00 21.51  ? 76   HIS A CA    1 
ATOM   526  C  C     . HIS A 1 75  ? 9.315   1.065   31.863 1.00 19.54  ? 76   HIS A C     1 
ATOM   527  O  O     . HIS A 1 75  ? 8.573   2.038   32.001 1.00 21.30  ? 76   HIS A O     1 
ATOM   528  C  CB    . HIS A 1 75  ? 11.027  1.052   33.676 1.00 25.22  ? 76   HIS A CB    1 
ATOM   529  C  CG    . HIS A 1 75  ? 10.583  -0.260  34.213 1.00 28.01  ? 76   HIS A CG    1 
ATOM   530  N  ND1   . HIS A 1 75  ? 9.307   -0.461  34.691 1.00 30.48  ? 76   HIS A ND1   1 
ATOM   531  C  CD2   . HIS A 1 75  ? 11.226  -1.452  34.317 1.00 32.22  ? 76   HIS A CD2   1 
ATOM   532  C  CE1   . HIS A 1 75  ? 9.182   -1.719  35.079 1.00 36.78  ? 76   HIS A CE1   1 
ATOM   533  N  NE2   . HIS A 1 75  ? 10.329  -2.341  34.861 1.00 33.96  ? 76   HIS A NE2   1 
ATOM   534  N  N     . TYR A 1 76  ? 8.897   -0.130  31.407 1.00 17.76  ? 77   TYR A N     1 
ATOM   535  C  CA    . TYR A 1 76  ? 7.512   -0.355  31.010 1.00 16.30  ? 77   TYR A CA    1 
ATOM   536  C  C     . TYR A 1 76  ? 6.891   -1.517  31.724 1.00 19.21  ? 77   TYR A C     1 
ATOM   537  O  O     . TYR A 1 76  ? 7.524   -2.565  31.934 1.00 19.60  ? 77   TYR A O     1 
ATOM   538  C  CB    . TYR A 1 76  ? 7.420   -0.639  29.500 1.00 15.87  ? 77   TYR A CB    1 
ATOM   539  C  CG    . TYR A 1 76  ? 7.783   0.569   28.636 1.00 16.52  ? 77   TYR A CG    1 
ATOM   540  C  CD1   . TYR A 1 76  ? 6.838   1.533   28.348 1.00 16.16  ? 77   TYR A CD1   1 
ATOM   541  C  CD2   . TYR A 1 76  ? 9.096   0.802   28.240 1.00 17.52  ? 77   TYR A CD2   1 
ATOM   542  C  CE1   . TYR A 1 76  ? 7.123   2.655   27.591 1.00 17.72  ? 77   TYR A CE1   1 
ATOM   543  C  CE2   . TYR A 1 76  ? 9.417   1.904   27.525 1.00 16.94  ? 77   TYR A CE2   1 
ATOM   544  C  CZ    . TYR A 1 76  ? 8.428   2.837   27.179 1.00 18.02  ? 77   TYR A CZ    1 
ATOM   545  O  OH    . TYR A 1 76  ? 8.736   3.971   26.447 1.00 17.45  ? 77   TYR A OH    1 
ATOM   546  N  N     . ALA A 1 77  ? 5.615   -1.344  32.052 1.00 19.47  ? 78   ALA A N     1 
ATOM   547  C  CA    . ALA A 1 77  ? 4.724   -2.458  32.334 1.00 17.63  ? 78   ALA A CA    1 
ATOM   548  C  C     . ALA A 1 77  ? 3.836   -2.554  31.119 1.00 17.07  ? 78   ALA A C     1 
ATOM   549  O  O     . ALA A 1 77  ? 3.356   -1.527  30.646 1.00 21.00  ? 78   ALA A O     1 
ATOM   550  C  CB    . ALA A 1 77  ? 3.879   -2.212  33.604 1.00 19.06  ? 78   ALA A CB    1 
ATOM   551  N  N     . HIS A 1 78  ? 3.648   -3.754  30.601 1.00 16.33  ? 79   HIS A N     1 
ATOM   552  C  CA    . HIS A 1 78  ? 2.978   -3.917  29.319 1.00 14.89  ? 79   HIS A CA    1 
ATOM   553  C  C     . HIS A 1 78  ? 1.943   -5.016  29.428 1.00 18.51  ? 79   HIS A C     1 
ATOM   554  O  O     . HIS A 1 78  ? 2.265   -6.131  29.875 1.00 19.39  ? 79   HIS A O     1 
ATOM   555  C  CB    . HIS A 1 78  ? 4.055   -4.308  28.291 1.00 15.87  ? 79   HIS A CB    1 
ATOM   556  C  CG    . HIS A 1 78  ? 3.597   -4.640  26.899 1.00 16.28  ? 79   HIS A CG    1 
ATOM   557  N  ND1   . HIS A 1 78  ? 4.169   -4.084  25.770 1.00 17.57  ? 79   HIS A ND1   1 
ATOM   558  C  CD2   . HIS A 1 78  ? 2.653   -5.511  26.469 1.00 17.78  ? 79   HIS A CD2   1 
ATOM   559  C  CE1   . HIS A 1 78  ? 3.593   -4.598  24.690 1.00 18.45  ? 79   HIS A CE1   1 
ATOM   560  N  NE2   . HIS A 1 78  ? 2.679   -5.473  25.074 1.00 17.04  ? 79   HIS A NE2   1 
ATOM   561  N  N     . VAL A 1 79  ? 0.683   -4.707  29.103 1.00 15.69  ? 80   VAL A N     1 
ATOM   562  C  CA    . VAL A 1 79  ? -0.363  -5.738  29.115 1.00 17.43  ? 80   VAL A CA    1 
ATOM   563  C  C     . VAL A 1 79  ? -0.744  -6.205  27.721 1.00 15.27  ? 80   VAL A C     1 
ATOM   564  O  O     . VAL A 1 79  ? -0.722  -5.447  26.763 1.00 16.05  ? 80   VAL A O     1 
ATOM   565  C  CB    . VAL A 1 79  ? -1.579  -5.238  29.891 1.00 19.29  ? 80   VAL A CB    1 
ATOM   566  C  CG1   . VAL A 1 79  ? -1.227  -5.134  31.376 1.00 23.71  ? 80   VAL A CG1   1 
ATOM   567  C  CG2   . VAL A 1 79  ? -2.182  -3.981  29.282 1.00 19.04  ? 80   VAL A CG2   1 
ATOM   568  N  N     . ASP A 1 80  ? -1.094  -7.477  27.646 1.00 17.56  ? 81   ASP A N     1 
ATOM   569  C  CA    . ASP A 1 80  ? -1.537  -8.110  26.418 1.00 16.81  ? 81   ASP A CA    1 
ATOM   570  C  C     . ASP A 1 80  ? -2.626  -9.095  26.804 1.00 17.28  ? 81   ASP A C     1 
ATOM   571  O  O     . ASP A 1 80  ? -2.499  -9.761  27.822 1.00 20.19  ? 81   ASP A O     1 
ATOM   572  C  CB    . ASP A 1 80  ? -0.337  -8.794  25.757 1.00 18.23  ? 81   ASP A CB    1 
ATOM   573  C  CG    . ASP A 1 80  ? -0.731  -9.562  24.488 1.00 17.96  ? 81   ASP A CG    1 
ATOM   574  O  OD1   . ASP A 1 80  ? -1.189  -8.870  23.542 1.00 18.04  ? 81   ASP A OD1   1 
ATOM   575  O  OD2   . ASP A 1 80  ? -0.575  -10.806 24.441 1.00 19.92  ? 81   ASP A OD2   1 
ATOM   576  N  N     . CYS A 1 81  ? -3.709  -9.193  26.034 1.00 17.39  ? 82   CYS A N     1 
ATOM   577  C  CA    . CYS A 1 81  ? -4.857  -10.027 26.435 1.00 20.24  ? 82   CYS A CA    1 
ATOM   578  C  C     . CYS A 1 81  ? -5.269  -10.943 25.284 1.00 16.77  ? 82   CYS A C     1 
ATOM   579  O  O     . CYS A 1 81  ? -5.210  -10.529 24.124 1.00 17.21  ? 82   CYS A O     1 
ATOM   580  C  CB    . CYS A 1 81  ? -6.091  -9.188  26.766 1.00 21.87  ? 82   CYS A CB    1 
ATOM   581  S  SG    . CYS A 1 81  ? -5.825  -8.042  28.139 1.00 24.69  ? 82   CYS A SG    1 
ATOM   582  N  N     . PRO A 1 82  ? -5.787  -12.126 25.570 1.00 19.43  ? 83   PRO A N     1 
ATOM   583  C  CA    . PRO A 1 82  ? -6.141  -13.052 24.479 1.00 20.63  ? 83   PRO A CA    1 
ATOM   584  C  C     . PRO A 1 82  ? -7.301  -12.564 23.653 1.00 20.38  ? 83   PRO A C     1 
ATOM   585  O  O     . PRO A 1 82  ? -7.200  -12.500 22.417 1.00 21.35  ? 83   PRO A O     1 
ATOM   586  C  CB    . PRO A 1 82  ? -6.484  -14.367 25.215 1.00 22.14  ? 83   PRO A CB    1 
ATOM   587  C  CG    . PRO A 1 82  ? -5.684  -14.292 26.433 1.00 23.34  ? 83   PRO A CG    1 
ATOM   588  C  CD    . PRO A 1 82  ? -5.678  -12.832 26.874 1.00 22.63  ? 83   PRO A CD    1 
ATOM   589  N  N     . GLY A 1 83  ? -8.365  -12.152 24.295 1.00 20.40  ? 84   GLY A N     1 
ATOM   590  C  CA    . GLY A 1 83  ? -9.595  -11.941 23.560 1.00 22.75  ? 84   GLY A CA    1 
ATOM   591  C  C     . GLY A 1 83  ? -10.080 -10.507 23.582 1.00 20.94  ? 84   GLY A C     1 
ATOM   592  O  O     . GLY A 1 83  ? -9.811  -9.727  24.502 1.00 21.08  ? 84   GLY A O     1 
ATOM   593  N  N     . HIS A 1 84  ? -10.910 -10.191 22.595 1.00 21.87  ? 85   HIS A N     1 
ATOM   594  C  CA    . HIS A 1 84  ? -11.564 -8.902  22.541 1.00 23.41  ? 85   HIS A CA    1 
ATOM   595  C  C     . HIS A 1 84  ? -12.296 -8.544  23.841 1.00 25.22  ? 85   HIS A C     1 
ATOM   596  O  O     . HIS A 1 84  ? -12.166 -7.417  24.336 1.00 24.42  ? 85   HIS A O     1 
ATOM   597  C  CB    . HIS A 1 84  ? -12.532 -8.910  21.358 1.00 22.52  ? 85   HIS A CB    1 
ATOM   598  C  CG    . HIS A 1 84  ? -13.315 -7.664  21.277 1.00 26.25  ? 85   HIS A CG    1 
ATOM   599  N  ND1   . HIS A 1 84  ? -12.701 -6.435  21.143 1.00 23.09  ? 85   HIS A ND1   1 
ATOM   600  C  CD2   . HIS A 1 84  ? -14.646 -7.430  21.292 1.00 32.26  ? 85   HIS A CD2   1 
ATOM   601  C  CE1   . HIS A 1 84  ? -13.627 -5.497  21.053 1.00 32.28  ? 85   HIS A CE1   1 
ATOM   602  N  NE2   . HIS A 1 84  ? -14.818 -6.073  21.162 1.00 37.80  ? 85   HIS A NE2   1 
ATOM   603  N  N     . ALA A 1 85  ? -13.033 -9.486  24.417 1.00 20.78  ? 86   ALA A N     1 
ATOM   604  C  CA    . ALA A 1 85  ? -13.724 -9.237  25.667 1.00 21.75  ? 86   ALA A CA    1 
ATOM   605  C  C     . ALA A 1 85  ? -12.776 -8.857  26.791 1.00 24.29  ? 86   ALA A C     1 
ATOM   606  O  O     . ALA A 1 85  ? -13.137 -8.072  27.663 1.00 25.42  ? 86   ALA A O     1 
ATOM   607  C  CB    . ALA A 1 85  ? -14.505 -10.491 26.093 1.00 25.60  ? 86   ALA A CB    1 
ATOM   608  N  N     . ASP A 1 86  ? -11.582 -9.447  26.821 1.00 22.60  ? 87   ASP A N     1 
ATOM   609  C  CA    . ASP A 1 86  ? -10.601 -9.096  27.846 1.00 22.72  ? 87   ASP A CA    1 
ATOM   610  C  C     . ASP A 1 86  ? -10.191 -7.635  27.720 1.00 21.65  ? 87   ASP A C     1 
ATOM   611  O  O     . ASP A 1 86  ? -10.045 -6.939  28.727 1.00 23.03  ? 87   ASP A O     1 
ATOM   612  C  CB    . ASP A 1 86  ? -9.362  -9.982  27.678 1.00 21.68  ? 87   ASP A CB    1 
ATOM   613  C  CG    . ASP A 1 86  ? -9.662  -11.441 27.956 1.00 23.58  ? 87   ASP A CG    1 
ATOM   614  O  OD1   . ASP A 1 86  ? -10.258 -11.762 29.014 1.00 25.15  ? 87   ASP A OD1   1 
ATOM   615  O  OD2   . ASP A 1 86  ? -9.306  -12.288 27.091 1.00 26.21  ? 87   ASP A OD2   1 
ATOM   616  N  N     . TYR A 1 87  ? -10.033 -7.131  26.492 1.00 19.64  ? 88   TYR A N     1 
ATOM   617  C  CA    . TYR A 1 87  ? -9.689  -5.719  26.302 1.00 18.78  ? 88   TYR A CA    1 
ATOM   618  C  C     . TYR A 1 87  ? -10.835 -4.812  26.719 1.00 20.34  ? 88   TYR A C     1 
ATOM   619  O  O     . TYR A 1 87  ? -10.605 -3.782  27.355 1.00 22.17  ? 88   TYR A O     1 
ATOM   620  C  CB    . TYR A 1 87  ? -9.348  -5.426  24.835 1.00 18.45  ? 88   TYR A CB    1 
ATOM   621  C  CG    . TYR A 1 87  ? -7.999  -5.978  24.489 1.00 19.09  ? 88   TYR A CG    1 
ATOM   622  C  CD1   . TYR A 1 87  ? -6.834  -5.273  24.877 1.00 20.89  ? 88   TYR A CD1   1 
ATOM   623  C  CD2   . TYR A 1 87  ? -7.846  -7.195  23.825 1.00 18.84  ? 88   TYR A CD2   1 
ATOM   624  C  CE1   . TYR A 1 87  ? -5.599  -5.767  24.624 1.00 20.44  ? 88   TYR A CE1   1 
ATOM   625  C  CE2   . TYR A 1 87  ? -6.571  -7.695  23.591 1.00 16.79  ? 88   TYR A CE2   1 
ATOM   626  C  CZ    . TYR A 1 87  ? -5.456  -6.969  24.001 1.00 17.18  ? 88   TYR A CZ    1 
ATOM   627  O  OH    . TYR A 1 87  ? -4.175  -7.429  23.717 1.00 17.99  ? 88   TYR A OH    1 
ATOM   628  N  N     . VAL A 1 88  ? -12.063 -5.168  26.348 1.00 20.50  ? 89   VAL A N     1 
ATOM   629  C  CA    . VAL A 1 88  ? -13.212 -4.346  26.730 1.00 21.79  ? 89   VAL A CA    1 
ATOM   630  C  C     . VAL A 1 88  ? -13.259 -4.203  28.239 1.00 25.70  ? 89   VAL A C     1 
ATOM   631  O  O     . VAL A 1 88  ? -13.391 -3.095  28.782 1.00 23.44  ? 89   VAL A O     1 
ATOM   632  C  CB    . VAL A 1 88  ? -14.525 -4.949  26.177 1.00 24.25  ? 89   VAL A CB    1 
ATOM   633  C  CG1   . VAL A 1 88  ? -15.725 -4.198  26.744 1.00 26.49  ? 89   VAL A CG1   1 
ATOM   634  C  CG2   . VAL A 1 88  ? -14.538 -4.881  24.639 1.00 23.21  ? 89   VAL A CG2   1 
ATOM   635  N  N     . LYS A 1 89  ? -13.160 -5.330  28.951 1.00 21.81  ? 90   LYS A N     1 
ATOM   636  C  CA    . LYS A 1 89  ? -13.242 -5.296  30.406 1.00 21.86  ? 90   LYS A CA    1 
ATOM   637  C  C     . LYS A 1 89  ? -12.043 -4.567  31.008 1.00 21.03  ? 90   LYS A C     1 
ATOM   638  O  O     . LYS A 1 89  ? -12.193 -3.822  31.988 1.00 26.01  ? 90   LYS A O     1 
ATOM   639  C  CB    . LYS A 1 89  ? -13.327 -6.712  30.953 1.00 24.71  ? 90   LYS A CB    1 
ATOM   640  C  CG    . LYS A 1 89  ? -14.711 -7.340  30.643 1.00 26.81  ? 90   LYS A CG    1 
ATOM   641  C  CD    . LYS A 1 89  ? -14.879 -8.694  31.297 1.00 28.77  ? 90   LYS A CD    1 
ATOM   642  C  CE    . LYS A 1 89  ? -14.144 -9.738  30.538 1.00 29.05  ? 90   LYS A CE    1 
ATOM   643  N  NZ    . LYS A 1 89  ? -14.431 -11.097 31.108 1.00 34.47  ? 90   LYS A NZ    1 
ATOM   644  N  N     . ASN A 1 90  ? -10.833 -4.825  30.500 1.00 22.75  ? 91   ASN A N     1 
ATOM   645  C  CA    . ASN A 1 90  ? -9.664  -4.193  31.080 1.00 24.18  ? 91   ASN A CA    1 
ATOM   646  C  C     . ASN A 1 90  ? -9.706  -2.691  30.888 1.00 23.81  ? 91   ASN A C     1 
ATOM   647  O  O     . ASN A 1 90  ? -9.470  -1.931  31.843 1.00 27.41  ? 91   ASN A O     1 
ATOM   648  C  CB    . ASN A 1 90  ? -8.411  -4.781  30.436 1.00 24.21  ? 91   ASN A CB    1 
ATOM   649  C  CG    . ASN A 1 90  ? -7.132  -4.451  31.227 1.00 48.76  ? 91   ASN A CG    1 
ATOM   650  O  OD1   . ASN A 1 90  ? -7.093  -3.481  31.982 1.00 60.81  ? 91   ASN A OD1   1 
ATOM   651  N  ND2   . ASN A 1 90  ? -6.158  -5.338  31.148 1.00 60.67  ? 91   ASN A ND2   1 
ATOM   652  N  N     . MET A 1 91  ? -10.115 -2.245  29.715 1.00 23.07  ? 92   MET A N     1 
ATOM   653  C  CA    . MET A 1 91  ? -10.113 -0.819  29.463 1.00 24.88  ? 92   MET A CA    1 
ATOM   654  C  C     . MET A 1 91  ? -11.217 -0.147  30.258 1.00 21.97  ? 92   MET A C     1 
ATOM   655  O  O     . MET A 1 91  ? -11.002 0.897   30.865 1.00 25.31  ? 92   MET A O     1 
ATOM   656  C  CB    . MET A 1 91  ? -10.199 -0.533  27.957 1.00 25.65  ? 92   MET A CB    1 
ATOM   657  C  CG    . MET A 1 91  ? -8.914  -1.077  27.303 1.00 24.35  ? 92   MET A CG    1 
ATOM   658  S  SD    . MET A 1 91  ? -8.912  -1.061  25.514 1.00 31.27  ? 92   MET A SD    1 
ATOM   659  C  CE    . MET A 1 91  ? -8.696  0.704   25.408 1.00 32.40  ? 92   MET A CE    1 
ATOM   660  N  N     . ILE A 1 92  ? -12.427 -0.743  30.331 1.00 21.52  ? 93   ILE A N     1 
ATOM   661  C  CA    . ILE A 1 92  ? -13.514 -0.073  31.029 1.00 22.10  ? 93   ILE A CA    1 
ATOM   662  C  C     . ILE A 1 92  ? -13.266 -0.098  32.536 1.00 26.27  ? 93   ILE A C     1 
ATOM   663  O  O     . ILE A 1 92  ? -13.539 0.877   33.239 1.00 30.02  ? 93   ILE A O     1 
ATOM   664  C  CB    . ILE A 1 92  ? -14.909 -0.667  30.672 1.00 22.47  ? 93   ILE A CB    1 
ATOM   665  C  CG1   . ILE A 1 92  ? -15.215 -0.251  29.220 1.00 24.90  ? 93   ILE A CG1   1 
ATOM   666  C  CG2   . ILE A 1 92  ? -16.002 -0.207  31.681 1.00 24.77  ? 93   ILE A CG2   1 
ATOM   667  C  CD1   . ILE A 1 92  ? -16.491 -0.919  28.646 1.00 25.52  ? 93   ILE A CD1   1 
ATOM   668  N  N     . THR A 1 93  ? -12.766 -1.224  33.082 1.00 24.79  ? 94   THR A N     1 
ATOM   669  C  CA    . THR A 1 93  ? -12.542 -1.185  34.531 1.00 27.57  ? 94   THR A CA    1 
ATOM   670  C  C     . THR A 1 93  ? -11.244 -0.477  34.907 1.00 28.56  ? 94   THR A C     1 
ATOM   671  O  O     . THR A 1 93  ? -11.055 -0.171  36.094 1.00 31.73  ? 94   THR A O     1 
ATOM   672  C  CB    . THR A 1 93  ? -12.519 -2.586  35.094 1.00 26.14  ? 94   THR A CB    1 
ATOM   673  O  OG1   . THR A 1 93  ? -11.422 -3.301  34.531 1.00 28.54  ? 94   THR A OG1   1 
ATOM   674  C  CG2   . THR A 1 93  ? -13.751 -3.329  34.779 1.00 29.23  ? 94   THR A CG2   1 
ATOM   675  N  N     . GLY A 1 94  ? -10.380 -0.193  33.958 1.00 29.69  ? 95   GLY A N     1 
ATOM   676  C  CA    . GLY A 1 94  ? -9.080  0.380   34.258 1.00 36.23  ? 95   GLY A CA    1 
ATOM   677  C  C     . GLY A 1 94  ? -8.164  -0.554  35.017 1.00 36.26  ? 95   GLY A C     1 
ATOM   678  O  O     . GLY A 1 94  ? -7.277  -0.089  35.733 1.00 34.99  ? 95   GLY A O     1 
ATOM   679  N  N     . ALA A 1 95  ? -8.330  -1.868  34.841 1.00 31.83  ? 96   ALA A N     1 
ATOM   680  C  CA    . ALA A 1 95  ? -7.521  -2.854  35.548 1.00 29.28  ? 96   ALA A CA    1 
ATOM   681  C  C     . ALA A 1 95  ? -6.045  -2.726  35.209 1.00 29.71  ? 96   ALA A C     1 
ATOM   682  O  O     . ALA A 1 95  ? -5.207  -3.098  36.033 1.00 35.80  ? 96   ALA A O     1 
ATOM   683  C  CB    . ALA A 1 95  ? -7.993  -4.267  35.224 1.00 37.88  ? 96   ALA A CB    1 
ATOM   684  N  N     . ALA A 1 96  ? -5.710  -2.201  34.035 1.00 31.81  ? 97   ALA A N     1 
ATOM   685  C  CA    . ALA A 1 96  ? -4.339  -1.816  33.695 1.00 40.23  ? 97   ALA A CA    1 
ATOM   686  C  C     . ALA A 1 96  ? -4.290  -0.327  33.378 1.00 35.85  ? 97   ALA A C     1 
ATOM   687  O  O     . ALA A 1 96  ? -5.081  0.154   32.566 1.00 42.73  ? 97   ALA A O     1 
ATOM   688  C  CB    . ALA A 1 96  ? -3.820  -2.607  32.491 1.00 45.52  ? 97   ALA A CB    1 
ATOM   689  N  N     . GLN A 1 97  ? -3.368  0.402   34.016 1.00 34.23  ? 98   GLN A N     1 
ATOM   690  C  CA    . GLN A 1 97  ? -3.112  1.778   33.614 1.00 31.34  ? 98   GLN A CA    1 
ATOM   691  C  C     . GLN A 1 97  ? -2.572  1.756   32.197 1.00 27.73  ? 98   GLN A C     1 
ATOM   692  O  O     . GLN A 1 97  ? -1.744  0.909   31.859 1.00 26.01  ? 98   GLN A O     1 
ATOM   693  C  CB    . GLN A 1 97  ? -2.133  2.452   34.580 1.00 29.78  ? 98   GLN A CB    1 
ATOM   694  C  CG    . GLN A 1 97  ? -1.710  3.878   34.190 1.00 35.32  ? 98   GLN A CG    1 
ATOM   695  C  CD    . GLN A 1 97  ? -0.960  4.608   35.306 1.00 52.62  ? 98   GLN A CD    1 
ATOM   696  O  OE1   . GLN A 1 97  ? -0.894  4.130   36.448 1.00 60.49  ? 98   GLN A OE1   1 
ATOM   697  N  NE2   . GLN A 1 97  ? -0.355  5.749   34.972 1.00 40.91  ? 98   GLN A NE2   1 
ATOM   698  N  N     . MET A 1 98  ? -3.142  2.619   31.358 1.00 26.95  ? 99   MET A N     1 
ATOM   699  C  CA    . MET A 1 98  ? -2.615  2.742   29.973 1.00 23.14  ? 99   MET A CA    1 
ATOM   700  C  C     . MET A 1 98  ? -2.253  4.193   29.696 1.00 23.17  ? 99   MET A C     1 
ATOM   701  O  O     . MET A 1 98  ? -3.126  4.960   29.327 1.00 29.82  ? 99   MET A O     1 
ATOM   702  C  CB    . MET A 1 98  ? -3.559  2.200   28.898 1.00 28.49  ? 99   MET A CB    1 
ATOM   703  C  CG    . MET A 1 98  ? -3.999  0.802   29.170 1.00 31.37  ? 99   MET A CG    1 
ATOM   704  S  SD    . MET A 1 98  ? -2.882  -0.302  28.323 1.00 52.84  ? 99   MET A SD    1 
ATOM   705  C  CE    . MET A 1 98  ? -3.608  -0.262  26.689 1.00 63.13  ? 99   MET A CE    1 
ATOM   706  N  N     . ASP A 1 99  ? -0.994  4.515   29.898 1.00 18.23  ? 100  ASP A N     1 
ATOM   707  C  CA    . ASP A 1 99  ? -0.459  5.818   29.580 1.00 21.86  ? 100  ASP A CA    1 
ATOM   708  C  C     . ASP A 1 99  ? -0.354  5.973   28.088 1.00 17.84  ? 100  ASP A C     1 
ATOM   709  O  O     . ASP A 1 99  ? -0.288  7.097   27.581 1.00 19.96  ? 100  ASP A O     1 
ATOM   710  C  CB    . ASP A 1 99  ? 0.932   5.935   30.220 1.00 19.62  ? 100  ASP A CB    1 
ATOM   711  C  CG    . ASP A 1 99  ? 0.845   5.828   31.738 1.00 21.11  ? 100  ASP A CG    1 
ATOM   712  O  OD1   . ASP A 1 99  ? -0.103  6.403   32.374 1.00 23.52  ? 100  ASP A OD1   1 
ATOM   713  O  OD2   . ASP A 1 99  ? 1.645   5.059   32.316 1.00 21.59  ? 100  ASP A OD2   1 
ATOM   714  N  N     . GLY A 1 100 ? -0.331  4.837   27.378 1.00 17.80  ? 101  GLY A N     1 
ATOM   715  C  CA    . GLY A 1 100 ? -0.420  4.826   25.931 1.00 17.75  ? 101  GLY A CA    1 
ATOM   716  C  C     . GLY A 1 100 ? -0.657  3.410   25.493 1.00 16.20  ? 101  GLY A C     1 
ATOM   717  O  O     . GLY A 1 100 ? -0.647  2.467   26.303 1.00 17.19  ? 101  GLY A O     1 
ATOM   718  N  N     . ALA A 1 101 ? -0.908  3.243   24.201 1.00 15.16  ? 102  ALA A N     1 
ATOM   719  C  CA    . ALA A 1 101 ? -1.176  1.917   23.685 1.00 15.29  ? 102  ALA A CA    1 
ATOM   720  C  C     . ALA A 1 101 ? -0.441  1.748   22.386 1.00 14.90  ? 102  ALA A C     1 
ATOM   721  O  O     . ALA A 1 101 ? -0.308  2.724   21.629 1.00 15.75  ? 102  ALA A O     1 
ATOM   722  C  CB    . ALA A 1 101 ? -2.669  1.673   23.411 1.00 16.66  ? 102  ALA A CB    1 
ATOM   723  N  N     . ILE A 1 102 ? 0.045   0.534   22.128 1.00 13.82  ? 103  ILE A N     1 
ATOM   724  C  CA    . ILE A 1 102 ? 0.531   0.148   20.785 1.00 11.92  ? 103  ILE A CA    1 
ATOM   725  C  C     . ILE A 1 102 ? -0.624  -0.546  20.100 1.00 12.82  ? 103  ILE A C     1 
ATOM   726  O  O     . ILE A 1 102 ? -1.055  -1.643  20.507 1.00 14.24  ? 103  ILE A O     1 
ATOM   727  C  CB    . ILE A 1 102 ? 1.729   -0.789  20.884 1.00 14.58  ? 103  ILE A CB    1 
ATOM   728  C  CG1   . ILE A 1 102 ? 2.876   -0.139  21.675 1.00 15.58  ? 103  ILE A CG1   1 
ATOM   729  C  CG2   . ILE A 1 102 ? 2.144   -1.257  19.464 1.00 14.42  ? 103  ILE A CG2   1 
ATOM   730  C  CD1   . ILE A 1 102 ? 3.954   -1.178  22.006 1.00 18.81  ? 103  ILE A CD1   1 
ATOM   731  N  N     . LEU A 1 103 ? -1.131  0.085   19.030 1.00 13.24  ? 104  LEU A N     1 
ATOM   732  C  CA    . LEU A 1 103 ? -2.183  -0.481  18.207 1.00 13.42  ? 104  LEU A CA    1 
ATOM   733  C  C     . LEU A 1 103 ? -1.519  -1.336  17.152 1.00 13.21  ? 104  LEU A C     1 
ATOM   734  O  O     . LEU A 1 103 ? -0.763  -0.806  16.342 1.00 14.61  ? 104  LEU A O     1 
ATOM   735  C  CB    . LEU A 1 103 ? -3.019  0.633   17.588 1.00 14.01  ? 104  LEU A CB    1 
ATOM   736  C  CG    . LEU A 1 103 ? -4.062  0.115   16.588 1.00 14.67  ? 104  LEU A CG    1 
ATOM   737  C  CD1   . LEU A 1 103 ? -5.157  -0.668  17.297 1.00 16.17  ? 104  LEU A CD1   1 
ATOM   738  C  CD2   . LEU A 1 103 ? -4.711  1.243   15.784 1.00 18.58  ? 104  LEU A CD2   1 
ATOM   739  N  N     . VAL A 1 104 ? -1.803  -2.620  17.132 1.00 12.71  ? 105  VAL A N     1 
ATOM   740  C  CA    . VAL A 1 104 ? -1.251  -3.550  16.138 1.00 11.30  ? 105  VAL A CA    1 
ATOM   741  C  C     . VAL A 1 104 ? -2.286  -3.754  15.054 1.00 13.15  ? 105  VAL A C     1 
ATOM   742  O  O     . VAL A 1 104 ? -3.446  -4.151  15.330 1.00 15.12  ? 105  VAL A O     1 
ATOM   743  C  CB    . VAL A 1 104 ? -0.912  -4.869  16.831 1.00 13.03  ? 105  VAL A CB    1 
ATOM   744  C  CG1   . VAL A 1 104 ? -0.258  -5.862  15.833 1.00 16.61  ? 105  VAL A CG1   1 
ATOM   745  C  CG2   . VAL A 1 104 ? 0.098   -4.616  17.981 1.00 14.90  ? 105  VAL A CG2   1 
ATOM   746  N  N     . VAL A 1 105 ? -1.879  -3.475  13.804 1.00 13.85  ? 106  VAL A N     1 
ATOM   747  C  CA    . VAL A 1 105 ? -2.779  -3.664  12.663 1.00 14.03  ? 106  VAL A CA    1 
ATOM   748  C  C     . VAL A 1 105 ? -2.068  -4.577  11.677 1.00 15.64  ? 106  VAL A C     1 
ATOM   749  O  O     . VAL A 1 105 ? -0.922  -4.293  11.306 1.00 14.72  ? 106  VAL A O     1 
ATOM   750  C  CB    . VAL A 1 105 ? -3.115  -2.348  11.987 1.00 13.39  ? 106  VAL A CB    1 
ATOM   751  C  CG1   . VAL A 1 105 ? -4.059  -2.578  10.797 1.00 16.09  ? 106  VAL A CG1   1 
ATOM   752  C  CG2   . VAL A 1 105 ? -3.748  -1.355  12.946 1.00 14.24  ? 106  VAL A CG2   1 
ATOM   753  N  N     . SER A 1 106 ? -2.712  -5.651  11.262 1.00 14.31  ? 107  SER A N     1 
ATOM   754  C  CA    . SER A 1 106 ? -2.091  -6.489  10.247 1.00 13.76  ? 107  SER A CA    1 
ATOM   755  C  C     . SER A 1 106 ? -2.093  -5.802  8.908  1.00 17.57  ? 107  SER A C     1 
ATOM   756  O  O     . SER A 1 106 ? -3.150  -5.365  8.423  1.00 18.44  ? 107  SER A O     1 
ATOM   757  C  CB    . SER A 1 106 ? -2.857  -7.798  10.120 1.00 18.29  ? 107  SER A CB    1 
ATOM   758  O  OG    . SER A 1 106 ? -2.491  -8.486  8.900  1.00 19.69  ? 107  SER A OG    1 
ATOM   759  N  N     . ALA A 1 107 ? -0.934  -5.716  8.292  1.00 16.33  ? 108  ALA A N     1 
ATOM   760  C  CA    . ALA A 1 107 ? -0.883  -5.130  6.957  1.00 18.31  ? 108  ALA A CA    1 
ATOM   761  C  C     . ALA A 1 107 ? -1.545  -5.991  5.899  1.00 20.80  ? 108  ALA A C     1 
ATOM   762  O  O     . ALA A 1 107 ? -1.991  -5.441  4.876  1.00 23.00  ? 108  ALA A O     1 
ATOM   763  C  CB    . ALA A 1 107 ? 0.583   -4.932  6.567  1.00 21.55  ? 108  ALA A CB    1 
ATOM   764  N  N     . ALA A 1 108 ? -1.696  -7.291  6.156  1.00 18.89  ? 109  ALA A N     1 
ATOM   765  C  CA    . ALA A 1 108 ? -2.322  -8.215  5.211  1.00 20.76  ? 109  ALA A CA    1 
ATOM   766  C  C     . ALA A 1 108 ? -3.833  -8.089  5.237  1.00 22.32  ? 109  ALA A C     1 
ATOM   767  O  O     . ALA A 1 108 ? -4.509  -8.390  4.244  1.00 26.11  ? 109  ALA A O     1 
ATOM   768  C  CB    . ALA A 1 108 ? -1.895  -9.658  5.537  1.00 22.21  ? 109  ALA A CB    1 
ATOM   769  N  N     . ASP A 1 109 ? -4.395  -7.653  6.360  1.00 20.29  ? 110  ASP A N     1 
ATOM   770  C  CA    . ASP A 1 109 ? -5.845  -7.575  6.528  1.00 21.20  ? 110  ASP A CA    1 
ATOM   771  C  C     . ASP A 1 109 ? -6.374  -6.154  6.561  1.00 19.78  ? 110  ASP A C     1 
ATOM   772  O  O     . ASP A 1 109 ? -7.569  -5.952  6.288  1.00 24.24  ? 110  ASP A O     1 
ATOM   773  C  CB    . ASP A 1 109 ? -6.227  -8.242  7.867  1.00 24.19  ? 110  ASP A CB    1 
ATOM   774  C  CG    . ASP A 1 109 ? -5.788  -9.677  7.908  1.00 35.89  ? 110  ASP A CG    1 
ATOM   775  O  OD1   . ASP A 1 109 ? -6.273  -10.448 7.082  1.00 35.14  ? 110  ASP A OD1   1 
ATOM   776  O  OD2   . ASP A 1 109 ? -4.770  -9.969  8.587  1.00 33.26  ? 110  ASP A OD2   1 
ATOM   777  N  N     . GLY A 1 110 ? -5.545  -5.192  6.928  1.00 20.30  ? 111  GLY A N     1 
ATOM   778  C  CA    . GLY A 1 110 ? -6.000  -3.851  7.208  1.00 19.33  ? 111  GLY A CA    1 
ATOM   779  C  C     . GLY A 1 110 ? -6.784  -3.746  8.505  1.00 17.73  ? 111  GLY A C     1 
ATOM   780  O  O     . GLY A 1 110 ? -6.981  -4.719  9.243  1.00 18.78  ? 111  GLY A O     1 
ATOM   781  N  N     . PRO A 1 111 ? -7.295  -2.564  8.804  1.00 18.83  ? 112  PRO A N     1 
ATOM   782  C  CA    . PRO A 1 111 ? -8.107  -2.395  10.026 1.00 19.07  ? 112  PRO A CA    1 
ATOM   783  C  C     . PRO A 1 111 ? -9.356  -3.261  9.938  1.00 19.33  ? 112  PRO A C     1 
ATOM   784  O  O     . PRO A 1 111 ? -10.029 -3.336  8.899  1.00 21.44  ? 112  PRO A O     1 
ATOM   785  C  CB    . PRO A 1 111 ? -8.502  -0.916  10.006 1.00 25.26  ? 112  PRO A CB    1 
ATOM   786  C  CG    . PRO A 1 111 ? -7.690  -0.270  8.950  1.00 25.25  ? 112  PRO A CG    1 
ATOM   787  C  CD    . PRO A 1 111 ? -7.133  -1.317  8.046  1.00 19.19  ? 112  PRO A CD    1 
ATOM   788  N  N     . MET A 1 112 ? -9.740  -3.813  11.076 1.00 17.70  ? 113  MET A N     1 
ATOM   789  C  CA    . MET A 1 112 ? -10.881 -4.717  11.197 1.00 19.60  ? 113  MET A CA    1 
ATOM   790  C  C     . MET A 1 112 ? -11.778 -4.242  12.345 1.00 18.23  ? 113  MET A C     1 
ATOM   791  O  O     . MET A 1 112 ? -11.483 -3.240  12.991 1.00 17.52  ? 113  MET A O     1 
ATOM   792  C  CB    . MET A 1 112 ? -10.363 -6.162  11.356 1.00 21.39  ? 113  MET A CB    1 
ATOM   793  C  CG    . MET A 1 112 ? -9.685  -6.710  10.098 1.00 22.88  ? 113  MET A CG    1 
ATOM   794  S  SD    . MET A 1 112 ? -10.874 -6.984  8.789  1.00 27.49  ? 113  MET A SD    1 
ATOM   795  C  CE    . MET A 1 112 ? -11.632 -8.482  9.380  1.00 32.36  ? 113  MET A CE    1 
ATOM   796  N  N     . PRO A 1 113 ? -12.920 -4.885  12.604 1.00 19.77  ? 114  PRO A N     1 
ATOM   797  C  CA    . PRO A 1 113 ? -13.855 -4.262  13.550 1.00 19.00  ? 114  PRO A CA    1 
ATOM   798  C  C     . PRO A 1 113 ? -13.286 -4.030  14.920 1.00 18.75  ? 114  PRO A C     1 
ATOM   799  O  O     . PRO A 1 113 ? -13.657 -3.031  15.545 1.00 20.55  ? 114  PRO A O     1 
ATOM   800  C  CB    . PRO A 1 113 ? -15.038 -5.243  13.580 1.00 20.63  ? 114  PRO A CB    1 
ATOM   801  C  CG    . PRO A 1 113 ? -15.080 -5.769  12.126 1.00 22.77  ? 114  PRO A CG    1 
ATOM   802  C  CD    . PRO A 1 113 ? -13.578 -5.916  11.777 1.00 21.02  ? 114  PRO A CD    1 
ATOM   803  N  N     . GLN A 1 114 ? -12.385 -4.882  15.398 1.00 17.55  ? 115  GLN A N     1 
ATOM   804  C  CA    . GLN A 1 114 ? -11.866 -4.629  16.734 1.00 17.82  ? 115  GLN A CA    1 
ATOM   805  C  C     . GLN A 1 114 ? -10.761 -3.583  16.705 1.00 18.54  ? 115  GLN A C     1 
ATOM   806  O  O     . GLN A 1 114 ? -10.462 -2.993  17.732 1.00 19.42  ? 115  GLN A O     1 
ATOM   807  C  CB    . GLN A 1 114 ? -11.362 -5.919  17.386 1.00 18.14  ? 115  GLN A CB    1 
ATOM   808  C  CG    . GLN A 1 114 ? -12.464 -6.978  17.464 1.00 26.12  ? 115  GLN A CG    1 
ATOM   809  C  CD    . GLN A 1 114 ? -11.950 -8.418  17.665 1.00 21.43  ? 115  GLN A CD    1 
ATOM   810  O  OE1   . GLN A 1 114 ? -10.794 -8.674  17.870 1.00 19.54  ? 115  GLN A OE1   1 
ATOM   811  N  NE2   . GLN A 1 114 ? -12.861 -9.369  17.494 1.00 27.02  ? 115  GLN A NE2   1 
ATOM   812  N  N     . THR A 1 115 ? -10.131 -3.355  15.538 1.00 17.51  ? 116  THR A N     1 
ATOM   813  C  CA    . THR A 1 115 ? -9.257  -2.203  15.413 1.00 15.49  ? 116  THR A CA    1 
ATOM   814  C  C     . THR A 1 115 ? -10.036 -0.932  15.728 1.00 15.86  ? 116  THR A C     1 
ATOM   815  O  O     . THR A 1 115 ? -9.621  -0.116  16.559 1.00 17.69  ? 116  THR A O     1 
ATOM   816  C  CB    . THR A 1 115 ? -8.702  -2.125  13.977 1.00 16.87  ? 116  THR A CB    1 
ATOM   817  O  OG1   . THR A 1 115 ? -8.226  -3.402  13.560 1.00 17.53  ? 116  THR A OG1   1 
ATOM   818  C  CG2   . THR A 1 115 ? -7.576  -1.114  13.935 1.00 18.38  ? 116  THR A CG2   1 
ATOM   819  N  N     . ARG A 1 116 ? -11.227 -0.797  15.108 1.00 16.72  ? 117  ARG A N     1 
ATOM   820  C  CA    . ARG A 1 116 ? -12.070 0.360   15.321 1.00 16.61  ? 117  ARG A CA    1 
ATOM   821  C  C     . ARG A 1 116 ? -12.562 0.387   16.755 1.00 17.71  ? 117  ARG A C     1 
ATOM   822  O  O     . ARG A 1 116 ? -12.474 1.414   17.440 1.00 18.26  ? 117  ARG A O     1 
ATOM   823  C  CB    . ARG A 1 116 ? -13.227 0.273   14.355 1.00 18.13  ? 117  ARG A CB    1 
ATOM   824  C  CG    . ARG A 1 116 ? -14.207 1.406   14.475 1.00 23.21  ? 117  ARG A CG    1 
ATOM   825  C  CD    . ARG A 1 116 ? -15.425 1.244   13.518 1.00 29.70  ? 117  ARG A CD    1 
ATOM   826  N  NE    . ARG A 1 116 ? -15.055 1.358   12.104 1.00 32.40  ? 117  ARG A NE    1 
ATOM   827  C  CZ    . ARG A 1 116 ? -14.957 2.525   11.459 1.00 35.39  ? 117  ARG A CZ    1 
ATOM   828  N  NH1   . ARG A 1 116 ? -15.197 3.668   12.106 1.00 30.69  ? 117  ARG A NH1   1 
ATOM   829  N  NH2   . ARG A 1 116 ? -14.625 2.559   10.162 1.00 34.57  ? 117  ARG A NH2   1 
ATOM   830  N  N     . GLU A 1 117 ? -12.998 -0.769  17.259 1.00 18.07  ? 118  GLU A N     1 
ATOM   831  C  CA    . GLU A 1 117 ? -13.561 -0.745  18.609 1.00 18.46  ? 118  GLU A CA    1 
ATOM   832  C  C     . GLU A 1 117 ? -12.526 -0.428  19.663 1.00 17.48  ? 118  GLU A C     1 
ATOM   833  O  O     . GLU A 1 117 ? -12.830 0.266   20.652 1.00 18.33  ? 118  GLU A O     1 
ATOM   834  C  CB    . GLU A 1 117 ? -14.276 -2.055  18.911 1.00 20.72  ? 118  GLU A CB    1 
ATOM   835  C  CG    . GLU A 1 117 ? -15.144 -1.958  20.179 1.00 21.21  ? 118  GLU A CG    1 
ATOM   836  C  CD    . GLU A 1 117 ? -16.068 -3.142  20.410 1.00 28.42  ? 118  GLU A CD    1 
ATOM   837  O  OE1   . GLU A 1 117 ? -16.160 -4.055  19.564 1.00 26.64  ? 118  GLU A OE1   1 
ATOM   838  O  OE2   . GLU A 1 117 ? -16.703 -3.141  21.481 1.00 27.64  ? 118  GLU A OE2   1 
ATOM   839  N  N     . HIS A 1 118 ? -11.306 -0.932  19.494 1.00 17.56  ? 119  HIS A N     1 
ATOM   840  C  CA    . HIS A 1 118 ? -10.278 -0.628  20.485 1.00 17.92  ? 119  HIS A CA    1 
ATOM   841  C  C     . HIS A 1 118 ? -9.826  0.825   20.436 1.00 15.48  ? 119  HIS A C     1 
ATOM   842  O  O     . HIS A 1 118 ? -9.533  1.397   21.490 1.00 18.07  ? 119  HIS A O     1 
ATOM   843  C  CB    . HIS A 1 118 ? -9.073  -1.528  20.325 1.00 15.71  ? 119  HIS A CB    1 
ATOM   844  C  CG    . HIS A 1 118 ? -9.354  -2.938  20.707 1.00 16.67  ? 119  HIS A CG    1 
ATOM   845  N  ND1   . HIS A 1 118 ? -8.367  -3.894  20.748 1.00 16.39  ? 119  HIS A ND1   1 
ATOM   846  C  CD2   . HIS A 1 118 ? -10.505 -3.564  21.051 1.00 18.88  ? 119  HIS A CD2   1 
ATOM   847  C  CE1   . HIS A 1 118 ? -8.896  -5.061  21.090 1.00 18.20  ? 119  HIS A CE1   1 
ATOM   848  N  NE2   . HIS A 1 118 ? -10.193 -4.888  21.283 1.00 19.04  ? 119  HIS A NE2   1 
ATOM   849  N  N     . ILE A 1 119 ? -9.817  1.432   19.252 1.00 15.84  ? 120  ILE A N     1 
ATOM   850  C  CA    . ILE A 1 119 ? -9.555  2.857   19.184 1.00 17.84  ? 120  ILE A CA    1 
ATOM   851  C  C     . ILE A 1 119 ? -10.678 3.637   19.827 1.00 18.04  ? 120  ILE A C     1 
ATOM   852  O  O     . ILE A 1 119 ? -10.414 4.575   20.564 1.00 18.28  ? 120  ILE A O     1 
ATOM   853  C  CB    . ILE A 1 119 ? -9.343  3.289   17.723 1.00 16.80  ? 120  ILE A CB    1 
ATOM   854  C  CG1   . ILE A 1 119 ? -8.061  2.645   17.185 1.00 19.48  ? 120  ILE A CG1   1 
ATOM   855  C  CG2   . ILE A 1 119 ? -9.200  4.820   17.677 1.00 21.43  ? 120  ILE A CG2   1 
ATOM   856  C  CD1   . ILE A 1 119 ? -8.094  2.800   15.577 1.00 21.01  ? 120  ILE A CD1   1 
ATOM   857  N  N     . LEU A 1 120 ? -11.929 3.260   19.569 1.00 16.62  ? 121  LEU A N     1 
ATOM   858  C  CA    . LEU A 1 120 ? -13.051 3.937   20.200 1.00 17.40  ? 121  LEU A CA    1 
ATOM   859  C  C     . LEU A 1 120 ? -12.902 3.883   21.700 1.00 21.29  ? 121  LEU A C     1 
ATOM   860  O  O     . LEU A 1 120 ? -13.080 4.898   22.371 1.00 19.88  ? 121  LEU A O     1 
ATOM   861  C  CB    . LEU A 1 120 ? -14.347 3.274   19.783 1.00 18.47  ? 121  LEU A CB    1 
ATOM   862  C  CG    . LEU A 1 120 ? -15.628 3.745   20.525 1.00 20.43  ? 121  LEU A CG    1 
ATOM   863  C  CD1   . LEU A 1 120 ? -15.874 5.275   20.460 1.00 24.65  ? 121  LEU A CD1   1 
ATOM   864  C  CD2   . LEU A 1 120 ? -16.831 2.924   20.041 1.00 25.19  ? 121  LEU A CD2   1 
ATOM   865  N  N     . LEU A 1 121 ? -12.670 2.681   22.225 1.00 19.89  ? 122  LEU A N     1 
ATOM   866  C  CA    . LEU A 1 121 ? -12.586 2.559   23.681 1.00 20.71  ? 122  LEU A CA    1 
ATOM   867  C  C     . LEU A 1 121 ? -11.387 3.317   24.216 1.00 19.60  ? 122  LEU A C     1 
ATOM   868  O  O     . LEU A 1 121 ? -11.465 3.915   25.292 1.00 20.16  ? 122  LEU A O     1 
ATOM   869  C  CB    . LEU A 1 121 ? -12.454 1.102   24.092 1.00 25.34  ? 122  LEU A CB    1 
ATOM   870  C  CG    . LEU A 1 121 ? -13.685 0.271   24.288 1.00 40.35  ? 122  LEU A CG    1 
ATOM   871  C  CD1   . LEU A 1 121 ? -13.233 -1.134  24.621 1.00 43.07  ? 122  LEU A CD1   1 
ATOM   872  C  CD2   . LEU A 1 121 ? -14.451 0.925   25.467 1.00 33.02  ? 122  LEU A CD2   1 
ATOM   873  N  N     . ALA A 1 122 ? -10.256 3.303   23.501 1.00 18.20  ? 123  ALA A N     1 
ATOM   874  C  CA    . ALA A 1 122 ? -9.096  4.038   23.994 1.00 18.04  ? 123  ALA A CA    1 
ATOM   875  C  C     . ALA A 1 122 ? -9.418  5.509   24.147 1.00 20.16  ? 123  ALA A C     1 
ATOM   876  O  O     . ALA A 1 122 ? -9.102  6.123   25.170 1.00 21.86  ? 123  ALA A O     1 
ATOM   877  C  CB    . ALA A 1 122 ? -7.891  3.815   23.060 1.00 18.18  ? 123  ALA A CB    1 
ATOM   878  N  N     . LYS A 1 123 ? -10.141 6.082   23.183 1.00 18.81  ? 124  LYS A N     1 
ATOM   879  C  CA    . LYS A 1 123 ? -10.563 7.468   23.311 1.00 18.13  ? 124  LYS A CA    1 
ATOM   880  C  C     . LYS A 1 123 ? -11.524 7.645   24.472 1.00 21.20  ? 124  LYS A C     1 
ATOM   881  O  O     . LYS A 1 123 ? -11.365 8.573   25.282 1.00 22.21  ? 124  LYS A O     1 
ATOM   882  C  CB    . LYS A 1 123 ? -11.236 7.932   22.005 1.00 21.23  ? 124  LYS A CB    1 
ATOM   883  C  CG    . LYS A 1 123 ? -11.782 9.356   22.097 1.00 26.00  ? 124  LYS A CG    1 
ATOM   884  C  CD    . LYS A 1 123 ? -10.631 10.318  22.535 1.00 38.46  ? 124  LYS A CD    1 
ATOM   885  C  CE    . LYS A 1 123 ? -9.408  10.419  21.567 1.00 33.16  ? 124  LYS A CE    1 
ATOM   886  N  NZ    . LYS A 1 123 ? -8.445  11.454  22.112 1.00 46.19  ? 124  LYS A NZ    1 
ATOM   887  N  N     . GLN A 1 124 ? -12.528 6.772   24.563 1.00 19.02  ? 125  GLN A N     1 
ATOM   888  C  CA    . GLN A 1 124 ? -13.556 6.993   25.582 1.00 23.36  ? 125  GLN A CA    1 
ATOM   889  C  C     . GLN A 1 124 ? -13.013 6.841   26.995 1.00 21.80  ? 125  GLN A C     1 
ATOM   890  O  O     . GLN A 1 124 ? -13.467 7.566   27.892 1.00 23.60  ? 125  GLN A O     1 
ATOM   891  C  CB    . GLN A 1 124 ? -14.721 6.045   25.368 1.00 21.79  ? 125  GLN A CB    1 
ATOM   892  C  CG    . GLN A 1 124 ? -15.522 6.432   24.119 1.00 22.17  ? 125  GLN A CG    1 
ATOM   893  C  CD    . GLN A 1 124 ? -16.322 7.694   24.409 1.00 25.15  ? 125  GLN A CD    1 
ATOM   894  O  OE1   . GLN A 1 124 ? -15.834 8.811   24.209 1.00 35.67  ? 125  GLN A OE1   1 
ATOM   895  N  NE2   . GLN A 1 124 ? -17.532 7.518   24.858 1.00 27.55  ? 125  GLN A NE2   1 
ATOM   896  N  N     . VAL A 1 125 ? -12.046 5.937   27.216 1.00 20.98  ? 126  VAL A N     1 
ATOM   897  C  CA    . VAL A 1 125 ? -11.536 5.749   28.578 1.00 25.45  ? 126  VAL A CA    1 
ATOM   898  C  C     . VAL A 1 125 ? -10.323 6.626   28.849 1.00 22.18  ? 126  VAL A C     1 
ATOM   899  O  O     . VAL A 1 125 ? -9.849  6.672   30.004 1.00 30.26  ? 126  VAL A O     1 
ATOM   900  C  CB    . VAL A 1 125 ? -11.210 4.267   28.889 1.00 22.94  ? 126  VAL A CB    1 
ATOM   901  C  CG1   . VAL A 1 125 ? -12.380 3.346   28.585 1.00 27.36  ? 126  VAL A CG1   1 
ATOM   902  C  CG2   . VAL A 1 125 ? -9.940  3.800   28.125 1.00 24.55  ? 126  VAL A CG2   1 
ATOM   903  N  N     . GLY A 1 126 ? -9.862  7.407   27.879 1.00 22.77  ? 127  GLY A N     1 
ATOM   904  C  CA    . GLY A 1 126 ? -8.831  8.397   28.126 1.00 22.03  ? 127  GLY A CA    1 
ATOM   905  C  C     . GLY A 1 126 ? -7.402  7.951   27.933 1.00 23.43  ? 127  GLY A C     1 
ATOM   906  O  O     . GLY A 1 126 ? -6.492  8.534   28.544 1.00 27.32  ? 127  GLY A O     1 
ATOM   907  N  N     . VAL A 1 127 ? -7.162  6.957   27.086 1.00 22.41  ? 128  VAL A N     1 
ATOM   908  C  CA    . VAL A 1 127 ? -5.758  6.623   26.813 1.00 19.63  ? 128  VAL A CA    1 
ATOM   909  C  C     . VAL A 1 127 ? -5.103  7.816   26.140 1.00 22.55  ? 128  VAL A C     1 
ATOM   910  O  O     . VAL A 1 127 ? -5.624  8.313   25.123 1.00 23.94  ? 128  VAL A O     1 
ATOM   911  C  CB    . VAL A 1 127 ? -5.681  5.382   25.913 1.00 19.90  ? 128  VAL A CB    1 
ATOM   912  C  CG1   . VAL A 1 127 ? -4.186  5.126   25.477 1.00 19.72  ? 128  VAL A CG1   1 
ATOM   913  C  CG2   . VAL A 1 127 ? -6.313  4.165   26.651 1.00 22.42  ? 128  VAL A CG2   1 
ATOM   914  N  N     . PRO A 1 128 ? -3.985  8.325   26.626 1.00 20.08  ? 129  PRO A N     1 
ATOM   915  C  CA    . PRO A 1 128 ? -3.518  9.617   26.103 1.00 21.56  ? 129  PRO A CA    1 
ATOM   916  C  C     . PRO A 1 128 ? -3.032  9.573   24.669 1.00 21.80  ? 129  PRO A C     1 
ATOM   917  O  O     . PRO A 1 128 ? -3.311  10.514  23.898 1.00 24.07  ? 129  PRO A O     1 
ATOM   918  C  CB    . PRO A 1 128 ? -2.393  9.984   27.078 1.00 25.27  ? 129  PRO A CB    1 
ATOM   919  C  CG    . PRO A 1 128 ? -2.828  9.305   28.359 1.00 22.99  ? 129  PRO A CG    1 
ATOM   920  C  CD    . PRO A 1 128 ? -3.442  8.038   27.993 1.00 19.90  ? 129  PRO A CD    1 
ATOM   921  N  N     . ASN A 1 129 ? -2.298  8.527   24.316 1.00 18.21  ? 130  ASN A N     1 
ATOM   922  C  CA    . ASN A 1 129 ? -1.560  8.519   23.068 1.00 17.41  ? 130  ASN A CA    1 
ATOM   923  C  C     . ASN A 1 129 ? -1.481  7.103   22.523 1.00 17.60  ? 130  ASN A C     1 
ATOM   924  O  O     . ASN A 1 129 ? -1.447  6.119   23.262 1.00 18.75  ? 130  ASN A O     1 
ATOM   925  C  CB    . ASN A 1 129 ? -0.125  9.045   23.296 1.00 18.89  ? 130  ASN A CB    1 
ATOM   926  C  CG    . ASN A 1 129 ? -0.103  10.531  23.550 1.00 23.11  ? 130  ASN A CG    1 
ATOM   927  O  OD1   . ASN A 1 129 ? -0.251  10.966  24.697 1.00 26.31  ? 130  ASN A OD1   1 
ATOM   928  N  ND2   . ASN A 1 129 ? 0.145   11.332  22.512 1.00 24.63  ? 130  ASN A ND2   1 
ATOM   929  N  N     . ILE A 1 130 ? -1.426  7.007   21.198 1.00 14.23  ? 131  ILE A N     1 
ATOM   930  C  CA    . ILE A 1 130 ? -1.307  5.738   20.492 1.00 16.84  ? 131  ILE A CA    1 
ATOM   931  C  C     . ILE A 1 130 ? -0.063  5.757   19.585 1.00 14.07  ? 131  ILE A C     1 
ATOM   932  O  O     . ILE A 1 130 ? 0.286   6.799   18.999 1.00 16.20  ? 131  ILE A O     1 
ATOM   933  C  CB    . ILE A 1 130 ? -2.568  5.445   19.642 1.00 15.75  ? 131  ILE A CB    1 
ATOM   934  C  CG1   . ILE A 1 130 ? -3.788  5.185   20.593 1.00 22.93  ? 131  ILE A CG1   1 
ATOM   935  C  CG2   . ILE A 1 130 ? -2.325  4.237   18.710 1.00 15.91  ? 131  ILE A CG2   1 
ATOM   936  C  CD1   . ILE A 1 130 ? -5.139  4.870   19.872 1.00 24.26  ? 131  ILE A CD1   1 
ATOM   937  N  N     . VAL A 1 131 ? 0.656   4.623   19.559 1.00 14.26  ? 132  VAL A N     1 
ATOM   938  C  CA    . VAL A 1 131 ? 1.635   4.340   18.507 1.00 13.51  ? 132  VAL A CA    1 
ATOM   939  C  C     . VAL A 1 131 ? 1.145   3.106   17.758 1.00 13.69  ? 132  VAL A C     1 
ATOM   940  O  O     . VAL A 1 131 ? 0.618   2.177   18.370 1.00 15.17  ? 132  VAL A O     1 
ATOM   941  C  CB    . VAL A 1 131 ? 3.008   4.048   19.137 1.00 14.60  ? 132  VAL A CB    1 
ATOM   942  C  CG1   . VAL A 1 131 ? 4.012   3.531   18.097 1.00 16.38  ? 132  VAL A CG1   1 
ATOM   943  C  CG2   . VAL A 1 131 ? 3.524   5.325   19.844 1.00 17.66  ? 132  VAL A CG2   1 
ATOM   944  N  N     . VAL A 1 132 ? 1.304   3.074   16.440 1.00 14.14  ? 133  VAL A N     1 
ATOM   945  C  CA    . VAL A 1 132 ? 0.844   1.945   15.632 1.00 13.93  ? 133  VAL A CA    1 
ATOM   946  C  C     . VAL A 1 132 ? 2.014   1.086   15.186 1.00 13.05  ? 133  VAL A C     1 
ATOM   947  O  O     . VAL A 1 132 ? 3.025   1.621   14.692 1.00 14.14  ? 133  VAL A O     1 
ATOM   948  C  CB    . VAL A 1 132 ? 0.065   2.464   14.412 1.00 12.92  ? 133  VAL A CB    1 
ATOM   949  C  CG1   . VAL A 1 132 ? -0.372  1.308   13.495 1.00 15.40  ? 133  VAL A CG1   1 
ATOM   950  C  CG2   . VAL A 1 132 ? -1.109  3.337   14.792 1.00 13.84  ? 133  VAL A CG2   1 
ATOM   951  N  N     . PHE A 1 133 ? 1.872   -0.219  15.304 1.00 11.94  ? 134  PHE A N     1 
ATOM   952  C  CA    . PHE A 1 133 ? 2.755   -1.162  14.628 1.00 12.44  ? 134  PHE A CA    1 
ATOM   953  C  C     . PHE A 1 133 ? 1.947   -1.850  13.540 1.00 13.57  ? 134  PHE A C     1 
ATOM   954  O  O     . PHE A 1 133 ? 0.972   -2.553  13.835 1.00 13.68  ? 134  PHE A O     1 
ATOM   955  C  CB    . PHE A 1 133 ? 3.343   -2.157  15.636 1.00 13.71  ? 134  PHE A CB    1 
ATOM   956  C  CG    . PHE A 1 133 ? 4.485   -2.975  15.029 1.00 12.73  ? 134  PHE A CG    1 
ATOM   957  C  CD1   . PHE A 1 133 ? 5.733   -2.376  14.851 1.00 15.51  ? 134  PHE A CD1   1 
ATOM   958  C  CD2   . PHE A 1 133 ? 4.298   -4.277  14.563 1.00 14.80  ? 134  PHE A CD2   1 
ATOM   959  C  CE1   . PHE A 1 133 ? 6.785   -3.119  14.282 1.00 14.99  ? 134  PHE A CE1   1 
ATOM   960  C  CE2   . PHE A 1 133 ? 5.380   -5.000  13.985 1.00 14.62  ? 134  PHE A CE2   1 
ATOM   961  C  CZ    . PHE A 1 133 ? 6.605   -4.395  13.871 1.00 13.67  ? 134  PHE A CZ    1 
ATOM   962  N  N     . LEU A 1 134 ? 2.361   -1.615  12.281 1.00 14.29  ? 135  LEU A N     1 
ATOM   963  C  CA    . LEU A 1 134 ? 1.725   -2.224  11.107 1.00 13.95  ? 135  LEU A CA    1 
ATOM   964  C  C     . LEU A 1 134 ? 2.459   -3.557  10.892 1.00 15.20  ? 135  LEU A C     1 
ATOM   965  O  O     . LEU A 1 134 ? 3.576   -3.567  10.385 1.00 16.16  ? 135  LEU A O     1 
ATOM   966  C  CB    . LEU A 1 134 ? 1.849   -1.284  9.920  1.00 15.17  ? 135  LEU A CB    1 
ATOM   967  C  CG    . LEU A 1 134 ? 1.217   -1.808  8.665  1.00 19.04  ? 135  LEU A CG    1 
ATOM   968  C  CD1   . LEU A 1 134 ? -0.292  -2.014  8.862  1.00 23.31  ? 135  LEU A CD1   1 
ATOM   969  C  CD2   . LEU A 1 134 ? 1.419   -0.673  7.627  1.00 26.47  ? 135  LEU A CD2   1 
ATOM   970  N  N     . ASN A 1 135 ? 1.875   -4.650  11.390 1.00 13.56  ? 136  ASN A N     1 
ATOM   971  C  CA    . ASN A 1 135 ? 2.520   -5.932  11.474 1.00 13.31  ? 136  ASN A CA    1 
ATOM   972  C  C     . ASN A 1 135 ? 2.314   -6.724  10.194 1.00 16.01  ? 136  ASN A C     1 
ATOM   973  O  O     . ASN A 1 135 ? 1.537   -6.373  9.308  1.00 15.84  ? 136  ASN A O     1 
ATOM   974  C  CB    . ASN A 1 135 ? 1.918   -6.695  12.668 1.00 13.93  ? 136  ASN A CB    1 
ATOM   975  C  CG    . ASN A 1 135 ? 2.729   -7.873  13.069 1.00 14.75  ? 136  ASN A CG    1 
ATOM   976  O  OD1   . ASN A 1 135 ? 3.967   -7.867  12.952 1.00 14.17  ? 136  ASN A OD1   1 
ATOM   977  N  ND2   . ASN A 1 135 ? 2.053   -8.940  13.500 1.00 14.08  ? 136  ASN A ND2   1 
ATOM   978  N  N     . LYS A 1 136 ? 3.035   -7.832  10.109 1.00 14.61  ? 137  LYS A N     1 
ATOM   979  C  CA    . LYS A 1 136 ? 2.904   -8.782  8.995  1.00 14.38  ? 137  LYS A CA    1 
ATOM   980  C  C     . LYS A 1 136 ? 3.352   -8.135  7.685  1.00 16.44  ? 137  LYS A C     1 
ATOM   981  O  O     . LYS A 1 136 ? 2.862   -8.483  6.605  1.00 16.83  ? 137  LYS A O     1 
ATOM   982  C  CB    . LYS A 1 136 ? 1.472   -9.395  8.873  1.00 15.38  ? 137  LYS A CB    1 
ATOM   983  C  CG    . LYS A 1 136 ? 0.939   -9.985  10.213 1.00 15.45  ? 137  LYS A CG    1 
ATOM   984  C  CD    . LYS A 1 136 ? -0.145  -11.006 9.956  1.00 15.90  ? 137  LYS A CD    1 
ATOM   985  C  CE    . LYS A 1 136 ? -0.655  -11.481 11.291 1.00 16.58  ? 137  LYS A CE    1 
ATOM   986  N  NZ    . LYS A 1 136 ? -1.727  -12.512 11.145 1.00 17.65  ? 137  LYS A NZ    1 
ATOM   987  N  N     . GLU A 1 137 ? 4.343   -7.221  7.793  1.00 15.31  ? 138  GLU A N     1 
ATOM   988  C  CA    . GLU A 1 137 ? 4.911   -6.618  6.592  1.00 15.06  ? 138  GLU A CA    1 
ATOM   989  C  C     . GLU A 1 137 ? 5.494   -7.685  5.661  1.00 16.61  ? 138  GLU A C     1 
ATOM   990  O  O     . GLU A 1 137 ? 5.540   -7.522  4.440  1.00 18.78  ? 138  GLU A O     1 
ATOM   991  C  CB    . GLU A 1 137 ? 5.986   -5.609  6.998  1.00 18.15  ? 138  GLU A CB    1 
ATOM   992  C  CG    . GLU A 1 137 ? 6.423   -4.766  5.831  1.00 18.93  ? 138  GLU A CG    1 
ATOM   993  C  CD    . GLU A 1 137 ? 7.542   -3.830  6.147  1.00 23.12  ? 138  GLU A CD    1 
ATOM   994  O  OE1   . GLU A 1 137 ? 8.192   -3.982  7.158  1.00 20.96  ? 138  GLU A OE1   1 
ATOM   995  O  OE2   . GLU A 1 137 ? 7.829   -2.946  5.305  1.00 29.74  ? 138  GLU A OE2   1 
ATOM   996  N  N     . ASP A 1 138 ? 5.940   -8.813  6.230  1.00 16.29  ? 139  ASP A N     1 
ATOM   997  C  CA    . ASP A 1 138 ? 6.448   -9.904  5.407  1.00 17.73  ? 139  ASP A CA    1 
ATOM   998  C  C     . ASP A 1 138 ? 5.429   -10.496 4.460  1.00 16.28  ? 139  ASP A C     1 
ATOM   999  O  O     . ASP A 1 138 ? 5.830   -11.185 3.513  1.00 22.18  ? 139  ASP A O     1 
ATOM   1000 C  CB    . ASP A 1 138 ? 7.004   -11.042 6.296  1.00 17.99  ? 139  ASP A CB    1 
ATOM   1001 C  CG    . ASP A 1 138 ? 5.969   -11.608 7.321  1.00 16.66  ? 139  ASP A CG    1 
ATOM   1002 O  OD1   . ASP A 1 138 ? 5.262   -10.857 8.015  1.00 17.38  ? 139  ASP A OD1   1 
ATOM   1003 O  OD2   . ASP A 1 138 ? 5.838   -12.807 7.321  1.00 20.60  ? 139  ASP A OD2   1 
ATOM   1004 N  N     . MET A 1 139 ? 4.143   -10.304 4.709  1.00 18.58  ? 140  MET A N     1 
ATOM   1005 C  CA    . MET A 1 139 ? 3.078   -10.812 3.865  1.00 19.61  ? 140  MET A CA    1 
ATOM   1006 C  C     . MET A 1 139 ? 2.697   -9.870  2.749  1.00 23.19  ? 140  MET A C     1 
ATOM   1007 O  O     . MET A 1 139 ? 1.857   -10.236 1.913  1.00 25.84  ? 140  MET A O     1 
ATOM   1008 C  CB    . MET A 1 139 ? 1.839   -11.088 4.739  1.00 21.75  ? 140  MET A CB    1 
ATOM   1009 C  CG    . MET A 1 139 ? 2.043   -12.174 5.853  1.00 20.92  ? 140  MET A CG    1 
ATOM   1010 S  SD    . MET A 1 139 ? 2.592   -13.742 5.133  1.00 25.76  ? 140  MET A SD    1 
ATOM   1011 C  CE    . MET A 1 139 ? 1.198   -14.309 4.135  1.00 32.33  ? 140  MET A CE    1 
ATOM   1012 N  N     . VAL A 1 140 ? 3.249   -8.666  2.715  1.00 20.24  ? 141  VAL A N     1 
ATOM   1013 C  CA    . VAL A 1 140 ? 2.803   -7.674  1.752  1.00 20.70  ? 141  VAL A CA    1 
ATOM   1014 C  C     . VAL A 1 140 ? 4.038   -7.201  0.984  1.00 26.11  ? 141  VAL A C     1 
ATOM   1015 O  O     . VAL A 1 140 ? 4.811   -6.394  1.508  1.00 37.09  ? 141  VAL A O     1 
ATOM   1016 C  CB    . VAL A 1 140 ? 2.090   -6.502  2.426  1.00 25.61  ? 141  VAL A CB    1 
ATOM   1017 C  CG1   . VAL A 1 140 ? 1.700   -5.492  1.323  1.00 23.48  ? 141  VAL A CG1   1 
ATOM   1018 C  CG2   . VAL A 1 140 ? 0.847   -7.003  3.149  1.00 28.75  ? 141  VAL A CG2   1 
ATOM   1019 N  N     . ASP A 1 141 ? 4.145   -7.584  -0.271 1.00 33.18  ? 142  ASP A N     1 
ATOM   1020 C  CA    . ASP A 1 141 ? 5.340   -7.279  -1.053 1.00 49.49  ? 142  ASP A CA    1 
ATOM   1021 C  C     . ASP A 1 141 ? 5.256   -5.973  -1.849 1.00 49.36  ? 142  ASP A C     1 
ATOM   1022 O  O     . ASP A 1 141 ? 6.164   -5.687  -2.631 1.00 55.13  ? 142  ASP A O     1 
ATOM   1023 C  CB    . ASP A 1 141 ? 5.649   -8.446  -1.995 1.00 68.22  ? 142  ASP A CB    1 
ATOM   1024 C  CG    . ASP A 1 141 ? 4.475   -8.795  -2.895 1.00 84.52  ? 142  ASP A CG    1 
ATOM   1025 O  OD1   . ASP A 1 141 ? 3.407   -8.146  -2.773 1.00 84.82  ? 142  ASP A OD1   1 
ATOM   1026 O  OD2   . ASP A 1 141 ? 4.615   -9.732  -3.715 1.00 94.72  ? 142  ASP A OD2   1 
ATOM   1027 N  N     . ASP A 1 142 ? 4.210   -5.172  -1.665 1.00 42.54  ? 143  ASP A N     1 
ATOM   1028 C  CA    . ASP A 1 142 ? 4.001   -3.962  -2.450 1.00 40.12  ? 143  ASP A CA    1 
ATOM   1029 C  C     . ASP A 1 142 ? 3.966   -2.775  -1.493 1.00 28.98  ? 143  ASP A C     1 
ATOM   1030 O  O     . ASP A 1 142 ? 3.027   -2.640  -0.706 1.00 29.53  ? 143  ASP A O     1 
ATOM   1031 C  CB    . ASP A 1 142 ? 2.717   -4.074  -3.268 1.00 50.47  ? 143  ASP A CB    1 
ATOM   1032 C  CG    . ASP A 1 142 ? 2.571   -2.959  -4.289 1.00 77.36  ? 143  ASP A CG    1 
ATOM   1033 O  OD1   . ASP A 1 142 ? 3.398   -2.016  -4.283 1.00 85.68  ? 143  ASP A OD1   1 
ATOM   1034 O  OD2   . ASP A 1 142 ? 1.648   -3.042  -5.132 1.00 86.71  ? 143  ASP A OD2   1 
ATOM   1035 N  N     . ALA A 1 143 ? 4.997   -1.924  -1.559 1.00 28.62  ? 144  ALA A N     1 
ATOM   1036 C  CA    . ALA A 1 143 ? 5.047   -0.691  -0.764 1.00 29.69  ? 144  ALA A CA    1 
ATOM   1037 C  C     . ALA A 1 143 ? 3.809   0.186   -0.947 1.00 28.97  ? 144  ALA A C     1 
ATOM   1038 O  O     . ALA A 1 143 ? 3.366   0.843   0.013  1.00 28.85  ? 144  ALA A O     1 
ATOM   1039 C  CB    . ALA A 1 143 ? 6.269   0.133   -1.151 1.00 27.28  ? 144  ALA A CB    1 
ATOM   1040 N  N     . GLU A 1 144 ? 3.263   0.240   -2.167 1.00 26.62  ? 145  GLU A N     1 
ATOM   1041 C  CA    . GLU A 1 144 ? 2.024   0.972   -2.433 1.00 28.02  ? 145  GLU A CA    1 
ATOM   1042 C  C     . GLU A 1 144 ? 0.918   0.540   -1.496 1.00 27.75  ? 145  GLU A C     1 
ATOM   1043 O  O     . GLU A 1 144 ? 0.152   1.376   -0.997 1.00 21.76  ? 145  GLU A O     1 
ATOM   1044 C  CB    . GLU A 1 144 ? 1.556   0.748   -3.901 1.00 30.69  ? 145  GLU A CB    1 
ATOM   1045 C  CG    . GLU A 1 144 ? 0.093   1.153   -4.120 1.00 55.88  ? 145  GLU A CG    1 
ATOM   1046 C  CD    . GLU A 1 144 ? -0.545  0.546   -5.367 1.00 73.87  ? 145  GLU A CD    1 
ATOM   1047 O  OE1   . GLU A 1 144 ? 0.140   -0.219  -6.088 1.00 74.92  ? 145  GLU A OE1   1 
ATOM   1048 O  OE2   . GLU A 1 144 ? -1.752  0.811   -5.600 1.00 75.60  ? 145  GLU A OE2   1 
ATOM   1049 N  N     . LEU A 1 145 ? 0.779   -0.771  -1.291 1.00 26.57  ? 146  LEU A N     1 
ATOM   1050 C  CA    . LEU A 1 145 ? -0.317  -1.256  -0.476 1.00 23.13  ? 146  LEU A CA    1 
ATOM   1051 C  C     . LEU A 1 145 ? -0.073  -0.900  0.981  1.00 19.94  ? 146  LEU A C     1 
ATOM   1052 O  O     . LEU A 1 145 ? -1.020  -0.604  1.732  1.00 21.14  ? 146  LEU A O     1 
ATOM   1053 C  CB    . LEU A 1 145 ? -0.460  -2.779  -0.636 1.00 24.35  ? 146  LEU A CB    1 
ATOM   1054 C  CG    . LEU A 1 145 ? -1.195  -3.354  -1.852 1.00 43.27  ? 146  LEU A CG    1 
ATOM   1055 C  CD1   . LEU A 1 145 ? -2.697  -3.073  -1.774 1.00 52.32  ? 146  LEU A CD1   1 
ATOM   1056 C  CD2   . LEU A 1 145 ? -0.679  -2.804  -3.130 1.00 57.78  ? 146  LEU A CD2   1 
ATOM   1057 N  N     . LEU A 1 146 ? 1.192   -0.912  1.425  1.00 20.72  ? 147  LEU A N     1 
ATOM   1058 C  CA    . LEU A 1 146 ? 1.453   -0.553  2.820  1.00 20.74  ? 147  LEU A CA    1 
ATOM   1059 C  C     . LEU A 1 146 ? 1.089   0.908   3.081  1.00 20.57  ? 147  LEU A C     1 
ATOM   1060 O  O     . LEU A 1 146 ? 0.576   1.259   4.160  1.00 19.56  ? 147  LEU A O     1 
ATOM   1061 C  CB    . LEU A 1 146 ? 2.917   -0.814  3.189  1.00 22.05  ? 147  LEU A CB    1 
ATOM   1062 C  CG    . LEU A 1 146 ? 3.461   -2.241  3.360  1.00 32.44  ? 147  LEU A CG    1 
ATOM   1063 C  CD1   . LEU A 1 146 ? 2.646   -3.100  4.338  1.00 25.60  ? 147  LEU A CD1   1 
ATOM   1064 C  CD2   . LEU A 1 146 ? 3.802   -2.938  2.114  1.00 55.19  ? 147  LEU A CD2   1 
ATOM   1065 N  N     . GLU A 1 147 ? 1.382   1.803   2.133  1.00 20.26  ? 148  GLU A N     1 
ATOM   1066 C  CA    . GLU A 1 147 ? 1.012   3.195   2.353  1.00 19.29  ? 148  GLU A CA    1 
ATOM   1067 C  C     . GLU A 1 147 ? -0.495  3.383   2.442  1.00 18.17  ? 148  GLU A C     1 
ATOM   1068 O  O     . GLU A 1 147 ? -0.972  4.200   3.243  1.00 17.93  ? 148  GLU A O     1 
ATOM   1069 C  CB    . GLU A 1 147 ? 1.562   4.043   1.217  1.00 20.09  ? 148  GLU A CB    1 
ATOM   1070 C  CG    . GLU A 1 147 ? 1.059   5.470   1.125  1.00 19.98  ? 148  GLU A CG    1 
ATOM   1071 C  CD    . GLU A 1 147 ? 1.557   6.341   2.219  1.00 25.17  ? 148  GLU A CD    1 
ATOM   1072 O  OE1   . GLU A 1 147 ? 2.454   5.941   3.008  1.00 28.15  ? 148  GLU A OE1   1 
ATOM   1073 O  OE2   . GLU A 1 147 ? 1.043   7.500   2.312  1.00 25.13  ? 148  GLU A OE2   1 
ATOM   1074 N  N     . LEU A 1 148 ? -1.246  2.646   1.621  1.00 18.22  ? 149  LEU A N     1 
ATOM   1075 C  CA    . LEU A 1 148 ? -2.706  2.725   1.680  1.00 17.38  ? 149  LEU A CA    1 
ATOM   1076 C  C     . LEU A 1 148 ? -3.234  2.233   3.038  1.00 16.62  ? 149  LEU A C     1 
ATOM   1077 O  O     . LEU A 1 148 ? -4.161  2.849   3.596  1.00 18.54  ? 149  LEU A O     1 
ATOM   1078 C  CB    . LEU A 1 148 ? -3.357  1.961   0.520  1.00 19.33  ? 149  LEU A CB    1 
ATOM   1079 C  CG    . LEU A 1 148 ? -3.348  2.630   -0.865 1.00 26.36  ? 149  LEU A CG    1 
ATOM   1080 C  CD1   . LEU A 1 148 ? -3.859  4.057   -0.846 1.00 25.11  ? 149  LEU A CD1   1 
ATOM   1081 C  CD2   . LEU A 1 148 ? -2.218  2.525   -1.783 1.00 52.67  ? 149  LEU A CD2   1 
ATOM   1082 N  N     . VAL A 1 149 ? -2.669  1.146   3.585  1.00 16.51  ? 150  VAL A N     1 
ATOM   1083 C  CA    . VAL A 1 149 ? -3.104  0.721   4.906  1.00 15.89  ? 150  VAL A CA    1 
ATOM   1084 C  C     . VAL A 1 149 ? -2.737  1.788   5.949  1.00 17.66  ? 150  VAL A C     1 
ATOM   1085 O  O     . VAL A 1 149 ? -3.554  2.100   6.829  1.00 17.39  ? 150  VAL A O     1 
ATOM   1086 C  CB    . VAL A 1 149 ? -2.507  -0.656  5.306  1.00 20.09  ? 150  VAL A CB    1 
ATOM   1087 C  CG1   . VAL A 1 149 ? -3.003  -1.010  6.729  1.00 21.74  ? 150  VAL A CG1   1 
ATOM   1088 C  CG2   . VAL A 1 149 ? -2.944  -1.710  4.354  1.00 22.69  ? 150  VAL A CG2   1 
ATOM   1089 N  N     . GLU A 1 150 ? -1.521  2.411   5.859  1.00 16.22  ? 151  GLU A N     1 
ATOM   1090 C  CA    . GLU A 1 150 ? -1.172  3.486   6.805  1.00 14.84  ? 151  GLU A CA    1 
ATOM   1091 C  C     . GLU A 1 150 ? -2.167  4.634   6.723  1.00 17.44  ? 151  GLU A C     1 
ATOM   1092 O  O     . GLU A 1 150 ? -2.615  5.120   7.767  1.00 16.85  ? 151  GLU A O     1 
ATOM   1093 C  CB    . GLU A 1 150 ? 0.247   4.024   6.555  1.00 17.25  ? 151  GLU A CB    1 
ATOM   1094 C  CG    . GLU A 1 150 ? 0.652   5.114   7.482  1.00 34.73  ? 151  GLU A CG    1 
ATOM   1095 C  CD    . GLU A 1 150 ? 2.156   5.421   7.435  1.00 44.70  ? 151  GLU A CD    1 
ATOM   1096 O  OE1   . GLU A 1 150 ? 2.890   4.580   6.928  1.00 34.03  ? 151  GLU A OE1   1 
ATOM   1097 O  OE2   . GLU A 1 150 ? 2.570   6.536   7.852  1.00 48.01  ? 151  GLU A OE2   1 
ATOM   1098 N  N     . LEU A 1 151 ? -2.534  5.066   5.505  1.00 16.46  ? 152  LEU A N     1 
ATOM   1099 C  CA    . LEU A 1 151 ? -3.485  6.174   5.412  1.00 15.57  ? 152  LEU A CA    1 
ATOM   1100 C  C     . LEU A 1 151 ? -4.846  5.777   5.989  1.00 17.93  ? 152  LEU A C     1 
ATOM   1101 O  O     . LEU A 1 151 ? -5.520  6.607   6.618  1.00 16.69  ? 152  LEU A O     1 
ATOM   1102 C  CB    . LEU A 1 151 ? -3.637  6.612   3.936  1.00 16.09  ? 152  LEU A CB    1 
ATOM   1103 C  CG    . LEU A 1 151 ? -2.343  7.258   3.401  1.00 18.81  ? 152  LEU A CG    1 
ATOM   1104 C  CD1   . LEU A 1 151 ? -2.521  7.383   1.883  1.00 18.42  ? 152  LEU A CD1   1 
ATOM   1105 C  CD2   . LEU A 1 151 ? -2.105  8.631   3.996  1.00 21.83  ? 152  LEU A CD2   1 
ATOM   1106 N  N     . GLU A 1 152 ? -5.287  4.560   5.715  1.00 17.24  ? 153  GLU A N     1 
ATOM   1107 C  CA    . GLU A 1 152 ? -6.556  4.088   6.277  1.00 16.04  ? 153  GLU A CA    1 
ATOM   1108 C  C     . GLU A 1 152 ? -6.535  4.132   7.802  1.00 16.97  ? 153  GLU A C     1 
ATOM   1109 O  O     . GLU A 1 152 ? -7.501  4.571   8.445  1.00 17.57  ? 153  GLU A O     1 
ATOM   1110 C  CB    . GLU A 1 152 ? -6.853  2.677   5.835  1.00 18.38  ? 153  GLU A CB    1 
ATOM   1111 C  CG    . GLU A 1 152 ? -8.268  2.303   6.204  1.00 28.40  ? 153  GLU A CG    1 
ATOM   1112 C  CD    . GLU A 1 152 ? -8.675  0.953   5.657  1.00 41.01  ? 153  GLU A CD    1 
ATOM   1113 O  OE1   . GLU A 1 152 ? -7.848  0.356   4.938  1.00 33.19  ? 153  GLU A OE1   1 
ATOM   1114 O  OE2   . GLU A 1 152 ? -9.800  0.500   5.974  1.00 53.66  ? 153  GLU A OE2   1 
ATOM   1115 N  N     . VAL A 1 153 ? -5.426  3.709   8.405  1.00 15.42  ? 154  VAL A N     1 
ATOM   1116 C  CA    . VAL A 1 153 ? -5.293  3.738   9.868  1.00 14.54  ? 154  VAL A CA    1 
ATOM   1117 C  C     . VAL A 1 153 ? -5.244  5.171   10.372 1.00 15.26  ? 154  VAL A C     1 
ATOM   1118 O  O     . VAL A 1 153 ? -5.874  5.505   11.389 1.00 15.84  ? 154  VAL A O     1 
ATOM   1119 C  CB    . VAL A 1 153 ? -4.040  2.948   10.249 1.00 14.48  ? 154  VAL A CB    1 
ATOM   1120 C  CG1   . VAL A 1 153 ? -3.764  3.108   11.765 1.00 18.39  ? 154  VAL A CG1   1 
ATOM   1121 C  CG2   . VAL A 1 153 ? -4.298  1.447   9.982  1.00 18.49  ? 154  VAL A CG2   1 
ATOM   1122 N  N     . ARG A 1 154 ? -4.501  6.064   9.692  1.00 14.68  ? 155  ARG A N     1 
ATOM   1123 C  CA    . ARG A 1 154 ? -4.500  7.450   10.133 1.00 17.15  ? 155  ARG A CA    1 
ATOM   1124 C  C     . ARG A 1 154 ? -5.893  8.054   10.073 1.00 15.48  ? 155  ARG A C     1 
ATOM   1125 O  O     . ARG A 1 154 ? -6.270  8.820   10.964 1.00 16.48  ? 155  ARG A O     1 
ATOM   1126 C  CB    . ARG A 1 154 ? -3.549  8.296   9.283  1.00 16.97  ? 155  ARG A CB    1 
ATOM   1127 C  CG    . ARG A 1 154 ? -2.088  7.865   9.475  1.00 17.29  ? 155  ARG A CG    1 
ATOM   1128 C  CD    . ARG A 1 154 ? -1.130  8.899   8.788  1.00 16.04  ? 155  ARG A CD    1 
ATOM   1129 N  NE    . ARG A 1 154 ? 0.231   8.450   8.988  1.00 18.34  ? 155  ARG A NE    1 
ATOM   1130 C  CZ    . ARG A 1 154 ? 0.891   8.578   10.148 1.00 17.13  ? 155  ARG A CZ    1 
ATOM   1131 N  NH1   . ARG A 1 154 ? 0.368   9.187   11.195 1.00 18.72  ? 155  ARG A NH1   1 
ATOM   1132 N  NH2   . ARG A 1 154 ? 2.127   8.037   10.181 1.00 19.42  ? 155  ARG A NH2   1 
ATOM   1133 N  N     . GLU A 1 155 ? -6.660  7.740   9.012  1.00 16.97  ? 156  GLU A N     1 
ATOM   1134 C  CA    . GLU A 1 155 ? -8.015  8.273   8.922  1.00 15.58  ? 156  GLU A CA    1 
ATOM   1135 C  C     . GLU A 1 155 ? -8.886  7.718   10.052 1.00 16.05  ? 156  GLU A C     1 
ATOM   1136 O  O     . GLU A 1 155 ? -9.701  8.471   10.621 1.00 17.31  ? 156  GLU A O     1 
ATOM   1137 C  CB    . GLU A 1 155 ? -8.596  7.894   7.568  1.00 17.46  ? 156  GLU A CB    1 
ATOM   1138 C  CG    . GLU A 1 155 ? -10.029 8.343   7.367  1.00 18.16  ? 156  GLU A CG    1 
ATOM   1139 C  CD    . GLU A 1 155 ? -10.544 7.921   5.991  1.00 20.08  ? 156  GLU A CD    1 
ATOM   1140 O  OE1   . GLU A 1 155 ? -10.553 6.723   5.659  1.00 22.52  ? 156  GLU A OE1   1 
ATOM   1141 O  OE2   . GLU A 1 155 ? -10.800 8.820   5.199  1.00 20.83  ? 156  GLU A OE2   1 
ATOM   1142 N  N     . LEU A 1 156 ? -8.739  6.437   10.343 1.00 15.49  ? 157  LEU A N     1 
ATOM   1143 C  CA    . LEU A 1 156 ? -9.525  5.826   11.401 1.00 16.61  ? 157  LEU A CA    1 
ATOM   1144 C  C     . LEU A 1 156 ? -9.225  6.499   12.727 1.00 17.28  ? 157  LEU A C     1 
ATOM   1145 O  O     . LEU A 1 156 ? -10.142 6.842   13.484 1.00 17.52  ? 157  LEU A O     1 
ATOM   1146 C  CB    . LEU A 1 156 ? -9.181  4.321   11.446 1.00 18.40  ? 157  LEU A CB    1 
ATOM   1147 C  CG    . LEU A 1 156 ? -9.988  3.442   12.399 1.00 17.67  ? 157  LEU A CG    1 
ATOM   1148 C  CD1   . LEU A 1 156 ? -11.506 3.559   11.983 1.00 28.45  ? 157  LEU A CD1   1 
ATOM   1149 C  CD2   . LEU A 1 156 ? -9.543  2.010   12.225 1.00 20.04  ? 157  LEU A CD2   1 
ATOM   1150 N  N     . LEU A 1 157 ? -7.929  6.699   13.026 1.00 14.95  ? 158  LEU A N     1 
ATOM   1151 C  CA    . LEU A 1 157 ? -7.543  7.338   14.274 1.00 15.82  ? 158  LEU A CA    1 
ATOM   1152 C  C     . LEU A 1 157 ? -8.142  8.725   14.361 1.00 15.46  ? 158  LEU A C     1 
ATOM   1153 O  O     . LEU A 1 157 ? -8.700  9.107   15.412 1.00 17.90  ? 158  LEU A O     1 
ATOM   1154 C  CB    . LEU A 1 157 ? -6.004  7.408   14.368 1.00 15.89  ? 158  LEU A CB    1 
ATOM   1155 C  CG    . LEU A 1 157 ? -5.390  6.027   14.644 1.00 16.24  ? 158  LEU A CG    1 
ATOM   1156 C  CD1   . LEU A 1 157 ? -3.893  6.129   14.263 1.00 17.86  ? 158  LEU A CD1   1 
ATOM   1157 C  CD2   . LEU A 1 157 ? -5.519  5.678   16.180 1.00 18.54  ? 158  LEU A CD2   1 
ATOM   1158 N  N     . SER A 1 158 ? -8.049  9.513   13.262 1.00 14.77  ? 159  SER A N     1 
ATOM   1159 C  CA    . SER A 1 158 ? -8.625  10.859  13.251 1.00 16.69  ? 159  SER A CA    1 
ATOM   1160 C  C     . SER A 1 158 ? -10.130 10.862  13.481 1.00 17.25  ? 159  SER A C     1 
ATOM   1161 O  O     . SER A 1 158 ? -10.647 11.789  14.139 1.00 21.34  ? 159  SER A O     1 
ATOM   1162 C  CB    . SER A 1 158 ? -8.277  11.541  11.932 1.00 19.80  ? 159  SER A CB    1 
ATOM   1163 O  OG    . SER A 1 158 ? -6.873  11.837  11.925 1.00 23.86  ? 159  SER A OG    1 
ATOM   1164 N  N     . SER A 1 159 ? -10.808 9.818   13.043 1.00 17.75  ? 160  SER A N     1 
ATOM   1165 C  CA    . SER A 1 159 ? -12.259 9.791   13.173 1.00 18.28  ? 160  SER A CA    1 
ATOM   1166 C  C     . SER A 1 159 ? -12.705 9.583   14.619 1.00 21.75  ? 160  SER A C     1 
ATOM   1167 O  O     . SER A 1 159 ? -13.879 9.878   14.936 1.00 23.87  ? 160  SER A O     1 
ATOM   1168 C  CB    . SER A 1 159 ? -12.884 8.742   12.289 1.00 21.73  ? 160  SER A CB    1 
ATOM   1169 O  OG    . SER A 1 159 ? -12.689 7.432   12.739 1.00 27.43  ? 160  SER A OG    1 
ATOM   1170 N  N     . TYR A 1 160 ? -11.788 9.162   15.489 1.00 18.60  ? 161  TYR A N     1 
ATOM   1171 C  CA    . TYR A 1 160 ? -12.022 9.039   16.935 1.00 20.00  ? 161  TYR A CA    1 
ATOM   1172 C  C     . TYR A 1 160 ? -11.285 10.126  17.717 1.00 21.32  ? 161  TYR A C     1 
ATOM   1173 O  O     . TYR A 1 160 ? -11.019 9.957   18.914 1.00 24.82  ? 161  TYR A O     1 
ATOM   1174 C  CB    . TYR A 1 160 ? -11.632 7.625   17.404 1.00 19.14  ? 161  TYR A CB    1 
ATOM   1175 C  CG    . TYR A 1 160 ? -12.569 6.619   16.808 1.00 20.28  ? 161  TYR A CG    1 
ATOM   1176 C  CD1   . TYR A 1 160 ? -13.865 6.469   17.336 1.00 25.40  ? 161  TYR A CD1   1 
ATOM   1177 C  CD2   . TYR A 1 160 ? -12.235 5.883   15.694 1.00 23.22  ? 161  TYR A CD2   1 
ATOM   1178 C  CE1   . TYR A 1 160 ? -14.752 5.619   16.776 1.00 25.53  ? 161  TYR A CE1   1 
ATOM   1179 C  CE2   . TYR A 1 160 ? -13.137 5.007   15.137 1.00 28.66  ? 161  TYR A CE2   1 
ATOM   1180 C  CZ    . TYR A 1 160 ? -14.407 4.899   15.680 1.00 35.26  ? 161  TYR A CZ    1 
ATOM   1181 O  OH    . TYR A 1 160 ? -15.343 4.057   15.123 1.00 37.46  ? 161  TYR A OH    1 
ATOM   1182 N  N     . ASP A 1 161 ? -10.923 11.222  17.058 1.00 20.64  ? 162  ASP A N     1 
ATOM   1183 C  CA    . ASP A 1 161 ? -10.283 12.419  17.602 1.00 21.51  ? 162  ASP A CA    1 
ATOM   1184 C  C     . ASP A 1 161 ? -8.892  12.169  18.171 1.00 24.96  ? 162  ASP A C     1 
ATOM   1185 O  O     . ASP A 1 161 ? -8.416  12.922  19.053 1.00 28.32  ? 162  ASP A O     1 
ATOM   1186 C  CB    . ASP A 1 161 ? -11.165 13.095  18.665 1.00 30.24  ? 162  ASP A CB    1 
ATOM   1187 C  CG    . ASP A 1 161 ? -12.459 13.608  18.077 1.00 52.36  ? 162  ASP A CG    1 
ATOM   1188 O  OD1   . ASP A 1 161 ? -12.450 14.015  16.893 1.00 52.58  ? 162  ASP A OD1   1 
ATOM   1189 O  OD2   . ASP A 1 161 ? -13.491 13.562  18.785 1.00 62.67  ? 162  ASP A OD2   1 
ATOM   1190 N  N     . PHE A 1 162 ? -8.202  11.116  17.731 1.00 20.55  ? 163  PHE A N     1 
ATOM   1191 C  CA    . PHE A 1 162 ? -6.770  11.051  17.932 1.00 19.51  ? 163  PHE A CA    1 
ATOM   1192 C  C     . PHE A 1 162 ? -6.097  11.816  16.813 1.00 19.27  ? 163  PHE A C     1 
ATOM   1193 O  O     . PHE A 1 162 ? -6.697  12.021  15.749 1.00 23.85  ? 163  PHE A O     1 
ATOM   1194 C  CB    . PHE A 1 162 ? -6.289  9.587   17.950 1.00 18.48  ? 163  PHE A CB    1 
ATOM   1195 C  CG    . PHE A 1 162 ? -6.608  8.831   19.233 1.00 17.33  ? 163  PHE A CG    1 
ATOM   1196 C  CD1   . PHE A 1 162 ? -5.856  9.097   20.382 1.00 17.88  ? 163  PHE A CD1   1 
ATOM   1197 C  CD2   . PHE A 1 162 ? -7.596  7.868   19.293 1.00 17.74  ? 163  PHE A CD2   1 
ATOM   1198 C  CE1   . PHE A 1 162 ? -6.096  8.408   21.557 1.00 17.16  ? 163  PHE A CE1   1 
ATOM   1199 C  CE2   . PHE A 1 162 ? -7.827  7.180   20.498 1.00 18.90  ? 163  PHE A CE2   1 
ATOM   1200 C  CZ    . PHE A 1 162 ? -7.077  7.480   21.604 1.00 18.21  ? 163  PHE A CZ    1 
ATOM   1201 N  N     . PRO A 1 163 ? -4.865  12.267  17.005 1.00 21.04  ? 164  PRO A N     1 
ATOM   1202 C  CA    . PRO A 1 163 ? -4.203  13.107  15.986 1.00 23.51  ? 164  PRO A CA    1 
ATOM   1203 C  C     . PRO A 1 163 ? -3.563  12.184  14.963 1.00 21.50  ? 164  PRO A C     1 
ATOM   1204 O  O     . PRO A 1 163 ? -2.388  11.827  15.045 1.00 20.09  ? 164  PRO A O     1 
ATOM   1205 C  CB    . PRO A 1 163 ? -3.151  13.869  16.793 1.00 22.58  ? 164  PRO A CB    1 
ATOM   1206 C  CG    . PRO A 1 163 ? -2.837  12.940  17.934 1.00 24.97  ? 164  PRO A CG    1 
ATOM   1207 C  CD    . PRO A 1 163 ? -4.090  12.200  18.279 1.00 22.11  ? 164  PRO A CD    1 
ATOM   1208 N  N     . GLY A 1 164 ? -4.372  11.743  13.996 1.00 21.94  ? 165  GLY A N     1 
ATOM   1209 C  CA    . GLY A 1 164 ? -3.916  10.775  13.016 1.00 22.46  ? 165  GLY A CA    1 
ATOM   1210 C  C     . GLY A 1 164 ? -2.754  11.240  12.176 1.00 20.61  ? 165  GLY A C     1 
ATOM   1211 O  O     . GLY A 1 164 ? -2.080  10.383  11.577 1.00 23.73  ? 165  GLY A O     1 
ATOM   1212 N  N     . ASP A 1 165 ? -2.540  12.544  12.076 1.00 21.16  ? 166  ASP A N     1 
ATOM   1213 C  CA    . ASP A 1 165 ? -1.395  13.080  11.361 1.00 27.52  ? 166  ASP A CA    1 
ATOM   1214 C  C     . ASP A 1 165 ? -0.090  12.937  12.140 1.00 25.04  ? 166  ASP A C     1 
ATOM   1215 O  O     . ASP A 1 165 ? 0.983   12.883  11.524 1.00 27.73  ? 166  ASP A O     1 
ATOM   1216 C  CB    . ASP A 1 165 ? -1.657  14.556  11.039 1.00 42.24  ? 166  ASP A CB    1 
ATOM   1217 C  CG    . ASP A 1 165 ? -2.171  15.361  12.265 1.00 72.05  ? 166  ASP A CG    1 
ATOM   1218 O  OD1   . ASP A 1 165 ? -2.568  14.757  13.294 1.00 74.02  ? 166  ASP A OD1   1 
ATOM   1219 O  OD2   . ASP A 1 165 ? -2.156  16.615  12.204 1.00 80.14  ? 166  ASP A OD2   1 
ATOM   1220 N  N     . ASP A 1 166 ? -0.157  12.884  13.473 1.00 20.86  ? 167  ASP A N     1 
ATOM   1221 C  CA    . ASP A 1 166 ? 1.057   12.946  14.300 1.00 19.78  ? 167  ASP A CA    1 
ATOM   1222 C  C     . ASP A 1 166 ? 1.430   11.591  14.892 1.00 20.86  ? 167  ASP A C     1 
ATOM   1223 O  O     . ASP A 1 166 ? 2.556   11.414  15.374 1.00 22.04  ? 167  ASP A O     1 
ATOM   1224 C  CB    . ASP A 1 166 ? 0.847   13.940  15.440 1.00 25.43  ? 167  ASP A CB    1 
ATOM   1225 C  CG    . ASP A 1 166 ? 0.572   15.355  14.948 1.00 35.78  ? 167  ASP A CG    1 
ATOM   1226 O  OD1   . ASP A 1 166 ? 1.130   15.749  13.906 1.00 38.36  ? 167  ASP A OD1   1 
ATOM   1227 O  OD2   . ASP A 1 166 ? -0.237  16.045  15.598 1.00 47.05  ? 167  ASP A OD2   1 
ATOM   1228 N  N     . ILE A 1 167 ? 0.532   10.630  14.832 1.00 17.52  ? 168  ILE A N     1 
ATOM   1229 C  CA    . ILE A 1 167 ? 0.790   9.336   15.457 1.00 17.66  ? 168  ILE A CA    1 
ATOM   1230 C  C     . ILE A 1 167 ? 1.880   8.575   14.698 1.00 18.73  ? 168  ILE A C     1 
ATOM   1231 O  O     . ILE A 1 167 ? 1.816   8.436   13.477 1.00 18.54  ? 168  ILE A O     1 
ATOM   1232 C  CB    . ILE A 1 167 ? -0.502  8.555   15.546 1.00 16.98  ? 168  ILE A CB    1 
ATOM   1233 C  CG1   . ILE A 1 167 ? -1.307  9.114   16.769 1.00 16.59  ? 168  ILE A CG1   1 
ATOM   1234 C  CG2   . ILE A 1 167 ? -0.276  7.006   15.668 1.00 15.90  ? 168  ILE A CG2   1 
ATOM   1235 C  CD1   . ILE A 1 167 ? -2.761  8.647   16.794 1.00 19.84  ? 168  ILE A CD1   1 
ATOM   1236 N  N     . PRO A 1 168 ? 2.908   8.075   15.367 1.00 15.52  ? 169  PRO A N     1 
ATOM   1237 C  CA    . PRO A 1 168 ? 3.938   7.303   14.678 1.00 17.11  ? 169  PRO A CA    1 
ATOM   1238 C  C     . PRO A 1 168 ? 3.391   5.972   14.255 1.00 15.74  ? 169  PRO A C     1 
ATOM   1239 O  O     . PRO A 1 168 ? 2.677   5.315   15.009 1.00 14.95  ? 169  PRO A O     1 
ATOM   1240 C  CB    . PRO A 1 168 ? 5.028   7.090   15.726 1.00 19.12  ? 169  PRO A CB    1 
ATOM   1241 C  CG    . PRO A 1 168 ? 4.708   8.046   16.816 1.00 20.16  ? 169  PRO A CG    1 
ATOM   1242 C  CD    . PRO A 1 168 ? 3.218   8.292   16.797 1.00 18.58  ? 169  PRO A CD    1 
ATOM   1243 N  N     . ILE A 1 169 ? 3.693   5.578   13.017 1.00 15.65  ? 170  ILE A N     1 
ATOM   1244 C  CA    . ILE A 1 169 ? 3.330   4.281   12.487 1.00 15.21  ? 170  ILE A CA    1 
ATOM   1245 C  C     . ILE A 1 169 ? 4.617   3.610   12.026 1.00 15.79  ? 170  ILE A C     1 
ATOM   1246 O  O     . ILE A 1 169 ? 5.313   4.104   11.120 1.00 18.40  ? 170  ILE A O     1 
ATOM   1247 C  CB    . ILE A 1 169 ? 2.322   4.390   11.317 1.00 18.87  ? 170  ILE A CB    1 
ATOM   1248 C  CG1   . ILE A 1 169 ? 1.087   5.065   11.866 1.00 20.84  ? 170  ILE A CG1   1 
ATOM   1249 C  CG2   . ILE A 1 169 ? 1.966   2.984   10.802 1.00 18.54  ? 170  ILE A CG2   1 
ATOM   1250 C  CD1   . ILE A 1 169 ? -0.046  5.212   10.838 1.00 24.62  ? 170  ILE A CD1   1 
ATOM   1251 N  N     . VAL A 1 170 ? 4.946   2.473   12.614 1.00 14.10  ? 171  VAL A N     1 
ATOM   1252 C  CA    . VAL A 1 170 ? 6.135   1.704   12.288 1.00 14.26  ? 171  VAL A CA    1 
ATOM   1253 C  C     . VAL A 1 170 ? 5.673   0.391   11.664 1.00 14.49  ? 171  VAL A C     1 
ATOM   1254 O  O     . VAL A 1 170 ? 4.897   -0.344  12.300 1.00 15.31  ? 171  VAL A O     1 
ATOM   1255 C  CB    . VAL A 1 170 ? 6.981   1.463   13.557 1.00 15.76  ? 171  VAL A CB    1 
ATOM   1256 C  CG1   . VAL A 1 170 ? 8.190   0.565   13.166 1.00 16.60  ? 171  VAL A CG1   1 
ATOM   1257 C  CG2   . VAL A 1 170 ? 7.441   2.772   14.144 1.00 18.08  ? 171  VAL A CG2   1 
ATOM   1258 N  N     . ALA A 1 171 ? 6.125   0.070   10.447 1.00 15.08  ? 172  ALA A N     1 
ATOM   1259 C  CA    . ALA A 1 171 ? 5.780   -1.189  9.822  1.00 14.33  ? 172  ALA A CA    1 
ATOM   1260 C  C     . ALA A 1 171 ? 6.882   -2.227  10.059 1.00 16.35  ? 172  ALA A C     1 
ATOM   1261 O  O     . ALA A 1 171 ? 8.075   -1.904  10.125 1.00 18.23  ? 172  ALA A O     1 
ATOM   1262 C  CB    . ALA A 1 171 ? 5.617   -0.970  8.296  1.00 16.51  ? 172  ALA A CB    1 
ATOM   1263 N  N     . GLY A 1 172 ? 6.461   -3.480  10.204 1.00 15.04  ? 173  GLY A N     1 
ATOM   1264 C  CA    . GLY A 1 172 ? 7.442   -4.544  10.368 1.00 14.26  ? 173  GLY A CA    1 
ATOM   1265 C  C     . GLY A 1 172 ? 6.785   -5.883  10.526 1.00 14.07  ? 173  GLY A C     1 
ATOM   1266 O  O     . GLY A 1 172 ? 5.623   -6.057  10.179 1.00 13.95  ? 173  GLY A O     1 
ATOM   1267 N  N     . SER A 1 173 ? 7.571   -6.854  11.021 1.00 14.10  ? 174  SER A N     1 
ATOM   1268 C  CA    . SER A 1 173 ? 7.077   -8.203  11.253 1.00 13.98  ? 174  SER A CA    1 
ATOM   1269 C  C     . SER A 1 173 ? 7.522   -8.678  12.624 1.00 13.90  ? 174  SER A C     1 
ATOM   1270 O  O     . SER A 1 173 ? 8.729   -8.897  12.847 1.00 14.20  ? 174  SER A O     1 
ATOM   1271 C  CB    . SER A 1 173 ? 7.609   -9.175  10.199 1.00 14.19  ? 174  SER A CB    1 
ATOM   1272 O  OG    . SER A 1 173 ? 7.218   -10.497 10.556 1.00 14.68  ? 174  SER A OG    1 
ATOM   1273 N  N     . ALA A 1 174 ? 6.570   -8.851  13.526 1.00 13.68  ? 175  ALA A N     1 
ATOM   1274 C  CA    . ALA A 1 174 ? 6.932   -9.359  14.844 1.00 13.64  ? 175  ALA A CA    1 
ATOM   1275 C  C     . ALA A 1 174 ? 7.474   -10.770 14.719 1.00 14.87  ? 175  ALA A C     1 
ATOM   1276 O  O     . ALA A 1 174 ? 8.450   -11.130 15.401 1.00 13.92  ? 175  ALA A O     1 
ATOM   1277 C  CB    . ALA A 1 174 ? 5.686   -9.336  15.725 1.00 16.65  ? 175  ALA A CB    1 
ATOM   1278 N  N     . LEU A 1 175 ? 6.905   -11.564 13.804 1.00 13.80  ? 176  LEU A N     1 
ATOM   1279 C  CA    . LEU A 1 175 ? 7.344   -12.962 13.674 1.00 13.96  ? 176  LEU A CA    1 
ATOM   1280 C  C     . LEU A 1 175 ? 8.735   -13.066 13.069 1.00 14.63  ? 176  LEU A C     1 
ATOM   1281 O  O     . LEU A 1 175 ? 9.591   -13.813 13.583 1.00 14.42  ? 176  LEU A O     1 
ATOM   1282 C  CB    . LEU A 1 175 ? 6.300   -13.746 12.892 1.00 13.93  ? 176  LEU A CB    1 
ATOM   1283 C  CG    . LEU A 1 175 ? 6.694   -15.239 12.708 1.00 14.71  ? 176  LEU A CG    1 
ATOM   1284 C  CD1   . LEU A 1 175 ? 6.746   -15.932 14.099 1.00 17.71  ? 176  LEU A CD1   1 
ATOM   1285 C  CD2   . LEU A 1 175 ? 5.614   -15.890 11.820 1.00 17.64  ? 176  LEU A CD2   1 
ATOM   1286 N  N     . GLN A 1 176 ? 9.032   -12.241 12.086 1.00 14.29  ? 177  GLN A N     1 
ATOM   1287 C  CA    . GLN A 1 176 ? 10.373  -12.287 11.523 1.00 14.58  ? 177  GLN A CA    1 
ATOM   1288 C  C     . GLN A 1 176 ? 11.412  -11.753 12.483 1.00 14.69  ? 177  GLN A C     1 
ATOM   1289 O  O     . GLN A 1 176 ? 12.535  -12.266 12.474 1.00 16.35  ? 177  GLN A O     1 
ATOM   1290 C  CB    . GLN A 1 176 ? 10.506  -11.474 10.196 1.00 15.57  ? 177  GLN A CB    1 
ATOM   1291 C  CG    . GLN A 1 176 ? 9.616   -12.053 9.065  1.00 15.99  ? 177  GLN A CG    1 
ATOM   1292 C  CD    . GLN A 1 176 ? 10.024  -13.461 8.722  1.00 24.65  ? 177  GLN A CD    1 
ATOM   1293 O  OE1   . GLN A 1 176 ? 11.204  -13.760 8.668  1.00 33.87  ? 177  GLN A OE1   1 
ATOM   1294 N  NE2   . GLN A 1 176 ? 9.046   -14.317 8.495  1.00 35.79  ? 177  GLN A NE2   1 
ATOM   1295 N  N     . ALA A 1 177 ? 11.071  -10.755 13.314 1.00 14.53  ? 178  ALA A N     1 
ATOM   1296 C  CA    . ALA A 1 177 ? 12.047  -10.330 14.319 1.00 14.66  ? 178  ALA A CA    1 
ATOM   1297 C  C     . ALA A 1 177 ? 12.314  -11.421 15.334 1.00 14.71  ? 178  ALA A C     1 
ATOM   1298 O  O     . ALA A 1 177 ? 13.469  -11.631 15.712 1.00 15.48  ? 178  ALA A O     1 
ATOM   1299 C  CB    . ALA A 1 177 ? 11.509  -9.093  15.041 1.00 16.61  ? 178  ALA A CB    1 
ATOM   1300 N  N     . LEU A 1 178 ? 11.285  -12.102 15.840 1.00 14.50  ? 179  LEU A N     1 
ATOM   1301 C  CA    . LEU A 1 178 ? 11.533  -13.229 16.746 1.00 15.35  ? 179  LEU A CA    1 
ATOM   1302 C  C     . LEU A 1 178 ? 12.378  -14.326 16.092 1.00 16.29  ? 179  LEU A C     1 
ATOM   1303 O  O     . LEU A 1 178 ? 13.343  -14.813 16.686 1.00 18.53  ? 179  LEU A O     1 
ATOM   1304 C  CB    . LEU A 1 178 ? 10.179  -13.771 17.209 1.00 18.68  ? 179  LEU A CB    1 
ATOM   1305 C  CG    . LEU A 1 178 ? 9.899   -14.593 18.422 1.00 33.50  ? 179  LEU A CG    1 
ATOM   1306 C  CD1   . LEU A 1 178 ? 10.264  -13.630 19.603 1.00 25.68  ? 179  LEU A CD1   1 
ATOM   1307 C  CD2   . LEU A 1 178 ? 8.400   -14.814 18.396 1.00 34.87  ? 179  LEU A CD2   1 
ATOM   1308 N  N     . GLU A 1 179 ? 12.077  -14.685 14.846 1.00 15.48  ? 180  GLU A N     1 
ATOM   1309 C  CA    . GLU A 1 179 ? 12.868  -15.710 14.178 1.00 15.86  ? 180  GLU A CA    1 
ATOM   1310 C  C     . GLU A 1 179 ? 14.300  -15.223 13.973 1.00 17.34  ? 180  GLU A C     1 
ATOM   1311 O  O     . GLU A 1 179 ? 15.250  -16.027 13.975 1.00 18.84  ? 180  GLU A O     1 
ATOM   1312 C  CB    . GLU A 1 179 ? 12.176  -16.091 12.855 1.00 18.32  ? 180  GLU A CB    1 
ATOM   1313 C  CG    . GLU A 1 179 ? 10.877  -16.860 13.122 1.00 20.46  ? 180  GLU A CG    1 
ATOM   1314 C  CD    . GLU A 1 179 ? 10.056  -17.117 11.913 1.00 25.61  ? 180  GLU A CD    1 
ATOM   1315 O  OE1   . GLU A 1 179 ? 10.375  -16.582 10.837 1.00 24.00  ? 180  GLU A OE1   1 
ATOM   1316 O  OE2   . GLU A 1 179 ? 9.085   -17.890 12.087 1.00 23.61  ? 180  GLU A OE2   1 
ATOM   1317 N  N     . ALA A 1 180 ? 14.483  -13.928 13.679 1.00 16.08  ? 181  ALA A N     1 
ATOM   1318 C  CA    . ALA A 1 180 ? 15.842  -13.427 13.484 1.00 17.22  ? 181  ALA A CA    1 
ATOM   1319 C  C     . ALA A 1 180 ? 16.668  -13.598 14.740 1.00 16.56  ? 181  ALA A C     1 
ATOM   1320 O  O     . ALA A 1 180 ? 17.836  -14.008 14.673 1.00 17.92  ? 181  ALA A O     1 
ATOM   1321 C  CB    . ALA A 1 180 ? 15.818  -11.946 13.094 1.00 17.91  ? 181  ALA A CB    1 
ATOM   1322 N  N     . ILE A 1 181 ? 16.090  -13.242 15.901 1.00 16.62  ? 182  ILE A N     1 
ATOM   1323 C  CA    . ILE A 1 181 ? 16.841  -13.416 17.151 1.00 17.91  ? 182  ILE A CA    1 
ATOM   1324 C  C     . ILE A 1 181 ? 17.126  -14.898 17.391 1.00 20.86  ? 182  ILE A C     1 
ATOM   1325 O  O     . ILE A 1 181 ? 18.237  -15.282 17.799 1.00 19.92  ? 182  ILE A O     1 
ATOM   1326 C  CB    . ILE A 1 181 ? 16.069  -12.770 18.315 1.00 19.02  ? 182  ILE A CB    1 
ATOM   1327 C  CG1   . ILE A 1 181 ? 15.916  -11.256 18.135 1.00 19.97  ? 182  ILE A CG1   1 
ATOM   1328 C  CG2   . ILE A 1 181 ? 16.800  -13.097 19.665 1.00 20.88  ? 182  ILE A CG2   1 
ATOM   1329 C  CD1   . ILE A 1 181 ? 17.232  -10.457 18.276 1.00 22.31  ? 182  ILE A CD1   1 
ATOM   1330 N  N     . GLN A 1 182 ? 16.155  -15.761 17.143 1.00 19.21  ? 183  GLN A N     1 
ATOM   1331 C  CA    . GLN A 1 182 ? 16.368  -17.200 17.310 1.00 18.20  ? 183  GLN A CA    1 
ATOM   1332 C  C     . GLN A 1 182 ? 17.488  -17.718 16.414 1.00 19.11  ? 183  GLN A C     1 
ATOM   1333 O  O     . GLN A 1 182 ? 18.269  -18.600 16.833 1.00 24.26  ? 183  GLN A O     1 
ATOM   1334 C  CB    . GLN A 1 182 ? 15.007  -17.875 17.046 1.00 20.86  ? 183  GLN A CB    1 
ATOM   1335 C  CG    . GLN A 1 182 ? 14.021  -17.497 18.239 1.00 27.64  ? 183  GLN A CG    1 
ATOM   1336 C  CD    . GLN A 1 182 ? 12.553  -17.936 17.992 1.00 33.29  ? 183  GLN A CD    1 
ATOM   1337 O  OE1   . GLN A 1 182 ? 12.143  -18.188 16.865 1.00 32.15  ? 183  GLN A OE1   1 
ATOM   1338 N  NE2   . GLN A 1 182 ? 11.789  -18.074 19.068 1.00 32.30  ? 183  GLN A NE2   1 
ATOM   1339 N  N     . GLY A 1 183 ? 17.674  -17.121 15.233 1.00 18.47  ? 184  GLY A N     1 
ATOM   1340 C  CA    . GLY A 1 183 ? 18.711  -17.488 14.291 1.00 18.13  ? 184  GLY A CA    1 
ATOM   1341 C  C     . GLY A 1 183 ? 20.052  -16.827 14.519 1.00 20.78  ? 184  GLY A C     1 
ATOM   1342 O  O     . GLY A 1 183 ? 20.979  -17.031 13.727 1.00 25.92  ? 184  GLY A O     1 
ATOM   1343 N  N     . GLY A 1 184 ? 20.171  -16.026 15.581 1.00 19.61  ? 185  GLY A N     1 
ATOM   1344 C  CA    . GLY A 1 184 ? 21.452  -15.461 15.971 1.00 24.17  ? 185  GLY A CA    1 
ATOM   1345 C  C     . GLY A 1 184 ? 21.585  -13.947 15.879 1.00 22.70  ? 185  GLY A C     1 
ATOM   1346 O  O     . GLY A 1 184 ? 22.706  -13.443 16.048 1.00 22.95  ? 185  GLY A O     1 
ATOM   1347 N  N     . ALA A 1 185 ? 20.502  -13.212 15.561 1.00 20.94  ? 186  ALA A N     1 
ATOM   1348 C  CA    . ALA A 1 185 ? 20.626  -11.755 15.448 1.00 18.74  ? 186  ALA A CA    1 
ATOM   1349 C  C     . ALA A 1 185 ? 21.040  -11.164 16.795 1.00 20.29  ? 186  ALA A C     1 
ATOM   1350 O  O     . ALA A 1 185 ? 20.696  -11.682 17.857 1.00 21.65  ? 186  ALA A O     1 
ATOM   1351 C  CB    . ALA A 1 185 ? 19.296  -11.141 14.973 1.00 20.17  ? 186  ALA A CB    1 
ATOM   1352 N  N     . SER A 1 186 ? 21.828  -10.086 16.730 1.00 20.23  ? 187  SER A N     1 
ATOM   1353 C  CA    . SER A 1 186 ? 22.498  -9.601  17.933 1.00 19.36  ? 187  SER A CA    1 
ATOM   1354 C  C     . SER A 1 186 ? 21.643  -8.705  18.804 1.00 20.47  ? 187  SER A C     1 
ATOM   1355 O  O     . SER A 1 186 ? 21.941  -8.561  20.009 1.00 22.55  ? 187  SER A O     1 
ATOM   1356 C  CB    . SER A 1 186 ? 23.754  -8.837  17.554 1.00 21.71  ? 187  SER A CB    1 
ATOM   1357 O  OG    . SER A 1 186 ? 23.428  -7.653  16.842 1.00 23.28  ? 187  SER A OG    1 
ATOM   1358 N  N     . GLY A 1 187 ? 20.602  -8.072  18.228 1.00 18.80  ? 188  GLY A N     1 
ATOM   1359 C  CA    . GLY A 1 187 ? 19.860  -7.053  18.952 1.00 17.65  ? 188  GLY A CA    1 
ATOM   1360 C  C     . GLY A 1 187 ? 20.437  -5.662  18.825 1.00 19.27  ? 188  GLY A C     1 
ATOM   1361 O  O     . GLY A 1 187 ? 19.867  -4.721  19.410 1.00 21.10  ? 188  GLY A O     1 
ATOM   1362 N  N     . GLN A 1 188 ? 21.573  -5.516  18.162 1.00 20.73  ? 189  GLN A N     1 
ATOM   1363 C  CA    . GLN A 1 188 ? 22.160  -4.210  17.919 1.00 20.76  ? 189  GLN A CA    1 
ATOM   1364 C  C     . GLN A 1 188 ? 21.568  -3.592  16.677 1.00 21.32  ? 189  GLN A C     1 
ATOM   1365 O  O     . GLN A 1 188 ? 21.300  -4.302  15.701 1.00 20.27  ? 189  GLN A O     1 
ATOM   1366 C  CB    . GLN A 1 188 ? 23.676  -4.360  17.746 1.00 23.37  ? 189  GLN A CB    1 
ATOM   1367 C  CG    . GLN A 1 188 ? 24.461  -4.711  18.981 1.00 27.51  ? 189  GLN A CG    1 
ATOM   1368 C  CD    . GLN A 1 188 ? 24.855  -3.413  19.727 1.00 49.50  ? 189  GLN A CD    1 
ATOM   1369 O  OE1   . GLN A 1 188 ? 24.320  -3.088  20.769 1.00 61.98  ? 189  GLN A OE1   1 
ATOM   1370 N  NE2   . GLN A 1 188 ? 25.768  -2.653  19.134 1.00 65.48  ? 189  GLN A NE2   1 
ATOM   1371 N  N     . LYS A 1 189 ? 21.385  -2.270  16.685 1.00 21.29  ? 190  LYS A N     1 
ATOM   1372 C  CA    . LYS A 1 189 ? 20.835  -1.603  15.514 1.00 20.37  ? 190  LYS A CA    1 
ATOM   1373 C  C     . LYS A 1 189 ? 21.751  -1.791  14.326 1.00 22.67  ? 190  LYS A C     1 
ATOM   1374 O  O     . LYS A 1 189 ? 22.967  -1.590  14.421 1.00 24.64  ? 190  LYS A O     1 
ATOM   1375 C  CB    . LYS A 1 189 ? 20.644  -0.096  15.784 1.00 24.74  ? 190  LYS A CB    1 
ATOM   1376 C  CG    . LYS A 1 189 ? 19.896  0.618   14.658 1.00 29.21  ? 190  LYS A CG    1 
ATOM   1377 C  CD    . LYS A 1 189 ? 19.685  2.098   14.901 1.00 39.16  ? 190  LYS A CD    1 
ATOM   1378 C  CE    . LYS A 1 189 ? 18.528  2.340   15.867 1.00 47.67  ? 190  LYS A CE    1 
ATOM   1379 N  NZ    . LYS A 1 189 ? 18.342  3.804   16.086 1.00 47.85  ? 190  LYS A NZ    1 
ATOM   1380 N  N     . GLY A 1 190 ? 21.154  -2.124  13.186 1.00 22.33  ? 191  GLY A N     1 
ATOM   1381 C  CA    . GLY A 1 190 ? 21.889  -2.334  11.967 1.00 21.94  ? 191  GLY A CA    1 
ATOM   1382 C  C     . GLY A 1 190 ? 22.238  -3.773  11.694 1.00 23.35  ? 191  GLY A C     1 
ATOM   1383 O  O     . GLY A 1 190 ? 22.624  -4.101  10.568 1.00 28.70  ? 191  GLY A O     1 
ATOM   1384 N  N     . ASP A 1 191 ? 22.129  -4.647  12.685 1.00 21.63  ? 192  ASP A N     1 
ATOM   1385 C  CA    . ASP A 1 191 ? 22.489  -6.049  12.470 1.00 20.07  ? 192  ASP A CA    1 
ATOM   1386 C  C     . ASP A 1 191 ? 21.436  -6.815  11.662 1.00 20.29  ? 192  ASP A C     1 
ATOM   1387 O  O     . ASP A 1 191 ? 21.782  -7.728  10.899 1.00 23.83  ? 192  ASP A O     1 
ATOM   1388 C  CB    . ASP A 1 191 ? 22.713  -6.698  13.835 1.00 22.44  ? 192  ASP A CB    1 
ATOM   1389 C  CG    . ASP A 1 191 ? 22.888  -8.206  13.765 1.00 24.99  ? 192  ASP A CG    1 
ATOM   1390 O  OD1   . ASP A 1 191 ? 24.016  -8.661  13.422 1.00 28.56  ? 192  ASP A OD1   1 
ATOM   1391 O  OD2   . ASP A 1 191 ? 21.924  -8.951  14.093 1.00 23.15  ? 192  ASP A OD2   1 
ATOM   1392 N  N     . ASN A 1 192 ? 20.149  -6.496  11.822 1.00 20.39  ? 193  ASN A N     1 
ATOM   1393 C  CA    . ASN A 1 192 ? 19.081  -7.228  11.145 1.00 18.44  ? 193  ASN A CA    1 
ATOM   1394 C  C     . ASN A 1 192 ? 17.911  -6.291  10.909 1.00 18.77  ? 193  ASN A C     1 
ATOM   1395 O  O     . ASN A 1 192 ? 17.527  -5.548  11.839 1.00 17.82  ? 193  ASN A O     1 
ATOM   1396 C  CB    . ASN A 1 192 ? 18.679  -8.447  11.981 1.00 17.84  ? 193  ASN A CB    1 
ATOM   1397 C  CG    . ASN A 1 192 ? 17.469  -9.206  11.435 1.00 18.39  ? 193  ASN A CG    1 
ATOM   1398 O  OD1   . ASN A 1 192 ? 16.307  -8.782  11.512 1.00 19.42  ? 193  ASN A OD1   1 
ATOM   1399 N  ND2   . ASN A 1 192 ? 17.776  -10.263 10.703 1.00 21.51  ? 193  ASN A ND2   1 
ATOM   1400 N  N     . PRO A 1 193 ? 17.320  -6.285  9.716  1.00 18.08  ? 194  PRO A N     1 
ATOM   1401 C  CA    . PRO A 1 193 ? 16.333  -5.229  9.397  1.00 18.52  ? 194  PRO A CA    1 
ATOM   1402 C  C     . PRO A 1 193 ? 15.020  -5.425  10.108 1.00 17.12  ? 194  PRO A C     1 
ATOM   1403 O  O     . PRO A 1 193 ? 14.326  -4.442  10.435 1.00 18.89  ? 194  PRO A O     1 
ATOM   1404 C  CB    . PRO A 1 193 ? 16.153  -5.358  7.876  1.00 23.59  ? 194  PRO A CB    1 
ATOM   1405 C  CG    . PRO A 1 193 ? 16.597  -6.738  7.572  1.00 22.42  ? 194  PRO A CG    1 
ATOM   1406 C  CD    . PRO A 1 193 ? 17.722  -7.048  8.503  1.00 20.10  ? 194  PRO A CD    1 
ATOM   1407 N  N     . TRP A 1 194 ? 14.663  -6.664  10.409 1.00 16.83  ? 195  TRP A N     1 
ATOM   1408 C  CA    . TRP A 1 194 ? 13.439  -6.923  11.160 1.00 16.88  ? 195  TRP A CA    1 
ATOM   1409 C  C     . TRP A 1 194 ? 13.589  -6.557  12.629 1.00 15.19  ? 195  TRP A C     1 
ATOM   1410 O  O     . TRP A 1 194 ? 12.697  -5.931  13.229 1.00 16.81  ? 195  TRP A O     1 
ATOM   1411 C  CB    . TRP A 1 194 ? 13.040  -8.401  11.038 1.00 16.40  ? 195  TRP A CB    1 
ATOM   1412 C  CG    . TRP A 1 194 ? 12.754  -8.862  9.653  1.00 18.00  ? 195  TRP A CG    1 
ATOM   1413 C  CD1   . TRP A 1 194 ? 13.500  -9.746  8.904  1.00 19.25  ? 195  TRP A CD1   1 
ATOM   1414 C  CD2   . TRP A 1 194 ? 11.666  -8.442  8.819  1.00 16.40  ? 195  TRP A CD2   1 
ATOM   1415 N  NE1   . TRP A 1 194 ? 12.872  -9.944  7.671  1.00 20.95  ? 195  TRP A NE1   1 
ATOM   1416 C  CE2   . TRP A 1 194 ? 11.771  -9.130  7.608  1.00 17.21  ? 195  TRP A CE2   1 
ATOM   1417 C  CE3   . TRP A 1 194 ? 10.594  -7.544  9.006  1.00 17.75  ? 195  TRP A CE3   1 
ATOM   1418 C  CZ2   . TRP A 1 194 ? 10.806  -8.973  6.569  1.00 18.64  ? 195  TRP A CZ2   1 
ATOM   1419 C  CZ3   . TRP A 1 194 ? 9.677   -7.334  7.939  1.00 20.10  ? 195  TRP A CZ3   1 
ATOM   1420 C  CH2   . TRP A 1 194 ? 9.809   -8.060  6.759  1.00 20.16  ? 195  TRP A CH2   1 
ATOM   1421 N  N     . VAL A 1 195 ? 14.728  -6.879  13.232 1.00 15.43  ? 196  VAL A N     1 
ATOM   1422 C  CA    . VAL A 1 195 ? 14.983  -6.437  14.603 1.00 15.41  ? 196  VAL A CA    1 
ATOM   1423 C  C     . VAL A 1 195 ? 15.021  -4.915  14.659 1.00 16.60  ? 196  VAL A C     1 
ATOM   1424 O  O     . VAL A 1 195 ? 14.504  -4.308  15.611 1.00 15.84  ? 196  VAL A O     1 
ATOM   1425 C  CB    . VAL A 1 195 ? 16.298  -7.054  15.067 1.00 16.20  ? 196  VAL A CB    1 
ATOM   1426 C  CG1   . VAL A 1 195 ? 16.694  -6.463  16.420 1.00 16.41  ? 196  VAL A CG1   1 
ATOM   1427 C  CG2   . VAL A 1 195 ? 16.166  -8.552  15.112 1.00 18.76  ? 196  VAL A CG2   1 
ATOM   1428 N  N     . ASP A 1 196 ? 15.582  -4.267  13.614 1.00 16.70  ? 197  ASP A N     1 
ATOM   1429 C  CA    . ASP A 1 196 ? 15.639  -2.802  13.616 1.00 15.90  ? 197  ASP A CA    1 
ATOM   1430 C  C     . ASP A 1 196 ? 14.250  -2.187  13.678 1.00 15.86  ? 197  ASP A C     1 
ATOM   1431 O  O     . ASP A 1 196 ? 14.100  -1.114  14.258 1.00 17.71  ? 197  ASP A O     1 
ATOM   1432 C  CB    . ASP A 1 196 ? 16.338  -2.268  12.357 1.00 17.77  ? 197  ASP A CB    1 
ATOM   1433 C  CG    . ASP A 1 196 ? 17.830  -2.440  12.379 1.00 22.76  ? 197  ASP A CG    1 
ATOM   1434 O  OD1   . ASP A 1 196 ? 18.397  -2.766  13.426 1.00 21.54  ? 197  ASP A OD1   1 
ATOM   1435 O  OD2   . ASP A 1 196 ? 18.484  -2.181  11.293 1.00 25.41  ? 197  ASP A OD2   1 
ATOM   1436 N  N     . LYS A 1 197 ? 13.238  -2.841  13.095 1.00 15.26  ? 198  LYS A N     1 
ATOM   1437 C  CA    . LYS A 1 197 ? 11.881  -2.270  13.136 1.00 15.75  ? 198  LYS A CA    1 
ATOM   1438 C  C     . LYS A 1 197 ? 11.308  -2.374  14.536 1.00 14.79  ? 198  LYS A C     1 
ATOM   1439 O  O     . LYS A 1 197 ? 10.545  -1.492  14.934 1.00 15.04  ? 198  LYS A O     1 
ATOM   1440 C  CB    . LYS A 1 197 ? 11.006  -2.949  12.106 1.00 16.25  ? 198  LYS A CB    1 
ATOM   1441 C  CG    . LYS A 1 197 ? 11.500  -2.548  10.711 1.00 17.43  ? 198  LYS A CG    1 
ATOM   1442 C  CD    . LYS A 1 197 ? 10.988  -3.479  9.701  1.00 23.58  ? 198  LYS A CD    1 
ATOM   1443 C  CE    . LYS A 1 197 ? 11.600  -3.087  8.345  1.00 32.77  ? 198  LYS A CE    1 
ATOM   1444 N  NZ    . LYS A 1 197 ? 11.151  -3.959  7.251  1.00 37.70  ? 198  LYS A NZ    1 
ATOM   1445 N  N     . ILE A 1 198 ? 11.678  -3.400  15.311 1.00 14.60  ? 199  ILE A N     1 
ATOM   1446 C  CA    . ILE A 1 198 ? 11.251  -3.451  16.711 1.00 14.38  ? 199  ILE A CA    1 
ATOM   1447 C  C     . ILE A 1 198 ? 11.961  -2.374  17.520 1.00 15.25  ? 199  ILE A C     1 
ATOM   1448 O  O     . ILE A 1 198 ? 11.340  -1.723  18.401 1.00 15.55  ? 199  ILE A O     1 
ATOM   1449 C  CB    . ILE A 1 198 ? 11.558  -4.844  17.302 1.00 14.42  ? 199  ILE A CB    1 
ATOM   1450 C  CG1   . ILE A 1 198 ? 10.863  -5.949  16.505 1.00 15.57  ? 199  ILE A CG1   1 
ATOM   1451 C  CG2   . ILE A 1 198 ? 11.125  -4.883  18.796 1.00 16.13  ? 199  ILE A CG2   1 
ATOM   1452 C  CD1   . ILE A 1 198 ? 9.384   -5.844  16.398 1.00 17.46  ? 199  ILE A CD1   1 
ATOM   1453 N  N     . LEU A 1 199 ? 13.249  -2.169  17.244 1.00 14.93  ? 200  LEU A N     1 
ATOM   1454 C  CA    . LEU A 1 199 ? 13.956  -1.094  17.938 1.00 15.16  ? 200  LEU A CA    1 
ATOM   1455 C  C     . LEU A 1 199 ? 13.341  0.248   17.588 1.00 15.76  ? 200  LEU A C     1 
ATOM   1456 O  O     . LEU A 1 199 ? 13.216  1.132   18.447 1.00 15.10  ? 200  LEU A O     1 
ATOM   1457 C  CB    . LEU A 1 199 ? 15.434  -1.122  17.586 1.00 15.93  ? 200  LEU A CB    1 
ATOM   1458 C  CG    . LEU A 1 199 ? 16.196  -2.379  18.088 1.00 17.12  ? 200  LEU A CG    1 
ATOM   1459 C  CD1   . LEU A 1 199 ? 17.615  -2.422  17.529 1.00 19.31  ? 200  LEU A CD1   1 
ATOM   1460 C  CD2   . LEU A 1 199 ? 16.283  -2.365  19.608 1.00 19.19  ? 200  LEU A CD2   1 
ATOM   1461 N  N     . LYS A 1 200 ? 12.963  0.449   16.320 1.00 15.14  ? 201  LYS A N     1 
ATOM   1462 C  CA    . LYS A 1 200 ? 12.331  1.708   15.930 1.00 15.14  ? 201  LYS A CA    1 
ATOM   1463 C  C     . LYS A 1 200 ? 10.983  1.899   16.591 1.00 16.21  ? 201  LYS A C     1 
ATOM   1464 O  O     . LYS A 1 200 ? 10.678  3.000   17.056 1.00 16.43  ? 201  LYS A O     1 
ATOM   1465 C  CB    . LYS A 1 200 ? 12.174  1.731   14.406 1.00 16.85  ? 201  LYS A CB    1 
ATOM   1466 C  CG    . LYS A 1 200 ? 11.465  2.954   13.914 1.00 20.27  ? 201  LYS A CG    1 
ATOM   1467 C  CD    . LYS A 1 200 ? 12.296  4.256   14.037 1.00 22.72  ? 201  LYS A CD    1 
ATOM   1468 C  CE    . LYS A 1 200 ? 11.505  5.308   13.257 1.00 28.40  ? 201  LYS A CE    1 
ATOM   1469 N  NZ    . LYS A 1 200 ? 12.216  6.595   13.297 1.00 37.13  ? 201  LYS A NZ    1 
ATOM   1470 N  N     . LEU A 1 201 ? 10.178  0.817   16.695 1.00 14.41  ? 202  LEU A N     1 
ATOM   1471 C  CA    . LEU A 1 201 ? 8.929   0.899   17.436 1.00 14.06  ? 202  LEU A CA    1 
ATOM   1472 C  C     . LEU A 1 201 ? 9.167   1.404   18.858 1.00 14.03  ? 202  LEU A C     1 
ATOM   1473 O  O     . LEU A 1 201 ? 8.495   2.335   19.294 1.00 14.35  ? 202  LEU A O     1 
ATOM   1474 C  CB    . LEU A 1 201 ? 8.263   -0.482  17.479 1.00 14.81  ? 202  LEU A CB    1 
ATOM   1475 C  CG    . LEU A 1 201 ? 7.061   -0.535  18.437 1.00 15.18  ? 202  LEU A CG    1 
ATOM   1476 C  CD1   . LEU A 1 201 ? 5.896   0.392   17.985 1.00 15.76  ? 202  LEU A CD1   1 
ATOM   1477 C  CD2   . LEU A 1 201 ? 6.604   -1.988  18.498 1.00 17.15  ? 202  LEU A CD2   1 
ATOM   1478 N  N     . MET A 1 202 ? 10.186  0.876   19.527 1.00 14.18  ? 203  MET A N     1 
ATOM   1479 C  CA    . MET A 1 202 ? 10.389  1.280   20.922 1.00 15.16  ? 203  MET A CA    1 
ATOM   1480 C  C     . MET A 1 202 ? 10.983  2.676   21.062 1.00 16.08  ? 203  MET A C     1 
ATOM   1481 O  O     . MET A 1 202 ? 10.629  3.386   22.014 1.00 15.97  ? 203  MET A O     1 
ATOM   1482 C  CB    . MET A 1 202 ? 11.254  0.264   21.662 1.00 16.98  ? 203  MET A CB    1 
ATOM   1483 C  CG    . MET A 1 202 ? 10.521  -1.084  21.794 1.00 19.99  ? 203  MET A CG    1 
ATOM   1484 S  SD    . MET A 1 202 ? 8.756   -1.078  22.276 1.00 21.65  ? 203  MET A SD    1 
ATOM   1485 C  CE    . MET A 1 202 ? 8.871   -0.329  23.894 1.00 29.52  ? 203  MET A CE    1 
ATOM   1486 N  N     . GLU A 1 203 ? 11.731  3.135   20.061 1.00 16.18  ? 204  GLU A N     1 
ATOM   1487 C  CA    . GLU A 1 203 ? 12.139  4.546   19.999 1.00 15.81  ? 204  GLU A CA    1 
ATOM   1488 C  C     . GLU A 1 203 ? 10.925  5.453   19.891 1.00 16.19  ? 204  GLU A C     1 
ATOM   1489 O  O     . GLU A 1 203 ? 10.884  6.514   20.541 1.00 17.32  ? 204  GLU A O     1 
ATOM   1490 C  CB    . GLU A 1 203 ? 13.069  4.806   18.793 1.00 15.98  ? 204  GLU A CB    1 
ATOM   1491 C  CG    . GLU A 1 203 ? 14.423  4.092   18.983 1.00 20.97  ? 204  GLU A CG    1 
ATOM   1492 C  CD    . GLU A 1 203 ? 15.303  4.186   17.743 1.00 40.48  ? 204  GLU A CD    1 
ATOM   1493 O  OE1   . GLU A 1 203 ? 14.861  4.805   16.739 1.00 33.14  ? 204  GLU A OE1   1 
ATOM   1494 O  OE2   . GLU A 1 203 ? 16.418  3.609   17.765 1.00 39.79  ? 204  GLU A OE2   1 
ATOM   1495 N  N     . GLU A 1 204 ? 9.942   5.061   19.069 1.00 16.03  ? 205  GLU A N     1 
ATOM   1496 C  CA    . GLU A 1 204 ? 8.747   5.886   18.903 1.00 15.48  ? 205  GLU A CA    1 
ATOM   1497 C  C     . GLU A 1 204 ? 7.891   5.865   20.149 1.00 15.44  ? 205  GLU A C     1 
ATOM   1498 O  O     . GLU A 1 204 ? 7.316   6.900   20.513 1.00 16.86  ? 205  GLU A O     1 
ATOM   1499 C  CB    . GLU A 1 204 ? 7.941   5.423   17.702 1.00 15.64  ? 205  GLU A CB    1 
ATOM   1500 C  CG    . GLU A 1 204 ? 8.660   5.624   16.328 1.00 16.54  ? 205  GLU A CG    1 
ATOM   1501 C  CD    . GLU A 1 204 ? 8.856   7.076   15.979 1.00 25.97  ? 205  GLU A CD    1 
ATOM   1502 O  OE1   . GLU A 1 204 ? 8.272   7.977   16.607 1.00 24.43  ? 205  GLU A OE1   1 
ATOM   1503 O  OE2   . GLU A 1 204 ? 9.588   7.309   14.996 1.00 41.87  ? 205  GLU A OE2   1 
ATOM   1504 N  N     . VAL A 1 205 ? 7.725   4.690   20.776 1.00 15.18  ? 206  VAL A N     1 
ATOM   1505 C  CA    . VAL A 1 205 ? 7.034   4.604   22.067 1.00 14.06  ? 206  VAL A CA    1 
ATOM   1506 C  C     . VAL A 1 205 ? 7.701   5.496   23.110 1.00 14.96  ? 206  VAL A C     1 
ATOM   1507 O  O     . VAL A 1 205 ? 7.019   6.313   23.768 1.00 16.87  ? 206  VAL A O     1 
ATOM   1508 C  CB    . VAL A 1 205 ? 6.945   3.149   22.545 1.00 16.41  ? 206  VAL A CB    1 
ATOM   1509 C  CG1   . VAL A 1 205 ? 6.464   3.051   24.048 1.00 17.06  ? 206  VAL A CG1   1 
ATOM   1510 C  CG2   . VAL A 1 205 ? 6.031   2.322   21.579 1.00 17.82  ? 206  VAL A CG2   1 
ATOM   1511 N  N     . ASP A 1 206 ? 9.019   5.434   23.212 1.00 14.72  ? 207  ASP A N     1 
ATOM   1512 C  CA    . ASP A 1 206 ? 9.733   6.290   24.175 1.00 15.07  ? 207  ASP A CA    1 
ATOM   1513 C  C     . ASP A 1 206 ? 9.474   7.750   23.925 1.00 17.81  ? 207  ASP A C     1 
ATOM   1514 O  O     . ASP A 1 206 ? 9.297   8.530   24.886 1.00 20.47  ? 207  ASP A O     1 
ATOM   1515 C  CB    . ASP A 1 206 ? 11.257  6.092   24.088 1.00 16.99  ? 207  ASP A CB    1 
ATOM   1516 C  CG    . ASP A 1 206 ? 11.763  4.783   24.739 1.00 18.51  ? 207  ASP A CG    1 
ATOM   1517 O  OD1   . ASP A 1 206 ? 11.084  4.079   25.541 1.00 20.45  ? 207  ASP A OD1   1 
ATOM   1518 O  OD2   . ASP A 1 206 ? 12.942  4.493   24.496 1.00 18.94  ? 207  ASP A OD2   1 
ATOM   1519 N  N     . ALA A 1 207 ? 9.507   8.162   22.659 1.00 16.43  ? 208  ALA A N     1 
ATOM   1520 C  CA    . ALA A 1 207 ? 9.441   9.593   22.342 1.00 16.15  ? 208  ALA A CA    1 
ATOM   1521 C  C     . ALA A 1 207 ? 8.017   10.141  22.389 1.00 19.04  ? 208  ALA A C     1 
ATOM   1522 O  O     . ALA A 1 207 ? 7.851   11.336  22.692 1.00 23.87  ? 208  ALA A O     1 
ATOM   1523 C  CB    . ALA A 1 207 ? 10.041  9.854   20.970 1.00 19.05  ? 208  ALA A CB    1 
ATOM   1524 N  N     . TYR A 1 208 ? 7.010   9.352   22.014 1.00 16.34  ? 209  TYR A N     1 
ATOM   1525 C  CA    . TYR A 1 208 ? 5.682   9.880   21.724 1.00 16.67  ? 209  TYR A CA    1 
ATOM   1526 C  C     . TYR A 1 208 ? 4.699   9.650   22.855 1.00 17.94  ? 209  TYR A C     1 
ATOM   1527 O  O     . TYR A 1 208 ? 3.797   10.487  23.035 1.00 21.74  ? 209  TYR A O     1 
ATOM   1528 C  CB    . TYR A 1 208 ? 5.139   9.226   20.431 1.00 18.44  ? 209  TYR A CB    1 
ATOM   1529 C  CG    . TYR A 1 208 ? 3.805   9.818   19.983 1.00 16.15  ? 209  TYR A CG    1 
ATOM   1530 C  CD1   . TYR A 1 208 ? 3.767   11.114  19.482 1.00 18.49  ? 209  TYR A CD1   1 
ATOM   1531 C  CD2   . TYR A 1 208 ? 2.651   9.091   20.074 1.00 16.50  ? 209  TYR A CD2   1 
ATOM   1532 C  CE1   . TYR A 1 208 ? 2.530   11.694  19.117 1.00 20.29  ? 209  TYR A CE1   1 
ATOM   1533 C  CE2   . TYR A 1 208 ? 1.404   9.661   19.702 1.00 17.20  ? 209  TYR A CE2   1 
ATOM   1534 C  CZ    . TYR A 1 208 ? 1.390   10.944  19.238 1.00 20.33  ? 209  TYR A CZ    1 
ATOM   1535 O  OH    . TYR A 1 208 ? 0.165   11.526  18.871 1.00 20.98  ? 209  TYR A OH    1 
ATOM   1536 N  N     . ILE A 1 209 ? 4.800   8.550   23.594 1.00 16.81  ? 210  ILE A N     1 
ATOM   1537 C  CA    . ILE A 1 209 ? 3.902   8.320   24.732 1.00 18.01  ? 210  ILE A CA    1 
ATOM   1538 C  C     . ILE A 1 209 ? 4.461   9.062   25.952 1.00 18.92  ? 210  ILE A C     1 
ATOM   1539 O  O     . ILE A 1 209 ? 5.593   8.795   26.346 1.00 18.48  ? 210  ILE A O     1 
ATOM   1540 C  CB    . ILE A 1 209 ? 3.729   6.826   24.973 1.00 17.34  ? 210  ILE A CB    1 
ATOM   1541 C  CG1   . ILE A 1 209 ? 2.916   6.219   23.806 1.00 19.65  ? 210  ILE A CG1   1 
ATOM   1542 C  CG2   . ILE A 1 209 ? 3.013   6.520   26.302 1.00 18.47  ? 210  ILE A CG2   1 
ATOM   1543 C  CD1   . ILE A 1 209 ? 2.832   4.696   23.814 1.00 22.18  ? 210  ILE A CD1   1 
ATOM   1544 N  N     . PRO A 1 210 ? 3.753   10.045  26.525 1.00 19.36  ? 211  PRO A N     1 
ATOM   1545 C  CA    . PRO A 1 210 ? 4.299   10.790  27.680 1.00 18.74  ? 211  PRO A CA    1 
ATOM   1546 C  C     . PRO A 1 210 ? 4.343   9.945   28.926 1.00 17.00  ? 211  PRO A C     1 
ATOM   1547 O  O     . PRO A 1 210 ? 3.472   9.099   29.183 1.00 19.43  ? 211  PRO A O     1 
ATOM   1548 C  CB    . PRO A 1 210 ? 3.280   11.916  27.878 1.00 21.90  ? 211  PRO A CB    1 
ATOM   1549 C  CG    . PRO A 1 210 ? 2.504   11.967  26.571 1.00 24.52  ? 211  PRO A CG    1 
ATOM   1550 C  CD    . PRO A 1 210 ? 2.426   10.540  26.138 1.00 20.85  ? 211  PRO A CD    1 
ATOM   1551 N  N     . THR A 1 211 ? 5.374   10.212  29.733 1.00 20.22  ? 212  THR A N     1 
ATOM   1552 C  CA    . THR A 1 211 ? 5.412   9.630   31.074 1.00 20.68  ? 212  THR A CA    1 
ATOM   1553 C  C     . THR A 1 211 ? 4.299   10.258  31.897 1.00 19.56  ? 212  THR A C     1 
ATOM   1554 O  O     . THR A 1 211 ? 4.127   11.466  31.846 1.00 22.61  ? 212  THR A O     1 
ATOM   1555 C  CB    . THR A 1 211 ? 6.778   9.918   31.727 1.00 23.31  ? 212  THR A CB    1 
ATOM   1556 O  OG1   . THR A 1 211 ? 7.803   9.324   30.917 1.00 22.38  ? 212  THR A OG1   1 
ATOM   1557 C  CG2   . THR A 1 211 ? 6.871   9.353   33.140 1.00 23.59  ? 212  THR A CG2   1 
ATOM   1558 N  N     . PRO A 1 212 ? 3.535   9.474   32.635 1.00 20.66  ? 213  PRO A N     1 
ATOM   1559 C  CA    . PRO A 1 212 ? 2.456   10.055  33.446 1.00 25.41  ? 213  PRO A CA    1 
ATOM   1560 C  C     . PRO A 1 212 ? 3.004   10.954  34.546 1.00 21.66  ? 213  PRO A C     1 
ATOM   1561 O  O     . PRO A 1 212 ? 4.126   10.773  35.023 1.00 22.90  ? 213  PRO A O     1 
ATOM   1562 C  CB    . PRO A 1 212 ? 1.772   8.824   34.034 1.00 23.15  ? 213  PRO A CB    1 
ATOM   1563 C  CG    . PRO A 1 212 ? 2.868   7.744   34.046 1.00 27.83  ? 213  PRO A CG    1 
ATOM   1564 C  CD    . PRO A 1 212 ? 3.659   8.019   32.786 1.00 23.20  ? 213  PRO A CD    1 
ATOM   1565 N  N     . GLU A 1 213 ? 2.190   11.944  34.902 1.00 21.64  ? 214  GLU A N     1 
ATOM   1566 C  CA    . GLU A 1 213 ? 2.472   12.770  36.082 1.00 22.41  ? 214  GLU A CA    1 
ATOM   1567 C  C     . GLU A 1 213 ? 2.510   11.886  37.320 1.00 25.90  ? 214  GLU A C     1 
ATOM   1568 O  O     . GLU A 1 213 ? 1.752   10.929  37.436 1.00 27.41  ? 214  GLU A O     1 
ATOM   1569 C  CB    . GLU A 1 213 ? 1.398   13.858  36.192 1.00 28.05  ? 214  GLU A CB    1 
ATOM   1570 C  CG    . GLU A 1 213 ? 1.693   14.927  37.214 1.00 47.19  ? 214  GLU A CG    1 
ATOM   1571 C  CD    . GLU A 1 213 ? 0.607   16.004  37.280 1.00 58.97  ? 214  GLU A CD    1 
ATOM   1572 O  OE1   . GLU A 1 213 ? -0.444  15.849  36.617 1.00 54.81  ? 214  GLU A OE1   1 
ATOM   1573 O  OE2   . GLU A 1 213 ? 0.821   17.015  37.985 1.00 62.69  ? 214  GLU A OE2   1 
ATOM   1574 N  N     . ARG A 1 214 ? 3.463   12.170  38.216 1.00 25.42  ? 215  ARG A N     1 
ATOM   1575 C  CA    . ARG A 1 214 ? 3.478   11.442  39.490 1.00 29.35  ? 215  ARG A CA    1 
ATOM   1576 C  C     . ARG A 1 214 ? 2.156   11.689  40.207 1.00 21.19  ? 215  ARG A C     1 
ATOM   1577 O  O     . ARG A 1 214 ? 1.674   12.828  40.223 1.00 22.38  ? 215  ARG A O     1 
ATOM   1578 C  CB    . ARG A 1 214 ? 4.622   11.912  40.403 1.00 31.57  ? 215  ARG A CB    1 
ATOM   1579 C  CG    . ARG A 1 214 ? 5.999   11.763  39.802 1.00 35.39  ? 215  ARG A CG    1 
ATOM   1580 C  CD    . ARG A 1 214 ? 7.131   12.032  40.791 1.00 41.29  ? 215  ARG A CD    1 
ATOM   1581 N  NE    . ARG A 1 214 ? 7.116   13.373  41.366 1.00 50.92  ? 215  ARG A NE    1 
ATOM   1582 C  CZ    . ARG A 1 214 ? 7.229   13.617  42.672 1.00 62.16  ? 215  ARG A CZ    1 
ATOM   1583 N  NH1   . ARG A 1 214 ? 7.200   14.864  43.138 1.00 59.70  ? 215  ARG A NH1   1 
ATOM   1584 N  NH2   . ARG A 1 214 ? 7.421   12.605  43.517 1.00 66.60  ? 215  ARG A NH2   1 
ATOM   1585 N  N     . GLU A 1 215 ? 1.611   10.625  40.818 1.00 26.95  ? 216  GLU A N     1 
ATOM   1586 C  CA    . GLU A 1 215 ? 0.325   10.729  41.507 1.00 24.82  ? 216  GLU A CA    1 
ATOM   1587 C  C     . GLU A 1 215 ? 0.363   11.767  42.622 1.00 19.14  ? 216  GLU A C     1 
ATOM   1588 O  O     . GLU A 1 215 ? -0.597  12.512  42.799 1.00 20.30  ? 216  GLU A O     1 
ATOM   1589 C  CB    . GLU A 1 215 ? -0.108  9.382   42.077 1.00 29.57  ? 216  GLU A CB    1 
ATOM   1590 C  CG    . GLU A 1 215 ? -0.365  8.323   41.005 1.00 30.27  ? 216  GLU A CG    1 
ATOM   1591 C  CD    . GLU A 1 215 ? -1.497  8.715   40.064 1.00 50.26  ? 216  GLU A CD    1 
ATOM   1592 O  OE1   . GLU A 1 215 ? -2.458  9.384   40.504 1.00 48.61  ? 216  GLU A OE1   1 
ATOM   1593 O  OE2   . GLU A 1 215 ? -1.406  8.366   38.864 1.00 60.83  ? 216  GLU A OE2   1 
ATOM   1594 N  N     . VAL A 1 216 ? 1.497   11.894  43.323 1.00 21.56  ? 217  VAL A N     1 
ATOM   1595 C  CA    . VAL A 1 216 ? 1.581   12.858  44.425 1.00 19.52  ? 217  VAL A CA    1 
ATOM   1596 C  C     . VAL A 1 216 ? 1.561   14.294  43.942 1.00 19.99  ? 217  VAL A C     1 
ATOM   1597 O  O     . VAL A 1 216 ? 1.307   15.233  44.709 1.00 21.69  ? 217  VAL A O     1 
ATOM   1598 C  CB    . VAL A 1 216 ? 2.830   12.580  45.294 1.00 20.98  ? 217  VAL A CB    1 
ATOM   1599 C  CG1   . VAL A 1 216 ? 4.139   12.964  44.529 1.00 23.72  ? 217  VAL A CG1   1 
ATOM   1600 C  CG2   . VAL A 1 216 ? 2.735   13.339  46.589 1.00 26.34  ? 217  VAL A CG2   1 
ATOM   1601 N  N     . ASP A 1 217 ? 1.826   14.531  42.631 1.00 20.01  ? 218  ASP A N     1 
ATOM   1602 C  CA    . ASP A 1 217 ? 1.816   15.872  42.083 1.00 23.59  ? 218  ASP A CA    1 
ATOM   1603 C  C     . ASP A 1 217 ? 0.459   16.315  41.533 1.00 21.41  ? 218  ASP A C     1 
ATOM   1604 O  O     . ASP A 1 217 ? 0.301   17.502  41.224 1.00 26.87  ? 218  ASP A O     1 
ATOM   1605 C  CB    . ASP A 1 217 ? 2.862   15.940  40.951 1.00 23.09  ? 218  ASP A CB    1 
ATOM   1606 C  CG    . ASP A 1 217 ? 4.299   15.859  41.496 1.00 34.90  ? 218  ASP A CG    1 
ATOM   1607 O  OD1   . ASP A 1 217 ? 4.537   16.298  42.665 1.00 31.19  ? 218  ASP A OD1   1 
ATOM   1608 O  OD2   . ASP A 1 217 ? 5.168   15.363  40.739 1.00 39.44  ? 218  ASP A OD2   1 
ATOM   1609 N  N     . ARG A 1 218 ? -0.491  15.402  41.411 1.00 20.39  ? 219  ARG A N     1 
ATOM   1610 C  CA    . ARG A 1 218 ? -1.845  15.702  40.904 1.00 21.16  ? 219  ARG A CA    1 
ATOM   1611 C  C     . ARG A 1 218 ? -2.659  16.336  42.037 1.00 23.03  ? 219  ARG A C     1 
ATOM   1612 O  O     . ARG A 1 218 ? -2.250  16.282  43.193 1.00 21.64  ? 219  ARG A O     1 
ATOM   1613 C  CB    . ARG A 1 218 ? -2.460  14.408  40.395 1.00 22.32  ? 219  ARG A CB    1 
ATOM   1614 C  CG    . ARG A 1 218 ? -1.627  13.659  39.322 1.00 23.39  ? 219  ARG A CG    1 
ATOM   1615 C  CD    . ARG A 1 218 ? -2.281  12.390  38.929 1.00 30.43  ? 219  ARG A CD    1 
ATOM   1616 N  NE    . ARG A 1 218 ? -3.579  12.682  38.323 1.00 33.47  ? 219  ARG A NE    1 
ATOM   1617 C  CZ    . ARG A 1 218 ? -4.487  11.743  38.074 1.00 33.00  ? 219  ARG A CZ    1 
ATOM   1618 N  NH1   . ARG A 1 218 ? -4.250  10.474  38.401 1.00 32.98  ? 219  ARG A NH1   1 
ATOM   1619 N  NH2   . ARG A 1 218 ? -5.647  12.085  37.523 1.00 37.92  ? 219  ARG A NH2   1 
ATOM   1620 N  N     . PRO A 1 219 ? -3.821  16.933  41.762 1.00 19.61  ? 220  PRO A N     1 
ATOM   1621 C  CA    . PRO A 1 219 ? -4.606  17.556  42.841 1.00 18.99  ? 220  PRO A CA    1 
ATOM   1622 C  C     . PRO A 1 219 ? -5.110  16.518  43.845 1.00 15.76  ? 220  PRO A C     1 
ATOM   1623 O  O     . PRO A 1 219 ? -5.565  15.441  43.474 1.00 17.83  ? 220  PRO A O     1 
ATOM   1624 C  CB    . PRO A 1 219 ? -5.777  18.226  42.109 1.00 21.73  ? 220  PRO A CB    1 
ATOM   1625 C  CG    . PRO A 1 219 ? -5.258  18.413  40.683 1.00 28.97  ? 220  PRO A CG    1 
ATOM   1626 C  CD    . PRO A 1 219 ? -4.391  17.219  40.416 1.00 21.54  ? 220  PRO A CD    1 
ATOM   1627 N  N     . PHE A 1 220 ? -5.000  16.904  45.109 1.00 18.85  ? 221  PHE A N     1 
ATOM   1628 C  CA    . PHE A 1 220 ? -5.425  16.032  46.194 1.00 17.46  ? 221  PHE A CA    1 
ATOM   1629 C  C     . PHE A 1 220 ? -6.839  15.510  45.966 1.00 15.38  ? 221  PHE A C     1 
ATOM   1630 O  O     . PHE A 1 220 ? -7.772  16.285  45.702 1.00 16.04  ? 221  PHE A O     1 
ATOM   1631 C  CB    . PHE A 1 220 ? -5.325  16.834  47.461 1.00 16.88  ? 221  PHE A CB    1 
ATOM   1632 C  CG    . PHE A 1 220 ? -5.907  16.143  48.672 1.00 15.59  ? 221  PHE A CG    1 
ATOM   1633 C  CD1   . PHE A 1 220 ? -5.343  14.969  49.146 1.00 17.61  ? 221  PHE A CD1   1 
ATOM   1634 C  CD2   . PHE A 1 220 ? -6.953  16.712  49.329 1.00 15.81  ? 221  PHE A CD2   1 
ATOM   1635 C  CE1   . PHE A 1 220 ? -5.909  14.316  50.286 1.00 17.77  ? 221  PHE A CE1   1 
ATOM   1636 C  CE2   . PHE A 1 220 ? -7.525  16.091  50.461 1.00 18.74  ? 221  PHE A CE2   1 
ATOM   1637 C  CZ    . PHE A 1 220 ? -6.987  14.902  50.917 1.00 16.56  ? 221  PHE A CZ    1 
ATOM   1638 N  N     . LEU A 1 221 ? -7.019  14.223  46.240 1.00 14.95  ? 222  LEU A N     1 
ATOM   1639 C  CA    . LEU A 1 221 ? -8.329  13.599  46.260 1.00 14.46  ? 222  LEU A CA    1 
ATOM   1640 C  C     . LEU A 1 221 ? -8.307  12.437  47.248 1.00 16.09  ? 222  LEU A C     1 
ATOM   1641 O  O     . LEU A 1 221 ? -7.400  11.590  47.180 1.00 16.43  ? 222  LEU A O     1 
ATOM   1642 C  CB    . LEU A 1 221 ? -8.742  13.070  44.867 1.00 16.09  ? 222  LEU A CB    1 
ATOM   1643 C  CG    . LEU A 1 221 ? -10.099 12.397  44.781 1.00 18.65  ? 222  LEU A CG    1 
ATOM   1644 C  CD1   . LEU A 1 221 ? -11.227 13.360  45.026 1.00 21.70  ? 222  LEU A CD1   1 
ATOM   1645 C  CD2   . LEU A 1 221 ? -10.290 11.674  43.315 1.00 18.17  ? 222  LEU A CD2   1 
ATOM   1646 N  N     . MET A 1 222 ? -9.292  12.389  48.159 1.00 14.29  ? 223  MET A N     1 
ATOM   1647 C  CA    . MET A 1 222 ? -9.424  11.250  49.070 1.00 15.47  ? 223  MET A CA    1 
ATOM   1648 C  C     . MET A 1 222 ? -10.901 10.969  49.237 1.00 15.25  ? 223  MET A C     1 
ATOM   1649 O  O     . MET A 1 222 ? -11.620 11.862  49.689 1.00 16.26  ? 223  MET A O     1 
ATOM   1650 C  CB    . MET A 1 222 ? -8.833  11.569  50.455 1.00 16.49  ? 223  MET A CB    1 
ATOM   1651 C  CG    . MET A 1 222 ? -8.890  10.300  51.316 1.00 17.62  ? 223  MET A CG    1 
ATOM   1652 S  SD    . MET A 1 222 ? -8.305  10.525  53.004 1.00 21.80  ? 223  MET A SD    1 
ATOM   1653 C  CE    . MET A 1 222 ? -9.853  11.036  53.774 1.00 23.29  ? 223  MET A CE    1 
ATOM   1654 N  N     . ALA A 1 223 ? -11.343 9.753   48.985 1.00 14.57  ? 224  ALA A N     1 
ATOM   1655 C  CA    . ALA A 1 223 ? -12.710 9.387   49.303 1.00 14.79  ? 224  ALA A CA    1 
ATOM   1656 C  C     . ALA A 1 223 ? -12.866 9.158   50.807 1.00 13.37  ? 224  ALA A C     1 
ATOM   1657 O  O     . ALA A 1 223 ? -12.045 8.473   51.433 1.00 16.84  ? 224  ALA A O     1 
ATOM   1658 C  CB    . ALA A 1 223 ? -13.141 8.125   48.522 1.00 18.44  ? 224  ALA A CB    1 
ATOM   1659 N  N     . VAL A 1 224 ? -13.913 9.720   51.412 1.00 14.48  ? 225  VAL A N     1 
ATOM   1660 C  CA    . VAL A 1 224 ? -14.156 9.506   52.836 1.00 14.39  ? 225  VAL A CA    1 
ATOM   1661 C  C     . VAL A 1 224 ? -14.709 8.111   53.084 1.00 15.94  ? 225  VAL A C     1 
ATOM   1662 O  O     . VAL A 1 224 ? -15.716 7.710   52.453 1.00 19.27  ? 225  VAL A O     1 
ATOM   1663 C  CB    . VAL A 1 224 ? -15.139 10.559  53.357 1.00 17.20  ? 225  VAL A CB    1 
ATOM   1664 C  CG1   . VAL A 1 224 ? -15.448 10.295  54.830 1.00 18.35  ? 225  VAL A CG1   1 
ATOM   1665 C  CG2   . VAL A 1 224 ? -14.510 11.959  53.182 1.00 19.65  ? 225  VAL A CG2   1 
ATOM   1666 N  N     . GLU A 1 225 ? -14.055 7.368   53.973 1.00 16.24  ? 226  GLU A N     1 
ATOM   1667 C  CA    . GLU A 1 225 ? -14.531 6.016   54.279 1.00 18.21  ? 226  GLU A CA    1 
ATOM   1668 C  C     . GLU A 1 225 ? -15.164 5.903   55.630 1.00 22.25  ? 226  GLU A C     1 
ATOM   1669 O  O     . GLU A 1 225 ? -16.074 5.094   55.788 1.00 25.02  ? 226  GLU A O     1 
ATOM   1670 C  CB    . GLU A 1 225 ? -13.375 5.013   54.204 1.00 18.66  ? 226  GLU A CB    1 
ATOM   1671 C  CG    . GLU A 1 225 ? -12.850 4.806   52.791 1.00 25.12  ? 226  GLU A CG    1 
ATOM   1672 C  CD    . GLU A 1 225 ? -11.534 4.007   52.721 1.00 36.27  ? 226  GLU A CD    1 
ATOM   1673 O  OE1   . GLU A 1 225 ? -10.886 3.759   53.770 1.00 49.20  ? 226  GLU A OE1   1 
ATOM   1674 O  OE2   . GLU A 1 225 ? -11.135 3.619   51.614 1.00 46.53  ? 226  GLU A OE2   1 
ATOM   1675 N  N     . ASP A 1 226 ? -14.685 6.650   56.608 1.00 19.27  ? 227  ASP A N     1 
ATOM   1676 C  CA    . ASP A 1 226 ? -15.237 6.607   57.951 1.00 19.56  ? 227  ASP A CA    1 
ATOM   1677 C  C     . ASP A 1 226 ? -14.990 7.975   58.569 1.00 19.11  ? 227  ASP A C     1 
ATOM   1678 O  O     . ASP A 1 226 ? -14.225 8.805   58.054 1.00 21.63  ? 227  ASP A O     1 
ATOM   1679 C  CB    . ASP A 1 226 ? -14.652 5.520   58.823 1.00 20.86  ? 227  ASP A CB    1 
ATOM   1680 C  CG    . ASP A 1 226 ? -15.659 5.045   59.852 1.00 31.60  ? 227  ASP A CG    1 
ATOM   1681 O  OD1   . ASP A 1 226 ? -16.730 5.723   60.013 1.00 30.89  ? 227  ASP A OD1   1 
ATOM   1682 O  OD2   . ASP A 1 226 ? -15.433 3.938   60.391 1.00 33.55  ? 227  ASP A OD2   1 
ATOM   1683 N  N     . VAL A 1 227 ? -15.687 8.235   59.658 1.00 18.67  ? 228  VAL A N     1 
ATOM   1684 C  CA    . VAL A 1 227 ? -15.631 9.541   60.278 1.00 17.32  ? 228  VAL A CA    1 
ATOM   1685 C  C     . VAL A 1 227 ? -15.710 9.331   61.779 1.00 17.20  ? 228  VAL A C     1 
ATOM   1686 O  O     . VAL A 1 227 ? -16.453 8.472   62.242 1.00 19.41  ? 228  VAL A O     1 
ATOM   1687 C  CB    . VAL A 1 227 ? -16.802 10.416  59.772 1.00 17.92  ? 228  VAL A CB    1 
ATOM   1688 C  CG1   . VAL A 1 227 ? -17.056 11.522  60.602 1.00 39.88  ? 228  VAL A CG1   1 
ATOM   1689 C  CG2   . VAL A 1 227 ? -16.525 10.899  58.338 1.00 20.88  ? 228  VAL A CG2   1 
ATOM   1690 N  N     . PHE A 1 228 ? -14.965 10.142  62.520 1.00 16.04  ? 229  PHE A N     1 
ATOM   1691 C  CA    . PHE A 1 228 ? -14.906 10.000  63.960 1.00 16.47  ? 229  PHE A CA    1 
ATOM   1692 C  C     . PHE A 1 228 ? -15.021 11.354  64.641 1.00 16.84  ? 229  PHE A C     1 
ATOM   1693 O  O     . PHE A 1 228 ? -14.453 12.350  64.177 1.00 19.62  ? 229  PHE A O     1 
ATOM   1694 C  CB    . PHE A 1 228 ? -13.618 9.349   64.428 1.00 16.72  ? 229  PHE A CB    1 
ATOM   1695 C  CG    . PHE A 1 228 ? -13.363 7.993   63.833 1.00 16.79  ? 229  PHE A CG    1 
ATOM   1696 C  CD1   . PHE A 1 228 ? -12.898 7.830   62.542 1.00 17.77  ? 229  PHE A CD1   1 
ATOM   1697 C  CD2   . PHE A 1 228 ? -13.794 6.847   64.511 1.00 18.11  ? 229  PHE A CD2   1 
ATOM   1698 C  CE1   . PHE A 1 228 ? -12.705 6.550   61.989 1.00 17.90  ? 229  PHE A CE1   1 
ATOM   1699 C  CE2   . PHE A 1 228 ? -13.650 5.562   63.906 1.00 17.55  ? 229  PHE A CE2   1 
ATOM   1700 C  CZ    . PHE A 1 228 ? -13.109 5.422   62.681 1.00 17.96  ? 229  PHE A CZ    1 
ATOM   1701 N  N     . THR A 1 229 ? -15.714 11.371  65.797 1.00 17.20  ? 230  THR A N     1 
ATOM   1702 C  CA    . THR A 1 229 ? -15.798 12.532  66.693 1.00 19.59  ? 230  THR A CA    1 
ATOM   1703 C  C     . THR A 1 229 ? -14.931 12.258  67.900 1.00 17.78  ? 230  THR A C     1 
ATOM   1704 O  O     . THR A 1 229 ? -15.241 11.391  68.719 1.00 19.92  ? 230  THR A O     1 
ATOM   1705 C  CB    . THR A 1 229 ? -17.222 12.756  67.190 1.00 22.75  ? 230  THR A CB    1 
ATOM   1706 O  OG1   . THR A 1 229 ? -18.058 13.035  66.064 1.00 25.05  ? 230  THR A OG1   1 
ATOM   1707 C  CG2   . THR A 1 229 ? -17.270 13.955  68.136 1.00 22.80  ? 230  THR A CG2   1 
ATOM   1708 N  N     . ILE A 1 230 ? -13.878 13.025  68.060 1.00 17.68  ? 231  ILE A N     1 
ATOM   1709 C  CA    . ILE A 1 230 ? -12.973 12.853  69.188 1.00 19.82  ? 231  ILE A CA    1 
ATOM   1710 C  C     . ILE A 1 230 ? -12.894 14.100  70.038 1.00 19.66  ? 231  ILE A C     1 
ATOM   1711 O  O     . ILE A 1 230 ? -12.902 14.011  71.276 1.00 24.78  ? 231  ILE A O     1 
ATOM   1712 C  CB    . ILE A 1 230 ? -11.581 12.400  68.711 1.00 20.48  ? 231  ILE A CB    1 
ATOM   1713 C  CG1   . ILE A 1 230 ? -11.763 11.012  68.071 1.00 24.36  ? 231  ILE A CG1   1 
ATOM   1714 C  CG2   . ILE A 1 230 ? -10.574 12.324  69.830 1.00 21.25  ? 231  ILE A CG2   1 
ATOM   1715 C  CD1   . ILE A 1 230 ? -10.566 10.601  67.322 1.00 24.07  ? 231  ILE A CD1   1 
ATOM   1716 N  N     . THR A 1 231 ? -12.755 15.259  69.412 1.00 20.12  ? 232  THR A N     1 
ATOM   1717 C  CA    . THR A 1 231 ? -12.928 16.544  70.079 1.00 25.47  ? 232  THR A CA    1 
ATOM   1718 C  C     . THR A 1 231 ? -14.121 17.310  69.505 1.00 40.71  ? 232  THR A C     1 
ATOM   1719 O  O     . THR A 1 231 ? -14.673 16.980  68.443 1.00 31.90  ? 232  THR A O     1 
ATOM   1720 C  CB    . THR A 1 231 ? -11.661 17.410  69.946 1.00 40.52  ? 232  THR A CB    1 
ATOM   1721 O  OG1   . THR A 1 231 ? -11.450 17.737  68.566 1.00 54.48  ? 232  THR A OG1   1 
ATOM   1722 C  CG2   . THR A 1 231 ? -10.425 16.677  70.472 1.00 32.46  ? 232  THR A CG2   1 
ATOM   1723 N  N     . GLY A 1 232 ? -14.482 18.393  70.204 1.00 32.50  ? 233  GLY A N     1 
ATOM   1724 C  CA    . GLY A 1 232 ? -15.507 19.277  69.703 1.00 36.12  ? 233  GLY A CA    1 
ATOM   1725 C  C     . GLY A 1 232 ? -15.073 20.198  68.588 1.00 49.92  ? 233  GLY A C     1 
ATOM   1726 O  O     . GLY A 1 232 ? -15.914 20.916  68.038 1.00 42.46  ? 233  GLY A O     1 
ATOM   1727 N  N     . ARG A 1 233 ? -13.799 20.177  68.203 1.00 38.83  ? 234  ARG A N     1 
ATOM   1728 C  CA    . ARG A 1 233 ? -13.277 21.160  67.266 1.00 49.57  ? 234  ARG A CA    1 
ATOM   1729 C  C     . ARG A 1 233 ? -13.373 20.748  65.792 1.00 52.05  ? 234  ARG A C     1 
ATOM   1730 O  O     . ARG A 1 233 ? -13.120 21.592  64.928 1.00 42.80  ? 234  ARG A O     1 
ATOM   1731 C  CB    . ARG A 1 233 ? -11.820 21.464  67.614 1.00 60.38  ? 234  ARG A CB    1 
ATOM   1732 C  CG    . ARG A 1 233 ? -11.632 21.840  69.087 1.00 69.18  ? 234  ARG A CG    1 
ATOM   1733 C  CD    . ARG A 1 233 ? -10.204 22.243  69.407 1.00 78.71  ? 234  ARG A CD    1 
ATOM   1734 N  NE    . ARG A 1 233 ? -9.914  23.574  68.883 1.00 86.85  ? 234  ARG A NE    1 
ATOM   1735 C  CZ    . ARG A 1 233 ? -10.189 24.695  69.545 1.00 90.65  ? 234  ARG A CZ    1 
ATOM   1736 N  NH1   . ARG A 1 233 ? -10.758 24.628  70.741 1.00 90.35  ? 234  ARG A NH1   1 
ATOM   1737 N  NH2   . ARG A 1 233 ? -9.904  25.878  69.016 1.00 92.60  ? 234  ARG A NH2   1 
ATOM   1738 N  N     . GLY A 1 234 ? -13.741 19.507  65.477 1.00 38.93  ? 235  GLY A N     1 
ATOM   1739 C  CA    . GLY A 1 234 ? -13.858 19.077  64.085 1.00 25.02  ? 235  GLY A CA    1 
ATOM   1740 C  C     . GLY A 1 234 ? -14.137 17.581  64.040 1.00 26.33  ? 235  GLY A C     1 
ATOM   1741 O  O     . GLY A 1 234 ? -14.382 16.939  65.056 1.00 27.91  ? 235  GLY A O     1 
ATOM   1742 N  N     . THR A 1 235 ? -14.144 17.026  62.829 1.00 23.68  ? 236  THR A N     1 
ATOM   1743 C  CA    . THR A 1 235 ? -14.338 15.601  62.704 1.00 23.08  ? 236  THR A CA    1 
ATOM   1744 C  C     . THR A 1 235 ? -13.049 15.007  62.123 1.00 21.78  ? 236  THR A C     1 
ATOM   1745 O  O     . THR A 1 235 ? -12.435 15.663  61.290 1.00 24.82  ? 236  THR A O     1 
ATOM   1746 C  CB    . THR A 1 235 ? -15.536 15.401  61.764 1.00 21.71  ? 236  THR A CB    1 
ATOM   1747 O  OG1   . THR A 1 235 ? -16.739 15.897  62.445 1.00 26.55  ? 236  THR A OG1   1 
ATOM   1748 C  CG2   . THR A 1 235 ? -15.725 14.029  61.459 1.00 24.24  ? 236  THR A CG2   1 
ATOM   1749 N  N     . VAL A 1 236 ? -12.630 13.787  62.512 1.00 16.80  ? 237  VAL A N     1 
ATOM   1750 C  CA    . VAL A 1 236 ? -11.557 13.090  61.788 1.00 17.40  ? 237  VAL A CA    1 
ATOM   1751 C  C     . VAL A 1 236 ? -12.161 12.253  60.669 1.00 16.50  ? 237  VAL A C     1 
ATOM   1752 O  O     . VAL A 1 236 ? -13.003 11.391  60.915 1.00 18.37  ? 237  VAL A O     1 
ATOM   1753 C  CB    . VAL A 1 236 ? -10.753 12.191  62.735 1.00 17.48  ? 237  VAL A CB    1 
ATOM   1754 C  CG1   . VAL A 1 236 ? -9.656  11.450  61.914 1.00 18.24  ? 237  VAL A CG1   1 
ATOM   1755 C  CG2   . VAL A 1 236 ? -10.104 13.042  63.836 1.00 18.73  ? 237  VAL A CG2   1 
ATOM   1756 N  N     . ALA A 1 237 ? -11.743 12.494  59.443 1.00 14.91  ? 238  ALA A N     1 
ATOM   1757 C  CA    . ALA A 1 237 ? -12.195 11.750  58.267 1.00 14.66  ? 238  ALA A CA    1 
ATOM   1758 C  C     . ALA A 1 237 ? -11.087 10.812  57.815 1.00 16.12  ? 238  ALA A C     1 
ATOM   1759 O  O     . ALA A 1 237 ? -9.947  11.260  57.660 1.00 17.16  ? 238  ALA A O     1 
ATOM   1760 C  CB    . ALA A 1 237 ? -12.534 12.738  57.111 1.00 17.68  ? 238  ALA A CB    1 
ATOM   1761 N  N     . THR A 1 238 ? -11.393 9.548   57.609 1.00 15.31  ? 239  THR A N     1 
ATOM   1762 C  CA    . THR A 1 238 ? -10.371 8.576   57.222 1.00 15.99  ? 239  THR A CA    1 
ATOM   1763 C  C     . THR A 1 238 ? -10.594 8.074   55.808 1.00 16.64  ? 239  THR A C     1 
ATOM   1764 O  O     . THR A 1 238 ? -11.718 8.064   55.270 1.00 16.77  ? 239  THR A O     1 
ATOM   1765 C  CB    . THR A 1 238 ? -10.344 7.371   58.182 1.00 17.26  ? 239  THR A CB    1 
ATOM   1766 O  OG1   . THR A 1 238 ? -11.593 6.670   58.085 1.00 20.44  ? 239  THR A OG1   1 
ATOM   1767 C  CG2   . THR A 1 238 ? -10.070 7.818   59.572 1.00 19.24  ? 239  THR A CG2   1 
ATOM   1768 N  N     . GLY A 1 239 ? -9.481  7.724   55.156 1.00 15.11  ? 240  GLY A N     1 
ATOM   1769 C  CA    . GLY A 1 239 ? -9.563  7.125   53.823 1.00 15.84  ? 240  GLY A CA    1 
ATOM   1770 C  C     . GLY A 1 239 ? -8.159  6.918   53.320 1.00 17.52  ? 240  GLY A C     1 
ATOM   1771 O  O     . GLY A 1 239 ? -7.178  7.153   54.033 1.00 20.45  ? 240  GLY A O     1 
ATOM   1772 N  N     . ARG A 1 240 ? -8.082  6.458   52.071 1.00 17.53  ? 241  ARG A N     1 
ATOM   1773 C  CA    . ARG A 1 240 ? -6.797  6.308   51.411 1.00 18.70  ? 241  ARG A CA    1 
ATOM   1774 C  C     . ARG A 1 240 ? -6.674  7.422   50.385 1.00 19.03  ? 241  ARG A C     1 
ATOM   1775 O  O     . ARG A 1 240 ? -7.545  7.571   49.529 1.00 22.80  ? 241  ARG A O     1 
ATOM   1776 C  CB    . ARG A 1 240 ? -6.721  4.968   50.676 1.00 24.07  ? 241  ARG A CB    1 
ATOM   1777 C  CG    . ARG A 1 240 ? -5.267  4.741   50.181 1.00 23.51  ? 241  ARG A CG    1 
ATOM   1778 C  CD    . ARG A 1 240 ? -5.127  3.434   49.379 1.00 35.06  ? 241  ARG A CD    1 
ATOM   1779 N  NE    . ARG A 1 240 ? -5.414  2.270   50.195 1.00 57.81  ? 241  ARG A NE    1 
ATOM   1780 C  CZ    . ARG A 1 240 ? -4.532  1.684   50.997 1.00 70.89  ? 241  ARG A CZ    1 
ATOM   1781 N  NH1   . ARG A 1 240 ? -3.300  2.172   51.105 1.00 71.15  ? 241  ARG A NH1   1 
ATOM   1782 N  NH2   . ARG A 1 240 ? -4.890  0.614   51.701 1.00 74.41  ? 241  ARG A NH2   1 
ATOM   1783 N  N     . ILE A 1 241 ? -5.578  8.167   50.453 1.00 17.44  ? 242  ILE A N     1 
ATOM   1784 C  CA    . ILE A 1 241 ? -5.401  9.289   49.525 1.00 16.07  ? 242  ILE A CA    1 
ATOM   1785 C  C     . ILE A 1 241 ? -5.202  8.717   48.129 1.00 20.60  ? 242  ILE A C     1 
ATOM   1786 O  O     . ILE A 1 241 ? -4.302  7.892   47.912 1.00 19.86  ? 242  ILE A O     1 
ATOM   1787 C  CB    . ILE A 1 241 ? -4.231  10.163  49.955 1.00 16.77  ? 242  ILE A CB    1 
ATOM   1788 C  CG1   . ILE A 1 241 ? -4.518  10.806  51.323 1.00 16.36  ? 242  ILE A CG1   1 
ATOM   1789 C  CG2   . ILE A 1 241 ? -4.044  11.311  48.953 1.00 19.03  ? 242  ILE A CG2   1 
ATOM   1790 C  CD1   . ILE A 1 241 ? -3.348  11.658  51.856 1.00 19.29  ? 242  ILE A CD1   1 
ATOM   1791 N  N     . GLU A 1 242 ? -6.046  9.127   47.185 1.00 17.57  ? 243  GLU A N     1 
ATOM   1792 C  CA    . GLU A 1 242 ? -5.994  8.513   45.837 1.00 18.40  ? 243  GLU A CA    1 
ATOM   1793 C  C     . GLU A 1 242 ? -4.912  9.177   45.007 1.00 22.24  ? 243  GLU A C     1 
ATOM   1794 O  O     . GLU A 1 242 ? -4.229  8.498   44.216 1.00 23.49  ? 243  GLU A O     1 
ATOM   1795 C  CB    . GLU A 1 242 ? -7.359  8.613   45.109 1.00 20.68  ? 243  GLU A CB    1 
ATOM   1796 C  CG    . GLU A 1 242 ? -7.312  8.131   43.622 1.00 25.30  ? 243  GLU A CG    1 
ATOM   1797 C  CD    . GLU A 1 242 ? -8.671  8.123   42.899 1.00 41.66  ? 243  GLU A CD    1 
ATOM   1798 O  OE1   . GLU A 1 242 ? -9.715  8.172   43.573 1.00 35.51  ? 243  GLU A OE1   1 
ATOM   1799 O  OE2   . GLU A 1 242 ? -8.675  8.149   41.634 1.00 45.70  ? 243  GLU A OE2   1 
ATOM   1800 N  N     . ARG A 1 243 ? -4.755  10.476  45.152 1.00 19.03  ? 244  ARG A N     1 
ATOM   1801 C  CA    . ARG A 1 243 ? -3.739  11.210  44.419 1.00 19.66  ? 244  ARG A CA    1 
ATOM   1802 C  C     . ARG A 1 243 ? -3.445  12.496  45.158 1.00 20.96  ? 244  ARG A C     1 
ATOM   1803 O  O     . ARG A 1 243 ? -4.198  12.935  46.039 1.00 19.39  ? 244  ARG A O     1 
ATOM   1804 C  CB    . ARG A 1 243 ? -4.178  11.462  42.944 1.00 21.63  ? 244  ARG A CB    1 
ATOM   1805 C  CG    . ARG A 1 243 ? -5.384  12.366  42.894 1.00 22.59  ? 244  ARG A CG    1 
ATOM   1806 C  CD    . ARG A 1 243 ? -5.867  12.659  41.477 1.00 21.62  ? 244  ARG A CD    1 
ATOM   1807 N  NE    . ARG A 1 243 ? -6.926  13.635  41.561 1.00 18.68  ? 244  ARG A NE    1 
ATOM   1808 C  CZ    . ARG A 1 243 ? -8.040  13.515  40.835 1.00 20.03  ? 244  ARG A CZ    1 
ATOM   1809 N  NH1   . ARG A 1 243 ? -9.008  14.427  40.964 1.00 20.26  ? 244  ARG A NH1   1 
ATOM   1810 N  NH2   . ARG A 1 243 ? -8.215  12.430  40.107 1.00 22.16  ? 244  ARG A NH2   1 
ATOM   1811 N  N     . GLY A 1 244 ? -2.315  13.112  44.810 1.00 19.40  ? 245  GLY A N     1 
ATOM   1812 C  CA    . GLY A 1 244 ? -1.853  14.328  45.414 1.00 19.02  ? 245  GLY A CA    1 
ATOM   1813 C  C     . GLY A 1 244 ? -1.391  14.215  46.855 1.00 18.91  ? 245  GLY A C     1 
ATOM   1814 O  O     . GLY A 1 244 ? -0.980  13.152  47.296 1.00 20.75  ? 245  GLY A O     1 
ATOM   1815 N  N     . SER A 1 245 ? -1.476  15.321  47.553 1.00 21.81  ? 246  SER A N     1 
ATOM   1816 C  CA    . SER A 1 245 ? -1.025  15.390  48.935 1.00 19.53  ? 246  SER A CA    1 
ATOM   1817 C  C     . SER A 1 245 ? -1.782  16.482  49.655 1.00 19.12  ? 246  SER A C     1 
ATOM   1818 O  O     . SER A 1 245 ? -2.324  17.402  49.036 1.00 21.55  ? 246  SER A O     1 
ATOM   1819 C  CB    . SER A 1 245 ? 0.498   15.661  49.026 1.00 28.56  ? 246  SER A CB    1 
ATOM   1820 O  OG    . SER A 1 245 ? 0.782   17.009  48.672 1.00 28.94  ? 246  SER A OG    1 
ATOM   1821 N  N     . VAL A 1 246 ? -1.793  16.396  50.999 1.00 17.51  ? 247  VAL A N     1 
ATOM   1822 C  CA    . VAL A 1 246 ? -2.511  17.366  51.809 1.00 20.03  ? 247  VAL A CA    1 
ATOM   1823 C  C     . VAL A 1 246 ? -1.649  17.697  53.011 1.00 24.09  ? 247  VAL A C     1 
ATOM   1824 O  O     . VAL A 1 246 ? -1.048  16.801  53.611 1.00 22.19  ? 247  VAL A O     1 
ATOM   1825 C  CB    . VAL A 1 246 ? -3.910  16.808  52.196 1.00 21.00  ? 247  VAL A CB    1 
ATOM   1826 C  CG1   . VAL A 1 246 ? -3.809  15.512  53.002 1.00 21.69  ? 247  VAL A CG1   1 
ATOM   1827 C  CG2   . VAL A 1 246 ? -4.683  17.838  52.929 1.00 26.62  ? 247  VAL A CG2   1 
ATOM   1828 N  N     . LYS A 1 247 ? -1.550  18.976  53.324 1.00 23.00  ? 248  LYS A N     1 
ATOM   1829 C  CA    . LYS A 1 247 ? -0.672  19.460  54.372 1.00 20.49  ? 248  LYS A CA    1 
ATOM   1830 C  C     . LYS A 1 247 ? -1.503  20.140  55.449 1.00 19.91  ? 248  LYS A C     1 
ATOM   1831 O  O     . LYS A 1 247 ? -2.541  20.783  55.159 1.00 22.03  ? 248  LYS A O     1 
ATOM   1832 C  CB    . LYS A 1 247 ? 0.353   20.469  53.832 1.00 27.84  ? 248  LYS A CB    1 
ATOM   1833 C  CG    . LYS A 1 247 ? 1.278   19.916  52.797 1.00 44.68  ? 248  LYS A CG    1 
ATOM   1834 C  CD    . LYS A 1 247 ? 2.293   20.964  52.346 1.00 62.17  ? 248  LYS A CD    1 
ATOM   1835 C  CE    . LYS A 1 247 ? 3.334   21.234  53.434 1.00 71.33  ? 248  LYS A CE    1 
ATOM   1836 N  NZ    . LYS A 1 247 ? 4.457   22.109  52.948 1.00 74.99  ? 248  LYS A NZ    1 
ATOM   1837 N  N     . VAL A 1 248 ? -1.036  20.055  56.693 1.00 21.93  ? 249  VAL A N     1 
ATOM   1838 C  CA    . VAL A 1 248 ? -1.690  20.798  57.760 1.00 19.38  ? 249  VAL A CA    1 
ATOM   1839 C  C     . VAL A 1 248 ? -1.767  22.286  57.423 1.00 21.27  ? 249  VAL A C     1 
ATOM   1840 O  O     . VAL A 1 248 ? -0.760  22.895  57.021 1.00 24.77  ? 249  VAL A O     1 
ATOM   1841 C  CB    . VAL A 1 248 ? -0.945  20.532  59.088 1.00 22.61  ? 249  VAL A CB    1 
ATOM   1842 C  CG1   . VAL A 1 248 ? -1.482  21.401  60.184 1.00 23.98  ? 249  VAL A CG1   1 
ATOM   1843 C  CG2   . VAL A 1 248 ? -1.129  19.062  59.413 1.00 26.64  ? 249  VAL A CG2   1 
ATOM   1844 N  N     . GLY A 1 249 ? -2.944  22.896  57.641 1.00 21.56  ? 250  GLY A N     1 
ATOM   1845 C  CA    . GLY A 1 249 ? -3.165  24.306  57.341 1.00 20.64  ? 250  GLY A CA    1 
ATOM   1846 C  C     . GLY A 1 249 ? -3.803  24.576  56.001 1.00 19.99  ? 250  GLY A C     1 
ATOM   1847 O  O     . GLY A 1 249 ? -4.282  25.712  55.774 1.00 22.59  ? 250  GLY A O     1 
ATOM   1848 N  N     . GLU A 1 250 ? -3.826  23.587  55.121 1.00 20.01  ? 251  GLU A N     1 
ATOM   1849 C  CA    . GLU A 1 250 ? -4.415  23.777  53.798 1.00 18.90  ? 251  GLU A CA    1 
ATOM   1850 C  C     . GLU A 1 250 ? -5.936  23.765  53.828 1.00 18.62  ? 251  GLU A C     1 
ATOM   1851 O  O     . GLU A 1 250 ? -6.572  23.090  54.641 1.00 20.59  ? 251  GLU A O     1 
ATOM   1852 C  CB    . GLU A 1 250 ? -3.933  22.692  52.859 1.00 20.05  ? 251  GLU A CB    1 
ATOM   1853 C  CG    . GLU A 1 250 ? -2.497  22.936  52.401 1.00 28.29  ? 251  GLU A CG    1 
ATOM   1854 C  CD    . GLU A 1 250 ? -1.997  21.922  51.366 1.00 45.06  ? 251  GLU A CD    1 
ATOM   1855 O  OE1   . GLU A 1 250 ? -2.619  20.855  51.180 1.00 30.27  ? 251  GLU A OE1   1 
ATOM   1856 O  OE2   . GLU A 1 250 ? -0.990  22.238  50.688 1.00 58.26  ? 251  GLU A OE2   1 
ATOM   1857 N  N     . THR A 1 251 ? -6.521  24.566  52.931 1.00 18.85  ? 252  THR A N     1 
ATOM   1858 C  CA    . THR A 1 251 ? -7.947  24.535  52.684 1.00 17.42  ? 252  THR A CA    1 
ATOM   1859 C  C     . THR A 1 251 ? -8.250  23.423  51.699 1.00 15.76  ? 252  THR A C     1 
ATOM   1860 O  O     . THR A 1 251 ? -7.622  23.334  50.642 1.00 18.14  ? 252  THR A O     1 
ATOM   1861 C  CB    . THR A 1 251 ? -8.407  25.867  52.079 1.00 19.22  ? 252  THR A CB    1 
ATOM   1862 O  OG1   . THR A 1 251 ? -8.210  26.905  53.075 1.00 20.07  ? 252  THR A OG1   1 
ATOM   1863 C  CG2   . THR A 1 251 ? -9.906  25.808  51.719 1.00 19.07  ? 252  THR A CG2   1 
ATOM   1864 N  N     . ILE A 1 252 ? -9.218  22.584  52.057 1.00 16.05  ? 253  ILE A N     1 
ATOM   1865 C  CA    . ILE A 1 252 ? -9.720  21.579  51.115 1.00 16.17  ? 253  ILE A CA    1 
ATOM   1866 C  C     . ILE A 1 252 ? -11.223 21.756  50.972 1.00 15.65  ? 253  ILE A C     1 
ATOM   1867 O  O     . ILE A 1 252 ? -11.868 22.445  51.755 1.00 16.67  ? 253  ILE A O     1 
ATOM   1868 C  CB    . ILE A 1 252 ? -9.393  20.130  51.587 1.00 16.41  ? 253  ILE A CB    1 
ATOM   1869 C  CG1   . ILE A 1 252 ? -9.967  19.758  52.963 1.00 18.20  ? 253  ILE A CG1   1 
ATOM   1870 C  CG2   . ILE A 1 252 ? -7.870  19.912  51.578 1.00 20.85  ? 253  ILE A CG2   1 
ATOM   1871 C  CD1   . ILE A 1 252 ? -9.741  18.306  53.207 1.00 28.51  ? 253  ILE A CD1   1 
ATOM   1872 N  N     . GLU A 1 253 ? -11.789 21.082  49.981 1.00 15.59  ? 254  GLU A N     1 
ATOM   1873 C  CA    . GLU A 1 253 ? -13.226 21.036  49.831 1.00 14.94  ? 254  GLU A CA    1 
ATOM   1874 C  C     . GLU A 1 253 ? -13.759 19.651  50.151 1.00 15.84  ? 254  GLU A C     1 
ATOM   1875 O  O     . GLU A 1 253 ? -13.106 18.648  49.835 1.00 15.29  ? 254  GLU A O     1 
ATOM   1876 C  CB    . GLU A 1 253 ? -13.663 21.398  48.399 1.00 17.53  ? 254  GLU A CB    1 
ATOM   1877 C  CG    . GLU A 1 253 ? -13.768 22.916  48.223 1.00 19.71  ? 254  GLU A CG    1 
ATOM   1878 C  CD    . GLU A 1 253 ? -14.181 23.311  46.813 1.00 21.57  ? 254  GLU A CD    1 
ATOM   1879 O  OE1   . GLU A 1 253 ? -13.964 22.543  45.843 1.00 20.09  ? 254  GLU A OE1   1 
ATOM   1880 O  OE2   . GLU A 1 253 ? -14.783 24.425  46.711 1.00 20.07  ? 254  GLU A OE2   1 
ATOM   1881 N  N     . ILE A 1 254 ? -14.975 19.634  50.673 1.00 14.61  ? 255  ILE A N     1 
ATOM   1882 C  CA    . ILE A 1 254 ? -15.790 18.420  50.846 1.00 14.82  ? 255  ILE A CA    1 
ATOM   1883 C  C     . ILE A 1 254 ? -16.800 18.432  49.705 1.00 14.41  ? 255  ILE A C     1 
ATOM   1884 O  O     . ILE A 1 254 ? -17.610 19.378  49.611 1.00 15.88  ? 255  ILE A O     1 
ATOM   1885 C  CB    . ILE A 1 254 ? -16.497 18.417  52.212 1.00 15.02  ? 255  ILE A CB    1 
ATOM   1886 C  CG1   . ILE A 1 254 ? -15.445 18.563  53.315 1.00 16.49  ? 255  ILE A CG1   1 
ATOM   1887 C  CG2   . ILE A 1 254 ? -17.321 17.134  52.386 1.00 17.24  ? 255  ILE A CG2   1 
ATOM   1888 C  CD1   . ILE A 1 254 ? -16.122 18.953  54.687 1.00 20.55  ? 255  ILE A CD1   1 
ATOM   1889 N  N     . VAL A 1 255 ? -16.738 17.447  48.806 1.00 13.27  ? 256  VAL A N     1 
ATOM   1890 C  CA    . VAL A 1 255 ? -17.524 17.485  47.575 1.00 14.76  ? 256  VAL A CA    1 
ATOM   1891 C  C     . VAL A 1 255 ? -18.418 16.267  47.522 1.00 14.71  ? 256  VAL A C     1 
ATOM   1892 O  O     . VAL A 1 255 ? -17.964 15.130  47.759 1.00 15.14  ? 256  VAL A O     1 
ATOM   1893 C  CB    . VAL A 1 255 ? -16.581 17.511  46.361 1.00 12.98  ? 256  VAL A CB    1 
ATOM   1894 C  CG1   . VAL A 1 255 ? -17.431 17.659  45.061 1.00 15.09  ? 256  VAL A CG1   1 
ATOM   1895 C  CG2   . VAL A 1 255 ? -15.544 18.699  46.419 1.00 17.16  ? 256  VAL A CG2   1 
ATOM   1896 N  N     . GLY A 1 256 ? -19.669 16.505  47.132 1.00 13.40  ? 257  GLY A N     1 
ATOM   1897 C  CA    . GLY A 1 256 ? -20.667 15.451  46.929 1.00 15.06  ? 257  GLY A CA    1 
ATOM   1898 C  C     . GLY A 1 256 ? -21.676 15.449  48.036 1.00 16.39  ? 257  GLY A C     1 
ATOM   1899 O  O     . GLY A 1 256 ? -21.378 15.793  49.178 1.00 17.85  ? 257  GLY A O     1 
ATOM   1900 N  N     . LEU A 1 257 ? -22.923 15.063  47.690 1.00 16.24  ? 258  LEU A N     1 
ATOM   1901 C  CA    . LEU A 1 257 ? -24.076 14.758  48.542 1.00 17.24  ? 258  LEU A CA    1 
ATOM   1902 C  C     . LEU A 1 257 ? -24.698 15.927  49.295 1.00 23.58  ? 258  LEU A C     1 
ATOM   1903 O  O     . LEU A 1 257 ? -25.925 16.084  49.305 1.00 26.42  ? 258  LEU A O     1 
ATOM   1904 C  CB    . LEU A 1 257 ? -23.715 13.692  49.608 1.00 19.81  ? 258  LEU A CB    1 
ATOM   1905 C  CG    . LEU A 1 257 ? -23.344 12.315  49.008 1.00 20.10  ? 258  LEU A CG    1 
ATOM   1906 C  CD1   . LEU A 1 257 ? -24.515 11.730  48.145 1.00 24.19  ? 258  LEU A CD1   1 
ATOM   1907 C  CD2   . LEU A 1 257 ? -22.019 12.182  48.318 1.00 31.38  ? 258  LEU A CD2   1 
ATOM   1908 N  N     . ARG A 1 258 ? -23.880 16.853  49.749 1.00 18.21  ? 259  ARG A N     1 
ATOM   1909 C  CA    . ARG A 1 258 ? -24.314 18.105  50.316 1.00 17.63  ? 259  ARG A CA    1 
ATOM   1910 C  C     . ARG A 1 258 ? -23.614 19.202  49.536 1.00 17.33  ? 259  ARG A C     1 
ATOM   1911 O  O     . ARG A 1 258 ? -22.658 18.939  48.799 1.00 20.14  ? 259  ARG A O     1 
ATOM   1912 C  CB    . ARG A 1 258 ? -23.928 18.203  51.783 1.00 19.94  ? 259  ARG A CB    1 
ATOM   1913 C  CG    . ARG A 1 258 ? -24.625 17.159  52.660 1.00 22.96  ? 259  ARG A CG    1 
ATOM   1914 C  CD    . ARG A 1 258 ? -24.232 17.431  54.142 1.00 26.21  ? 259  ARG A CD    1 
ATOM   1915 N  NE    . ARG A 1 258 ? -24.821 16.433  55.028 1.00 37.35  ? 259  ARG A NE    1 
ATOM   1916 C  CZ    . ARG A 1 258 ? -25.981 16.589  55.649 1.00 46.58  ? 259  ARG A CZ    1 
ATOM   1917 N  NH1   . ARG A 1 258 ? -26.672 17.721  55.495 1.00 40.96  ? 259  ARG A NH1   1 
ATOM   1918 N  NH2   . ARG A 1 258 ? -26.440 15.613  56.420 1.00 40.00  ? 259  ARG A NH2   1 
ATOM   1919 N  N     . ASP A 1 259 ? -24.070 20.437  49.731 1.00 19.78  ? 260  ASP A N     1 
ATOM   1920 C  CA    . ASP A 1 259 ? -23.411 21.548  49.041 1.00 21.70  ? 260  ASP A CA    1 
ATOM   1921 C  C     . ASP A 1 259 ? -21.915 21.519  49.347 1.00 17.39  ? 260  ASP A C     1 
ATOM   1922 O  O     . ASP A 1 259 ? -21.507 21.268  50.479 1.00 19.88  ? 260  ASP A O     1 
ATOM   1923 C  CB    . ASP A 1 259 ? -23.984 22.892  49.515 1.00 23.37  ? 260  ASP A CB    1 
ATOM   1924 C  CG    . ASP A 1 259 ? -25.428 23.115  49.079 1.00 32.54  ? 260  ASP A CG    1 
ATOM   1925 O  OD1   . ASP A 1 259 ? -25.880 22.455  48.134 1.00 35.42  ? 260  ASP A OD1   1 
ATOM   1926 O  OD2   . ASP A 1 259 ? -26.078 23.987  49.696 1.00 43.79  ? 260  ASP A OD2   1 
ATOM   1927 N  N     . THR A 1 260 ? -21.096 21.815  48.341 1.00 17.15  ? 261  THR A N     1 
ATOM   1928 C  CA    . THR A 1 260 ? -19.650 21.882  48.529 1.00 14.90  ? 261  THR A CA    1 
ATOM   1929 C  C     . THR A 1 260 ? -19.314 22.890  49.608 1.00 17.79  ? 261  THR A C     1 
ATOM   1930 O  O     . THR A 1 260 ? -19.841 24.021  49.604 1.00 20.79  ? 261  THR A O     1 
ATOM   1931 C  CB    . THR A 1 260 ? -18.979 22.279  47.236 1.00 15.75  ? 261  THR A CB    1 
ATOM   1932 O  OG1   . THR A 1 260 ? -19.280 21.287  46.245 1.00 17.03  ? 261  THR A OG1   1 
ATOM   1933 C  CG2   . THR A 1 260 ? -17.478 22.295  47.426 1.00 17.48  ? 261  THR A CG2   1 
ATOM   1934 N  N     . ARG A 1 261 ? -18.391 22.498  50.498 1.00 16.40  ? 262  ARG A N     1 
ATOM   1935 C  CA    . ARG A 1 261 ? -17.954 23.318  51.613 1.00 18.08  ? 262  ARG A CA    1 
ATOM   1936 C  C     . ARG A 1 261 ? -16.451 23.221  51.759 1.00 18.43  ? 262  ARG A C     1 
ATOM   1937 O  O     . ARG A 1 261 ? -15.844 22.209  51.402 1.00 21.56  ? 262  ARG A O     1 
ATOM   1938 C  CB    . ARG A 1 261 ? -18.645 22.814  52.868 1.00 24.34  ? 262  ARG A CB    1 
ATOM   1939 C  CG    . ARG A 1 261 ? -18.453 23.577  54.091 1.00 48.00  ? 262  ARG A CG    1 
ATOM   1940 C  CD    . ARG A 1 261 ? -19.265 22.857  55.134 1.00 49.00  ? 262  ARG A CD    1 
ATOM   1941 N  NE    . ARG A 1 261 ? -19.140 23.471  56.439 1.00 55.59  ? 262  ARG A NE    1 
ATOM   1942 C  CZ    . ARG A 1 261 ? -19.868 23.074  57.463 1.00 60.37  ? 262  ARG A CZ    1 
ATOM   1943 N  NH1   . ARG A 1 261 ? -20.748 22.093  57.268 1.00 54.12  ? 262  ARG A NH1   1 
ATOM   1944 N  NH2   . ARG A 1 261 ? -19.727 23.647  58.653 1.00 68.45  ? 262  ARG A NH2   1 
ATOM   1945 N  N     . SER A 1 262 ? -15.832 24.275  52.281 1.00 16.53  ? 263  SER A N     1 
ATOM   1946 C  CA    . SER A 1 262 ? -14.390 24.229  52.482 1.00 15.31  ? 263  SER A CA    1 
ATOM   1947 C  C     . SER A 1 262 ? -14.074 24.190  53.964 1.00 18.28  ? 263  SER A C     1 
ATOM   1948 O  O     . SER A 1 262 ? -14.882 24.613  54.781 1.00 24.23  ? 263  SER A O     1 
ATOM   1949 C  CB    . SER A 1 262 ? -13.671 25.357  51.745 1.00 22.90  ? 263  SER A CB    1 
ATOM   1950 O  OG    . SER A 1 262 ? -14.188 26.605  52.100 1.00 34.09  ? 263  SER A OG    1 
ATOM   1951 N  N     . THR A 1 263 ? -12.929 23.595  54.279 1.00 18.02  ? 264  THR A N     1 
ATOM   1952 C  CA    . THR A 1 263 ? -12.497 23.403  55.685 1.00 19.65  ? 264  THR A CA    1 
ATOM   1953 C  C     . THR A 1 263 ? -10.988 23.460  55.666 1.00 16.84  ? 264  THR A C     1 
ATOM   1954 O  O     . THR A 1 263 ? -10.360 23.132  54.665 1.00 18.43  ? 264  THR A O     1 
ATOM   1955 C  CB    . THR A 1 263 ? -12.961 21.987  56.232 1.00 23.29  ? 264  THR A CB    1 
ATOM   1956 O  OG1   . THR A 1 263 ? -12.451 21.652  57.526 1.00 28.87  ? 264  THR A OG1   1 
ATOM   1957 C  CG2   . THR A 1 263 ? -12.548 20.830  55.319 1.00 27.01  ? 264  THR A CG2   1 
ATOM   1958 N  N     . THR A 1 264 ? -10.391 23.750  56.832 1.00 18.61  ? 265  THR A N     1 
ATOM   1959 C  CA    . THR A 1 264 ? -8.948  23.642  56.983 1.00 19.19  ? 265  THR A CA    1 
ATOM   1960 C  C     . THR A 1 264 ? -8.585  22.291  57.590 1.00 19.04  ? 265  THR A C     1 
ATOM   1961 O  O     . THR A 1 264 ? -9.216  21.855  58.557 1.00 21.85  ? 265  THR A O     1 
ATOM   1962 C  CB    . THR A 1 264 ? -8.462  24.741  57.922 1.00 23.99  ? 265  THR A CB    1 
ATOM   1963 O  OG1   . THR A 1 264 ? -8.891  26.024  57.399 1.00 26.28  ? 265  THR A OG1   1 
ATOM   1964 C  CG2   . THR A 1 264 ? -6.959  24.733  58.039 1.00 23.92  ? 265  THR A CG2   1 
ATOM   1965 N  N     . VAL A 1 265 ? -7.578  21.648  57.008 1.00 18.66  ? 266  VAL A N     1 
ATOM   1966 C  CA    . VAL A 1 265 ? -7.010  20.422  57.591 1.00 18.14  ? 266  VAL A CA    1 
ATOM   1967 C  C     . VAL A 1 265 ? -6.070  20.823  58.715 1.00 21.12  ? 266  VAL A C     1 
ATOM   1968 O  O     . VAL A 1 265 ? -5.092  21.545  58.486 1.00 25.24  ? 266  VAL A O     1 
ATOM   1969 C  CB    . VAL A 1 265 ? -6.279  19.607  56.535 1.00 18.08  ? 266  VAL A CB    1 
ATOM   1970 C  CG1   . VAL A 1 265 ? -5.587  18.378  57.143 1.00 20.49  ? 266  VAL A CG1   1 
ATOM   1971 C  CG2   . VAL A 1 265 ? -7.240  19.192  55.476 1.00 21.23  ? 266  VAL A CG2   1 
ATOM   1972 N  N     . THR A 1 266 ? -6.394  20.414  59.938 1.00 17.44  ? 267  THR A N     1 
ATOM   1973 C  CA    . THR A 1 266 ? -5.577  20.813  61.077 1.00 18.46  ? 267  THR A CA    1 
ATOM   1974 C  C     . THR A 1 266 ? -4.798  19.652  61.669 1.00 20.63  ? 267  THR A C     1 
ATOM   1975 O  O     . THR A 1 266 ? -4.086  19.858  62.694 1.00 24.74  ? 267  THR A O     1 
ATOM   1976 C  CB    . THR A 1 266 ? -6.459  21.452  62.122 1.00 24.41  ? 267  THR A CB    1 
ATOM   1977 O  OG1   . THR A 1 266 ? -7.490  20.546  62.464 1.00 27.80  ? 267  THR A OG1   1 
ATOM   1978 C  CG2   . THR A 1 266 ? -7.141  22.762  61.595 1.00 23.65  ? 267  THR A CG2   1 
ATOM   1979 N  N     . GLY A 1 267 ? -4.872  18.474  61.074 1.00 20.58  ? 268  GLY A N     1 
ATOM   1980 C  CA    . GLY A 1 267 ? -4.066  17.340  61.517 1.00 17.95  ? 268  GLY A CA    1 
ATOM   1981 C  C     . GLY A 1 267 ? -4.079  16.227  60.505 1.00 16.92  ? 268  GLY A C     1 
ATOM   1982 O  O     . GLY A 1 267 ? -5.077  16.038  59.801 1.00 18.38  ? 268  GLY A O     1 
ATOM   1983 N  N     . VAL A 1 268 ? -2.991  15.498  60.413 1.00 19.67  ? 269  VAL A N     1 
ATOM   1984 C  CA    . VAL A 1 268 ? -2.811  14.325  59.559 1.00 19.95  ? 269  VAL A CA    1 
ATOM   1985 C  C     . VAL A 1 268 ? -2.241  13.227  60.429 1.00 21.72  ? 269  VAL A C     1 
ATOM   1986 O  O     . VAL A 1 268 ? -1.176  13.416  61.042 1.00 23.60  ? 269  VAL A O     1 
ATOM   1987 C  CB    . VAL A 1 268 ? -1.879  14.577  58.370 1.00 20.86  ? 269  VAL A CB    1 
ATOM   1988 C  CG1   . VAL A 1 268 ? -1.782  13.301  57.526 1.00 21.27  ? 269  VAL A CG1   1 
ATOM   1989 C  CG2   . VAL A 1 268 ? -2.363  15.795  57.523 1.00 21.45  ? 269  VAL A CG2   1 
ATOM   1990 N  N     . GLU A 1 269 ? -2.930  12.090  60.490 1.00 17.78  ? 270  GLU A N     1 
ATOM   1991 C  CA    . GLU A 1 269 ? -2.508  11.004  61.362 1.00 18.03  ? 270  GLU A CA    1 
ATOM   1992 C  C     . GLU A 1 269 ? -2.487  9.684   60.617 1.00 19.68  ? 270  GLU A C     1 
ATOM   1993 O  O     . GLU A 1 269 ? -3.340  9.425   59.763 1.00 19.18  ? 270  GLU A O     1 
ATOM   1994 C  CB    . GLU A 1 269 ? -3.440  10.906  62.574 1.00 22.87  ? 270  GLU A CB    1 
ATOM   1995 C  CG    . GLU A 1 269 ? -2.986  9.891   63.633 1.00 41.43  ? 270  GLU A CG    1 
ATOM   1996 C  CD    . GLU A 1 269 ? -3.776  10.020  64.932 1.00 59.85  ? 270  GLU A CD    1 
ATOM   1997 O  OE1   . GLU A 1 269 ? -4.551  10.986  65.067 1.00 74.12  ? 270  GLU A OE1   1 
ATOM   1998 O  OE2   . GLU A 1 269 ? -3.653  9.147   65.801 1.00 72.24  ? 270  GLU A OE2   1 
ATOM   1999 N  N     . MET A 1 270 ? -1.464  8.860   60.909 1.00 20.81  ? 271  MET A N     1 
ATOM   2000 C  CA    . MET A 1 270 ? -1.412  7.460   60.497 1.00 20.05  ? 271  MET A CA    1 
ATOM   2001 C  C     . MET A 1 270 ? -1.083  6.672   61.755 1.00 18.42  ? 271  MET A C     1 
ATOM   2002 O  O     . MET A 1 270 ? -0.823  7.269   62.792 1.00 19.98  ? 271  MET A O     1 
ATOM   2003 C  CB    . MET A 1 270 ? -0.371  7.196   59.396 1.00 23.49  ? 271  MET A CB    1 
ATOM   2004 C  CG    . MET A 1 270 ? -0.728  7.958   58.153 1.00 20.33  ? 271  MET A CG    1 
ATOM   2005 S  SD    . MET A 1 270 ? 0.512   7.712   56.811 1.00 23.97  ? 271  MET A SD    1 
ATOM   2006 C  CE    . MET A 1 270 ? 0.262   6.055   56.386 1.00 23.49  ? 271  MET A CE    1 
ATOM   2007 N  N     . PHE A 1 271 ? -1.103  5.344   61.668 1.00 18.90  ? 272  PHE A N     1 
ATOM   2008 C  CA    . PHE A 1 271 ? -0.821  4.546   62.871 1.00 18.19  ? 272  PHE A CA    1 
ATOM   2009 C  C     . PHE A 1 271 ? 0.537   4.929   63.441 1.00 21.36  ? 272  PHE A C     1 
ATOM   2010 O  O     . PHE A 1 271 ? 1.553   4.825   62.750 1.00 25.52  ? 272  PHE A O     1 
ATOM   2011 C  CB    . PHE A 1 271 ? -0.885  3.055   62.550 1.00 21.08  ? 272  PHE A CB    1 
ATOM   2012 C  CG    . PHE A 1 271 ? -0.633  2.158   63.716 1.00 24.00  ? 272  PHE A CG    1 
ATOM   2013 C  CD1   . PHE A 1 271 ? -1.443  2.219   64.802 1.00 25.37  ? 272  PHE A CD1   1 
ATOM   2014 C  CD2   . PHE A 1 271 ? 0.368   1.196   63.633 1.00 23.77  ? 272  PHE A CD2   1 
ATOM   2015 C  CE1   . PHE A 1 271 ? -1.194  1.367   65.881 1.00 32.76  ? 272  PHE A CE1   1 
ATOM   2016 C  CE2   . PHE A 1 271 ? 0.613   0.358   64.689 1.00 26.54  ? 272  PHE A CE2   1 
ATOM   2017 C  CZ    . PHE A 1 271 ? -0.189  0.464   65.792 1.00 28.54  ? 272  PHE A CZ    1 
ATOM   2018 N  N     . GLN A 1 272 ? 0.544   5.368   64.694 1.00 22.32  ? 273  GLN A N     1 
ATOM   2019 C  CA    . GLN A 1 272 ? 1.773   5.661   65.409 1.00 25.62  ? 273  GLN A CA    1 
ATOM   2020 C  C     . GLN A 1 272 ? 2.535   6.844   64.802 1.00 26.92  ? 273  GLN A C     1 
ATOM   2021 O  O     . GLN A 1 272 ? 3.732   7.014   65.066 1.00 34.81  ? 273  GLN A O     1 
ATOM   2022 C  CB    . GLN A 1 272 ? 2.659   4.394   65.516 1.00 28.53  ? 273  GLN A CB    1 
ATOM   2023 C  CG    . GLN A 1 272 ? 2.037   3.303   66.441 1.00 23.52  ? 273  GLN A CG    1 
ATOM   2024 C  CD    . GLN A 1 272 ? 2.912   2.066   66.591 1.00 32.93  ? 273  GLN A CD    1 
ATOM   2025 O  OE1   . GLN A 1 272 ? 3.854   1.845   65.819 1.00 45.41  ? 273  GLN A OE1   1 
ATOM   2026 N  NE2   . GLN A 1 272 ? 2.628   1.271   67.617 1.00 29.36  ? 273  GLN A NE2   1 
ATOM   2027 N  N     . LYS A 1 273 ? 1.871   7.716   64.031 1.00 24.01  ? 274  LYS A N     1 
ATOM   2028 C  CA    . LYS A 1 273 ? 2.547   8.853   63.405 1.00 28.03  ? 274  LYS A CA    1 
ATOM   2029 C  C     . LYS A 1 273 ? 1.627   10.063  63.388 1.00 23.92  ? 274  LYS A C     1 
ATOM   2030 O  O     . LYS A 1 273 ? 0.472   9.968   62.934 1.00 26.54  ? 274  LYS A O     1 
ATOM   2031 C  CB    . LYS A 1 273 ? 2.933   8.529   61.954 1.00 28.53  ? 274  LYS A CB    1 
ATOM   2032 C  CG    . LYS A 1 273 ? 3.914   7.391   61.769 1.00 39.13  ? 274  LYS A CG    1 
ATOM   2033 C  CD    . LYS A 1 273 ? 4.004   6.940   60.312 1.00 54.33  ? 274  LYS A CD    1 
ATOM   2034 C  CE    . LYS A 1 273 ? 4.722   7.942   59.416 1.00 71.33  ? 274  LYS A CE    1 
ATOM   2035 N  NZ    . LYS A 1 273 ? 4.903   7.426   58.013 1.00 79.13  ? 274  LYS A NZ    1 
ATOM   2036 N  N     . THR A 1 274 ? 2.148   11.192  63.811 1.00 24.56  ? 275  THR A N     1 
ATOM   2037 C  CA    . THR A 1 274 ? 1.546   12.506  63.622 1.00 28.40  ? 275  THR A CA    1 
ATOM   2038 C  C     . THR A 1 274 ? 2.318   13.230  62.507 1.00 26.73  ? 275  THR A C     1 
ATOM   2039 O  O     . THR A 1 274 ? 3.527   13.452  62.627 1.00 32.56  ? 275  THR A O     1 
ATOM   2040 C  CB    . THR A 1 274 ? 1.591   13.251  64.974 1.00 32.63  ? 275  THR A CB    1 
ATOM   2041 O  OG1   . THR A 1 274 ? 1.014   14.559  64.853 1.00 41.97  ? 275  THR A OG1   1 
ATOM   2042 C  CG2   . THR A 1 274 ? 3.006   13.369  65.506 1.00 55.72  ? 275  THR A CG2   1 
ATOM   2043 N  N     . LEU A 1 275 ? 1.644   13.595  61.413 1.00 24.20  ? 276  LEU A N     1 
ATOM   2044 C  CA    . LEU A 1 275 ? 2.342   13.997  60.185 1.00 25.39  ? 276  LEU A CA    1 
ATOM   2045 C  C     . LEU A 1 275 ? 1.983   15.438  59.860 1.00 26.20  ? 276  LEU A C     1 
ATOM   2046 O  O     . LEU A 1 275 ? 0.917   15.925  60.247 1.00 29.73  ? 276  LEU A O     1 
ATOM   2047 C  CB    . LEU A 1 275 ? 1.958   13.112  59.010 1.00 28.04  ? 276  LEU A CB    1 
ATOM   2048 C  CG    . LEU A 1 275 ? 2.207   11.622  59.197 1.00 32.32  ? 276  LEU A CG    1 
ATOM   2049 C  CD1   . LEU A 1 275 ? 1.585   10.871  58.028 1.00 37.53  ? 276  LEU A CD1   1 
ATOM   2050 C  CD2   . LEU A 1 275 ? 3.680   11.333  59.292 1.00 34.85  ? 276  LEU A CD2   1 
ATOM   2051 N  N     . ASP A 1 276 ? 2.875   16.112  59.127 1.00 21.91  ? 277  ASP A N     1 
ATOM   2052 C  CA    . ASP A 1 276 ? 2.515   17.411  58.546 1.00 25.76  ? 277  ASP A CA    1 
ATOM   2053 C  C     . ASP A 1 276 ? 1.854   17.281  57.186 1.00 23.12  ? 277  ASP A C     1 
ATOM   2054 O  O     . ASP A 1 276 ? 1.123   18.202  56.760 1.00 26.19  ? 277  ASP A O     1 
ATOM   2055 C  CB    . ASP A 1 276 ? 3.761   18.294  58.400 1.00 29.62  ? 277  ASP A CB    1 
ATOM   2056 C  CG    . ASP A 1 276 ? 3.415   19.706  57.943 1.00 47.43  ? 277  ASP A CG    1 
ATOM   2057 O  OD1   . ASP A 1 276 ? 2.769   20.435  58.721 1.00 50.86  ? 277  ASP A OD1   1 
ATOM   2058 O  OD2   . ASP A 1 276 ? 3.788   20.084  56.810 1.00 57.69  ? 277  ASP A OD2   1 
ATOM   2059 N  N     . GLU A 1 277 ? 2.018   16.149  56.532 1.00 22.49  ? 278  GLU A N     1 
ATOM   2060 C  CA    . GLU A 1 277 ? 1.724   15.944  55.120 1.00 29.51  ? 278  GLU A CA    1 
ATOM   2061 C  C     . GLU A 1 277 ? 1.202   14.523  54.969 1.00 25.19  ? 278  GLU A C     1 
ATOM   2062 O  O     . GLU A 1 277 ? 1.844   13.575  55.431 1.00 26.33  ? 278  GLU A O     1 
ATOM   2063 C  CB    . GLU A 1 277 ? 3.036   16.082  54.346 1.00 48.68  ? 278  GLU A CB    1 
ATOM   2064 C  CG    . GLU A 1 277 ? 3.100   15.766  52.875 1.00 63.81  ? 278  GLU A CG    1 
ATOM   2065 C  CD    . GLU A 1 277 ? 3.243   16.973  51.988 1.00 71.30  ? 278  GLU A CD    1 
ATOM   2066 O  OE1   . GLU A 1 277 ? 3.699   18.016  52.486 1.00 77.19  ? 278  GLU A OE1   1 
ATOM   2067 O  OE2   . GLU A 1 277 ? 3.008   16.855  50.772 1.00 72.35  ? 278  GLU A OE2   1 
ATOM   2068 N  N     . GLY A 1 278 ? 0.055   14.335  54.330 1.00 20.31  ? 279  GLY A N     1 
ATOM   2069 C  CA    . GLY A 1 278 ? -0.322  13.033  53.825 1.00 20.16  ? 279  GLY A CA    1 
ATOM   2070 C  C     . GLY A 1 278 ? -0.120  12.930  52.315 1.00 19.88  ? 279  GLY A C     1 
ATOM   2071 O  O     . GLY A 1 278 ? -0.353  13.899  51.592 1.00 22.34  ? 279  GLY A O     1 
ATOM   2072 N  N     . LEU A 1 279 ? 0.328   11.767  51.860 1.00 19.21  ? 280  LEU A N     1 
ATOM   2073 C  CA    . LEU A 1 279 ? 0.658   11.582  50.435 1.00 19.24  ? 280  LEU A CA    1 
ATOM   2074 C  C     . LEU A 1 279 ? -0.214  10.531  49.783 1.00 20.92  ? 280  LEU A C     1 
ATOM   2075 O  O     . LEU A 1 279 ? -0.667  9.589   50.427 1.00 20.58  ? 280  LEU A O     1 
ATOM   2076 C  CB    . LEU A 1 279 ? 2.149   11.148  50.319 1.00 23.64  ? 280  LEU A CB    1 
ATOM   2077 C  CG    . LEU A 1 279 ? 3.179   12.047  50.999 1.00 26.35  ? 280  LEU A CG    1 
ATOM   2078 C  CD1   . LEU A 1 279 ? 4.588   11.439  50.843 1.00 32.11  ? 280  LEU A CD1   1 
ATOM   2079 C  CD2   . LEU A 1 279 ? 3.165   13.438  50.436 1.00 26.88  ? 280  LEU A CD2   1 
ATOM   2080 N  N     . ALA A 1 280 ? -0.357  10.617  48.438 1.00 18.51  ? 281  ALA A N     1 
ATOM   2081 C  CA    . ALA A 1 280 ? -1.004  9.590   47.668 1.00 18.95  ? 281  ALA A CA    1 
ATOM   2082 C  C     . ALA A 1 280 ? -0.562  8.206   48.069 1.00 19.91  ? 281  ALA A C     1 
ATOM   2083 O  O     . ALA A 1 280 ? 0.641   7.947   48.175 1.00 24.13  ? 281  ALA A O     1 
ATOM   2084 C  CB    . ALA A 1 280 ? -0.690  9.834   46.181 1.00 21.04  ? 281  ALA A CB    1 
ATOM   2085 N  N     . GLY A 1 281 ? -1.535  7.321   48.271 1.00 21.73  ? 282  GLY A N     1 
ATOM   2086 C  CA    . GLY A 1 281 ? -1.307  5.961   48.711 1.00 24.58  ? 282  GLY A CA    1 
ATOM   2087 C  C     . GLY A 1 281 ? -1.457  5.767   50.204 1.00 24.44  ? 282  GLY A C     1 
ATOM   2088 O  O     . GLY A 1 281 ? -1.643  4.602   50.632 1.00 31.01  ? 282  GLY A O     1 
ATOM   2089 N  N     . ASP A 1 282 ? -1.311  6.833   51.000 1.00 21.98  ? 283  ASP A N     1 
ATOM   2090 C  CA    . ASP A 1 282 ? -1.331  6.752   52.474 1.00 19.03  ? 283  ASP A CA    1 
ATOM   2091 C  C     . ASP A 1 282 ? -2.793  6.578   52.919 1.00 21.83  ? 283  ASP A C     1 
ATOM   2092 O  O     . ASP A 1 282 ? -3.690  7.300   52.469 1.00 20.51  ? 283  ASP A O     1 
ATOM   2093 C  CB    . ASP A 1 282 ? -0.817  8.020   53.144 1.00 20.77  ? 283  ASP A CB    1 
ATOM   2094 C  CG    . ASP A 1 282 ? 0.700   8.269   53.048 1.00 28.60  ? 283  ASP A CG    1 
ATOM   2095 O  OD1   . ASP A 1 282 ? 1.415   7.291   52.801 1.00 26.59  ? 283  ASP A OD1   1 
ATOM   2096 O  OD2   . ASP A 1 282 ? 1.160   9.411   53.391 1.00 26.19  ? 283  ASP A OD2   1 
ATOM   2097 N  N     . ASN A 1 283 ? -3.019  5.670   53.873 1.00 22.48  ? 284  ASN A N     1 
ATOM   2098 C  CA    . ASN A 1 283 ? -4.267  5.603   54.628 1.00 23.70  ? 284  ASN A CA    1 
ATOM   2099 C  C     . ASN A 1 283 ? -4.107  6.549   55.802 1.00 19.83  ? 284  ASN A C     1 
ATOM   2100 O  O     . ASN A 1 283 ? -3.158  6.433   56.582 1.00 22.19  ? 284  ASN A O     1 
ATOM   2101 C  CB    . ASN A 1 283 ? -4.493  4.194   55.153 1.00 23.92  ? 284  ASN A CB    1 
ATOM   2102 C  CG    . ASN A 1 283 ? -4.716  3.219   54.060 1.00 34.15  ? 284  ASN A CG    1 
ATOM   2103 O  OD1   . ASN A 1 283 ? -3.824  2.430   53.721 1.00 50.35  ? 284  ASN A OD1   1 
ATOM   2104 N  ND2   . ASN A 1 283 ? -5.909  3.223   53.528 1.00 33.05  ? 284  ASN A ND2   1 
ATOM   2105 N  N     . VAL A 1 284 ? -4.985  7.550   55.894 1.00 18.52  ? 285  VAL A N     1 
ATOM   2106 C  CA    . VAL A 1 284 ? -4.808  8.624   56.851 1.00 17.06  ? 285  VAL A CA    1 
ATOM   2107 C  C     . VAL A 1 284 ? -6.102  8.918   57.579 1.00 18.25  ? 285  VAL A C     1 
ATOM   2108 O  O     . VAL A 1 284 ? -7.195  8.551   57.126 1.00 18.72  ? 285  VAL A O     1 
ATOM   2109 C  CB    . VAL A 1 284 ? -4.323  9.932   56.180 1.00 17.97  ? 285  VAL A CB    1 
ATOM   2110 C  CG1   . VAL A 1 284 ? -2.982  9.702   55.540 1.00 21.20  ? 285  VAL A CG1   1 
ATOM   2111 C  CG2   . VAL A 1 284 ? -5.384  10.470  55.159 1.00 17.88  ? 285  VAL A CG2   1 
ATOM   2112 N  N     . GLY A 1 285 ? -5.966  9.617   58.689 1.00 17.02  ? 286  GLY A N     1 
ATOM   2113 C  CA    . GLY A 1 285 ? -7.049  10.326  59.334 1.00 18.94  ? 286  GLY A CA    1 
ATOM   2114 C  C     . GLY A 1 285 ? -6.768  11.810  59.272 1.00 18.10  ? 286  GLY A C     1 
ATOM   2115 O  O     . GLY A 1 285 ? -5.702  12.251  59.700 1.00 20.65  ? 286  GLY A O     1 
ATOM   2116 N  N     . LEU A 1 286 ? -7.693  12.592  58.715 1.00 16.69  ? 287  LEU A N     1 
ATOM   2117 C  CA    . LEU A 1 286 ? -7.533  14.026  58.572 1.00 16.05  ? 287  LEU A CA    1 
ATOM   2118 C  C     . LEU A 1 286 ? -8.492  14.727  59.521 1.00 15.16  ? 287  LEU A C     1 
ATOM   2119 O  O     . LEU A 1 286 ? -9.701  14.493  59.472 1.00 16.38  ? 287  LEU A O     1 
ATOM   2120 C  CB    . LEU A 1 286 ? -7.842  14.494  57.134 1.00 15.65  ? 287  LEU A CB    1 
ATOM   2121 C  CG    . LEU A 1 286 ? -6.998  13.814  56.081 1.00 17.13  ? 287  LEU A CG    1 
ATOM   2122 C  CD1   . LEU A 1 286 ? -7.343  14.323  54.666 1.00 20.15  ? 287  LEU A CD1   1 
ATOM   2123 C  CD2   . LEU A 1 286 ? -5.502  14.085  56.361 1.00 21.71  ? 287  LEU A CD2   1 
ATOM   2124 N  N     . LEU A 1 287 ? -7.968  15.620  60.344 1.00 16.55  ? 288  LEU A N     1 
ATOM   2125 C  CA    . LEU A 1 287 ? -8.792  16.439  61.235 1.00 17.90  ? 288  LEU A CA    1 
ATOM   2126 C  C     . LEU A 1 287 ? -9.297  17.649  60.462 1.00 17.87  ? 288  LEU A C     1 
ATOM   2127 O  O     . LEU A 1 287 ? -8.479  18.405  59.934 1.00 18.96  ? 288  LEU A O     1 
ATOM   2128 C  CB    . LEU A 1 287 ? -7.980  16.858  62.485 1.00 20.11  ? 288  LEU A CB    1 
ATOM   2129 C  CG    . LEU A 1 287 ? -8.832  17.723  63.451 1.00 26.47  ? 288  LEU A CG    1 
ATOM   2130 C  CD1   . LEU A 1 287 ? -10.176 17.076  63.882 1.00 28.69  ? 288  LEU A CD1   1 
ATOM   2131 C  CD2   . LEU A 1 287 ? -7.975  18.081  64.678 1.00 27.91  ? 288  LEU A CD2   1 
ATOM   2132 N  N     . LEU A 1 288 ? -10.614 17.785  60.372 1.00 16.48  ? 289  LEU A N     1 
ATOM   2133 C  CA    . LEU A 1 288 ? -11.269 18.822  59.559 1.00 16.97  ? 289  LEU A CA    1 
ATOM   2134 C  C     . LEU A 1 288 ? -11.895 19.847  60.494 1.00 18.55  ? 289  LEU A C     1 
ATOM   2135 O  O     . LEU A 1 288 ? -12.912 19.563  61.151 1.00 21.69  ? 289  LEU A O     1 
ATOM   2136 C  CB    . LEU A 1 288 ? -12.328 18.220  58.638 1.00 17.66  ? 289  LEU A CB    1 
ATOM   2137 C  CG    . LEU A 1 288 ? -11.757 17.103  57.737 1.00 17.26  ? 289  LEU A CG    1 
ATOM   2138 C  CD1   . LEU A 1 288 ? -12.876 16.588  56.901 1.00 19.76  ? 289  LEU A CD1   1 
ATOM   2139 C  CD2   . LEU A 1 288 ? -10.562 17.529  56.873 1.00 19.13  ? 289  LEU A CD2   1 
ATOM   2140 N  N     . ARG A 1 289 ? -11.348 21.065  60.446 1.00 18.03  ? 290  ARG A N     1 
ATOM   2141 C  CA    . ARG A 1 289 ? -11.797 22.142  61.341 1.00 21.06  ? 290  ARG A CA    1 
ATOM   2142 C  C     . ARG A 1 289 ? -13.254 22.520  61.122 1.00 22.01  ? 290  ARG A C     1 
ATOM   2143 O  O     . ARG A 1 289 ? -13.668 22.737  59.971 1.00 23.01  ? 290  ARG A O     1 
ATOM   2144 C  CB    . ARG A 1 289 ? -10.938 23.373  61.107 1.00 21.09  ? 290  ARG A CB    1 
ATOM   2145 C  CG    . ARG A 1 289 ? -11.320 24.531  62.055 1.00 31.00  ? 290  ARG A CG    1 
ATOM   2146 C  CD    . ARG A 1 289 ? -10.393 25.702  61.824 1.00 35.45  ? 290  ARG A CD    1 
ATOM   2147 N  NE    . ARG A 1 289 ? -9.106  25.504  62.462 1.00 49.16  ? 290  ARG A NE    1 
ATOM   2148 C  CZ    . ARG A 1 289 ? -8.008  26.181  62.151 1.00 58.40  ? 290  ARG A CZ    1 
ATOM   2149 N  NH1   . ARG A 1 289 ? -8.042  27.083  61.179 1.00 62.58  ? 290  ARG A NH1   1 
ATOM   2150 N  NH2   . ARG A 1 289 ? -6.874  25.936  62.797 1.00 62.48  ? 290  ARG A NH2   1 
ATOM   2151 N  N     . GLY A 1 290 ? -14.026 22.570  62.210 1.00 23.74  ? 291  GLY A N     1 
ATOM   2152 C  CA    . GLY A 1 290 ? -15.374 23.100  62.165 1.00 28.28  ? 291  GLY A CA    1 
ATOM   2153 C  C     . GLY A 1 290 ? -16.424 22.183  61.579 1.00 31.30  ? 291  GLY A C     1 
ATOM   2154 O  O     . GLY A 1 290 ? -17.600 22.554  61.553 1.00 34.57  ? 291  GLY A O     1 
ATOM   2155 N  N     . ILE A 1 291 ? -16.053 20.993  61.115 1.00 22.49  ? 292  ILE A N     1 
ATOM   2156 C  CA    . ILE A 1 291 ? -16.990 20.080  60.484 1.00 22.13  ? 292  ILE A CA    1 
ATOM   2157 C  C     . ILE A 1 291 ? -17.593 19.189  61.562 1.00 21.55  ? 292  ILE A C     1 
ATOM   2158 O  O     . ILE A 1 291 ? -16.867 18.640  62.416 1.00 26.28  ? 292  ILE A O     1 
ATOM   2159 C  CB    . ILE A 1 291 ? -16.264 19.233  59.416 1.00 23.60  ? 292  ILE A CB    1 
ATOM   2160 C  CG1   . ILE A 1 291 ? -15.709 20.140  58.316 1.00 20.91  ? 292  ILE A CG1   1 
ATOM   2161 C  CG2   . ILE A 1 291 ? -17.184 18.139  58.854 1.00 28.86  ? 292  ILE A CG2   1 
ATOM   2162 C  CD1   . ILE A 1 291 ? -16.748 21.023  57.595 1.00 24.02  ? 292  ILE A CD1   1 
ATOM   2163 N  N     . GLN A 1 292 ? -18.899 19.027  61.544 1.00 23.42  ? 293  GLN A N     1 
ATOM   2164 C  CA    . GLN A 1 292 ? -19.506 18.085  62.459 1.00 26.68  ? 293  GLN A CA    1 
ATOM   2165 C  C     . GLN A 1 292 ? -19.703 16.763  61.746 1.00 24.92  ? 293  GLN A C     1 
ATOM   2166 O  O     . GLN A 1 292 ? -19.850 16.683  60.508 1.00 22.11  ? 293  GLN A O     1 
ATOM   2167 C  CB    . GLN A 1 292 ? -20.838 18.598  62.992 1.00 27.31  ? 293  GLN A CB    1 
ATOM   2168 C  CG    . GLN A 1 292 ? -20.620 19.819  63.853 1.00 48.63  ? 293  GLN A CG    1 
ATOM   2169 C  CD    . GLN A 1 292 ? -21.915 20.482  64.271 1.00 72.09  ? 293  GLN A CD    1 
ATOM   2170 O  OE1   . GLN A 1 292 ? -22.994 20.157  63.762 1.00 75.22  ? 293  GLN A OE1   1 
ATOM   2171 N  NE2   . GLN A 1 292 ? -21.821 21.399  65.230 1.00 81.23  ? 293  GLN A NE2   1 
ATOM   2172 N  N     . LYS A 1 293 ? -19.634 15.706  62.531 1.00 29.19  ? 294  LYS A N     1 
ATOM   2173 C  CA    . LYS A 1 293 ? -19.695 14.381  61.964 1.00 25.29  ? 294  LYS A CA    1 
ATOM   2174 C  C     . LYS A 1 293 ? -20.936 14.226  61.129 1.00 23.98  ? 294  LYS A C     1 
ATOM   2175 O  O     . LYS A 1 293 ? -20.889 13.573  60.074 1.00 27.19  ? 294  LYS A O     1 
ATOM   2176 C  CB    . LYS A 1 293 ? -19.667 13.348  63.112 1.00 27.21  ? 294  LYS A CB    1 
ATOM   2177 C  CG    . LYS A 1 293 ? -19.735 11.950  62.688 1.00 22.30  ? 294  LYS A CG    1 
ATOM   2178 C  CD    . LYS A 1 293 ? -19.492 11.038  63.898 1.00 25.94  ? 294  LYS A CD    1 
ATOM   2179 C  CE    . LYS A 1 293 ? -19.478 9.656   63.493 1.00 33.42  ? 294  LYS A CE    1 
ATOM   2180 N  NZ    . LYS A 1 293 ? -19.392 8.965   64.788 1.00 28.76  ? 294  LYS A NZ    1 
ATOM   2181 N  N     . THR A 1 294 ? -22.011 14.914  61.507 1.00 25.48  ? 295  THR A N     1 
ATOM   2182 C  CA    . THR A 1 294 ? -23.256 14.847  60.770 1.00 23.24  ? 295  THR A CA    1 
ATOM   2183 C  C     . THR A 1 294 ? -23.171 15.487  59.368 1.00 31.89  ? 295  THR A C     1 
ATOM   2184 O  O     . THR A 1 294 ? -23.981 15.143  58.503 1.00 45.90  ? 295  THR A O     1 
ATOM   2185 C  CB    . THR A 1 294 ? -24.381 15.500  61.589 1.00 47.20  ? 295  THR A CB    1 
ATOM   2186 O  OG1   . THR A 1 294 ? -25.640 15.279  60.947 1.00 66.11  ? 295  THR A OG1   1 
ATOM   2187 C  CG2   . THR A 1 294 ? -24.164 17.001  61.768 1.00 44.58  ? 295  THR A CG2   1 
ATOM   2188 N  N     . ASP A 1 295 ? -22.234 16.424  59.145 1.00 26.30  ? 296  ASP A N     1 
ATOM   2189 C  CA    . ASP A 1 295 ? -21.990 17.120  57.880 1.00 27.10  ? 296  ASP A CA    1 
ATOM   2190 C  C     . ASP A 1 295 ? -21.261 16.231  56.875 1.00 22.67  ? 296  ASP A C     1 
ATOM   2191 O  O     . ASP A 1 295 ? -21.070 16.650  55.729 1.00 23.04  ? 296  ASP A O     1 
ATOM   2192 C  CB    . ASP A 1 295 ? -21.051 18.328  58.047 1.00 30.78  ? 296  ASP A CB    1 
ATOM   2193 C  CG    . ASP A 1 295 ? -21.567 19.435  59.008 1.00 47.25  ? 296  ASP A CG    1 
ATOM   2194 O  OD1   . ASP A 1 295 ? -22.809 19.663  59.061 1.00 38.03  ? 296  ASP A OD1   1 
ATOM   2195 O  OD2   . ASP A 1 295 ? -20.696 20.083  59.699 1.00 30.73  ? 296  ASP A OD2   1 
ATOM   2196 N  N     . ILE A 1 296 ? -20.743 15.073  57.272 1.00 23.04  ? 297  ILE A N     1 
ATOM   2197 C  CA    . ILE A 1 296 ? -19.753 14.380  56.452 1.00 25.69  ? 297  ILE A CA    1 
ATOM   2198 C  C     . ILE A 1 296 ? -19.987 12.882  56.497 1.00 30.37  ? 297  ILE A C     1 
ATOM   2199 O  O     . ILE A 1 296 ? -20.289 12.316  57.549 1.00 31.88  ? 297  ILE A O     1 
ATOM   2200 C  CB    . ILE A 1 296 ? -18.291 14.795  56.872 1.00 23.52  ? 297  ILE A CB    1 
ATOM   2201 C  CG1   . ILE A 1 296 ? -17.266 14.197  55.901 1.00 32.53  ? 297  ILE A CG1   1 
ATOM   2202 C  CG2   . ILE A 1 296 ? -17.963 14.506  58.320 1.00 30.12  ? 297  ILE A CG2   1 
ATOM   2203 C  CD1   . ILE A 1 296 ? -15.916 14.923  55.967 1.00 33.73  ? 297  ILE A CD1   1 
ATOM   2204 N  N     . GLU A 1 297 ? -19.859 12.231  55.346 1.00 30.64  ? 298  GLU A N     1 
ATOM   2205 C  CA    . GLU A 1 297 ? -20.250 10.834  55.273 1.00 37.51  ? 298  GLU A CA    1 
ATOM   2206 C  C     . GLU A 1 297 ? -19.531 10.156  54.122 1.00 46.32  ? 298  GLU A C     1 
ATOM   2207 O  O     . GLU A 1 297 ? -18.978 10.804  53.231 1.00 38.57  ? 298  GLU A O     1 
ATOM   2208 C  CB    . GLU A 1 297 ? -21.765 10.701  55.113 1.00 31.17  ? 298  GLU A CB    1 
ATOM   2209 C  CG    . GLU A 1 297 ? -22.292 11.398  53.897 1.00 27.68  ? 298  GLU A CG    1 
ATOM   2210 C  CD    . GLU A 1 297 ? -23.785 11.518  53.905 1.00 52.17  ? 298  GLU A CD    1 
ATOM   2211 O  OE1   . GLU A 1 297 ? -24.436 10.728  54.616 1.00 68.12  ? 298  GLU A OE1   1 
ATOM   2212 O  OE2   . GLU A 1 297 ? -24.303 12.477  53.308 1.00 49.84  ? 298  GLU A OE2   1 
ATOM   2213 N  N     . ARG A 1 298 ? -19.563 8.827   54.166 1.00 35.98  ? 299  ARG A N     1 
ATOM   2214 C  CA    . ARG A 1 298 ? -19.035 7.986   53.096 1.00 31.62  ? 299  ARG A CA    1 
ATOM   2215 C  C     . ARG A 1 298 ? -19.699 8.314   51.739 1.00 40.21  ? 299  ARG A C     1 
ATOM   2216 O  O     . ARG A 1 298 ? -20.919 8.516   51.621 1.00 30.29  ? 299  ARG A O     1 
ATOM   2217 C  CB    . ARG A 1 298 ? -19.274 6.533   53.523 1.00 30.97  ? 299  ARG A CB    1 
ATOM   2218 C  CG    . ARG A 1 298 ? -18.519 5.506   52.806 1.00 27.76  ? 299  ARG A CG    1 
ATOM   2219 C  CD    . ARG A 1 298 ? -18.839 4.128   53.426 1.00 29.14  ? 299  ARG A CD    1 
ATOM   2220 N  NE    . ARG A 1 298 ? -18.335 3.110   52.527 1.00 35.73  ? 299  ARG A NE    1 
ATOM   2221 C  CZ    . ARG A 1 298 ? -17.124 2.583   52.589 1.00 43.96  ? 299  ARG A CZ    1 
ATOM   2222 N  NH1   . ARG A 1 298 ? -16.286 2.942   53.567 1.00 38.83  ? 299  ARG A NH1   1 
ATOM   2223 N  NH2   . ARG A 1 298 ? -16.775 1.669   51.695 1.00 42.57  ? 299  ARG A NH2   1 
ATOM   2224 N  N     . GLY A 1 299 ? -18.893 8.386   50.683 1.00 31.05  ? 300  GLY A N     1 
ATOM   2225 C  CA    . GLY A 1 299 ? -19.387 8.843   49.379 1.00 28.76  ? 300  GLY A CA    1 
ATOM   2226 C  C     . GLY A 1 299 ? -18.948 10.264  49.045 1.00 16.14  ? 300  GLY A C     1 
ATOM   2227 O  O     . GLY A 1 299 ? -18.705 10.581  47.892 1.00 17.53  ? 300  GLY A O     1 
ATOM   2228 N  N     . MET A 1 300 ? -18.851 11.104  50.061 1.00 16.47  ? 301  MET A N     1 
ATOM   2229 C  CA    . MET A 1 300 ? -18.158 12.376  49.873 1.00 14.26  ? 301  MET A CA    1 
ATOM   2230 C  C     . MET A 1 300 ? -16.686 12.146  49.602 1.00 13.87  ? 301  MET A C     1 
ATOM   2231 O  O     . MET A 1 300 ? -16.100 11.127  50.017 1.00 17.09  ? 301  MET A O     1 
ATOM   2232 C  CB    . MET A 1 300 ? -18.319 13.287  51.082 1.00 14.65  ? 301  MET A CB    1 
ATOM   2233 C  CG    . MET A 1 300 ? -19.759 13.701  51.238 1.00 16.83  ? 301  MET A CG    1 
ATOM   2234 S  SD    . MET A 1 300 ? -19.899 14.661  52.765 1.00 16.71  ? 301  MET A SD    1 
ATOM   2235 C  CE    . MET A 1 300 ? -21.523 15.233  52.607 1.00 19.79  ? 301  MET A CE    1 
ATOM   2236 N  N     . VAL A 1 301 ? -16.063 13.127  48.955 1.00 13.05  ? 302  VAL A N     1 
ATOM   2237 C  CA    . VAL A 1 301 ? -14.611 13.134  48.796 1.00 13.81  ? 302  VAL A CA    1 
ATOM   2238 C  C     . VAL A 1 301 ? -14.069 14.431  49.369 1.00 14.56  ? 302  VAL A C     1 
ATOM   2239 O  O     . VAL A 1 301 ? -14.775 15.445  49.458 1.00 14.82  ? 302  VAL A O     1 
ATOM   2240 C  CB    . VAL A 1 301 ? -14.144 13.004  47.321 1.00 13.82  ? 302  VAL A CB    1 
ATOM   2241 C  CG1   . VAL A 1 301 ? -14.768 11.776  46.667 1.00 15.58  ? 302  VAL A CG1   1 
ATOM   2242 C  CG2   . VAL A 1 301 ? -14.502 14.195  46.517 1.00 15.03  ? 302  VAL A CG2   1 
ATOM   2243 N  N     . LEU A 1 302 ? -12.801 14.390  49.748 1.00 14.49  ? 303  LEU A N     1 
ATOM   2244 C  CA    . LEU A 1 302 ? -12.023 15.567  50.102 1.00 14.33  ? 303  LEU A CA    1 
ATOM   2245 C  C     . LEU A 1 302 ? -11.094 15.862  48.937 1.00 15.12  ? 303  LEU A C     1 
ATOM   2246 O  O     . LEU A 1 302 ? -10.525 14.942  48.347 1.00 15.42  ? 303  LEU A O     1 
ATOM   2247 C  CB    . LEU A 1 302 ? -11.186 15.336  51.344 1.00 14.36  ? 303  LEU A CB    1 
ATOM   2248 C  CG    . LEU A 1 302 ? -12.000 14.781  52.504 1.00 14.86  ? 303  LEU A CG    1 
ATOM   2249 C  CD1   . LEU A 1 302 ? -11.090 14.596  53.755 1.00 16.87  ? 303  LEU A CD1   1 
ATOM   2250 C  CD2   . LEU A 1 302 ? -13.157 15.689  52.910 1.00 17.39  ? 303  LEU A CD2   1 
ATOM   2251 N  N     . ALA A 1 303 ? -10.963 17.136  48.565 1.00 13.29  ? 304  ALA A N     1 
ATOM   2252 C  CA    . ALA A 1 303 ? -10.199 17.444  47.359 1.00 14.51  ? 304  ALA A CA    1 
ATOM   2253 C  C     . ALA A 1 303 ? -9.578  18.829  47.449 1.00 13.91  ? 304  ALA A C     1 
ATOM   2254 O  O     . ALA A 1 303 ? -10.080 19.721  48.140 1.00 15.46  ? 304  ALA A O     1 
ATOM   2255 C  CB    . ALA A 1 303 ? -11.128 17.360  46.136 1.00 15.30  ? 304  ALA A CB    1 
ATOM   2256 N  N     . LYS A 1 304 ? -8.532  19.030  46.652 1.00 15.66  ? 305  LYS A N     1 
ATOM   2257 C  CA    . LYS A 1 304 ? -8.055  20.417  46.452 1.00 16.77  ? 305  LYS A CA    1 
ATOM   2258 C  C     . LYS A 1 304 ? -9.215  21.247  45.918 1.00 17.42  ? 305  LYS A C     1 
ATOM   2259 O  O     . LYS A 1 304 ? -9.893  20.798  44.988 1.00 16.32  ? 305  LYS A O     1 
ATOM   2260 C  CB    . LYS A 1 304 ? -6.906  20.446  45.456 1.00 20.48  ? 305  LYS A CB    1 
ATOM   2261 C  CG    . LYS A 1 304 ? -6.445  21.858  45.136 1.00 22.98  ? 305  LYS A CG    1 
ATOM   2262 C  CD    . LYS A 1 304 ? -5.292  21.739  44.160 1.00 35.59  ? 305  LYS A CD    1 
ATOM   2263 C  CE    . LYS A 1 304 ? -4.492  23.049  43.958 1.00 54.77  ? 305  LYS A CE    1 
ATOM   2264 N  NZ    . LYS A 1 304 ? -5.069  24.042  43.038 1.00 41.72  ? 305  LYS A NZ    1 
ATOM   2265 N  N     . PRO A 1 305 ? -9.482  22.450  46.453 1.00 18.64  ? 306  PRO A N     1 
ATOM   2266 C  CA    . PRO A 1 305 ? -10.711 23.171  46.036 1.00 18.46  ? 306  PRO A CA    1 
ATOM   2267 C  C     . PRO A 1 305 ? -10.749 23.460  44.536 1.00 19.32  ? 306  PRO A C     1 
ATOM   2268 O  O     . PRO A 1 305 ? -9.738  23.808  43.921 1.00 23.23  ? 306  PRO A O     1 
ATOM   2269 C  CB    . PRO A 1 305 ? -10.675 24.462  46.870 1.00 20.74  ? 306  PRO A CB    1 
ATOM   2270 C  CG    . PRO A 1 305 ? -9.766  24.088  48.091 1.00 19.11  ? 306  PRO A CG    1 
ATOM   2271 C  CD    . PRO A 1 305 ? -8.750  23.166  47.536 1.00 17.14  ? 306  PRO A CD    1 
ATOM   2272 N  N     . GLY A 1 306 ? -11.930 23.237  43.949 1.00 18.44  ? 307  GLY A N     1 
ATOM   2273 C  CA    . GLY A 1 306 ? -12.079 23.434  42.506 1.00 20.37  ? 307  GLY A CA    1 
ATOM   2274 C  C     . GLY A 1 306 ? -11.512 22.361  41.617 1.00 20.72  ? 307  GLY A C     1 
ATOM   2275 O  O     . GLY A 1 306 ? -11.658 22.427  40.383 1.00 25.68  ? 307  GLY A O     1 
ATOM   2276 N  N     . SER A 1 307 ? -10.851 21.339  42.164 1.00 17.07  ? 308  SER A N     1 
ATOM   2277 C  CA    . SER A 1 307 ? -10.259 20.323  41.317 1.00 16.46  ? 308  SER A CA    1 
ATOM   2278 C  C     . SER A 1 307 ? -11.204 19.227  40.867 1.00 18.78  ? 308  SER A C     1 
ATOM   2279 O  O     . SER A 1 307 ? -10.875 18.471  39.926 1.00 19.93  ? 308  SER A O     1 
ATOM   2280 C  CB    . SER A 1 307 ? -9.061  19.673  42.021 1.00 18.68  ? 308  SER A CB    1 
ATOM   2281 O  OG    . SER A 1 307 ? -9.483  18.893  43.181 1.00 17.91  ? 308  SER A OG    1 
ATOM   2282 N  N     . ILE A 1 308 ? -12.326 19.055  41.551 1.00 16.26  ? 309  ILE A N     1 
ATOM   2283 C  CA    . ILE A 1 308 ? -13.349 18.105  41.158 1.00 16.76  ? 309  ILE A CA    1 
ATOM   2284 C  C     . ILE A 1 308 ? -14.660 18.729  41.602 1.00 16.97  ? 309  ILE A C     1 
ATOM   2285 O  O     . ILE A 1 308 ? -14.730 19.441  42.613 1.00 16.93  ? 309  ILE A O     1 
ATOM   2286 C  CB    . ILE A 1 308 ? -13.114 16.686  41.738 1.00 17.03  ? 309  ILE A CB    1 
ATOM   2287 C  CG1   . ILE A 1 308 ? -14.091 15.670  41.128 1.00 18.37  ? 309  ILE A CG1   1 
ATOM   2288 C  CG2   . ILE A 1 308 ? -13.279 16.685  43.260 1.00 17.41  ? 309  ILE A CG2   1 
ATOM   2289 C  CD1   . ILE A 1 308 ? -13.659 14.236  41.419 1.00 20.49  ? 309  ILE A CD1   1 
ATOM   2290 N  N     . THR A 1 309 ? -15.709 18.524  40.815 1.00 16.85  ? 310  THR A N     1 
ATOM   2291 C  CA    . THR A 1 309 ? -17.005 19.148  41.058 1.00 15.72  ? 310  THR A CA    1 
ATOM   2292 C  C     . THR A 1 309 ? -18.081 18.071  41.145 1.00 15.07  ? 310  THR A C     1 
ATOM   2293 O  O     . THR A 1 309 ? -17.905 16.955  40.638 1.00 16.78  ? 310  THR A O     1 
ATOM   2294 C  CB    . THR A 1 309 ? -17.384 20.209  40.000 1.00 19.94  ? 310  THR A CB    1 
ATOM   2295 O  OG1   . THR A 1 309 ? -17.055 19.667  38.734 1.00 21.64  ? 310  THR A OG1   1 
ATOM   2296 C  CG2   . THR A 1 309 ? -16.532 21.485  40.254 1.00 23.25  ? 310  THR A CG2   1 
ATOM   2297 N  N     . PRO A 1 310 ? -19.188 18.361  41.827 1.00 15.90  ? 311  PRO A N     1 
ATOM   2298 C  CA    . PRO A 1 310 ? -20.272 17.367  41.931 1.00 16.44  ? 311  PRO A CA    1 
ATOM   2299 C  C     . PRO A 1 310 ? -21.179 17.427  40.715 1.00 16.56  ? 311  PRO A C     1 
ATOM   2300 O  O     . PRO A 1 310 ? -21.471 18.501  40.163 1.00 18.32  ? 311  PRO A O     1 
ATOM   2301 C  CB    . PRO A 1 310 ? -21.036 17.811  43.188 1.00 18.54  ? 311  PRO A CB    1 
ATOM   2302 C  CG    . PRO A 1 310 ? -20.845 19.381  43.147 1.00 18.49  ? 311  PRO A CG    1 
ATOM   2303 C  CD    . PRO A 1 310 ? -19.443 19.555  42.664 1.00 16.03  ? 311  PRO A CD    1 
ATOM   2304 N  N     . HIS A 1 311 ? -21.667 16.239  40.344 1.00 15.75  ? 312  HIS A N     1 
ATOM   2305 C  CA    . HIS A 1 311 ? -22.497 16.131  39.145 1.00 15.23  ? 312  HIS A CA    1 
ATOM   2306 C  C     . HIS A 1 311 ? -23.521 15.054  39.357 1.00 16.14  ? 312  HIS A C     1 
ATOM   2307 O  O     . HIS A 1 311 ? -23.396 14.183  40.215 1.00 16.50  ? 312  HIS A O     1 
ATOM   2308 C  CB    . HIS A 1 311 ? -21.643 15.806  37.911 1.00 17.48  ? 312  HIS A CB    1 
ATOM   2309 C  CG    . HIS A 1 311 ? -20.701 16.901  37.591 1.00 18.04  ? 312  HIS A CG    1 
ATOM   2310 N  ND1   . HIS A 1 311 ? -21.128 18.104  37.060 1.00 20.15  ? 312  HIS A ND1   1 
ATOM   2311 C  CD2   . HIS A 1 311 ? -19.383 17.035  37.845 1.00 18.12  ? 312  HIS A CD2   1 
ATOM   2312 C  CE1   . HIS A 1 311 ? -20.091 18.927  36.991 1.00 19.72  ? 312  HIS A CE1   1 
ATOM   2313 N  NE2   . HIS A 1 311 ? -19.015 18.284  37.402 1.00 20.71  ? 312  HIS A NE2   1 
ATOM   2314 N  N     . THR A 1 312 ? -24.556 15.108  38.504 1.00 16.86  ? 313  THR A N     1 
ATOM   2315 C  CA    . THR A 1 312 ? -25.584 14.083  38.546 1.00 16.63  ? 313  THR A CA    1 
ATOM   2316 C  C     . THR A 1 312 ? -25.762 13.390  37.230 1.00 17.70  ? 313  THR A C     1 
ATOM   2317 O  O     . THR A 1 312 ? -26.372 12.325  37.224 1.00 21.88  ? 313  THR A O     1 
ATOM   2318 C  CB    . THR A 1 312 ? -26.959 14.645  38.955 1.00 19.20  ? 313  THR A CB    1 
ATOM   2319 O  OG1   . THR A 1 312 ? -27.273 15.779  38.113 1.00 22.21  ? 313  THR A OG1   1 
ATOM   2320 C  CG2   . THR A 1 312 ? -26.909 15.093  40.394 1.00 21.09  ? 313  THR A CG2   1 
ATOM   2321 N  N     . LYS A 1 313 ? -25.279 13.936  36.126 1.00 14.84  ? 314  LYS A N     1 
ATOM   2322 C  CA    . LYS A 1 313 ? -25.603 13.284  34.859 1.00 17.29  ? 314  LYS A CA    1 
ATOM   2323 C  C     . LYS A 1 313 ? -24.371 13.234  33.981 1.00 16.73  ? 314  LYS A C     1 
ATOM   2324 O  O     . LYS A 1 313 ? -23.657 14.228  33.839 1.00 15.89  ? 314  LYS A O     1 
ATOM   2325 C  CB    . LYS A 1 313 ? -26.739 14.045  34.135 1.00 18.38  ? 314  LYS A CB    1 
ATOM   2326 C  CG    . LYS A 1 313 ? -27.369 13.269  32.968 1.00 20.76  ? 314  LYS A CG    1 
ATOM   2327 C  CD    . LYS A 1 313 ? -28.583 14.109  32.381 1.00 26.39  ? 314  LYS A CD    1 
ATOM   2328 C  CE    . LYS A 1 313 ? -29.119 13.560  31.116 1.00 32.68  ? 314  LYS A CE    1 
ATOM   2329 N  NZ    . LYS A 1 313 ? -30.194 14.520  30.701 1.00 46.95  ? 314  LYS A NZ    1 
ATOM   2330 N  N     . PHE A 1 314 ? -24.124 12.081  33.337 1.00 15.11  ? 315  PHE A N     1 
ATOM   2331 C  CA    . PHE A 1 314 ? -22.902 11.927  32.561 1.00 15.38  ? 315  PHE A CA    1 
ATOM   2332 C  C     . PHE A 1 314 ? -23.074 10.817  31.552 1.00 16.66  ? 315  PHE A C     1 
ATOM   2333 O  O     . PHE A 1 314 ? -23.871 9.892   31.731 1.00 17.23  ? 315  PHE A O     1 
ATOM   2334 C  CB    . PHE A 1 314 ? -21.731 11.742  33.568 1.00 16.98  ? 315  PHE A CB    1 
ATOM   2335 C  CG    . PHE A 1 314 ? -21.802 10.533  34.471 1.00 15.83  ? 315  PHE A CG    1 
ATOM   2336 C  CD1   . PHE A 1 314 ? -21.676 9.229   34.030 1.00 20.35  ? 315  PHE A CD1   1 
ATOM   2337 C  CD2   . PHE A 1 314 ? -22.334 10.764  35.753 1.00 19.17  ? 315  PHE A CD2   1 
ATOM   2338 C  CE1   . PHE A 1 314 ? -21.764 8.115   34.930 1.00 21.91  ? 315  PHE A CE1   1 
ATOM   2339 C  CE2   . PHE A 1 314 ? -22.500 9.636   36.641 1.00 18.24  ? 315  PHE A CE2   1 
ATOM   2340 C  CZ    . PHE A 1 314 ? -22.222 8.339   36.167 1.00 20.60  ? 315  PHE A CZ    1 
ATOM   2341 N  N     . GLU A 1 315 ? -22.270 10.895  30.501 1.00 16.34  ? 316  GLU A N     1 
ATOM   2342 C  CA    . GLU A 1 315 ? -22.173 9.774   29.591 1.00 15.11  ? 316  GLU A CA    1 
ATOM   2343 C  C     . GLU A 1 315 ? -21.073 8.858   30.057 1.00 17.72  ? 316  GLU A C     1 
ATOM   2344 O  O     . GLU A 1 315 ? -20.102 9.289   30.714 1.00 15.89  ? 316  GLU A O     1 
ATOM   2345 C  CB    . GLU A 1 315 ? -21.818 10.254  28.190 1.00 17.50  ? 316  GLU A CB    1 
ATOM   2346 C  CG    . GLU A 1 315 ? -22.880 11.214  27.591 1.00 16.84  ? 316  GLU A CG    1 
ATOM   2347 C  CD    . GLU A 1 315 ? -22.515 11.758  26.184 1.00 23.27  ? 316  GLU A CD    1 
ATOM   2348 O  OE1   . GLU A 1 315 ? -21.403 11.497  25.639 1.00 23.42  ? 316  GLU A OE1   1 
ATOM   2349 O  OE2   . GLU A 1 315 ? -23.395 12.451  25.570 1.00 26.10  ? 316  GLU A OE2   1 
ATOM   2350 N  N     . SER A 1 316 ? -21.213 7.570   29.728 1.00 16.84  ? 317  SER A N     1 
ATOM   2351 C  CA    . SER A 1 316 ? -20.294 6.558   30.211 1.00 14.91  ? 317  SER A CA    1 
ATOM   2352 C  C     . SER A 1 316 ? -20.189 5.465   29.166 1.00 15.33  ? 317  SER A C     1 
ATOM   2353 O  O     . SER A 1 316 ? -21.086 5.296   28.333 1.00 18.09  ? 317  SER A O     1 
ATOM   2354 C  CB    . SER A 1 316 ? -20.738 5.961   31.532 1.00 17.19  ? 317  SER A CB    1 
ATOM   2355 O  OG    . SER A 1 316 ? -22.007 5.365   31.379 1.00 22.59  ? 317  SER A OG    1 
ATOM   2356 N  N     . GLU A 1 317 ? -19.099 4.726   29.195 1.00 15.20  ? 318  GLU A N     1 
ATOM   2357 C  CA    . GLU A 1 317 ? -19.007 3.439   28.528 1.00 15.76  ? 318  GLU A CA    1 
ATOM   2358 C  C     . GLU A 1 317 ? -19.270 2.387   29.569 1.00 17.01  ? 318  GLU A C     1 
ATOM   2359 O  O     . GLU A 1 317 ? -18.603 2.375   30.614 1.00 18.10  ? 318  GLU A O     1 
ATOM   2360 C  CB    . GLU A 1 317 ? -17.619 3.232   27.920 1.00 19.39  ? 318  GLU A CB    1 
ATOM   2361 C  CG    . GLU A 1 317 ? -17.347 4.130   26.718 1.00 21.18  ? 318  GLU A CG    1 
ATOM   2362 C  CD    . GLU A 1 317 ? -18.192 3.742   25.479 1.00 19.60  ? 318  GLU A CD    1 
ATOM   2363 O  OE1   . GLU A 1 317 ? -18.528 2.538   25.305 1.00 25.80  ? 318  GLU A OE1   1 
ATOM   2364 O  OE2   . GLU A 1 317 ? -18.378 4.684   24.690 1.00 26.01  ? 318  GLU A OE2   1 
ATOM   2365 N  N     . VAL A 1 318 ? -20.236 1.495   29.296 1.00 16.52  ? 319  VAL A N     1 
ATOM   2366 C  CA    . VAL A 1 318 ? -20.681 0.479   30.230 1.00 16.35  ? 319  VAL A CA    1 
ATOM   2367 C  C     . VAL A 1 318 ? -20.534 -0.903  29.608 1.00 17.32  ? 319  VAL A C     1 
ATOM   2368 O  O     . VAL A 1 318 ? -20.984 -1.128  28.469 1.00 18.54  ? 319  VAL A O     1 
ATOM   2369 C  CB    . VAL A 1 318 ? -22.142 0.760   30.658 1.00 16.41  ? 319  VAL A CB    1 
ATOM   2370 C  CG1   . VAL A 1 318 ? -22.733 -0.440  31.424 1.00 17.84  ? 319  VAL A CG1   1 
ATOM   2371 C  CG2   . VAL A 1 318 ? -22.175 2.032   31.498 1.00 16.92  ? 319  VAL A CG2   1 
ATOM   2372 N  N     . TYR A 1 319 ? -20.020 -1.832  30.400 1.00 17.19  ? 320  TYR A N     1 
ATOM   2373 C  CA    . TYR A 1 319 ? -19.959 -3.255  30.083 1.00 16.10  ? 320  TYR A CA    1 
ATOM   2374 C  C     . TYR A 1 319 ? -20.923 -3.994  30.982 1.00 16.21  ? 320  TYR A C     1 
ATOM   2375 O  O     . TYR A 1 319 ? -20.930 -3.785  32.208 1.00 17.57  ? 320  TYR A O     1 
ATOM   2376 C  CB    . TYR A 1 319 ? -18.525 -3.790  30.333 1.00 17.52  ? 320  TYR A CB    1 
ATOM   2377 C  CG    . TYR A 1 319 ? -18.404 -5.313  30.221 1.00 16.34  ? 320  TYR A CG    1 
ATOM   2378 C  CD1   . TYR A 1 319 ? -18.414 -5.918  28.981 1.00 20.54  ? 320  TYR A CD1   1 
ATOM   2379 C  CD2   . TYR A 1 319 ? -18.380 -6.116  31.355 1.00 17.03  ? 320  TYR A CD2   1 
ATOM   2380 C  CE1   . TYR A 1 319 ? -18.348 -7.301  28.867 1.00 19.96  ? 320  TYR A CE1   1 
ATOM   2381 C  CE2   . TYR A 1 319 ? -18.308 -7.506  31.261 1.00 19.31  ? 320  TYR A CE2   1 
ATOM   2382 C  CZ    . TYR A 1 319 ? -18.289 -8.078  29.997 1.00 18.83  ? 320  TYR A CZ    1 
ATOM   2383 O  OH    . TYR A 1 319 ? -18.234 -9.459  29.878 1.00 26.69  ? 320  TYR A OH    1 
ATOM   2384 N  N     . VAL A 1 320 ? -21.733 -4.866  30.395 1.00 15.51  ? 321  VAL A N     1 
ATOM   2385 C  CA    . VAL A 1 320 ? -22.677 -5.673  31.137 1.00 14.78  ? 321  VAL A CA    1 
ATOM   2386 C  C     . VAL A 1 320 ? -22.066 -7.048  31.377 1.00 16.27  ? 321  VAL A C     1 
ATOM   2387 O  O     . VAL A 1 320 ? -21.706 -7.744  30.407 1.00 17.36  ? 321  VAL A O     1 
ATOM   2388 C  CB    . VAL A 1 320 ? -24.002 -5.809  30.372 1.00 16.51  ? 321  VAL A CB    1 
ATOM   2389 C  CG1   . VAL A 1 320 ? -25.007 -6.616  31.187 1.00 17.61  ? 321  VAL A CG1   1 
ATOM   2390 C  CG2   . VAL A 1 320 ? -24.586 -4.435  30.057 1.00 19.90  ? 321  VAL A CG2   1 
ATOM   2391 N  N     . LEU A 1 321 ? -22.014 -7.474  32.651 1.00 18.77  ? 322  LEU A N     1 
ATOM   2392 C  CA    . LEU A 1 321 ? -21.406 -8.776  32.947 1.00 19.27  ? 322  LEU A CA    1 
ATOM   2393 C  C     . LEU A 1 321 ? -22.280 -9.925  32.472 1.00 20.83  ? 322  LEU A C     1 
ATOM   2394 O  O     . LEU A 1 321 ? -23.511 -9.867  32.531 1.00 20.96  ? 322  LEU A O     1 
ATOM   2395 C  CB    . LEU A 1 321 ? -21.174 -8.951  34.443 1.00 19.12  ? 322  LEU A CB    1 
ATOM   2396 C  CG    . LEU A 1 321 ? -19.854 -8.420  35.034 1.00 21.69  ? 322  LEU A CG    1 
ATOM   2397 C  CD1   . LEU A 1 321 ? -19.723 -6.889  35.084 1.00 22.08  ? 322  LEU A CD1   1 
ATOM   2398 C  CD2   . LEU A 1 321 ? -19.673 -9.070  36.416 1.00 22.19  ? 322  LEU A CD2   1 
ATOM   2399 N  N     . LYS A 1 322 ? -21.643 -10.983 31.980 1.00 21.83  ? 323  LYS A N     1 
ATOM   2400 C  CA    . LYS A 1 322 ? -22.362 -12.211 31.675 1.00 22.96  ? 323  LYS A CA    1 
ATOM   2401 C  C     . LYS A 1 322 ? -22.754 -12.934 32.961 1.00 25.23  ? 323  LYS A C     1 
ATOM   2402 O  O     . LYS A 1 322 ? -22.118 -12.768 34.004 1.00 28.23  ? 323  LYS A O     1 
ATOM   2403 C  CB    . LYS A 1 322 ? -21.475 -13.093 30.809 1.00 21.68  ? 323  LYS A CB    1 
ATOM   2404 C  CG    . LYS A 1 322 ? -21.215 -12.539 29.390 1.00 26.91  ? 323  LYS A CG    1 
ATOM   2405 C  CD    . LYS A 1 322 ? -20.393 -13.535 28.566 1.00 37.47  ? 323  LYS A CD    1 
ATOM   2406 C  CE    . LYS A 1 322 ? -20.328 -13.131 27.126 1.00 54.21  ? 323  LYS A CE    1 
ATOM   2407 N  NZ    . LYS A 1 322 ? -19.688 -14.213 26.317 1.00 64.60  ? 323  LYS A NZ    1 
ATOM   2408 N  N     . LYS A 1 323 ? -23.802 -13.770 32.873 1.00 26.76  ? 324  LYS A N     1 
ATOM   2409 C  CA    . LYS A 1 323 ? -24.203 -14.573 34.023 1.00 30.87  ? 324  LYS A CA    1 
ATOM   2410 C  C     . LYS A 1 323 ? -23.032 -15.416 34.538 1.00 29.60  ? 324  LYS A C     1 
ATOM   2411 O  O     . LYS A 1 323 ? -22.825 -15.540 35.753 1.00 33.88  ? 324  LYS A O     1 
ATOM   2412 C  CB    . LYS A 1 323 ? -25.367 -15.483 33.619 1.00 39.88  ? 324  LYS A CB    1 
ATOM   2413 C  CG    . LYS A 1 323 ? -25.994 -16.233 34.817 1.00 50.81  ? 324  LYS A CG    1 
ATOM   2414 C  CD    . LYS A 1 323 ? -26.838 -17.419 34.340 1.00 68.94  ? 324  LYS A CD    1 
ATOM   2415 C  CE    . LYS A 1 323 ? -28.094 -16.975 33.616 1.00 75.47  ? 324  LYS A CE    1 
ATOM   2416 N  NZ    . LYS A 1 323 ? -28.986 -18.084 33.176 1.00 75.86  ? 324  LYS A NZ    1 
ATOM   2417 N  N     . GLU A 1 324 ? -22.228 -15.941 33.613 1.00 29.96  ? 325  GLU A N     1 
ATOM   2418 C  CA    . GLU A 1 324 ? -21.065 -16.780 33.928 1.00 39.42  ? 325  GLU A CA    1 
ATOM   2419 C  C     . GLU A 1 324 ? -20.045 -16.052 34.795 1.00 42.91  ? 325  GLU A C     1 
ATOM   2420 O  O     . GLU A 1 324 ? -19.346 -16.679 35.598 1.00 43.72  ? 325  GLU A O     1 
ATOM   2421 C  CB    . GLU A 1 324 ? -20.387 -17.216 32.628 1.00 48.64  ? 325  GLU A CB    1 
ATOM   2422 C  CG    . GLU A 1 324 ? -21.258 -18.058 31.697 1.00 70.29  ? 325  GLU A CG    1 
ATOM   2423 C  CD    . GLU A 1 324 ? -22.273 -17.228 30.894 1.00 78.92  ? 325  GLU A CD    1 
ATOM   2424 O  OE1   . GLU A 1 324 ? -22.329 -16.004 31.074 1.00 80.07  ? 325  GLU A OE1   1 
ATOM   2425 O  OE2   . GLU A 1 324 ? -23.020 -17.801 30.076 1.00 85.13  ? 325  GLU A OE2   1 
ATOM   2426 N  N     . GLU A 1 325 ? -19.913 -14.741 34.642 1.00 31.21  ? 326  GLU A N     1 
ATOM   2427 C  CA    . GLU A 1 325 ? -18.953 -14.013 35.455 1.00 32.75  ? 326  GLU A CA    1 
ATOM   2428 C  C     . GLU A 1 325 ? -19.629 -13.280 36.608 1.00 29.76  ? 326  GLU A C     1 
ATOM   2429 O  O     . GLU A 1 325 ? -19.026 -12.417 37.241 1.00 35.24  ? 326  GLU A O     1 
ATOM   2430 C  CB    . GLU A 1 325 ? -18.103 -13.106 34.557 1.00 42.49  ? 326  GLU A CB    1 
ATOM   2431 C  CG    . GLU A 1 325 ? -18.897 -12.324 33.669 1.00 38.77  ? 326  GLU A CG    1 
ATOM   2432 C  CD    . GLU A 1 325 ? -18.129 -11.622 32.563 1.00 32.66  ? 326  GLU A CD    1 
ATOM   2433 O  OE1   . GLU A 1 325 ? -16.901 -11.723 32.423 1.00 39.23  ? 326  GLU A OE1   1 
ATOM   2434 O  OE2   . GLU A 1 325 ? -18.791 -10.928 31.817 1.00 27.52  ? 326  GLU A OE2   1 
ATOM   2435 N  N     . GLY A 1 326 ? -20.857 -13.645 36.923 1.00 33.69  ? 327  GLY A N     1 
ATOM   2436 C  CA    . GLY A 1 326 ? -21.499 -13.140 38.103 1.00 32.05  ? 327  GLY A CA    1 
ATOM   2437 C  C     . GLY A 1 326 ? -22.592 -12.134 37.840 1.00 38.94  ? 327  GLY A C     1 
ATOM   2438 O  O     . GLY A 1 326 ? -23.205 -11.653 38.794 1.00 33.84  ? 327  GLY A O     1 
ATOM   2439 N  N     . GLY A 1 327 ? -22.870 -11.815 36.578 1.00 32.63  ? 328  GLY A N     1 
ATOM   2440 C  CA    . GLY A 1 327 ? -23.929 -10.888 36.268 1.00 31.33  ? 328  GLY A CA    1 
ATOM   2441 C  C     . GLY A 1 327 ? -25.262 -11.583 36.189 1.00 35.10  ? 328  GLY A C     1 
ATOM   2442 O  O     . GLY A 1 327 ? -25.492 -12.653 36.764 1.00 33.64  ? 328  GLY A O     1 
ATOM   2443 N  N     . ARG A 1 328 ? -26.160 -10.942 35.468 1.00 26.85  ? 329  ARG A N     1 
ATOM   2444 C  CA    . ARG A 1 328 ? -27.490 -11.476 35.187 1.00 28.77  ? 329  ARG A CA    1 
ATOM   2445 C  C     . ARG A 1 328 ? -27.649 -11.808 33.711 1.00 26.39  ? 329  ARG A C     1 
ATOM   2446 O  O     . ARG A 1 328 ? -26.915 -11.324 32.868 1.00 28.83  ? 329  ARG A O     1 
ATOM   2447 C  CB    . ARG A 1 328 ? -28.531 -10.475 35.636 1.00 30.48  ? 329  ARG A CB    1 
ATOM   2448 C  CG    . ARG A 1 328 ? -28.622 -10.558 37.125 1.00 38.30  ? 329  ARG A CG    1 
ATOM   2449 C  CD    . ARG A 1 328 ? -29.584 -9.591  37.737 1.00 54.69  ? 329  ARG A CD    1 
ATOM   2450 N  NE    . ARG A 1 328 ? -30.024 -10.103 39.036 1.00 70.95  ? 329  ARG A NE    1 
ATOM   2451 C  CZ    . ARG A 1 328 ? -30.571 -9.367  39.998 1.00 74.07  ? 329  ARG A CZ    1 
ATOM   2452 N  NH1   . ARG A 1 328 ? -30.979 -9.939  41.123 1.00 79.12  ? 329  ARG A NH1   1 
ATOM   2453 N  NH2   . ARG A 1 328 ? -30.656 -8.053  39.862 1.00 69.78  ? 329  ARG A NH2   1 
ATOM   2454 N  N     . HIS A 1 329 ? -28.624 -12.670 33.407 1.00 30.89  ? 330  HIS A N     1 
ATOM   2455 C  CA    . HIS A 1 329 ? -28.897 -13.065 32.040 1.00 31.78  ? 330  HIS A CA    1 
ATOM   2456 C  C     . HIS A 1 329 ? -29.624 -11.996 31.223 1.00 34.92  ? 330  HIS A C     1 
ATOM   2457 O  O     . HIS A 1 329 ? -29.601 -12.050 29.987 1.00 41.45  ? 330  HIS A O     1 
ATOM   2458 C  CB    . HIS A 1 329 ? -29.651 -14.407 32.104 1.00 49.00  ? 330  HIS A CB    1 
ATOM   2459 C  CG    . HIS A 1 329 ? -30.544 -14.540 33.312 1.00 74.51  ? 330  HIS A CG    1 
ATOM   2460 N  ND1   . HIS A 1 329 ? -30.045 -14.619 34.601 1.00 76.48  ? 330  HIS A ND1   1 
ATOM   2461 C  CD2   . HIS A 1 329 ? -31.886 -14.683 33.429 1.00 78.86  ? 330  HIS A CD2   1 
ATOM   2462 C  CE1   . HIS A 1 329 ? -31.040 -14.742 35.458 1.00 75.28  ? 330  HIS A CE1   1 
ATOM   2463 N  NE2   . HIS A 1 329 ? -32.169 -14.794 34.773 1.00 79.27  ? 330  HIS A NE2   1 
ATOM   2464 N  N     . THR A 1 330 ? -30.174 -11.006 31.852 1.00 28.11  ? 331  THR A N     1 
ATOM   2465 C  CA    . THR A 1 330 ? -31.052 -10.045 31.206 1.00 32.86  ? 331  THR A CA    1 
ATOM   2466 C  C     . THR A 1 330 ? -30.302 -8.783  30.776 1.00 24.82  ? 331  THR A C     1 
ATOM   2467 O  O     . THR A 1 330 ? -29.315 -8.382  31.413 1.00 27.99  ? 331  THR A O     1 
ATOM   2468 C  CB    . THR A 1 330 ? -32.182 -9.684  32.167 1.00 43.57  ? 331  THR A CB    1 
ATOM   2469 O  OG1   . THR A 1 330 ? -32.976 -8.612  31.646 1.00 59.01  ? 331  THR A OG1   1 
ATOM   2470 C  CG2   . THR A 1 330 ? -31.626 -9.315  33.473 1.00 37.74  ? 331  THR A CG2   1 
ATOM   2471 N  N     . PRO A 1 331 ? -30.675 -8.202  29.636 1.00 20.38  ? 332  PRO A N     1 
ATOM   2472 C  CA    . PRO A 1 331 ? -29.983 -7.012  29.138 1.00 20.48  ? 332  PRO A CA    1 
ATOM   2473 C  C     . PRO A 1 331 ? -30.262 -5.799  30.009 1.00 18.36  ? 332  PRO A C     1 
ATOM   2474 O  O     . PRO A 1 331 ? -31.250 -5.711  30.750 1.00 21.46  ? 332  PRO A O     1 
ATOM   2475 C  CB    . PRO A 1 331 ? -30.582 -6.823  27.723 1.00 21.55  ? 332  PRO A CB    1 
ATOM   2476 C  CG    . PRO A 1 331 ? -31.147 -8.130  27.378 1.00 22.08  ? 332  PRO A CG    1 
ATOM   2477 C  CD    . PRO A 1 331 ? -31.646 -8.730  28.642 1.00 20.97  ? 332  PRO A CD    1 
ATOM   2478 N  N     . PHE A 1 332 ? -29.358 -4.812  29.891 1.00 17.48  ? 333  PHE A N     1 
ATOM   2479 C  CA    . PHE A 1 332 ? -29.679 -3.486  30.424 1.00 18.32  ? 333  PHE A CA    1 
ATOM   2480 C  C     . PHE A 1 332 ? -30.575 -2.783  29.405 1.00 20.67  ? 333  PHE A C     1 
ATOM   2481 O  O     . PHE A 1 332 ? -30.424 -2.981  28.192 1.00 19.77  ? 333  PHE A O     1 
ATOM   2482 C  CB    . PHE A 1 332 ? -28.452 -2.603  30.636 1.00 16.90  ? 333  PHE A CB    1 
ATOM   2483 C  CG    . PHE A 1 332 ? -27.570 -2.946  31.822 1.00 17.86  ? 333  PHE A CG    1 
ATOM   2484 C  CD1   . PHE A 1 332 ? -27.674 -4.119  32.529 1.00 21.22  ? 333  PHE A CD1   1 
ATOM   2485 C  CD2   . PHE A 1 332 ? -26.687 -1.980  32.243 1.00 20.87  ? 333  PHE A CD2   1 
ATOM   2486 C  CE1   . PHE A 1 332 ? -26.826 -4.382  33.648 1.00 19.30  ? 333  PHE A CE1   1 
ATOM   2487 C  CE2   . PHE A 1 332 ? -25.871 -2.183  33.351 1.00 19.90  ? 333  PHE A CE2   1 
ATOM   2488 C  CZ    . PHE A 1 332 ? -25.938 -3.399  34.036 1.00 19.64  ? 333  PHE A CZ    1 
ATOM   2489 N  N     . PHE A 1 333 ? -31.474 -1.944  29.889 1.00 18.34  ? 334  PHE A N     1 
ATOM   2490 C  CA    . PHE A 1 333 ? -32.485 -1.292  29.052 1.00 17.07  ? 334  PHE A CA    1 
ATOM   2491 C  C     . PHE A 1 333 ? -32.690 0.137   29.511 1.00 17.83  ? 334  PHE A C     1 
ATOM   2492 O  O     . PHE A 1 333 ? -32.359 0.494   30.654 1.00 17.38  ? 334  PHE A O     1 
ATOM   2493 C  CB    . PHE A 1 333 ? -33.751 -2.158  29.100 1.00 18.59  ? 334  PHE A CB    1 
ATOM   2494 C  CG    . PHE A 1 333 ? -34.445 -2.227  30.408 1.00 18.20  ? 334  PHE A CG    1 
ATOM   2495 C  CD1   . PHE A 1 333 ? -35.122 -1.181  31.070 1.00 19.15  ? 334  PHE A CD1   1 
ATOM   2496 C  CD2   . PHE A 1 333 ? -34.021 -3.310  31.212 1.00 20.62  ? 334  PHE A CD2   1 
ATOM   2497 C  CE1   . PHE A 1 333 ? -35.625 -1.351  32.380 1.00 20.91  ? 334  PHE A CE1   1 
ATOM   2498 C  CE2   . PHE A 1 333 ? -34.513 -3.477  32.509 1.00 22.53  ? 334  PHE A CE2   1 
ATOM   2499 C  CZ    . PHE A 1 333 ? -35.326 -2.488  33.101 1.00 22.21  ? 334  PHE A CZ    1 
ATOM   2500 N  N     . PRO A 1 334 ? -33.173 1.007   28.634 1.00 18.29  ? 335  PRO A N     1 
ATOM   2501 C  CA    . PRO A 1 334 ? -33.371 2.406   29.008 1.00 19.82  ? 335  PRO A CA    1 
ATOM   2502 C  C     . PRO A 1 334 ? -34.372 2.530   30.149 1.00 20.23  ? 335  PRO A C     1 
ATOM   2503 O  O     . PRO A 1 334 ? -35.447 1.933   30.112 1.00 18.44  ? 335  PRO A O     1 
ATOM   2504 C  CB    . PRO A 1 334 ? -33.885 3.061   27.712 1.00 19.84  ? 335  PRO A CB    1 
ATOM   2505 C  CG    . PRO A 1 334 ? -33.475 2.109   26.602 1.00 27.27  ? 335  PRO A CG    1 
ATOM   2506 C  CD    . PRO A 1 334 ? -33.456 0.739   27.202 1.00 22.06  ? 335  PRO A CD    1 
ATOM   2507 N  N     . GLY A 1 335 ? -34.000 3.324   31.147 1.00 19.04  ? 336  GLY A N     1 
ATOM   2508 C  CA    . GLY A 1 335 ? -34.813 3.556   32.321 1.00 19.10  ? 336  GLY A CA    1 
ATOM   2509 C  C     . GLY A 1 335 ? -34.640 2.519   33.385 1.00 18.83  ? 336  GLY A C     1 
ATOM   2510 O  O     . GLY A 1 335 ? -35.257 2.652   34.452 1.00 22.24  ? 336  GLY A O     1 
ATOM   2511 N  N     . TYR A 1 336 ? -33.770 1.528   33.162 1.00 17.06  ? 337  TYR A N     1 
ATOM   2512 C  CA    . TYR A 1 336 ? -33.358 0.677   34.268 1.00 18.08  ? 337  TYR A CA    1 
ATOM   2513 C  C     . TYR A 1 336 ? -32.701 1.540   35.354 1.00 17.52  ? 337  TYR A C     1 
ATOM   2514 O  O     . TYR A 1 336 ? -31.949 2.475   35.059 1.00 16.96  ? 337  TYR A O     1 
ATOM   2515 C  CB    . TYR A 1 336 ? -32.399 -0.414  33.735 1.00 18.62  ? 337  TYR A CB    1 
ATOM   2516 C  CG    . TYR A 1 336 ? -31.809 -1.361  34.741 1.00 20.15  ? 337  TYR A CG    1 
ATOM   2517 C  CD1   . TYR A 1 336 ? -32.609 -2.023  35.656 1.00 20.91  ? 337  TYR A CD1   1 
ATOM   2518 C  CD2   . TYR A 1 336 ? -30.471 -1.726  34.630 1.00 20.64  ? 337  TYR A CD2   1 
ATOM   2519 C  CE1   . TYR A 1 336 ? -32.079 -2.953  36.538 1.00 24.01  ? 337  TYR A CE1   1 
ATOM   2520 C  CE2   . TYR A 1 336 ? -29.918 -2.684  35.505 1.00 22.03  ? 337  TYR A CE2   1 
ATOM   2521 C  CZ    . TYR A 1 336 ? -30.732 -3.263  36.454 1.00 28.14  ? 337  TYR A CZ    1 
ATOM   2522 O  OH    . TYR A 1 336 ? -30.200 -4.178  37.358 1.00 32.94  ? 337  TYR A OH    1 
ATOM   2523 N  N     . ARG A 1 337 ? -33.000 1.241   36.621 1.00 19.40  ? 338  ARG A N     1 
ATOM   2524 C  CA    . ARG A 1 337 ? -32.558 2.050   37.760 1.00 21.12  ? 338  ARG A CA    1 
ATOM   2525 C  C     . ARG A 1 337 ? -31.821 1.208   38.784 1.00 22.03  ? 338  ARG A C     1 
ATOM   2526 O  O     . ARG A 1 337 ? -32.319 0.987   39.906 1.00 24.37  ? 338  ARG A O     1 
ATOM   2527 C  CB    . ARG A 1 337 ? -33.770 2.751   38.376 1.00 22.52  ? 338  ARG A CB    1 
ATOM   2528 C  CG    . ARG A 1 337 ? -34.256 3.920   37.514 1.00 23.92  ? 338  ARG A CG    1 
ATOM   2529 C  CD    . ARG A 1 337 ? -35.752 4.180   37.754 1.00 26.94  ? 338  ARG A CD    1 
ATOM   2530 N  NE    . ARG A 1 337 ? -36.188 5.517   37.354 1.00 26.48  ? 338  ARG A NE    1 
ATOM   2531 C  CZ    . ARG A 1 337 ? -36.587 5.870   36.124 1.00 24.64  ? 338  ARG A CZ    1 
ATOM   2532 N  NH1   . ARG A 1 337 ? -37.021 7.109   35.927 1.00 24.65  ? 338  ARG A NH1   1 
ATOM   2533 N  NH2   . ARG A 1 337 ? -36.567 5.003   35.113 1.00 24.19  ? 338  ARG A NH2   1 
ATOM   2534 N  N     . PRO A 1 338 ? -30.586 0.770   38.445 1.00 21.21  ? 339  PRO A N     1 
ATOM   2535 C  CA    . PRO A 1 338 ? -29.767 -0.003  39.400 1.00 21.10  ? 339  PRO A CA    1 
ATOM   2536 C  C     . PRO A 1 338 ? -29.040 0.908   40.382 1.00 20.59  ? 339  PRO A C     1 
ATOM   2537 O  O     . PRO A 1 338 ? -29.228 2.130   40.382 1.00 21.74  ? 339  PRO A O     1 
ATOM   2538 C  CB    . PRO A 1 338 ? -28.781 -0.742  38.493 1.00 20.35  ? 339  PRO A CB    1 
ATOM   2539 C  CG    . PRO A 1 338 ? -28.534 0.262   37.352 1.00 17.32  ? 339  PRO A CG    1 
ATOM   2540 C  CD    . PRO A 1 338 ? -29.905 0.909   37.124 1.00 18.48  ? 339  PRO A CD    1 
ATOM   2541 N  N     . GLN A 1 339 ? -28.120 0.312   41.137 1.00 21.18  ? 340  GLN A N     1 
ATOM   2542 C  CA    . GLN A 1 339 ? -27.236 1.079   42.014 1.00 21.28  ? 340  GLN A CA    1 
ATOM   2543 C  C     . GLN A 1 339 ? -25.901 1.315   41.339 1.00 19.54  ? 340  GLN A C     1 
ATOM   2544 O  O     . GLN A 1 339 ? -25.385 0.447   40.618 1.00 20.32  ? 340  GLN A O     1 
ATOM   2545 C  CB    . GLN A 1 339 ? -27.011 0.341   43.336 1.00 22.02  ? 340  GLN A CB    1 
ATOM   2546 C  CG    . GLN A 1 339 ? -28.285 0.169   44.154 1.00 23.25  ? 340  GLN A CG    1 
ATOM   2547 C  CD    . GLN A 1 339 ? -28.804 1.476   44.628 1.00 23.54  ? 340  GLN A CD    1 
ATOM   2548 O  OE1   . GLN A 1 339 ? -28.083 2.245   45.297 1.00 30.91  ? 340  GLN A OE1   1 
ATOM   2549 N  NE2   . GLN A 1 339 ? -30.020 1.824   44.219 1.00 25.37  ? 340  GLN A NE2   1 
ATOM   2550 N  N     . PHE A 1 340 ? -25.359 2.508   41.542 1.00 18.63  ? 341  PHE A N     1 
ATOM   2551 C  CA    . PHE A 1 340 ? -24.060 2.879   41.038 1.00 16.07  ? 341  PHE A CA    1 
ATOM   2552 C  C     . PHE A 1 340 ? -23.093 2.995   42.209 1.00 19.03  ? 341  PHE A C     1 
ATOM   2553 O  O     . PHE A 1 340 ? -23.255 3.886   43.057 1.00 19.46  ? 341  PHE A O     1 
ATOM   2554 C  CB    . PHE A 1 340 ? -24.070 4.171   40.227 1.00 17.40  ? 341  PHE A CB    1 
ATOM   2555 C  CG    . PHE A 1 340 ? -24.954 4.044   38.999 1.00 20.07  ? 341  PHE A CG    1 
ATOM   2556 C  CD1   . PHE A 1 340 ? -26.316 3.937   39.119 1.00 21.02  ? 341  PHE A CD1   1 
ATOM   2557 C  CD2   . PHE A 1 340 ? -24.323 3.716   37.782 1.00 21.67  ? 341  PHE A CD2   1 
ATOM   2558 C  CE1   . PHE A 1 340 ? -27.105 3.703   37.996 1.00 25.01  ? 341  PHE A CE1   1 
ATOM   2559 C  CE2   . PHE A 1 340 ? -25.083 3.426   36.677 1.00 22.12  ? 341  PHE A CE2   1 
ATOM   2560 C  CZ    . PHE A 1 340 ? -26.451 3.425   36.806 1.00 19.34  ? 341  PHE A CZ    1 
ATOM   2561 N  N     . TYR A 1 341 ? -22.086 2.118   42.220 1.00 17.51  ? 342  TYR A N     1 
ATOM   2562 C  CA    . TYR A 1 341 ? -21.081 2.139   43.305 1.00 16.47  ? 342  TYR A CA    1 
ATOM   2563 C  C     . TYR A 1 341 ? -19.965 3.092   42.896 1.00 16.81  ? 342  TYR A C     1 
ATOM   2564 O  O     . TYR A 1 341 ? -19.179 2.821   41.976 1.00 17.37  ? 342  TYR A O     1 
ATOM   2565 C  CB    . TYR A 1 341 ? -20.539 0.745   43.574 1.00 18.67  ? 342  TYR A CB    1 
ATOM   2566 C  CG    . TYR A 1 341 ? -19.726 0.693   44.851 1.00 22.45  ? 342  TYR A CG    1 
ATOM   2567 C  CD1   . TYR A 1 341 ? -20.348 0.528   46.089 1.00 23.71  ? 342  TYR A CD1   1 
ATOM   2568 C  CD2   . TYR A 1 341 ? -18.347 0.807   44.785 1.00 23.00  ? 342  TYR A CD2   1 
ATOM   2569 C  CE1   . TYR A 1 341 ? -19.555 0.445   47.297 1.00 23.37  ? 342  TYR A CE1   1 
ATOM   2570 C  CE2   . TYR A 1 341 ? -17.570 0.740   45.948 1.00 26.08  ? 342  TYR A CE2   1 
ATOM   2571 C  CZ    . TYR A 1 341 ? -18.177 0.589   47.139 1.00 25.74  ? 342  TYR A CZ    1 
ATOM   2572 O  OH    . TYR A 1 341 ? -17.366 0.525   48.276 1.00 28.18  ? 342  TYR A OH    1 
ATOM   2573 N  N     . VAL A 1 342 ? -19.917 4.240   43.593 1.00 17.00  ? 343  VAL A N     1 
ATOM   2574 C  CA    . VAL A 1 342 ? -19.042 5.339   43.248 1.00 17.03  ? 343  VAL A CA    1 
ATOM   2575 C  C     . VAL A 1 342 ? -18.081 5.510   44.418 1.00 19.53  ? 343  VAL A C     1 
ATOM   2576 O  O     . VAL A 1 342 ? -18.427 6.114   45.455 1.00 18.69  ? 343  VAL A O     1 
ATOM   2577 C  CB    . VAL A 1 342 ? -19.795 6.634   42.987 1.00 17.79  ? 343  VAL A CB    1 
ATOM   2578 C  CG1   . VAL A 1 342 ? -18.813 7.689   42.535 1.00 19.36  ? 343  VAL A CG1   1 
ATOM   2579 C  CG2   . VAL A 1 342 ? -20.877 6.410   41.890 1.00 22.97  ? 343  VAL A CG2   1 
ATOM   2580 N  N     . ARG A 1 343 ? -16.930 4.865   44.290 1.00 17.51  ? 344  ARG A N     1 
ATOM   2581 C  CA    . ARG A 1 343 ? -15.765 4.807   45.217 1.00 14.85  ? 344  ARG A CA    1 
ATOM   2582 C  C     . ARG A 1 343 ? -16.024 4.098   46.525 1.00 19.09  ? 344  ARG A C     1 
ATOM   2583 O  O     . ARG A 1 343 ? -15.334 3.102   46.792 1.00 23.94  ? 344  ARG A O     1 
ATOM   2584 C  CB    . ARG A 1 343 ? -15.260 6.223   45.579 1.00 16.37  ? 344  ARG A CB    1 
ATOM   2585 C  CG    . ARG A 1 343 ? -15.006 7.119   44.370 1.00 16.22  ? 344  ARG A CG    1 
ATOM   2586 C  CD    . ARG A 1 343 ? -14.359 8.440   44.816 1.00 17.51  ? 344  ARG A CD    1 
ATOM   2587 N  NE    . ARG A 1 343 ? -14.170 9.322   43.664 1.00 19.09  ? 344  ARG A NE    1 
ATOM   2588 C  CZ    . ARG A 1 343 ? -15.122 10.114  43.193 1.00 14.74  ? 344  ARG A CZ    1 
ATOM   2589 N  NH1   . ARG A 1 343 ? -16.324 10.218  43.728 1.00 16.68  ? 344  ARG A NH1   1 
ATOM   2590 N  NH2   . ARG A 1 343 ? -14.818 10.848  42.091 1.00 17.13  ? 344  ARG A NH2   1 
ATOM   2591 N  N     . THR A 1 344 ? -17.118 4.431   47.197 1.00 17.91  ? 345  THR A N     1 
ATOM   2592 C  CA    . THR A 1 344 ? -17.372 3.910   48.549 1.00 17.43  ? 345  THR A CA    1 
ATOM   2593 C  C     . THR A 1 344 ? -18.818 3.591   48.827 1.00 23.03  ? 345  THR A C     1 
ATOM   2594 O  O     . THR A 1 344 ? -19.095 3.032   49.890 1.00 24.89  ? 345  THR A O     1 
ATOM   2595 C  CB    . THR A 1 344 ? -16.931 4.941   49.598 1.00 19.75  ? 345  THR A CB    1 
ATOM   2596 O  OG1   . THR A 1 344 ? -17.596 6.188   49.290 1.00 22.23  ? 345  THR A OG1   1 
ATOM   2597 C  CG2   . THR A 1 344 ? -15.466 5.141   49.580 1.00 20.64  ? 345  THR A CG2   1 
ATOM   2598 N  N     . THR A 1 345 ? -19.778 3.996   47.979 1.00 19.06  ? 346  THR A N     1 
ATOM   2599 C  CA    . THR A 1 345 ? -21.163 3.821   48.342 1.00 19.88  ? 346  THR A CA    1 
ATOM   2600 C  C     . THR A 1 345 ? -22.006 3.679   47.081 1.00 19.99  ? 346  THR A C     1 
ATOM   2601 O  O     . THR A 1 345 ? -21.620 4.175   46.011 1.00 21.40  ? 346  THR A O     1 
ATOM   2602 C  CB    . THR A 1 345 ? -21.666 5.013   49.207 1.00 28.43  ? 346  THR A CB    1 
ATOM   2603 O  OG1   . THR A 1 345 ? -22.904 4.640   49.838 1.00 34.18  ? 346  THR A OG1   1 
ATOM   2604 C  CG2   . THR A 1 345 ? -21.854 6.263   48.376 1.00 29.69  ? 346  THR A CG2   1 
ATOM   2605 N  N     . ASP A 1 346 ? -23.135 3.000   47.240 1.00 24.05  ? 347  ASP A N     1 
ATOM   2606 C  CA    . ASP A 1 346 ? -24.135 2.904   46.182 1.00 21.08  ? 347  ASP A CA    1 
ATOM   2607 C  C     . ASP A 1 346 ? -24.969 4.174   46.118 1.00 24.96  ? 347  ASP A C     1 
ATOM   2608 O  O     . ASP A 1 346 ? -25.455 4.666   47.141 1.00 26.26  ? 347  ASP A O     1 
ATOM   2609 C  CB    . ASP A 1 346 ? -25.093 1.742   46.431 1.00 20.80  ? 347  ASP A CB    1 
ATOM   2610 C  CG    . ASP A 1 346 ? -24.523 0.363   46.042 1.00 27.64  ? 347  ASP A CG    1 
ATOM   2611 O  OD1   . ASP A 1 346 ? -23.667 0.241   45.119 1.00 26.11  ? 347  ASP A OD1   1 
ATOM   2612 O  OD2   . ASP A 1 346 ? -25.022 -0.623  46.640 1.00 32.88  ? 347  ASP A OD2   1 
ATOM   2613 N  N     . VAL A 1 347 ? -25.222 4.642   44.895 1.00 20.35  ? 348  VAL A N     1 
ATOM   2614 C  CA    . VAL A 1 347 ? -26.120 5.756   44.622 1.00 18.83  ? 348  VAL A CA    1 
ATOM   2615 C  C     . VAL A 1 347 ? -27.120 5.234   43.592 1.00 18.63  ? 348  VAL A C     1 
ATOM   2616 O  O     . VAL A 1 347 ? -26.700 4.725   42.555 1.00 21.80  ? 348  VAL A O     1 
ATOM   2617 C  CB    . VAL A 1 347 ? -25.351 6.962   44.049 1.00 21.06  ? 348  VAL A CB    1 
ATOM   2618 C  CG1   . VAL A 1 347 ? -26.273 8.167   43.830 1.00 22.79  ? 348  VAL A CG1   1 
ATOM   2619 C  CG2   . VAL A 1 347 ? -24.170 7.329   45.012 1.00 24.14  ? 348  VAL A CG2   1 
ATOM   2620 N  N     . THR A 1 348 ? -28.401 5.442   43.821 1.00 19.02  ? 349  THR A N     1 
ATOM   2621 C  CA    . THR A 1 348 ? -29.395 5.080   42.813 1.00 20.11  ? 349  THR A CA    1 
ATOM   2622 C  C     . THR A 1 348 ? -29.287 5.967   41.574 1.00 20.25  ? 349  THR A C     1 
ATOM   2623 O  O     . THR A 1 348 ? -29.018 7.175   41.673 1.00 19.35  ? 349  THR A O     1 
ATOM   2624 C  CB    . THR A 1 348 ? -30.755 5.253   43.418 1.00 21.16  ? 349  THR A CB    1 
ATOM   2625 O  OG1   . THR A 1 348 ? -30.835 4.461   44.618 1.00 24.51  ? 349  THR A OG1   1 
ATOM   2626 C  CG2   . THR A 1 348 ? -31.826 4.769   42.411 1.00 22.90  ? 349  THR A CG2   1 
ATOM   2627 N  N     . GLY A 1 349 ? -29.437 5.358   40.381 1.00 21.03  ? 350  GLY A N     1 
ATOM   2628 C  CA    . GLY A 1 349 ? -29.372 6.129   39.155 1.00 20.29  ? 350  GLY A CA    1 
ATOM   2629 C  C     . GLY A 1 349 ? -30.282 5.515   38.111 1.00 17.93  ? 350  GLY A C     1 
ATOM   2630 O  O     . GLY A 1 349 ? -30.912 4.492   38.363 1.00 23.75  ? 350  GLY A O     1 
ATOM   2631 N  N     . ALA A 1 350 ? -30.480 6.248   37.037 1.00 17.95  ? 351  ALA A N     1 
ATOM   2632 C  CA    . ALA A 1 350 ? -31.251 5.736   35.931 1.00 16.61  ? 351  ALA A CA    1 
ATOM   2633 C  C     . ALA A 1 350 ? -30.408 5.845   34.686 1.00 17.77  ? 351  ALA A C     1 
ATOM   2634 O  O     . ALA A 1 350 ? -29.699 6.839   34.480 1.00 17.62  ? 351  ALA A O     1 
ATOM   2635 C  CB    . ALA A 1 350 ? -32.499 6.572   35.783 1.00 19.29  ? 351  ALA A CB    1 
ATOM   2636 N  N     . ILE A 1 351 ? -30.485 4.821   33.827 1.00 17.05  ? 352  ILE A N     1 
ATOM   2637 C  CA    . ILE A 1 351 ? -29.707 4.834   32.598 1.00 16.71  ? 352  ILE A CA    1 
ATOM   2638 C  C     . ILE A 1 351 ? -30.616 5.166   31.408 1.00 17.95  ? 352  ILE A C     1 
ATOM   2639 O  O     . ILE A 1 351 ? -31.852 4.935   31.415 1.00 18.88  ? 352  ILE A O     1 
ATOM   2640 C  CB    . ILE A 1 351 ? -28.953 3.520   32.349 1.00 17.41  ? 352  ILE A CB    1 
ATOM   2641 C  CG1   . ILE A 1 351 ? -29.931 2.354   32.208 1.00 18.09  ? 352  ILE A CG1   1 
ATOM   2642 C  CG2   . ILE A 1 351 ? -27.932 3.296   33.511 1.00 20.55  ? 352  ILE A CG2   1 
ATOM   2643 C  CD1   . ILE A 1 351 ? -29.162 1.058   31.983 1.00 18.19  ? 352  ILE A CD1   1 
ATOM   2644 N  N     . SER A 1 352 ? -30.023 5.771   30.394 1.00 16.73  ? 353  SER A N     1 
ATOM   2645 C  CA    . SER A 1 352 ? -30.817 6.270   29.263 1.00 17.41  ? 353  SER A CA    1 
ATOM   2646 C  C     . SER A 1 352 ? -29.930 6.492   28.050 1.00 17.88  ? 353  SER A C     1 
ATOM   2647 O  O     . SER A 1 352 ? -28.707 6.352   28.122 1.00 16.91  ? 353  SER A O     1 
ATOM   2648 C  CB    . SER A 1 352 ? -31.551 7.567   29.616 1.00 18.96  ? 353  SER A CB    1 
ATOM   2649 O  OG    . SER A 1 352 ? -30.589 8.620   29.823 1.00 20.39  ? 353  SER A OG    1 
ATOM   2650 N  N     . ASP A 1 353 ? -30.558 6.800   26.913 1.00 20.29  ? 354  ASP A N     1 
ATOM   2651 C  CA    . ASP A 1 353 ? -29.864 7.317   25.724 1.00 18.21  ? 354  ASP A CA    1 
ATOM   2652 C  C     . ASP A 1 353 ? -28.749 6.356   25.275 1.00 16.41  ? 354  ASP A C     1 
ATOM   2653 O  O     . ASP A 1 353 ? -27.583 6.742   25.063 1.00 20.22  ? 354  ASP A O     1 
ATOM   2654 C  CB    . ASP A 1 353 ? -29.297 8.720   25.951 1.00 22.19  ? 354  ASP A CB    1 
ATOM   2655 C  CG    . ASP A 1 353 ? -28.993 9.456   24.639 1.00 50.46  ? 354  ASP A CG    1 
ATOM   2656 O  OD1   . ASP A 1 353 ? -29.243 8.895   23.540 1.00 53.83  ? 354  ASP A OD1   1 
ATOM   2657 O  OD2   . ASP A 1 353 ? -28.501 10.607  24.705 1.00 55.11  ? 354  ASP A OD2   1 
ATOM   2658 N  N     . PHE A 1 354 ? -29.098 5.077   25.123 1.00 18.65  ? 355  PHE A N     1 
ATOM   2659 C  CA    . PHE A 1 354 ? -28.125 4.100   24.654 1.00 17.21  ? 355  PHE A CA    1 
ATOM   2660 C  C     . PHE A 1 354 ? -27.757 4.411   23.214 1.00 18.07  ? 355  PHE A C     1 
ATOM   2661 O  O     . PHE A 1 354 ? -28.640 4.588   22.367 1.00 20.55  ? 355  PHE A O     1 
ATOM   2662 C  CB    . PHE A 1 354 ? -28.687 2.675   24.697 1.00 20.14  ? 355  PHE A CB    1 
ATOM   2663 C  CG    . PHE A 1 354 ? -29.007 2.122   26.073 1.00 17.58  ? 355  PHE A CG    1 
ATOM   2664 C  CD1   . PHE A 1 354 ? -28.982 2.906   27.216 1.00 18.05  ? 355  PHE A CD1   1 
ATOM   2665 C  CD2   . PHE A 1 354 ? -29.312 0.792   26.166 1.00 19.60  ? 355  PHE A CD2   1 
ATOM   2666 C  CE1   . PHE A 1 354 ? -29.251 2.309   28.426 1.00 16.62  ? 355  PHE A CE1   1 
ATOM   2667 C  CE2   . PHE A 1 354 ? -29.597 0.185   27.380 1.00 17.90  ? 355  PHE A CE2   1 
ATOM   2668 C  CZ    . PHE A 1 354 ? -29.599 0.961   28.500 1.00 16.33  ? 355  PHE A CZ    1 
ATOM   2669 N  N     . THR A 1 355 ? -26.454 4.510   22.945 1.00 17.53  ? 356  THR A N     1 
ATOM   2670 C  CA    . THR A 1 355 ? -25.952 4.971   21.642 1.00 16.92  ? 356  THR A CA    1 
ATOM   2671 C  C     . THR A 1 355 ? -24.954 3.943   21.146 1.00 19.62  ? 356  THR A C     1 
ATOM   2672 O  O     . THR A 1 355 ? -23.921 3.693   21.781 1.00 21.11  ? 356  THR A O     1 
ATOM   2673 C  CB    . THR A 1 355 ? -25.310 6.346   21.793 1.00 20.47  ? 356  THR A CB    1 
ATOM   2674 O  OG1   . THR A 1 355 ? -26.277 7.262   22.366 1.00 23.55  ? 356  THR A OG1   1 
ATOM   2675 C  CG2   . THR A 1 355 ? -24.802 6.855   20.438 1.00 25.17  ? 356  THR A CG2   1 
ATOM   2676 N  N     . ALA A 1 356 ? -25.298 3.313   20.037 1.00 19.51  ? 357  ALA A N     1 
ATOM   2677 C  CA    . ALA A 1 356 ? -24.483 2.310   19.402 1.00 20.58  ? 357  ALA A CA    1 
ATOM   2678 C  C     . ALA A 1 356 ? -23.249 2.961   18.783 1.00 22.43  ? 357  ALA A C     1 
ATOM   2679 O  O     . ALA A 1 356 ? -23.137 4.195   18.687 1.00 22.61  ? 357  ALA A O     1 
ATOM   2680 C  CB    . ALA A 1 356 ? -25.329 1.571   18.361 1.00 21.90  ? 357  ALA A CB    1 
ATOM   2681 N  N     . ASP A 1 357 ? -22.280 2.104   18.456 1.00 21.28  ? 358  ASP A N     1 
ATOM   2682 C  CA    . ASP A 1 357 ? -20.995 2.645   18.008 1.00 23.57  ? 358  ASP A CA    1 
ATOM   2683 C  C     . ASP A 1 357 ? -21.161 3.436   16.708 1.00 28.14  ? 358  ASP A C     1 
ATOM   2684 O  O     . ASP A 1 357 ? -20.377 4.353   16.459 1.00 30.10  ? 358  ASP A O     1 
ATOM   2685 C  CB    . ASP A 1 357 ? -19.966 1.545   17.790 1.00 22.77  ? 358  ASP A CB    1 
ATOM   2686 C  CG    . ASP A 1 357 ? -19.570 0.837   19.058 1.00 22.83  ? 358  ASP A CG    1 
ATOM   2687 O  OD1   . ASP A 1 357 ? -20.032 1.283   20.144 1.00 23.53  ? 358  ASP A OD1   1 
ATOM   2688 O  OD2   . ASP A 1 357 ? -18.708 -0.096  18.997 1.00 24.29  ? 358  ASP A OD2   1 
ATOM   2689 N  N     . ASP A 1 358 ? -22.181 3.127   15.896 1.00 25.26  ? 359  ASP A N     1 
ATOM   2690 C  CA    . ASP A 1 358 ? -22.400 3.921   14.694 1.00 28.80  ? 359  ASP A CA    1 
ATOM   2691 C  C     . ASP A 1 358 ? -23.214 5.204   14.932 1.00 30.30  ? 359  ASP A C     1 
ATOM   2692 O  O     . ASP A 1 358 ? -23.534 5.888   13.949 1.00 34.02  ? 359  ASP A O     1 
ATOM   2693 C  CB    . ASP A 1 358 ? -23.045 3.064   13.594 1.00 28.06  ? 359  ASP A CB    1 
ATOM   2694 C  CG    . ASP A 1 358 ? -24.465 2.644   13.908 1.00 37.99  ? 359  ASP A CG    1 
ATOM   2695 O  OD1   . ASP A 1 358 ? -25.026 3.093   14.919 1.00 28.58  ? 359  ASP A OD1   1 
ATOM   2696 O  OD2   . ASP A 1 358 ? -25.038 1.834   13.145 1.00 40.23  ? 359  ASP A OD2   1 
ATOM   2697 N  N     . GLY A 1 359 ? -23.539 5.557   16.195 1.00 25.91  ? 360  GLY A N     1 
ATOM   2698 C  CA    . GLY A 1 359 ? -24.268 6.760   16.559 1.00 29.17  ? 360  GLY A CA    1 
ATOM   2699 C  C     . GLY A 1 359 ? -25.759 6.594   16.678 1.00 26.40  ? 360  GLY A C     1 
ATOM   2700 O  O     . GLY A 1 359 ? -26.437 7.528   17.133 1.00 27.59  ? 360  GLY A O     1 
ATOM   2701 N  N     . SER A 1 360 ? -26.289 5.464   16.240 1.00 26.26  ? 361  SER A N     1 
ATOM   2702 C  CA    . SER A 1 360 ? -27.718 5.263   16.295 1.00 24.23  ? 361  SER A CA    1 
ATOM   2703 C  C     . SER A 1 360 ? -28.165 4.858   17.692 1.00 22.55  ? 361  SER A C     1 
ATOM   2704 O  O     . SER A 1 360 ? -27.386 4.421   18.542 1.00 24.97  ? 361  SER A O     1 
ATOM   2705 C  CB    . SER A 1 360 ? -28.170 4.206   15.301 1.00 25.37  ? 361  SER A CB    1 
ATOM   2706 O  OG    . SER A 1 360 ? -27.602 2.954   15.554 1.00 29.59  ? 361  SER A OG    1 
ATOM   2707 N  N     . ALA A 1 361 ? -29.450 5.014   17.913 1.00 22.98  ? 362  ALA A N     1 
ATOM   2708 C  CA    . ALA A 1 361 ? -30.039 4.643   19.196 1.00 22.94  ? 362  ALA A CA    1 
ATOM   2709 C  C     . ALA A 1 361 ? -30.125 3.133   19.289 1.00 26.04  ? 362  ALA A C     1 
ATOM   2710 O  O     . ALA A 1 361 ? -30.374 2.449   18.293 1.00 28.39  ? 362  ALA A O     1 
ATOM   2711 C  CB    . ALA A 1 361 ? -31.418 5.227   19.325 1.00 25.33  ? 362  ALA A CB    1 
ATOM   2712 N  N     . ALA A 1 362 ? -29.929 2.608   20.481 1.00 22.03  ? 363  ALA A N     1 
ATOM   2713 C  CA    . ALA A 1 362 ? -30.028 1.181   20.717 1.00 20.38  ? 363  ALA A CA    1 
ATOM   2714 C  C     . ALA A 1 362 ? -31.122 0.929   21.731 1.00 18.85  ? 363  ALA A C     1 
ATOM   2715 O  O     . ALA A 1 362 ? -31.323 1.731   22.638 1.00 21.88  ? 363  ALA A O     1 
ATOM   2716 C  CB    . ALA A 1 362 ? -28.727 0.563   21.231 1.00 21.08  ? 363  ALA A CB    1 
ATOM   2717 N  N     . GLU A 1 363 ? -31.741 -0.256  21.599 1.00 25.03  ? 364  GLU A N     1 
ATOM   2718 C  CA    . GLU A 1 363 ? -32.838 -0.674  22.461 1.00 23.32  ? 364  GLU A CA    1 
ATOM   2719 C  C     . GLU A 1 363 ? -32.358 -1.278  23.773 1.00 20.85  ? 364  GLU A C     1 
ATOM   2720 O  O     . GLU A 1 363 ? -33.083 -1.277  24.774 1.00 21.58  ? 364  GLU A O     1 
ATOM   2721 C  CB    . GLU A 1 363 ? -33.756 -1.668  21.701 1.00 21.43  ? 364  GLU A CB    1 
ATOM   2722 C  CG    . GLU A 1 363 ? -34.831 -0.989  20.814 1.00 39.26  ? 364  GLU A CG    1 
ATOM   2723 C  CD    . GLU A 1 363 ? -34.334 -0.311  19.537 1.00 58.16  ? 364  GLU A CD    1 
ATOM   2724 O  OE1   . GLU A 1 363 ? -33.203 -0.579  19.039 1.00 49.67  ? 364  GLU A OE1   1 
ATOM   2725 O  OE2   . GLU A 1 363 ? -35.102 0.567   19.066 1.00 66.96  ? 364  GLU A OE2   1 
ATOM   2726 N  N     . MET A 1 364 ? -31.138 -1.802  23.805 1.00 20.51  ? 365  MET A N     1 
ATOM   2727 C  CA    . MET A 1 364 ? -30.710 -2.545  24.972 1.00 19.41  ? 365  MET A CA    1 
ATOM   2728 C  C     . MET A 1 364 ? -29.234 -2.805  24.774 1.00 19.64  ? 365  MET A C     1 
ATOM   2729 O  O     . MET A 1 364 ? -28.697 -2.549  23.690 1.00 21.84  ? 365  MET A O     1 
ATOM   2730 C  CB    . MET A 1 364 ? -31.508 -3.851  25.182 1.00 22.28  ? 365  MET A CB    1 
ATOM   2731 C  CG    . MET A 1 364 ? -31.096 -5.026  24.373 1.00 22.27  ? 365  MET A CG    1 
ATOM   2732 S  SD    . MET A 1 364 ? -31.907 -5.034  22.746 1.00 39.84  ? 365  MET A SD    1 
ATOM   2733 C  CE    . MET A 1 364 ? -33.514 -5.757  22.696 1.00 53.30  ? 365  MET A CE    1 
ATOM   2734 N  N     . VAL A 1 365 ? -28.562 -3.272  25.835 1.00 18.27  ? 366  VAL A N     1 
ATOM   2735 C  CA    . VAL A 1 365 ? -27.226 -3.839  25.690 1.00 17.63  ? 366  VAL A CA    1 
ATOM   2736 C  C     . VAL A 1 365 ? -27.187 -5.158  26.432 1.00 16.33  ? 366  VAL A C     1 
ATOM   2737 O  O     . VAL A 1 365 ? -27.610 -5.243  27.589 1.00 19.28  ? 366  VAL A O     1 
ATOM   2738 C  CB    . VAL A 1 365 ? -26.162 -2.863  26.137 1.00 19.47  ? 366  VAL A CB    1 
ATOM   2739 C  CG1   . VAL A 1 365 ? -24.730 -3.456  26.050 1.00 19.08  ? 366  VAL A CG1   1 
ATOM   2740 C  CG2   . VAL A 1 365 ? -26.287 -1.770  25.273 1.00 46.34  ? 366  VAL A CG2   1 
ATOM   2741 N  N     . ILE A 1 366 ? -26.792 -6.206  25.711 1.00 18.94  ? 367  ILE A N     1 
ATOM   2742 C  CA    . ILE A 1 366 ? -26.949 -7.568  26.212 1.00 19.60  ? 367  ILE A CA    1 
ATOM   2743 C  C     . ILE A 1 366 ? -25.729 -7.893  27.064 1.00 18.66  ? 367  ILE A C     1 
ATOM   2744 O  O     . ILE A 1 366 ? -24.675 -7.244  26.953 1.00 20.69  ? 367  ILE A O     1 
ATOM   2745 C  CB    . ILE A 1 366 ? -27.098 -8.589  25.065 1.00 20.74  ? 367  ILE A CB    1 
ATOM   2746 C  CG1   . ILE A 1 366 ? -25.833 -8.671  24.271 1.00 22.90  ? 367  ILE A CG1   1 
ATOM   2747 C  CG2   . ILE A 1 366 ? -28.334 -8.211  24.208 1.00 28.77  ? 367  ILE A CG2   1 
ATOM   2748 C  CD1   . ILE A 1 366 ? -25.846 -9.834  23.191 1.00 28.31  ? 367  ILE A CD1   1 
ATOM   2749 N  N     . PRO A 1 367 ? -25.849 -8.875  27.940 1.00 20.74  ? 368  PRO A N     1 
ATOM   2750 C  CA    . PRO A 1 367 ? -24.669 -9.296  28.722 1.00 21.89  ? 368  PRO A CA    1 
ATOM   2751 C  C     . PRO A 1 367 ? -23.494 -9.692  27.843 1.00 20.00  ? 368  PRO A C     1 
ATOM   2752 O  O     . PRO A 1 367 ? -23.638 -10.399 26.838 1.00 22.72  ? 368  PRO A O     1 
ATOM   2753 C  CB    . PRO A 1 367 ? -25.192 -10.484 29.540 1.00 21.31  ? 368  PRO A CB    1 
ATOM   2754 C  CG    . PRO A 1 367 ? -26.711 -10.226 29.670 1.00 23.87  ? 368  PRO A CG    1 
ATOM   2755 C  CD    . PRO A 1 367 ? -27.046 -9.654  28.285 1.00 22.48  ? 368  PRO A CD    1 
ATOM   2756 N  N     . GLY A 1 368 ? -22.301 -9.258  28.259 1.00 19.13  ? 369  GLY A N     1 
ATOM   2757 C  CA    . GLY A 1 368 ? -21.093 -9.456  27.499 1.00 21.34  ? 369  GLY A CA    1 
ATOM   2758 C  C     . GLY A 1 368 ? -20.817 -8.382  26.501 1.00 20.51  ? 369  GLY A C     1 
ATOM   2759 O  O     . GLY A 1 368 ? -19.750 -8.399  25.885 1.00 22.01  ? 369  GLY A O     1 
ATOM   2760 N  N     . ASP A 1 369 ? -21.747 -7.443  26.301 1.00 20.60  ? 370  ASP A N     1 
ATOM   2761 C  CA    . ASP A 1 369 ? -21.545 -6.346  25.358 1.00 22.00  ? 370  ASP A CA    1 
ATOM   2762 C  C     . ASP A 1 369 ? -21.291 -5.054  26.131 1.00 19.43  ? 370  ASP A C     1 
ATOM   2763 O  O     . ASP A 1 369 ? -21.498 -4.968  27.334 1.00 18.94  ? 370  ASP A O     1 
ATOM   2764 C  CB    . ASP A 1 369 ? -22.755 -6.139  24.418 1.00 20.25  ? 370  ASP A CB    1 
ATOM   2765 C  CG    . ASP A 1 369 ? -22.904 -7.238  23.359 1.00 39.45  ? 370  ASP A CG    1 
ATOM   2766 O  OD1   . ASP A 1 369 ? -22.052 -8.141  23.274 1.00 39.21  ? 370  ASP A OD1   1 
ATOM   2767 O  OD2   . ASP A 1 369 ? -23.833 -7.114  22.521 1.00 41.78  ? 370  ASP A OD2   1 
ATOM   2768 N  N     . ARG A 1 370 ? -20.871 -4.055  25.406 1.00 17.15  ? 371  ARG A N     1 
ATOM   2769 C  CA    . ARG A 1 370 ? -20.592 -2.719  25.912 1.00 16.53  ? 371  ARG A CA    1 
ATOM   2770 C  C     . ARG A 1 370 ? -21.283 -1.686  25.045 1.00 17.38  ? 371  ARG A C     1 
ATOM   2771 O  O     . ARG A 1 370 ? -21.510 -1.898  23.850 1.00 18.50  ? 371  ARG A O     1 
ATOM   2772 C  CB    . ARG A 1 370 ? -19.044 -2.404  26.052 1.00 19.97  ? 371  ARG A CB    1 
ATOM   2773 C  CG    . ARG A 1 370 ? -18.399 -2.479  24.642 1.00 20.01  ? 371  ARG A CG    1 
ATOM   2774 C  CD    . ARG A 1 370 ? -17.176 -1.617  24.364 1.00 24.59  ? 371  ARG A CD    1 
ATOM   2775 N  NE    . ARG A 1 370 ? -17.852 -0.337  24.170 1.00 25.99  ? 371  ARG A NE    1 
ATOM   2776 C  CZ    . ARG A 1 370 ? -18.150 0.120   22.940 1.00 22.24  ? 371  ARG A CZ    1 
ATOM   2777 N  NH1   . ARG A 1 370 ? -18.802 1.284   22.791 1.00 23.25  ? 371  ARG A NH1   1 
ATOM   2778 N  NH2   . ARG A 1 370 ? -17.994 -0.719  21.913 1.00 23.83  ? 371  ARG A NH2   1 
ATOM   2779 N  N     . ILE A 1 371 ? -21.627 -0.548  25.647 1.00 17.55  ? 372  ILE A N     1 
ATOM   2780 C  CA    . ILE A 1 371 ? -22.244 0.532   24.899 1.00 17.37  ? 372  ILE A CA    1 
ATOM   2781 C  C     . ILE A 1 371 ? -22.045 1.852   25.618 1.00 16.39  ? 372  ILE A C     1 
ATOM   2782 O  O     . ILE A 1 371 ? -21.786 1.889   26.826 1.00 17.71  ? 372  ILE A O     1 
ATOM   2783 C  CB    . ILE A 1 371 ? -23.742 0.241   24.670 1.00 18.66  ? 372  ILE A CB    1 
ATOM   2784 C  CG1   . ILE A 1 371 ? -24.280 1.025   23.475 1.00 21.64  ? 372  ILE A CG1   1 
ATOM   2785 C  CG2   . ILE A 1 371 ? -24.542 0.694   25.915 1.00 19.92  ? 372  ILE A CG2   1 
ATOM   2786 C  CD1   . ILE A 1 371 ? -25.630 0.522   22.966 1.00 20.17  ? 372  ILE A CD1   1 
ATOM   2787 N  N     . LYS A 1 372 ? -22.176 2.945   24.875 1.00 16.02  ? 373  LYS A N     1 
ATOM   2788 C  CA    . LYS A 1 372 ? -22.264 4.288   25.446 1.00 15.94  ? 373  LYS A CA    1 
ATOM   2789 C  C     . LYS A 1 372 ? -23.690 4.531   25.962 1.00 16.22  ? 373  LYS A C     1 
ATOM   2790 O  O     . LYS A 1 372 ? -24.664 4.279   25.253 1.00 16.58  ? 373  LYS A O     1 
ATOM   2791 C  CB    . LYS A 1 372 ? -21.942 5.336   24.385 1.00 17.36  ? 373  LYS A CB    1 
ATOM   2792 C  CG    . LYS A 1 372 ? -21.975 6.784   24.963 1.00 20.17  ? 373  LYS A CG    1 
ATOM   2793 C  CD    . LYS A 1 372 ? -22.040 7.830   23.878 1.00 35.51  ? 373  LYS A CD    1 
ATOM   2794 C  CE    . LYS A 1 372 ? -20.820 7.964   23.033 1.00 50.49  ? 373  LYS A CE    1 
ATOM   2795 N  NZ    . LYS A 1 372 ? -21.252 8.952   21.985 1.00 38.30  ? 373  LYS A NZ    1 
ATOM   2796 N  N     . MET A 1 373 ? -23.822 4.984   27.198 1.00 16.63  ? 374  MET A N     1 
ATOM   2797 C  CA    . MET A 1 373 ? -25.129 5.341   27.738 1.00 15.73  ? 374  MET A CA    1 
ATOM   2798 C  C     . MET A 1 373 ? -24.985 6.476   28.713 1.00 15.24  ? 374  MET A C     1 
ATOM   2799 O  O     . MET A 1 373 ? -23.898 6.779   29.188 1.00 17.10  ? 374  MET A O     1 
ATOM   2800 C  CB    . MET A 1 373 ? -25.827 4.167   28.459 1.00 15.99  ? 374  MET A CB    1 
ATOM   2801 C  CG    . MET A 1 373 ? -24.980 3.668   29.672 1.00 18.28  ? 374  MET A CG    1 
ATOM   2802 S  SD    . MET A 1 373 ? -25.824 2.284   30.542 1.00 18.80  ? 374  MET A SD    1 
ATOM   2803 C  CE    . MET A 1 373 ? -25.794 0.952   29.316 1.00 17.06  ? 374  MET A CE    1 
ATOM   2804 N  N     . THR A 1 374 ? -26.084 7.122   28.996 1.00 14.65  ? 375  THR A N     1 
ATOM   2805 C  CA    . THR A 1 374 ? -26.164 8.200   29.954 1.00 14.94  ? 375  THR A CA    1 
ATOM   2806 C  C     . THR A 1 374 ? -26.660 7.668   31.282 1.00 15.15  ? 375  THR A C     1 
ATOM   2807 O  O     . THR A 1 374 ? -27.567 6.823   31.360 1.00 16.60  ? 375  THR A O     1 
ATOM   2808 C  CB    . THR A 1 374 ? -27.047 9.313   29.415 1.00 16.74  ? 375  THR A CB    1 
ATOM   2809 O  OG1   . THR A 1 374 ? -26.403 9.898   28.255 1.00 21.87  ? 375  THR A OG1   1 
ATOM   2810 C  CG2   . THR A 1 374 ? -27.370 10.397  30.486 1.00 18.37  ? 375  THR A CG2   1 
ATOM   2811 N  N     . VAL A 1 375 ? -26.035 8.155   32.351 1.00 16.15  ? 376  VAL A N     1 
ATOM   2812 C  CA    . VAL A 1 375 ? -26.396 7.844   33.742 1.00 16.39  ? 376  VAL A CA    1 
ATOM   2813 C  C     . VAL A 1 375 ? -26.842 9.136   34.415 1.00 15.62  ? 376  VAL A C     1 
ATOM   2814 O  O     . VAL A 1 375 ? -26.163 10.171  34.310 1.00 16.85  ? 376  VAL A O     1 
ATOM   2815 C  CB    . VAL A 1 375 ? -25.202 7.266   34.524 1.00 15.12  ? 376  VAL A CB    1 
ATOM   2816 C  CG1   . VAL A 1 375 ? -25.603 7.045   35.998 1.00 16.49  ? 376  VAL A CG1   1 
ATOM   2817 C  CG2   . VAL A 1 375 ? -24.705 5.981   33.869 1.00 17.15  ? 376  VAL A CG2   1 
ATOM   2818 N  N     . GLU A 1 376 ? -27.953 9.080   35.146 1.00 15.96  ? 377  GLU A N     1 
ATOM   2819 C  CA    . GLU A 1 376 ? -28.410 10.191  35.958 1.00 16.95  ? 377  GLU A CA    1 
ATOM   2820 C  C     . GLU A 1 376 ? -28.564 9.674   37.374 1.00 18.68  ? 377  GLU A C     1 
ATOM   2821 O  O     . GLU A 1 376 ? -29.332 8.739   37.622 1.00 18.16  ? 377  GLU A O     1 
ATOM   2822 C  CB    . GLU A 1 376 ? -29.754 10.757  35.465 1.00 18.18  ? 377  GLU A CB    1 
ATOM   2823 C  CG    . GLU A 1 376 ? -30.071 12.031  36.285 1.00 21.28  ? 377  GLU A CG    1 
ATOM   2824 C  CD    . GLU A 1 376 ? -31.336 12.763  35.851 1.00 35.65  ? 377  GLU A CD    1 
ATOM   2825 O  OE1   . GLU A 1 376 ? -31.988 12.328  34.883 1.00 38.79  ? 377  GLU A OE1   1 
ATOM   2826 O  OE2   . GLU A 1 376 ? -31.696 13.771  36.497 1.00 39.15  ? 377  GLU A OE2   1 
ATOM   2827 N  N     . LEU A 1 377 ? -27.806 10.258  38.310 1.00 16.02  ? 378  LEU A N     1 
ATOM   2828 C  CA    . LEU A 1 377 ? -27.848 9.834   39.715 1.00 16.73  ? 378  LEU A CA    1 
ATOM   2829 C  C     . LEU A 1 377 ? -28.898 10.637  40.500 1.00 17.79  ? 378  LEU A C     1 
ATOM   2830 O  O     . LEU A 1 377 ? -29.180 11.784  40.174 1.00 20.25  ? 378  LEU A O     1 
ATOM   2831 C  CB    . LEU A 1 377 ? -26.466 10.067  40.359 1.00 16.16  ? 378  LEU A CB    1 
ATOM   2832 C  CG    . LEU A 1 377 ? -25.363 9.292   39.684 1.00 17.52  ? 378  LEU A CG    1 
ATOM   2833 C  CD1   . LEU A 1 377 ? -23.999 9.700   40.310 1.00 17.95  ? 378  LEU A CD1   1 
ATOM   2834 C  CD2   . LEU A 1 377 ? -25.619 7.803   39.710 1.00 18.67  ? 378  LEU A CD2   1 
ATOM   2835 N  N     . ILE A 1 378 ? -29.445 10.022  41.546 1.00 17.13  ? 379  ILE A N     1 
ATOM   2836 C  CA    . ILE A 1 378 ? -30.473 10.687  42.348 1.00 18.36  ? 379  ILE A CA    1 
ATOM   2837 C  C     . ILE A 1 378 ? -29.879 11.811  43.184 1.00 20.99  ? 379  ILE A C     1 
ATOM   2838 O  O     . ILE A 1 378 ? -30.580 12.788  43.472 1.00 23.55  ? 379  ILE A O     1 
ATOM   2839 C  CB    . ILE A 1 378 ? -31.191 9.658   43.222 1.00 21.44  ? 379  ILE A CB    1 
ATOM   2840 C  CG1   . ILE A 1 378 ? -32.414 10.330  43.887 1.00 25.77  ? 379  ILE A CG1   1 
ATOM   2841 C  CG2   . ILE A 1 378 ? -30.262 9.037   44.283 1.00 21.32  ? 379  ILE A CG2   1 
ATOM   2842 C  CD1   . ILE A 1 378 ? -33.380 9.321   44.493 1.00 31.08  ? 379  ILE A CD1   1 
ATOM   2843 N  N     . ASN A 1 379 ? -28.605 11.707  43.553 1.00 19.99  ? 380  ASN A N     1 
ATOM   2844 C  CA    . ASN A 1 379 ? -27.935 12.706  44.377 1.00 23.05  ? 380  ASN A CA    1 
ATOM   2845 C  C     . ASN A 1 379 ? -26.626 13.075  43.691 1.00 19.35  ? 380  ASN A C     1 
ATOM   2846 O  O     . ASN A 1 379 ? -26.013 12.227  43.042 1.00 18.28  ? 380  ASN A O     1 
ATOM   2847 C  CB    . ASN A 1 379 ? -27.628 12.143  45.775 1.00 23.03  ? 380  ASN A CB    1 
ATOM   2848 C  CG    . ASN A 1 379 ? -28.878 11.836  46.570 1.00 25.10  ? 380  ASN A CG    1 
ATOM   2849 O  OD1   . ASN A 1 379 ? -29.828 12.616  46.573 1.00 30.30  ? 380  ASN A OD1   1 
ATOM   2850 N  ND2   . ASN A 1 379 ? -28.845 10.744  47.288 1.00 28.23  ? 380  ASN A ND2   1 
ATOM   2851 N  N     . PRO A 1 380 ? -26.152 14.304  43.851 1.00 17.06  ? 381  PRO A N     1 
ATOM   2852 C  CA    . PRO A 1 380 ? -24.870 14.692  43.248 1.00 17.73  ? 381  PRO A CA    1 
ATOM   2853 C  C     . PRO A 1 380 ? -23.687 14.059  43.974 1.00 17.29  ? 381  PRO A C     1 
ATOM   2854 O  O     . PRO A 1 380 ? -23.685 13.892  45.193 1.00 19.03  ? 381  PRO A O     1 
ATOM   2855 C  CB    . PRO A 1 380 ? -24.845 16.207  43.425 1.00 20.25  ? 381  PRO A CB    1 
ATOM   2856 C  CG    . PRO A 1 380 ? -25.776 16.446  44.582 1.00 29.90  ? 381  PRO A CG    1 
ATOM   2857 C  CD    . PRO A 1 380 ? -26.809 15.371  44.610 1.00 23.66  ? 381  PRO A CD    1 
ATOM   2858 N  N     . ILE A 1 381 ? -22.681 13.685  43.202 1.00 15.16  ? 382  ILE A N     1 
ATOM   2859 C  CA    . ILE A 1 381 ? -21.474 13.091  43.767 1.00 16.25  ? 382  ILE A CA    1 
ATOM   2860 C  C     . ILE A 1 381 ? -20.298 13.632  42.960 1.00 16.60  ? 382  ILE A C     1 
ATOM   2861 O  O     . ILE A 1 381 ? -20.449 14.149  41.824 1.00 15.88  ? 382  ILE A O     1 
ATOM   2862 C  CB    . ILE A 1 381 ? -21.606 11.566  43.744 1.00 21.18  ? 382  ILE A CB    1 
ATOM   2863 C  CG1   . ILE A 1 381 ? -20.653 10.905  44.776 1.00 28.64  ? 382  ILE A CG1   1 
ATOM   2864 C  CG2   . ILE A 1 381 ? -21.375 11.043  42.406 1.00 21.60  ? 382  ILE A CG2   1 
ATOM   2865 C  CD1   . ILE A 1 381 ? -21.177 9.597   45.395 1.00 26.49  ? 382  ILE A CD1   1 
ATOM   2866 N  N     . ALA A 1 382 ? -19.096 13.622  43.570 1.00 15.98  ? 383  ALA A N     1 
ATOM   2867 C  CA    . ALA A 1 382 ? -17.945 14.127  42.822 1.00 13.13  ? 383  ALA A CA    1 
ATOM   2868 C  C     . ALA A 1 382 ? -17.713 13.191  41.631 1.00 16.56  ? 383  ALA A C     1 
ATOM   2869 O  O     . ALA A 1 382 ? -17.597 11.984  41.804 1.00 18.32  ? 383  ALA A O     1 
ATOM   2870 C  CB    . ALA A 1 382 ? -16.708 14.184  43.715 1.00 15.98  ? 383  ALA A CB    1 
ATOM   2871 N  N     . ILE A 1 383 ? -17.721 13.749  40.424 1.00 15.86  ? 384  ILE A N     1 
ATOM   2872 C  CA    . ILE A 1 383 ? -17.582 12.949  39.214 1.00 16.97  ? 384  ILE A CA    1 
ATOM   2873 C  C     . ILE A 1 383 ? -16.554 13.661  38.356 1.00 16.09  ? 384  ILE A C     1 
ATOM   2874 O  O     . ILE A 1 383 ? -16.593 14.882  38.247 1.00 17.89  ? 384  ILE A O     1 
ATOM   2875 C  CB    . ILE A 1 383 ? -18.931 12.853  38.428 1.00 17.00  ? 384  ILE A CB    1 
ATOM   2876 C  CG1   . ILE A 1 383 ? -20.034 12.094  39.153 1.00 21.77  ? 384  ILE A CG1   1 
ATOM   2877 C  CG2   . ILE A 1 383 ? -18.658 12.204  37.022 1.00 21.05  ? 384  ILE A CG2   1 
ATOM   2878 C  CD1   . ILE A 1 383 ? -19.798 10.650  39.417 1.00 27.93  ? 384  ILE A CD1   1 
ATOM   2879 N  N     . GLU A 1 384 ? -15.676 12.891  37.701 1.00 16.59  ? 385  GLU A N     1 
ATOM   2880 C  CA    . GLU A 1 384 ? -14.765 13.443  36.690 1.00 15.93  ? 385  GLU A CA    1 
ATOM   2881 C  C     . GLU A 1 384 ? -14.639 12.432  35.564 1.00 14.22  ? 385  GLU A C     1 
ATOM   2882 O  O     . GLU A 1 384 ? -14.858 11.247  35.763 1.00 15.90  ? 385  GLU A O     1 
ATOM   2883 C  CB    . GLU A 1 384 ? -13.383 13.757  37.307 1.00 19.95  ? 385  GLU A CB    1 
ATOM   2884 C  CG    . GLU A 1 384 ? -12.688 12.548  37.862 1.00 18.86  ? 385  GLU A CG    1 
ATOM   2885 C  CD    . GLU A 1 384 ? -11.423 12.888  38.700 1.00 19.56  ? 385  GLU A CD    1 
ATOM   2886 O  OE1   . GLU A 1 384 ? -11.118 14.093  38.823 1.00 23.28  ? 385  GLU A OE1   1 
ATOM   2887 O  OE2   . GLU A 1 384 ? -10.841 11.897  39.200 1.00 22.72  ? 385  GLU A OE2   1 
ATOM   2888 N  N     . GLN A 1 385 ? -14.235 12.950  34.403 1.00 17.45  ? 386  GLN A N     1 
ATOM   2889 C  CA    . GLN A 1 385 ? -13.918 12.059  33.300 1.00 19.40  ? 386  GLN A CA    1 
ATOM   2890 C  C     . GLN A 1 385 ? -12.870 11.033  33.702 1.00 22.11  ? 386  GLN A C     1 
ATOM   2891 O  O     . GLN A 1 385 ? -11.850 11.371  34.338 1.00 20.87  ? 386  GLN A O     1 
ATOM   2892 C  CB    . GLN A 1 385 ? -13.448 12.843  32.088 1.00 24.36  ? 386  GLN A CB    1 
ATOM   2893 C  CG    . GLN A 1 385 ? -14.506 13.552  31.354 1.00 27.59  ? 386  GLN A CG    1 
ATOM   2894 C  CD    . GLN A 1 385 ? -14.020 13.953  29.956 1.00 37.61  ? 386  GLN A CD    1 
ATOM   2895 O  OE1   . GLN A 1 385 ? -12.902 13.631  29.560 1.00 52.08  ? 386  GLN A OE1   1 
ATOM   2896 N  NE2   . GLN A 1 385 ? -14.851 14.643  29.226 1.00 42.63  ? 386  GLN A NE2   1 
ATOM   2897 N  N     . GLY A 1 386 ? -13.082 9.789   33.341 1.00 18.73  ? 387  GLY A N     1 
ATOM   2898 C  CA    . GLY A 1 386 ? -12.175 8.713   33.705 1.00 18.40  ? 387  GLY A CA    1 
ATOM   2899 C  C     . GLY A 1 386 ? -12.473 8.010   35.003 1.00 18.76  ? 387  GLY A C     1 
ATOM   2900 O  O     . GLY A 1 386 ? -11.839 6.993   35.312 1.00 22.52  ? 387  GLY A O     1 
ATOM   2901 N  N     . MET A 1 387 ? -13.400 8.521   35.797 1.00 16.83  ? 388  MET A N     1 
ATOM   2902 C  CA    . MET A 1 387 ? -13.793 7.849   37.024 1.00 17.32  ? 388  MET A CA    1 
ATOM   2903 C  C     . MET A 1 387 ? -14.475 6.531   36.671 1.00 20.24  ? 388  MET A C     1 
ATOM   2904 O  O     . MET A 1 387 ? -15.351 6.481   35.770 1.00 19.46  ? 388  MET A O     1 
ATOM   2905 C  CB    . MET A 1 387 ? -14.764 8.721   37.805 1.00 20.11  ? 388  MET A CB    1 
ATOM   2906 C  CG    . MET A 1 387 ? -15.087 8.181   39.238 1.00 22.57  ? 388  MET A CG    1 
ATOM   2907 S  SD    . MET A 1 387 ? -16.575 8.965   39.878 1.00 22.55  ? 388  MET A SD    1 
ATOM   2908 C  CE    . MET A 1 387 ? -17.797 7.974   38.980 1.00 19.58  ? 388  MET A CE    1 
ATOM   2909 N  N     . ARG A 1 388 ? -14.071 5.478   37.326 1.00 19.58  ? 389  ARG A N     1 
ATOM   2910 C  CA    . ARG A 1 388 ? -14.740 4.195   37.233 1.00 17.98  ? 389  ARG A CA    1 
ATOM   2911 C  C     . ARG A 1 388 ? -15.822 4.025   38.283 1.00 20.08  ? 389  ARG A C     1 
ATOM   2912 O  O     . ARG A 1 388 ? -15.786 4.583   39.400 1.00 20.90  ? 389  ARG A O     1 
ATOM   2913 C  CB    . ARG A 1 388 ? -13.746 3.030   37.348 1.00 20.33  ? 389  ARG A CB    1 
ATOM   2914 C  CG    . ARG A 1 388 ? -13.183 2.607   36.052 1.00 24.69  ? 389  ARG A CG    1 
ATOM   2915 C  CD    . ARG A 1 388 ? -12.358 3.635   35.386 1.00 26.88  ? 389  ARG A CD    1 
ATOM   2916 N  NE    . ARG A 1 388 ? -11.768 3.121   34.122 1.00 27.64  ? 389  ARG A NE    1 
ATOM   2917 C  CZ    . ARG A 1 388 ? -10.816 3.777   33.455 1.00 25.30  ? 389  ARG A CZ    1 
ATOM   2918 N  NH1   . ARG A 1 388 ? -10.378 4.963   33.922 1.00 27.86  ? 389  ARG A NH1   1 
ATOM   2919 N  NH2   . ARG A 1 388 ? -10.291 3.240   32.351 1.00 24.69  ? 389  ARG A NH2   1 
ATOM   2920 N  N     . PHE A 1 389 ? -16.801 3.201   37.943 1.00 18.65  ? 390  PHE A N     1 
ATOM   2921 C  CA    . PHE A 1 389 ? -17.858 2.866   38.865 1.00 17.33  ? 390  PHE A CA    1 
ATOM   2922 C  C     . PHE A 1 389 ? -18.338 1.457   38.544 1.00 18.22  ? 390  PHE A C     1 
ATOM   2923 O  O     . PHE A 1 389 ? -18.128 0.954   37.434 1.00 19.58  ? 390  PHE A O     1 
ATOM   2924 C  CB    . PHE A 1 389 ? -19.030 3.849   38.790 1.00 17.63  ? 390  PHE A CB    1 
ATOM   2925 C  CG    . PHE A 1 389 ? -19.601 3.991   37.397 1.00 17.64  ? 390  PHE A CG    1 
ATOM   2926 C  CD1   . PHE A 1 389 ? -19.086 4.955   36.520 1.00 17.65  ? 390  PHE A CD1   1 
ATOM   2927 C  CD2   . PHE A 1 389 ? -20.677 3.211   37.010 1.00 20.02  ? 390  PHE A CD2   1 
ATOM   2928 C  CE1   . PHE A 1 389 ? -19.622 5.109   35.217 1.00 16.71  ? 390  PHE A CE1   1 
ATOM   2929 C  CE2   . PHE A 1 389 ? -21.249 3.338   35.729 1.00 19.14  ? 390  PHE A CE2   1 
ATOM   2930 C  CZ    . PHE A 1 389 ? -20.728 4.273   34.808 1.00 17.52  ? 390  PHE A CZ    1 
ATOM   2931 N  N     . ALA A 1 390 ? -18.943 0.809   39.525 1.00 16.96  ? 391  ALA A N     1 
ATOM   2932 C  CA    . ALA A 1 390 ? -19.601 -0.464  39.330 1.00 18.26  ? 391  ALA A CA    1 
ATOM   2933 C  C     . ALA A 1 390 ? -21.110 -0.255  39.317 1.00 18.18  ? 391  ALA A C     1 
ATOM   2934 O  O     . ALA A 1 390 ? -21.647 0.694   39.895 1.00 20.08  ? 391  ALA A O     1 
ATOM   2935 C  CB    . ALA A 1 390 ? -19.216 -1.451  40.427 1.00 20.16  ? 391  ALA A CB    1 
ATOM   2936 N  N     . ILE A 1 391 ? -21.823 -1.117  38.590 1.00 18.71  ? 392  ILE A N     1 
ATOM   2937 C  CA    . ILE A 1 391 ? -23.279 -1.124  38.591 1.00 19.39  ? 392  ILE A CA    1 
ATOM   2938 C  C     . ILE A 1 391 ? -23.698 -2.374  39.343 1.00 20.35  ? 392  ILE A C     1 
ATOM   2939 O  O     . ILE A 1 391 ? -23.225 -3.471  39.045 1.00 20.04  ? 392  ILE A O     1 
ATOM   2940 C  CB    . ILE A 1 391 ? -23.834 -1.087  37.152 1.00 18.38  ? 392  ILE A CB    1 
ATOM   2941 C  CG1   . ILE A 1 391 ? -23.230 0.151   36.520 1.00 19.02  ? 392  ILE A CG1   1 
ATOM   2942 C  CG2   . ILE A 1 391 ? -25.344 -1.054  37.214 1.00 20.08  ? 392  ILE A CG2   1 
ATOM   2943 C  CD1   . ILE A 1 391 ? -23.435 0.177   34.971 1.00 26.42  ? 392  ILE A CD1   1 
ATOM   2944 N  N     . ARG A 1 392 ? -24.570 -2.217  40.318 1.00 19.67  ? 393  ARG A N     1 
ATOM   2945 C  CA    . ARG A 1 392 ? -24.871 -3.277  41.276 1.00 20.21  ? 393  ARG A CA    1 
ATOM   2946 C  C     . ARG A 1 392 ? -26.369 -3.468  41.430 1.00 21.41  ? 393  ARG A C     1 
ATOM   2947 O  O     . ARG A 1 392 ? -27.171 -2.528  41.290 1.00 25.04  ? 393  ARG A O     1 
ATOM   2948 C  CB    . ARG A 1 392 ? -24.221 -2.913  42.674 1.00 20.48  ? 393  ARG A CB    1 
ATOM   2949 C  CG    . ARG A 1 392 ? -22.670 -2.906  42.542 1.00 24.18  ? 393  ARG A CG    1 
ATOM   2950 C  CD    . ARG A 1 392 ? -21.830 -2.840  43.807 1.00 24.21  ? 393  ARG A CD    1 
ATOM   2951 N  NE    . ARG A 1 392 ? -22.614 -2.603  44.990 1.00 33.96  ? 393  ARG A NE    1 
ATOM   2952 C  CZ    . ARG A 1 392 ? -22.093 -2.547  46.204 1.00 43.37  ? 393  ARG A CZ    1 
ATOM   2953 N  NH1   . ARG A 1 392 ? -20.837 -2.917  46.386 1.00 55.93  ? 393  ARG A NH1   1 
ATOM   2954 N  NH2   . ARG A 1 392 ? -22.865 -2.293  47.237 1.00 31.97  ? 393  ARG A NH2   1 
ATOM   2955 N  N     . GLU A 1 393 ? -26.759 -4.701  41.730 1.00 25.85  ? 394  GLU A N     1 
ATOM   2956 C  CA    . GLU A 1 393 ? -28.115 -4.946  42.180 1.00 31.15  ? 394  GLU A CA    1 
ATOM   2957 C  C     . GLU A 1 393 ? -27.989 -5.924  43.339 1.00 43.44  ? 394  GLU A C     1 
ATOM   2958 O  O     . GLU A 1 393 ? -27.340 -6.965  43.203 1.00 40.13  ? 394  GLU A O     1 
ATOM   2959 C  CB    . GLU A 1 393 ? -29.003 -5.459  41.038 1.00 37.72  ? 394  GLU A CB    1 
ATOM   2960 C  CG    . GLU A 1 393 ? -30.462 -5.089  41.284 1.00 57.79  ? 394  GLU A CG    1 
ATOM   2961 C  CD    . GLU A 1 393 ? -31.337 -5.245  40.064 1.00 75.17  ? 394  GLU A CD    1 
ATOM   2962 O  OE1   . GLU A 1 393 ? -30.859 -5.807  39.059 1.00 80.84  ? 394  GLU A OE1   1 
ATOM   2963 O  OE2   . GLU A 1 393 ? -32.492 -4.771  40.097 1.00 82.67  ? 394  GLU A OE2   1 
ATOM   2964 N  N     . GLY A 1 394 ? -28.490 -5.514  44.505 1.00 46.94  ? 395  GLY A N     1 
ATOM   2965 C  CA    . GLY A 1 394 ? -28.332 -6.279  45.735 1.00 47.20  ? 395  GLY A CA    1 
ATOM   2966 C  C     . GLY A 1 394 ? -26.898 -6.556  46.129 1.00 45.09  ? 395  GLY A C     1 
ATOM   2967 O  O     . GLY A 1 394 ? -26.580 -7.662  46.583 1.00 54.72  ? 395  GLY A O     1 
ATOM   2968 N  N     . GLY A 1 395 ? -26.010 -5.592  45.934 1.00 41.77  ? 396  GLY A N     1 
ATOM   2969 C  CA    . GLY A 1 395 ? -24.636 -5.766  46.341 1.00 44.29  ? 396  GLY A CA    1 
ATOM   2970 C  C     . GLY A 1 395 ? -23.771 -6.590  45.416 1.00 41.78  ? 396  GLY A C     1 
ATOM   2971 O  O     . GLY A 1 395 ? -22.555 -6.641  45.639 1.00 47.00  ? 396  GLY A O     1 
ATOM   2972 N  N     . ARG A 1 396 ? -24.332 -7.221  44.378 1.00 34.68  ? 397  ARG A N     1 
ATOM   2973 C  CA    . ARG A 1 396 ? -23.514 -7.950  43.412 1.00 34.29  ? 397  ARG A CA    1 
ATOM   2974 C  C     . ARG A 1 396 ? -23.256 -7.051  42.205 1.00 26.70  ? 397  ARG A C     1 
ATOM   2975 O  O     . ARG A 1 396 ? -24.152 -6.334  41.746 1.00 27.47  ? 397  ARG A O     1 
ATOM   2976 C  CB    . ARG A 1 396 ? -24.158 -9.266  42.942 1.00 43.29  ? 397  ARG A CB    1 
ATOM   2977 C  CG    . ARG A 1 396 ? -25.294 -9.135  41.937 1.00 60.72  ? 397  ARG A CG    1 
ATOM   2978 C  CD    . ARG A 1 396 ? -25.662 -10.464 41.243 1.00 69.18  ? 397  ARG A CD    1 
ATOM   2979 N  NE    . ARG A 1 396 ? -26.292 -11.448 42.122 1.00 82.93  ? 397  ARG A NE    1 
ATOM   2980 C  CZ    . ARG A 1 396 ? -27.598 -11.487 42.376 1.00 86.87  ? 397  ARG A CZ    1 
ATOM   2981 N  NH1   . ARG A 1 396 ? -28.394 -10.580 41.826 1.00 88.25  ? 397  ARG A NH1   1 
ATOM   2982 N  NH2   . ARG A 1 396 ? -28.103 -12.419 43.181 1.00 84.31  ? 397  ARG A NH2   1 
ATOM   2983 N  N     . THR A 1 397 ? -22.045 -7.094  41.704 1.00 28.74  ? 398  THR A N     1 
ATOM   2984 C  CA    . THR A 1 397 ? -21.710 -6.291  40.533 1.00 21.81  ? 398  THR A CA    1 
ATOM   2985 C  C     . THR A 1 397 ? -22.308 -6.943  39.279 1.00 23.66  ? 398  THR A C     1 
ATOM   2986 O  O     . THR A 1 397 ? -22.093 -8.125  39.004 1.00 28.90  ? 398  THR A O     1 
ATOM   2987 C  CB    . THR A 1 397 ? -20.185 -6.105  40.427 1.00 28.51  ? 398  THR A CB    1 
ATOM   2988 O  OG1   . THR A 1 397 ? -19.748 -5.283  41.532 1.00 28.95  ? 398  THR A OG1   1 
ATOM   2989 C  CG2   . THR A 1 397 ? -19.703 -5.424  39.104 1.00 22.52  ? 398  THR A CG2   1 
ATOM   2990 N  N     . ILE A 1 398 ? -23.075 -6.164  38.522 1.00 22.02  ? 399  ILE A N     1 
ATOM   2991 C  CA    . ILE A 1 398 ? -23.707 -6.641  37.290 1.00 22.64  ? 399  ILE A CA    1 
ATOM   2992 C  C     . ILE A 1 398 ? -23.227 -5.868  36.080 1.00 19.39  ? 399  ILE A C     1 
ATOM   2993 O  O     . ILE A 1 398 ? -23.511 -6.280  34.937 1.00 18.75  ? 399  ILE A O     1 
ATOM   2994 C  CB    . ILE A 1 398 ? -25.260 -6.577  37.358 1.00 21.13  ? 399  ILE A CB    1 
ATOM   2995 C  CG1   . ILE A 1 398 ? -25.727 -5.138  37.616 1.00 22.05  ? 399  ILE A CG1   1 
ATOM   2996 C  CG2   . ILE A 1 398 ? -25.830 -7.530  38.454 1.00 24.72  ? 399  ILE A CG2   1 
ATOM   2997 C  CD1   . ILE A 1 398 ? -27.262 -4.878  37.395 1.00 26.52  ? 399  ILE A CD1   1 
ATOM   2998 N  N     . GLY A 1 399 ? -22.445 -4.815  36.278 1.00 18.61  ? 400  GLY A N     1 
ATOM   2999 C  CA    . GLY A 1 399 ? -21.930 -4.023  35.182 1.00 15.34  ? 400  GLY A CA    1 
ATOM   3000 C  C     . GLY A 1 399 ? -20.755 -3.217  35.679 1.00 16.93  ? 400  GLY A C     1 
ATOM   3001 O  O     . GLY A 1 399 ? -20.576 -3.066  36.889 1.00 18.54  ? 400  GLY A O     1 
ATOM   3002 N  N     . ALA A 1 400 ? -20.005 -2.649  34.732 1.00 16.04  ? 401  ALA A N     1 
ATOM   3003 C  CA    . ALA A 1 400 ? -18.905 -1.749  35.067 1.00 15.54  ? 401  ALA A CA    1 
ATOM   3004 C  C     . ALA A 1 400 ? -18.926 -0.597  34.108 1.00 17.04  ? 401  ALA A C     1 
ATOM   3005 O  O     . ALA A 1 400 ? -19.246 -0.770  32.934 1.00 17.95  ? 401  ALA A O     1 
ATOM   3006 C  CB    . ALA A 1 400 ? -17.547 -2.476  34.969 1.00 21.13  ? 401  ALA A CB    1 
ATOM   3007 N  N     . GLY A 1 401 ? -18.546 0.583   34.565 1.00 16.08  ? 402  GLY A N     1 
ATOM   3008 C  CA    . GLY A 1 401 ? -18.550 1.738   33.715 1.00 15.44  ? 402  GLY A CA    1 
ATOM   3009 C  C     . GLY A 1 401 ? -17.375 2.661   33.954 1.00 16.05  ? 402  GLY A C     1 
ATOM   3010 O  O     . GLY A 1 401 ? -16.702 2.588   34.975 1.00 17.40  ? 402  GLY A O     1 
ATOM   3011 N  N     . VAL A 1 402 ? -17.170 3.533   32.994 1.00 14.41  ? 403  VAL A N     1 
ATOM   3012 C  CA    . VAL A 1 402 ? -16.234 4.656   33.075 1.00 17.11  ? 403  VAL A CA    1 
ATOM   3013 C  C     . VAL A 1 402 ? -16.907 5.922   32.559 1.00 16.98  ? 403  VAL A C     1 
ATOM   3014 O  O     . VAL A 1 402 ? -17.573 5.928   31.516 1.00 16.23  ? 403  VAL A O     1 
ATOM   3015 C  CB    . VAL A 1 402 ? -14.950 4.346   32.288 1.00 18.56  ? 403  VAL A CB    1 
ATOM   3016 C  CG1   . VAL A 1 402 ? -15.241 4.015   30.824 1.00 22.99  ? 403  VAL A CG1   1 
ATOM   3017 C  CG2   . VAL A 1 402 ? -13.912 5.451   32.523 1.00 21.89  ? 403  VAL A CG2   1 
ATOM   3018 N  N     . VAL A 1 403 ? -16.785 6.999   33.302 1.00 15.81  ? 404  VAL A N     1 
ATOM   3019 C  CA    . VAL A 1 403 ? -17.308 8.281   32.891 1.00 14.57  ? 404  VAL A CA    1 
ATOM   3020 C  C     . VAL A 1 403 ? -16.550 8.782   31.673 1.00 15.73  ? 404  VAL A C     1 
ATOM   3021 O  O     . VAL A 1 403 ? -15.321 8.962   31.712 1.00 16.98  ? 404  VAL A O     1 
ATOM   3022 C  CB    . VAL A 1 403 ? -17.217 9.301   34.038 1.00 15.56  ? 404  VAL A CB    1 
ATOM   3023 C  CG1   . VAL A 1 403 ? -17.792 10.662  33.599 1.00 17.38  ? 404  VAL A CG1   1 
ATOM   3024 C  CG2   . VAL A 1 403 ? -17.957 8.767   35.254 1.00 17.09  ? 404  VAL A CG2   1 
ATOM   3025 N  N     . SER A 1 404 ? -17.268 9.040   30.589 1.00 15.82  ? 405  SER A N     1 
ATOM   3026 C  CA    . SER A 1 404 ? -16.642 9.620   29.403 1.00 15.56  ? 405  SER A CA    1 
ATOM   3027 C  C     . SER A 1 404 ? -16.991 11.066  29.123 1.00 19.04  ? 405  SER A C     1 
ATOM   3028 O  O     . SER A 1 404 ? -16.212 11.756  28.426 1.00 21.30  ? 405  SER A O     1 
ATOM   3029 C  CB    . SER A 1 404 ? -16.976 8.750   28.184 1.00 16.89  ? 405  SER A CB    1 
ATOM   3030 O  OG    . SER A 1 404 ? -18.407 8.593   28.032 1.00 18.70  ? 405  SER A OG    1 
ATOM   3031 N  N     . LYS A 1 405 ? -18.111 11.560  29.620 1.00 18.81  ? 406  LYS A N     1 
ATOM   3032 C  CA    . LYS A 1 405 ? -18.427 12.990  29.417 1.00 18.10  ? 406  LYS A CA    1 
ATOM   3033 C  C     . LYS A 1 405 ? -19.396 13.480  30.487 1.00 18.66  ? 406  LYS A C     1 
ATOM   3034 O  O     . LYS A 1 405 ? -20.409 12.852  30.681 1.00 23.42  ? 406  LYS A O     1 
ATOM   3035 C  CB    . LYS A 1 405 ? -19.041 13.248  28.039 1.00 20.52  ? 406  LYS A CB    1 
ATOM   3036 C  CG    . LYS A 1 405 ? -19.279 14.714  27.707 1.00 21.68  ? 406  LYS A CG    1 
ATOM   3037 C  CD    . LYS A 1 405 ? -20.086 14.921  26.453 1.00 26.33  ? 406  LYS A CD    1 
ATOM   3038 C  CE    . LYS A 1 405 ? -19.400 14.383  25.219 1.00 44.42  ? 406  LYS A CE    1 
ATOM   3039 N  NZ    . LYS A 1 405 ? -20.004 14.930  23.981 1.00 56.95  ? 406  LYS A NZ    1 
ATOM   3040 N  N     . ILE A 1 406 ? -19.059 14.596  31.120 1.00 17.48  ? 407  ILE A N     1 
ATOM   3041 C  CA    . ILE A 1 406 ? -19.977 15.166  32.105 1.00 17.06  ? 407  ILE A CA    1 
ATOM   3042 C  C     . ILE A 1 406 ? -21.057 15.950  31.367 1.00 19.08  ? 407  ILE A C     1 
ATOM   3043 O  O     . ILE A 1 406 ? -20.745 16.770  30.477 1.00 22.55  ? 407  ILE A O     1 
ATOM   3044 C  CB    . ILE A 1 406 ? -19.222 16.082  33.101 1.00 18.04  ? 407  ILE A CB    1 
ATOM   3045 C  CG1   . ILE A 1 406 ? -18.119 15.332  33.829 1.00 25.97  ? 407  ILE A CG1   1 
ATOM   3046 C  CG2   . ILE A 1 406 ? -20.208 16.703  34.105 1.00 22.21  ? 407  ILE A CG2   1 
ATOM   3047 C  CD1   . ILE A 1 406 ? -18.633 14.301  34.592 1.00 32.48  ? 407  ILE A CD1   1 
ATOM   3048 N  N     . LEU A 1 407 ? -22.315 15.732  31.755 1.00 17.77  ? 408  LEU A N     1 
ATOM   3049 C  CA    . LEU A 1 407 ? -23.455 16.455  31.174 1.00 19.48  ? 408  LEU A CA    1 
ATOM   3050 C  C     . LEU A 1 407 ? -24.070 17.493  32.094 1.00 20.85  ? 408  LEU A C     1 
ATOM   3051 O  O     . LEU A 1 407 ? -24.472 18.565  31.613 1.00 26.16  ? 408  LEU A O     1 
ATOM   3052 C  CB    . LEU A 1 407 ? -24.574 15.489  30.732 1.00 19.42  ? 408  LEU A CB    1 
ATOM   3053 C  CG    . LEU A 1 407 ? -24.138 14.489  29.644 1.00 20.33  ? 408  LEU A CG    1 
ATOM   3054 C  CD1   . LEU A 1 407 ? -25.311 13.508  29.376 1.00 19.99  ? 408  LEU A CD1   1 
ATOM   3055 C  CD2   . LEU A 1 407 ? -23.705 15.256  28.356 1.00 19.91  ? 408  LEU A CD2   1 
ATOM   3056 N  N     . GLN A 1 408 ? -24.281 17.168  33.369 1.00 19.64  ? 409  GLN A N     1 
ATOM   3057 C  CA    . GLN A 1 408 ? -24.822 18.133  34.336 1.00 22.10  ? 409  GLN A CA    1 
ATOM   3058 C  C     . GLN A 1 408 ? -24.188 17.837  35.692 1.00 28.36  ? 409  GLN A C     1 
ATOM   3059 O  O     . GLN A 1 408 ? -24.247 16.680  36.118 1.00 21.66  ? 409  GLN A O     1 
ATOM   3060 C  CB    . GLN A 1 408 ? -26.350 18.045  34.389 1.00 25.59  ? 409  GLN A CB    1 
ATOM   3061 C  CG    . GLN A 1 408 ? -26.962 19.123  35.270 1.00 49.95  ? 409  GLN A CG    1 
ATOM   3062 C  CD    . GLN A 1 408 ? -28.466 19.206  35.126 1.00 71.25  ? 409  GLN A CD    1 
ATOM   3063 O  OE1   . GLN A 1 408 ? -29.074 18.429  34.387 1.00 74.80  ? 409  GLN A OE1   1 
ATOM   3064 N  NE2   . GLN A 1 408 ? -29.077 20.167  35.821 1.00 78.68  ? 409  GLN A NE2   1 
HETATM 3065 C  C1    . GOL B 2 .   ? -31.157 -3.007  46.437 1.00 73.75  ? 501  GOL A C1    1 
HETATM 3066 O  O1    . GOL B 2 .   ? -30.210 -2.783  47.420 1.00 71.08  ? 501  GOL A O1    1 
HETATM 3067 C  C2    . GOL B 2 .   ? -30.472 -2.589  45.125 1.00 75.38  ? 501  GOL A C2    1 
HETATM 3068 O  O2    . GOL B 2 .   ? -29.232 -3.168  45.004 1.00 73.92  ? 501  GOL A O2    1 
HETATM 3069 C  C3    . GOL B 2 .   ? -31.440 -3.001  43.985 1.00 75.79  ? 501  GOL A C3    1 
HETATM 3070 O  O3    . GOL B 2 .   ? -31.075 -2.282  42.832 1.00 69.29  ? 501  GOL A O3    1 
HETATM 3071 C  C1    . BME C 3 .   ? -10.711 -5.478  38.247 1.00 83.07  ? 502  BME A C1    1 
HETATM 3072 C  C2    . BME C 3 .   ? -10.307 -6.814  37.624 1.00 87.67  ? 502  BME A C2    1 
HETATM 3073 O  O1    . BME C 3 .   ? -11.066 -4.568  37.227 1.00 83.21  ? 502  BME A O1    1 
HETATM 3074 S  S2    . BME C 3 .   ? -9.070  -7.612  38.686 1.00 92.83  ? 502  BME A S2    1 
HETATM 3075 P  PB    . GDP D 4 .   ? -3.048  -11.677 18.486 1.00 20.00  ? 503  GDP A PB    1 
HETATM 3076 O  O1B   . GDP D 4 .   ? -3.185  -10.284 17.990 1.00 20.00  ? 503  GDP A O1B   1 
HETATM 3077 O  O2B   . GDP D 4 .   ? -4.347  -12.424 18.509 1.00 20.00  ? 503  GDP A O2B   1 
HETATM 3078 O  O3B   . GDP D 4 .   ? -2.315  -11.773 19.777 1.00 20.00  ? 503  GDP A O3B   1 
HETATM 3079 O  O3A   . GDP D 4 .   ? -2.136  -12.417 17.403 1.00 20.00  ? 503  GDP A O3A   1 
HETATM 3080 P  PA    . GDP D 4 .   ? -0.941  -13.467 17.532 1.00 20.00  ? 503  GDP A PA    1 
HETATM 3081 O  O1A   . GDP D 4 .   ? 0.276   -12.783 18.040 1.00 20.00  ? 503  GDP A O1A   1 
HETATM 3082 O  O2A   . GDP D 4 .   ? -1.433  -14.660 18.271 1.00 20.00  ? 503  GDP A O2A   1 
HETATM 3083 O  "O5'" . GDP D 4 .   ? -0.711  -13.823 15.998 1.00 20.00  ? 503  GDP A "O5'" 1 
HETATM 3084 C  "C5'" . GDP D 4 .   ? -1.740  -14.505 15.263 1.00 20.00  ? 503  GDP A "C5'" 1 
HETATM 3085 C  "C4'" . GDP D 4 .   ? -1.078  -15.372 14.228 1.00 20.00  ? 503  GDP A "C4'" 1 
HETATM 3086 O  "O4'" . GDP D 4 .   ? -0.382  -14.521 13.283 1.00 20.00  ? 503  GDP A "O4'" 1 
HETATM 3087 C  "C3'" . GDP D 4 .   ? -0.028  -16.346 14.781 1.00 20.00  ? 503  GDP A "C3'" 1 
HETATM 3088 O  "O3'" . GDP D 4 .   ? -0.077  -17.612 14.140 1.00 20.00  ? 503  GDP A "O3'" 1 
HETATM 3089 C  "C2'" . GDP D 4 .   ? 1.288   -15.619 14.497 1.00 20.00  ? 503  GDP A "C2'" 1 
HETATM 3090 O  "O2'" . GDP D 4 .   ? 2.403   -16.469 14.355 1.00 20.00  ? 503  GDP A "O2'" 1 
HETATM 3091 C  "C1'" . GDP D 4 .   ? 0.966   -14.906 13.192 1.00 20.00  ? 503  GDP A "C1'" 1 
HETATM 3092 N  N9    . GDP D 4 .   ? 1.797   -13.728 13.015 1.00 20.00  ? 503  GDP A N9    1 
HETATM 3093 C  C8    . GDP D 4 .   ? 2.098   -12.800 13.975 1.00 20.00  ? 503  GDP A C8    1 
HETATM 3094 N  N7    . GDP D 4 .   ? 2.910   -11.868 13.553 1.00 20.00  ? 503  GDP A N7    1 
HETATM 3095 C  C5    . GDP D 4 .   ? 3.172   -12.216 12.238 1.00 20.00  ? 503  GDP A C5    1 
HETATM 3096 C  C6    . GDP D 4 .   ? 3.985   -11.579 11.276 1.00 20.00  ? 503  GDP A C6    1 
HETATM 3097 O  O6    . GDP D 4 .   ? 4.660   -10.555 11.405 1.00 20.00  ? 503  GDP A O6    1 
HETATM 3098 N  N1    . GDP D 4 .   ? 3.973   -12.269 10.068 1.00 20.00  ? 503  GDP A N1    1 
HETATM 3099 C  C2    . GDP D 4 .   ? 3.265   -13.415 9.815  1.00 20.00  ? 503  GDP A C2    1 
HETATM 3100 N  N2    . GDP D 4 .   ? 3.381   -13.936 8.589  1.00 20.00  ? 503  GDP A N2    1 
HETATM 3101 N  N3    . GDP D 4 .   ? 2.503   -14.019 10.716 1.00 20.00  ? 503  GDP A N3    1 
HETATM 3102 C  C4    . GDP D 4 .   ? 2.501   -13.365 11.898 1.00 20.00  ? 503  GDP A C4    1 
HETATM 3103 C  C1    . BME E 3 .   ? -12.693 -0.091  9.164  1.00 66.18  ? 504  BME A C1    1 
HETATM 3104 C  C2    . BME E 3 .   ? -12.902 -0.770  10.511 1.00 66.20  ? 504  BME A C2    1 
HETATM 3105 O  O1    . BME E 3 .   ? -11.781 0.979   9.330  1.00 66.71  ? 504  BME A O1    1 
HETATM 3106 S  S2    . BME E 3 .   ? -13.825 -2.297  10.212 1.00 71.50  ? 504  BME A S2    1 
HETATM 3107 C  C1    . GOL F 2 .   ? -8.477  14.160  67.102 1.00 59.93  ? 505  GOL A C1    1 
HETATM 3108 O  O1    . GOL F 2 .   ? -8.294  15.423  67.690 1.00 60.85  ? 505  GOL A O1    1 
HETATM 3109 C  C2    . GOL F 2 .   ? -7.099  13.476  66.842 1.00 59.88  ? 505  GOL A C2    1 
HETATM 3110 O  O2    . GOL F 2 .   ? -6.697  13.583  65.497 1.00 65.81  ? 505  GOL A O2    1 
HETATM 3111 C  C3    . GOL F 2 .   ? -7.267  12.006  67.257 1.00 57.86  ? 505  GOL A C3    1 
HETATM 3112 O  O3    . GOL F 2 .   ? -6.013  11.444  67.438 1.00 43.97  ? 505  GOL A O3    1 
HETATM 3113 C  C1    . GOL G 2 .   ? -31.966 -6.592  35.606 1.00 63.50  ? 506  GOL A C1    1 
HETATM 3114 O  O1    . GOL G 2 .   ? -31.870 -7.280  36.817 1.00 65.27  ? 506  GOL A O1    1 
HETATM 3115 C  C2    . GOL G 2 .   ? -30.507 -6.317  35.107 1.00 58.31  ? 506  GOL A C2    1 
HETATM 3116 O  O2    . GOL G 2 .   ? -29.671 -7.369  35.290 1.00 49.67  ? 506  GOL A O2    1 
HETATM 3117 C  C3    . GOL G 2 .   ? -30.626 -5.927  33.643 1.00 66.66  ? 506  GOL A C3    1 
HETATM 3118 O  O3    . GOL G 2 .   ? -31.855 -5.276  33.456 1.00 68.26  ? 506  GOL A O3    1 
HETATM 3119 C  C1    . GOL H 2 .   ? 14.319  10.678  41.489 1.00 60.17  ? 507  GOL A C1    1 
HETATM 3120 O  O1    . GOL H 2 .   ? 15.623  10.896  41.954 1.00 62.56  ? 507  GOL A O1    1 
HETATM 3121 C  C2    . GOL H 2 .   ? 14.202  9.172   41.441 1.00 56.42  ? 507  GOL A C2    1 
HETATM 3122 O  O2    . GOL H 2 .   ? 13.965  8.716   40.158 1.00 44.77  ? 507  GOL A O2    1 
HETATM 3123 C  C3    . GOL H 2 .   ? 13.143  8.767   42.509 1.00 56.49  ? 507  GOL A C3    1 
HETATM 3124 O  O3    . GOL H 2 .   ? 13.386  7.411   42.857 1.00 57.88  ? 507  GOL A O3    1 
HETATM 3125 C  C1    . BME I 3 .   ? -15.548 -8.065  9.495  1.00 72.73  ? 508  BME A C1    1 
HETATM 3126 C  C2    . BME I 3 .   ? -14.982 -9.441  9.846  1.00 72.07  ? 508  BME A C2    1 
HETATM 3127 O  O1    . BME I 3 .   ? -14.666 -7.324  8.662  1.00 68.83  ? 508  BME A O1    1 
HETATM 3128 S  S2    . BME I 3 .   ? -14.339 -9.431  11.543 1.00 78.87  ? 508  BME A S2    1 
HETATM 3129 C  C1    . BME J 3 .   ? -17.532 -2.943  44.092 1.00 54.95  ? 509  BME A C1    1 
HETATM 3130 C  C2    . BME J 3 .   ? -16.673 -3.564  45.187 1.00 64.23  ? 509  BME A C2    1 
HETATM 3131 O  O1    . BME J 3 .   ? -16.657 -2.228  43.244 1.00 54.11  ? 509  BME A O1    1 
HETATM 3132 S  S2    . BME J 3 .   ? -17.370 -3.017  46.763 1.00 72.84  ? 509  BME A S2    1 
HETATM 3133 C  C1    . GOL K 2 .   ? 22.130  6.562   46.981 1.00 85.19  ? 510  GOL A C1    1 
HETATM 3134 O  O1    . GOL K 2 .   ? 22.194  5.358   46.224 1.00 76.95  ? 510  GOL A O1    1 
HETATM 3135 C  C2    . GOL K 2 .   ? 23.416  6.809   47.737 1.00 88.86  ? 510  GOL A C2    1 
HETATM 3136 O  O2    . GOL K 2 .   ? 23.208  6.622   49.135 1.00 92.77  ? 510  GOL A O2    1 
HETATM 3137 C  C3    . GOL K 2 .   ? 24.036  8.163   47.463 1.00 85.49  ? 510  GOL A C3    1 
HETATM 3138 O  O3    . GOL K 2 .   ? 23.443  9.206   48.234 1.00 83.96  ? 510  GOL A O3    1 
HETATM 3139 C  C1    . GOL L 2 .   ? -7.241  6.569   31.976 1.00 65.53  ? 511  GOL A C1    1 
HETATM 3140 O  O1    . GOL L 2 .   ? -8.591  6.332   32.275 1.00 62.09  ? 511  GOL A O1    1 
HETATM 3141 C  C2    . GOL L 2 .   ? -6.554  5.205   31.748 1.00 66.41  ? 511  GOL A C2    1 
HETATM 3142 O  O2    . GOL L 2 .   ? -5.303  5.380   31.188 1.00 69.98  ? 511  GOL A O2    1 
HETATM 3143 C  C3    . GOL L 2 .   ? -7.510  4.424   30.813 1.00 60.89  ? 511  GOL A C3    1 
HETATM 3144 O  O3    . GOL L 2 .   ? -7.419  3.062   31.120 1.00 57.28  ? 511  GOL A O3    1 
HETATM 3145 MG MG    . MG  M 5 .   ? -2.744  -12.576 21.658 1.00 15.54  ? 512  MG  A MG    1 
HETATM 3146 O  O     . HOH N 6 .   ? 23.503  10.055  48.283 1.00 45.70  ? 601  HOH A O     1 
HETATM 3147 O  O     . HOH N 6 .   ? 23.115  6.470   47.756 1.00 30.00  ? 602  HOH A O     1 
HETATM 3148 O  O     . HOH N 6 .   ? -16.969 8.445   50.375 1.00 32.26  ? 603  HOH A O     1 
HETATM 3149 O  O     . HOH N 6 .   ? 3.453   2.770   7.485  1.00 30.47  ? 604  HOH A O     1 
HETATM 3150 O  O     . HOH N 6 .   ? -9.763  -17.599 37.825 1.00 59.39  ? 605  HOH A O     1 
HETATM 3151 O  O     . HOH N 6 .   ? 7.712   9.403   18.090 1.00 57.57  ? 606  HOH A O     1 
HETATM 3152 O  O     . HOH N 6 .   ? 6.952   -14.201 9.152  1.00 36.92  ? 607  HOH A O     1 
HETATM 3153 O  O     . HOH N 6 .   ? 1.354   7.768   6.439  1.00 36.75  ? 608  HOH A O     1 
HETATM 3154 O  O     . HOH N 6 .   ? -17.261 24.632  56.872 1.00 53.74  ? 609  HOH A O     1 
HETATM 3155 O  O     . HOH N 6 .   ? -0.633  16.391  17.798 1.00 43.83  ? 610  HOH A O     1 
HETATM 3156 O  O     . HOH N 6 .   ? 10.561  -4.755  36.177 1.00 54.32  ? 611  HOH A O     1 
HETATM 3157 O  O     . HOH N 6 .   ? -26.368 13.359  52.972 1.00 47.96  ? 612  HOH A O     1 
HETATM 3158 O  O     . HOH N 6 .   ? 27.560  -1.567  18.157 1.00 42.03  ? 613  HOH A O     1 
HETATM 3159 O  O     . HOH N 6 .   ? 23.395  -12.803 20.680 1.00 45.35  ? 614  HOH A O     1 
HETATM 3160 O  O     . HOH N 6 .   ? -24.161 -19.059 31.693 1.00 52.83  ? 615  HOH A O     1 
HETATM 3161 O  O     . HOH N 6 .   ? -20.432 -8.419  21.581 1.00 49.39  ? 616  HOH A O     1 
HETATM 3162 O  O     . HOH N 6 .   ? -13.590 2.523   59.926 1.00 52.94  ? 617  HOH A O     1 
HETATM 3163 O  O     . HOH N 6 .   ? -7.371  1.434   29.373 1.00 42.92  ? 618  HOH A O     1 
HETATM 3164 O  O     . HOH N 6 .   ? -33.154 -2.472  40.259 1.00 51.24  ? 619  HOH A O     1 
HETATM 3165 O  O     . HOH N 6 .   ? -17.085 2.759   16.168 1.00 33.21  ? 620  HOH A O     1 
HETATM 3166 O  O     . HOH N 6 .   ? -18.232 5.021   17.349 1.00 46.60  ? 621  HOH A O     1 
HETATM 3167 O  O     . HOH N 6 .   ? 1.193   -7.949  -1.817 1.00 47.99  ? 622  HOH A O     1 
HETATM 3168 O  O     . HOH N 6 .   ? -7.166  -0.196  31.385 1.00 45.07  ? 623  HOH A O     1 
HETATM 3169 O  O     . HOH N 6 .   ? -10.068 -14.598 26.998 1.00 37.96  ? 624  HOH A O     1 
HETATM 3170 O  O     . HOH N 6 .   ? -31.665 0.075   42.583 1.00 31.23  ? 625  HOH A O     1 
HETATM 3171 O  O     . HOH N 6 .   ? -9.320  2.184   52.407 1.00 42.64  ? 626  HOH A O     1 
HETATM 3172 O  O     . HOH N 6 .   ? -13.055 8.609   30.078 1.00 25.34  ? 627  HOH A O     1 
HETATM 3173 O  O     . HOH N 6 .   ? -14.505 1.025   51.007 1.00 50.76  ? 628  HOH A O     1 
HETATM 3174 O  O     . HOH N 6 .   ? 10.139  -14.566 22.742 1.00 43.35  ? 629  HOH A O     1 
HETATM 3175 O  O     . HOH N 6 .   ? -32.050 10.752  32.989 1.00 35.44  ? 630  HOH A O     1 
HETATM 3176 O  O     . HOH N 6 .   ? -17.121 -4.166  41.214 1.00 38.90  ? 631  HOH A O     1 
HETATM 3177 O  O     . HOH N 6 .   ? -22.954 7.565   52.659 1.00 38.57  ? 632  HOH A O     1 
HETATM 3178 O  O     . HOH N 6 .   ? -34.660 -7.283  32.893 1.00 35.61  ? 633  HOH A O     1 
HETATM 3179 O  O     . HOH N 6 .   ? -10.653 7.058   45.598 1.00 39.57  ? 634  HOH A O     1 
HETATM 3180 O  O     . HOH N 6 .   ? 0.259   -17.944 11.684 1.00 39.40  ? 635  HOH A O     1 
HETATM 3181 O  O     . HOH N 6 .   ? 12.843  -5.809  6.985  1.00 41.76  ? 636  HOH A O     1 
HETATM 3182 O  O     . HOH N 6 .   ? -27.831 -7.602  33.564 1.00 25.20  ? 637  HOH A O     1 
HETATM 3183 O  O     . HOH N 6 .   ? -7.364  24.609  44.341 1.00 30.99  ? 638  HOH A O     1 
HETATM 3184 O  O     . HOH N 6 .   ? -19.288 4.555   22.305 1.00 27.24  ? 639  HOH A O     1 
HETATM 3185 O  O     . HOH N 6 .   ? -13.200 23.614  38.724 1.00 24.99  ? 640  HOH A O     1 
HETATM 3186 O  O     . HOH N 6 .   ? -17.870 4.142   57.341 1.00 50.86  ? 641  HOH A O     1 
HETATM 3187 O  O     . HOH N 6 .   ? -5.907  28.054  60.151 1.00 49.39  ? 642  HOH A O     1 
HETATM 3188 O  O     . HOH N 6 .   ? 18.103  -10.199 30.089 1.00 51.15  ? 643  HOH A O     1 
HETATM 3189 O  O     . HOH N 6 .   ? -10.063 13.437  22.331 1.00 58.26  ? 644  HOH A O     1 
HETATM 3190 O  O     . HOH N 6 .   ? -31.391 10.955  29.096 1.00 37.55  ? 645  HOH A O     1 
HETATM 3191 O  O     . HOH N 6 .   ? -21.034 11.455  23.090 1.00 32.93  ? 646  HOH A O     1 
HETATM 3192 O  O     . HOH N 6 .   ? -22.832 14.355  23.925 1.00 34.37  ? 647  HOH A O     1 
HETATM 3193 O  O     . HOH N 6 .   ? -21.369 2.797   21.747 1.00 25.33  ? 648  HOH A O     1 
HETATM 3194 O  O     . HOH N 6 .   ? -11.220 -1.593  5.460  1.00 57.40  ? 649  HOH A O     1 
HETATM 3195 O  O     . HOH N 6 .   ? -24.187 -8.167  20.190 1.00 44.22  ? 650  HOH A O     1 
HETATM 3196 O  O     . HOH N 6 .   ? -4.375  -16.172 23.252 1.00 34.11  ? 651  HOH A O     1 
HETATM 3197 O  O     . HOH N 6 .   ? 19.542  -3.653  9.449  1.00 35.46  ? 652  HOH A O     1 
HETATM 3198 O  O     . HOH N 6 .   ? 13.664  -15.734 29.616 1.00 51.30  ? 653  HOH A O     1 
HETATM 3199 O  O     . HOH N 6 .   ? -20.198 19.286  51.524 1.00 33.74  ? 654  HOH A O     1 
HETATM 3200 O  O     . HOH N 6 .   ? 16.872  9.052   28.444 1.00 52.93  ? 655  HOH A O     1 
HETATM 3201 O  O     . HOH N 6 .   ? 9.856   -1.344  5.558  1.00 38.45  ? 656  HOH A O     1 
HETATM 3202 O  O     . HOH N 6 .   ? 20.450  -14.027 18.945 1.00 26.08  ? 657  HOH A O     1 
HETATM 3203 O  O     . HOH N 6 .   ? -3.354  -12.145 8.677  1.00 39.53  ? 658  HOH A O     1 
HETATM 3204 O  O     . HOH N 6 .   ? 17.129  1.952   19.638 1.00 36.56  ? 659  HOH A O     1 
HETATM 3205 O  O     . HOH N 6 .   ? 19.237  -5.226  14.392 1.00 20.69  ? 660  HOH A O     1 
HETATM 3206 O  O     . HOH N 6 .   ? -30.155 8.781   32.394 1.00 20.88  ? 661  HOH A O     1 
HETATM 3207 O  O     . HOH N 6 .   ? -3.424  11.663  21.551 1.00 24.92  ? 662  HOH A O     1 
HETATM 3208 O  O     . HOH N 6 .   ? -24.669 -14.601 38.305 1.00 49.03  ? 663  HOH A O     1 
HETATM 3209 O  O     . HOH N 6 .   ? 8.644   -17.407 28.563 1.00 30.58  ? 664  HOH A O     1 
HETATM 3210 O  O     . HOH N 6 .   ? -9.966  7.536   39.427 1.00 36.85  ? 665  HOH A O     1 
HETATM 3211 O  O     . HOH N 6 .   ? 1.136   -1.161  35.871 1.00 38.14  ? 666  HOH A O     1 
HETATM 3212 O  O     . HOH N 6 .   ? -11.685 16.582  38.187 1.00 26.57  ? 667  HOH A O     1 
HETATM 3213 O  O     . HOH N 6 .   ? -5.581  -17.427 28.476 1.00 44.27  ? 668  HOH A O     1 
HETATM 3214 O  O     . HOH N 6 .   ? 15.427  -18.579 13.342 1.00 27.82  ? 669  HOH A O     1 
HETATM 3215 O  O     . HOH N 6 .   ? -4.841  -15.032 18.344 1.00 29.21  ? 670  HOH A O     1 
HETATM 3216 O  O     . HOH N 6 .   ? -18.433 21.041  68.807 1.00 55.46  ? 671  HOH A O     1 
HETATM 3217 O  O     . HOH N 6 .   ? -12.015 8.125   42.284 1.00 28.77  ? 672  HOH A O     1 
HETATM 3218 O  O     . HOH N 6 .   ? -9.691  7.745   48.006 1.00 22.94  ? 673  HOH A O     1 
HETATM 3219 O  O     . HOH N 6 .   ? 20.431  -20.007 16.275 1.00 45.96  ? 674  HOH A O     1 
HETATM 3220 O  O     . HOH N 6 .   ? 1.255   17.592  45.895 1.00 36.53  ? 675  HOH A O     1 
HETATM 3221 O  O     . HOH N 6 .   ? -7.061  9.754   40.291 1.00 31.43  ? 676  HOH A O     1 
HETATM 3222 O  O     . HOH N 6 .   ? -22.459 -10.814 24.508 1.00 37.90  ? 677  HOH A O     1 
HETATM 3223 O  O     . HOH N 6 .   ? 11.734  8.295   38.798 1.00 49.89  ? 678  HOH A O     1 
HETATM 3224 O  O     . HOH N 6 .   ? 3.682   9.776   54.109 1.00 39.65  ? 679  HOH A O     1 
HETATM 3225 O  O     . HOH N 6 .   ? 1.859   22.712  57.717 1.00 36.94  ? 680  HOH A O     1 
HETATM 3226 O  O     . HOH N 6 .   ? -16.981 -11.376 28.539 1.00 45.46  ? 681  HOH A O     1 
HETATM 3227 O  O     . HOH N 6 .   ? -12.499 20.320  44.844 1.00 34.74  ? 682  HOH A O     1 
HETATM 3228 O  O     . HOH N 6 .   ? 3.631   13.095  22.568 1.00 30.94  ? 683  HOH A O     1 
HETATM 3229 O  O     . HOH N 6 .   ? 10.008  10.790  31.158 1.00 38.23  ? 684  HOH A O     1 
HETATM 3230 O  O     . HOH N 6 .   ? -5.927  -4.472  14.362 1.00 16.35  ? 685  HOH A O     1 
HETATM 3231 O  O     . HOH N 6 .   ? -12.844 15.111  66.225 1.00 21.35  ? 686  HOH A O     1 
HETATM 3232 O  O     . HOH N 6 .   ? -0.832  16.312  62.215 1.00 23.32  ? 687  HOH A O     1 
HETATM 3233 O  O     . HOH N 6 .   ? -4.714  -12.767 21.125 1.00 17.78  ? 688  HOH A O     1 
HETATM 3234 O  O     . HOH N 6 .   ? -21.134 21.129  39.886 1.00 31.29  ? 689  HOH A O     1 
HETATM 3235 O  O     . HOH N 6 .   ? -21.897 11.150  59.325 1.00 41.39  ? 690  HOH A O     1 
HETATM 3236 O  O     . HOH N 6 .   ? -27.765 11.879  27.103 1.00 27.16  ? 691  HOH A O     1 
HETATM 3237 O  O     . HOH N 6 .   ? 10.337  6.208   37.815 1.00 41.94  ? 692  HOH A O     1 
HETATM 3238 O  O     . HOH N 6 .   ? -7.592  10.034  24.595 1.00 42.80  ? 693  HOH A O     1 
HETATM 3239 O  O     . HOH N 6 .   ? -16.679 16.044  30.577 1.00 27.17  ? 694  HOH A O     1 
HETATM 3240 O  O     . HOH N 6 .   ? -15.731 3.757   41.946 1.00 24.23  ? 695  HOH A O     1 
HETATM 3241 O  O     . HOH N 6 .   ? -3.106  -10.701 22.477 1.00 16.65  ? 696  HOH A O     1 
HETATM 3242 O  O     . HOH N 6 .   ? -18.454 -0.671  50.415 1.00 46.20  ? 697  HOH A O     1 
HETATM 3243 O  O     . HOH N 6 .   ? -0.893  13.392  25.646 1.00 41.54  ? 698  HOH A O     1 
HETATM 3244 O  O     . HOH N 6 .   ? -2.235  -14.480 20.905 1.00 16.54  ? 699  HOH A O     1 
HETATM 3245 O  O     . HOH N 6 .   ? -23.646 0.795   11.097 1.00 58.26  ? 700  HOH A O     1 
HETATM 3246 O  O     . HOH N 6 .   ? -25.932 -5.480  22.893 1.00 24.20  ? 701  HOH A O     1 
HETATM 3247 O  O     . HOH N 6 .   ? -25.933 13.332  25.577 1.00 31.49  ? 702  HOH A O     1 
HETATM 3248 O  O     . HOH N 6 .   ? 17.397  -1.289  9.001  1.00 36.00  ? 703  HOH A O     1 
HETATM 3249 O  O     . HOH N 6 .   ? 4.493   13.122  16.133 1.00 38.50  ? 704  HOH A O     1 
HETATM 3250 O  O     . HOH N 6 .   ? -6.530  1.087   2.703  1.00 37.81  ? 705  HOH A O     1 
HETATM 3251 O  O     . HOH N 6 .   ? 0.181   14.203  19.190 1.00 28.67  ? 706  HOH A O     1 
HETATM 3252 O  O     . HOH N 6 .   ? -17.590 15.510  65.096 1.00 27.40  ? 707  HOH A O     1 
HETATM 3253 O  O     . HOH N 6 .   ? 8.469   -16.401 21.237 1.00 38.69  ? 708  HOH A O     1 
HETATM 3254 O  O     . HOH N 6 .   ? 9.796   -0.613  8.494  1.00 39.48  ? 709  HOH A O     1 
HETATM 3255 O  O     . HOH N 6 .   ? -9.558  -4.085  6.348  1.00 29.31  ? 710  HOH A O     1 
HETATM 3256 O  O     . HOH N 6 .   ? -30.652 14.036  40.403 1.00 36.57  ? 711  HOH A O     1 
HETATM 3257 O  O     . HOH N 6 .   ? -23.490 14.153  55.605 1.00 38.47  ? 712  HOH A O     1 
HETATM 3258 O  O     . HOH N 6 .   ? 23.398  -10.112 23.966 1.00 27.14  ? 713  HOH A O     1 
HETATM 3259 O  O     . HOH N 6 .   ? 9.815   -9.423  29.777 1.00 21.82  ? 714  HOH A O     1 
HETATM 3260 O  O     . HOH N 6 .   ? -12.860 -12.500 29.015 1.00 36.08  ? 715  HOH A O     1 
HETATM 3261 O  O     . HOH N 6 .   ? 1.392   -5.109  33.310 1.00 42.62  ? 716  HOH A O     1 
HETATM 3262 O  O     . HOH N 6 .   ? -19.046 10.160  25.918 1.00 21.71  ? 717  HOH A O     1 
HETATM 3263 O  O     . HOH N 6 .   ? -28.643 0.844   16.966 1.00 40.65  ? 718  HOH A O     1 
HETATM 3264 O  O     . HOH N 6 .   ? -12.759 15.386  73.605 1.00 40.43  ? 719  HOH A O     1 
HETATM 3265 O  O     . HOH N 6 .   ? -20.885 19.039  46.754 1.00 15.89  ? 720  HOH A O     1 
HETATM 3266 O  O     . HOH N 6 .   ? -27.626 14.127  48.517 1.00 34.37  ? 721  HOH A O     1 
HETATM 3267 O  O     . HOH N 6 .   ? -16.158 -1.994  15.379 1.00 28.17  ? 722  HOH A O     1 
HETATM 3268 O  O     . HOH N 6 .   ? -18.287 22.336  43.948 1.00 23.27  ? 723  HOH A O     1 
HETATM 3269 O  O     . HOH N 6 .   ? 20.086  -10.608 28.879 1.00 50.82  ? 724  HOH A O     1 
HETATM 3270 O  O     . HOH N 6 .   ? -2.531  -4.727  2.310  1.00 49.37  ? 725  HOH A O     1 
HETATM 3271 O  O     . HOH N 6 .   ? -15.251 17.244  38.159 1.00 22.90  ? 726  HOH A O     1 
HETATM 3272 O  O     . HOH N 6 .   ? -8.865  16.247  43.086 1.00 17.74  ? 727  HOH A O     1 
HETATM 3273 O  O     . HOH N 6 .   ? -10.616 4.514   56.371 1.00 33.18  ? 728  HOH A O     1 
HETATM 3274 O  O     . HOH N 6 .   ? -26.571 -3.003  22.051 1.00 30.08  ? 729  HOH A O     1 
HETATM 3275 O  O     . HOH N 6 .   ? -4.816  8.183   41.149 1.00 44.56  ? 730  HOH A O     1 
HETATM 3276 O  O     . HOH N 6 .   ? 2.176   20.086  61.357 1.00 40.22  ? 731  HOH A O     1 
HETATM 3277 O  O     . HOH N 6 .   ? -25.157 -8.431  34.160 1.00 21.40  ? 732  HOH A O     1 
HETATM 3278 O  O     . HOH N 6 .   ? 15.724  3.608   14.448 1.00 31.85  ? 733  HOH A O     1 
HETATM 3279 O  O     . HOH N 6 .   ? 5.474   3.685   8.432  1.00 29.73  ? 734  HOH A O     1 
HETATM 3280 O  O     . HOH N 6 .   ? 0.764   9.264   28.914 1.00 23.59  ? 735  HOH A O     1 
HETATM 3281 O  O     . HOH N 6 .   ? 24.021  -9.813  21.250 1.00 30.19  ? 736  HOH A O     1 
HETATM 3282 O  O     . HOH N 6 .   ? -15.550 -5.298  17.215 1.00 37.37  ? 737  HOH A O     1 
HETATM 3283 O  O     . HOH N 6 .   ? 14.468  3.297   22.577 1.00 24.85  ? 738  HOH A O     1 
HETATM 3284 O  O     . HOH N 6 .   ? -10.630 6.267   50.665 1.00 21.37  ? 739  HOH A O     1 
HETATM 3285 O  O     . HOH N 6 .   ? -21.481 -0.871  21.318 1.00 29.76  ? 740  HOH A O     1 
HETATM 3286 O  O     . HOH N 6 .   ? 11.788  -8.446  32.299 1.00 24.44  ? 741  HOH A O     1 
HETATM 3287 O  O     . HOH N 6 .   ? 1.330   2.026   69.901 1.00 25.10  ? 742  HOH A O     1 
HETATM 3288 O  O     . HOH N 6 .   ? -15.493 25.803  44.458 1.00 33.11  ? 743  HOH A O     1 
HETATM 3289 O  O     . HOH N 6 .   ? -3.346  -1.928  1.158  1.00 37.28  ? 744  HOH A O     1 
HETATM 3290 O  O     . HOH N 6 .   ? -3.967  -20.010 23.508 1.00 48.50  ? 745  HOH A O     1 
HETATM 3291 O  O     . HOH N 6 .   ? 17.343  0.725   35.122 1.00 38.33  ? 746  HOH A O     1 
HETATM 3292 O  O     . HOH N 6 .   ? -0.788  10.235  36.667 1.00 42.65  ? 747  HOH A O     1 
HETATM 3293 O  O     . HOH N 6 .   ? -16.717 3.443   62.764 1.00 30.00  ? 748  HOH A O     1 
HETATM 3294 O  O     . HOH N 6 .   ? -7.994  -2.352  4.517  1.00 40.52  ? 749  HOH A O     1 
HETATM 3295 O  O     . HOH N 6 .   ? -15.541 21.883  43.696 1.00 21.59  ? 750  HOH A O     1 
HETATM 3296 O  O     . HOH N 6 .   ? 25.902  -6.729  16.094 1.00 36.14  ? 751  HOH A O     1 
HETATM 3297 O  O     . HOH N 6 .   ? -28.795 4.035   47.260 1.00 32.67  ? 752  HOH A O     1 
HETATM 3298 O  O     . HOH N 6 .   ? -3.807  -17.762 15.562 1.00 41.64  ? 753  HOH A O     1 
HETATM 3299 O  O     . HOH N 6 .   ? 14.671  -2.125  8.983  1.00 30.54  ? 754  HOH A O     1 
HETATM 3300 O  O     . HOH N 6 .   ? 20.675  4.617   17.312 1.00 42.17  ? 755  HOH A O     1 
HETATM 3301 O  O     . HOH N 6 .   ? -1.959  -12.755 25.820 1.00 20.36  ? 756  HOH A O     1 
HETATM 3302 O  O     . HOH N 6 .   ? -27.711 -13.489 28.582 1.00 54.30  ? 757  HOH A O     1 
HETATM 3303 O  O     . HOH N 6 .   ? -17.276 10.789  70.484 1.00 24.20  ? 758  HOH A O     1 
HETATM 3304 O  O     . HOH N 6 .   ? -9.883  10.338  35.977 1.00 57.10  ? 759  HOH A O     1 
HETATM 3305 O  O     . HOH N 6 .   ? 4.860   14.550  38.103 1.00 33.48  ? 760  HOH A O     1 
HETATM 3306 O  O     . HOH N 6 .   ? -22.601 6.191   11.366 1.00 56.34  ? 761  HOH A O     1 
HETATM 3307 O  O     . HOH N 6 .   ? 2.118   6.632   50.105 1.00 42.92  ? 762  HOH A O     1 
HETATM 3308 O  O     . HOH N 6 .   ? -16.296 -12.011 37.387 1.00 43.04  ? 763  HOH A O     1 
HETATM 3309 O  O     . HOH N 6 .   ? 3.563   -16.338 16.861 1.00 20.69  ? 764  HOH A O     1 
HETATM 3310 O  O     . HOH N 6 .   ? -13.711 24.245  65.437 1.00 49.16  ? 765  HOH A O     1 
HETATM 3311 O  O     . HOH N 6 .   ? 8.173   10.792  26.012 1.00 35.10  ? 766  HOH A O     1 
HETATM 3312 O  O     . HOH N 6 .   ? -10.252 4.709   7.534  1.00 24.05  ? 767  HOH A O     1 
HETATM 3313 O  O     . HOH N 6 .   ? -1.663  17.517  45.600 1.00 29.55  ? 768  HOH A O     1 
HETATM 3314 O  O     . HOH N 6 .   ? -18.229 -10.712 25.862 1.00 36.15  ? 769  HOH A O     1 
HETATM 3315 O  O     . HOH N 6 .   ? -12.541 10.232  40.618 1.00 23.50  ? 770  HOH A O     1 
HETATM 3316 O  O     . HOH N 6 .   ? -35.671 -0.357  24.402 1.00 27.11  ? 771  HOH A O     1 
HETATM 3317 O  O     . HOH N 6 .   ? 12.964  9.595   36.779 1.00 47.38  ? 772  HOH A O     1 
HETATM 3318 O  O     . HOH N 6 .   ? 24.147  -8.781  9.898  1.00 47.74  ? 773  HOH A O     1 
HETATM 3319 O  O     . HOH N 6 .   ? 22.555  11.788  47.735 1.00 53.74  ? 774  HOH A O     1 
HETATM 3320 O  O     . HOH N 6 .   ? -27.402 -0.330  48.040 1.00 41.64  ? 775  HOH A O     1 
HETATM 3321 O  O     . HOH N 6 .   ? -31.702 2.830   15.882 1.00 46.29  ? 776  HOH A O     1 
HETATM 3322 O  O     . HOH N 6 .   ? -27.071 8.610   47.462 1.00 38.03  ? 777  HOH A O     1 
HETATM 3323 O  O     . HOH N 6 .   ? 2.952   9.026   47.058 1.00 41.65  ? 778  HOH A O     1 
HETATM 3324 O  O     . HOH N 6 .   ? -10.516 13.804  34.573 1.00 39.50  ? 779  HOH A O     1 
HETATM 3325 O  O     . HOH N 6 .   ? -25.507 8.530   26.001 1.00 21.47  ? 780  HOH A O     1 
HETATM 3326 O  O     . HOH N 6 .   ? -9.053  -8.204  19.993 1.00 19.55  ? 781  HOH A O     1 
HETATM 3327 O  O     . HOH N 6 .   ? 19.786  -7.801  15.462 1.00 19.65  ? 782  HOH A O     1 
HETATM 3328 O  O     . HOH N 6 .   ? 4.475   12.760  55.003 1.00 46.50  ? 783  HOH A O     1 
HETATM 3329 O  O     . HOH N 6 .   ? 13.379  7.033   15.793 1.00 48.46  ? 784  HOH A O     1 
HETATM 3330 O  O     . HOH N 6 .   ? -9.596  21.501  64.023 1.00 46.41  ? 785  HOH A O     1 
HETATM 3331 O  O     . HOH N 6 .   ? 4.351   6.262   5.028  1.00 27.19  ? 786  HOH A O     1 
HETATM 3332 O  O     . HOH N 6 .   ? 6.341   -14.719 5.351  1.00 48.01  ? 787  HOH A O     1 
HETATM 3333 O  O     . HOH N 6 .   ? -30.487 6.736   22.278 1.00 33.68  ? 788  HOH A O     1 
HETATM 3334 O  O     . HOH N 6 .   ? 9.226   -19.106 18.651 1.00 29.04  ? 789  HOH A O     1 
HETATM 3335 O  O     . HOH N 6 .   ? -27.672 0.903   13.068 1.00 71.44  ? 790  HOH A O     1 
HETATM 3336 O  O     . HOH N 6 .   ? 10.028  -6.459  12.419 1.00 17.72  ? 791  HOH A O     1 
HETATM 3337 O  O     . HOH N 6 .   ? 14.204  -1.215  35.724 1.00 42.98  ? 792  HOH A O     1 
HETATM 3338 O  O     . HOH N 6 .   ? 19.960  6.066   29.169 1.00 28.89  ? 793  HOH A O     1 
HETATM 3339 O  O     . HOH N 6 .   ? -17.281 6.276   63.773 1.00 25.01  ? 794  HOH A O     1 
HETATM 3340 O  O     . HOH N 6 .   ? 11.555  -4.799  34.306 1.00 52.83  ? 795  HOH A O     1 
HETATM 3341 O  O     . HOH N 6 .   ? -25.529 -12.398 26.297 1.00 37.11  ? 796  HOH A O     1 
HETATM 3342 O  O     . HOH N 6 .   ? -26.470 -2.805  45.327 1.00 36.82  ? 797  HOH A O     1 
HETATM 3343 O  O     . HOH N 6 .   ? -6.000  21.672  49.069 1.00 33.83  ? 798  HOH A O     1 
HETATM 3344 O  O     . HOH N 6 .   ? -5.638  27.525  54.007 1.00 33.69  ? 799  HOH A O     1 
HETATM 3345 O  O     . HOH N 6 .   ? 13.670  -13.318 10.134 1.00 23.88  ? 800  HOH A O     1 
HETATM 3346 O  O     . HOH N 6 .   ? -24.700 19.157  28.879 1.00 40.17  ? 801  HOH A O     1 
HETATM 3347 O  O     . HOH N 6 .   ? -16.907 17.404  66.787 1.00 34.90  ? 802  HOH A O     1 
HETATM 3348 O  O     . HOH N 6 .   ? 16.870  2.375   39.758 1.00 44.44  ? 803  HOH A O     1 
HETATM 3349 O  O     . HOH N 6 .   ? 24.208  -12.860 18.356 1.00 39.78  ? 804  HOH A O     1 
HETATM 3350 O  O     . HOH N 6 .   ? -7.297  -10.414 20.396 1.00 20.50  ? 805  HOH A O     1 
HETATM 3351 O  O     . HOH N 6 .   ? -4.014  27.872  57.563 1.00 30.85  ? 806  HOH A O     1 
HETATM 3352 O  O     . HOH N 6 .   ? 10.880  8.009   27.158 1.00 30.07  ? 807  HOH A O     1 
HETATM 3353 O  O     . HOH N 6 .   ? 19.906  4.500   41.682 1.00 30.62  ? 808  HOH A O     1 
HETATM 3354 O  O     . HOH N 6 .   ? -3.293  26.199  43.412 1.00 37.24  ? 809  HOH A O     1 
HETATM 3355 O  O     . HOH N 6 .   ? 13.268  7.755   21.396 1.00 25.13  ? 810  HOH A O     1 
HETATM 3356 O  O     . HOH N 6 .   ? -31.878 4.649   24.911 1.00 29.69  ? 811  HOH A O     1 
HETATM 3357 O  O     . HOH N 6 .   ? -19.464 -2.536  17.795 1.00 48.39  ? 812  HOH A O     1 
HETATM 3358 O  O     . HOH N 6 .   ? 1.272   4.485   53.095 1.00 44.97  ? 813  HOH A O     1 
HETATM 3359 O  O     . HOH N 6 .   ? -18.346 12.818  46.181 1.00 30.00  ? 814  HOH A O     1 
HETATM 3360 O  O     . HOH N 6 .   ? -3.871  19.762  48.867 1.00 48.12  ? 815  HOH A O     1 
HETATM 3361 O  O     . HOH N 6 .   ? -0.183  -1.403  31.394 1.00 24.73  ? 816  HOH A O     1 
HETATM 3362 O  O     . HOH N 6 .   ? 16.031  0.953   14.210 1.00 31.98  ? 817  HOH A O     1 
HETATM 3363 O  O     . HOH N 6 .   ? 16.706  -12.654 23.584 1.00 24.21  ? 818  HOH A O     1 
HETATM 3364 O  O     . HOH N 6 .   ? -20.031 -5.823  44.299 1.00 40.02  ? 819  HOH A O     1 
HETATM 3365 O  O     . HOH N 6 .   ? -26.660 18.384  39.044 1.00 43.76  ? 820  HOH A O     1 
HETATM 3366 O  O     . HOH N 6 .   ? -8.228  -11.959 12.187 1.00 37.07  ? 821  HOH A O     1 
HETATM 3367 O  O     . HOH N 6 .   ? -30.435 15.087  45.320 1.00 48.01  ? 822  HOH A O     1 
HETATM 3368 O  O     . HOH N 6 .   ? 14.730  1.182   20.848 1.00 22.16  ? 823  HOH A O     1 
HETATM 3369 O  O     . HOH N 6 .   ? -17.593 8.855   45.931 1.00 18.09  ? 824  HOH A O     1 
HETATM 3370 O  O     . HOH N 6 .   ? -8.436  14.109  14.920 1.00 40.88  ? 825  HOH A O     1 
HETATM 3371 O  O     . HOH N 6 .   ? 3.805   -5.690  33.777 1.00 42.64  ? 826  HOH A O     1 
HETATM 3372 O  O     . HOH N 6 .   ? -16.508 0.389   17.264 1.00 28.12  ? 827  HOH A O     1 
HETATM 3373 O  O     . HOH N 6 .   ? 5.934   -2.315  36.731 1.00 42.80  ? 828  HOH A O     1 
HETATM 3374 O  O     . HOH N 6 .   ? -10.314 26.698  55.031 1.00 26.64  ? 829  HOH A O     1 
HETATM 3375 O  O     . HOH N 6 .   ? -3.124  -13.583 23.458 1.00 16.25  ? 830  HOH A O     1 
HETATM 3376 O  O     . HOH N 6 .   ? -20.383 18.940  54.173 1.00 33.80  ? 831  HOH A O     1 
HETATM 3377 O  O     . HOH N 6 .   ? -16.137 -10.021 34.584 1.00 39.73  ? 832  HOH A O     1 
HETATM 3378 O  O     . HOH N 6 .   ? -34.429 2.031   41.527 1.00 37.61  ? 833  HOH A O     1 
HETATM 3379 O  O     . HOH N 6 .   ? 18.430  -4.694  21.882 1.00 19.36  ? 834  HOH A O     1 
HETATM 3380 O  O     . HOH N 6 .   ? -17.491 -7.088  24.721 1.00 38.04  ? 835  HOH A O     1 
HETATM 3381 O  O     . HOH N 6 .   ? -23.010 21.962  52.813 1.00 31.11  ? 836  HOH A O     1 
HETATM 3382 O  O     . HOH N 6 .   ? 4.518   8.614   7.561  1.00 57.87  ? 837  HOH A O     1 
HETATM 3383 O  O     . HOH N 6 .   ? -10.301 9.575   37.614 1.00 41.51  ? 838  HOH A O     1 
HETATM 3384 O  O     . HOH N 6 .   ? 16.697  1.943   24.028 1.00 29.55  ? 839  HOH A O     1 
HETATM 3385 O  O     . HOH N 6 .   ? -8.302  -9.958  10.336 1.00 29.29  ? 840  HOH A O     1 
HETATM 3386 O  O     . HOH N 6 .   ? -0.229  -14.668 9.965  1.00 19.35  ? 841  HOH A O     1 
HETATM 3387 O  O     . HOH N 6 .   ? 19.812  11.094  36.024 1.00 41.76  ? 842  HOH A O     1 
HETATM 3388 O  O     . HOH N 6 .   ? 19.313  -14.276 12.212 1.00 32.32  ? 843  HOH A O     1 
HETATM 3389 O  O     . HOH N 6 .   ? -15.540 -15.486 36.646 1.00 53.54  ? 844  HOH A O     1 
HETATM 3390 O  O     . HOH N 6 .   ? 21.384  -5.719  8.521  1.00 42.23  ? 845  HOH A O     1 
HETATM 3391 O  O     . HOH N 6 .   ? -25.010 9.885   18.005 1.00 44.48  ? 846  HOH A O     1 
HETATM 3392 O  O     . HOH N 6 .   ? 0.184   -20.672 24.144 1.00 33.40  ? 847  HOH A O     1 
HETATM 3393 O  O     . HOH N 6 .   ? 5.426   6.716   36.338 1.00 44.78  ? 848  HOH A O     1 
HETATM 3394 O  O     . HOH N 6 .   ? -7.834  10.228  37.128 1.00 52.25  ? 849  HOH A O     1 
HETATM 3395 O  O     . HOH N 6 .   ? 22.154  -10.996 12.055 1.00 36.04  ? 850  HOH A O     1 
HETATM 3396 O  O     . HOH N 6 .   ? -12.003 5.549   39.359 1.00 30.49  ? 851  HOH A O     1 
HETATM 3397 O  O     . HOH N 6 .   ? 15.892  2.309   37.017 1.00 29.88  ? 852  HOH A O     1 
HETATM 3398 O  O     . HOH N 6 .   ? 8.189   7.711   36.201 1.00 31.12  ? 853  HOH A O     1 
HETATM 3399 O  O     . HOH N 6 .   ? -0.974  3.683   54.443 1.00 28.39  ? 854  HOH A O     1 
HETATM 3400 O  O     . HOH N 6 .   ? -3.431  -17.700 19.871 1.00 32.64  ? 855  HOH A O     1 
HETATM 3401 O  O     . HOH N 6 .   ? -13.797 15.815  34.153 1.00 25.16  ? 856  HOH A O     1 
HETATM 3402 O  O     . HOH N 6 .   ? -0.256  19.923  49.086 1.00 56.67  ? 857  HOH A O     1 
HETATM 3403 O  O     . HOH N 6 .   ? 16.071  -13.668 28.948 1.00 30.98  ? 858  HOH A O     1 
HETATM 3404 O  O     . HOH N 6 .   ? -15.797 13.850  26.445 1.00 50.14  ? 859  HOH A O     1 
HETATM 3405 O  O     . HOH N 6 .   ? -1.538  -0.751  35.967 1.00 37.33  ? 860  HOH A O     1 
HETATM 3406 O  O     . HOH N 6 .   ? -11.675 -11.817 12.419 1.00 37.56  ? 861  HOH A O     1 
HETATM 3407 O  O     . HOH N 6 .   ? 25.255  -3.258  13.730 1.00 50.98  ? 862  HOH A O     1 
HETATM 3408 O  O     . HOH N 6 .   ? 5.234   8.702   36.751 1.00 47.58  ? 863  HOH A O     1 
HETATM 3409 O  O     . HOH N 6 .   ? -18.013 -5.583  22.403 1.00 32.27  ? 864  HOH A O     1 
HETATM 3410 O  O     . HOH N 6 .   ? -15.352 0.149   35.849 1.00 22.55  ? 865  HOH A O     1 
HETATM 3411 O  O     . HOH N 6 .   ? 4.993   7.554   11.302 1.00 24.32  ? 866  HOH A O     1 
HETATM 3412 O  O     . HOH N 6 .   ? 6.765   -16.985 32.780 1.00 54.57  ? 867  HOH A O     1 
HETATM 3413 O  O     . HOH N 6 .   ? -3.663  -14.705 11.100 1.00 36.01  ? 868  HOH A O     1 
HETATM 3414 O  O     . HOH N 6 .   ? -5.886  12.712  21.442 1.00 32.47  ? 869  HOH A O     1 
HETATM 3415 O  O     . HOH N 6 .   ? -0.167  24.992  55.062 1.00 40.20  ? 870  HOH A O     1 
HETATM 3416 O  O     . HOH N 6 .   ? 20.610  -10.678 10.068 1.00 32.75  ? 871  HOH A O     1 
HETATM 3417 O  O     . HOH N 6 .   ? -19.895 -9.901  39.799 1.00 39.44  ? 872  HOH A O     1 
HETATM 3418 O  O     . HOH N 6 .   ? -6.346  15.006  19.030 1.00 49.00  ? 873  HOH A O     1 
HETATM 3419 O  O     . HOH N 6 .   ? 11.338  -16.871 8.075  1.00 25.95  ? 874  HOH A O     1 
HETATM 3420 O  O     . HOH N 6 .   ? 16.101  -12.201 9.252  1.00 26.46  ? 875  HOH A O     1 
HETATM 3421 O  O     . HOH N 6 .   ? 3.489   9.720   43.293 1.00 33.37  ? 876  HOH A O     1 
HETATM 3422 O  O     . HOH N 6 .   ? -22.976 -0.657  19.223 1.00 31.65  ? 877  HOH A O     1 
HETATM 3423 O  O     . HOH N 6 .   ? -2.074  -19.620 13.317 1.00 48.98  ? 878  HOH A O     1 
HETATM 3424 O  O     . HOH N 6 .   ? -1.692  19.676  41.268 1.00 51.11  ? 879  HOH A O     1 
HETATM 3425 O  O     . HOH N 6 .   ? -37.025 6.349   32.527 1.00 32.00  ? 880  HOH A O     1 
HETATM 3426 O  O     . HOH N 6 .   ? -21.408 6.484   19.384 1.00 41.91  ? 881  HOH A O     1 
HETATM 3427 O  O     . HOH N 6 .   ? 8.064   -10.017 31.800 1.00 26.38  ? 882  HOH A O     1 
HETATM 3428 O  O     . HOH N 6 .   ? 7.133   12.470  28.990 1.00 40.83  ? 883  HOH A O     1 
HETATM 3429 O  O     . HOH N 6 .   ? -1.978  9.843   20.026 1.00 19.48  ? 884  HOH A O     1 
HETATM 3430 O  O     . HOH N 6 .   ? -11.372 -12.254 20.521 1.00 30.00  ? 885  HOH A O     1 
HETATM 3431 O  O     . HOH N 6 .   ? -8.424  19.130  38.391 1.00 33.69  ? 886  HOH A O     1 
HETATM 3432 O  O     . HOH N 6 .   ? 0.278   4.110   -2.142 1.00 31.10  ? 887  HOH A O     1 
HETATM 3433 O  O     . HOH N 6 .   ? -28.403 23.145  46.729 1.00 50.49  ? 888  HOH A O     1 
HETATM 3434 O  O     . HOH N 6 .   ? -20.488 -5.070  22.642 1.00 25.63  ? 889  HOH A O     1 
HETATM 3435 O  O     . HOH N 6 .   ? -28.581 8.662   18.849 1.00 57.43  ? 890  HOH A O     1 
HETATM 3436 O  O     . HOH N 6 .   ? 11.858  -15.660 23.292 1.00 48.64  ? 891  HOH A O     1 
HETATM 3437 O  O     . HOH N 6 .   ? -35.347 -0.491  37.208 1.00 29.80  ? 892  HOH A O     1 
HETATM 3438 O  O     . HOH N 6 .   ? -16.048 10.442  12.977 1.00 58.92  ? 893  HOH A O     1 
HETATM 3439 O  O     . HOH N 6 .   ? -20.904 13.067  66.945 1.00 40.62  ? 894  HOH A O     1 
HETATM 3440 O  O     . HOH N 6 .   ? 13.786  -11.772 5.497  1.00 42.41  ? 895  HOH A O     1 
HETATM 3441 O  O     . HOH N 6 .   ? 6.835   -2.494  -3.841 1.00 47.54  ? 896  HOH A O     1 
HETATM 3442 O  O     . HOH N 6 .   ? -25.166 -14.120 30.236 1.00 33.09  ? 897  HOH A O     1 
HETATM 3443 O  O     . HOH N 6 .   ? 17.186  -1.952  35.776 1.00 51.54  ? 898  HOH A O     1 
HETATM 3444 O  O     . HOH N 6 .   ? -13.808 1.363   44.893 1.00 47.31  ? 899  HOH A O     1 
HETATM 3445 O  O     . HOH N 6 .   ? 19.845  0.447   10.842 1.00 43.77  ? 900  HOH A O     1 
HETATM 3446 O  O     . HOH N 6 .   ? -5.269  -17.884 25.449 1.00 42.52  ? 901  HOH A O     1 
HETATM 3447 O  O     . HOH N 6 .   ? 13.544  -4.387  32.906 1.00 37.33  ? 902  HOH A O     1 
HETATM 3448 O  O     . HOH N 6 .   ? -20.364 7.635   56.796 1.00 37.03  ? 903  HOH A O     1 
HETATM 3449 O  O     . HOH N 6 .   ? -20.029 -8.937  42.938 1.00 45.18  ? 904  HOH A O     1 
HETATM 3450 O  O     . HOH N 6 .   ? -3.153  22.685  63.053 1.00 35.54  ? 905  HOH A O     1 
HETATM 3451 O  O     . HOH N 6 .   ? 8.695   -11.367 2.644  1.00 52.45  ? 906  HOH A O     1 
HETATM 3452 O  O     . HOH N 6 .   ? -20.426 15.957  65.414 1.00 50.30  ? 907  HOH A O     1 
HETATM 3453 O  O     . HOH N 6 .   ? -5.196  22.469  40.481 1.00 36.14  ? 908  HOH A O     1 
HETATM 3454 O  O     . HOH N 6 .   ? -4.834  26.173  51.031 1.00 24.53  ? 909  HOH A O     1 
HETATM 3455 O  O     . HOH N 6 .   ? -28.907 6.610   46.547 1.00 27.64  ? 910  HOH A O     1 
HETATM 3456 O  O     . HOH N 6 .   ? 13.470  -20.521 19.585 1.00 38.07  ? 911  HOH A O     1 
HETATM 3457 O  O     . HOH N 6 .   ? -23.091 0.259   15.679 1.00 35.69  ? 912  HOH A O     1 
HETATM 3458 O  O     . HOH N 6 .   ? -22.755 15.796  64.296 1.00 37.66  ? 913  HOH A O     1 
HETATM 3459 O  O     . HOH N 6 .   ? -0.439  11.968  33.417 1.00 43.56  ? 914  HOH A O     1 
HETATM 3460 O  O     . HOH N 6 .   ? -31.113 6.478   15.857 1.00 36.09  ? 915  HOH A O     1 
HETATM 3461 O  O     . HOH N 6 .   ? 10.506  -16.753 30.433 1.00 44.65  ? 916  HOH A O     1 
HETATM 3462 O  O     . HOH N 6 .   ? -16.944 11.571  24.796 1.00 33.10  ? 917  HOH A O     1 
HETATM 3463 O  O     . HOH N 6 .   ? -22.236 20.496  55.160 1.00 44.50  ? 918  HOH A O     1 
HETATM 3464 O  O     . HOH N 6 .   ? -24.788 10.298  23.941 1.00 41.60  ? 919  HOH A O     1 
HETATM 3465 O  O     . HOH N 6 .   ? -3.488  19.424  45.881 1.00 30.13  ? 920  HOH A O     1 
HETATM 3466 O  O     . HOH N 6 .   ? -10.483 25.350  66.068 1.00 64.97  ? 921  HOH A O     1 
HETATM 3467 O  O     . HOH N 6 .   ? 20.438  -14.664 24.080 1.00 51.65  ? 922  HOH A O     1 
HETATM 3468 O  O     . HOH N 6 .   ? 8.152   -3.774  2.379  1.00 49.05  ? 923  HOH A O     1 
HETATM 3469 O  O     . HOH N 6 .   ? 16.234  7.643   31.440 1.00 46.89  ? 924  HOH A O     1 
HETATM 3470 O  O     . HOH N 6 .   ? -21.080 22.926  61.324 1.00 54.94  ? 925  HOH A O     1 
HETATM 3471 O  O     . HOH N 6 .   ? 24.638  -11.430 14.620 1.00 44.07  ? 926  HOH A O     1 
HETATM 3472 O  O     . HOH N 6 .   ? 1.432   6.755   37.272 1.00 59.16  ? 927  HOH A O     1 
HETATM 3473 O  O     . HOH N 6 .   ? -26.424 20.932  51.658 1.00 37.07  ? 928  HOH A O     1 
HETATM 3474 O  O     . HOH N 6 .   ? -33.631 6.611   26.680 1.00 25.10  ? 929  HOH A O     1 
HETATM 3475 O  O     . HOH N 6 .   ? 0.811   -14.900 30.219 1.00 36.26  ? 930  HOH A O     1 
HETATM 3476 O  O     . HOH N 6 .   ? -23.815 10.678  21.889 1.00 53.29  ? 931  HOH A O     1 
HETATM 3477 O  O     . HOH N 6 .   ? -0.552  9.274   31.318 1.00 39.84  ? 932  HOH A O     1 
HETATM 3478 O  O     . HOH N 6 .   ? 0.071   5.136   39.211 1.00 51.89  ? 933  HOH A O     1 
HETATM 3479 O  O     . HOH N 6 .   ? -22.531 9.388   19.200 1.00 54.08  ? 934  HOH A O     1 
HETATM 3480 O  O     . HOH N 6 .   ? -9.629  -8.113  5.470  1.00 44.29  ? 935  HOH A O     1 
HETATM 3481 O  O     . HOH N 6 .   ? 1.899   -13.043 32.136 1.00 32.62  ? 936  HOH A O     1 
HETATM 3482 O  O     . HOH N 6 .   ? -32.934 -7.686  42.003 1.00 56.89  ? 937  HOH A O     1 
HETATM 3483 O  O     . HOH N 6 .   ? -29.971 15.789  42.891 1.00 35.17  ? 938  HOH A O     1 
HETATM 3484 O  O     . HOH N 6 .   ? -14.878 15.130  73.413 1.00 62.32  ? 939  HOH A O     1 
HETATM 3485 O  O     . HOH N 6 .   ? 11.198  2.310   36.580 1.00 38.73  ? 940  HOH A O     1 
HETATM 3486 O  O     . HOH N 6 .   ? 6.750   12.367  35.593 1.00 46.71  ? 941  HOH A O     1 
HETATM 3487 O  O     . HOH N 6 .   ? -17.375 19.502  65.377 1.00 41.62  ? 942  HOH A O     1 
HETATM 3488 O  O     . HOH N 6 .   ? 15.431  6.227   21.772 1.00 42.90  ? 943  HOH A O     1 
HETATM 3489 O  O     . HOH N 6 .   ? -15.836 -8.530  17.003 1.00 46.67  ? 944  HOH A O     1 
HETATM 3490 O  O     . HOH N 6 .   ? 6.186   12.545  25.055 1.00 43.89  ? 945  HOH A O     1 
HETATM 3491 O  O     . HOH N 6 .   ? -23.699 1.267   49.789 1.00 43.10  ? 946  HOH A O     1 
HETATM 3492 O  O     . HOH N 6 .   ? -20.795 10.463  67.165 1.00 47.18  ? 947  HOH A O     1 
HETATM 3493 O  O     . HOH N 6 .   ? -12.576 -12.229 18.775 1.00 30.00  ? 948  HOH A O     1 
HETATM 3494 O  O     . HOH N 6 .   ? -5.056  -18.651 35.778 1.00 46.69  ? 949  HOH A O     1 
HETATM 3495 O  O     . HOH N 6 .   ? 17.217  -5.200  33.582 1.00 54.23  ? 950  HOH A O     1 
HETATM 3496 O  O     . HOH N 6 .   ? -13.590 -12.267 23.017 1.00 35.76  ? 951  HOH A O     1 
HETATM 3497 O  O     . HOH N 6 .   ? -14.350 -17.665 34.655 1.00 56.29  ? 952  HOH A O     1 
HETATM 3498 O  O     . HOH N 6 .   ? -14.584 -14.003 32.377 1.00 52.37  ? 953  HOH A O     1 
HETATM 3499 O  O     . HOH N 6 .   ? -20.318 6.272   63.383 1.00 30.00  ? 954  HOH A O     1 
HETATM 3500 O  O     . HOH N 6 .   ? -1.820  12.541  65.545 1.00 35.24  ? 955  HOH A O     1 
HETATM 3501 O  O     . HOH N 6 .   ? 7.988   5.735   11.719 1.00 45.50  ? 956  HOH A O     1 
HETATM 3502 O  O     . HOH N 6 .   ? -8.616  24.418  65.423 1.00 56.93  ? 957  HOH A O     1 
HETATM 3503 O  O     . HOH N 6 .   ? 12.070  -17.160 26.463 1.00 45.76  ? 958  HOH A O     1 
HETATM 3504 O  O     . HOH N 6 .   ? -5.660  -12.289 10.621 1.00 47.63  ? 959  HOH A O     1 
HETATM 3505 O  O     . HOH N 6 .   ? 19.679  4.427   44.418 1.00 45.10  ? 960  HOH A O     1 
HETATM 3506 O  O     . HOH N 6 .   ? -27.814 2.884   11.828 1.00 59.69  ? 961  HOH A O     1 
HETATM 3507 O  O     . HOH N 6 .   ? -17.990 17.826  29.069 1.00 46.43  ? 962  HOH A O     1 
HETATM 3508 O  O     . HOH N 6 .   ? -18.827 5.717   57.491 1.00 41.54  ? 963  HOH A O     1 
HETATM 3509 O  O     . HOH N 6 .   ? -19.951 7.161   62.103 1.00 30.00  ? 964  HOH A O     1 
HETATM 3510 O  O     . HOH N 6 .   ? 1.525   13.231  30.895 1.00 42.68  ? 965  HOH A O     1 
HETATM 3511 O  O     . HOH N 6 .   ? 21.726  -13.731 12.556 1.00 36.70  ? 966  HOH A O     1 
HETATM 3512 O  O     . HOH N 6 .   ? -7.167  5.252   47.198 1.00 47.66  ? 967  HOH A O     1 
HETATM 3513 O  O     . HOH N 6 .   ? -24.671 18.882  40.926 1.00 41.31  ? 968  HOH A O     1 
HETATM 3514 O  O     . HOH N 6 .   ? 21.035  -8.676  7.813  1.00 36.99  ? 969  HOH A O     1 
HETATM 3515 O  O     . HOH N 6 .   ? -6.498  -6.712  2.192  1.00 56.59  ? 970  HOH A O     1 
HETATM 3516 O  O     . HOH N 6 .   ? -13.039 -4.217  7.800  1.00 52.32  ? 971  HOH A O     1 
HETATM 3517 O  O     . HOH N 6 .   ? -34.538 6.878   31.739 1.00 38.02  ? 972  HOH A O     1 
HETATM 3518 O  O     . HOH N 6 .   ? 6.276   9.578   44.307 1.00 63.63  ? 973  HOH A O     1 
HETATM 3519 O  O     . HOH N 6 .   ? -24.644 17.489  64.976 1.00 54.91  ? 974  HOH A O     1 
HETATM 3520 O  O     . HOH N 6 .   ? -16.961 21.763  64.955 1.00 53.63  ? 975  HOH A O     1 
HETATM 3521 O  O     . HOH N 6 .   ? -0.189  9.056   66.351 1.00 59.93  ? 976  HOH A O     1 
HETATM 3522 O  O     . HOH N 6 .   ? -29.521 15.884  47.386 1.00 51.61  ? 977  HOH A O     1 
HETATM 3523 O  O     . HOH N 6 .   ? -19.963 -3.622  20.715 1.00 48.14  ? 978  HOH A O     1 
HETATM 3524 O  O     . HOH N 6 .   ? 13.451  -16.213 9.474  1.00 39.99  ? 979  HOH A O     1 
HETATM 3525 O  O     . HOH N 6 .   ? 8.731   -18.285 21.219 1.00 28.29  ? 980  HOH A O     1 
HETATM 3526 O  O     . HOH N 6 .   ? -10.922 4.464   48.337 1.00 53.21  ? 981  HOH A O     1 
HETATM 3527 O  O     . HOH N 6 .   ? -23.512 18.633  45.525 1.00 26.48  ? 982  HOH A O     1 
HETATM 3528 O  O     . HOH N 6 .   ? -27.532 10.122  20.858 1.00 57.63  ? 983  HOH A O     1 
HETATM 3529 O  O     . HOH N 6 .   ? -28.087 12.195  50.280 1.00 43.75  ? 984  HOH A O     1 
HETATM 3530 O  O     . HOH N 6 .   ? -4.427  4.665   46.802 1.00 49.81  ? 985  HOH A O     1 
HETATM 3531 O  O     . HOH N 6 .   ? -12.344 4.684   46.269 1.00 49.31  ? 986  HOH A O     1 
HETATM 3532 O  O     . HOH N 6 .   ? -8.545  14.127  36.560 1.00 56.54  ? 987  HOH A O     1 
HETATM 3533 O  O     . HOH N 6 .   ? -2.780  14.635  63.826 1.00 31.96  ? 988  HOH A O     1 
HETATM 3534 O  O     . HOH N 6 .   ? 5.620   -14.492 2.582  1.00 51.10  ? 989  HOH A O     1 
HETATM 3535 O  O     . HOH N 6 .   ? -6.349  -13.251 40.702 1.00 47.88  ? 990  HOH A O     1 
HETATM 3536 O  O     . HOH N 6 .   ? 7.408   12.234  19.380 1.00 45.29  ? 991  HOH A O     1 
HETATM 3537 O  O     . HOH N 6 .   ? -13.253 5.061   41.709 1.00 30.00  ? 992  HOH A O     1 
HETATM 3538 O  O     . HOH N 6 .   ? -25.951 19.158  47.075 1.00 43.57  ? 993  HOH A O     1 
HETATM 3539 O  O     . HOH N 6 .   ? -7.606  5.120   56.872 1.00 30.63  ? 994  HOH A O     1 
HETATM 3540 O  O     . HOH N 6 .   ? -5.004  -5.130  3.139  1.00 53.96  ? 995  HOH A O     1 
HETATM 3541 O  O     . HOH N 6 .   ? 18.793  -12.687 25.357 1.00 31.96  ? 996  HOH A O     1 
HETATM 3542 O  O     . HOH N 6 .   ? -11.869 13.118  11.122 1.00 31.46  ? 997  HOH A O     1 
HETATM 3543 O  O     . HOH N 6 .   ? -12.356 26.670  43.146 1.00 39.62  ? 998  HOH A O     1 
HETATM 3544 O  O     . HOH N 6 .   ? -8.376  -17.017 27.205 1.00 51.73  ? 999  HOH A O     1 
HETATM 3545 O  O     . HOH N 6 .   ? -16.012 -14.735 30.731 1.00 51.69  ? 1000 HOH A O     1 
HETATM 3546 O  O     . HOH N 6 .   ? -7.523  -14.799 40.240 1.00 56.35  ? 1001 HOH A O     1 
HETATM 3547 O  O     . HOH N 6 .   ? -8.072  10.612  35.344 1.00 60.40  ? 1002 HOH A O     1 
HETATM 3548 O  O     . HOH N 6 .   ? -9.215  2.138   38.116 1.00 66.26  ? 1003 HOH A O     1 
HETATM 3549 O  O     . HOH N 6 .   ? -10.678 10.340  30.748 1.00 48.84  ? 1004 HOH A O     1 
HETATM 3550 O  O     . HOH N 6 .   ? -1.951  -4.036  34.870 1.00 49.10  ? 1005 HOH A O     1 
HETATM 3551 O  O     . HOH N 6 .   ? -13.528 11.491  24.846 1.00 54.25  ? 1006 HOH A O     1 
HETATM 3552 O  O     . HOH N 6 .   ? 11.451  8.920   29.299 1.00 40.70  ? 1007 HOH A O     1 
HETATM 3553 O  O     . HOH N 6 .   ? -16.234 15.304  71.676 1.00 52.25  ? 1008 HOH A O     1 
HETATM 3554 O  O     . HOH N 6 .   ? -25.905 -1.105  15.055 1.00 56.63  ? 1009 HOH A O     1 
HETATM 3555 O  O     . HOH N 6 .   ? -6.826  -15.662 20.703 1.00 30.00  ? 1010 HOH A O     1 
HETATM 3556 O  O     . HOH N 6 .   ? -15.815 0.779   41.409 1.00 30.00  ? 1011 HOH A O     1 
HETATM 3557 O  O     . HOH N 6 .   ? 12.134  -1.460  4.807  1.00 54.92  ? 1012 HOH A O     1 
HETATM 3558 O  O     . HOH N 6 .   ? -34.533 3.321   21.377 1.00 48.67  ? 1013 HOH A O     1 
HETATM 3559 O  O     . HOH N 6 .   ? -12.684 14.255  25.979 1.00 56.06  ? 1014 HOH A O     1 
HETATM 3560 O  O     . HOH N 6 .   ? 15.836  -7.904  33.063 1.00 49.54  ? 1015 HOH A O     1 
HETATM 3561 O  O     . HOH N 6 .   ? -9.627  -15.642 23.702 1.00 30.00  ? 1016 HOH A O     1 
HETATM 3562 O  O     . HOH N 6 .   ? -3.623  24.328  61.066 1.00 44.52  ? 1017 HOH A O     1 
HETATM 3563 O  O     . HOH N 6 .   ? 17.123  -21.477 19.029 1.00 54.10  ? 1018 HOH A O     1 
HETATM 3564 O  O     . HOH N 6 .   ? -8.144  20.844  66.922 1.00 44.04  ? 1019 HOH A O     1 
HETATM 3565 O  O     . HOH N 6 .   ? 18.819  -16.021 21.902 1.00 53.55  ? 1020 HOH A O     1 
HETATM 3566 O  O     . HOH N 6 .   ? 12.959  9.484   25.829 1.00 43.64  ? 1021 HOH A O     1 
HETATM 3567 O  O     . HOH N 6 .   ? 9.323   1.803   38.216 1.00 54.63  ? 1022 HOH A O     1 
HETATM 3568 O  O     . HOH N 6 .   ? 17.968  -14.017 9.862  1.00 41.96  ? 1023 HOH A O     1 
HETATM 3569 O  O     . HOH N 6 .   ? 9.030   12.829  29.892 1.00 50.70  ? 1024 HOH A O     1 
HETATM 3570 O  O     . HOH N 6 .   ? -16.714 -9.374  23.253 1.00 44.46  ? 1025 HOH A O     1 
HETATM 3571 O  O     . HOH N 6 .   ? 14.521  -2.361  6.226  1.00 45.72  ? 1026 HOH A O     1 
HETATM 3572 O  O     . HOH N 6 .   ? -33.779 0.895   44.073 1.00 51.87  ? 1027 HOH A O     1 
HETATM 3573 O  O     . HOH N 6 .   ? 13.025  9.583   23.474 1.00 34.63  ? 1028 HOH A O     1 
HETATM 3574 O  O     . HOH N 6 .   ? -15.504 -11.159 21.927 1.00 47.46  ? 1029 HOH A O     1 
HETATM 3575 O  O     . HOH N 6 .   ? 14.176  -16.326 21.603 1.00 47.80  ? 1030 HOH A O     1 
HETATM 3576 O  O     . HOH N 6 .   ? 21.917  1.400   11.701 1.00 54.25  ? 1031 HOH A O     1 
HETATM 3577 O  O     . HOH N 6 .   ? -12.463 6.031   9.095  1.00 40.36  ? 1032 HOH A O     1 
HETATM 3578 O  O     . HOH N 6 .   ? 14.072  0.364   10.627 1.00 33.79  ? 1033 HOH A O     1 
HETATM 3579 O  O     . HOH N 6 .   ? -15.116 -8.687  14.332 1.00 44.42  ? 1034 HOH A O     1 
HETATM 3580 O  O     . HOH N 6 .   ? 1.112   24.477  60.149 1.00 55.22  ? 1035 HOH A O     1 
HETATM 3581 O  O     . HOH N 6 .   ? -0.873  25.287  60.194 1.00 46.72  ? 1036 HOH A O     1 
HETATM 3582 O  O     . HOH N 6 .   ? -26.390 13.461  22.885 1.00 50.17  ? 1037 HOH A O     1 
HETATM 3583 O  O     . HOH N 6 .   ? 22.662  -16.126 19.394 1.00 49.05  ? 1038 HOH A O     1 
HETATM 3584 O  O     . HOH N 6 .   ? -7.007  0.359   39.693 1.00 57.73  ? 1039 HOH A O     1 
HETATM 3585 O  O     . HOH N 6 .   ? -21.577 22.092  37.018 1.00 53.92  ? 1040 HOH A O     1 
HETATM 3586 O  O     . HOH N 6 .   ? -10.201 2.729   38.734 1.00 30.00  ? 1041 HOH A O     1 
HETATM 3587 O  O     . HOH N 6 .   ? 15.751  10.409  23.658 1.00 50.69  ? 1042 HOH A O     1 
HETATM 3588 O  O     . HOH N 6 .   ? -15.093 -11.839 19.762 1.00 53.37  ? 1043 HOH A O     1 
HETATM 3589 O  O     . HOH N 6 .   ? 3.485   3.656   57.841 1.00 59.37  ? 1044 HOH A O     1 
HETATM 3590 O  O     . HOH N 6 .   ? 29.630  -1.716  19.860 1.00 39.86  ? 1045 HOH A O     1 
HETATM 3591 O  O     . HOH N 6 .   ? -15.906 -13.620 28.318 1.00 51.92  ? 1046 HOH A O     1 
HETATM 3592 O  O     . HOH N 6 .   ? 3.243   -1.949  37.400 1.00 47.05  ? 1047 HOH A O     1 
HETATM 3593 O  O     . HOH N 6 .   ? -2.433  14.289  21.346 1.00 39.79  ? 1048 HOH A O     1 
HETATM 3594 O  O     . HOH N 6 .   ? -2.366  20.574  42.946 1.00 45.64  ? 1049 HOH A O     1 
HETATM 3595 O  O     . HOH N 6 .   ? 0.202   -2.650  33.648 1.00 34.85  ? 1050 HOH A O     1 
HETATM 3596 O  O     . HOH N 6 .   ? 10.397  11.718  33.054 1.00 49.99  ? 1051 HOH A O     1 
HETATM 3597 O  O     . HOH N 6 .   ? -10.826 16.085  35.209 1.00 51.32  ? 1052 HOH A O     1 
HETATM 3598 O  O     . HOH N 6 .   ? -18.044 -4.687  15.934 1.00 46.33  ? 1053 HOH A O     1 
HETATM 3599 O  O     . HOH N 6 .   ? -6.328  -3.602  3.112  1.00 53.92  ? 1054 HOH A O     1 
HETATM 3600 O  O     . HOH N 6 .   ? -13.493 7.525   8.467  1.00 55.97  ? 1055 HOH A O     1 
HETATM 3601 O  O     . HOH N 6 .   ? 22.023  -12.169 27.462 1.00 55.62  ? 1056 HOH A O     1 
HETATM 3602 O  O     . HOH N 6 .   ? 7.404   5.913   8.008  1.00 45.35  ? 1057 HOH A O     1 
HETATM 3603 O  O     . HOH N 6 .   ? -33.655 9.093   32.623 1.00 48.08  ? 1058 HOH A O     1 
HETATM 3604 O  O     . HOH N 6 .   ? 3.472   1.543   60.953 1.00 54.45  ? 1059 HOH A O     1 
HETATM 3605 O  O     . HOH N 6 .   ? 9.426   3.393   10.362 1.00 39.43  ? 1060 HOH A O     1 
HETATM 3606 O  O     . HOH N 6 .   ? 14.385  -17.559 26.829 1.00 59.11  ? 1061 HOH A O     1 
HETATM 3607 O  O     . HOH N 6 .   ? 10.107  -10.453 33.454 1.00 47.82  ? 1062 HOH A O     1 
HETATM 3608 O  O     . HOH N 6 .   ? 1.334   -21.791 21.731 1.00 30.84  ? 1063 HOH A O     1 
HETATM 3609 O  O     . HOH N 6 .   ? -17.257 -2.330  12.340 1.00 52.86  ? 1064 HOH A O     1 
HETATM 3610 O  O     . HOH N 6 .   ? -27.817 2.118   49.690 1.00 53.25  ? 1065 HOH A O     1 
HETATM 3611 O  O     . HOH N 6 .   ? -1.520  22.329  44.784 1.00 58.79  ? 1066 HOH A O     1 
HETATM 3612 O  O     . HOH N 6 .   ? -24.413 19.793  43.073 1.00 34.84  ? 1067 HOH A O     1 
HETATM 3613 O  O     . HOH N 6 .   ? 5.755   14.251  53.270 1.00 50.19  ? 1068 HOH A O     1 
HETATM 3614 O  O     . HOH N 6 .   ? 13.807  -6.715  4.893  1.00 46.97  ? 1069 HOH A O     1 
HETATM 3615 O  O     . HOH N 6 .   ? -15.246 17.426  32.571 1.00 44.83  ? 1070 HOH A O     1 
HETATM 3616 O  O     . HOH N 6 .   ? 7.686   18.119  57.106 1.00 60.16  ? 1071 HOH A O     1 
HETATM 3617 O  O     . HOH N 6 .   ? 13.672  0.773   36.178 1.00 44.86  ? 1072 HOH A O     1 
HETATM 3618 O  O     . HOH N 6 .   ? -35.588 2.334   23.556 1.00 39.66  ? 1073 HOH A O     1 
HETATM 3619 O  O     . HOH N 6 .   ? 17.074  3.230   44.294 1.00 57.61  ? 1074 HOH A O     1 
HETATM 3620 O  O     . HOH N 6 .   ? -22.760 13.332  65.566 1.00 52.23  ? 1075 HOH A O     1 
HETATM 3621 O  O     . HOH N 6 .   ? 6.689   12.266  16.722 1.00 51.07  ? 1076 HOH A O     1 
HETATM 3622 O  O     . HOH N 6 .   ? -0.092  11.767  29.471 1.00 35.33  ? 1077 HOH A O     1 
HETATM 3623 O  O     . HOH N 6 .   ? -1.427  27.580  58.677 1.00 44.79  ? 1078 HOH A O     1 
HETATM 3624 O  O     . HOH N 6 .   ? 18.328  -5.222  35.428 1.00 57.18  ? 1079 HOH A O     1 
HETATM 3625 O  O     . HOH N 6 .   ? -29.714 -10.933 25.592 1.00 37.23  ? 1080 HOH A O     1 
HETATM 3626 O  O     . HOH N 6 .   ? -17.261 -8.955  18.540 1.00 56.38  ? 1081 HOH A O     1 
HETATM 3627 O  O     . HOH N 6 .   ? -35.550 -4.204  36.777 1.00 50.07  ? 1082 HOH A O     1 
HETATM 3628 O  O     . HOH N 6 .   ? -28.844 18.188  41.642 1.00 54.40  ? 1083 HOH A O     1 
HETATM 3629 O  O     . HOH N 6 .   ? -26.382 15.887  25.656 1.00 42.08  ? 1084 HOH A O     1 
HETATM 3630 O  O     . HOH N 6 .   ? -13.559 10.003  8.627  1.00 42.68  ? 1085 HOH A O     1 
HETATM 3631 O  O     . HOH N 6 .   ? 5.675   1.492   71.010 1.00 58.31  ? 1086 HOH A O     1 
HETATM 3632 O  O     . HOH N 6 .   ? 3.163   3.828   55.257 1.00 55.79  ? 1087 HOH A O     1 
HETATM 3633 O  O     . HOH N 6 .   ? 15.901  -0.329  22.952 1.00 27.58  ? 1088 HOH A O     1 
HETATM 3634 O  O     . HOH N 6 .   ? 26.527  -9.361  20.503 1.00 41.32  ? 1089 HOH A O     1 
HETATM 3635 O  O     . HOH N 6 .   ? -13.642 -14.343 27.060 1.00 56.40  ? 1090 HOH A O     1 
HETATM 3636 O  O     . HOH N 6 .   ? -37.285 -2.165  22.888 1.00 22.52  ? 1091 HOH A O     1 
HETATM 3637 O  O     . HOH N 6 .   ? -0.684  23.927  41.376 1.00 55.45  ? 1092 HOH A O     1 
HETATM 3638 O  O     . HOH N 6 .   ? -12.550 3.815   42.862 1.00 30.00  ? 1093 HOH A O     1 
HETATM 3639 O  O     . HOH N 6 .   ? -3.921  30.448  56.736 1.00 38.72  ? 1094 HOH A O     1 
HETATM 3640 O  O     . HOH N 6 .   ? 4.570   14.760  18.453 1.00 39.68  ? 1095 HOH A O     1 
HETATM 3641 O  O     . HOH N 6 .   ? 16.444  -15.198 23.208 1.00 44.40  ? 1096 HOH A O     1 
HETATM 3642 O  O     . HOH N 6 .   ? -27.999 -12.450 24.935 1.00 46.36  ? 1097 HOH A O     1 
HETATM 3643 O  O     . HOH N 6 .   ? 5.291   10.186  47.654 1.00 53.39  ? 1098 HOH A O     1 
HETATM 3644 O  O     . HOH N 6 .   ? -18.355 -4.326  11.869 1.00 44.27  ? 1099 HOH A O     1 
HETATM 3645 O  O     . HOH N 6 .   ? -28.112 19.474  43.418 1.00 56.98  ? 1100 HOH A O     1 
HETATM 3646 O  O     . HOH N 6 .   ? -15.355 -14.391 20.932 1.00 56.38  ? 1101 HOH A O     1 
# 
