data_9IQH
# 
_entry.id   9IQH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9IQH         pdb_00009iqh 10.2210/pdb9iqh/pdb 
WWPDB D_1300049088 ?            ?                   
# 
_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       2025-05-14 
_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                        9IQH 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-12 
_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              lixiaoju@sdu.edu.cn 
_pdbx_contact_author.name_first         Xiaoju 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7305-7313 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, X.J.'   1 ? 
'Chen, L.X.' 2 ? 
'Lin, J.Q.'  3 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Rsc Chem Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2633-0679 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            6 
_citation.language                  ? 
_citation.page_first                281 
_citation.page_last                 294 
_citation.title                     
'A one-step route for the conversion of Cd waste into CdS quantum dots by Acidithiobacillus sp. via unique biosynthesis pathways.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1039/d4cb00195h 
_citation.pdbx_database_id_PubMed   39802632 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, X.J.'    1 0000-0001-7305-7313 
primary 'Wang, T.Q.'  2 ?                   
primary 'Qi, L.'      3 ?                   
primary 'Li, F.W.'    4 ?                   
primary 'Xia, Y.Z.'   5 ?                   
primary 'Zhang, C.J.' 6 ?                   
primary 'Chen, L.X.'  7 ?                   
primary 'Lin, J.Q.'   8 ?                   
# 
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 'O-succinylhomoserine sulfhydrylase' 43663.398 2   2.5.1.- ? ? ? 
2 non-polymer syn "PYRIDOXAL-5'-PHOSPHATE"             247.142   2   ?       ? ? ? 
3 water       nat water                                18.015    489 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'OSH sulfhydrylase,OSHS sulfhydrylase' 
# 
_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       
;MNTKNTNPDWADRLRPETIAIRAGIHRTQEQEHSEAIFPTSSFVFDSAEEAADRFAGRVPGNIYARFTNPTVRTFEERLA
ALEGAEACVATASGMAACLTAFMGILKAGDHVVASRSIFGTTVQLLGNILSRFGVETSFVPLADVPAWRAALRPNTRMLF
LETPSNPLTEIGDMQALADLAHVHDAWLVVDNCFCTPALQQPLKFGADLVIHSATKYLDGQGRTLGGAVCGSTELLNSGP
RNFVRTAGPSLSPFNAWVQLKGLETLGLRMERHCANAQKIAEWLEARPEVARVYYPGLDSHPQQALAARQQRLPGAILSF
DLHGGQKAAWAFVDALRLLSLTANLGDAKTTITHPASTTHSRVSPEARAAAGVGDGLLRISVGLEHADDLREDMERGFAA
LVAR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNTKNTNPDWADRLRPETIAIRAGIHRTQEQEHSEAIFPTSSFVFDSAEEAADRFAGRVPGNIYARFTNPTVRTFEERLA
ALEGAEACVATASGMAACLTAFMGILKAGDHVVASRSIFGTTVQLLGNILSRFGVETSFVPLADVPAWRAALRPNTRMLF
LETPSNPLTEIGDMQALADLAHVHDAWLVVDNCFCTPALQQPLKFGADLVIHSATKYLDGQGRTLGGAVCGSTELLNSGP
RNFVRTAGPSLSPFNAWVQLKGLETLGLRMERHCANAQKIAEWLEARPEVARVYYPGLDSHPQQALAARQQRLPGAILSF
DLHGGQKAAWAFVDALRLLSLTANLGDAKTTITHPASTTHSRVSPEARAAAGVGDGLLRISVGLEHADDLREDMERGFAA
LVAR
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "PYRIDOXAL-5'-PHOSPHATE" PLP 
3 water                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   THR n 
1 4   LYS n 
1 5   ASN n 
1 6   THR n 
1 7   ASN n 
1 8   PRO n 
1 9   ASP n 
1 10  TRP n 
1 11  ALA n 
1 12  ASP n 
1 13  ARG n 
1 14  LEU n 
1 15  ARG n 
1 16  PRO n 
1 17  GLU n 
1 18  THR n 
1 19  ILE n 
1 20  ALA n 
1 21  ILE n 
1 22  ARG n 
1 23  ALA n 
1 24  GLY n 
1 25  ILE n 
1 26  HIS n 
1 27  ARG n 
1 28  THR n 
1 29  GLN n 
1 30  GLU n 
1 31  GLN n 
1 32  GLU n 
1 33  HIS n 
1 34  SER n 
1 35  GLU n 
1 36  ALA n 
1 37  ILE n 
1 38  PHE n 
1 39  PRO n 
1 40  THR n 
1 41  SER n 
1 42  SER n 
1 43  PHE n 
1 44  VAL n 
1 45  PHE n 
1 46  ASP n 
1 47  SER n 
1 48  ALA n 
1 49  GLU n 
1 50  GLU n 
1 51  ALA n 
1 52  ALA n 
1 53  ASP n 
1 54  ARG n 
1 55  PHE n 
1 56  ALA n 
1 57  GLY n 
1 58  ARG n 
1 59  VAL n 
1 60  PRO n 
1 61  GLY n 
1 62  ASN n 
1 63  ILE n 
1 64  TYR n 
1 65  ALA n 
1 66  ARG n 
1 67  PHE n 
1 68  THR n 
1 69  ASN n 
1 70  PRO n 
1 71  THR n 
1 72  VAL n 
1 73  ARG n 
1 74  THR n 
1 75  PHE n 
1 76  GLU n 
1 77  GLU n 
1 78  ARG n 
1 79  LEU n 
1 80  ALA n 
1 81  ALA n 
1 82  LEU n 
1 83  GLU n 
1 84  GLY n 
1 85  ALA n 
1 86  GLU n 
1 87  ALA n 
1 88  CYS n 
1 89  VAL n 
1 90  ALA n 
1 91  THR n 
1 92  ALA n 
1 93  SER n 
1 94  GLY n 
1 95  MET n 
1 96  ALA n 
1 97  ALA n 
1 98  CYS n 
1 99  LEU n 
1 100 THR n 
1 101 ALA n 
1 102 PHE n 
1 103 MET n 
1 104 GLY n 
1 105 ILE n 
1 106 LEU n 
1 107 LYS n 
1 108 ALA n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 VAL n 
1 113 VAL n 
1 114 ALA n 
1 115 SER n 
1 116 ARG n 
1 117 SER n 
1 118 ILE n 
1 119 PHE n 
1 120 GLY n 
1 121 THR n 
1 122 THR n 
1 123 VAL n 
1 124 GLN n 
1 125 LEU n 
1 126 LEU n 
1 127 GLY n 
1 128 ASN n 
1 129 ILE n 
1 130 LEU n 
1 131 SER n 
1 132 ARG n 
1 133 PHE n 
1 134 GLY n 
1 135 VAL n 
1 136 GLU n 
1 137 THR n 
1 138 SER n 
1 139 PHE n 
1 140 VAL n 
1 141 PRO n 
1 142 LEU n 
1 143 ALA n 
1 144 ASP n 
1 145 VAL n 
1 146 PRO n 
1 147 ALA n 
1 148 TRP n 
1 149 ARG n 
1 150 ALA n 
1 151 ALA n 
1 152 LEU n 
1 153 ARG n 
1 154 PRO n 
1 155 ASN n 
1 156 THR n 
1 157 ARG n 
1 158 MET n 
1 159 LEU n 
1 160 PHE n 
1 161 LEU n 
1 162 GLU n 
1 163 THR n 
1 164 PRO n 
1 165 SER n 
1 166 ASN n 
1 167 PRO n 
1 168 LEU n 
1 169 THR n 
1 170 GLU n 
1 171 ILE n 
1 172 GLY n 
1 173 ASP n 
1 174 MET n 
1 175 GLN n 
1 176 ALA n 
1 177 LEU n 
1 178 ALA n 
1 179 ASP n 
1 180 LEU n 
1 181 ALA n 
1 182 HIS n 
1 183 VAL n 
1 184 HIS n 
1 185 ASP n 
1 186 ALA n 
1 187 TRP n 
1 188 LEU n 
1 189 VAL n 
1 190 VAL n 
1 191 ASP n 
1 192 ASN n 
1 193 CYS n 
1 194 PHE n 
1 195 CYS n 
1 196 THR n 
1 197 PRO n 
1 198 ALA n 
1 199 LEU n 
1 200 GLN n 
1 201 GLN n 
1 202 PRO n 
1 203 LEU n 
1 204 LYS n 
1 205 PHE n 
1 206 GLY n 
1 207 ALA n 
1 208 ASP n 
1 209 LEU n 
1 210 VAL n 
1 211 ILE n 
1 212 HIS n 
1 213 SER n 
1 214 ALA n 
1 215 THR n 
1 216 LYS n 
1 217 TYR n 
1 218 LEU n 
1 219 ASP n 
1 220 GLY n 
1 221 GLN n 
1 222 GLY n 
1 223 ARG n 
1 224 THR n 
1 225 LEU n 
1 226 GLY n 
1 227 GLY n 
1 228 ALA n 
1 229 VAL n 
1 230 CYS n 
1 231 GLY n 
1 232 SER n 
1 233 THR n 
1 234 GLU n 
1 235 LEU n 
1 236 LEU n 
1 237 ASN n 
1 238 SER n 
1 239 GLY n 
1 240 PRO n 
1 241 ARG n 
1 242 ASN n 
1 243 PHE n 
1 244 VAL n 
1 245 ARG n 
1 246 THR n 
1 247 ALA n 
1 248 GLY n 
1 249 PRO n 
1 250 SER n 
1 251 LEU n 
1 252 SER n 
1 253 PRO n 
1 254 PHE n 
1 255 ASN n 
1 256 ALA n 
1 257 TRP n 
1 258 VAL n 
1 259 GLN n 
1 260 LEU n 
1 261 LYS n 
1 262 GLY n 
1 263 LEU n 
1 264 GLU n 
1 265 THR n 
1 266 LEU n 
1 267 GLY n 
1 268 LEU n 
1 269 ARG n 
1 270 MET n 
1 271 GLU n 
1 272 ARG n 
1 273 HIS n 
1 274 CYS n 
1 275 ALA n 
1 276 ASN n 
1 277 ALA n 
1 278 GLN n 
1 279 LYS n 
1 280 ILE n 
1 281 ALA n 
1 282 GLU n 
1 283 TRP n 
1 284 LEU n 
1 285 GLU n 
1 286 ALA n 
1 287 ARG n 
1 288 PRO n 
1 289 GLU n 
1 290 VAL n 
1 291 ALA n 
1 292 ARG n 
1 293 VAL n 
1 294 TYR n 
1 295 TYR n 
1 296 PRO n 
1 297 GLY n 
1 298 LEU n 
1 299 ASP n 
1 300 SER n 
1 301 HIS n 
1 302 PRO n 
1 303 GLN n 
1 304 GLN n 
1 305 ALA n 
1 306 LEU n 
1 307 ALA n 
1 308 ALA n 
1 309 ARG n 
1 310 GLN n 
1 311 GLN n 
1 312 ARG n 
1 313 LEU n 
1 314 PRO n 
1 315 GLY n 
1 316 ALA n 
1 317 ILE n 
1 318 LEU n 
1 319 SER n 
1 320 PHE n 
1 321 ASP n 
1 322 LEU n 
1 323 HIS n 
1 324 GLY n 
1 325 GLY n 
1 326 GLN n 
1 327 LYS n 
1 328 ALA n 
1 329 ALA n 
1 330 TRP n 
1 331 ALA n 
1 332 PHE n 
1 333 VAL n 
1 334 ASP n 
1 335 ALA n 
1 336 LEU n 
1 337 ARG n 
1 338 LEU n 
1 339 LEU n 
1 340 SER n 
1 341 LEU n 
1 342 THR n 
1 343 ALA n 
1 344 ASN n 
1 345 LEU n 
1 346 GLY n 
1 347 ASP n 
1 348 ALA n 
1 349 LYS n 
1 350 THR n 
1 351 THR n 
1 352 ILE n 
1 353 THR n 
1 354 HIS n 
1 355 PRO n 
1 356 ALA n 
1 357 SER n 
1 358 THR n 
1 359 THR n 
1 360 HIS n 
1 361 SER n 
1 362 ARG n 
1 363 VAL n 
1 364 SER n 
1 365 PRO n 
1 366 GLU n 
1 367 ALA n 
1 368 ARG n 
1 369 ALA n 
1 370 ALA n 
1 371 ALA n 
1 372 GLY n 
1 373 VAL n 
1 374 GLY n 
1 375 ASP n 
1 376 GLY n 
1 377 LEU n 
1 378 LEU n 
1 379 ARG n 
1 380 ILE n 
1 381 SER n 
1 382 VAL n 
1 383 GLY n 
1 384 LEU n 
1 385 GLU n 
1 386 HIS n 
1 387 ALA n 
1 388 ASP n 
1 389 ASP n 
1 390 LEU n 
1 391 ARG n 
1 392 GLU n 
1 393 ASP n 
1 394 MET n 
1 395 GLU n 
1 396 ARG n 
1 397 GLY n 
1 398 PHE n 
1 399 ALA n 
1 400 ALA n 
1 401 LEU n 
1 402 VAL n 
1 403 ALA n 
1 404 ARG 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                   404 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'metZ, DN052_15485' 
_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      Acidithiobacillus 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     920 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                  ?                      'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                 ?                      'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE               ?                      'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'          ?                      'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                 ?                      'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                ?                      'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'          ?                      'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                  ?                      'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                ?                      'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                    ?                      'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE               ?                      'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                  ?                      'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                   ?                      'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE               ?                      'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE            ?                      'C9 H11 N O2'    165.189 
PLP non-polymer         . "PYRIDOXAL-5'-PHOSPHATE" 'VITAMIN B6 Phosphate' 'C8 H10 N O6 P'  247.142 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASN 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   ?   ?   ?   A . n 
A 1 5   ASN 5   5   ?   ?   ?   A . n 
A 1 6   THR 6   6   ?   ?   ?   A . n 
A 1 7   ASN 7   7   ?   ?   ?   A . n 
A 1 8   PRO 8   8   ?   ?   ?   A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  ARG 13  13  13  ARG ARG A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  ARG 15  15  15  ARG ARG A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  HIS 26  26  26  HIS HIS A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  THR 28  28  28  THR THR A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  PHE 55  55  55  PHE PHE A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  CYS 88  88  88  CYS CYS A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  MET 95  95  95  MET MET A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  CYS 98  98  98  CYS CYS A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 PHE 102 102 102 PHE PHE A . n 
A 1 103 MET 103 103 103 MET MET A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 GLN 124 124 124 GLN GLN A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 PRO 146 146 146 PRO PRO A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 TRP 148 148 148 TRP TRP A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 ARG 153 153 153 ARG ARG A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 MET 158 158 158 MET MET A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 PHE 160 160 160 PHE PHE A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 PRO 164 164 164 PRO PRO A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ASN 166 166 166 ASN ASN A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLU 170 170 170 GLU GLU A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 MET 174 174 174 MET MET A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 HIS 182 182 182 HIS HIS A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 HIS 184 184 184 HIS HIS A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 TRP 187 187 187 TRP TRP A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 ASN 192 192 192 ASN ASN A . n 
A 1 193 CYS 193 193 193 CYS CYS A . n 
A 1 194 PHE 194 194 194 PHE PHE A . n 
A 1 195 CYS 195 195 195 CYS CYS A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 GLN 200 200 200 GLN GLN A . n 
A 1 201 GLN 201 201 201 GLN GLN A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 GLY 206 206 206 GLY GLY A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 HIS 212 212 212 HIS HIS A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 THR 215 215 215 THR THR A . n 
A 1 216 LYS 216 216 216 LYS LYS A . n 
A 1 217 TYR 217 217 217 TYR TYR A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 VAL 229 229 229 VAL VAL A . n 
A 1 230 CYS 230 230 230 CYS CYS A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 GLU 234 234 234 GLU GLU A . n 
A 1 235 LEU 235 235 235 LEU LEU A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 ARG 241 241 241 ARG ARG A . n 
A 1 242 ASN 242 242 242 ASN ASN A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 GLY 248 248 248 GLY GLY A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 PHE 254 254 254 PHE PHE A . n 
A 1 255 ASN 255 255 255 ASN ASN A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 TRP 257 257 257 TRP TRP A . n 
A 1 258 VAL 258 258 258 VAL VAL A . n 
A 1 259 GLN 259 259 259 GLN GLN A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 LYS 261 261 261 LYS LYS A . n 
A 1 262 GLY 262 262 262 GLY GLY A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 ARG 269 269 269 ARG ARG A . n 
A 1 270 MET 270 270 270 MET MET A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 ARG 272 272 272 ARG ARG A . n 
A 1 273 HIS 273 273 273 HIS HIS A . n 
A 1 274 CYS 274 274 274 CYS CYS A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 ASN 276 276 276 ASN ASN A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 GLN 278 278 278 GLN GLN A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 GLU 282 282 282 GLU GLU A . n 
A 1 283 TRP 283 283 283 TRP TRP A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 GLU 285 285 285 GLU GLU A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 ARG 287 287 287 ARG ARG A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 GLU 289 289 289 GLU GLU A . n 
A 1 290 VAL 290 290 290 VAL VAL A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ARG 292 292 292 ARG ARG A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 TYR 294 294 294 TYR TYR A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 PRO 296 296 296 PRO PRO A . n 
A 1 297 GLY 297 297 297 GLY GLY A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 ASP 299 299 299 ASP ASP A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 HIS 301 301 301 HIS HIS A . n 
A 1 302 PRO 302 302 302 PRO PRO A . n 
A 1 303 GLN 303 303 303 GLN GLN A . n 
A 1 304 GLN 304 304 304 GLN GLN A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 ARG 309 309 309 ARG ARG A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 GLN 311 311 311 GLN GLN A . n 
A 1 312 ARG 312 312 312 ARG ARG A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 PRO 314 314 314 PRO PRO A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 ILE 317 317 317 ILE ILE A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 SER 319 319 319 SER SER A . n 
A 1 320 PHE 320 320 320 PHE PHE A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 HIS 323 323 323 HIS HIS A . n 
A 1 324 GLY 324 324 324 GLY GLY A . n 
A 1 325 GLY 325 325 325 GLY GLY A . n 
A 1 326 GLN 326 326 326 GLN GLN A . n 
A 1 327 LYS 327 327 327 LYS LYS A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 ALA 329 329 329 ALA ALA A . n 
A 1 330 TRP 330 330 330 TRP TRP A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 PHE 332 332 332 PHE PHE A . n 
A 1 333 VAL 333 333 333 VAL VAL A . n 
A 1 334 ASP 334 334 334 ASP ASP A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 LEU 336 336 336 LEU LEU A . n 
A 1 337 ARG 337 337 337 ARG ARG A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 THR 342 342 342 THR THR A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 ASN 344 344 344 ASN ASN A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 GLY 346 346 346 GLY GLY A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 THR 350 350 350 THR THR A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 ILE 352 352 352 ILE ILE A . n 
A 1 353 THR 353 353 353 THR THR A . n 
A 1 354 HIS 354 354 354 HIS HIS A . n 
A 1 355 PRO 355 355 355 PRO PRO A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 SER 357 357 357 SER SER A . n 
A 1 358 THR 358 358 358 THR THR A . n 
A 1 359 THR 359 359 359 THR THR A . n 
A 1 360 HIS 360 360 360 HIS HIS A . n 
A 1 361 SER 361 361 361 SER SER A . n 
A 1 362 ARG 362 362 362 ARG ARG A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 SER 364 364 364 SER SER A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 ALA 367 367 367 ALA ALA A . n 
A 1 368 ARG 368 368 368 ARG ARG A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 ALA 370 370 370 ALA ALA A . n 
A 1 371 ALA 371 371 371 ALA ALA A . n 
A 1 372 GLY 372 372 372 GLY GLY A . n 
A 1 373 VAL 373 373 373 VAL VAL A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 ASP 375 375 375 ASP ASP A . n 
A 1 376 GLY 376 376 376 GLY GLY A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 ILE 380 380 380 ILE ILE A . n 
A 1 381 SER 381 381 381 SER SER A . n 
A 1 382 VAL 382 382 382 VAL VAL A . n 
A 1 383 GLY 383 383 383 GLY GLY A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 GLU 385 385 385 GLU GLU A . n 
A 1 386 HIS 386 386 386 HIS HIS A . n 
A 1 387 ALA 387 387 387 ALA ALA A . n 
A 1 388 ASP 388 388 388 ASP ASP A . n 
A 1 389 ASP 389 389 389 ASP ASP A . n 
A 1 390 LEU 390 390 390 LEU LEU A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 GLU 392 392 392 GLU GLU A . n 
A 1 393 ASP 393 393 393 ASP ASP A . n 
A 1 394 MET 394 394 394 MET MET A . n 
A 1 395 GLU 395 395 395 GLU GLU A . n 
A 1 396 ARG 396 396 396 ARG ARG A . n 
A 1 397 GLY 397 397 397 GLY GLY A . n 
A 1 398 PHE 398 398 398 PHE PHE A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 ALA 403 403 ?   ?   ?   A . n 
A 1 404 ARG 404 404 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ASN 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   LYS 4   4   ?   ?   ?   B . n 
B 1 5   ASN 5   5   ?   ?   ?   B . n 
B 1 6   THR 6   6   ?   ?   ?   B . n 
B 1 7   ASN 7   7   ?   ?   ?   B . n 
B 1 8   PRO 8   8   ?   ?   ?   B . n 
B 1 9   ASP 9   9   9   ASP ASP B . n 
B 1 10  TRP 10  10  10  TRP TRP B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  ARG 13  13  13  ARG ARG B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  ARG 15  15  15  ARG ARG B . n 
B 1 16  PRO 16  16  16  PRO PRO B . n 
B 1 17  GLU 17  17  17  GLU GLU B . n 
B 1 18  THR 18  18  18  THR THR B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  ILE 21  21  21  ILE ILE B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  ILE 25  25  25  ILE ILE B . n 
B 1 26  HIS 26  26  26  HIS HIS B . n 
B 1 27  ARG 27  27  27  ARG ARG B . n 
B 1 28  THR 28  28  28  THR THR B . n 
B 1 29  GLN 29  29  29  GLN GLN B . n 
B 1 30  GLU 30  30  30  GLU GLU B . n 
B 1 31  GLN 31  31  31  GLN GLN B . n 
B 1 32  GLU 32  32  32  GLU GLU B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  ILE 37  37  37  ILE ILE B . n 
B 1 38  PHE 38  38  38  PHE PHE B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  SER 41  41  41  SER SER B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  PHE 43  43  43  PHE PHE B . n 
B 1 44  VAL 44  44  44  VAL VAL B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  ASP 46  46  46  ASP ASP B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  GLU 50  50  50  GLU GLU B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  ASP 53  53  53  ASP ASP B . n 
B 1 54  ARG 54  54  54  ARG ARG B . n 
B 1 55  PHE 55  55  55  PHE PHE B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  ASN 62  62  62  ASN ASN B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  TYR 64  64  64  TYR TYR B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  PHE 67  67  67  PHE PHE B . n 
B 1 68  THR 68  68  68  THR THR B . n 
B 1 69  ASN 69  69  69  ASN ASN B . n 
B 1 70  PRO 70  70  70  PRO PRO B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  THR 74  74  74  THR THR B . n 
B 1 75  PHE 75  75  75  PHE PHE B . n 
B 1 76  GLU 76  76  76  GLU GLU B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  ARG 78  78  78  ARG ARG B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  GLU 83  83  83  GLU GLU B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  ALA 85  85  85  ALA ALA B . n 
B 1 86  GLU 86  86  86  GLU GLU B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  CYS 88  88  88  CYS CYS B . n 
B 1 89  VAL 89  89  89  VAL VAL B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  GLY 94  94  94  GLY GLY B . n 
B 1 95  MET 95  95  95  MET MET B . n 
B 1 96  ALA 96  96  96  ALA ALA B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  CYS 98  98  98  CYS CYS B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 THR 100 100 100 THR THR B . n 
B 1 101 ALA 101 101 101 ALA ALA B . n 
B 1 102 PHE 102 102 102 PHE PHE B . n 
B 1 103 MET 103 103 103 MET MET B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 VAL 113 113 113 VAL VAL B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 ARG 116 116 116 ARG ARG B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 THR 121 121 121 THR THR B . n 
B 1 122 THR 122 122 122 THR THR B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 GLN 124 124 124 GLN GLN B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 ASN 128 128 128 ASN ASN B . n 
B 1 129 ILE 129 129 129 ILE ILE B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 SER 131 131 131 SER SER B . n 
B 1 132 ARG 132 132 132 ARG ARG B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 GLY 134 134 134 GLY GLY B . n 
B 1 135 VAL 135 135 135 VAL VAL B . n 
B 1 136 GLU 136 136 136 GLU GLU B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 SER 138 138 138 SER SER B . n 
B 1 139 PHE 139 139 139 PHE PHE B . n 
B 1 140 VAL 140 140 140 VAL VAL B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 ASP 144 144 144 ASP ASP B . n 
B 1 145 VAL 145 145 145 VAL VAL B . n 
B 1 146 PRO 146 146 146 PRO PRO B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 TRP 148 148 148 TRP TRP B . n 
B 1 149 ARG 149 149 149 ARG ARG B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 ALA 151 151 151 ALA ALA B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 ARG 153 153 153 ARG ARG B . n 
B 1 154 PRO 154 154 154 PRO PRO B . n 
B 1 155 ASN 155 155 155 ASN ASN B . n 
B 1 156 THR 156 156 156 THR THR B . n 
B 1 157 ARG 157 157 157 ARG ARG B . n 
B 1 158 MET 158 158 158 MET MET B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 PHE 160 160 160 PHE PHE B . n 
B 1 161 LEU 161 161 161 LEU LEU B . n 
B 1 162 GLU 162 162 162 GLU GLU B . n 
B 1 163 THR 163 163 163 THR THR B . n 
B 1 164 PRO 164 164 164 PRO PRO B . n 
B 1 165 SER 165 165 165 SER SER B . n 
B 1 166 ASN 166 166 166 ASN ASN B . n 
B 1 167 PRO 167 167 167 PRO PRO B . n 
B 1 168 LEU 168 168 168 LEU LEU B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLU 170 170 170 GLU GLU B . n 
B 1 171 ILE 171 171 171 ILE ILE B . n 
B 1 172 GLY 172 172 172 GLY GLY B . n 
B 1 173 ASP 173 173 173 ASP ASP B . n 
B 1 174 MET 174 174 174 MET MET B . n 
B 1 175 GLN 175 175 175 GLN GLN B . n 
B 1 176 ALA 176 176 176 ALA ALA B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 ALA 178 178 178 ALA ALA B . n 
B 1 179 ASP 179 179 179 ASP ASP B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 ALA 181 181 181 ALA ALA B . n 
B 1 182 HIS 182 182 182 HIS HIS B . n 
B 1 183 VAL 183 183 183 VAL VAL B . n 
B 1 184 HIS 184 184 184 HIS HIS B . n 
B 1 185 ASP 185 185 185 ASP ASP B . n 
B 1 186 ALA 186 186 186 ALA ALA B . n 
B 1 187 TRP 187 187 187 TRP TRP B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 VAL 189 189 189 VAL VAL B . n 
B 1 190 VAL 190 190 190 VAL VAL B . n 
B 1 191 ASP 191 191 191 ASP ASP B . n 
B 1 192 ASN 192 192 192 ASN ASN B . n 
B 1 193 CYS 193 193 193 CYS CYS B . n 
B 1 194 PHE 194 194 194 PHE PHE B . n 
B 1 195 CYS 195 195 195 CYS CYS B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 PRO 197 197 197 PRO PRO B . n 
B 1 198 ALA 198 198 198 ALA ALA B . n 
B 1 199 LEU 199 199 199 LEU LEU B . n 
B 1 200 GLN 200 200 200 GLN GLN B . n 
B 1 201 GLN 201 201 201 GLN GLN B . n 
B 1 202 PRO 202 202 202 PRO PRO B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 LYS 204 204 204 LYS LYS B . n 
B 1 205 PHE 205 205 205 PHE PHE B . n 
B 1 206 GLY 206 206 206 GLY GLY B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 LEU 209 209 209 LEU LEU B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 ILE 211 211 211 ILE ILE B . n 
B 1 212 HIS 212 212 212 HIS HIS B . n 
B 1 213 SER 213 213 213 SER SER B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 THR 215 215 215 THR THR B . n 
B 1 216 LYS 216 216 216 LYS LYS B . n 
B 1 217 TYR 217 217 217 TYR TYR B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 ASP 219 219 219 ASP ASP B . n 
B 1 220 GLY 220 220 220 GLY GLY B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 GLY 222 222 222 GLY GLY B . n 
B 1 223 ARG 223 223 223 ARG ARG B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLY 226 226 226 GLY GLY B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 VAL 229 229 229 VAL VAL B . n 
B 1 230 CYS 230 230 230 CYS CYS B . n 
B 1 231 GLY 231 231 231 GLY GLY B . n 
B 1 232 SER 232 232 232 SER SER B . n 
B 1 233 THR 233 233 233 THR THR B . n 
B 1 234 GLU 234 234 234 GLU GLU B . n 
B 1 235 LEU 235 235 235 LEU LEU B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 ASN 237 237 237 ASN ASN B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 GLY 239 239 239 GLY GLY B . n 
B 1 240 PRO 240 240 240 PRO PRO B . n 
B 1 241 ARG 241 241 241 ARG ARG B . n 
B 1 242 ASN 242 242 242 ASN ASN B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 VAL 244 244 244 VAL VAL B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 THR 246 246 246 THR THR B . n 
B 1 247 ALA 247 247 247 ALA ALA B . n 
B 1 248 GLY 248 248 248 GLY GLY B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 SER 250 250 250 SER SER B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 SER 252 252 252 SER SER B . n 
B 1 253 PRO 253 253 253 PRO PRO B . n 
B 1 254 PHE 254 254 254 PHE PHE B . n 
B 1 255 ASN 255 255 255 ASN ASN B . n 
B 1 256 ALA 256 256 256 ALA ALA B . n 
B 1 257 TRP 257 257 257 TRP TRP B . n 
B 1 258 VAL 258 258 258 VAL VAL B . n 
B 1 259 GLN 259 259 259 GLN GLN B . n 
B 1 260 LEU 260 260 260 LEU LEU B . n 
B 1 261 LYS 261 261 261 LYS LYS B . n 
B 1 262 GLY 262 262 262 GLY GLY B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 GLU 264 264 264 GLU GLU B . n 
B 1 265 THR 265 265 265 THR THR B . n 
B 1 266 LEU 266 266 266 LEU LEU B . n 
B 1 267 GLY 267 267 267 GLY GLY B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 ARG 269 269 269 ARG ARG B . n 
B 1 270 MET 270 270 270 MET MET B . n 
B 1 271 GLU 271 271 271 GLU GLU B . n 
B 1 272 ARG 272 272 272 ARG ARG B . n 
B 1 273 HIS 273 273 273 HIS HIS B . n 
B 1 274 CYS 274 274 274 CYS CYS B . n 
B 1 275 ALA 275 275 275 ALA ALA B . n 
B 1 276 ASN 276 276 276 ASN ASN B . n 
B 1 277 ALA 277 277 277 ALA ALA B . n 
B 1 278 GLN 278 278 278 GLN GLN B . n 
B 1 279 LYS 279 279 279 LYS LYS B . n 
B 1 280 ILE 280 280 280 ILE ILE B . n 
B 1 281 ALA 281 281 281 ALA ALA B . n 
B 1 282 GLU 282 282 282 GLU GLU B . n 
B 1 283 TRP 283 283 283 TRP TRP B . n 
B 1 284 LEU 284 284 284 LEU LEU B . n 
B 1 285 GLU 285 285 285 GLU GLU B . n 
B 1 286 ALA 286 286 286 ALA ALA B . n 
B 1 287 ARG 287 287 287 ARG ARG B . n 
B 1 288 PRO 288 288 288 PRO PRO B . n 
B 1 289 GLU 289 289 289 GLU GLU B . n 
B 1 290 VAL 290 290 290 VAL VAL B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 ARG 292 292 292 ARG ARG B . n 
B 1 293 VAL 293 293 293 VAL VAL B . n 
B 1 294 TYR 294 294 294 TYR TYR B . n 
B 1 295 TYR 295 295 295 TYR TYR B . n 
B 1 296 PRO 296 296 296 PRO PRO B . n 
B 1 297 GLY 297 297 297 GLY GLY B . n 
B 1 298 LEU 298 298 298 LEU LEU B . n 
B 1 299 ASP 299 299 299 ASP ASP B . n 
B 1 300 SER 300 300 300 SER SER B . n 
B 1 301 HIS 301 301 301 HIS HIS B . n 
B 1 302 PRO 302 302 302 PRO PRO B . n 
B 1 303 GLN 303 303 303 GLN GLN B . n 
B 1 304 GLN 304 304 304 GLN GLN B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 LEU 306 306 306 LEU LEU B . n 
B 1 307 ALA 307 307 307 ALA ALA B . n 
B 1 308 ALA 308 308 308 ALA ALA B . n 
B 1 309 ARG 309 309 309 ARG ARG B . n 
B 1 310 GLN 310 310 310 GLN GLN B . n 
B 1 311 GLN 311 311 311 GLN GLN B . n 
B 1 312 ARG 312 312 312 ARG ARG B . n 
B 1 313 LEU 313 313 313 LEU LEU B . n 
B 1 314 PRO 314 314 314 PRO PRO B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 ALA 316 316 316 ALA ALA B . n 
B 1 317 ILE 317 317 317 ILE ILE B . n 
B 1 318 LEU 318 318 318 LEU LEU B . n 
B 1 319 SER 319 319 319 SER SER B . n 
B 1 320 PHE 320 320 320 PHE PHE B . n 
B 1 321 ASP 321 321 321 ASP ASP B . n 
B 1 322 LEU 322 322 322 LEU LEU B . n 
B 1 323 HIS 323 323 323 HIS HIS B . n 
B 1 324 GLY 324 324 324 GLY GLY B . n 
B 1 325 GLY 325 325 325 GLY GLY B . n 
B 1 326 GLN 326 326 326 GLN GLN B . n 
B 1 327 LYS 327 327 327 LYS LYS B . n 
B 1 328 ALA 328 328 328 ALA ALA B . n 
B 1 329 ALA 329 329 329 ALA ALA B . n 
B 1 330 TRP 330 330 330 TRP TRP B . n 
B 1 331 ALA 331 331 331 ALA ALA B . n 
B 1 332 PHE 332 332 332 PHE PHE B . n 
B 1 333 VAL 333 333 333 VAL VAL B . n 
B 1 334 ASP 334 334 334 ASP ASP B . n 
B 1 335 ALA 335 335 335 ALA ALA B . n 
B 1 336 LEU 336 336 336 LEU LEU B . n 
B 1 337 ARG 337 337 337 ARG ARG B . n 
B 1 338 LEU 338 338 338 LEU LEU B . n 
B 1 339 LEU 339 339 339 LEU LEU B . n 
B 1 340 SER 340 340 340 SER SER B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 THR 342 342 342 THR THR B . n 
B 1 343 ALA 343 343 343 ALA ALA B . n 
B 1 344 ASN 344 344 344 ASN ASN B . n 
B 1 345 LEU 345 345 345 LEU LEU B . n 
B 1 346 GLY 346 346 346 GLY GLY B . n 
B 1 347 ASP 347 347 347 ASP ASP B . n 
B 1 348 ALA 348 348 348 ALA ALA B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 THR 350 350 350 THR THR B . n 
B 1 351 THR 351 351 351 THR THR B . n 
B 1 352 ILE 352 352 352 ILE ILE B . n 
B 1 353 THR 353 353 353 THR THR B . n 
B 1 354 HIS 354 354 354 HIS HIS B . n 
B 1 355 PRO 355 355 355 PRO PRO B . n 
B 1 356 ALA 356 356 356 ALA ALA B . n 
B 1 357 SER 357 357 357 SER SER B . n 
B 1 358 THR 358 358 358 THR THR B . n 
B 1 359 THR 359 359 359 THR THR B . n 
B 1 360 HIS 360 360 360 HIS HIS B . n 
B 1 361 SER 361 361 361 SER SER B . n 
B 1 362 ARG 362 362 362 ARG ARG B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 SER 364 364 364 SER SER B . n 
B 1 365 PRO 365 365 365 PRO PRO B . n 
B 1 366 GLU 366 366 366 GLU GLU B . n 
B 1 367 ALA 367 367 367 ALA ALA B . n 
B 1 368 ARG 368 368 368 ARG ARG B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 ALA 370 370 370 ALA ALA B . n 
B 1 371 ALA 371 371 371 ALA ALA B . n 
B 1 372 GLY 372 372 372 GLY GLY B . n 
B 1 373 VAL 373 373 373 VAL VAL B . n 
B 1 374 GLY 374 374 374 GLY GLY B . n 
B 1 375 ASP 375 375 375 ASP ASP B . n 
B 1 376 GLY 376 376 376 GLY GLY B . n 
B 1 377 LEU 377 377 377 LEU LEU B . n 
B 1 378 LEU 378 378 378 LEU LEU B . n 
B 1 379 ARG 379 379 379 ARG ARG B . n 
B 1 380 ILE 380 380 380 ILE ILE B . n 
B 1 381 SER 381 381 381 SER SER B . n 
B 1 382 VAL 382 382 382 VAL VAL B . n 
B 1 383 GLY 383 383 383 GLY GLY B . n 
B 1 384 LEU 384 384 384 LEU LEU B . n 
B 1 385 GLU 385 385 385 GLU GLU B . n 
B 1 386 HIS 386 386 386 HIS HIS B . n 
B 1 387 ALA 387 387 387 ALA ALA B . n 
B 1 388 ASP 388 388 388 ASP ASP B . n 
B 1 389 ASP 389 389 389 ASP ASP B . n 
B 1 390 LEU 390 390 390 LEU LEU B . n 
B 1 391 ARG 391 391 391 ARG ARG B . n 
B 1 392 GLU 392 392 392 GLU GLU B . n 
B 1 393 ASP 393 393 393 ASP ASP B . n 
B 1 394 MET 394 394 394 MET MET B . n 
B 1 395 GLU 395 395 395 GLU GLU B . n 
B 1 396 ARG 396 396 396 ARG ARG B . n 
B 1 397 GLY 397 397 397 GLY GLY B . n 
B 1 398 PHE 398 398 398 PHE PHE B . n 
B 1 399 ALA 399 399 399 ALA ALA B . n 
B 1 400 ALA 400 400 400 ALA ALA B . n 
B 1 401 LEU 401 401 401 LEU LEU B . n 
B 1 402 VAL 402 402 402 VAL VAL B . n 
B 1 403 ALA 403 403 403 ALA ALA B . n 
B 1 404 ARG 404 404 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        PLP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   PLP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 PLP 1   501 501 PLP PLP A . 
D 2 PLP 1   501 501 PLP PLP B . 
E 3 HOH 1   601 403 HOH HOH A . 
E 3 HOH 2   602 386 HOH HOH A . 
E 3 HOH 3   603 50  HOH HOH A . 
E 3 HOH 4   604 159 HOH HOH A . 
E 3 HOH 5   605 293 HOH HOH A . 
E 3 HOH 6   606 45  HOH HOH A . 
E 3 HOH 7   607 168 HOH HOH A . 
E 3 HOH 8   608 291 HOH HOH A . 
E 3 HOH 9   609 280 HOH HOH A . 
E 3 HOH 10  610 170 HOH HOH A . 
E 3 HOH 11  611 148 HOH HOH A . 
E 3 HOH 12  612 15  HOH HOH A . 
E 3 HOH 13  613 354 HOH HOH A . 
E 3 HOH 14  614 371 HOH HOH A . 
E 3 HOH 15  615 313 HOH HOH A . 
E 3 HOH 16  616 421 HOH HOH A . 
E 3 HOH 17  617 367 HOH HOH A . 
E 3 HOH 18  618 331 HOH HOH A . 
E 3 HOH 19  619 8   HOH HOH A . 
E 3 HOH 20  620 343 HOH HOH A . 
E 3 HOH 21  621 44  HOH HOH A . 
E 3 HOH 22  622 198 HOH HOH A . 
E 3 HOH 23  623 413 HOH HOH A . 
E 3 HOH 24  624 266 HOH HOH A . 
E 3 HOH 25  625 174 HOH HOH A . 
E 3 HOH 26  626 80  HOH HOH A . 
E 3 HOH 27  627 58  HOH HOH A . 
E 3 HOH 28  628 85  HOH HOH A . 
E 3 HOH 29  629 344 HOH HOH A . 
E 3 HOH 30  630 199 HOH HOH A . 
E 3 HOH 31  631 35  HOH HOH A . 
E 3 HOH 32  632 67  HOH HOH A . 
E 3 HOH 33  633 361 HOH HOH A . 
E 3 HOH 34  634 273 HOH HOH A . 
E 3 HOH 35  635 32  HOH HOH A . 
E 3 HOH 36  636 20  HOH HOH A . 
E 3 HOH 37  637 28  HOH HOH A . 
E 3 HOH 38  638 414 HOH HOH A . 
E 3 HOH 39  639 153 HOH HOH A . 
E 3 HOH 40  640 192 HOH HOH A . 
E 3 HOH 41  641 37  HOH HOH A . 
E 3 HOH 42  642 326 HOH HOH A . 
E 3 HOH 43  643 395 HOH HOH A . 
E 3 HOH 44  644 362 HOH HOH A . 
E 3 HOH 45  645 141 HOH HOH A . 
E 3 HOH 46  646 228 HOH HOH A . 
E 3 HOH 47  647 152 HOH HOH A . 
E 3 HOH 48  648 209 HOH HOH A . 
E 3 HOH 49  649 126 HOH HOH A . 
E 3 HOH 50  650 231 HOH HOH A . 
E 3 HOH 51  651 95  HOH HOH A . 
E 3 HOH 52  652 55  HOH HOH A . 
E 3 HOH 53  653 203 HOH HOH A . 
E 3 HOH 54  654 17  HOH HOH A . 
E 3 HOH 55  655 462 HOH HOH A . 
E 3 HOH 56  656 81  HOH HOH A . 
E 3 HOH 57  657 388 HOH HOH A . 
E 3 HOH 58  658 214 HOH HOH A . 
E 3 HOH 59  659 104 HOH HOH A . 
E 3 HOH 60  660 441 HOH HOH A . 
E 3 HOH 61  661 304 HOH HOH A . 
E 3 HOH 62  662 391 HOH HOH A . 
E 3 HOH 63  663 30  HOH HOH A . 
E 3 HOH 64  664 90  HOH HOH A . 
E 3 HOH 65  665 487 HOH HOH A . 
E 3 HOH 66  666 495 HOH HOH A . 
E 3 HOH 67  667 146 HOH HOH A . 
E 3 HOH 68  668 259 HOH HOH A . 
E 3 HOH 69  669 29  HOH HOH A . 
E 3 HOH 70  670 145 HOH HOH A . 
E 3 HOH 71  671 124 HOH HOH A . 
E 3 HOH 72  672 43  HOH HOH A . 
E 3 HOH 73  673 356 HOH HOH A . 
E 3 HOH 74  674 89  HOH HOH A . 
E 3 HOH 75  675 13  HOH HOH A . 
E 3 HOH 76  676 366 HOH HOH A . 
E 3 HOH 77  677 177 HOH HOH A . 
E 3 HOH 78  678 53  HOH HOH A . 
E 3 HOH 79  679 38  HOH HOH A . 
E 3 HOH 80  680 151 HOH HOH A . 
E 3 HOH 81  681 143 HOH HOH A . 
E 3 HOH 82  682 180 HOH HOH A . 
E 3 HOH 83  683 40  HOH HOH A . 
E 3 HOH 84  684 4   HOH HOH A . 
E 3 HOH 85  685 140 HOH HOH A . 
E 3 HOH 86  686 22  HOH HOH A . 
E 3 HOH 87  687 315 HOH HOH A . 
E 3 HOH 88  688 460 HOH HOH A . 
E 3 HOH 89  689 260 HOH HOH A . 
E 3 HOH 90  690 14  HOH HOH A . 
E 3 HOH 91  691 187 HOH HOH A . 
E 3 HOH 92  692 171 HOH HOH A . 
E 3 HOH 93  693 385 HOH HOH A . 
E 3 HOH 94  694 424 HOH HOH A . 
E 3 HOH 95  695 282 HOH HOH A . 
E 3 HOH 96  696 368 HOH HOH A . 
E 3 HOH 97  697 200 HOH HOH A . 
E 3 HOH 98  698 150 HOH HOH A . 
E 3 HOH 99  699 92  HOH HOH A . 
E 3 HOH 100 700 77  HOH HOH A . 
E 3 HOH 101 701 160 HOH HOH A . 
E 3 HOH 102 702 18  HOH HOH A . 
E 3 HOH 103 703 482 HOH HOH A . 
E 3 HOH 104 704 136 HOH HOH A . 
E 3 HOH 105 705 109 HOH HOH A . 
E 3 HOH 106 706 233 HOH HOH A . 
E 3 HOH 107 707 390 HOH HOH A . 
E 3 HOH 108 708 176 HOH HOH A . 
E 3 HOH 109 709 184 HOH HOH A . 
E 3 HOH 110 710 270 HOH HOH A . 
E 3 HOH 111 711 156 HOH HOH A . 
E 3 HOH 112 712 268 HOH HOH A . 
E 3 HOH 113 713 24  HOH HOH A . 
E 3 HOH 114 714 54  HOH HOH A . 
E 3 HOH 115 715 305 HOH HOH A . 
E 3 HOH 116 716 335 HOH HOH A . 
E 3 HOH 117 717 155 HOH HOH A . 
E 3 HOH 118 718 254 HOH HOH A . 
E 3 HOH 119 719 135 HOH HOH A . 
E 3 HOH 120 720 88  HOH HOH A . 
E 3 HOH 121 721 252 HOH HOH A . 
E 3 HOH 122 722 452 HOH HOH A . 
E 3 HOH 123 723 300 HOH HOH A . 
E 3 HOH 124 724 76  HOH HOH A . 
E 3 HOH 125 725 27  HOH HOH A . 
E 3 HOH 126 726 137 HOH HOH A . 
E 3 HOH 127 727 418 HOH HOH A . 
E 3 HOH 128 728 206 HOH HOH A . 
E 3 HOH 129 729 195 HOH HOH A . 
E 3 HOH 130 730 172 HOH HOH A . 
E 3 HOH 131 731 355 HOH HOH A . 
E 3 HOH 132 732 34  HOH HOH A . 
E 3 HOH 133 733 417 HOH HOH A . 
E 3 HOH 134 734 167 HOH HOH A . 
E 3 HOH 135 735 179 HOH HOH A . 
E 3 HOH 136 736 237 HOH HOH A . 
E 3 HOH 137 737 222 HOH HOH A . 
E 3 HOH 138 738 325 HOH HOH A . 
E 3 HOH 139 739 327 HOH HOH A . 
E 3 HOH 140 740 234 HOH HOH A . 
E 3 HOH 141 741 248 HOH HOH A . 
E 3 HOH 142 742 62  HOH HOH A . 
E 3 HOH 143 743 213 HOH HOH A . 
E 3 HOH 144 744 269 HOH HOH A . 
E 3 HOH 145 745 211 HOH HOH A . 
E 3 HOH 146 746 193 HOH HOH A . 
E 3 HOH 147 747 59  HOH HOH A . 
E 3 HOH 148 748 108 HOH HOH A . 
E 3 HOH 149 749 205 HOH HOH A . 
E 3 HOH 150 750 272 HOH HOH A . 
E 3 HOH 151 751 317 HOH HOH A . 
E 3 HOH 152 752 466 HOH HOH A . 
E 3 HOH 153 753 111 HOH HOH A . 
E 3 HOH 154 754 102 HOH HOH A . 
E 3 HOH 155 755 295 HOH HOH A . 
E 3 HOH 156 756 440 HOH HOH A . 
E 3 HOH 157 757 333 HOH HOH A . 
E 3 HOH 158 758 264 HOH HOH A . 
E 3 HOH 159 759 478 HOH HOH A . 
E 3 HOH 160 760 374 HOH HOH A . 
E 3 HOH 161 761 65  HOH HOH A . 
E 3 HOH 162 762 165 HOH HOH A . 
E 3 HOH 163 763 289 HOH HOH A . 
E 3 HOH 164 764 467 HOH HOH A . 
E 3 HOH 165 765 445 HOH HOH A . 
E 3 HOH 166 766 194 HOH HOH A . 
E 3 HOH 167 767 492 HOH HOH A . 
E 3 HOH 168 768 474 HOH HOH A . 
E 3 HOH 169 769 389 HOH HOH A . 
E 3 HOH 170 770 190 HOH HOH A . 
E 3 HOH 171 771 279 HOH HOH A . 
E 3 HOH 172 772 431 HOH HOH A . 
E 3 HOH 173 773 341 HOH HOH A . 
E 3 HOH 174 774 178 HOH HOH A . 
E 3 HOH 175 775 384 HOH HOH A . 
E 3 HOH 176 776 342 HOH HOH A . 
E 3 HOH 177 777 480 HOH HOH A . 
E 3 HOH 178 778 491 HOH HOH A . 
E 3 HOH 179 779 490 HOH HOH A . 
E 3 HOH 180 780 392 HOH HOH A . 
E 3 HOH 181 781 419 HOH HOH A . 
E 3 HOH 182 782 267 HOH HOH A . 
E 3 HOH 183 783 470 HOH HOH A . 
E 3 HOH 184 784 208 HOH HOH A . 
E 3 HOH 185 785 379 HOH HOH A . 
E 3 HOH 186 786 426 HOH HOH A . 
E 3 HOH 187 787 444 HOH HOH A . 
E 3 HOH 188 788 456 HOH HOH A . 
E 3 HOH 189 789 224 HOH HOH A . 
E 3 HOH 190 790 465 HOH HOH A . 
E 3 HOH 191 791 263 HOH HOH A . 
E 3 HOH 192 792 463 HOH HOH A . 
E 3 HOH 193 793 404 HOH HOH A . 
E 3 HOH 194 794 472 HOH HOH A . 
E 3 HOH 195 795 163 HOH HOH A . 
E 3 HOH 196 796 350 HOH HOH A . 
E 3 HOH 197 797 497 HOH HOH A . 
E 3 HOH 198 798 464 HOH HOH A . 
E 3 HOH 199 799 394 HOH HOH A . 
E 3 HOH 200 800 459 HOH HOH A . 
E 3 HOH 201 801 255 HOH HOH A . 
E 3 HOH 202 802 411 HOH HOH A . 
E 3 HOH 203 803 358 HOH HOH A . 
E 3 HOH 204 804 451 HOH HOH A . 
E 3 HOH 205 805 438 HOH HOH A . 
E 3 HOH 206 806 284 HOH HOH A . 
E 3 HOH 207 807 207 HOH HOH A . 
E 3 HOH 208 808 229 HOH HOH A . 
E 3 HOH 209 809 415 HOH HOH A . 
E 3 HOH 210 810 363 HOH HOH A . 
E 3 HOH 211 811 265 HOH HOH A . 
E 3 HOH 212 812 473 HOH HOH A . 
E 3 HOH 213 813 496 HOH HOH A . 
E 3 HOH 214 814 307 HOH HOH A . 
E 3 HOH 215 815 396 HOH HOH A . 
E 3 HOH 216 816 500 HOH HOH A . 
E 3 HOH 217 817 364 HOH HOH A . 
E 3 HOH 218 818 189 HOH HOH A . 
E 3 HOH 219 819 454 HOH HOH A . 
E 3 HOH 220 820 409 HOH HOH A . 
E 3 HOH 221 821 425 HOH HOH A . 
E 3 HOH 222 822 370 HOH HOH A . 
E 3 HOH 223 823 71  HOH HOH A . 
E 3 HOH 224 824 115 HOH HOH A . 
F 3 HOH 1   601 246 HOH HOH B . 
F 3 HOH 2   602 41  HOH HOH B . 
F 3 HOH 3   603 51  HOH HOH B . 
F 3 HOH 4   604 397 HOH HOH B . 
F 3 HOH 5   605 458 HOH HOH B . 
F 3 HOH 6   606 378 HOH HOH B . 
F 3 HOH 7   607 221 HOH HOH B . 
F 3 HOH 8   608 134 HOH HOH B . 
F 3 HOH 9   609 436 HOH HOH B . 
F 3 HOH 10  610 278 HOH HOH B . 
F 3 HOH 11  611 11  HOH HOH B . 
F 3 HOH 12  612 427 HOH HOH B . 
F 3 HOH 13  613 25  HOH HOH B . 
F 3 HOH 14  614 72  HOH HOH B . 
F 3 HOH 15  615 175 HOH HOH B . 
F 3 HOH 16  616 60  HOH HOH B . 
F 3 HOH 17  617 73  HOH HOH B . 
F 3 HOH 18  618 86  HOH HOH B . 
F 3 HOH 19  619 468 HOH HOH B . 
F 3 HOH 20  620 357 HOH HOH B . 
F 3 HOH 21  621 147 HOH HOH B . 
F 3 HOH 22  622 330 HOH HOH B . 
F 3 HOH 23  623 2   HOH HOH B . 
F 3 HOH 24  624 215 HOH HOH B . 
F 3 HOH 25  625 36  HOH HOH B . 
F 3 HOH 26  626 387 HOH HOH B . 
F 3 HOH 27  627 138 HOH HOH B . 
F 3 HOH 28  628 316 HOH HOH B . 
F 3 HOH 29  629 230 HOH HOH B . 
F 3 HOH 30  630 298 HOH HOH B . 
F 3 HOH 31  631 57  HOH HOH B . 
F 3 HOH 32  632 294 HOH HOH B . 
F 3 HOH 33  633 103 HOH HOH B . 
F 3 HOH 34  634 448 HOH HOH B . 
F 3 HOH 35  635 428 HOH HOH B . 
F 3 HOH 36  636 481 HOH HOH B . 
F 3 HOH 37  637 23  HOH HOH B . 
F 3 HOH 38  638 375 HOH HOH B . 
F 3 HOH 39  639 449 HOH HOH B . 
F 3 HOH 40  640 39  HOH HOH B . 
F 3 HOH 41  641 245 HOH HOH B . 
F 3 HOH 42  642 87  HOH HOH B . 
F 3 HOH 43  643 121 HOH HOH B . 
F 3 HOH 44  644 471 HOH HOH B . 
F 3 HOH 45  645 240 HOH HOH B . 
F 3 HOH 46  646 3   HOH HOH B . 
F 3 HOH 47  647 6   HOH HOH B . 
F 3 HOH 48  648 323 HOH HOH B . 
F 3 HOH 49  649 262 HOH HOH B . 
F 3 HOH 50  650 352 HOH HOH B . 
F 3 HOH 51  651 70  HOH HOH B . 
F 3 HOH 52  652 244 HOH HOH B . 
F 3 HOH 53  653 48  HOH HOH B . 
F 3 HOH 54  654 64  HOH HOH B . 
F 3 HOH 55  655 47  HOH HOH B . 
F 3 HOH 56  656 297 HOH HOH B . 
F 3 HOH 57  657 216 HOH HOH B . 
F 3 HOH 58  658 461 HOH HOH B . 
F 3 HOH 59  659 322 HOH HOH B . 
F 3 HOH 60  660 21  HOH HOH B . 
F 3 HOH 61  661 256 HOH HOH B . 
F 3 HOH 62  662 154 HOH HOH B . 
F 3 HOH 63  663 346 HOH HOH B . 
F 3 HOH 64  664 116 HOH HOH B . 
F 3 HOH 65  665 12  HOH HOH B . 
F 3 HOH 66  666 301 HOH HOH B . 
F 3 HOH 67  667 84  HOH HOH B . 
F 3 HOH 68  668 114 HOH HOH B . 
F 3 HOH 69  669 107 HOH HOH B . 
F 3 HOH 70  670 5   HOH HOH B . 
F 3 HOH 71  671 201 HOH HOH B . 
F 3 HOH 72  672 99  HOH HOH B . 
F 3 HOH 73  673 149 HOH HOH B . 
F 3 HOH 74  674 276 HOH HOH B . 
F 3 HOH 75  675 250 HOH HOH B . 
F 3 HOH 76  676 56  HOH HOH B . 
F 3 HOH 77  677 131 HOH HOH B . 
F 3 HOH 78  678 42  HOH HOH B . 
F 3 HOH 79  679 97  HOH HOH B . 
F 3 HOH 80  680 7   HOH HOH B . 
F 3 HOH 81  681 183 HOH HOH B . 
F 3 HOH 82  682 118 HOH HOH B . 
F 3 HOH 83  683 402 HOH HOH B . 
F 3 HOH 84  684 258 HOH HOH B . 
F 3 HOH 85  685 494 HOH HOH B . 
F 3 HOH 86  686 161 HOH HOH B . 
F 3 HOH 87  687 166 HOH HOH B . 
F 3 HOH 88  688 142 HOH HOH B . 
F 3 HOH 89  689 308 HOH HOH B . 
F 3 HOH 90  690 437 HOH HOH B . 
F 3 HOH 91  691 382 HOH HOH B . 
F 3 HOH 92  692 74  HOH HOH B . 
F 3 HOH 93  693 182 HOH HOH B . 
F 3 HOH 94  694 16  HOH HOH B . 
F 3 HOH 95  695 123 HOH HOH B . 
F 3 HOH 96  696 453 HOH HOH B . 
F 3 HOH 97  697 10  HOH HOH B . 
F 3 HOH 98  698 129 HOH HOH B . 
F 3 HOH 99  699 422 HOH HOH B . 
F 3 HOH 100 700 31  HOH HOH B . 
F 3 HOH 101 701 100 HOH HOH B . 
F 3 HOH 102 702 204 HOH HOH B . 
F 3 HOH 103 703 113 HOH HOH B . 
F 3 HOH 104 704 106 HOH HOH B . 
F 3 HOH 105 705 359 HOH HOH B . 
F 3 HOH 106 706 303 HOH HOH B . 
F 3 HOH 107 707 226 HOH HOH B . 
F 3 HOH 108 708 324 HOH HOH B . 
F 3 HOH 109 709 169 HOH HOH B . 
F 3 HOH 110 710 125 HOH HOH B . 
F 3 HOH 111 711 485 HOH HOH B . 
F 3 HOH 112 712 243 HOH HOH B . 
F 3 HOH 113 713 434 HOH HOH B . 
F 3 HOH 114 714 318 HOH HOH B . 
F 3 HOH 115 715 61  HOH HOH B . 
F 3 HOH 116 716 33  HOH HOH B . 
F 3 HOH 117 717 502 HOH HOH B . 
F 3 HOH 118 718 239 HOH HOH B . 
F 3 HOH 119 719 410 HOH HOH B . 
F 3 HOH 120 720 217 HOH HOH B . 
F 3 HOH 121 721 78  HOH HOH B . 
F 3 HOH 122 722 91  HOH HOH B . 
F 3 HOH 123 723 186 HOH HOH B . 
F 3 HOH 124 724 68  HOH HOH B . 
F 3 HOH 125 725 329 HOH HOH B . 
F 3 HOH 126 726 328 HOH HOH B . 
F 3 HOH 127 727 132 HOH HOH B . 
F 3 HOH 128 728 236 HOH HOH B . 
F 3 HOH 129 729 336 HOH HOH B . 
F 3 HOH 130 730 286 HOH HOH B . 
F 3 HOH 131 731 479 HOH HOH B . 
F 3 HOH 132 732 281 HOH HOH B . 
F 3 HOH 133 733 287 HOH HOH B . 
F 3 HOH 134 734 63  HOH HOH B . 
F 3 HOH 135 735 101 HOH HOH B . 
F 3 HOH 136 736 321 HOH HOH B . 
F 3 HOH 137 737 49  HOH HOH B . 
F 3 HOH 138 738 112 HOH HOH B . 
F 3 HOH 139 739 19  HOH HOH B . 
F 3 HOH 140 740 26  HOH HOH B . 
F 3 HOH 141 741 46  HOH HOH B . 
F 3 HOH 142 742 75  HOH HOH B . 
F 3 HOH 143 743 98  HOH HOH B . 
F 3 HOH 144 744 253 HOH HOH B . 
F 3 HOH 145 745 484 HOH HOH B . 
F 3 HOH 146 746 157 HOH HOH B . 
F 3 HOH 147 747 96  HOH HOH B . 
F 3 HOH 148 748 210 HOH HOH B . 
F 3 HOH 149 749 283 HOH HOH B . 
F 3 HOH 150 750 158 HOH HOH B . 
F 3 HOH 151 751 66  HOH HOH B . 
F 3 HOH 152 752 52  HOH HOH B . 
F 3 HOH 153 753 416 HOH HOH B . 
F 3 HOH 154 754 196 HOH HOH B . 
F 3 HOH 155 755 285 HOH HOH B . 
F 3 HOH 156 756 128 HOH HOH B . 
F 3 HOH 157 757 120 HOH HOH B . 
F 3 HOH 158 758 94  HOH HOH B . 
F 3 HOH 159 759 110 HOH HOH B . 
F 3 HOH 160 760 423 HOH HOH B . 
F 3 HOH 161 761 347 HOH HOH B . 
F 3 HOH 162 762 144 HOH HOH B . 
F 3 HOH 163 763 83  HOH HOH B . 
F 3 HOH 164 764 257 HOH HOH B . 
F 3 HOH 165 765 9   HOH HOH B . 
F 3 HOH 166 766 69  HOH HOH B . 
F 3 HOH 167 767 242 HOH HOH B . 
F 3 HOH 168 768 429 HOH HOH B . 
F 3 HOH 169 769 173 HOH HOH B . 
F 3 HOH 170 770 296 HOH HOH B . 
F 3 HOH 171 771 188 HOH HOH B . 
F 3 HOH 172 772 119 HOH HOH B . 
F 3 HOH 173 773 369 HOH HOH B . 
F 3 HOH 174 774 311 HOH HOH B . 
F 3 HOH 175 775 443 HOH HOH B . 
F 3 HOH 176 776 377 HOH HOH B . 
F 3 HOH 177 777 105 HOH HOH B . 
F 3 HOH 178 778 202 HOH HOH B . 
F 3 HOH 179 779 314 HOH HOH B . 
F 3 HOH 180 780 309 HOH HOH B . 
F 3 HOH 181 781 277 HOH HOH B . 
F 3 HOH 182 782 319 HOH HOH B . 
F 3 HOH 183 783 249 HOH HOH B . 
F 3 HOH 184 784 251 HOH HOH B . 
F 3 HOH 185 785 219 HOH HOH B . 
F 3 HOH 186 786 432 HOH HOH B . 
F 3 HOH 187 787 337 HOH HOH B . 
F 3 HOH 188 788 430 HOH HOH B . 
F 3 HOH 189 789 93  HOH HOH B . 
F 3 HOH 190 790 288 HOH HOH B . 
F 3 HOH 191 791 292 HOH HOH B . 
F 3 HOH 192 792 469 HOH HOH B . 
F 3 HOH 193 793 400 HOH HOH B . 
F 3 HOH 194 794 475 HOH HOH B . 
F 3 HOH 195 795 164 HOH HOH B . 
F 3 HOH 196 796 312 HOH HOH B . 
F 3 HOH 197 797 489 HOH HOH B . 
F 3 HOH 198 798 339 HOH HOH B . 
F 3 HOH 199 799 486 HOH HOH B . 
F 3 HOH 200 800 380 HOH HOH B . 
F 3 HOH 201 801 299 HOH HOH B . 
F 3 HOH 202 802 232 HOH HOH B . 
F 3 HOH 203 803 130 HOH HOH B . 
F 3 HOH 204 804 225 HOH HOH B . 
F 3 HOH 205 805 401 HOH HOH B . 
F 3 HOH 206 806 338 HOH HOH B . 
F 3 HOH 207 807 275 HOH HOH B . 
F 3 HOH 208 808 420 HOH HOH B . 
F 3 HOH 209 809 381 HOH HOH B . 
F 3 HOH 210 810 483 HOH HOH B . 
F 3 HOH 211 811 435 HOH HOH B . 
F 3 HOH 212 812 493 HOH HOH B . 
F 3 HOH 213 813 408 HOH HOH B . 
F 3 HOH 214 814 274 HOH HOH B . 
F 3 HOH 215 815 334 HOH HOH B . 
F 3 HOH 216 816 351 HOH HOH B . 
F 3 HOH 217 817 406 HOH HOH B . 
F 3 HOH 218 818 332 HOH HOH B . 
F 3 HOH 219 819 117 HOH HOH B . 
F 3 HOH 220 820 405 HOH HOH B . 
F 3 HOH 221 821 306 HOH HOH B . 
F 3 HOH 222 822 162 HOH HOH B . 
F 3 HOH 223 823 271 HOH HOH B . 
F 3 HOH 224 824 340 HOH HOH B . 
F 3 HOH 225 825 383 HOH HOH B . 
F 3 HOH 226 826 122 HOH HOH B . 
F 3 HOH 227 827 345 HOH HOH B . 
F 3 HOH 228 828 127 HOH HOH B . 
F 3 HOH 229 829 320 HOH HOH B . 
F 3 HOH 230 830 450 HOH HOH B . 
F 3 HOH 231 831 139 HOH HOH B . 
F 3 HOH 232 832 223 HOH HOH B . 
F 3 HOH 233 833 191 HOH HOH B . 
F 3 HOH 234 834 220 HOH HOH B . 
F 3 HOH 235 835 197 HOH HOH B . 
F 3 HOH 236 836 393 HOH HOH B . 
F 3 HOH 237 837 235 HOH HOH B . 
F 3 HOH 238 838 412 HOH HOH B . 
F 3 HOH 239 839 477 HOH HOH B . 
F 3 HOH 240 840 498 HOH HOH B . 
F 3 HOH 241 841 261 HOH HOH B . 
F 3 HOH 242 842 181 HOH HOH B . 
F 3 HOH 243 843 376 HOH HOH B . 
F 3 HOH 244 844 499 HOH HOH B . 
F 3 HOH 245 845 302 HOH HOH B . 
F 3 HOH 246 846 399 HOH HOH B . 
F 3 HOH 247 847 212 HOH HOH B . 
F 3 HOH 248 848 476 HOH HOH B . 
F 3 HOH 249 849 433 HOH HOH B . 
F 3 HOH 250 850 407 HOH HOH B . 
F 3 HOH 251 851 227 HOH HOH B . 
F 3 HOH 252 852 133 HOH HOH B . 
F 3 HOH 253 853 372 HOH HOH B . 
F 3 HOH 254 854 501 HOH HOH B . 
F 3 HOH 255 855 455 HOH HOH B . 
F 3 HOH 256 856 349 HOH HOH B . 
F 3 HOH 257 857 457 HOH HOH B . 
F 3 HOH 258 858 241 HOH HOH B . 
F 3 HOH 259 859 353 HOH HOH B . 
F 3 HOH 260 860 238 HOH HOH B . 
F 3 HOH 261 861 373 HOH HOH B . 
F 3 HOH 262 862 488 HOH HOH B . 
F 3 HOH 263 863 290 HOH HOH B . 
F 3 HOH 264 864 398 HOH HOH B . 
F 3 HOH 265 865 503 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 A PLP 501 ? O4A ? C PLP 1 O4A 
2 1 N 1 B PLP 501 ? O4A ? D PLP 1 O4A 
# 
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      ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   110.320 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IQH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     130.732 
_cell.length_a_esd                 ? 
_cell.length_b                     82.799 
_cell.length_b_esd                 ? 
_cell.length_c                     77.496 
_cell.length_c_esd                 ? 
_cell.volume                       786650.074 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9IQH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IQH 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.38 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% (w/v) polyethylene glycol 3350 and 200 mM magnesium sulfate heptahydrate at pH 5.9' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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                         'RIGAKU HyPix-6000HE' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-01-04 
_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   1.5405 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        RIGAKU 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5405 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          23.74 
_reflns.entry_id                                       9IQH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.27 
_reflns.d_resolution_low                               23.14 
_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                                     34171 
_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                           95.10 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.80 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.27 
_reflns_shell.d_res_low                                     2.351 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2285 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.967 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_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                               26.44 
_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                                 9IQH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.27 
_refine.ls_d_res_low                             23.14 
_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                     34094 
_refine.ls_number_reflns_R_free                  1734 
_refine.ls_number_reflns_R_work                  32360 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.97 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1650 
_refine.ls_R_factor_R_free                       0.2148 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1623 
_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                          1.34 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 22.8564 
_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                            0.2492 
_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                       2.27 
_refine_hist.d_res_low                        23.14 
_refine_hist.number_atoms_solvent             489 
_refine_hist.number_atoms_total               6508 
_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        5989 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_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' ? 0.0039  ? 6216 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6731  ? 8469 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0439  ? 951  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0069  ? 1120 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.9918 ? 2243 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.27 2.34  . . 92  1942 68.30 . . . . 0.1964 . . . . . . . . . . . 0.2749 
'X-RAY DIFFRACTION' 2.34 2.41  . . 140 2278 81.28 . . . . 0.1902 . . . . . . . . . . . 0.2763 
'X-RAY DIFFRACTION' 2.41 2.50  . . 139 2642 93.23 . . . . 0.2005 . . . . . . . . . . . 0.3460 
'X-RAY DIFFRACTION' 2.50 2.60  . . 122 2813 99.22 . . . . 0.1834 . . . . . . . . . . . 0.2685 
'X-RAY DIFFRACTION' 2.60 2.72  . . 151 2804 99.56 . . . . 0.1839 . . . . . . . . . . . 0.2282 
'X-RAY DIFFRACTION' 2.72 2.86  . . 172 2829 99.54 . . . . 0.1962 . . . . . . . . . . . 0.2842 
'X-RAY DIFFRACTION' 2.86 3.04  . . 143 2801 99.83 . . . . 0.1815 . . . . . . . . . . . 0.2254 
'X-RAY DIFFRACTION' 3.04 3.27  . . 157 2835 99.80 . . . . 0.1805 . . . . . . . . . . . 0.2493 
'X-RAY DIFFRACTION' 3.27 3.60  . . 142 2826 99.46 . . . . 0.1619 . . . . . . . . . . . 0.2198 
'X-RAY DIFFRACTION' 3.60 4.12  . . 161 2839 99.73 . . . . 0.1440 . . . . . . . . . . . 0.1890 
'X-RAY DIFFRACTION' 4.12 5.18  . . 152 2872 99.70 . . . . 0.1244 . . . . . . . . . . . 0.1565 
'X-RAY DIFFRACTION' 5.18 23.14 . . 163 2879 99.77 . . . . 0.1400 . . . . . . . . . . . 0.1512 
# 
_struct.entry_id                     9IQH 
_struct.title                        'Crystal structure of sulfhydrylase' 
_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        9IQH 
_struct_keywords.text            
'Biosynthesis, CdS quantum dots, SQR enzyme, Extracellular polyphosphate, Cadmium waste recycle, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A2W1K030_ACIFR 
_struct_ref.pdbx_db_accession          A0A2W1K030 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MNTKNTNPDWADRLRPETIAIRAGIHRTQEQEHSEAIFPTSSFVFDSAEEAADRFAGRVPGNIYARFTNPTVRTFEERLA
ALEGAEACVATASGMAACLTAFMGILKAGDHVVASRSIFGTTVQLLGNILSRFGVETSFVPLADVPAWRAALRPNTRMLF
LETPSNPLTEIGDMQALADLAHVHDAWLVVDNCFCTPALQQPLKFGADLVIHSATKYLDGQGRTLGGAVCGSTELLNSGP
RNFVRTAGPSLSPFNAWVQLKGLETLGLRMERHCANAQKIAEWLEARPEVARVYYPGLDSHPQQALAARQQRLPGAILSF
DLHGGQKAAWAFVDALRLLSLTANLGDAKTTITHPASTTHSRVSPEARAAAGVGDGLLRISVGLEHADDLREDMERGFAA
LVAR
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9IQH A 1 ? 404 ? A0A2W1K030 1 ? 404 ? 1 404 
2 1 9IQH B 1 ? 404 ? A0A2W1K030 1 ? 404 ? 1 404 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6440  ? 
1 MORE         -39   ? 
1 'SSA (A^2)'  29140 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 9   ? LEU A 14  ? ASP A 9   LEU A 14  5 ? 6  
HELX_P HELX_P2  AA2 ARG A 15  ? ALA A 23  ? ARG A 15  ALA A 23  1 ? 9  
HELX_P HELX_P3  AA3 SER A 47  ? ALA A 56  ? SER A 47  ALA A 56  1 ? 10 
HELX_P HELX_P4  AA4 ASN A 69  ? GLY A 84  ? ASN A 69  GLY A 84  1 ? 16 
HELX_P HELX_P5  AA5 SER A 93  ? LEU A 106 ? SER A 93  LEU A 106 1 ? 14 
HELX_P HELX_P6  AA6 PHE A 119 ? ILE A 129 ? PHE A 119 ILE A 129 1 ? 11 
HELX_P HELX_P7  AA7 LEU A 130 ? GLY A 134 ? LEU A 130 GLY A 134 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 144 ? LEU A 152 ? ASP A 144 LEU A 152 1 ? 9  
HELX_P HELX_P9  AA9 ASP A 173 ? HIS A 184 ? ASP A 173 HIS A 184 1 ? 12 
HELX_P HELX_P10 AB1 GLN A 201 ? GLY A 206 ? GLN A 201 GLY A 206 5 ? 6  
HELX_P HELX_P11 AB2 SER A 232 ? ASN A 237 ? SER A 232 ASN A 237 1 ? 6  
HELX_P HELX_P12 AB3 GLY A 239 ? GLY A 248 ? GLY A 239 GLY A 248 1 ? 10 
HELX_P HELX_P13 AB4 SER A 252 ? GLU A 264 ? SER A 252 GLU A 264 1 ? 13 
HELX_P HELX_P14 AB5 THR A 265 ? ALA A 286 ? THR A 265 ALA A 286 1 ? 22 
HELX_P HELX_P15 AB6 GLN A 303 ? GLN A 311 ? GLN A 303 GLN A 311 1 ? 9  
HELX_P HELX_P16 AB7 GLY A 324 ? ALA A 335 ? GLY A 324 ALA A 335 1 ? 12 
HELX_P HELX_P17 AB8 SER A 364 ? GLY A 372 ? SER A 364 GLY A 372 1 ? 9  
HELX_P HELX_P18 AB9 HIS A 386 ? ALA A 400 ? HIS A 386 ALA A 400 1 ? 15 
HELX_P HELX_P19 AC1 LEU A 401 ? VAL A 402 ? LEU A 401 VAL A 402 5 ? 2  
HELX_P HELX_P20 AC2 ASP B 9   ? LEU B 14  ? ASP B 9   LEU B 14  5 ? 6  
HELX_P HELX_P21 AC3 ARG B 15  ? ALA B 23  ? ARG B 15  ALA B 23  1 ? 9  
HELX_P HELX_P22 AC4 SER B 47  ? GLY B 57  ? SER B 47  GLY B 57  1 ? 11 
HELX_P HELX_P23 AC5 ASN B 69  ? GLY B 84  ? ASN B 69  GLY B 84  1 ? 16 
HELX_P HELX_P24 AC6 SER B 93  ? LEU B 106 ? SER B 93  LEU B 106 1 ? 14 
HELX_P HELX_P25 AC7 PHE B 119 ? ASN B 128 ? PHE B 119 ASN B 128 1 ? 10 
HELX_P HELX_P26 AC8 ILE B 129 ? GLY B 134 ? ILE B 129 GLY B 134 5 ? 6  
HELX_P HELX_P27 AC9 ASP B 144 ? LEU B 152 ? ASP B 144 LEU B 152 1 ? 9  
HELX_P HELX_P28 AD1 ASP B 173 ? HIS B 184 ? ASP B 173 HIS B 184 1 ? 12 
HELX_P HELX_P29 AD2 GLN B 201 ? GLY B 206 ? GLN B 201 GLY B 206 5 ? 6  
HELX_P HELX_P30 AD3 SER B 232 ? ASN B 237 ? SER B 232 ASN B 237 1 ? 6  
HELX_P HELX_P31 AD4 GLY B 239 ? GLY B 248 ? GLY B 239 GLY B 248 1 ? 10 
HELX_P HELX_P32 AD5 SER B 252 ? GLU B 264 ? SER B 252 GLU B 264 1 ? 13 
HELX_P HELX_P33 AD6 THR B 265 ? ALA B 286 ? THR B 265 ALA B 286 1 ? 22 
HELX_P HELX_P34 AD7 GLN B 303 ? GLN B 311 ? GLN B 303 GLN B 311 1 ? 9  
HELX_P HELX_P35 AD8 GLY B 325 ? ALA B 335 ? GLY B 325 ALA B 335 1 ? 11 
HELX_P HELX_P36 AD9 SER B 364 ? GLY B 372 ? SER B 364 GLY B 372 1 ? 9  
HELX_P HELX_P37 AE1 HIS B 386 ? ALA B 400 ? HIS B 386 ALA B 400 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 THR 163 A . ? THR 163 A PRO 164 A ? PRO 164 A 1 -3.91 
2 ASN 166 A . ? ASN 166 A PRO 167 A ? PRO 167 A 1 0.06  
3 THR 163 B . ? THR 163 B PRO 164 B ? PRO 164 B 1 -7.86 
4 ASN 166 B . ? ASN 166 B PRO 167 B ? PRO 167 B 1 1.02  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 7 ? 
AA4 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? 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 87  ? THR A 91  ? ALA A 87  THR A 91  
AA1 2 GLY A 227 ? GLY A 231 ? GLY A 227 GLY A 231 
AA1 3 LEU A 209 ? SER A 213 ? LEU A 209 SER A 213 
AA1 4 TRP A 187 ? ASP A 191 ? TRP A 187 ASP A 191 
AA1 5 THR A 156 ? GLU A 162 ? THR A 156 GLU A 162 
AA1 6 HIS A 111 ? SER A 115 ? HIS A 111 SER A 115 
AA1 7 GLU A 136 ? VAL A 140 ? GLU A 136 VAL A 140 
AA2 1 VAL A 290 ? TYR A 294 ? VAL A 290 TYR A 294 
AA2 2 ILE A 317 ? LEU A 322 ? ILE A 317 LEU A 322 
AA2 3 LEU A 377 ? SER A 381 ? LEU A 377 SER A 381 
AA2 4 THR A 351 ? THR A 353 ? THR A 351 THR A 353 
AA2 5 SER A 340 ? LEU A 341 ? SER A 340 LEU A 341 
AA3 1 ALA B 87  ? THR B 91  ? ALA B 87  THR B 91  
AA3 2 GLY B 227 ? GLY B 231 ? GLY B 227 GLY B 231 
AA3 3 LEU B 209 ? SER B 213 ? LEU B 209 SER B 213 
AA3 4 TRP B 187 ? ASP B 191 ? TRP B 187 ASP B 191 
AA3 5 THR B 156 ? GLU B 162 ? THR B 156 GLU B 162 
AA3 6 HIS B 111 ? SER B 115 ? HIS B 111 SER B 115 
AA3 7 GLU B 136 ? VAL B 140 ? GLU B 136 VAL B 140 
AA4 1 VAL B 290 ? TYR B 294 ? VAL B 290 TYR B 294 
AA4 2 ILE B 317 ? LEU B 322 ? ILE B 317 LEU B 322 
AA4 3 LEU B 377 ? SER B 381 ? LEU B 377 SER B 381 
AA4 4 THR B 351 ? THR B 353 ? THR B 351 THR B 353 
AA4 5 SER B 340 ? LEU B 341 ? SER B 340 LEU B 341 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N THR A 91  ? N THR A 91  O GLY A 227 ? O GLY A 227 
AA1 2 3 O CYS A 230 ? O CYS A 230 N VAL A 210 ? N VAL A 210 
AA1 3 4 O ILE A 211 ? O ILE A 211 N VAL A 190 ? N VAL A 190 
AA1 4 5 O VAL A 189 ? O VAL A 189 N LEU A 159 ? N LEU A 159 
AA1 5 6 O PHE A 160 ? O PHE A 160 N VAL A 113 ? N VAL A 113 
AA1 6 7 N VAL A 112 ? N VAL A 112 O SER A 138 ? O SER A 138 
AA2 1 2 N TYR A 294 ? N TYR A 294 O SER A 319 ? O SER A 319 
AA2 2 3 N LEU A 318 ? N LEU A 318 O ILE A 380 ? O ILE A 380 
AA2 3 4 O ARG A 379 ? O ARG A 379 N THR A 353 ? N THR A 353 
AA2 4 5 O ILE A 352 ? O ILE A 352 N SER A 340 ? N SER A 340 
AA3 1 2 N THR B 91  ? N THR B 91  O GLY B 227 ? O GLY B 227 
AA3 2 3 O CYS B 230 ? O CYS B 230 N VAL B 210 ? N VAL B 210 
AA3 3 4 O ILE B 211 ? O ILE B 211 N VAL B 190 ? N VAL B 190 
AA3 4 5 O VAL B 189 ? O VAL B 189 N LEU B 159 ? N LEU B 159 
AA3 5 6 O PHE B 160 ? O PHE B 160 N VAL B 113 ? N VAL B 113 
AA3 6 7 N ALA B 114 ? N ALA B 114 O SER B 138 ? O SER B 138 
AA4 1 2 N TYR B 294 ? N TYR B 294 O SER B 319 ? O SER B 319 
AA4 2 3 N LEU B 318 ? N LEU B 318 O ILE B 380 ? O ILE B 380 
AA4 3 4 O ARG B 379 ? O ARG B 379 N THR B 353 ? N THR B 353 
AA4 4 5 O ILE B 352 ? O ILE B 352 N SER B 340 ? N SER B 340 
# 
_pdbx_entry_details.entry_id                   9IQH 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 NZ B LYS 216 ? ? C4A B PLP 501 ? ? 1.29 
2 1 NZ A LYS 216 ? ? C4A A PLP 501 ? ? 1.39 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ILE A 63  ? ? -123.29 -56.69 
2  1 PHE A 119 ? ? -39.33  128.98 
3  1 THR A 196 ? ? 66.39   161.69 
4  1 LYS A 216 ? ? -85.98  -79.64 
5  1 GLN A 221 ? ? -140.54 18.82  
6  1 ILE B 63  ? ? -121.02 -59.63 
7  1 PHE B 119 ? ? -37.98  129.23 
8  1 ILE B 129 ? ? -91.44  -62.15 
9  1 THR B 196 ? ? 68.93   165.13 
10 1 LYS B 216 ? ? -92.18  -80.79 
11 1 THR B 358 ? ? -119.78 -72.92 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 673 ? E HOH . 
2 1 B HOH 663 ? F HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,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                       824 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.84 
_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 MET 1   ? A MET 1   
2  1 Y 1 A ASN 2   ? A ASN 2   
3  1 Y 1 A THR 3   ? A THR 3   
4  1 Y 1 A LYS 4   ? A LYS 4   
5  1 Y 1 A ASN 5   ? A ASN 5   
6  1 Y 1 A THR 6   ? A THR 6   
7  1 Y 1 A ASN 7   ? A ASN 7   
8  1 Y 1 A PRO 8   ? A PRO 8   
9  1 Y 1 A ALA 403 ? A ALA 403 
10 1 Y 1 A ARG 404 ? A ARG 404 
11 1 Y 1 B MET 1   ? B MET 1   
12 1 Y 1 B ASN 2   ? B ASN 2   
13 1 Y 1 B THR 3   ? B THR 3   
14 1 Y 1 B LYS 4   ? B LYS 4   
15 1 Y 1 B ASN 5   ? B ASN 5   
16 1 Y 1 B THR 6   ? B THR 6   
17 1 Y 1 B ASN 7   ? B ASN 7   
18 1 Y 1 B PRO 8   ? B PRO 8   
19 1 Y 1 B ARG 404 ? B ARG 404 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PLP N1   N Y N 273 
PLP C2   C Y N 274 
PLP C2A  C N N 275 
PLP C3   C Y N 276 
PLP O3   O N N 277 
PLP C4   C Y N 278 
PLP C4A  C N N 279 
PLP O4A  O N N 280 
PLP C5   C Y N 281 
PLP C6   C Y N 282 
PLP C5A  C N N 283 
PLP O4P  O N N 284 
PLP P    P N N 285 
PLP O1P  O N N 286 
PLP O2P  O N N 287 
PLP O3P  O N N 288 
PLP H2A1 H N N 289 
PLP H2A2 H N N 290 
PLP H2A3 H N N 291 
PLP HO3  H N N 292 
PLP H4A  H N N 293 
PLP H6   H N N 294 
PLP H5A1 H N N 295 
PLP H5A2 H N N 296 
PLP HOP2 H N N 297 
PLP HOP3 H N N 298 
PRO N    N N N 299 
PRO CA   C N S 300 
PRO C    C N N 301 
PRO O    O N N 302 
PRO CB   C N N 303 
PRO CG   C N N 304 
PRO CD   C N N 305 
PRO OXT  O N N 306 
PRO H    H N N 307 
PRO HA   H N N 308 
PRO HB2  H N N 309 
PRO HB3  H N N 310 
PRO HG2  H N N 311 
PRO HG3  H N N 312 
PRO HD2  H N N 313 
PRO HD3  H N N 314 
PRO HXT  H N N 315 
SER N    N N N 316 
SER CA   C N S 317 
SER C    C N N 318 
SER O    O N N 319 
SER CB   C N N 320 
SER OG   O N N 321 
SER OXT  O N N 322 
SER H    H N N 323 
SER H2   H N N 324 
SER HA   H N N 325 
SER HB2  H N N 326 
SER HB3  H N N 327 
SER HG   H N N 328 
SER HXT  H N N 329 
THR N    N N N 330 
THR CA   C N S 331 
THR C    C N N 332 
THR O    O N N 333 
THR CB   C N R 334 
THR OG1  O N N 335 
THR CG2  C N N 336 
THR OXT  O N N 337 
THR H    H N N 338 
THR H2   H N N 339 
THR HA   H N N 340 
THR HB   H N N 341 
THR HG1  H N N 342 
THR HG21 H N N 343 
THR HG22 H N N 344 
THR HG23 H N N 345 
THR HXT  H N N 346 
TRP N    N N N 347 
TRP CA   C N S 348 
TRP C    C N N 349 
TRP O    O N N 350 
TRP CB   C N N 351 
TRP CG   C Y N 352 
TRP CD1  C Y N 353 
TRP CD2  C Y N 354 
TRP NE1  N Y N 355 
TRP CE2  C Y N 356 
TRP CE3  C Y N 357 
TRP CZ2  C Y N 358 
TRP CZ3  C Y N 359 
TRP CH2  C Y N 360 
TRP OXT  O N N 361 
TRP H    H N N 362 
TRP H2   H N N 363 
TRP HA   H N N 364 
TRP HB2  H N N 365 
TRP HB3  H N N 366 
TRP HD1  H N N 367 
TRP HE1  H N N 368 
TRP HE3  H N N 369 
TRP HZ2  H N N 370 
TRP HZ3  H N N 371 
TRP HH2  H N N 372 
TRP HXT  H N N 373 
TYR N    N N N 374 
TYR CA   C N S 375 
TYR C    C N N 376 
TYR O    O N N 377 
TYR CB   C N N 378 
TYR CG   C Y N 379 
TYR CD1  C Y N 380 
TYR CD2  C Y N 381 
TYR CE1  C Y N 382 
TYR CE2  C Y N 383 
TYR CZ   C Y N 384 
TYR OH   O N N 385 
TYR OXT  O N N 386 
TYR H    H N N 387 
TYR H2   H N N 388 
TYR HA   H N N 389 
TYR HB2  H N N 390 
TYR HB3  H N N 391 
TYR HD1  H N N 392 
TYR HD2  H N N 393 
TYR HE1  H N N 394 
TYR HE2  H N N 395 
TYR HH   H N N 396 
TYR HXT  H N N 397 
VAL N    N N N 398 
VAL CA   C N S 399 
VAL C    C N N 400 
VAL O    O N N 401 
VAL CB   C N N 402 
VAL CG1  C N N 403 
VAL CG2  C N N 404 
VAL OXT  O N N 405 
VAL H    H N N 406 
VAL H2   H N N 407 
VAL HA   H N N 408 
VAL HB   H N N 409 
VAL HG11 H N N 410 
VAL HG12 H N N 411 
VAL HG13 H N N 412 
VAL HG21 H N N 413 
VAL HG22 H N N 414 
VAL HG23 H N N 415 
VAL HXT  H N N 416 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PLP N1  C2   doub Y N 260 
PLP N1  C6   sing Y N 261 
PLP C2  C2A  sing N N 262 
PLP C2  C3   sing Y N 263 
PLP C2A H2A1 sing N N 264 
PLP C2A H2A2 sing N N 265 
PLP C2A H2A3 sing N N 266 
PLP C3  O3   sing N N 267 
PLP C3  C4   doub Y N 268 
PLP O3  HO3  sing N N 269 
PLP C4  C4A  sing N N 270 
PLP C4  C5   sing Y N 271 
PLP C4A O4A  doub N N 272 
PLP C4A H4A  sing N N 273 
PLP C5  C6   doub Y N 274 
PLP C5  C5A  sing N N 275 
PLP C6  H6   sing N N 276 
PLP C5A O4P  sing N N 277 
PLP C5A H5A1 sing N N 278 
PLP C5A H5A2 sing N N 279 
PLP O4P P    sing N N 280 
PLP P   O1P  doub N N 281 
PLP P   O2P  sing N N 282 
PLP P   O3P  sing N N 283 
PLP O2P HOP2 sing N N 284 
PLP O3P HOP3 sing N N 285 
PRO N   CA   sing N N 286 
PRO N   CD   sing N N 287 
PRO N   H    sing N N 288 
PRO CA  C    sing N N 289 
PRO CA  CB   sing N N 290 
PRO CA  HA   sing N N 291 
PRO C   O    doub N N 292 
PRO C   OXT  sing N N 293 
PRO CB  CG   sing N N 294 
PRO CB  HB2  sing N N 295 
PRO CB  HB3  sing N N 296 
PRO CG  CD   sing N N 297 
PRO CG  HG2  sing N N 298 
PRO CG  HG3  sing N N 299 
PRO CD  HD2  sing N N 300 
PRO CD  HD3  sing N N 301 
PRO OXT HXT  sing N N 302 
SER N   CA   sing N N 303 
SER N   H    sing N N 304 
SER N   H2   sing N N 305 
SER CA  C    sing N N 306 
SER CA  CB   sing N N 307 
SER CA  HA   sing N N 308 
SER C   O    doub N N 309 
SER C   OXT  sing N N 310 
SER CB  OG   sing N N 311 
SER CB  HB2  sing N N 312 
SER CB  HB3  sing N N 313 
SER OG  HG   sing N N 314 
SER OXT HXT  sing N N 315 
THR N   CA   sing N N 316 
THR N   H    sing N N 317 
THR N   H2   sing N N 318 
THR CA  C    sing N N 319 
THR CA  CB   sing N N 320 
THR CA  HA   sing N N 321 
THR C   O    doub N N 322 
THR C   OXT  sing N N 323 
THR CB  OG1  sing N N 324 
THR CB  CG2  sing N N 325 
THR CB  HB   sing N N 326 
THR OG1 HG1  sing N N 327 
THR CG2 HG21 sing N N 328 
THR CG2 HG22 sing N N 329 
THR CG2 HG23 sing N N 330 
THR OXT HXT  sing N N 331 
TRP N   CA   sing N N 332 
TRP N   H    sing N N 333 
TRP N   H2   sing N N 334 
TRP CA  C    sing N N 335 
TRP CA  CB   sing N N 336 
TRP CA  HA   sing N N 337 
TRP C   O    doub N N 338 
TRP C   OXT  sing N N 339 
TRP CB  CG   sing N N 340 
TRP CB  HB2  sing N N 341 
TRP CB  HB3  sing N N 342 
TRP CG  CD1  doub Y N 343 
TRP CG  CD2  sing Y N 344 
TRP CD1 NE1  sing Y N 345 
TRP CD1 HD1  sing N N 346 
TRP CD2 CE2  doub Y N 347 
TRP CD2 CE3  sing Y N 348 
TRP NE1 CE2  sing Y N 349 
TRP NE1 HE1  sing N N 350 
TRP CE2 CZ2  sing Y N 351 
TRP CE3 CZ3  doub Y N 352 
TRP CE3 HE3  sing N N 353 
TRP CZ2 CH2  doub Y N 354 
TRP CZ2 HZ2  sing N N 355 
TRP CZ3 CH2  sing Y N 356 
TRP CZ3 HZ3  sing N N 357 
TRP CH2 HH2  sing N N 358 
TRP OXT HXT  sing N N 359 
TYR N   CA   sing N N 360 
TYR N   H    sing N N 361 
TYR N   H2   sing N N 362 
TYR CA  C    sing N N 363 
TYR CA  CB   sing N N 364 
TYR CA  HA   sing N N 365 
TYR C   O    doub N N 366 
TYR C   OXT  sing N N 367 
TYR CB  CG   sing N N 368 
TYR CB  HB2  sing N N 369 
TYR CB  HB3  sing N N 370 
TYR CG  CD1  doub Y N 371 
TYR CG  CD2  sing Y N 372 
TYR CD1 CE1  sing Y N 373 
TYR CD1 HD1  sing N N 374 
TYR CD2 CE2  doub Y N 375 
TYR CD2 HD2  sing N N 376 
TYR CE1 CZ   doub Y N 377 
TYR CE1 HE1  sing N N 378 
TYR CE2 CZ   sing Y N 379 
TYR CE2 HE2  sing N N 380 
TYR CZ  OH   sing N N 381 
TYR OH  HH   sing N N 382 
TYR OXT HXT  sing N N 383 
VAL N   CA   sing N N 384 
VAL N   H    sing N N 385 
VAL N   H2   sing N N 386 
VAL CA  C    sing N N 387 
VAL CA  CB   sing N N 388 
VAL CA  HA   sing N N 389 
VAL C   O    doub N N 390 
VAL C   OXT  sing N N 391 
VAL CB  CG1  sing N N 392 
VAL CB  CG2  sing N N 393 
VAL CB  HB   sing N N 394 
VAL CG1 HG11 sing N N 395 
VAL CG1 HG12 sing N N 396 
VAL CG1 HG13 sing N N 397 
VAL CG2 HG21 sing N N 398 
VAL CG2 HG22 sing N N 399 
VAL CG2 HG23 sing N N 400 
VAL OXT HXT  sing N N 401 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32271525 
_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   3NDN 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9IQH 
_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]   0.007649 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002833 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012077 
_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]   0.013760 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ASP A 1 9   ? 23.36300  0.56400   89.99900  1.000 69.07418 ? 9   ASP A N   1 
ATOM   2    C CA  . ASP A 1 9   ? 23.97200  0.02100   91.20600  1.000 62.16661 ? 9   ASP A CA  1 
ATOM   3    C C   . ASP A 1 9   ? 24.29700  1.15200   92.18600  1.000 64.22152 ? 9   ASP A C   1 
ATOM   4    O O   . ASP A 1 9   ? 23.40000  1.83400   92.68600  1.000 59.28616 ? 9   ASP A O   1 
ATOM   5    C CB  . ASP A 1 9   ? 25.23600  -0.78000  90.85300  1.000 64.01961 ? 9   ASP A CB  1 
ATOM   6    C CG  . ASP A 1 9   ? 25.59300  -1.83200  91.90700  1.000 67.53615 ? 9   ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 9   ? 25.48300  -1.54700  93.12000  1.000 65.25602 ? 9   ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 9   ? 25.99200  -2.95000  91.51700  1.000 63.05295 ? 9   ASP A OD2 1 
ATOM   9    N N   . TRP A 1 10  ? 25.59500  1.35800   92.42500  1.000 62.52294 ? 10  TRP A N   1 
ATOM   10   C CA  . TRP A 1 10  ? 26.04400  2.26800   93.47700  1.000 58.20815 ? 10  TRP A CA  1 
ATOM   11   C C   . TRP A 1 10  ? 25.77700  3.73100   93.14100  1.000 54.32817 ? 10  TRP A C   1 
ATOM   12   O O   . TRP A 1 10  ? 25.55500  4.54000   94.05000  1.000 48.15632 ? 10  TRP A O   1 
ATOM   13   C CB  . TRP A 1 10  ? 27.53600  2.05900   93.72900  1.000 54.77558 ? 10  TRP A CB  1 
ATOM   14   C CG  . TRP A 1 10  ? 28.37300  2.34600   92.52000  1.000 51.80840 ? 10  TRP A CG  1 
ATOM   15   C CD1 . TRP A 1 10  ? 28.60200  1.51200   91.46400  1.000 54.23561 ? 10  TRP A CD1 1 
ATOM   16   C CD2 . TRP A 1 10  ? 29.08600  3.55600   92.23800  1.000 50.82275 ? 10  TRP A CD2 1 
ATOM   17   N NE1 . TRP A 1 10  ? 29.41600  2.12600   90.54300  1.000 57.35487 ? 10  TRP A NE1 1 
ATOM   18   C CE2 . TRP A 1 10  ? 29.72800  3.38200   90.99500  1.000 52.60114 ? 10  TRP A CE2 1 
ATOM   19   C CE3 . TRP A 1 10  ? 29.24700  4.76900   92.91700  1.000 43.46260 ? 10  TRP A CE3 1 
ATOM   20   C CZ2 . TRP A 1 10  ? 30.51800  4.37600   90.41600  1.000 45.88432 ? 10  TRP A CZ2 1 
ATOM   21   C CZ3 . TRP A 1 10  ? 30.03000  5.75400   92.34000  1.000 39.62341 ? 10  TRP A CZ3 1 
ATOM   22   C CH2 . TRP A 1 10  ? 30.65400  5.55200   91.10300  1.000 38.42363 ? 10  TRP A CH2 1 
ATOM   23   N N   . ALA A 1 11  ? 25.80800  4.09600   91.85800  1.000 53.20357 ? 11  ALA A N   1 
ATOM   24   C CA  . ALA A 1 11  ? 25.72200  5.50100   91.47500  1.000 51.07485 ? 11  ALA A CA  1 
ATOM   25   C C   . ALA A 1 11  ? 24.37000  6.13000   91.78000  1.000 51.62784 ? 11  ALA A C   1 
ATOM   26   O O   . ALA A 1 11  ? 24.26600  7.36100   91.76200  1.000 49.68436 ? 11  ALA A O   1 
ATOM   27   C CB  . ALA A 1 11  ? 26.03400  5.66000   89.98700  1.000 46.84636 ? 11  ALA A CB  1 
ATOM   28   N N   . ASP A 1 12  ? 23.34100  5.32800   92.06900  1.000 56.59022 ? 12  ASP A N   1 
ATOM   29   C CA  . ASP A 1 12  ? 22.00000  5.87100   92.26000  1.000 55.07558 ? 12  ASP A CA  1 
ATOM   30   C C   . ASP A 1 12  ? 21.86200  6.66600   93.55400  1.000 51.63982 ? 12  ASP A C   1 
ATOM   31   O O   . ASP A 1 12  ? 20.90300  7.43400   93.69400  1.000 47.63238 ? 12  ASP A O   1 
ATOM   32   C CB  . ASP A 1 12  ? 20.96600  4.74300   92.23400  1.000 57.61117 ? 12  ASP A CB  1 
ATOM   33   C CG  . ASP A 1 12  ? 20.99700  3.95000   90.94300  1.000 58.89268 ? 12  ASP A CG  1 
ATOM   34   O OD1 . ASP A 1 12  ? 21.87800  4.21300   90.10000  1.000 59.67693 ? 12  ASP A OD1 1 
ATOM   35   O OD2 . ASP A 1 12  ? 20.13900  3.06000   90.77200  1.000 68.32742 ? 12  ASP A OD2 1 
ATOM   36   N N   . ARG A 1 13  ? 22.78700  6.50600   94.49700  1.000 48.48894 ? 13  ARG A N   1 
ATOM   37   C CA  . ARG A 1 13  ? 22.67900  7.14200   95.80300  1.000 50.90981 ? 13  ARG A CA  1 
ATOM   38   C C   . ARG A 1 13  ? 23.58200  8.36700   95.95300  1.000 40.34860 ? 13  ARG A C   1 
ATOM   39   O O   . ARG A 1 13  ? 23.67800  8.92100   97.05400  1.000 38.06237 ? 13  ARG A O   1 
ATOM   40   C CB  . ARG A 1 13  ? 22.98500  6.11900   96.90100  1.000 50.93487 ? 13  ARG A CB  1 
ATOM   41   C CG  . ARG A 1 13  ? 24.45300  5.72100   96.98900  1.000 56.23423 ? 13  ARG A CG  1 
ATOM   42   C CD  . ARG A 1 13  ? 24.69300  4.59700   97.99100  1.000 55.48851 ? 13  ARG A CD  1 
ATOM   43   N NE  . ARG A 1 13  ? 23.70900  4.57800   99.06700  1.000 55.59426 ? 13  ARG A NE  1 
ATOM   44   C CZ  . ARG A 1 13  ? 23.71900  5.38900   100.11700 1.000 66.30370 ? 13  ARG A CZ  1 
ATOM   45   N NH1 . ARG A 1 13  ? 24.63600  6.33400   100.25400 1.000 58.17427 ? 13  ARG A NH1 1 
ATOM   46   N NH2 . ARG A 1 13  ? 22.77900  5.25500   101.05000 1.000 70.00486 ? 13  ARG A NH2 1 
ATOM   47   N N   . LEU A 1 14  ? 24.23300  8.80700   94.87900  1.000 36.47445 ? 14  LEU A N   1 
ATOM   48   C CA  . LEU A 1 14  ? 25.16300  9.92500   94.97400  1.000 34.57534 ? 14  LEU A CA  1 
ATOM   49   C C   . LEU A 1 14  ? 24.42800  11.23900  95.23100  1.000 31.19434 ? 14  LEU A C   1 
ATOM   50   O O   . LEU A 1 14  ? 23.36500  11.50100  94.66000  1.000 34.56781 ? 14  LEU A O   1 
ATOM   51   C CB  . LEU A 1 14  ? 25.99700  10.03200  93.69700  1.000 28.02406 ? 14  LEU A CB  1 
ATOM   52   C CG  . LEU A 1 14  ? 26.93200  8.85300   93.41600  1.000 34.70287 ? 14  LEU A CG  1 
ATOM   53   C CD1 . LEU A 1 14  ? 27.64100  9.01900   92.08100  1.000 30.23430 ? 14  LEU A CD1 1 
ATOM   54   C CD2 . LEU A 1 14  ? 27.94100  8.69400   94.54000  1.000 28.54073 ? 14  LEU A CD2 1 
ATOM   55   N N   . ARG A 1 15  ? 25.00900  12.06600  96.10000  1.000 26.48926 ? 15  ARG A N   1 
ATOM   56   C CA  . ARG A 1 15  ? 24.46300  13.38000  96.40100  1.000 29.17468 ? 15  ARG A CA  1 
ATOM   57   C C   . ARG A 1 15  ? 24.70000  14.33800  95.23300  1.000 26.99199 ? 15  ARG A C   1 
ATOM   58   O O   . ARG A 1 15  ? 25.61300  14.13500  94.42600  1.000 21.84095 ? 15  ARG A O   1 
ATOM   59   C CB  . ARG A 1 15  ? 25.09600  13.94100  97.67600  1.000 29.95799 ? 15  ARG A CB  1 
ATOM   60   C CG  . ARG A 1 15  ? 24.58300  13.32100  98.97400  1.000 26.77560 ? 15  ARG A CG  1 
ATOM   61   C CD  . ARG A 1 15  ? 25.17200  11.93800  99.21400  1.000 29.33591 ? 15  ARG A CD  1 
ATOM   62   N NE  . ARG A 1 15  ? 24.78500  11.39700  100.51200 1.000 43.36070 ? 15  ARG A NE  1 
ATOM   63   C CZ  . ARG A 1 15  ? 25.03100  10.15900  100.91800 1.000 39.07195 ? 15  ARG A CZ  1 
ATOM   64   N NH1 . ARG A 1 15  ? 25.65700  9.28700   100.14400 1.000 30.30032 ? 15  ARG A NH1 1 
ATOM   65   N NH2 . ARG A 1 15  ? 24.63700  9.78500   102.13200 1.000 49.10975 ? 15  ARG A NH2 1 
ATOM   66   N N   . PRO A 1 16  ? 23.89300  15.40400  95.13300  1.000 23.83543 ? 16  PRO A N   1 
ATOM   67   C CA  . PRO A 1 16  ? 24.00100  16.29200  93.96100  1.000 23.86339 ? 16  PRO A CA  1 
ATOM   68   C C   . PRO A 1 16  ? 25.38900  16.87800  93.74500  1.000 28.42859 ? 16  PRO A C   1 
ATOM   69   O O   . PRO A 1 16  ? 25.79800  17.04600  92.58600  1.000 20.08981 ? 16  PRO A O   1 
ATOM   70   C CB  . PRO A 1 16  ? 22.96400  17.38800  94.25600  1.000 23.31848 ? 16  PRO A CB  1 
ATOM   71   C CG  . PRO A 1 16  ? 21.97200  16.73300  95.16400  1.000 23.93106 ? 16  PRO A CG  1 
ATOM   72   C CD  . PRO A 1 16  ? 22.77200  15.78500  96.01300  1.000 24.11476 ? 16  PRO A CD  1 
ATOM   73   N N   . GLU A 1 17  ? 26.13000  17.19400  94.81400  1.000 22.26704 ? 17  GLU A N   1 
ATOM   74   C CA  . GLU A 1 17  ? 27.46200  17.76900  94.62300  1.000 23.04129 ? 17  GLU A CA  1 
ATOM   75   C C   . GLU A 1 17  ? 28.37000  16.80700  93.86500  1.000 20.83326 ? 17  GLU A C   1 
ATOM   76   O O   . GLU A 1 17  ? 29.17300  17.22900  93.02500  1.000 20.52464 ? 17  GLU A O   1 
ATOM   77   C CB  . GLU A 1 17  ? 28.09700  18.14100  95.96600  1.000 24.10597 ? 17  GLU A CB  1 
ATOM   78   C CG  . GLU A 1 17  ? 27.50300  19.36500  96.65200  1.000 27.89595 ? 17  GLU A CG  1 
ATOM   79   C CD  . GLU A 1 17  ? 26.39600  19.01300  97.63500  1.000 34.33322 ? 17  GLU A CD  1 
ATOM   80   O OE1 . GLU A 1 17  ? 25.91400  17.86300  97.59700  1.000 25.56262 ? 17  GLU A OE1 1 
ATOM   81   O OE2 . GLU A 1 17  ? 26.01200  19.88600  98.44700  1.000 39.71880 ? 17  GLU A OE2 1 
ATOM   82   N N   . THR A 1 18  ? 28.27500  15.51300  94.17100  1.000 23.20084 ? 18  THR A N   1 
ATOM   83   C CA  . THR A 1 18  ? 29.08600  14.51700  93.47800  1.000 22.37167 ? 18  THR A CA  1 
ATOM   84   C C   . THR A 1 18  ? 28.63000  14.35400  92.03600  1.000 22.49856 ? 18  THR A C   1 
ATOM   85   O O   . THR A 1 18  ? 29.45500  14.24100  91.12200  1.000 20.42158 ? 18  THR A O   1 
ATOM   86   C CB  . THR A 1 18  ? 29.00500  13.18300  94.22000  1.000 24.45701 ? 18  THR A CB  1 
ATOM   87   O OG1 . THR A 1 18  ? 29.26700  13.40000  95.61200  1.000 22.25956 ? 18  THR A OG1 1 
ATOM   88   C CG2 . THR A 1 18  ? 30.00700  12.18400  93.65900  1.000 23.39553 ? 18  THR A CG2 1 
ATOM   89   N N   . ILE A 1 19  ? 27.31300  14.35200  91.82300  1.000 21.80914 ? 19  ILE A N   1 
ATOM   90   C CA  . ILE A 1 19  ? 26.74900  14.17200  90.48900  1.000 23.93728 ? 19  ILE A CA  1 
ATOM   91   C C   . ILE A 1 19  ? 27.23200  15.26700  89.54800  1.000 21.19352 ? 19  ILE A C   1 
ATOM   92   O O   . ILE A 1 19  ? 27.63100  14.99600  88.40800  1.000 19.79487 ? 19  ILE A O   1 
ATOM   93   C CB  . ILE A 1 19  ? 25.21200  14.13500  90.58300  1.000 24.46815 ? 19  ILE A CB  1 
ATOM   94   C CG1 . ILE A 1 19  ? 24.75200  12.84900  91.27900  1.000 29.29062 ? 19  ILE A CG1 1 
ATOM   95   C CG2 . ILE A 1 19  ? 24.57800  14.28500  89.21900  1.000 20.41850 ? 19  ILE A CG2 1 
ATOM   96   C CD1 . ILE A 1 19  ? 23.26200  12.82100  91.59200  1.000 34.60464 ? 19  ILE A CD1 1 
ATOM   97   N N   . ALA A 1 20  ? 27.22200  16.51800  90.01700  1.000 19.40907 ? 20  ALA A N   1 
ATOM   98   C CA  . ALA A 1 20  ? 27.62200  17.64700  89.18800  1.000 20.85948 ? 20  ALA A CA  1 
ATOM   99   C C   . ALA A 1 20  ? 29.08100  17.57000  88.75400  1.000 20.17948 ? 20  ALA A C   1 
ATOM   100  O O   . ALA A 1 20  ? 29.44700  18.17700  87.74400  1.000 20.28797 ? 20  ALA A O   1 
ATOM   101  C CB  . ALA A 1 20  ? 27.37300  18.95100  89.94300  1.000 17.02575 ? 20  ALA A CB  1 
ATOM   102  N N   . ILE A 1 21  ? 29.91900  16.84100  89.49000  1.000 19.83017 ? 21  ILE A N   1 
ATOM   103  C CA  . ILE A 1 21  ? 31.33600  16.71600  89.16600  1.000 17.04389 ? 21  ILE A CA  1 
ATOM   104  C C   . ILE A 1 21  ? 31.63600  15.44900  88.36000  1.000 22.09895 ? 21  ILE A C   1 
ATOM   105  O O   . ILE A 1 21  ? 32.62400  15.42100  87.60800  1.000 18.03486 ? 21  ILE A O   1 
ATOM   106  C CB  . ILE A 1 21  ? 32.17100  16.76600  90.47000  1.000 21.69929 ? 21  ILE A CB  1 
ATOM   107  C CG1 . ILE A 1 21  ? 32.03200  18.14800  91.12000  1.000 17.54326 ? 21  ILE A CG1 1 
ATOM   108  C CG2 . ILE A 1 21  ? 33.64000  16.41800  90.24000  1.000 13.56724 ? 21  ILE A CG2 1 
ATOM   109  C CD1 . ILE A 1 21  ? 32.44400  18.19800  92.57400  1.000 16.87125 ? 21  ILE A CD1 1 
ATOM   110  N N   . ARG A 1 22  ? 30.79300  14.42600  88.45200  1.000 20.36636 ? 22  ARG A N   1 
ATOM   111  C CA  . ARG A 1 22  ? 31.13000  13.11300  87.92600  1.000 18.85082 ? 22  ARG A CA  1 
ATOM   112  C C   . ARG A 1 22  ? 30.18200  12.58900  86.85800  1.000 18.20306 ? 22  ARG A C   1 
ATOM   113  O O   . ARG A 1 22  ? 30.60000  11.75600  86.05300  1.000 22.16828 ? 22  ARG A O   1 
ATOM   114  C CB  . ARG A 1 22  ? 31.18400  12.09600  89.07400  1.000 18.93253 ? 22  ARG A CB  1 
ATOM   115  C CG  . ARG A 1 22  ? 32.23100  12.42100  90.12500  1.000 21.95347 ? 22  ARG A CG  1 
ATOM   116  C CD  . ARG A 1 22  ? 33.63000  12.15300  89.59200  1.000 22.60160 ? 22  ARG A CD  1 
ATOM   117  N NE  . ARG A 1 22  ? 34.65600  12.36100  90.60700  1.000 23.63699 ? 22  ARG A NE  1 
ATOM   118  C CZ  . ARG A 1 22  ? 35.93300  12.03700  90.45000  1.000 20.77297 ? 22  ARG A CZ  1 
ATOM   119  N NH1 . ARG A 1 22  ? 36.36400  11.45700  89.34400  1.000 18.95987 ? 22  ARG A NH1 1 
ATOM   120  N NH2 . ARG A 1 22  ? 36.79700  12.30300  91.42700  1.000 16.86550 ? 22  ARG A NH2 1 
ATOM   121  N N   . ALA A 1 23  ? 28.92400  13.02400  86.83800  1.000 19.73323 ? 23  ALA A N   1 
ATOM   122  C CA  . ALA A 1 23  ? 27.95700  12.43900  85.91900  1.000 18.04743 ? 23  ALA A CA  1 
ATOM   123  C C   . ALA A 1 23  ? 28.23700  12.87300  84.48200  1.000 20.24677 ? 23  ALA A C   1 
ATOM   124  O O   . ALA A 1 23  ? 28.84900  13.91400  84.22100  1.000 19.92053 ? 23  ALA A O   1 
ATOM   125  C CB  . ALA A 1 23  ? 26.53300  12.83000  86.31000  1.000 16.46345 ? 23  ALA A CB  1 
ATOM   126  N N   . GLY A 1 24  ? 27.77700  12.04900  83.54100  1.000 20.68613 ? 24  GLY A N   1 
ATOM   127  C CA  . GLY A 1 24  ? 27.91200  12.31800  82.12500  1.000 20.89820 ? 24  GLY A CA  1 
ATOM   128  C C   . GLY A 1 24  ? 29.26200  11.99000  81.52600  1.000 21.37958 ? 24  GLY A C   1 
ATOM   129  O O   . GLY A 1 24  ? 29.46900  12.24800  80.33500  1.000 21.03186 ? 24  GLY A O   1 
ATOM   130  N N   . ILE A 1 25  ? 30.18400  11.43100  82.29600  1.000 19.97473 ? 25  ILE A N   1 
ATOM   131  C CA  . ILE A 1 25  ? 31.54800  11.22100  81.83100  1.000 23.65225 ? 25  ILE A CA  1 
ATOM   132  C C   . ILE A 1 25  ? 31.63600  9.88200   81.11300  1.000 22.05446 ? 25  ILE A C   1 
ATOM   133  O O   . ILE A 1 25  ? 31.24800  8.84500   81.66100  1.000 29.58326 ? 25  ILE A O   1 
ATOM   134  C CB  . ILE A 1 25  ? 32.53900  11.28900  83.00300  1.000 21.75011 ? 25  ILE A CB  1 
ATOM   135  C CG1 . ILE A 1 25  ? 32.56400  12.70700  83.58400  1.000 21.05974 ? 25  ILE A CG1 1 
ATOM   136  C CG2 . ILE A 1 25  ? 33.92000  10.84000  82.55600  1.000 19.95080 ? 25  ILE A CG2 1 
ATOM   137  C CD1 . ILE A 1 25  ? 33.42800  12.85800  84.82200  1.000 17.15708 ? 25  ILE A CD1 1 
ATOM   138  N N   . HIS A 1 26  ? 32.14000  9.90700   79.87900  1.000 24.68685 ? 26  HIS A N   1 
ATOM   139  C CA  . HIS A 1 26  ? 32.42900  8.70000   79.10100  1.000 24.01822 ? 26  HIS A CA  1 
ATOM   140  C C   . HIS A 1 26  ? 33.83600  8.85600   78.54000  1.000 20.48501 ? 26  HIS A C   1 
ATOM   141  O O   . HIS A 1 26  ? 34.01000  9.30100   77.40600  1.000 25.47788 ? 26  HIS A O   1 
ATOM   142  C CB  . HIS A 1 26  ? 31.39600  8.49700   77.99900  1.000 24.45099 ? 26  HIS A CB  1 
ATOM   143  C CG  . HIS A 1 26  ? 29.98800  8.47700   78.50300  1.000 29.02502 ? 26  HIS A CG  1 
ATOM   144  N ND1 . HIS A 1 26  ? 29.43400  7.37300   79.11500  1.000 30.20579 ? 26  HIS A ND1 1 
ATOM   145  C CD2 . HIS A 1 26  ? 29.03000  9.43300   78.51200  1.000 23.02513 ? 26  HIS A CD2 1 
ATOM   146  C CE1 . HIS A 1 26  ? 28.19100  7.64600   79.46900  1.000 30.61906 ? 26  HIS A CE1 1 
ATOM   147  N NE2 . HIS A 1 26  ? 27.92100  8.88900   79.11400  1.000 33.71127 ? 26  HIS A NE2 1 
ATOM   148  N N   . ARG A 1 27  ? 34.83800  8.47400   79.32300  1.000 19.46909 ? 27  ARG A N   1 
ATOM   149  C CA  . ARG A 1 27  ? 36.21400  8.73600   78.92700  1.000 24.67541 ? 27  ARG A CA  1 
ATOM   150  C C   . ARG A 1 27  ? 36.58900  7.93400   77.69100  1.000 26.81917 ? 27  ARG A C   1 
ATOM   151  O O   . ARG A 1 27  ? 36.18700  6.77800   77.52800  1.000 26.51701 ? 27  ARG A O   1 
ATOM   152  C CB  . ARG A 1 27  ? 37.17700  8.41800   80.06900  1.000 20.65558 ? 27  ARG A CB  1 
ATOM   153  C CG  . ARG A 1 27  ? 37.15000  9.45600   81.16400  1.000 24.77264 ? 27  ARG A CG  1 
ATOM   154  C CD  . ARG A 1 27  ? 38.27700  9.28300   82.15700  1.000 20.27765 ? 27  ARG A CD  1 
ATOM   155  N NE  . ARG A 1 27  ? 38.21700  10.35000  83.14800  1.000 23.11315 ? 27  ARG A NE  1 
ATOM   156  C CZ  . ARG A 1 27  ? 37.44900  10.31600  84.23000  1.000 30.34045 ? 27  ARG A CZ  1 
ATOM   157  N NH1 . ARG A 1 27  ? 36.70900  9.25700   84.51900  1.000 25.60929 ? 27  ARG A NH1 1 
ATOM   158  N NH2 . ARG A 1 27  ? 37.41800  11.37300  85.03900  1.000 23.86684 ? 27  ARG A NH2 1 
ATOM   159  N N   . THR A 1 28  ? 37.36600  8.56300   76.81500  1.000 24.74025 ? 28  THR A N   1 
ATOM   160  C CA  . THR A 1 28  ? 37.89200  7.88900   75.64600  1.000 20.74284 ? 28  THR A CA  1 
ATOM   161  C C   . THR A 1 28  ? 39.05200  6.99000   76.06200  1.000 23.23759 ? 28  THR A C   1 
ATOM   162  O O   . THR A 1 28  ? 39.46500  6.96100   77.22400  1.000 21.38536 ? 28  THR A O   1 
ATOM   163  C CB  . THR A 1 28  ? 38.33100  8.90600   74.59400  1.000 23.08135 ? 28  THR A CB  1 
ATOM   164  O OG1 . THR A 1 28  ? 39.61700  9.43300   74.94000  1.000 21.84199 ? 28  THR A OG1 1 
ATOM   165  C CG2 . THR A 1 28  ? 37.33500  10.05600  74.50900  1.000 21.91203 ? 28  THR A CG2 1 
ATOM   166  N N   . GLN A 1 29  ? 39.59500  6.25500   75.09100  1.000 21.47270 ? 29  GLN A N   1 
ATOM   167  C CA  . GLN A 1 29  ? 40.72000  5.36800   75.35800  1.000 23.68240 ? 29  GLN A CA  1 
ATOM   168  C C   . GLN A 1 29  ? 41.97300  6.12800   75.77800  1.000 23.68945 ? 29  GLN A C   1 
ATOM   169  O O   . GLN A 1 29  ? 42.89600  5.51700   76.32200  1.000 23.62377 ? 29  GLN A O   1 
ATOM   170  C CB  . GLN A 1 29  ? 41.00800  4.51200   74.12100  1.000 21.96837 ? 29  GLN A CB  1 
ATOM   171  C CG  . GLN A 1 29  ? 41.49200  5.31800   72.92300  1.000 30.22212 ? 29  GLN A CG  1 
ATOM   172  C CD  . GLN A 1 29  ? 41.03800  4.73000   71.59800  1.000 40.08847 ? 29  GLN A CD  1 
ATOM   173  O OE1 . GLN A 1 29  ? 40.13400  3.89300   71.55500  1.000 38.33993 ? 29  GLN A OE1 1 
ATOM   174  N NE2 . GLN A 1 29  ? 41.66300  5.17000   70.50700  1.000 36.71406 ? 29  GLN A NE2 1 
ATOM   175  N N   . GLU A 1 30  ? 42.03700  7.44100   75.53100  1.000 24.40938 ? 30  GLU A N   1 
ATOM   176  C CA  . GLU A 1 30  ? 43.15300  8.24200   76.03000  1.000 23.25309 ? 30  GLU A CA  1 
ATOM   177  C C   . GLU A 1 30  ? 43.10200  8.44100   77.54100  1.000 23.14865 ? 30  GLU A C   1 
ATOM   178  O O   . GLU A 1 30  ? 44.09600  8.89300   78.12000  1.000 22.19427 ? 30  GLU A O   1 
ATOM   179  C CB  . GLU A 1 30  ? 43.18400  9.60700   75.33900  1.000 19.12859 ? 30  GLU A CB  1 
ATOM   180  C CG  . GLU A 1 30  ? 43.11500  9.54900   73.81500  1.000 24.03627 ? 30  GLU A CG  1 
ATOM   181  C CD  . GLU A 1 30  ? 44.47300  9.35700   73.16300  1.000 25.16429 ? 30  GLU A CD  1 
ATOM   182  O OE1 . GLU A 1 30  ? 45.47300  9.17800   73.89300  1.000 26.05536 ? 30  GLU A OE1 1 
ATOM   183  O OE2 . GLU A 1 30  ? 44.53900  9.39100   71.91700  1.000 27.82994 ? 30  GLU A OE2 1 
ATOM   184  N N   . GLN A 1 31  ? 41.97300  8.12500   78.18100  1.000 21.84378 ? 31  GLN A N   1 
ATOM   185  C CA  . GLN A 1 31  ? 41.83600  8.18400   79.63600  1.000 23.62703 ? 31  GLN A CA  1 
ATOM   186  C C   . GLN A 1 31  ? 42.07400  9.59400   80.17200  1.000 20.75939 ? 31  GLN A C   1 
ATOM   187  O O   . GLN A 1 31  ? 42.63600  9.77900   81.25400  1.000 21.79594 ? 31  GLN A O   1 
ATOM   188  C CB  . GLN A 1 31  ? 42.77200  7.17900   80.31300  1.000 21.61201 ? 31  GLN A CB  1 
ATOM   189  C CG  . GLN A 1 31  ? 42.41800  5.73100   80.02000  1.000 29.32225 ? 31  GLN A CG  1 
ATOM   190  C CD  . GLN A 1 31  ? 43.57800  4.79100   80.26800  1.000 35.67283 ? 31  GLN A CD  1 
ATOM   191  O OE1 . GLN A 1 31  ? 44.60100  4.86100   79.58700  1.000 41.01916 ? 31  GLN A OE1 1 
ATOM   192  N NE2 . GLN A 1 31  ? 43.42900  3.90700   81.24700  1.000 40.04637 ? 31  GLN A NE2 1 
ATOM   193  N N   . GLU A 1 32  ? 41.64300  10.59700  79.41200  1.000 16.95812 ? 32  GLU A N   1 
ATOM   194  C CA  . GLU A 1 32  ? 41.75700  11.97400  79.87200  1.000 19.58861 ? 32  GLU A CA  1 
ATOM   195  C C   . GLU A 1 32  ? 40.99800  12.16000  81.18500  1.000 18.69355 ? 32  GLU A C   1 
ATOM   196  O O   . GLU A 1 32  ? 39.84100  11.75300  81.31300  1.000 15.71278 ? 32  GLU A O   1 
ATOM   197  C CB  . GLU A 1 32  ? 41.23100  12.93700  78.80000  1.000 16.76998 ? 32  GLU A CB  1 
ATOM   198  C CG  . GLU A 1 32  ? 39.73200  12.84300  78.48400  1.000 16.21670 ? 32  GLU A CG  1 
ATOM   199  C CD  . GLU A 1 32  ? 39.33400  11.57600  77.73700  1.000 20.49699 ? 32  GLU A CD  1 
ATOM   200  O OE1 . GLU A 1 32  ? 40.22600  10.78900  77.35900  1.000 19.47724 ? 32  GLU A OE1 1 
ATOM   201  O OE2 . GLU A 1 32  ? 38.12000  11.37200  77.51900  1.000 21.02780 ? 32  GLU A OE2 1 
ATOM   202  N N   . HIS A 1 33  ? 41.66400  12.76300  82.17000  1.000 19.22193 ? 33  HIS A N   1 
ATOM   203  C CA  . HIS A 1 33  ? 41.00300  13.03200  83.44300  1.000 16.77028 ? 33  HIS A CA  1 
ATOM   204  C C   . HIS A 1 33  ? 39.86200  14.02600  83.26600  1.000 17.26437 ? 33  HIS A C   1 
ATOM   205  O O   . HIS A 1 33  ? 38.75000  13.79900  83.75500  1.000 20.25718 ? 33  HIS A O   1 
ATOM   206  C CB  . HIS A 1 33  ? 42.01600  13.54400  84.46800  1.000 16.60350 ? 33  HIS A CB  1 
ATOM   207  C CG  . HIS A 1 33  ? 41.45600  13.69200  85.85000  1.000 16.39429 ? 33  HIS A CG  1 
ATOM   208  N ND1 . HIS A 1 33  ? 40.46400  12.87300  86.34400  1.000 19.90502 ? 33  HIS A ND1 1 
ATOM   209  C CD2 . HIS A 1 33  ? 41.76300  14.55200  86.84900  1.000 16.71051 ? 33  HIS A CD2 1 
ATOM   210  C CE1 . HIS A 1 33  ? 40.16900  13.23700  87.58000  1.000 16.76805 ? 33  HIS A CE1 1 
ATOM   211  N NE2 . HIS A 1 33  ? 40.94500  14.25200  87.91100  1.000 19.15081 ? 33  HIS A NE2 1 
ATOM   212  N N   . SER A 1 34  ? 40.11000  15.11900  82.55000  1.000 15.24161 ? 34  SER A N   1 
ATOM   213  C CA  . SER A 1 34  ? 39.11600  16.16100  82.34100  1.000 16.41454 ? 34  SER A CA  1 
ATOM   214  C C   . SER A 1 34  ? 38.40600  15.96100  81.00400  1.000 20.65415 ? 34  SER A C   1 
ATOM   215  O O   . SER A 1 34  ? 38.94300  15.35100  80.07600  1.000 16.89183 ? 34  SER A O   1 
ATOM   216  C CB  . SER A 1 34  ? 39.76700  17.54600  82.39400  1.000 16.65779 ? 34  SER A CB  1 
ATOM   217  O OG  . SER A 1 34  ? 38.79100  18.56100  82.57200  1.000 15.79462 ? 34  SER A OG  1 
ATOM   218  N N   . GLU A 1 35  ? 37.18700  16.49700  80.91400  1.000 16.25004 ? 35  GLU A N   1 
ATOM   219  C CA  . GLU A 1 35  ? 36.32100  16.22800  79.77000  1.000 17.86435 ? 35  GLU A CA  1 
ATOM   220  C C   . GLU A 1 35  ? 36.87500  16.84500  78.48800  1.000 16.81974 ? 35  GLU A C   1 
ATOM   221  O O   . GLU A 1 35  ? 37.32500  17.99300  78.47000  1.000 16.51107 ? 35  GLU A O   1 
ATOM   222  C CB  . GLU A 1 35  ? 34.91100  16.75800  80.03600  1.000 16.77548 ? 35  GLU A CB  1 
ATOM   223  C CG  . GLU A 1 35  ? 34.16100  16.04000  81.15600  1.000 19.49967 ? 35  GLU A CG  1 
ATOM   224  C CD  . GLU A 1 35  ? 34.60300  16.47800  82.54800  1.000 18.19556 ? 35  GLU A CD  1 
ATOM   225  O OE1 . GLU A 1 35  ? 35.50400  17.33300  82.64900  1.000 17.65119 ? 35  GLU A OE1 1 
ATOM   226  O OE2 . GLU A 1 35  ? 34.05000  15.96100  83.54300  1.000 16.95550 ? 35  GLU A OE2 1 
ATOM   227  N N   . ALA A 1 36  ? 36.82500  16.07700  77.40500  1.000 18.10632 ? 36  ALA A N   1 
ATOM   228  C CA  . ALA A 1 36  ? 37.36700  16.52400  76.13300  1.000 15.57358 ? 36  ALA A CA  1 
ATOM   229  C C   . ALA A 1 36  ? 36.35200  17.37500  75.38200  1.000 16.87213 ? 36  ALA A C   1 
ATOM   230  O O   . ALA A 1 36  ? 35.14500  17.31000  75.62300  1.000 17.57649 ? 36  ALA A O   1 
ATOM   231  C CB  . ALA A 1 36  ? 37.77200  15.33300  75.26800  1.000 15.96064 ? 36  ALA A CB  1 
ATOM   232  N N   . ILE A 1 37  ? 36.86500  18.19200  74.46800  1.000 14.61628 ? 37  ILE A N   1 
ATOM   233  C CA  . ILE A 1 37  ? 36.04800  18.95800  73.53600  1.000 16.68873 ? 37  ILE A CA  1 
ATOM   234  C C   . ILE A 1 37  ? 36.12000  18.26600  72.18400  1.000 15.74423 ? 37  ILE A C   1 
ATOM   235  O O   . ILE A 1 37  ? 37.21300  17.92900  71.70800  1.000 14.00515 ? 37  ILE A O   1 
ATOM   236  C CB  . ILE A 1 37  ? 36.52400  20.41900  73.43000  1.000 16.25259 ? 37  ILE A CB  1 
ATOM   237  C CG1 . ILE A 1 37  ? 36.63900  21.06200  74.80900  1.000 17.61216 ? 37  ILE A CG1 1 
ATOM   238  C CG2 . ILE A 1 37  ? 35.56800  21.23200  72.56600  1.000 16.55779 ? 37  ILE A CG2 1 
ATOM   239  C CD1 . ILE A 1 37  ? 37.17900  22.47600  74.76900  1.000 19.59410 ? 37  ILE A CD1 1 
ATOM   240  N N   . PHE A 1 38  ? 34.96500  18.03200  71.57500  1.000 12.34205 ? 38  PHE A N   1 
ATOM   241  C CA  . PHE A 1 38  ? 34.94800  17.42200  70.25400  1.000 14.79454 ? 38  PHE A CA  1 
ATOM   242  C C   . PHE A 1 38  ? 34.43200  18.43100  69.23800  1.000 19.42868 ? 38  PHE A C   1 
ATOM   243  O O   . PHE A 1 38  ? 33.23700  18.44500  68.91600  1.000 19.23119 ? 38  PHE A O   1 
ATOM   244  C CB  . PHE A 1 38  ? 34.10300  16.14700  70.25200  1.000 15.19334 ? 38  PHE A CB  1 
ATOM   245  C CG  . PHE A 1 38  ? 34.76000  14.98400  70.95800  1.000 14.89326 ? 38  PHE A CG  1 
ATOM   246  C CD1 . PHE A 1 38  ? 34.60100  14.80300  72.32100  1.000 15.74657 ? 38  PHE A CD1 1 
ATOM   247  C CD2 . PHE A 1 38  ? 35.54400  14.08300  70.25400  1.000 18.83643 ? 38  PHE A CD2 1 
ATOM   248  C CE1 . PHE A 1 38  ? 35.20500  13.74000  72.97400  1.000 15.64479 ? 38  PHE A CE1 1 
ATOM   249  C CE2 . PHE A 1 38  ? 36.15300  13.01700  70.89700  1.000 17.76693 ? 38  PHE A CE2 1 
ATOM   250  C CZ  . PHE A 1 38  ? 35.98400  12.84800  72.26000  1.000 17.10187 ? 38  PHE A CZ  1 
ATOM   251  N N   . PRO A 1 39  ? 35.29800  19.29900  68.72200  1.000 15.02256 ? 39  PRO A N   1 
ATOM   252  C CA  . PRO A 1 39  ? 34.87200  20.19200  67.64400  1.000 15.19260 ? 39  PRO A CA  1 
ATOM   253  C C   . PRO A 1 39  ? 34.88800  19.42200  66.34000  1.000 17.08965 ? 39  PRO A C   1 
ATOM   254  O O   . PRO A 1 39  ? 35.89400  19.41200  65.62700  1.000 17.45054 ? 39  PRO A O   1 
ATOM   255  C CB  . PRO A 1 39  ? 35.91300  21.32600  67.67000  1.000 15.84715 ? 39  PRO A CB  1 
ATOM   256  C CG  . PRO A 1 39  ? 36.98700  20.88600  68.68700  1.000 14.99700 ? 39  PRO A CG  1 
ATOM   257  C CD  . PRO A 1 39  ? 36.73700  19.43500  68.98500  1.000 13.49565 ? 39  PRO A CD  1 
ATOM   258  N N   . THR A 1 40  ? 33.79700  18.71800  66.05600  1.000 16.04314 ? 40  THR A N   1 
ATOM   259  C CA  . THR A 1 40  ? 33.65800  17.94500  64.83200  1.000 17.53929 ? 40  THR A CA  1 
ATOM   260  C C   . THR A 1 40  ? 32.21000  18.02200  64.37800  1.000 16.41423 ? 40  THR A C   1 
ATOM   261  O O   . THR A 1 40  ? 31.29900  18.05000  65.20600  1.000 23.86562 ? 40  THR A O   1 
ATOM   262  C CB  . THR A 1 40  ? 34.08300  16.47600  65.03400  1.000 16.90927 ? 40  THR A CB  1 
ATOM   263  O OG1 . THR A 1 40  ? 34.07500  15.79100  63.77600  1.000 15.20060 ? 40  THR A OG1 1 
ATOM   264  C CG2 . THR A 1 40  ? 33.15500  15.76200  65.99400  1.000 14.90222 ? 40  THR A CG2 1 
ATOM   265  N N   . SER A 1 41  ? 31.99200  18.08900  63.06700  1.000 18.50460 ? 41  SER A N   1 
ATOM   266  C CA  . SER A 1 41  ? 30.61700  18.10900  62.58900  1.000 22.33211 ? 41  SER A CA  1 
ATOM   267  C C   . SER A 1 41  ? 30.10300  16.72500  62.21400  1.000 20.69440 ? 41  SER A C   1 
ATOM   268  O O   . SER A 1 41  ? 28.90200  16.46300  62.34500  1.000 22.90137 ? 41  SER A O   1 
ATOM   269  C CB  . SER A 1 41  ? 30.47400  19.06700  61.40100  1.000 15.74154 ? 41  SER A CB  1 
ATOM   270  O OG  . SER A 1 41  ? 31.35600  18.75300  60.33800  1.000 18.28152 ? 41  SER A OG  1 
ATOM   271  N N   . SER A 1 42  ? 30.97100  15.82400  61.77100  1.000 16.43098 ? 42  SER A N   1 
ATOM   272  C CA  . SER A 1 42  ? 30.53800  14.48600  61.40400  1.000 22.06229 ? 42  SER A CA  1 
ATOM   273  C C   . SER A 1 42  ? 31.43100  13.45700  62.08200  1.000 20.97729 ? 42  SER A C   1 
ATOM   274  O O   . SER A 1 42  ? 32.35400  13.79000  62.83100  1.000 17.83242 ? 42  SER A O   1 
ATOM   275  C CB  . SER A 1 42  ? 30.54700  14.29000  59.88500  1.000 18.18994 ? 42  SER A CB  1 
ATOM   276  O OG  . SER A 1 42  ? 31.87900  14.20700  59.40700  1.000 23.02598 ? 42  SER A OG  1 
ATOM   277  N N   . PHE A 1 43  ? 31.14000  12.18900  61.81400  1.000 23.97473 ? 43  PHE A N   1 
ATOM   278  C CA  . PHE A 1 43  ? 31.85500  11.08500  62.42900  1.000 19.96069 ? 43  PHE A CA  1 
ATOM   279  C C   . PHE A 1 43  ? 32.13900  10.02600  61.37500  1.000 21.84165 ? 43  PHE A C   1 
ATOM   280  O O   . PHE A 1 43  ? 31.39500  9.88100   60.40300  1.000 23.28228 ? 43  PHE A O   1 
ATOM   281  C CB  . PHE A 1 43  ? 31.05400  10.52100  63.60400  1.000 19.65637 ? 43  PHE A CB  1 
ATOM   282  C CG  . PHE A 1 43  ? 30.74500  11.54800  64.66100  1.000 23.34512 ? 43  PHE A CG  1 
ATOM   283  C CD1 . PHE A 1 43  ? 29.61200  12.34800  64.56400  1.000 23.89622 ? 43  PHE A CD1 1 
ATOM   284  C CD2 . PHE A 1 43  ? 31.59300  11.72200  65.74800  1.000 22.74509 ? 43  PHE A CD2 1 
ATOM   285  C CE1 . PHE A 1 43  ? 29.32600  13.29600  65.52900  1.000 22.86586 ? 43  PHE A CE1 1 
ATOM   286  C CE2 . PHE A 1 43  ? 31.31400  12.67400  66.72200  1.000 22.31558 ? 43  PHE A CE2 1 
ATOM   287  C CZ  . PHE A 1 43  ? 30.17900  13.45900  66.61400  1.000 22.75069 ? 43  PHE A CZ  1 
ATOM   288  N N   . VAL A 1 44  ? 33.23000  9.30200   61.56800  1.000 19.11768 ? 44  VAL A N   1 
ATOM   289  C CA  . VAL A 1 44  ? 33.72100  8.34200   60.58900  1.000 20.68932 ? 44  VAL A CA  1 
ATOM   290  C C   . VAL A 1 44  ? 33.18500  6.95500   60.92900  1.000 26.98519 ? 44  VAL A C   1 
ATOM   291  O O   . VAL A 1 44  ? 33.04100  6.60000   62.10300  1.000 29.04863 ? 44  VAL A O   1 
ATOM   292  C CB  . VAL A 1 44  ? 35.26200  8.36400   60.55200  1.000 22.73071 ? 44  VAL A CB  1 
ATOM   293  C CG1 . VAL A 1 44  ? 35.80000  7.29600   59.62900  1.000 31.65859 ? 44  VAL A CG1 1 
ATOM   294  C CG2 . VAL A 1 44  ? 35.75200  9.72100   60.10300  1.000 21.29358 ? 44  VAL A CG2 1 
ATOM   295  N N   . PHE A 1 45  ? 32.87000  6.17000   59.90300  1.000 25.83394 ? 45  PHE A N   1 
ATOM   296  C CA  . PHE A 1 45  ? 32.42200  4.79800   60.08000  1.000 27.49496 ? 45  PHE A CA  1 
ATOM   297  C C   . PHE A 1 45  ? 33.52600  3.83400   59.66600  1.000 27.19085 ? 45  PHE A C   1 
ATOM   298  O O   . PHE A 1 45  ? 34.38500  4.16300   58.84300  1.000 27.01488 ? 45  PHE A O   1 
ATOM   299  C CB  . PHE A 1 45  ? 31.14700  4.53100   59.27400  1.000 24.13331 ? 45  PHE A CB  1 
ATOM   300  C CG  . PHE A 1 45  ? 30.07900  5.56000   59.49000  1.000 24.51453 ? 45  PHE A CG  1 
ATOM   301  C CD1 . PHE A 1 45  ? 29.44200  5.66800   60.71800  1.000 25.37212 ? 45  PHE A CD1 1 
ATOM   302  C CD2 . PHE A 1 45  ? 29.72100  6.43500   58.47300  1.000 23.53339 ? 45  PHE A CD2 1 
ATOM   303  C CE1 . PHE A 1 45  ? 28.46300  6.62400   60.92700  1.000 21.15111 ? 45  PHE A CE1 1 
ATOM   304  C CE2 . PHE A 1 45  ? 28.73500  7.38900   58.67600  1.000 22.79090 ? 45  PHE A CE2 1 
ATOM   305  C CZ  . PHE A 1 45  ? 28.10600  7.48200   59.90400  1.000 21.86948 ? 45  PHE A CZ  1 
ATOM   306  N N   . ASP A 1 46  ? 33.51300  2.64400   60.27500  1.000 27.13499 ? 46  ASP A N   1 
ATOM   307  C CA  . ASP A 1 46  ? 34.52000  1.62800   59.98500  1.000 31.61014 ? 46  ASP A CA  1 
ATOM   308  C C   . ASP A 1 46  ? 34.29700  0.94300   58.64500  1.000 27.13262 ? 46  ASP A C   1 
ATOM   309  O O   . ASP A 1 46  ? 35.25000  0.39900   58.07400  1.000 23.27514 ? 46  ASP A O   1 
ATOM   310  C CB  . ASP A 1 46  ? 34.53900  0.56800   61.09100  1.000 35.34286 ? 46  ASP A CB  1 
ATOM   311  C CG  . ASP A 1 46  ? 35.05000  1.11100   62.41400  1.000 51.71682 ? 46  ASP A CG  1 
ATOM   312  O OD1 . ASP A 1 46  ? 36.01600  1.90800   62.39700  1.000 55.64282 ? 46  ASP A OD1 1 
ATOM   313  O OD2 . ASP A 1 46  ? 34.48400  0.74300   63.47000  1.000 50.69425 ? 46  ASP A OD2 1 
ATOM   314  N N   . SER A 1 47  ? 33.06700  0.95900   58.14100  1.000 26.49811 ? 47  SER A N   1 
ATOM   315  C CA  . SER A 1 47  ? 32.70300  0.24900   56.92300  1.000 27.70453 ? 47  SER A CA  1 
ATOM   316  C C   . SER A 1 47  ? 31.37600  0.80300   56.43400  1.000 24.31946 ? 47  SER A C   1 
ATOM   317  O O   . SER A 1 47  ? 30.65900  1.48800   57.17000  1.000 24.44744 ? 47  SER A O   1 
ATOM   318  C CB  . SER A 1 47  ? 32.58900  -1.25800  57.16800  1.000 24.43158 ? 47  SER A CB  1 
ATOM   319  O OG  . SER A 1 47  ? 31.54600  -1.52100  58.09600  1.000 21.98079 ? 47  SER A OG  1 
ATOM   320  N N   . ALA A 1 48  ? 31.04700  0.48000   55.18000  1.000 23.70260 ? 48  ALA A N   1 
ATOM   321  C CA  . ALA A 1 48  ? 29.72400  0.81500   54.66400  1.000 22.83957 ? 48  ALA A CA  1 
ATOM   322  C C   . ALA A 1 48  ? 28.64300  0.14800   55.49300  1.000 25.36412 ? 48  ALA A C   1 
ATOM   323  O O   . ALA A 1 48  ? 27.61200  0.76300   55.79600  1.000 23.95516 ? 48  ALA A O   1 
ATOM   324  C CB  . ALA A 1 48  ? 29.59700  0.39600   53.19800  1.000 26.47696 ? 48  ALA A CB  1 
ATOM   325  N N   . GLU A 1 49  ? 28.87200  -1.11200  55.87600  1.000 24.50022 ? 49  GLU A N   1 
ATOM   326  C CA  A GLU A 1 49  ? 27.90100  -1.83600  56.68600  0.559 25.67404 ? 49  GLU A CA  1 
ATOM   327  C CA  B GLU A 1 49  ? 27.89200  -1.83100  56.68200  0.441 25.64778 ? 49  GLU A CA  1 
ATOM   328  C C   . GLU A 1 49  ? 27.61800  -1.09500  57.98700  1.000 27.77988 ? 49  GLU A C   1 
ATOM   329  O O   . GLU A 1 49  ? 26.45700  -0.89500  58.36600  1.000 28.97791 ? 49  GLU A O   1 
ATOM   330  C CB  A GLU A 1 49  ? 28.41600  -3.25200  56.96400  0.559 24.81236 ? 49  GLU A CB  1 
ATOM   331  C CB  B GLU A 1 49  ? 28.37900  -3.25700  56.95500  0.441 24.87244 ? 49  GLU A CB  1 
ATOM   332  C CG  A GLU A 1 49  ? 28.52100  -4.16000  55.73300  0.559 25.38503 ? 49  GLU A CG  1 
ATOM   333  C CG  B GLU A 1 49  ? 27.40800  -4.36600  56.54000  0.441 25.51713 ? 49  GLU A CG  1 
ATOM   334  C CD  A GLU A 1 49  ? 29.75500  -3.89900  54.86900  0.559 26.20656 ? 49  GLU A CD  1 
ATOM   335  C CD  B GLU A 1 49  ? 26.25300  -4.55400  57.51100  0.441 26.94161 ? 49  GLU A CD  1 
ATOM   336  O OE1 A GLU A 1 49  ? 30.51200  -2.94700  55.14900  0.559 20.42756 ? 49  GLU A OE1 1 
ATOM   337  O OE1 B GLU A 1 49  ? 25.48200  -3.59300  57.72500  0.441 26.36798 ? 49  GLU A OE1 1 
ATOM   338  O OE2 A GLU A 1 49  ? 29.96400  -4.66100  53.90100  0.559 27.37317 ? 49  GLU A OE2 1 
ATOM   339  O OE2 B GLU A 1 49  ? 26.11500  -5.66900  58.06100  0.441 25.01533 ? 49  GLU A OE2 1 
ATOM   340  N N   . GLU A 1 50  ? 28.67700  -0.66100  58.67900  1.000 23.98610 ? 50  GLU A N   1 
ATOM   341  C CA  . GLU A 1 50  ? 28.48800  0.08400   59.92100  1.000 25.80732 ? 50  GLU A CA  1 
ATOM   342  C C   . GLU A 1 50  ? 27.73200  1.38300   59.67200  1.000 24.12303 ? 50  GLU A C   1 
ATOM   343  O O   . GLU A 1 50  ? 26.83600  1.74400   60.44300  1.000 26.93727 ? 50  GLU A O   1 
ATOM   344  C CB  . GLU A 1 50  ? 29.83900  0.36800   60.58300  1.000 27.82374 ? 50  GLU A CB  1 
ATOM   345  C CG  . GLU A 1 50  ? 29.72400  1.18600   61.86300  1.000 30.43364 ? 50  GLU A CG  1 
ATOM   346  C CD  . GLU A 1 50  ? 31.03800  1.31400   62.60400  1.000 38.99670 ? 50  GLU A CD  1 
ATOM   347  O OE1 . GLU A 1 50  ? 31.86700  2.16200   62.20900  1.000 39.64104 ? 50  GLU A OE1 1 
ATOM   348  O OE2 . GLU A 1 50  ? 31.24400  0.56200   63.58300  1.000 43.75890 ? 50  GLU A OE2 1 
ATOM   349  N N   . ALA A 1 51  ? 28.06800  2.08800   58.58600  1.000 26.97216 ? 51  ALA A N   1 
ATOM   350  C CA  . ALA A 1 51  ? 27.36300  3.32500   58.26000  1.000 26.15458 ? 51  ALA A CA  1 
ATOM   351  C C   . ALA A 1 51  ? 25.87800  3.06900   58.05500  1.000 27.19196 ? 51  ALA A C   1 
ATOM   352  O O   . ALA A 1 51  ? 25.03400  3.83200   58.54100  1.000 29.90656 ? 51  ALA A O   1 
ATOM   353  C CB  . ALA A 1 51  ? 27.96200  3.96300   57.00400  1.000 22.14079 ? 51  ALA A CB  1 
ATOM   354  N N   . ALA A 1 52  ? 25.54300  1.99800   57.33400  1.000 25.98635 ? 52  ALA A N   1 
ATOM   355  C CA  . ALA A 1 52  ? 24.14300  1.66900   57.10300  1.000 31.21976 ? 52  ALA A CA  1 
ATOM   356  C C   . ALA A 1 52  ? 23.43700  1.31800   58.40600  1.000 29.16873 ? 52  ALA A C   1 
ATOM   357  O O   . ALA A 1 52  ? 22.32000  1.78400   58.65700  1.000 29.43726 ? 52  ALA A O   1 
ATOM   358  C CB  . ALA A 1 52  ? 24.03900  0.52100   56.09600  1.000 27.54509 ? 52  ALA A CB  1 
ATOM   359  N N   . ASP A 1 53  ? 24.08200  0.51000   59.25500  1.000 28.31730 ? 53  ASP A N   1 
ATOM   360  C CA  . ASP A 1 53  ? 23.47500  0.12700   60.52800  1.000 31.14495 ? 53  ASP A CA  1 
ATOM   361  C C   . ASP A 1 53  ? 23.21800  1.34300   61.40300  1.000 36.02859 ? 53  ASP A C   1 
ATOM   362  O O   . ASP A 1 53  ? 22.13400  1.49200   61.98100  1.000 38.66262 ? 53  ASP A O   1 
ATOM   363  C CB  . ASP A 1 53  ? 24.37500  -0.86200  61.26500  1.000 33.18261 ? 53  ASP A CB  1 
ATOM   364  C CG  . ASP A 1 53  ? 24.42700  -2.20600  60.59500  1.000 34.72658 ? 53  ASP A CG  1 
ATOM   365  O OD1 . ASP A 1 53  ? 23.44800  -2.56200  59.90400  1.000 40.30002 ? 53  ASP A OD1 1 
ATOM   366  O OD2 . ASP A 1 53  ? 25.45000  -2.90400  60.75900  1.000 34.60246 ? 53  ASP A OD2 1 
ATOM   367  N N   . ARG A 1 54  ? 24.21300  2.22300   61.52000  1.000 33.53237 ? 54  ARG A N   1 
ATOM   368  C CA  . ARG A 1 54  ? 24.05300  3.40100   62.36300  1.000 35.15357 ? 54  ARG A CA  1 
ATOM   369  C C   . ARG A 1 54  ? 22.96600  4.32500   61.81800  1.000 30.90175 ? 54  ARG A C   1 
ATOM   370  O O   . ARG A 1 54  ? 22.15100  4.85500   62.58100  1.000 29.57733 ? 54  ARG A O   1 
ATOM   371  C CB  . ARG A 1 54  ? 25.39200  4.12700   62.49400  1.000 34.00493 ? 54  ARG A CB  1 
ATOM   372  C CG  . ARG A 1 54  ? 25.52200  4.94000   63.76300  1.000 42.75118 ? 54  ARG A CG  1 
ATOM   373  C CD  . ARG A 1 54  ? 26.96300  5.31700   64.02100  1.000 39.35241 ? 54  ARG A CD  1 
ATOM   374  N NE  . ARG A 1 54  ? 27.74900  4.18200   64.48300  1.000 40.39244 ? 54  ARG A NE  1 
ATOM   375  C CZ  . ARG A 1 54  ? 29.04400  4.24200   64.76400  1.000 42.74978 ? 54  ARG A CZ  1 
ATOM   376  N NH1 . ARG A 1 54  ? 29.72800  5.36800   64.62800  1.000 43.82544 ? 54  ARG A NH1 1 
ATOM   377  N NH2 . ARG A 1 54  ? 29.66800  3.14600   65.18800  1.000 40.32591 ? 54  ARG A NH2 1 
ATOM   378  N N   . PHE A 1 55  ? 22.92100  4.51300   60.49600  1.000 31.41437 ? 55  PHE A N   1 
ATOM   379  C CA  . PHE A 1 55  ? 21.84800  5.31200   59.91400  1.000 29.64603 ? 55  PHE A CA  1 
ATOM   380  C C   . PHE A 1 55  ? 20.48900  4.64500   60.08700  1.000 36.26962 ? 55  PHE A C   1 
ATOM   381  O O   . PHE A 1 55  ? 19.47000  5.33700   60.19200  1.000 35.18467 ? 55  PHE A O   1 
ATOM   382  C CB  . PHE A 1 55  ? 22.12500  5.57600   58.43400  1.000 26.44010 ? 55  PHE A CB  1 
ATOM   383  C CG  . PHE A 1 55  ? 22.80000  6.88800   58.17300  1.000 27.42603 ? 55  PHE A CG  1 
ATOM   384  C CD1 . PHE A 1 55  ? 22.05200  8.04500   58.01400  1.000 26.20629 ? 55  PHE A CD1 1 
ATOM   385  C CD2 . PHE A 1 55  ? 24.18100  6.97300   58.10100  1.000 23.66152 ? 55  PHE A CD2 1 
ATOM   386  C CE1 . PHE A 1 55  ? 22.66300  9.26200   57.77700  1.000 21.87699 ? 55  PHE A CE1 1 
ATOM   387  C CE2 . PHE A 1 55  ? 24.80000  8.18600   57.87000  1.000 23.58323 ? 55  PHE A CE2 1 
ATOM   388  C CZ  . PHE A 1 55  ? 24.03900  9.33400   57.70800  1.000 21.35183 ? 55  PHE A CZ  1 
ATOM   389  N N   . ALA A 1 56  ? 20.44900  3.31500   60.11400  1.000 33.41282 ? 56  ALA A N   1 
ATOM   390  C CA  . ALA A 1 56  ? 19.19100  2.60000   60.27500  1.000 36.42614 ? 56  ALA A CA  1 
ATOM   391  C C   . ALA A 1 56  ? 18.77900  2.44000   61.73100  1.000 41.80253 ? 56  ALA A C   1 
ATOM   392  O O   . ALA A 1 56  ? 17.68200  1.93600   61.99300  1.000 43.33098 ? 56  ALA A O   1 
ATOM   393  C CB  . ALA A 1 56  ? 19.28100  1.22400   59.61700  1.000 36.15810 ? 56  ALA A CB  1 
ATOM   394  N N   . GLY A 1 57  ? 19.62200  2.85000   62.67600  1.000 40.55610 ? 57  GLY A N   1 
ATOM   395  C CA  . GLY A 1 57  ? 19.31800  2.69200   64.08300  1.000 40.52131 ? 57  GLY A CA  1 
ATOM   396  C C   . GLY A 1 57  ? 19.54500  1.30500   64.63800  1.000 38.54196 ? 57  GLY A C   1 
ATOM   397  O O   . GLY A 1 57  ? 19.14500  1.04300   65.77500  1.000 46.07871 ? 57  GLY A O   1 
ATOM   398  N N   . ARG A 1 58  ? 20.16300  0.40200   63.87200  1.000 38.10052 ? 58  ARG A N   1 
ATOM   399  C CA  . ARG A 1 58  ? 20.41000  -0.95000  64.36300  1.000 44.55769 ? 58  ARG A CA  1 
ATOM   400  C C   . ARG A 1 58  ? 21.55400  -1.00300  65.36300  1.000 42.20226 ? 58  ARG A C   1 
ATOM   401  O O   . ARG A 1 58  ? 21.59300  -1.90500  66.20500  1.000 43.68170 ? 58  ARG A O   1 
ATOM   402  C CB  . ARG A 1 58  ? 20.69900  -1.89400  63.20000  1.000 41.66161 ? 58  ARG A CB  1 
ATOM   403  C CG  . ARG A 1 58  ? 19.47500  -2.23400  62.37900  1.000 45.69977 ? 58  ARG A CG  1 
ATOM   404  C CD  . ARG A 1 58  ? 19.81500  -3.25300  61.31600  1.000 47.95647 ? 58  ARG A CD  1 
ATOM   405  N NE  . ARG A 1 58  ? 20.64900  -2.69500  60.25900  1.000 41.60810 ? 58  ARG A NE  1 
ATOM   406  C CZ  . ARG A 1 58  ? 20.17600  -2.12700  59.15800  1.000 47.92051 ? 58  ARG A CZ  1 
ATOM   407  N NH1 . ARG A 1 58  ? 18.87400  -1.97400  58.96400  1.000 42.33873 ? 58  ARG A NH1 1 
ATOM   408  N NH2 . ARG A 1 58  ? 21.02800  -1.70700  58.22600  1.000 44.77347 ? 58  ARG A NH2 1 
ATOM   409  N N   . VAL A 1 59  ? 22.49500  -0.07100  65.27700  1.000 45.13920 ? 59  VAL A N   1 
ATOM   410  C CA  . VAL A 1 59  ? 23.56600  0.03500   66.26200  1.000 44.38635 ? 59  VAL A CA  1 
ATOM   411  C C   . VAL A 1 59  ? 23.57200  1.46500   66.78800  1.000 48.84271 ? 59  VAL A C   1 
ATOM   412  O O   . VAL A 1 59  ? 23.17800  2.39500   66.06800  1.000 43.90291 ? 59  VAL A O   1 
ATOM   413  C CB  . VAL A 1 59  ? 24.93200  -0.35200  65.66500  1.000 44.41528 ? 59  VAL A CB  1 
ATOM   414  C CG1 . VAL A 1 59  ? 24.93000  -1.79900  65.18400  1.000 38.83442 ? 59  VAL A CG1 1 
ATOM   415  C CG2 . VAL A 1 59  ? 25.30300  0.58400   64.53300  1.000 43.55292 ? 59  VAL A CG2 1 
ATOM   416  N N   . PRO A 1 60  ? 23.97300  1.68900   68.03400  1.000 54.33064 ? 60  PRO A N   1 
ATOM   417  C CA  . PRO A 1 60  ? 24.18200  3.05800   68.50600  1.000 53.50144 ? 60  PRO A CA  1 
ATOM   418  C C   . PRO A 1 60  ? 25.47400  3.62800   67.94300  1.000 45.88294 ? 60  PRO A C   1 
ATOM   419  O O   . PRO A 1 60  ? 26.34500  2.90800   67.44900  1.000 50.07901 ? 60  PRO A O   1 
ATOM   420  C CB  . PRO A 1 60  ? 24.26600  2.89700   70.02700  1.000 60.12704 ? 60  PRO A CB  1 
ATOM   421  C CG  . PRO A 1 60  ? 24.84100  1.52200   70.20400  1.000 57.58989 ? 60  PRO A CG  1 
ATOM   422  C CD  . PRO A 1 60  ? 24.25600  0.69100   69.08300  1.000 52.59580 ? 60  PRO A CD  1 
ATOM   423  N N   . GLY A 1 61  ? 25.58500  4.93900   68.01900  1.000 43.98825 ? 61  GLY A N   1 
ATOM   424  C CA  . GLY A 1 61  ? 26.82400  5.59300   67.65000  1.000 41.52372 ? 61  GLY A CA  1 
ATOM   425  C C   . GLY A 1 61  ? 26.57500  6.99400   67.13500  1.000 36.15971 ? 61  GLY A C   1 
ATOM   426  O O   . GLY A 1 61  ? 25.44100  7.44600   66.99900  1.000 40.01474 ? 61  GLY A O   1 
ATOM   427  N N   . ASN A 1 62  ? 27.67900  7.67200   66.84500  1.000 32.08441 ? 62  ASN A N   1 
ATOM   428  C CA  . ASN A 1 62  ? 27.64700  9.05200   66.39400  1.000 29.76458 ? 62  ASN A CA  1 
ATOM   429  C C   . ASN A 1 62  ? 27.52900  9.10700   64.87700  1.000 31.02567 ? 62  ASN A C   1 
ATOM   430  O O   . ASN A 1 62  ? 28.13500  8.30300   64.16400  1.000 26.66575 ? 62  ASN A O   1 
ATOM   431  C CB  . ASN A 1 62  ? 28.90700  9.78300   66.85800  1.000 27.31019 ? 62  ASN A CB  1 
ATOM   432  C CG  . ASN A 1 62  ? 29.12300  9.67300   68.35800  1.000 30.05125 ? 62  ASN A CG  1 
ATOM   433  O OD1 . ASN A 1 62  ? 28.17200  9.76900   69.13700  1.000 24.98810 ? 62  ASN A OD1 1 
ATOM   434  N ND2 . ASN A 1 62  ? 30.37300  9.45200   68.76900  1.000 19.35107 ? 62  ASN A ND2 1 
ATOM   435  N N   . ILE A 1 63  ? 26.72900  10.05200  64.38700  1.000 29.92748 ? 63  ILE A N   1 
ATOM   436  C CA  . ILE A 1 63  ? 26.58800  10.25500  62.94900  1.000 29.45277 ? 63  ILE A CA  1 
ATOM   437  C C   . ILE A 1 63  ? 26.94200  11.69500  62.60600  1.000 29.49617 ? 63  ILE A C   1 
ATOM   438  O O   . ILE A 1 63  ? 27.83500  11.95400  61.79000  1.000 29.06456 ? 63  ILE A O   1 
ATOM   439  C CB  . ILE A 1 63  ? 25.16700  9.92000   62.46000  1.000 30.22020 ? 63  ILE A CB  1 
ATOM   440  C CG1 . ILE A 1 63  ? 24.81900  8.46300   62.76200  1.000 31.03246 ? 63  ILE A CG1 1 
ATOM   441  C CG2 . ILE A 1 63  ? 25.05300  10.19100  60.96600  1.000 29.05222 ? 63  ILE A CG2 1 
ATOM   442  C CD1 . ILE A 1 63  ? 23.42300  8.07300   62.32200  1.000 33.78879 ? 63  ILE A CD1 1 
ATOM   443  N N   . TYR A 1 64  ? 26.24900  12.63900  63.23500  1.000 26.31420 ? 64  TYR A N   1 
ATOM   444  C CA  . TYR A 1 64  ? 26.38000  14.04300  62.89400  1.000 26.83800 ? 64  TYR A CA  1 
ATOM   445  C C   . TYR A 1 64  ? 26.20800  14.87200  64.16000  1.000 24.80663 ? 64  TYR A C   1 
ATOM   446  O O   . TYR A 1 64  ? 25.31800  14.59600  64.96900  1.000 25.84144 ? 64  TYR A O   1 
ATOM   447  C CB  . TYR A 1 64  ? 25.34700  14.43000  61.82800  1.000 28.16170 ? 64  TYR A CB  1 
ATOM   448  C CG  . TYR A 1 64  ? 25.65900  15.71800  61.10600  1.000 29.36983 ? 64  TYR A CG  1 
ATOM   449  C CD1 . TYR A 1 64  ? 26.57100  15.74700  60.05600  1.000 25.52916 ? 64  TYR A CD1 1 
ATOM   450  C CD2 . TYR A 1 64  ? 25.04000  16.90400  61.46800  1.000 31.56013 ? 64  TYR A CD2 1 
ATOM   451  C CE1 . TYR A 1 64  ? 26.86100  16.93000  59.39000  1.000 27.23739 ? 64  TYR A CE1 1 
ATOM   452  C CE2 . TYR A 1 64  ? 25.32600  18.08800  60.81100  1.000 33.35403 ? 64  TYR A CE2 1 
ATOM   453  C CZ  . TYR A 1 64  ? 26.23100  18.09400  59.77300  1.000 29.41941 ? 64  TYR A CZ  1 
ATOM   454  O OH  . TYR A 1 64  ? 26.50100  19.27500  59.12900  1.000 23.78839 ? 64  TYR A OH  1 
ATOM   455  N N   . ALA A 1 65  ? 27.05200  15.90000  64.31300  1.000 22.84284 ? 65  ALA A N   1 
ATOM   456  C CA  . ALA A 1 65  ? 27.09500  16.66400  65.56100  1.000 29.05624 ? 65  ALA A CA  1 
ATOM   457  C C   . ALA A 1 65  ? 25.78800  17.38600  65.86500  1.000 26.94629 ? 65  ALA A C   1 
ATOM   458  O O   . ALA A 1 65  ? 25.51100  17.67900  67.03500  1.000 24.69044 ? 65  ALA A O   1 
ATOM   459  C CB  . ALA A 1 65  ? 28.23600  17.67900  65.52700  1.000 24.59195 ? 65  ALA A CB  1 
ATOM   460  N N   . ARG A 1 66  ? 24.98200  17.69600  64.84900  1.000 26.51751 ? 66  ARG A N   1 
ATOM   461  C CA  . ARG A 1 66  ? 23.66900  18.26200  65.13000  1.000 27.28298 ? 66  ARG A CA  1 
ATOM   462  C C   . ARG A 1 66  ? 22.78000  17.25500  65.85600  1.000 29.60754 ? 66  ARG A C   1 
ATOM   463  O O   . ARG A 1 66  ? 21.86500  17.65100  66.58800  1.000 28.32448 ? 66  ARG A O   1 
ATOM   464  C CB  . ARG A 1 66  ? 23.01500  18.73800  63.83200  1.000 24.65250 ? 66  ARG A CB  1 
ATOM   465  C CG  . ARG A 1 66  ? 22.27400  20.07100  63.94500  1.000 21.18776 ? 66  ARG A CG  1 
ATOM   466  C CD  . ARG A 1 66  ? 21.76900  20.55100  62.57600  1.000 23.92682 ? 66  ARG A CD  1 
ATOM   467  N NE  . ARG A 1 66  ? 21.04500  19.49500  61.87800  1.000 35.42941 ? 66  ARG A NE  1 
ATOM   468  C CZ  . ARG A 1 66  ? 21.48100  18.86700  60.79500  1.000 27.81810 ? 66  ARG A CZ  1 
ATOM   469  N NH1 . ARG A 1 66  ? 22.60000  19.22900  60.18800  1.000 24.31140 ? 66  ARG A NH1 1 
ATOM   470  N NH2 . ARG A 1 66  ? 20.77200  17.85700  60.30400  1.000 31.80781 ? 66  ARG A NH2 1 
ATOM   471  N N   . PHE A 1 67  ? 23.04300  15.95500  65.68300  1.000 31.76670 ? 67  PHE A N   1 
ATOM   472  C CA  . PHE A 1 67  ? 22.31500  14.90100  66.38500  1.000 31.54055 ? 67  PHE A CA  1 
ATOM   473  C C   . PHE A 1 67  ? 22.99100  14.53700  67.70300  1.000 30.43290 ? 67  PHE A C   1 
ATOM   474  O O   . PHE A 1 67  ? 22.33900  14.44200  68.74900  1.000 26.51822 ? 67  PHE A O   1 
ATOM   475  C CB  . PHE A 1 67  ? 22.21600  13.63000  65.52300  1.000 31.63018 ? 67  PHE A CB  1 
ATOM   476  C CG  . PHE A 1 67  ? 21.62700  13.83700  64.15000  1.000 36.98225 ? 67  PHE A CG  1 
ATOM   477  C CD1 . PHE A 1 67  ? 20.87900  14.96200  63.84200  1.000 34.15864 ? 67  PHE A CD1 1 
ATOM   478  C CD2 . PHE A 1 67  ? 21.81700  12.87700  63.16300  1.000 38.34479 ? 67  PHE A CD2 1 
ATOM   479  C CE1 . PHE A 1 67  ? 20.33200  15.13100  62.57300  1.000 33.81393 ? 67  PHE A CE1 1 
ATOM   480  C CE2 . PHE A 1 67  ? 21.27800  13.03900  61.89400  1.000 39.90093 ? 67  PHE A CE2 1 
ATOM   481  C CZ  . PHE A 1 67  ? 20.53400  14.16800  61.60000  1.000 37.52095 ? 67  PHE A CZ  1 
ATOM   482  N N   . THR A 1 68  ? 24.29700  14.30200  67.65200  1.000 25.10677 ? 68  THR A N   1 
ATOM   483  C CA  . THR A 1 68  ? 25.04000  13.75200  68.77700  1.000 25.47194 ? 68  THR A CA  1 
ATOM   484  C C   . THR A 1 68  ? 26.43000  14.35300  68.75800  1.000 24.54879 ? 68  THR A C   1 
ATOM   485  O O   . THR A 1 68  ? 27.14300  14.22800  67.75900  1.000 33.91284 ? 68  THR A O   1 
ATOM   486  C CB  . THR A 1 68  ? 25.14300  12.22900  68.68200  1.000 31.99553 ? 68  THR A CB  1 
ATOM   487  O OG1 . THR A 1 68  ? 25.67600  11.87900  67.39600  1.000 33.82115 ? 68  THR A OG1 1 
ATOM   488  C CG2 . THR A 1 68  ? 23.78600  11.56500  68.87600  1.000 31.69362 ? 68  THR A CG2 1 
ATOM   489  N N   . ASN A 1 69  ? 26.81800  14.99200  69.85000  1.000 23.78568 ? 69  ASN A N   1 
ATOM   490  C CA  . ASN A 1 69  ? 28.19700  15.38900  70.04100  1.000 23.19752 ? 69  ASN A CA  1 
ATOM   491  C C   . ASN A 1 69  ? 28.59400  14.95300  71.44500  1.000 20.81894 ? 69  ASN A C   1 
ATOM   492  O O   . ASN A 1 69  ? 27.84700  15.21100  72.40700  1.000 21.25439 ? 69  ASN A O   1 
ATOM   493  C CB  . ASN A 1 69  ? 28.40100  16.90300  69.85700  1.000 20.50438 ? 69  ASN A CB  1 
ATOM   494  C CG  . ASN A 1 69  ? 29.84700  17.31900  70.06700  1.000 20.67769 ? 69  ASN A CG  1 
ATOM   495  O OD1 . ASN A 1 69  ? 30.33400  17.35300  71.19900  1.000 18.78468 ? 69  ASN A OD1 1 
ATOM   496  N ND2 . ASN A 1 69  ? 30.54400  17.62900  68.97700  1.000 21.57078 ? 69  ASN A ND2 1 
ATOM   497  N N   . PRO A 1 70  ? 29.73400  14.27700  71.60500  1.000 17.07074 ? 70  PRO A N   1 
ATOM   498  C CA  . PRO A 1 70  ? 30.09200  13.76700  72.93900  1.000 18.33462 ? 70  PRO A CA  1 
ATOM   499  C C   . PRO A 1 70  ? 30.19700  14.85300  73.99800  1.000 17.72381 ? 70  PRO A C   1 
ATOM   500  O O   . PRO A 1 70  ? 29.73200  14.65000  75.12700  1.000 18.30442 ? 70  PRO A O   1 
ATOM   501  C CB  . PRO A 1 70  ? 31.43700  13.06800  72.69100  1.000 20.81170 ? 70  PRO A CB  1 
ATOM   502  C CG  . PRO A 1 70  ? 31.43200  12.74500  71.21100  1.000 20.88156 ? 70  PRO A CG  1 
ATOM   503  C CD  . PRO A 1 70  ? 30.70800  13.88500  70.57100  1.000 17.92152 ? 70  PRO A CD  1 
ATOM   504  N N   . THR A 1 71  ? 30.76900  16.01200  73.66700  1.000 17.44604 ? 71  THR A N   1 
ATOM   505  C CA  . THR A 1 71  ? 30.88100  17.07500  74.66100  1.000 15.19729 ? 71  THR A CA  1 
ATOM   506  C C   . THR A 1 71  ? 29.50300  17.57000  75.09000  1.000 20.47787 ? 71  THR A C   1 
ATOM   507  O O   . THR A 1 71  ? 29.24200  17.75100  76.28800  1.000 15.67481 ? 71  THR A O   1 
ATOM   508  C CB  . THR A 1 71  ? 31.72800  18.22500  74.11100  1.000 15.07514 ? 71  THR A CB  1 
ATOM   509  O OG1 . THR A 1 71  ? 32.95300  17.70300  73.58900  1.000 14.87184 ? 71  THR A OG1 1 
ATOM   510  C CG2 . THR A 1 71  ? 32.05300  19.21700  75.21300  1.000 12.95721 ? 71  THR A CG2 1 
ATOM   511  N N   . VAL A 1 72  ? 28.60200  17.77100  74.12700  1.000 16.46975 ? 72  VAL A N   1 
ATOM   512  C CA  . VAL A 1 72  ? 27.23500  18.17600  74.44700  1.000 16.58972 ? 72  VAL A CA  1 
ATOM   513  C C   . VAL A 1 72  ? 26.52200  17.07900  75.23200  1.000 18.17762 ? 72  VAL A C   1 
ATOM   514  O O   . VAL A 1 72  ? 25.73000  17.35800  76.14100  1.000 16.03769 ? 72  VAL A O   1 
ATOM   515  C CB  . VAL A 1 72  ? 26.47300  18.53600  73.15700  1.000 13.86962 ? 72  VAL A CB  1 
ATOM   516  C CG1 . VAL A 1 72  ? 25.04600  18.94600  73.48100  1.000 16.32229 ? 72  VAL A CG1 1 
ATOM   517  C CG2 . VAL A 1 72  ? 27.19300  19.64000  72.39900  1.000 14.66845 ? 72  VAL A CG2 1 
ATOM   518  N N   . ARG A 1 73  ? 26.78800  15.81600  74.89200  1.000 19.12330 ? 73  ARG A N   1 
ATOM   519  C CA  . ARG A 1 73  ? 26.16300  14.71400  75.61300  1.000 18.31652 ? 73  ARG A CA  1 
ATOM   520  C C   . ARG A 1 73  ? 26.55900  14.72900  77.08200  1.000 19.09808 ? 73  ARG A C   1 
ATOM   521  O O   . ARG A 1 73  ? 25.72000  14.49800  77.95900  1.000 19.29061 ? 73  ARG A O   1 
ATOM   522  C CB  . ARG A 1 73  ? 26.54200  13.38400  74.97500  1.000 19.89847 ? 73  ARG A CB  1 
ATOM   523  C CG  . ARG A 1 73  ? 26.07100  12.17600  75.76000  1.000 24.59012 ? 73  ARG A CG  1 
ATOM   524  C CD  . ARG A 1 73  ? 26.79000  10.92900  75.29100  1.000 28.28192 ? 73  ARG A CD  1 
ATOM   525  N NE  . ARG A 1 73  ? 26.47800  9.77500   76.12300  1.000 30.66825 ? 73  ARG A NE  1 
ATOM   526  C CZ  . ARG A 1 73  ? 26.96500  8.55700   75.92300  1.000 35.61058 ? 73  ARG A CZ  1 
ATOM   527  N NH1 . ARG A 1 73  ? 27.81400  8.30400   74.93800  1.000 30.60603 ? 73  ARG A NH1 1 
ATOM   528  N NH2 . ARG A 1 73  ? 26.58800  7.56700   76.72700  1.000 29.49165 ? 73  ARG A NH2 1 
ATOM   529  N N   . THR A 1 74  ? 27.82900  15.01500  77.37100  1.000 15.89886 ? 74  THR A N   1 
ATOM   530  C CA  . THR A 1 74  ? 28.25500  15.09600  78.76300  1.000 17.53827 ? 74  THR A CA  1 
ATOM   531  C C   . THR A 1 74  ? 27.46800  16.16600  79.51000  1.000 18.77193 ? 74  THR A C   1 
ATOM   532  O O   . THR A 1 74  ? 27.02400  15.94200  80.64100  1.000 19.52175 ? 74  THR A O   1 
ATOM   533  C CB  . THR A 1 74  ? 29.75700  15.37800  78.83700  1.000 15.32552 ? 74  THR A CB  1 
ATOM   534  O OG1 . THR A 1 74  ? 30.48100  14.26400  78.30500  1.000 20.50127 ? 74  THR A OG1 1 
ATOM   535  C CG2 . THR A 1 74  ? 30.19200  15.61800  80.27400  1.000 13.66042 ? 74  THR A CG2 1 
ATOM   536  N N   . PHE A 1 75  ? 27.27100  17.33000  78.88500  1.000 12.58898 ? 75  PHE A N   1 
ATOM   537  C CA  . PHE A 1 75  ? 26.51000  18.39800  79.52600  1.000 15.85766 ? 75  PHE A CA  1 
ATOM   538  C C   . PHE A 1 75  ? 25.05300  18.00300  79.73700  1.000 15.78966 ? 75  PHE A C   1 
ATOM   539  O O   . PHE A 1 75  ? 24.47500  18.28900  80.79300  1.000 16.82019 ? 75  PHE A O   1 
ATOM   540  C CB  . PHE A 1 75  ? 26.60200  19.68000  78.69300  1.000 17.08009 ? 75  PHE A CB  1 
ATOM   541  C CG  . PHE A 1 75  ? 25.65200  20.75500  79.13200  1.000 15.60002 ? 75  PHE A CG  1 
ATOM   542  C CD1 . PHE A 1 75  ? 25.81200  21.38200  80.35700  1.000 14.93326 ? 75  PHE A CD1 1 
ATOM   543  C CD2 . PHE A 1 75  ? 24.59900  21.13800  78.32100  1.000 14.10421 ? 75  PHE A CD2 1 
ATOM   544  C CE1 . PHE A 1 75  ? 24.94100  22.36700  80.76800  1.000 16.74062 ? 75  PHE A CE1 1 
ATOM   545  C CE2 . PHE A 1 75  ? 23.72200  22.12900  78.72700  1.000 20.94015 ? 75  PHE A CE2 1 
ATOM   546  C CZ  . PHE A 1 75  ? 23.89300  22.74300  79.95200  1.000 16.08221 ? 75  PHE A CZ  1 
ATOM   547  N N   . GLU A 1 76  ? 24.44300  17.35300  78.74200  1.000 14.65626 ? 76  GLU A N   1 
ATOM   548  C CA  . GLU A 1 76  ? 23.03000  16.99400  78.83300  1.000 14.85405 ? 76  GLU A CA  1 
ATOM   549  C C   . GLU A 1 76  ? 22.78300  15.99900  79.95700  1.000 16.60457 ? 76  GLU A C   1 
ATOM   550  O O   . GLU A 1 76  ? 21.87300  16.17900  80.77500  1.000 15.57649 ? 76  GLU A O   1 
ATOM   551  C CB  . GLU A 1 76  ? 22.55300  16.41500  77.50100  1.000 18.17619 ? 76  GLU A CB  1 
ATOM   552  C CG  . GLU A 1 76  ? 22.53500  17.42300  76.36400  1.000 18.14046 ? 76  GLU A CG  1 
ATOM   553  C CD  . GLU A 1 76  ? 22.13100  16.80600  75.03800  1.000 21.73665 ? 76  GLU A CD  1 
ATOM   554  O OE1 . GLU A 1 76  ? 22.37600  15.59400  74.83200  1.000 23.37104 ? 76  GLU A OE1 1 
ATOM   555  O OE2 . GLU A 1 76  ? 21.56100  17.53800  74.20100  1.000 19.93639 ? 76  GLU A OE2 1 
ATOM   556  N N   . GLU A 1 77  ? 23.58600  14.93600  80.00800  1.000 15.03511 ? 77  GLU A N   1 
ATOM   557  C CA  . GLU A 1 77  ? 23.40500  13.91300  81.03100  1.000 17.71879 ? 77  GLU A CA  1 
ATOM   558  C C   . GLU A 1 77  ? 23.67400  14.46600  82.42300  1.000 19.08925 ? 77  GLU A C   1 
ATOM   559  O O   . GLU A 1 77  ? 22.95800  14.14000  83.37800  1.000 21.04708 ? 77  GLU A O   1 
ATOM   560  C CB  . GLU A 1 77  ? 24.31300  12.72100  80.73800  1.000 15.76501 ? 77  GLU A CB  1 
ATOM   561  C CG  . GLU A 1 77  ? 23.97200  12.02200  79.43500  1.000 20.76994 ? 77  GLU A CG  1 
ATOM   562  C CD  . GLU A 1 77  ? 24.91100  10.87400  79.12000  1.000 22.22834 ? 77  GLU A CD  1 
ATOM   563  O OE1 . GLU A 1 77  ? 25.85200  10.63600  79.90300  1.000 22.98744 ? 77  GLU A OE1 1 
ATOM   564  O OE2 . GLU A 1 77  ? 24.70700  10.21100  78.08400  1.000 28.07463 ? 77  GLU A OE2 1 
ATOM   565  N N   . ARG A 1 78  ? 24.70600  15.29800  82.56100  1.000 16.86090 ? 78  ARG A N   1 
ATOM   566  C CA  . ARG A 1 78  ? 25.00700  15.89100  83.85900  1.000 19.12923 ? 78  ARG A CA  1 
ATOM   567  C C   . ARG A 1 78  ? 23.86800  16.79100  84.33100  1.000 18.15064 ? 78  ARG A C   1 
ATOM   568  O O   . ARG A 1 78  ? 23.43700  16.71100  85.48700  1.000 22.87227 ? 78  ARG A O   1 
ATOM   569  C CB  . ARG A 1 78  ? 26.32400  16.66400  83.77800  1.000 14.96461 ? 78  ARG A CB  1 
ATOM   570  C CG  . ARG A 1 78  ? 26.83900  17.19600  85.10200  1.000 16.00524 ? 78  ARG A CG  1 
ATOM   571  C CD  . ARG A 1 78  ? 28.23700  17.78700  84.93500  1.000 19.98935 ? 78  ARG A CD  1 
ATOM   572  N NE  . ARG A 1 78  ? 29.24900  16.77400  84.64500  1.000 17.34157 ? 78  ARG A NE  1 
ATOM   573  C CZ  . ARG A 1 78  ? 30.55600  17.00600  84.59900  1.000 21.65038 ? 78  ARG A CZ  1 
ATOM   574  N NH1 . ARG A 1 78  ? 31.05200  18.22200  84.77000  1.000 19.69886 ? 78  ARG A NH1 1 
ATOM   575  N NH2 . ARG A 1 78  ? 31.39000  15.99100  84.38900  1.000 17.78757 ? 78  ARG A NH2 1 
ATOM   576  N N   . LEU A 1 79  ? 23.35300  17.64900  83.44500  1.000 19.42402 ? 79  LEU A N   1 
ATOM   577  C CA  . LEU A 1 79  ? 22.27200  18.54300  83.84900  1.000 15.92829 ? 79  LEU A CA  1 
ATOM   578  C C   . LEU A 1 79  ? 20.99800  17.76600  84.15600  1.000 18.99645 ? 79  LEU A C   1 
ATOM   579  O O   . LEU A 1 79  ? 20.32500  18.03900  85.15700  1.000 20.49907 ? 79  LEU A O   1 
ATOM   580  C CB  . LEU A 1 79  ? 22.01300  19.58200  82.76900  1.000 15.51314 ? 79  LEU A CB  1 
ATOM   581  C CG  . LEU A 1 79  ? 20.89400  20.56900  83.09600  1.000 21.63644 ? 79  LEU A CG  1 
ATOM   582  C CD1 . LEU A 1 79  ? 21.23300  21.38300  84.33900  1.000 16.69306 ? 79  LEU A CD1 1 
ATOM   583  C CD2 . LEU A 1 79  ? 20.65600  21.48300  81.91300  1.000 17.76961 ? 79  LEU A CD2 1 
ATOM   584  N N   . ALA A 1 80  ? 20.66200  16.78100  83.32000  1.000 20.20818 ? 80  ALA A N   1 
ATOM   585  C CA  . ALA A 1 80  ? 19.48200  15.96000  83.58300  1.000 22.39394 ? 80  ALA A CA  1 
ATOM   586  C C   . ALA A 1 80  ? 19.58600  15.27100  84.93600  1.000 22.60515 ? 80  ALA A C   1 
ATOM   587  O O   . ALA A 1 80  ? 18.61700  15.24000  85.70400  1.000 20.72233 ? 80  ALA A O   1 
ATOM   588  C CB  . ALA A 1 80  ? 19.30000  14.92100  82.47900  1.000 16.59690 ? 80  ALA A CB  1 
ATOM   589  N N   . ALA A 1 81  ? 20.76400  14.72700  85.24800  1.000 20.68247 ? 81  ALA A N   1 
ATOM   590  C CA  . ALA A 1 81  ? 20.95800  14.07600  86.53600  1.000 18.89211 ? 81  ALA A CA  1 
ATOM   591  C C   . ALA A 1 81  ? 20.79800  15.05600  87.69600  1.000 20.82742 ? 81  ALA A C   1 
ATOM   592  O O   . ALA A 1 81  ? 20.32600  14.66600  88.76800  1.000 28.21109 ? 81  ALA A O   1 
ATOM   593  C CB  . ALA A 1 81  ? 22.33200  13.40600  86.57200  1.000 16.44290 ? 81  ALA A CB  1 
ATOM   594  N N   . LEU A 1 82  ? 21.18300  16.32500  87.51000  1.000 17.58043 ? 82  LEU A N   1 
ATOM   595  C CA  . LEU A 1 82  ? 20.98900  17.31200  88.57200  1.000 18.63469 ? 82  LEU A CA  1 
ATOM   596  C C   . LEU A 1 82  ? 19.52700  17.70100  88.72300  1.000 17.73932 ? 82  LEU A C   1 
ATOM   597  O O   . LEU A 1 82  ? 19.10200  18.08700  89.81600  1.000 23.86986 ? 82  LEU A O   1 
ATOM   598  C CB  . LEU A 1 82  ? 21.82000  18.56500  88.31100  1.000 17.82690 ? 82  LEU A CB  1 
ATOM   599  C CG  . LEU A 1 82  ? 23.33200  18.42100  88.44600  1.000 20.79020 ? 82  LEU A CG  1 
ATOM   600  C CD1 . LEU A 1 82  ? 24.01900  19.73200  88.11600  1.000 14.80332 ? 82  LEU A CD1 1 
ATOM   601  C CD2 . LEU A 1 82  ? 23.68800  17.95900  89.85000  1.000 20.56421 ? 82  LEU A CD2 1 
ATOM   602  N N   . GLU A 1 83  ? 18.75400  17.64800  87.63900  1.000 19.59454 ? 83  GLU A N   1 
ATOM   603  C CA  . GLU A 1 83  ? 17.32800  17.92900  87.71100  1.000 21.32087 ? 83  GLU A CA  1 
ATOM   604  C C   . GLU A 1 83  ? 16.50900  16.72000  88.13700  1.000 23.19872 ? 83  GLU A C   1 
ATOM   605  O O   . GLU A 1 83  ? 15.31200  16.87100  88.39500  1.000 23.22444 ? 83  GLU A O   1 
ATOM   606  C CB  . GLU A 1 83  ? 16.80900  18.42100  86.35700  1.000 23.76444 ? 83  GLU A CB  1 
ATOM   607  C CG  . GLU A 1 83  ? 17.12200  19.86800  86.03500  1.000 27.50729 ? 83  GLU A CG  1 
ATOM   608  C CD  . GLU A 1 83  ? 16.38800  20.83900  86.93800  1.000 26.95341 ? 83  GLU A CD  1 
ATOM   609  O OE1 . GLU A 1 83  ? 15.46100  20.41500  87.66100  1.000 25.70448 ? 83  GLU A OE1 1 
ATOM   610  O OE2 . GLU A 1 83  ? 16.74700  22.03000  86.92600  1.000 27.54320 ? 83  GLU A OE2 1 
ATOM   611  N N   . GLY A 1 84  ? 17.11700  15.53700  88.21200  1.000 24.52521 ? 84  GLY A N   1 
ATOM   612  C CA  . GLY A 1 84  ? 16.36100  14.31900  88.41100  1.000 22.78426 ? 84  GLY A CA  1 
ATOM   613  C C   . GLY A 1 84  ? 15.63000  13.83400  87.18100  1.000 23.53221 ? 84  GLY A C   1 
ATOM   614  O O   . GLY A 1 84  ? 14.74900  12.97800  87.29400  1.000 28.72019 ? 84  GLY A O   1 
ATOM   615  N N   . ALA A 1 85  ? 15.97000  14.35200  86.00700  1.000 24.44187 ? 85  ALA A N   1 
ATOM   616  C CA  . ALA A 1 85  ? 15.27800  14.01100  84.77300  1.000 25.48871 ? 85  ALA A CA  1 
ATOM   617  C C   . ALA A 1 85  ? 15.91600  12.80300  84.11100  1.000 22.74463 ? 85  ALA A C   1 
ATOM   618  O O   . ALA A 1 85  ? 17.11500  12.55200  84.25700  1.000 23.95329 ? 85  ALA A O   1 
ATOM   619  C CB  . ALA A 1 85  ? 15.29100  15.18900  83.79400  1.000 24.23616 ? 85  ALA A CB  1 
ATOM   620  N N   . GLU A 1 86  ? 15.09400  12.05200  83.37300  1.000 23.23829 ? 86  GLU A N   1 
ATOM   621  C CA  . GLU A 1 86  ? 15.61800  10.93500  82.59300  1.000 26.21187 ? 86  GLU A CA  1 
ATOM   622  C C   . GLU A 1 86  ? 16.53900  11.41900  81.48100  1.000 26.94436 ? 86  GLU A C   1 
ATOM   623  O O   . GLU A 1 86  ? 17.58300  10.80700  81.22000  1.000 24.25601 ? 86  GLU A O   1 
ATOM   624  C CB  . GLU A 1 86  ? 14.47000  10.10800  82.01100  1.000 22.14673 ? 86  GLU A CB  1 
ATOM   625  C CG  . GLU A 1 86  ? 13.76700  9.21500   83.02200  1.000 25.48884 ? 86  GLU A CG  1 
ATOM   626  C CD  . GLU A 1 86  ? 12.59400  8.45800   82.42000  1.000 26.24098 ? 86  GLU A CD  1 
ATOM   627  O OE1 . GLU A 1 86  ? 12.31200  8.64100   81.21400  1.000 23.12431 ? 86  GLU A OE1 1 
ATOM   628  O OE2 . GLU A 1 86  ? 11.95200  7.67500   83.15400  1.000 33.67335 ? 86  GLU A OE2 1 
ATOM   629  N N   . ALA A 1 87  ? 16.17300  12.51700  80.81900  1.000 25.50736 ? 87  ALA A N   1 
ATOM   630  C CA  . ALA A 1 87  ? 16.84000  12.93500  79.59500  1.000 27.31113 ? 87  ALA A CA  1 
ATOM   631  C C   . ALA A 1 87  ? 16.93100  14.45300  79.53800  1.000 27.80364 ? 87  ALA A C   1 
ATOM   632  O O   . ALA A 1 87  ? 16.18200  15.17400  80.20300  1.000 21.18043 ? 87  ALA A O   1 
ATOM   633  C CB  . ALA A 1 87  ? 16.11100  12.40800  78.35100  1.000 21.58104 ? 87  ALA A CB  1 
ATOM   634  N N   . CYS A 1 88  ? 17.86500  14.92900  78.71900  1.000 27.10577 ? 88  CYS A N   1 
ATOM   635  C CA  . CYS A 1 88  ? 18.04000  16.35200  78.48800  1.000 19.34859 ? 88  CYS A CA  1 
ATOM   636  C C   . CYS A 1 88  ? 18.54900  16.55400  77.06800  1.000 23.66869 ? 88  CYS A C   1 
ATOM   637  O O   . CYS A 1 88  ? 19.35600  15.76000  76.57600  1.000 23.64116 ? 88  CYS A O   1 
ATOM   638  C CB  . CYS A 1 88  ? 19.01500  16.95200  79.50100  1.000 20.12049 ? 88  CYS A CB  1 
ATOM   639  S SG  . CYS A 1 88  ? 19.47000  18.65900  79.18100  1.000 23.74157 ? 88  CYS A SG  1 
ATOM   640  N N   . VAL A 1 89  ? 18.07200  17.60600  76.40800  1.000 21.35890 ? 89  VAL A N   1 
ATOM   641  C CA  . VAL A 1 89  ? 18.58300  18.00000  75.10100  1.000 19.74184 ? 89  VAL A CA  1 
ATOM   642  C C   . VAL A 1 89  ? 19.02400  19.45800  75.18000  1.000 22.00388 ? 89  VAL A C   1 
ATOM   643  O O   . VAL A 1 89  ? 18.27200  20.32200  75.64800  1.000 18.97212 ? 89  VAL A O   1 
ATOM   644  C CB  . VAL A 1 89  ? 17.55100  17.77400  73.97700  1.000 22.33819 ? 89  VAL A CB  1 
ATOM   645  C CG1 . VAL A 1 89  ? 16.28600  18.59200  74.20200  1.000 21.27714 ? 89  VAL A CG1 1 
ATOM   646  C CG2 . VAL A 1 89  ? 18.17400  18.07800  72.61400  1.000 17.44108 ? 89  VAL A CG2 1 
ATOM   647  N N   . ALA A 1 90  ? 20.25400  19.71800  74.75300  1.000 15.13163 ? 90  ALA A N   1 
ATOM   648  C CA  . ALA A 1 90  ? 20.84000  21.04200  74.85900  1.000 18.84742 ? 90  ALA A CA  1 
ATOM   649  C C   . ALA A 1 90  ? 20.47500  21.88800  73.64600  1.000 18.29611 ? 90  ALA A C   1 
ATOM   650  O O   . ALA A 1 90  ? 20.15600  21.37200  72.57300  1.000 17.72727 ? 90  ALA A O   1 
ATOM   651  C CB  . ALA A 1 90  ? 22.35800  20.94100  74.99500  1.000 14.91050 ? 90  ALA A CB  1 
ATOM   652  N N   . THR A 1 91  ? 20.52800  23.20800  73.82800  1.000 15.71296 ? 91  THR A N   1 
ATOM   653  C CA  . THR A 1 91  ? 20.15300  24.15000  72.78200  1.000 17.80989 ? 91  THR A CA  1 
ATOM   654  C C   . THR A 1 91  ? 21.12800  25.31900  72.76000  1.000 18.46222 ? 91  THR A C   1 
ATOM   655  O O   . THR A 1 91  ? 21.85300  25.57500  73.72500  1.000 17.50548 ? 91  THR A O   1 
ATOM   656  C CB  . THR A 1 91  ? 18.73100  24.69300  72.96600  1.000 18.01387 ? 91  THR A CB  1 
ATOM   657  O OG1 . THR A 1 91  ? 18.64900  25.39700  74.21200  1.000 16.87002 ? 91  THR A OG1 1 
ATOM   658  C CG2 . THR A 1 91  ? 17.69400  23.55800  72.92800  1.000 16.32752 ? 91  THR A CG2 1 
ATOM   659  N N   . ALA A 1 92  ? 21.10400  26.05000  71.64000  1.000 16.40533 ? 92  ALA A N   1 
ATOM   660  C CA  . ALA A 1 92  ? 22.05500  27.13500  71.42100  1.000 17.28218 ? 92  ALA A CA  1 
ATOM   661  C C   . ALA A 1 92  ? 21.91400  28.24700  72.45100  1.000 21.07896 ? 92  ALA A C   1 
ATOM   662  O O   . ALA A 1 92  ? 22.88600  28.95800  72.72400  1.000 22.12305 ? 92  ALA A O   1 
ATOM   663  C CB  . ALA A 1 92  ? 21.88100  27.70100  70.01200  1.000 18.18478 ? 92  ALA A CB  1 
ATOM   664  N N   . SER A 1 93  ? 20.72500  28.42600  73.02200  1.000 19.54113 ? 93  SER A N   1 
ATOM   665  C CA  . SER A 1 93  ? 20.50900  29.46200  74.02600  1.000 19.68586 ? 93  SER A CA  1 
ATOM   666  C C   . SER A 1 93  ? 19.27300  29.10300  74.83400  1.000 18.64883 ? 93  SER A C   1 
ATOM   667  O O   . SER A 1 93  ? 18.53700  28.17000  74.50100  1.000 16.19398 ? 93  SER A O   1 
ATOM   668  C CB  . SER A 1 93  ? 20.34200  30.84800  73.39300  1.000 19.51832 ? 93  SER A CB  1 
ATOM   669  O OG  . SER A 1 93  ? 19.09200  30.94800  72.73200  1.000 20.02990 ? 93  SER A OG  1 
ATOM   670  N N   . GLY A 1 94  ? 19.05500  29.86700  75.90900  1.000 16.24288 ? 94  GLY A N   1 
ATOM   671  C CA  . GLY A 1 94  ? 17.84700  29.68200  76.69500  1.000 17.93922 ? 94  GLY A CA  1 
ATOM   672  C C   . GLY A 1 94  ? 16.58800  29.89400  75.87600  1.000 20.61972 ? 94  GLY A C   1 
ATOM   673  O O   . GLY A 1 94  ? 15.63400  29.11700  75.97600  1.000 17.35439 ? 94  GLY A O   1 
ATOM   674  N N   . MET A 1 95  ? 16.57500  30.93800  75.04000  1.000 18.79143 ? 95  MET A N   1 
ATOM   675  C CA  . MET A 1 95  ? 15.41500  31.17500  74.18600  1.000 20.14075 ? 95  MET A CA  1 
ATOM   676  C C   . MET A 1 95  ? 15.18200  30.00200  73.24400  1.000 18.77831 ? 95  MET A C   1 
ATOM   677  O O   . MET A 1 95  ? 14.03500  29.60400  73.00700  1.000 18.69037 ? 95  MET A O   1 
ATOM   678  C CB  . MET A 1 95  ? 15.58400  32.47600  73.39800  1.000 19.10682 ? 95  MET A CB  1 
ATOM   679  C CG  . MET A 1 95  ? 15.43400  33.74400  74.23300  1.000 21.60816 ? 95  MET A CG  1 
ATOM   680  S SD  . MET A 1 95  ? 14.05400  33.67200  75.40900  1.000 20.92729 ? 95  MET A SD  1 
ATOM   681  C CE  . MET A 1 95  ? 12.66400  33.34700  74.31700  1.000 19.09771 ? 95  MET A CE  1 
ATOM   682  N N   . ALA A 1 96  ? 16.25700  29.42700  72.70500  1.000 16.83583 ? 96  ALA A N   1 
ATOM   683  C CA  . ALA A 1 96  ? 16.10600  28.26900  71.83100  1.000 19.86295 ? 96  ALA A CA  1 
ATOM   684  C C   . ALA A 1 96  ? 15.54800  27.06700  72.58300  1.000 19.57644 ? 96  ALA A C   1 
ATOM   685  O O   . ALA A 1 96  ? 14.85100  26.23800  71.98800  1.000 21.91720 ? 96  ALA A O   1 
ATOM   686  C CB  . ALA A 1 96  ? 17.44400  27.92100  71.17600  1.000 15.49858 ? 96  ALA A CB  1 
ATOM   687  N N   . ALA A 1 97  ? 15.85500  26.94500  73.87700  1.000 17.75694 ? 97  ALA A N   1 
ATOM   688  C CA  . ALA A 1 97  ? 15.23000  25.90300  74.68900  1.000 20.13804 ? 97  ALA A CA  1 
ATOM   689  C C   . ALA A 1 97  ? 13.73200  26.14400  74.83400  1.000 17.83678 ? 97  ALA A C   1 
ATOM   690  O O   . ALA A 1 97  ? 12.93900  25.19800  74.77700  1.000 19.09390 ? 97  ALA A O   1 
ATOM   691  C CB  . ALA A 1 97  ? 15.89700  25.82800  76.06300  1.000 19.19018 ? 97  ALA A CB  1 
ATOM   692  N N   . CYS A 1 98  ? 13.32800  27.40100  75.03000  1.000 15.74311 ? 98  CYS A N   1 
ATOM   693  C CA  . CYS A 1 98  ? 11.90700  27.73400  74.98900  1.000 18.04764 ? 98  CYS A CA  1 
ATOM   694  C C   . CYS A 1 98  ? 11.31400  27.39000  73.63500  1.000 22.80013 ? 98  CYS A C   1 
ATOM   695  O O   . CYS A 1 98  ? 10.23300  26.79500  73.55000  1.000 21.58627 ? 98  CYS A O   1 
ATOM   696  C CB  . CYS A 1 98  ? 11.69400  29.21900  75.28500  1.000 16.46566 ? 98  CYS A CB  1 
ATOM   697  S SG  . CYS A 1 98  ? 12.18500  29.75100  76.94600  1.000 25.16932 ? 98  CYS A SG  1 
ATOM   698  N N   . LEU A 1 99  ? 12.02000  27.75000  72.56300  1.000 18.64284 ? 99  LEU A N   1 
ATOM   699  C CA  . LEU A 1 99  ? 11.54100  27.44500  71.22200  1.000 20.05691 ? 99  LEU A CA  1 
ATOM   700  C C   . LEU A 1 99  ? 11.40200  25.94200  71.01900  1.000 21.62233 ? 99  LEU A C   1 
ATOM   701  O O   . LEU A 1 99  ? 10.43000  25.47600  70.41200  1.000 22.64761 ? 99  LEU A O   1 
ATOM   702  C CB  . LEU A 1 99  ? 12.49400  28.04400  70.19300  1.000 18.79059 ? 99  LEU A CB  1 
ATOM   703  C CG  . LEU A 1 99  ? 12.19700  27.71900  68.73800  1.000 20.23944 ? 99  LEU A CG  1 
ATOM   704  C CD1 . LEU A 1 99  ? 11.03000  28.57800  68.25600  1.000 17.87797 ? 99  LEU A CD1 1 
ATOM   705  C CD2 . LEU A 1 99  ? 13.44900  27.93200  67.89700  1.000 20.67253 ? 99  LEU A CD2 1 
ATOM   706  N N   . THR A 1 100 ? 12.36700  25.16900  71.52200  1.000 20.64782 ? 100 THR A N   1 
ATOM   707  C CA  . THR A 1 100 ? 12.30300  23.71600  71.39700  1.000 19.58176 ? 100 THR A CA  1 
ATOM   708  C C   . THR A 1 100 ? 11.11900  23.13900  72.16900  1.000 23.29511 ? 100 THR A C   1 
ATOM   709  O O   . THR A 1 100 ? 10.43300  22.23400  71.67800  1.000 22.01692 ? 100 THR A O   1 
ATOM   710  C CB  . THR A 1 100 ? 13.61300  23.09200  71.87700  1.000 15.16695 ? 100 THR A CB  1 
ATOM   711  O OG1 . THR A 1 100 ? 14.67600  23.48300  71.00000  1.000 19.33442 ? 100 THR A OG1 1 
ATOM   712  C CG2 . THR A 1 100 ? 13.51000  21.57800  71.89400  1.000 16.58874 ? 100 THR A CG2 1 
ATOM   713  N N   . ALA A 1 101 ? 10.86800  23.64000  73.38300  1.000 18.99997 ? 101 ALA A N   1 
ATOM   714  C CA  . ALA A 1 101 ? 9.71700   23.16200  74.14300  1.000 18.54953 ? 101 ALA A CA  1 
ATOM   715  C C   . ALA A 1 101 ? 8.41600   23.49900  73.43000  1.000 20.67110 ? 101 ALA A C   1 
ATOM   716  O O   . ALA A 1 101 ? 7.53200   22.64600  73.29800  1.000 23.14617 ? 101 ALA A O   1 
ATOM   717  C CB  . ALA A 1 101 ? 9.72500   23.75400  75.55300  1.000 15.29878 ? 101 ALA A CB  1 
ATOM   718  N N   . PHE A 1 102 ? 8.29700   24.72900  72.93200  1.000 18.67927 ? 102 PHE A N   1 
ATOM   719  C CA  . PHE A 1 102 ? 7.07000   25.14800  72.26700  1.000 20.47693 ? 102 PHE A CA  1 
ATOM   720  C C   . PHE A 1 102 ? 6.85900   24.39200  70.96200  1.000 25.31696 ? 102 PHE A C   1 
ATOM   721  O O   . PHE A 1 102 ? 5.83500   23.72700  70.77400  1.000 28.39953 ? 102 PHE A O   1 
ATOM   722  C CB  . PHE A 1 102 ? 7.10500   26.65400  72.01400  1.000 22.67880 ? 102 PHE A CB  1 
ATOM   723  C CG  . PHE A 1 102 ? 7.17100   27.47200  73.26300  1.000 24.81785 ? 102 PHE A CG  1 
ATOM   724  C CD1 . PHE A 1 102 ? 6.61500   27.00300  74.44200  1.000 23.46969 ? 102 PHE A CD1 1 
ATOM   725  C CD2 . PHE A 1 102 ? 7.79700   28.70600  73.26500  1.000 21.93713 ? 102 PHE A CD2 1 
ATOM   726  C CE1 . PHE A 1 102 ? 6.67600   27.75400  75.60000  1.000 24.12523 ? 102 PHE A CE1 1 
ATOM   727  C CE2 . PHE A 1 102 ? 7.86300   29.46100  74.42200  1.000 22.26129 ? 102 PHE A CE2 1 
ATOM   728  C CZ  . PHE A 1 102 ? 7.30000   28.98400  75.59100  1.000 23.54471 ? 102 PHE A CZ  1 
ATOM   729  N N   . MET A 1 103 ? 7.82300   24.47900  70.04400  1.000 21.72638 ? 103 MET A N   1 
ATOM   730  C CA  . MET A 1 103 ? 7.62600   23.90900  68.71800  1.000 22.05819 ? 103 MET A CA  1 
ATOM   731  C C   . MET A 1 103 ? 7.76200   22.39200  68.68900  1.000 21.99050 ? 103 MET A C   1 
ATOM   732  O O   . MET A 1 103 ? 7.22000   21.75800  67.77700  1.000 24.67167 ? 103 MET A O   1 
ATOM   733  C CB  . MET A 1 103 ? 8.59800   24.54800  67.72500  1.000 24.57682 ? 103 MET A CB  1 
ATOM   734  C CG  . MET A 1 103 ? 8.29900   26.02200  67.47400  1.000 23.16807 ? 103 MET A CG  1 
ATOM   735  S SD  . MET A 1 103 ? 9.10000   26.63900  65.99300  1.000 24.61393 ? 103 MET A SD  1 
ATOM   736  C CE  . MET A 1 103 ? 8.20900   25.75900  64.70700  1.000 20.75808 ? 103 MET A CE  1 
ATOM   737  N N   . GLY A 1 104 ? 8.46400   21.79500  69.65000  1.000 22.05318 ? 104 GLY A N   1 
ATOM   738  C CA  . GLY A 1 104 ? 8.52200   20.34600  69.70400  1.000 23.53331 ? 104 GLY A CA  1 
ATOM   739  C C   . GLY A 1 104 ? 7.29300   19.67600  70.28100  1.000 25.96565 ? 104 GLY A C   1 
ATOM   740  O O   . GLY A 1 104 ? 7.11400   18.47000  70.09600  1.000 32.01839 ? 104 GLY A O   1 
ATOM   741  N N   . ILE A 1 105 ? 6.43600   20.43400  70.96600  1.000 25.63926 ? 105 ILE A N   1 
ATOM   742  C CA  . ILE A 1 105 ? 5.29400   19.88900  71.68800  1.000 30.29154 ? 105 ILE A CA  1 
ATOM   743  C C   . ILE A 1 105 ? 3.96900   20.39300  71.12700  1.000 29.29945 ? 105 ILE A C   1 
ATOM   744  O O   . ILE A 1 105 ? 2.98600   19.64600  71.07300  1.000 33.76484 ? 105 ILE A O   1 
ATOM   745  C CB  . ILE A 1 105 ? 5.40700   20.20600  73.20000  1.000 34.88722 ? 105 ILE A CB  1 
ATOM   746  C CG1 . ILE A 1 105 ? 6.37300   19.23400  73.88800  1.000 31.95018 ? 105 ILE A CG1 1 
ATOM   747  C CG2 . ILE A 1 105 ? 4.05100   20.22200  73.86900  1.000 34.03920 ? 105 ILE A CG2 1 
ATOM   748  C CD1 . ILE A 1 105 ? 6.04700   17.77400  73.66300  1.000 36.66107 ? 105 ILE A CD1 1 
ATOM   749  N N   . LEU A 1 106 ? 3.91600   21.65400  70.70900  1.000 27.21344 ? 106 LEU A N   1 
ATOM   750  C CA  . LEU A 1 106 ? 2.68000   22.27600  70.27100  1.000 26.34371 ? 106 LEU A CA  1 
ATOM   751  C C   . LEU A 1 106 ? 2.50500   22.15000  68.75900  1.000 27.68489 ? 106 LEU A C   1 
ATOM   752  O O   . LEU A 1 106 ? 3.33700   21.57800  68.04800  1.000 26.55042 ? 106 LEU A O   1 
ATOM   753  C CB  . LEU A 1 106 ? 2.65500   23.74100  70.69500  1.000 22.24100 ? 106 LEU A CB  1 
ATOM   754  C CG  . LEU A 1 106 ? 2.88400   24.00500  72.18300  1.000 24.93137 ? 106 LEU A CG  1 
ATOM   755  C CD1 . LEU A 1 106 ? 3.11200   25.48100  72.42800  1.000 19.98440 ? 106 LEU A CD1 1 
ATOM   756  C CD2 . LEU A 1 106 ? 1.70000   23.50600  72.99000  1.000 30.29092 ? 106 LEU A CD2 1 
ATOM   757  N N   . LYS A 1 107 ? 1.39800   22.70000  68.26600  1.000 25.54664 ? 107 LYS A N   1 
ATOM   758  C CA  . LYS A 1 107 ? 1.11300   22.78000  66.84100  1.000 26.05178 ? 107 LYS A CA  1 
ATOM   759  C C   . LYS A 1 107 ? 0.13600   23.92200  66.62700  1.000 27.93942 ? 107 LYS A C   1 
ATOM   760  O O   . LYS A 1 107 ? -0.49500  24.40400  67.57200  1.000 26.86531 ? 107 LYS A O   1 
ATOM   761  C CB  . LYS A 1 107 ? 0.53100   21.47000  66.29900  1.000 34.28154 ? 107 LYS A CB  1 
ATOM   762  C CG  . LYS A 1 107 ? -0.75200  21.04300  67.01000  1.000 37.84387 ? 107 LYS A CG  1 
ATOM   763  C CD  . LYS A 1 107 ? -1.34300  19.76500  66.42200  1.000 39.57991 ? 107 LYS A CD  1 
ATOM   764  C CE  . LYS A 1 107 ? -2.49200  19.25200  67.28100  1.000 42.19711 ? 107 LYS A CE  1 
ATOM   765  N NZ  . LYS A 1 107 ? -2.01200  18.83100  68.63500  1.000 50.15442 ? 107 LYS A NZ  1 
ATOM   766  N N   . ALA A 1 108 ? 0.01500   24.34600  65.37000  1.000 29.16432 ? 108 ALA A N   1 
ATOM   767  C CA  . ALA A 1 108 ? -0.97300  25.35500  65.01500  1.000 23.59504 ? 108 ALA A CA  1 
ATOM   768  C C   . ALA A 1 108 ? -2.34600  24.92300  65.51000  1.000 27.41347 ? 108 ALA A C   1 
ATOM   769  O O   . ALA A 1 108 ? -2.74500  23.76900  65.33600  1.000 28.49825 ? 108 ALA A O   1 
ATOM   770  C CB  . ALA A 1 108 ? -0.99000  25.56100  63.50100  1.000 23.19765 ? 108 ALA A CB  1 
ATOM   771  N N   . GLY A 1 109 ? -3.05600  25.84800  66.15400  1.000 28.95210 ? 109 GLY A N   1 
ATOM   772  C CA  . GLY A 1 109 ? -4.32500  25.56300  66.78200  1.000 28.43779 ? 109 GLY A CA  1 
ATOM   773  C C   . GLY A 1 109 ? -4.25300  25.33400  68.27900  1.000 32.67621 ? 109 GLY A C   1 
ATOM   774  O O   . GLY A 1 109 ? -5.29100  25.39300  68.94900  1.000 34.95168 ? 109 GLY A O   1 
ATOM   775  N N   . ASP A 1 110 ? -3.06300  25.07500  68.82100  1.000 31.90431 ? 110 ASP A N   1 
ATOM   776  C CA  . ASP A 1 110 ? -2.91200  24.89600  70.25600  1.000 25.35569 ? 110 ASP A CA  1 
ATOM   777  C C   . ASP A 1 110 ? -2.96100  26.24400  70.97300  1.000 31.43276 ? 110 ASP A C   1 
ATOM   778  O O   . ASP A 1 110 ? -2.83100  27.31100  70.36800  1.000 34.30728 ? 110 ASP A O   1 
ATOM   779  C CB  . ASP A 1 110 ? -1.60700  24.17100  70.58500  1.000 27.04451 ? 110 ASP A CB  1 
ATOM   780  C CG  . ASP A 1 110 ? -1.64200  22.70000  70.21000  1.000 33.11515 ? 110 ASP A CG  1 
ATOM   781  O OD1 . ASP A 1 110 ? -2.68700  22.23300  69.71500  1.000 36.72512 ? 110 ASP A OD1 1 
ATOM   782  O OD2 . ASP A 1 110 ? -0.62200  22.00700  70.40800  1.000 34.60260 ? 110 ASP A OD2 1 
ATOM   783  N N   . HIS A 1 111 ? -3.15700  26.17500  72.28800  1.000 30.35722 ? 111 HIS A N   1 
ATOM   784  C CA  . HIS A 1 111 ? -3.25600  27.33700  73.15600  1.000 31.21274 ? 111 HIS A CA  1 
ATOM   785  C C   . HIS A 1 111 ? -2.30500  27.14400  74.32900  1.000 28.86447 ? 111 HIS A C   1 
ATOM   786  O O   . HIS A 1 111 ? -2.06300  26.01700  74.77000  1.000 30.96932 ? 111 HIS A O   1 
ATOM   787  C CB  . HIS A 1 111 ? -4.71200  27.53900  73.64500  1.000 32.43186 ? 111 HIS A CB  1 
ATOM   788  C CG  . HIS A 1 111 ? -4.87500  28.59600  74.69500  1.000 33.30457 ? 111 HIS A CG  1 
ATOM   789  N ND1 . HIS A 1 111 ? -5.07700  28.29800  76.02700  1.000 34.32707 ? 111 HIS A ND1 1 
ATOM   790  C CD2 . HIS A 1 111 ? -4.89800  29.94800  74.60600  1.000 32.08498 ? 111 HIS A CD2 1 
ATOM   791  C CE1 . HIS A 1 111 ? -5.20100  29.41900  76.71400  1.000 29.38434 ? 111 HIS A CE1 1 
ATOM   792  N NE2 . HIS A 1 111 ? -5.09700  30.43500  75.87600  1.000 29.64232 ? 111 HIS A NE2 1 
ATOM   793  N N   . VAL A 1 112 ? -1.74600  28.24700  74.81600  1.000 26.51970 ? 112 VAL A N   1 
ATOM   794  C CA  . VAL A 1 112 ? -0.80500  28.22400  75.92800  1.000 27.08673 ? 112 VAL A CA  1 
ATOM   795  C C   . VAL A 1 112 ? -1.28900  29.19200  76.99100  1.000 31.35542 ? 112 VAL A C   1 
ATOM   796  O O   . VAL A 1 112 ? -1.71300  30.30900  76.67800  1.000 29.12418 ? 112 VAL A O   1 
ATOM   797  C CB  . VAL A 1 112 ? 0.62800   28.60400  75.49500  1.000 27.21490 ? 112 VAL A CB  1 
ATOM   798  C CG1 . VAL A 1 112 ? 1.58200   28.52500  76.68700  1.000 22.36353 ? 112 VAL A CG1 1 
ATOM   799  C CG2 . VAL A 1 112 ? 1.10700   27.71700  74.35700  1.000 26.34588 ? 112 VAL A CG2 1 
ATOM   800  N N   . VAL A 1 113 ? -1.21600  28.76900  78.24900  1.000 29.88881 ? 113 VAL A N   1 
ATOM   801  C CA  . VAL A 1 113 ? -1.37500  29.66700  79.38600  1.000 31.27218 ? 113 VAL A CA  1 
ATOM   802  C C   . VAL A 1 113 ? 0.00400   29.88600  79.98900  1.000 27.31331 ? 113 VAL A C   1 
ATOM   803  O O   . VAL A 1 113 ? 0.70000   28.92300  80.33200  1.000 25.52814 ? 113 VAL A O   1 
ATOM   804  C CB  . VAL A 1 113 ? -2.35900  29.11000  80.42100  1.000 29.26777 ? 113 VAL A CB  1 
ATOM   805  C CG1 . VAL A 1 113 ? -2.53700  30.10200  81.55700  1.000 28.88698 ? 113 VAL A CG1 1 
ATOM   806  C CG2 . VAL A 1 113 ? -3.69300  28.81000  79.75500  1.000 33.71286 ? 113 VAL A CG2 1 
ATOM   807  N N   . ALA A 1 114 ? 0.40600   31.14800  80.10400  1.000 27.25273 ? 114 ALA A N   1 
ATOM   808  C CA  . ALA A 1 114 ? 1.74500   31.49700  80.55100  1.000 31.58266 ? 114 ALA A CA  1 
ATOM   809  C C   . ALA A 1 114 ? 1.68300   32.60000  81.59600  1.000 31.70073 ? 114 ALA A C   1 
ATOM   810  O O   . ALA A 1 114 ? 0.83200   33.49200  81.53300  1.000 30.82669 ? 114 ALA A O   1 
ATOM   811  C CB  . ALA A 1 114 ? 2.62800   31.94800  79.37300  1.000 25.36703 ? 114 ALA A CB  1 
ATOM   812  N N   . SER A 1 115 ? 2.59800   32.53300  82.56200  1.000 28.11366 ? 115 SER A N   1 
ATOM   813  C CA  . SER A 1 115 ? 2.73600   33.61900  83.52200  1.000 29.79694 ? 115 SER A CA  1 
ATOM   814  C C   . SER A 1 115 ? 3.06400   34.92000  82.80000  1.000 27.94499 ? 115 SER A C   1 
ATOM   815  O O   . SER A 1 115 ? 3.90600   34.95000  81.90000  1.000 30.12942 ? 115 SER A O   1 
ATOM   816  C CB  . SER A 1 115 ? 3.82800   33.29800  84.53600  1.000 21.83713 ? 115 SER A CB  1 
ATOM   817  O OG  . SER A 1 115 ? 4.14800   34.44900  85.29100  1.000 31.77394 ? 115 SER A OG  1 
ATOM   818  N N   . ARG A 1 116 ? 2.38600   36.00100  83.19500  1.000 31.32305 ? 116 ARG A N   1 
ATOM   819  C CA  . ARG A 1 116 ? 2.58500   37.28300  82.52800  1.000 34.72124 ? 116 ARG A CA  1 
ATOM   820  C C   . ARG A 1 116 ? 3.98000   37.84700  82.75200  1.000 30.38968 ? 116 ARG A C   1 
ATOM   821  O O   . ARG A 1 116 ? 4.40400   38.73400  82.00200  1.000 29.73113 ? 116 ARG A O   1 
ATOM   822  C CB  . ARG A 1 116 ? 1.53800   38.30000  82.99700  1.000 35.09045 ? 116 ARG A CB  1 
ATOM   823  C CG  . ARG A 1 116 ? 1.32000   38.35500  84.51400  1.000 41.90494 ? 116 ARG A CG  1 
ATOM   824  C CD  . ARG A 1 116 ? 2.38400   39.17900  85.25600  1.000 48.12906 ? 116 ARG A CD  1 
ATOM   825  N NE  . ARG A 1 116 ? 2.21000   39.13800  86.70600  1.000 50.20501 ? 116 ARG A NE  1 
ATOM   826  C CZ  . ARG A 1 116 ? 2.64400   38.15700  87.49000  1.000 46.56165 ? 116 ARG A CZ  1 
ATOM   827  N NH1 . ARG A 1 116 ? 3.27600   37.10600  86.99600  1.000 42.62379 ? 116 ARG A NH1 1 
ATOM   828  N NH2 . ARG A 1 116 ? 2.43400   38.23100  88.80200  1.000 46.25843 ? 116 ARG A NH2 1 
ATOM   829  N N   . SER A 1 117 ? 4.69900   37.36200  83.76200  1.000 28.50155 ? 117 SER A N   1 
ATOM   830  C CA  . SER A 1 117 ? 5.98000   37.93500  84.14400  1.000 33.23484 ? 117 SER A CA  1 
ATOM   831  C C   . SER A 1 117 ? 7.16700   37.13300  83.62900  1.000 24.30383 ? 117 SER A C   1 
ATOM   832  O O   . SER A 1 117 ? 8.29300   37.35600  84.08600  1.000 22.39059 ? 117 SER A O   1 
ATOM   833  C CB  . SER A 1 117 ? 6.06400   38.06800  85.66600  1.000 30.69901 ? 117 SER A CB  1 
ATOM   834  O OG  . SER A 1 117 ? 5.79300   36.82900  86.29900  1.000 34.63248 ? 117 SER A OG  1 
ATOM   835  N N   . ILE A 1 118 ? 6.95100   36.20100  82.69800  1.000 19.75512 ? 118 ILE A N   1 
ATOM   836  C CA  . ILE A 1 118 ? 8.09500   35.47000  82.16800  1.000 25.75576 ? 118 ILE A CA  1 
ATOM   837  C C   . ILE A 1 118 ? 9.00200   36.42100  81.39500  1.000 25.09925 ? 118 ILE A C   1 
ATOM   838  O O   . ILE A 1 118 ? 8.63300   37.55500  81.06600  1.000 21.35820 ? 118 ILE A O   1 
ATOM   839  C CB  . ILE A 1 118 ? 7.66500   34.28700  81.28800  1.000 24.50505 ? 118 ILE A CB  1 
ATOM   840  C CG1 . ILE A 1 118 ? 6.82500   34.78000  80.10900  1.000 26.46537 ? 118 ILE A CG1 1 
ATOM   841  C CG2 . ILE A 1 118 ? 6.92900   33.24600  82.11500  1.000 22.49061 ? 118 ILE A CG2 1 
ATOM   842  C CD1 . ILE A 1 118 ? 6.40500   33.68900  79.16600  1.000 19.40926 ? 118 ILE A CD1 1 
ATOM   843  N N   . PHE A 1 119 ? 10.22100  35.94700  81.13200  1.000 26.98609 ? 119 PHE A N   1 
ATOM   844  C CA  . PHE A 1 119 ? 11.22800  36.66300  80.35500  1.000 23.33982 ? 119 PHE A CA  1 
ATOM   845  C C   . PHE A 1 119 ? 10.59800  37.38900  79.17300  1.000 24.36482 ? 119 PHE A C   1 
ATOM   846  O O   . PHE A 1 119 ? 9.83300   36.80100  78.40200  1.000 25.31956 ? 119 PHE A O   1 
ATOM   847  C CB  . PHE A 1 119 ? 12.28200  35.65900  79.87000  1.000 26.88572 ? 119 PHE A CB  1 
ATOM   848  C CG  . PHE A 1 119 ? 13.60900  36.27200  79.51900  1.000 23.30964 ? 119 PHE A CG  1 
ATOM   849  C CD1 . PHE A 1 119 ? 14.35500  36.93800  80.47500  1.000 19.39208 ? 119 PHE A CD1 1 
ATOM   850  C CD2 . PHE A 1 119 ? 14.13200  36.13600  78.24100  1.000 21.56336 ? 119 PHE A CD2 1 
ATOM   851  C CE1 . PHE A 1 119 ? 15.58600  37.48500  80.15900  1.000 21.60309 ? 119 PHE A CE1 1 
ATOM   852  C CE2 . PHE A 1 119 ? 15.36600  36.68100  77.91500  1.000 21.53416 ? 119 PHE A CE2 1 
ATOM   853  C CZ  . PHE A 1 119 ? 16.09600  37.35600  78.87400  1.000 21.82287 ? 119 PHE A CZ  1 
ATOM   854  N N   . GLY A 1 120 ? 10.90900  38.68000  79.04800  1.000 22.93951 ? 120 GLY A N   1 
ATOM   855  C CA  . GLY A 1 120 ? 10.24800  39.49200  78.03800  1.000 24.39204 ? 120 GLY A CA  1 
ATOM   856  C C   . GLY A 1 120 ? 10.42000  38.93100  76.64100  1.000 27.53603 ? 120 GLY A C   1 
ATOM   857  O O   . GLY A 1 120 ? 9.48200   38.92800  75.83900  1.000 29.84716 ? 120 GLY A O   1 
ATOM   858  N N   . THR A 1 121 ? 11.61400  38.42400  76.34000  1.000 26.93931 ? 121 THR A N   1 
ATOM   859  C CA  . THR A 1 121 ? 11.84400  37.80400  75.04200  1.000 26.92652 ? 121 THR A CA  1 
ATOM   860  C C   . THR A 1 121 ? 10.97700  36.56100  74.85400  1.000 25.12323 ? 121 THR A C   1 
ATOM   861  O O   . THR A 1 121 ? 10.57700  36.24900  73.72700  1.000 24.15283 ? 121 THR A O   1 
ATOM   862  C CB  . THR A 1 121 ? 13.32800  37.47200  74.90000  1.000 25.22947 ? 121 THR A CB  1 
ATOM   863  O OG1 . THR A 1 121 ? 14.09300  38.64800  75.18800  1.000 28.22278 ? 121 THR A OG1 1 
ATOM   864  C CG2 . THR A 1 121 ? 13.65200  37.00000  73.49300  1.000 24.92495 ? 121 THR A CG2 1 
ATOM   865  N N   . THR A 1 122 ? 10.67300  35.84300  75.93900  1.000 23.46520 ? 122 THR A N   1 
ATOM   866  C CA  . THR A 1 122 ? 9.77000   34.69900  75.83400  1.000 23.80498 ? 122 THR A CA  1 
ATOM   867  C C   . THR A 1 122 ? 8.34200   35.15100  75.55700  1.000 23.56076 ? 122 THR A C   1 
ATOM   868  O O   . THR A 1 122 ? 7.62700   34.51500  74.77400  1.000 27.44096 ? 122 THR A O   1 
ATOM   869  C CB  . THR A 1 122 ? 9.82000   33.85400  77.10800  1.000 21.92723 ? 122 THR A CB  1 
ATOM   870  O OG1 . THR A 1 122 ? 11.18400  33.65100  77.50200  1.000 22.21475 ? 122 THR A OG1 1 
ATOM   871  C CG2 . THR A 1 122 ? 9.16900   32.50100  76.86700  1.000 21.51731 ? 122 THR A CG2 1 
ATOM   872  N N   . VAL A 1 123 ? 7.91000   36.24400  76.19400  1.000 23.95389 ? 123 VAL A N   1 
ATOM   873  C CA  . VAL A 1 123 ? 6.60100   36.82000  75.89600  1.000 22.13917 ? 123 VAL A CA  1 
ATOM   874  C C   . VAL A 1 123 ? 6.49800   37.12600  74.41000  1.000 24.14815 ? 123 VAL A C   1 
ATOM   875  O O   . VAL A 1 123 ? 5.50400   36.79000  73.75500  1.000 23.66519 ? 123 VAL A O   1 
ATOM   876  C CB  . VAL A 1 123 ? 6.36200   38.08600  76.74400  1.000 24.90198 ? 123 VAL A CB  1 
ATOM   877  C CG1 . VAL A 1 123 ? 5.05100   38.75100  76.34800  1.000 23.82921 ? 123 VAL A CG1 1 
ATOM   878  C CG2 . VAL A 1 123 ? 6.37400   37.76800  78.23200  1.000 20.54423 ? 123 VAL A CG2 1 
ATOM   879  N N   . GLN A 1 124 ? 7.54300   37.74800  73.85500  1.000 24.13435 ? 124 GLN A N   1 
ATOM   880  C CA  . GLN A 1 124 ? 7.57000   38.06500  72.43100  1.000 24.52655 ? 124 GLN A CA  1 
ATOM   881  C C   . GLN A 1 124 ? 7.64800   36.81000  71.57200  1.000 24.29303 ? 124 GLN A C   1 
ATOM   882  O O   . GLN A 1 124 ? 7.08500   36.77600  70.47200  1.000 24.87856 ? 124 GLN A O   1 
ATOM   883  C CB  . GLN A 1 124 ? 8.74400   38.99200  72.12600  1.000 22.63498 ? 124 GLN A CB  1 
ATOM   884  C CG  . GLN A 1 124 ? 8.58700   40.38100  72.71500  1.000 32.51922 ? 124 GLN A CG  1 
ATOM   885  C CD  . GLN A 1 124 ? 9.83600   41.21900  72.55700  1.000 47.44208 ? 124 GLN A CD  1 
ATOM   886  O OE1 . GLN A 1 124 ? 10.84400  40.75600  72.01900  1.000 48.39127 ? 124 GLN A OE1 1 
ATOM   887  N NE2 . GLN A 1 124 ? 9.78000   42.46200  73.02500  1.000 58.72697 ? 124 GLN A NE2 1 
ATOM   888  N N   . LEU A 1 125 ? 8.36100   35.77900  72.03400  1.000 22.60514 ? 125 LEU A N   1 
ATOM   889  C CA  . LEU A 1 125 ? 8.40700   34.53700  71.27100  1.000 21.25124 ? 125 LEU A CA  1 
ATOM   890  C C   . LEU A 1 125 ? 7.01400   33.93000  71.13700  1.000 24.10736 ? 125 LEU A C   1 
ATOM   891  O O   . LEU A 1 125 ? 6.62000   33.49600  70.04800  1.000 24.52763 ? 125 LEU A O   1 
ATOM   892  C CB  . LEU A 1 125 ? 9.36900   33.54000  71.92400  1.000 19.08526 ? 125 LEU A CB  1 
ATOM   893  C CG  . LEU A 1 125 ? 9.44200   32.18100  71.22100  1.000 20.23950 ? 125 LEU A CG  1 
ATOM   894  C CD1 . LEU A 1 125 ? 10.05600  32.32300  69.82800  1.000 19.35334 ? 125 LEU A CD1 1 
ATOM   895  C CD2 . LEU A 1 125 ? 10.21000  31.16400  72.04500  1.000 20.38772 ? 125 LEU A CD2 1 
ATOM   896  N N   . LEU A 1 126 ? 6.25000   33.89500  72.23200  1.000 22.52917 ? 126 LEU A N   1 
ATOM   897  C CA  . LEU A 1 126 ? 4.88800   33.37600  72.15800  1.000 23.37200 ? 126 LEU A CA  1 
ATOM   898  C C   . LEU A 1 126 ? 3.96500   34.33700  71.41400  1.000 24.11841 ? 126 LEU A C   1 
ATOM   899  O O   . LEU A 1 126 ? 3.24500   33.93300  70.49300  1.000 27.80895 ? 126 LEU A O   1 
ATOM   900  C CB  . LEU A 1 126 ? 4.35600   33.09800  73.56200  1.000 23.84757 ? 126 LEU A CB  1 
ATOM   901  C CG  . LEU A 1 126 ? 4.88100   31.84200  74.25600  1.000 20.56245 ? 126 LEU A CG  1 
ATOM   902  C CD1 . LEU A 1 126 ? 4.39500   31.78000  75.69200  1.000 27.09761 ? 126 LEU A CD1 1 
ATOM   903  C CD2 . LEU A 1 126 ? 4.44900   30.60000  73.50000  1.000 26.36923 ? 126 LEU A CD2 1 
ATOM   904  N N   . GLY A 1 127 ? 3.99900   35.61800  71.77400  1.000 26.10893 ? 127 GLY A N   1 
ATOM   905  C CA  . GLY A 1 127 ? 2.99600   36.56500  71.32100  1.000 24.84232 ? 127 GLY A CA  1 
ATOM   906  C C   . GLY A 1 127 ? 3.22600   37.24600  69.98500  1.000 30.16233 ? 127 GLY A C   1 
ATOM   907  O O   . GLY A 1 127 ? 2.27400   37.74800  69.37900  1.000 34.99490 ? 127 GLY A O   1 
ATOM   908  N N   . ASN A 1 128 ? 4.46600   37.28500  69.50600  1.000 30.20671 ? 128 ASN A N   1 
ATOM   909  C CA  . ASN A 1 128 ? 4.76500   37.94200  68.23900  1.000 31.69657 ? 128 ASN A CA  1 
ATOM   910  C C   . ASN A 1 128 ? 5.20600   36.98600  67.14100  1.000 31.99812 ? 128 ASN A C   1 
ATOM   911  O O   . ASN A 1 128 ? 4.96800   37.26900  65.96600  1.000 34.98290 ? 128 ASN A O   1 
ATOM   912  C CB  . ASN A 1 128 ? 5.84700   39.01500  68.43500  1.000 31.58811 ? 128 ASN A CB  1 
ATOM   913  C CG  . ASN A 1 128 ? 5.34000   40.22000  69.22300  1.000 42.16974 ? 128 ASN A CG  1 
ATOM   914  O OD1 . ASN A 1 128 ? 4.18800   40.63400  69.07100  1.000 44.10390 ? 128 ASN A OD1 1 
ATOM   915  N ND2 . ASN A 1 128 ? 6.19900   40.78300  70.07300  1.000 42.96354 ? 128 ASN A ND2 1 
ATOM   916  N N   . ILE A 1 129 ? 5.81900   35.85700  67.49100  1.000 27.55598 ? 129 ILE A N   1 
ATOM   917  C CA  . ILE A 1 129 ? 6.33600   34.89800  66.51500  1.000 30.14622 ? 129 ILE A CA  1 
ATOM   918  C C   . ILE A 1 129 ? 5.43500   33.66800  66.41100  1.000 28.97353 ? 129 ILE A C   1 
ATOM   919  O O   . ILE A 1 129 ? 4.93000   33.35100  65.33400  1.000 27.02703 ? 129 ILE A O   1 
ATOM   920  C CB  . ILE A 1 129 ? 7.79400   34.50200  66.84200  1.000 29.98714 ? 129 ILE A CB  1 
ATOM   921  C CG1 . ILE A 1 129 ? 8.72800   35.70500  66.65200  1.000 27.12910 ? 129 ILE A CG1 1 
ATOM   922  C CG2 . ILE A 1 129 ? 8.24800   33.33300  65.97400  1.000 21.95212 ? 129 ILE A CG2 1 
ATOM   923  C CD1 . ILE A 1 129 ? 10.18700  35.39400  66.94200  1.000 23.17571 ? 129 ILE A CD1 1 
ATOM   924  N N   . LEU A 1 130 ? 5.22500   32.95700  67.52400  1.000 28.19911 ? 130 LEU A N   1 
ATOM   925  C CA  . LEU A 1 130 ? 4.44900   31.71900  67.45600  1.000 26.70389 ? 130 LEU A CA  1 
ATOM   926  C C   . LEU A 1 130 ? 2.97800   31.98900  67.18400  1.000 26.24576 ? 130 LEU A C   1 
ATOM   927  O O   . LEU A 1 130 ? 2.29100   31.13500  66.61700  1.000 28.53919 ? 130 LEU A O   1 
ATOM   928  C CB  . LEU A 1 130 ? 4.61900   30.91100  68.74100  1.000 23.34107 ? 130 LEU A CB  1 
ATOM   929  C CG  . LEU A 1 130 ? 6.00000   30.26200  68.82200  1.000 25.83568 ? 130 LEU A CG  1 
ATOM   930  C CD1 . LEU A 1 130 ? 6.10100   29.33900  70.02700  1.000 21.81333 ? 130 LEU A CD1 1 
ATOM   931  C CD2 . LEU A 1 130 ? 6.31800   29.51800  67.53100  1.000 19.25436 ? 130 LEU A CD2 1 
ATOM   932  N N   . SER A 1 131 ? 2.48500   33.16900  67.56500  1.000 26.85527 ? 131 SER A N   1 
ATOM   933  C CA  . SER A 1 131 ? 1.11400   33.54400  67.23800  1.000 27.07569 ? 131 SER A CA  1 
ATOM   934  C C   . SER A 1 131 ? 0.88700   33.54700  65.73200  1.000 28.21710 ? 131 SER A C   1 
ATOM   935  O O   . SER A 1 131 ? -0.19200  33.17000  65.26100  1.000 30.09528 ? 131 SER A O   1 
ATOM   936  C CB  . SER A 1 131 ? 0.79700   34.91700  67.82400  1.000 25.35556 ? 131 SER A CB  1 
ATOM   937  O OG  . SER A 1 131 ? 1.62400   35.90300  67.22800  1.000 27.83302 ? 131 SER A OG  1 
ATOM   938  N N   . ARG A 1 132 ? 1.89200   33.98000  64.96100  1.000 27.57007 ? 132 ARG A N   1 
ATOM   939  C CA  . ARG A 1 132 ? 1.82600   33.93300  63.50400  1.000 25.73623 ? 132 ARG A CA  1 
ATOM   940  C C   . ARG A 1 132 ? 1.88300   32.51500  62.95900  1.000 26.60361 ? 132 ARG A C   1 
ATOM   941  O O   . ARG A 1 132 ? 1.76700   32.33500  61.74300  1.000 25.99093 ? 132 ARG A O   1 
ATOM   942  C CB  . ARG A 1 132 ? 2.96200   34.75600  62.88700  1.000 30.61443 ? 132 ARG A CB  1 
ATOM   943  C CG  . ARG A 1 132 ? 2.89400   36.24900  63.16800  1.000 33.49596 ? 132 ARG A CG  1 
ATOM   944  C CD  . ARG A 1 132 ? 4.01400   37.01200  62.45600  1.000 38.61887 ? 132 ARG A CD  1 
ATOM   945  N NE  . ARG A 1 132 ? 5.34600   36.57500  62.86600  1.000 38.59249 ? 132 ARG A NE  1 
ATOM   946  C CZ  . ARG A 1 132 ? 6.17300   35.86800  62.10600  1.000 38.81305 ? 132 ARG A CZ  1 
ATOM   947  N NH1 . ARG A 1 132 ? 5.84300   35.51200  60.87400  1.000 38.57363 ? 132 ARG A NH1 1 
ATOM   948  N NH2 . ARG A 1 132 ? 7.36400   35.51800  62.59000  1.000 37.76939 ? 132 ARG A NH2 1 
ATOM   949  N N   . PHE A 1 133 ? 2.08300   31.51000  63.81200  1.000 23.80298 ? 133 PHE A N   1 
ATOM   950  C CA  . PHE A 1 133 ? 2.08700   30.12000  63.38400  1.000 25.84888 ? 133 PHE A CA  1 
ATOM   951  C C   . PHE A 1 133 ? 1.03500   29.30700  64.13000  1.000 24.36704 ? 133 PHE A C   1 
ATOM   952  O O   . PHE A 1 133 ? 1.21700   28.11400  64.37500  1.000 26.90903 ? 133 PHE A O   1 
ATOM   953  C CB  . PHE A 1 133 ? 3.47900   29.51000  63.54000  1.000 27.95894 ? 133 PHE A CB  1 
ATOM   954  C CG  . PHE A 1 133 ? 4.48400   30.07000  62.57300  1.000 29.52695 ? 133 PHE A CG  1 
ATOM   955  C CD1 . PHE A 1 133 ? 4.63600   29.51600  61.30900  1.000 22.93920 ? 133 PHE A CD1 1 
ATOM   956  C CD2 . PHE A 1 133 ? 5.25900   31.16700  62.91600  1.000 26.10598 ? 133 PHE A CD2 1 
ATOM   957  C CE1 . PHE A 1 133 ? 5.55500   30.03700  60.41500  1.000 26.88289 ? 133 PHE A CE1 1 
ATOM   958  C CE2 . PHE A 1 133 ? 6.18100   31.69300  62.02200  1.000 23.96108 ? 133 PHE A CE2 1 
ATOM   959  C CZ  . PHE A 1 133 ? 6.33100   31.13100  60.77500  1.000 22.42100 ? 133 PHE A CZ  1 
ATOM   960  N N   . GLY A 1 134 ? -0.07100  29.94700  64.49300  1.000 25.47599 ? 134 GLY A N   1 
ATOM   961  C CA  . GLY A 1 134 ? -1.24200  29.22900  64.94800  1.000 26.27375 ? 134 GLY A CA  1 
ATOM   962  C C   . GLY A 1 134 ? -1.26900  28.86600  66.41000  1.000 28.75109 ? 134 GLY A C   1 
ATOM   963  O O   . GLY A 1 134 ? -2.16200  28.11700  66.82300  1.000 25.62435 ? 134 GLY A O   1 
ATOM   964  N N   . VAL A 1 135 ? -0.33000  29.36400  67.20900  1.000 26.53941 ? 135 VAL A N   1 
ATOM   965  C CA  . VAL A 1 135 ? -0.31900  29.11300  68.64400  1.000 28.09504 ? 135 VAL A CA  1 
ATOM   966  C C   . VAL A 1 135 ? -0.86200  30.35000  69.34100  1.000 29.88287 ? 135 VAL A C   1 
ATOM   967  O O   . VAL A 1 135 ? -0.33000  31.45300  69.16800  1.000 27.77347 ? 135 VAL A O   1 
ATOM   968  C CB  . VAL A 1 135 ? 1.08800   28.76400  69.15100  1.000 26.43945 ? 135 VAL A CB  1 
ATOM   969  C CG1 . VAL A 1 135 ? 1.07300   28.59100  70.65900  1.000 23.17936 ? 135 VAL A CG1 1 
ATOM   970  C CG2 . VAL A 1 135 ? 1.60200   27.50500  68.48000  1.000 22.63810 ? 135 VAL A CG2 1 
ATOM   971  N N   . GLU A 1 136 ? -1.92500  30.17200  70.12000  1.000 31.00738 ? 136 GLU A N   1 
ATOM   972  C CA  . GLU A 1 136 ? -2.51000  31.24400  70.90700  1.000 28.78667 ? 136 GLU A CA  1 
ATOM   973  C C   . GLU A 1 136 ? -1.97800  31.17200  72.33100  1.000 30.20142 ? 136 GLU A C   1 
ATOM   974  O O   . GLU A 1 136 ? -1.67000  30.09300  72.84400  1.000 28.99717 ? 136 GLU A O   1 
ATOM   975  C CB  . GLU A 1 136 ? -4.03800  31.15500  70.92200  1.000 38.24482 ? 136 GLU A CB  1 
ATOM   976  C CG  . GLU A 1 136 ? -4.69200  30.94500  69.55900  1.000 41.75773 ? 136 GLU A CG  1 
ATOM   977  C CD  . GLU A 1 136 ? -6.06900  30.28700  69.66400  1.000 54.38307 ? 136 GLU A CD  1 
ATOM   978  O OE1 . GLU A 1 136 ? -6.65900  30.28700  70.76800  1.000 51.90058 ? 136 GLU A OE1 1 
ATOM   979  O OE2 . GLU A 1 136 ? -6.55900  29.75700  68.64400  1.000 58.66370 ? 136 GLU A OE2 1 
ATOM   980  N N   . THR A 1 137 ? -1.87400  32.33200  72.97100  1.000 28.90489 ? 137 THR A N   1 
ATOM   981  C CA  . THR A 1 137 ? -1.37200  32.39200  74.33300  1.000 30.28585 ? 137 THR A CA  1 
ATOM   982  C C   . THR A 1 137 ? -2.22900  33.33300  75.16400  1.000 26.72786 ? 137 THR A C   1 
ATOM   983  O O   . THR A 1 137 ? -2.67700  34.37200  74.67400  1.000 30.20097 ? 137 THR A O   1 
ATOM   984  C CB  . THR A 1 137 ? 0.09200   32.84800  74.36700  1.000 29.02350 ? 137 THR A CB  1 
ATOM   985  O OG1 . THR A 1 137 ? 0.88400   31.97800  73.54300  1.000 30.99188 ? 137 THR A OG1 1 
ATOM   986  C CG2 . THR A 1 137 ? 0.62700   32.81600  75.79100  1.000 27.19541 ? 137 THR A CG2 1 
ATOM   987  N N   . SER A 1 138 ? -2.45800  32.95400  76.41900  1.000 31.24182 ? 138 SER A N   1 
ATOM   988  C CA  . SER A 1 138 ? -3.12000  33.79300  77.41000  1.000 33.81556 ? 138 SER A CA  1 
ATOM   989  C C   . SER A 1 138 ? -2.18000  33.98200  78.59500  1.000 30.94848 ? 138 SER A C   1 
ATOM   990  O O   . SER A 1 138 ? -1.58200  33.01400  79.07500  1.000 31.46613 ? 138 SER A O   1 
ATOM   991  C CB  . SER A 1 138 ? -4.44400  33.16600  77.86300  1.000 33.58713 ? 138 SER A CB  1 
ATOM   992  O OG  . SER A 1 138 ? -5.31700  32.96700  76.75900  1.000 35.06689 ? 138 SER A OG  1 
ATOM   993  N N   . PHE A 1 139 ? -2.04700  35.22200  79.06100  1.000 31.17885 ? 139 PHE A N   1 
ATOM   994  C CA  . PHE A 1 139 ? -1.10900  35.57200  80.12300  1.000 32.76165 ? 139 PHE A CA  1 
ATOM   995  C C   . PHE A 1 139 ? -1.86600  35.89400  81.40400  1.000 34.40242 ? 139 PHE A C   1 
ATOM   996  O O   . PHE A 1 139 ? -2.81500  36.68500  81.38800  1.000 35.70782 ? 139 PHE A O   1 
ATOM   997  C CB  . PHE A 1 139 ? -0.22800  36.75600  79.70700  1.000 30.61741 ? 139 PHE A CB  1 
ATOM   998  C CG  . PHE A 1 139 ? 0.75000   36.42500  78.60800  1.000 29.52831 ? 139 PHE A CG  1 
ATOM   999  C CD1 . PHE A 1 139 ? 1.89400   35.69200  78.88000  1.000 30.08350 ? 139 PHE A CD1 1 
ATOM   1000 C CD2 . PHE A 1 139 ? 0.52100   36.84100  77.30800  1.000 29.08911 ? 139 PHE A CD2 1 
ATOM   1001 C CE1 . PHE A 1 139 ? 2.79100   35.38000  77.87600  1.000 29.17789 ? 139 PHE A CE1 1 
ATOM   1002 C CE2 . PHE A 1 139 ? 1.41300   36.53500  76.29700  1.000 27.84732 ? 139 PHE A CE2 1 
ATOM   1003 C CZ  . PHE A 1 139 ? 2.55000   35.80400  76.58000  1.000 31.03469 ? 139 PHE A CZ  1 
ATOM   1004 N N   . VAL A 1 140 ? -1.43500  35.29300  82.51000  1.000 29.86067 ? 140 VAL A N   1 
ATOM   1005 C CA  . VAL A 1 140 ? -2.14400  35.40300  83.78400  1.000 32.00046 ? 140 VAL A CA  1 
ATOM   1006 C C   . VAL A 1 140 ? -1.13600  35.70900  84.88400  1.000 35.51714 ? 140 VAL A C   1 
ATOM   1007 O O   . VAL A 1 140 ? 0.06100   35.40800  84.75500  1.000 34.26905 ? 140 VAL A O   1 
ATOM   1008 C CB  . VAL A 1 140 ? -2.93200  34.11100  84.10900  1.000 34.58173 ? 140 VAL A CB  1 
ATOM   1009 C CG1 . VAL A 1 140 ? -3.98300  33.84200  83.03900  1.000 33.45650 ? 140 VAL A CG1 1 
ATOM   1010 C CG2 . VAL A 1 140 ? -1.98200  32.92700  84.24900  1.000 31.95630 ? 140 VAL A CG2 1 
ATOM   1011 N N   . PRO A 1 141 ? -1.58900  36.31000  85.98600  1.000 35.38004 ? 141 PRO A N   1 
ATOM   1012 C CA  . PRO A 1 141 ? -0.69300  36.49900  87.13200  1.000 36.44434 ? 141 PRO A CA  1 
ATOM   1013 C C   . PRO A 1 141 ? -0.19200  35.16100  87.65400  1.000 36.92780 ? 141 PRO A C   1 
ATOM   1014 O O   . PRO A 1 141 ? -0.91600  34.16300  87.65800  1.000 41.22727 ? 141 PRO A O   1 
ATOM   1015 C CB  . PRO A 1 141 ? -1.57400  37.21800  88.16000  1.000 35.75481 ? 141 PRO A CB  1 
ATOM   1016 C CG  . PRO A 1 141 ? -2.62100  37.89800  87.34100  1.000 35.61548 ? 141 PRO A CG  1 
ATOM   1017 C CD  . PRO A 1 141 ? -2.89300  36.96100  86.19700  1.000 31.09968 ? 141 PRO A CD  1 
ATOM   1018 N N   . LEU A 1 142 ? 1.06600   35.15600  88.09900  1.000 36.83615 ? 142 LEU A N   1 
ATOM   1019 C CA  . LEU A 1 142 ? 1.74900   33.90700  88.42100  1.000 34.54655 ? 142 LEU A CA  1 
ATOM   1020 C C   . LEU A 1 142 ? 1.12200   33.19600  89.61900  1.000 36.35750 ? 142 LEU A C   1 
ATOM   1021 O O   . LEU A 1 142 ? 0.92500   31.97500  89.58600  1.000 29.90122 ? 142 LEU A O   1 
ATOM   1022 C CB  . LEU A 1 142 ? 3.23000   34.18500  88.67700  1.000 31.72535 ? 142 LEU A CB  1 
ATOM   1023 C CG  . LEU A 1 142 ? 4.07200   33.04100  89.24100  1.000 29.08107 ? 142 LEU A CG  1 
ATOM   1024 C CD1 . LEU A 1 142 ? 4.12700   31.87100  88.26500  1.000 28.62209 ? 142 LEU A CD1 1 
ATOM   1025 C CD2 . LEU A 1 142 ? 5.46100   33.54800  89.55700  1.000 28.24068 ? 142 LEU A CD2 1 
ATOM   1026 N N   . ALA A 1 143 ? 0.80400   33.93500  90.68200  1.000 34.88494 ? 143 ALA A N   1 
ATOM   1027 C CA  . ALA A 1 143 ? 0.38700   33.33500  91.94400  1.000 34.58442 ? 143 ALA A CA  1 
ATOM   1028 C C   . ALA A 1 143 ? -1.11800  33.11400  92.04800  1.000 39.98716 ? 143 ALA A C   1 
ATOM   1029 O O   . ALA A 1 143 ? -1.59300  32.66900  93.09800  1.000 42.31462 ? 143 ALA A O   1 
ATOM   1030 C CB  . ALA A 1 143 ? 0.86000   34.20400  93.11600  1.000 33.01958 ? 143 ALA A CB  1 
ATOM   1031 N N   . ASP A 1 144 ? -1.87700  33.40400  90.99300  1.000 36.79832 ? 144 ASP A N   1 
ATOM   1032 C CA  . ASP A 1 144 ? -3.33800  33.36800  91.03700  1.000 35.61641 ? 144 ASP A CA  1 
ATOM   1033 C C   . ASP A 1 144 ? -3.81100  32.08400  90.35400  1.000 38.69941 ? 144 ASP A C   1 
ATOM   1034 O O   . ASP A 1 144 ? -4.15300  32.06100  89.17000  1.000 39.02741 ? 144 ASP A O   1 
ATOM   1035 C CB  . ASP A 1 144 ? -3.90300  34.62600  90.37400  1.000 41.85451 ? 144 ASP A CB  1 
ATOM   1036 C CG  . ASP A 1 144 ? -5.36700  34.86400  90.69800  1.000 44.57968 ? 144 ASP A CG  1 
ATOM   1037 O OD1 . ASP A 1 144 ? -6.08100  33.89300  91.02400  1.000 46.31879 ? 144 ASP A OD1 1 
ATOM   1038 O OD2 . ASP A 1 144 ? -5.80500  36.03100  90.61400  1.000 46.40567 ? 144 ASP A OD2 1 
ATOM   1039 N N   . VAL A 1 145 ? -3.82500  30.99100  91.12700  1.000 37.37870 ? 145 VAL A N   1 
ATOM   1040 C CA  . VAL A 1 145 ? -4.28300  29.70600  90.58400  1.000 41.25916 ? 145 VAL A CA  1 
ATOM   1041 C C   . VAL A 1 145 ? -5.68200  29.80400  89.99100  1.000 47.36795 ? 145 VAL A C   1 
ATOM   1042 O O   . VAL A 1 145 ? -5.91200  29.23300  88.91200  1.000 45.56500 ? 145 VAL A O   1 
ATOM   1043 C CB  . VAL A 1 145 ? -4.15500  28.60500  91.64600  1.000 39.47051 ? 145 VAL A CB  1 
ATOM   1044 C CG1 . VAL A 1 145 ? -4.71200  27.28300  91.11800  1.000 33.15470 ? 145 VAL A CG1 1 
ATOM   1045 C CG2 . VAL A 1 145 ? -2.70700  28.43700  92.07700  1.000 34.67390 ? 145 VAL A CG2 1 
ATOM   1046 N N   . PRO A 1 146 ? -6.65900  30.47900  90.61800  1.000 45.79554 ? 146 PRO A N   1 
ATOM   1047 C CA  . PRO A 1 146 ? -7.95400  30.65900  89.93800  1.000 44.89739 ? 146 PRO A CA  1 
ATOM   1048 C C   . PRO A 1 146 ? -7.84400  31.33400  88.58200  1.000 38.07825 ? 146 PRO A C   1 
ATOM   1049 O O   . PRO A 1 146 ? -8.58100  30.97000  87.65800  1.000 40.58603 ? 146 PRO A O   1 
ATOM   1050 C CB  . PRO A 1 146 ? -8.74700  31.51700  90.93300  1.000 48.43333 ? 146 PRO A CB  1 
ATOM   1051 C CG  . PRO A 1 146 ? -8.18300  31.15500  92.25500  1.000 51.95786 ? 146 PRO A CG  1 
ATOM   1052 C CD  . PRO A 1 146 ? -6.71700  30.93700  92.02000  1.000 46.30805 ? 146 PRO A CD  1 
ATOM   1053 N N   . ALA A 1 147 ? -6.94800  32.31200  88.43500  1.000 38.70377 ? 147 ALA A N   1 
ATOM   1054 C CA  . ALA A 1 147 ? -6.76400  32.95000  87.13400  1.000 38.89480 ? 147 ALA A CA  1 
ATOM   1055 C C   . ALA A 1 147 ? -6.17400  31.97400  86.12100  1.000 41.05913 ? 147 ALA A C   1 
ATOM   1056 O O   . ALA A 1 147 ? -6.50500  32.02800  84.92900  1.000 35.25239 ? 147 ALA A O   1 
ATOM   1057 C CB  . ALA A 1 147 ? -5.88000  34.18900  87.27200  1.000 33.26092 ? 147 ALA A CB  1 
ATOM   1058 N N   . TRP A 1 148 ? -5.29100  31.08000  86.57400  1.000 38.61702 ? 148 TRP A N   1 
ATOM   1059 C CA  . TRP A 1 148 ? -4.80300  30.01500  85.70300  1.000 40.15311 ? 148 TRP A CA  1 
ATOM   1060 C C   . TRP A 1 148 ? -5.95100  29.13600  85.22500  1.000 40.52643 ? 148 TRP A C   1 
ATOM   1061 O O   . TRP A 1 148 ? -6.09700  28.88300  84.02200  1.000 37.30351 ? 148 TRP A O   1 
ATOM   1062 C CB  . TRP A 1 148 ? -3.75400  29.17100  86.43500  1.000 37.62849 ? 148 TRP A CB  1 
ATOM   1063 C CG  . TRP A 1 148 ? -2.39300  29.80900  86.54200  1.000 37.32371 ? 148 TRP A CG  1 
ATOM   1064 C CD1 . TRP A 1 148 ? -1.95100  30.64000  87.53100  1.000 36.08936 ? 148 TRP A CD1 1 
ATOM   1065 C CD2 . TRP A 1 148 ? -1.29400  29.64900  85.63200  1.000 34.19083 ? 148 TRP A CD2 1 
ATOM   1066 N NE1 . TRP A 1 148 ? -0.65100  31.01200  87.29100  1.000 37.64266 ? 148 TRP A NE1 1 
ATOM   1067 C CE2 . TRP A 1 148 ? -0.22400  30.41700  86.13200  1.000 34.41231 ? 148 TRP A CE2 1 
ATOM   1068 C CE3 . TRP A 1 148 ? -1.11300  28.93200  84.44400  1.000 33.00563 ? 148 TRP A CE3 1 
ATOM   1069 C CZ2 . TRP A 1 148 ? 1.01000   30.49400  85.48000  1.000 37.38812 ? 148 TRP A CZ2 1 
ATOM   1070 C CZ3 . TRP A 1 148 ? 0.11100   29.00800  83.79900  1.000 29.54777 ? 148 TRP A CZ3 1 
ATOM   1071 C CH2 . TRP A 1 148 ? 1.15600   29.78300  84.31800  1.000 33.74903 ? 148 TRP A CH2 1 
ATOM   1072 N N   . ARG A 1 149 ? -6.79000  28.67400  86.16200  1.000 42.65256 ? 149 ARG A N   1 
ATOM   1073 C CA  . ARG A 1 149 ? -7.89700  27.78600  85.81300  1.000 39.58412 ? 149 ARG A CA  1 
ATOM   1074 C C   . ARG A 1 149 ? -8.88700  28.47700  84.88600  1.000 38.72596 ? 149 ARG A C   1 
ATOM   1075 O O   . ARG A 1 149 ? -9.38600  27.86800  83.93000  1.000 38.01881 ? 149 ARG A O   1 
ATOM   1076 C CB  . ARG A 1 149 ? -8.59800  27.29700  87.08400  1.000 41.19405 ? 149 ARG A CB  1 
ATOM   1077 C CG  . ARG A 1 149 ? -9.66700  26.22300  86.85900  1.000 43.95617 ? 149 ARG A CG  1 
ATOM   1078 C CD  . ARG A 1 149 ? -10.09000 25.56000  88.17100  1.000 33.83115 ? 149 ARG A CD  1 
ATOM   1079 N NE  . ARG A 1 149 ? -9.62300  26.31400  89.33000  1.000 45.08573 ? 149 ARG A NE  1 
ATOM   1080 C CZ  . ARG A 1 149 ? -8.75600  25.85900  90.22500  1.000 42.51016 ? 149 ARG A CZ  1 
ATOM   1081 N NH1 . ARG A 1 149 ? -8.27500  24.62700  90.15700  1.000 40.80104 ? 149 ARG A NH1 1 
ATOM   1082 N NH2 . ARG A 1 149 ? -8.36800  26.65800  91.21800  1.000 33.55705 ? 149 ARG A NH2 1 
ATOM   1083 N N   . ALA A 1 150 ? -9.18000  29.75200  85.14700  1.000 33.86135 ? 150 ALA A N   1 
ATOM   1084 C CA  . ALA A 1 150 ? -10.14800 30.46100  84.32000  1.000 35.46714 ? 150 ALA A CA  1 
ATOM   1085 C C   . ALA A 1 150 ? -9.63200  30.67100  82.90300  1.000 42.80914 ? 150 ALA A C   1 
ATOM   1086 O O   . ALA A 1 150 ? -10.43100 30.82100  81.97100  1.000 45.05413 ? 150 ALA A O   1 
ATOM   1087 C CB  . ALA A 1 150 ? -10.50600 31.80300  84.96000  1.000 31.37315 ? 150 ALA A CB  1 
ATOM   1088 N N   . ALA A 1 151 ? -8.31000  30.68500  82.71500  1.000 38.88272 ? 151 ALA A N   1 
ATOM   1089 C CA  . ALA A 1 151 ? -7.75100  30.92400  81.39100  1.000 37.52298 ? 151 ALA A CA  1 
ATOM   1090 C C   . ALA A 1 151 ? -7.70500  29.67200  80.52900  1.000 32.90840 ? 151 ALA A C   1 
ATOM   1091 O O   . ALA A 1 151 ? -7.42000  29.77900  79.33200  1.000 32.94927 ? 151 ALA A O   1 
ATOM   1092 C CB  . ALA A 1 151 ? -6.34500  31.51400  81.51000  1.000 37.60313 ? 151 ALA A CB  1 
ATOM   1093 N N   . LEU A 1 152 ? -7.98200  28.50100  81.09700  1.000 31.95125 ? 152 LEU A N   1 
ATOM   1094 C CA  . LEU A 1 152 ? -7.89500  27.26700  80.33200  1.000 34.45782 ? 152 LEU A CA  1 
ATOM   1095 C C   . LEU A 1 152 ? -8.92500  27.25900  79.20900  1.000 36.32952 ? 152 LEU A C   1 
ATOM   1096 O O   . LEU A 1 152 ? -9.98300  27.88600  79.29600  1.000 36.28314 ? 152 LEU A O   1 
ATOM   1097 C CB  . LEU A 1 152 ? -8.09400  26.06000  81.24600  1.000 32.32185 ? 152 LEU A CB  1 
ATOM   1098 C CG  . LEU A 1 152 ? -7.03200  25.88500  82.33100  1.000 32.57443 ? 152 LEU A CG  1 
ATOM   1099 C CD1 . LEU A 1 152 ? -7.36000  24.70200  83.20900  1.000 34.14176 ? 152 LEU A CD1 1 
ATOM   1100 C CD2 . LEU A 1 152 ? -5.66800  25.71000  81.69700  1.000 31.90647 ? 152 LEU A CD2 1 
ATOM   1101 N N   . ARG A 1 153 ? -8.58700  26.56000  78.13700  1.000 35.58624 ? 153 ARG A N   1 
ATOM   1102 C CA  . ARG A 1 153 ? -9.41700  26.40700  76.95400  1.000 34.55996 ? 153 ARG A CA  1 
ATOM   1103 C C   . ARG A 1 153 ? -9.41500  24.94300  76.55400  1.000 36.74897 ? 153 ARG A C   1 
ATOM   1104 O O   . ARG A 1 153 ? -8.58000  24.16500  77.02800  1.000 34.34003 ? 153 ARG A O   1 
ATOM   1105 C CB  . ARG A 1 153 ? -8.90600  27.27000  75.79200  1.000 31.88781 ? 153 ARG A CB  1 
ATOM   1106 C CG  . ARG A 1 153 ? -9.02100  28.76100  76.02500  1.000 34.69938 ? 153 ARG A CG  1 
ATOM   1107 C CD  . ARG A 1 153 ? -8.51500  29.53500  74.81400  1.000 37.68874 ? 153 ARG A CD  1 
ATOM   1108 N NE  . ARG A 1 153 ? -8.50000  30.96900  75.06600  1.000 42.73888 ? 153 ARG A NE  1 
ATOM   1109 C CZ  . ARG A 1 153 ? -7.97000  31.87200  74.25400  1.000 43.56261 ? 153 ARG A CZ  1 
ATOM   1110 N NH1 . ARG A 1 153 ? -7.40500  31.52600  73.10800  1.000 43.93553 ? 153 ARG A NH1 1 
ATOM   1111 N NH2 . ARG A 1 153 ? -8.00100  33.15600  74.60500  1.000 44.75209 ? 153 ARG A NH2 1 
ATOM   1112 N N   . PRO A 1 154 ? -10.36600 24.52200  75.71500  1.000 37.83355 ? 154 PRO A N   1 
ATOM   1113 C CA  . PRO A 1 154 ? -10.31700 23.13300  75.23100  1.000 38.63403 ? 154 PRO A CA  1 
ATOM   1114 C C   . PRO A 1 154 ? -9.01100  22.79400  74.53100  1.000 38.73899 ? 154 PRO A C   1 
ATOM   1115 O O   . PRO A 1 154 ? -8.51800  21.66800  74.66600  1.000 42.94147 ? 154 PRO A O   1 
ATOM   1116 C CB  . PRO A 1 154 ? -11.52300 23.05500  74.28200  1.000 39.41745 ? 154 PRO A CB  1 
ATOM   1117 C CG  . PRO A 1 154 ? -12.47000 24.08400  74.80100  1.000 35.26914 ? 154 PRO A CG  1 
ATOM   1118 C CD  . PRO A 1 154 ? -11.60600 25.20800  75.30700  1.000 35.47147 ? 154 PRO A CD  1 
ATOM   1119 N N   . ASN A 1 155 ? -8.41700  23.74500  73.80800  1.000 41.90420 ? 155 ASN A N   1 
ATOM   1120 C CA  . ASN A 1 155 ? -7.18300  23.51000  73.06700  1.000 40.69596 ? 155 ASN A CA  1 
ATOM   1121 C C   . ASN A 1 155 ? -5.92100  23.86500  73.85800  1.000 39.31318 ? 155 ASN A C   1 
ATOM   1122 O O   . ASN A 1 155 ? -4.83000  23.88400  73.27700  1.000 36.67101 ? 155 ASN A O   1 
ATOM   1123 C CB  . ASN A 1 155 ? -7.20600  24.28400  71.74400  1.000 32.03676 ? 155 ASN A CB  1 
ATOM   1124 C CG  . ASN A 1 155 ? -7.29300  25.78500  71.94400  1.000 35.56941 ? 155 ASN A CG  1 
ATOM   1125 O OD1 . ASN A 1 155 ? -7.78500  26.26000  72.96900  1.000 36.16630 ? 155 ASN A OD1 1 
ATOM   1126 N ND2 . ASN A 1 155 ? -6.81900  26.54200  70.95800  1.000 35.32210 ? 155 ASN A ND2 1 
ATOM   1127 N N   . THR A 1 156 ? -6.04000  24.14800  75.15800  1.000 34.37373 ? 156 THR A N   1 
ATOM   1128 C CA  . THR A 1 156 ? -4.86700  24.40400  75.98800  1.000 34.02846 ? 156 THR A CA  1 
ATOM   1129 C C   . THR A 1 156 ? -4.03700  23.13200  76.11700  1.000 34.69132 ? 156 THR A C   1 
ATOM   1130 O O   . THR A 1 156 ? -4.52000  22.11400  76.62200  1.000 35.21973 ? 156 THR A O   1 
ATOM   1131 C CB  . THR A 1 156 ? -5.27600  24.90300  77.37400  1.000 28.49159 ? 156 THR A CB  1 
ATOM   1132 O OG1 . THR A 1 156 ? -6.02600  26.11800  77.25400  1.000 24.02952 ? 156 THR A OG1 1 
ATOM   1133 C CG2 . THR A 1 156 ? -4.03600  25.16600  78.22600  1.000 31.32778 ? 156 THR A CG2 1 
ATOM   1134 N N   . ARG A 1 157 ? -2.78500  23.19000  75.66700  1.000 36.32527 ? 157 ARG A N   1 
ATOM   1135 C CA  . ARG A 1 157 ? -1.89100  22.04700  75.74200  1.000 31.50856 ? 157 ARG A CA  1 
ATOM   1136 C C   . ARG A 1 157 ? -0.72100  22.25600  76.69200  1.000 30.48324 ? 157 ARG A C   1 
ATOM   1137 O O   . ARG A 1 157 ? -0.06900  21.27400  77.06500  1.000 27.90920 ? 157 ARG A O   1 
ATOM   1138 C CB  . ARG A 1 157 ? -1.35300  21.69900  74.34400  1.000 32.98970 ? 157 ARG A CB  1 
ATOM   1139 C CG  . ARG A 1 157 ? -2.41900  21.27500  73.33300  1.000 39.49367 ? 157 ARG A CG  1 
ATOM   1140 C CD  . ARG A 1 157 ? -2.72600  19.77600  73.40300  1.000 44.52967 ? 157 ARG A CD  1 
ATOM   1141 N NE  . ARG A 1 157 ? -3.42200  19.39000  74.62700  1.000 50.83717 ? 157 ARG A NE  1 
ATOM   1142 C CZ  . ARG A 1 157 ? -4.74300  19.36300  74.76500  1.000 51.61520 ? 157 ARG A CZ  1 
ATOM   1143 N NH1 . ARG A 1 157 ? -5.54900  19.70300  73.77100  1.000 50.39881 ? 157 ARG A NH1 1 
ATOM   1144 N NH2 . ARG A 1 157 ? -5.26700  18.98500  75.93000  1.000 44.57703 ? 157 ARG A NH2 1 
ATOM   1145 N N   . MET A 1 158 ? -0.44500  23.49100  77.11000  1.000 26.06916 ? 158 MET A N   1 
ATOM   1146 C CA  . MET A 1 158 ? 0.73600   23.75500  77.92000  1.000 30.30759 ? 158 MET A CA  1 
ATOM   1147 C C   . MET A 1 158 ? 0.46900   24.89400  78.89100  1.000 23.85052 ? 158 MET A C   1 
ATOM   1148 O O   . MET A 1 158 ? -0.23300  25.85300  78.56000  1.000 21.79315 ? 158 MET A O   1 
ATOM   1149 C CB  . MET A 1 158 ? 1.94000   24.09700  77.03300  1.000 26.85520 ? 158 MET A CB  1 
ATOM   1150 C CG  . MET A 1 158 ? 3.22100   24.43500  77.78000  1.000 27.83254 ? 158 MET A CG  1 
ATOM   1151 S SD  . MET A 1 158 ? 4.58500   24.77000  76.63600  1.000 27.50786 ? 158 MET A SD  1 
ATOM   1152 C CE  . MET A 1 158 ? 4.75200   23.17300  75.85900  1.000 28.06326 ? 158 MET A CE  1 
ATOM   1153 N N   . LEU A 1 159 ? 1.03400   24.77200  80.09000  1.000 20.73637 ? 159 LEU A N   1 
ATOM   1154 C CA  . LEU A 1 159 ? 1.15300   25.86900  81.04200  1.000 25.73475 ? 159 LEU A CA  1 
ATOM   1155 C C   . LEU A 1 159 ? 2.63400   26.15600  81.24500  1.000 24.15420 ? 159 LEU A C   1 
ATOM   1156 O O   . LEU A 1 159 ? 3.40000   25.24900  81.58600  1.000 26.60954 ? 159 LEU A O   1 
ATOM   1157 C CB  . LEU A 1 159 ? 0.49000   25.53100  82.38400  1.000 24.97190 ? 159 LEU A CB  1 
ATOM   1158 C CG  . LEU A 1 159 ? -1.03200  25.60900  82.54700  1.000 25.30758 ? 159 LEU A CG  1 
ATOM   1159 C CD1 . LEU A 1 159 ? -1.74600  24.62600  81.63600  1.000 22.39943 ? 159 LEU A CD1 1 
ATOM   1160 C CD2 . LEU A 1 159 ? -1.41900  25.35300  84.00300  1.000 24.52567 ? 159 LEU A CD2 1 
ATOM   1161 N N   . PHE A 1 160 ? 3.03700   27.40900  81.04000  1.000 26.84370 ? 160 PHE A N   1 
ATOM   1162 C CA  . PHE A 1 160 ? 4.44300   27.79500  81.04200  1.000 26.82054 ? 160 PHE A CA  1 
ATOM   1163 C C   . PHE A 1 160 ? 4.66900   28.89200  82.06900  1.000 25.53470 ? 160 PHE A C   1 
ATOM   1164 O O   . PHE A 1 160 ? 3.94600   29.89200  82.07800  1.000 25.82844 ? 160 PHE A O   1 
ATOM   1165 C CB  . PHE A 1 160 ? 4.88200   28.27300  79.64800  1.000 28.55179 ? 160 PHE A CB  1 
ATOM   1166 C CG  . PHE A 1 160 ? 6.33200   28.68000  79.56700  1.000 25.21745 ? 160 PHE A CG  1 
ATOM   1167 C CD1 . PHE A 1 160 ? 6.73300   29.96100  79.92200  1.000 23.52790 ? 160 PHE A CD1 1 
ATOM   1168 C CD2 . PHE A 1 160 ? 7.29000   27.78600  79.12300  1.000 29.69472 ? 160 PHE A CD2 1 
ATOM   1169 C CE1 . PHE A 1 160 ? 8.06100   30.33700  79.85000  1.000 20.75859 ? 160 PHE A CE1 1 
ATOM   1170 C CE2 . PHE A 1 160 ? 8.62400   28.16000  79.04300  1.000 27.57945 ? 160 PHE A CE2 1 
ATOM   1171 C CZ  . PHE A 1 160 ? 9.00700   29.43900  79.40900  1.000 24.92524 ? 160 PHE A CZ  1 
ATOM   1172 N N   . LEU A 1 161 ? 5.68800   28.72000  82.91200  1.000 25.04844 ? 161 LEU A N   1 
ATOM   1173 C CA  . LEU A 1 161 ? 5.97100   29.71100  83.94300  1.000 26.16266 ? 161 LEU A CA  1 
ATOM   1174 C C   . LEU A 1 161 ? 7.43800   29.65500  84.34000  1.000 25.25073 ? 161 LEU A C   1 
ATOM   1175 O O   . LEU A 1 161 ? 8.13800   28.67300  84.08300  1.000 23.33255 ? 161 LEU A O   1 
ATOM   1176 C CB  . LEU A 1 161 ? 5.09300   29.50200  85.18300  1.000 27.36901 ? 161 LEU A CB  1 
ATOM   1177 C CG  . LEU A 1 161 ? 5.22500   28.17700  85.95000  1.000 28.79505 ? 161 LEU A CG  1 
ATOM   1178 C CD1 . LEU A 1 161 ? 6.33600   28.20200  87.00000  1.000 25.55184 ? 161 LEU A CD1 1 
ATOM   1179 C CD2 . LEU A 1 161 ? 3.90100   27.81500  86.59900  1.000 25.25185 ? 161 LEU A CD2 1 
ATOM   1180 N N   . GLU A 1 162 ? 7.87700   30.72800  84.99300  1.000 20.99318 ? 162 GLU A N   1 
ATOM   1181 C CA  . GLU A 1 162 ? 9.11000   30.76000  85.76400  1.000 20.81532 ? 162 GLU A CA  1 
ATOM   1182 C C   . GLU A 1 162 ? 8.75200   30.92700  87.23400  1.000 26.42184 ? 162 GLU A C   1 
ATOM   1183 O O   . GLU A 1 162 ? 7.79400   31.63200  87.56600  1.000 27.15073 ? 162 GLU A O   1 
ATOM   1184 C CB  . GLU A 1 162 ? 10.01300  31.91500  85.32400  1.000 23.55130 ? 162 GLU A CB  1 
ATOM   1185 C CG  . GLU A 1 162 ? 10.13800  32.06900  83.82100  1.000 24.48916 ? 162 GLU A CG  1 
ATOM   1186 C CD  . GLU A 1 162 ? 10.79100  33.37500  83.42000  1.000 23.91366 ? 162 GLU A CD  1 
ATOM   1187 O OE1 . GLU A 1 162 ? 11.17300  34.16200  84.31600  1.000 22.75037 ? 162 GLU A OE1 1 
ATOM   1188 O OE2 . GLU A 1 162 ? 10.91400  33.61700  82.20500  1.000 23.40196 ? 162 GLU A OE2 1 
ATOM   1189 N N   . THR A 1 163 ? 9.50500   30.26700  88.11800  1.000 22.41130 ? 163 THR A N   1 
ATOM   1190 C CA  . THR A 1 163 ? 9.30400   30.55100  89.53600  1.000 24.20753 ? 163 THR A CA  1 
ATOM   1191 C C   . THR A 1 163 ? 10.63100  30.33500  90.25200  1.000 24.62496 ? 163 THR A C   1 
ATOM   1192 O O   . THR A 1 163 ? 11.25000  29.27500  90.07500  1.000 25.27881 ? 163 THR A O   1 
ATOM   1193 C CB  . THR A 1 163 ? 8.20200   29.71200  90.19900  1.000 23.61339 ? 163 THR A CB  1 
ATOM   1194 O OG1 . THR A 1 163 ? 8.14700   30.01600  91.59800  1.000 26.23167 ? 163 THR A OG1 1 
ATOM   1195 C CG2 . THR A 1 163 ? 8.42600   28.20800  90.01900  1.000 24.14177 ? 163 THR A CG2 1 
ATOM   1196 N N   . PRO A 1 164 ? 11.10700  31.31600  91.03300  1.000 26.10386 ? 164 PRO A N   1 
ATOM   1197 C CA  . PRO A 1 164 ? 10.53800  32.65700  91.24300  1.000 24.10226 ? 164 PRO A CA  1 
ATOM   1198 C C   . PRO A 1 164 ? 10.47700  33.50400  89.97900  1.000 25.27543 ? 164 PRO A C   1 
ATOM   1199 O O   . PRO A 1 164 ? 11.14500  33.22200  88.98500  1.000 23.80262 ? 164 PRO A O   1 
ATOM   1200 C CB  . PRO A 1 164 ? 11.49200  33.27200  92.27500  1.000 24.98541 ? 164 PRO A CB  1 
ATOM   1201 C CG  . PRO A 1 164 ? 11.94900  32.09500  93.07900  1.000 26.19260 ? 164 PRO A CG  1 
ATOM   1202 C CD  . PRO A 1 164 ? 12.11800  30.99900  92.05800  1.000 27.05647 ? 164 PRO A CD  1 
ATOM   1203 N N   . SER A 1 165 ? 9.64100   34.53900  90.01300  1.000 26.48800 ? 165 SER A N   1 
ATOM   1204 C CA  . SER A 1 165 ? 9.43900   35.43400  88.88900  1.000 28.47295 ? 165 SER A CA  1 
ATOM   1205 C C   . SER A 1 165 ? 10.51000  36.52000  88.86200  1.000 27.28665 ? 165 SER A C   1 
ATOM   1206 O O   . SER A 1 165 ? 11.23900  36.75200  89.82800  1.000 25.68120 ? 165 SER A O   1 
ATOM   1207 C CB  . SER A 1 165 ? 8.05900   36.08700  88.95700  1.000 29.94710 ? 165 SER A CB  1 
ATOM   1208 O OG  . SER A 1 165 ? 8.05400   37.15500  89.89400  1.000 28.23059 ? 165 SER A OG  1 
ATOM   1209 N N   . ASN A 1 166 ? 10.58500  37.20100  87.73000  1.000 26.45692 ? 166 ASN A N   1 
ATOM   1210 C CA  . ASN A 1 166 ? 11.45700  38.33700  87.57900  1.000 27.55629 ? 166 ASN A CA  1 
ATOM   1211 C C   . ASN A 1 166 ? 10.63900  39.54500  87.15400  1.000 25.31049 ? 166 ASN A C   1 
ATOM   1212 O O   . ASN A 1 166 ? 9.78700   39.42400  86.26700  1.000 23.80344 ? 166 ASN A O   1 
ATOM   1213 C CB  . ASN A 1 166 ? 12.54500  38.05300  86.53700  1.000 24.88932 ? 166 ASN A CB  1 
ATOM   1214 C CG  . ASN A 1 166 ? 13.31800  39.29600  86.14800  1.000 25.95380 ? 166 ASN A CG  1 
ATOM   1215 O OD1 . ASN A 1 166 ? 14.25400  39.69700  86.83600  1.000 24.47244 ? 166 ASN A OD1 1 
ATOM   1216 N ND2 . ASN A 1 166 ? 12.93000  39.91200  85.03800  1.000 27.47256 ? 166 ASN A ND2 1 
ATOM   1217 N N   . PRO A 1 167 ? 10.87600  40.72500  87.75200  1.000 26.98228 ? 167 PRO A N   1 
ATOM   1218 C CA  . PRO A 1 167 ? 11.86200  41.01700  88.80500  1.000 25.11869 ? 167 PRO A CA  1 
ATOM   1219 C C   . PRO A 1 167 ? 11.34300  40.94800  90.24500  1.000 27.50801 ? 167 PRO A C   1 
ATOM   1220 O O   . PRO A 1 167 ? 12.10800  41.19000  91.17500  1.000 25.75223 ? 167 PRO A O   1 
ATOM   1221 C CB  . PRO A 1 167 ? 12.28800  42.44500  88.45800  1.000 26.84403 ? 167 PRO A CB  1 
ATOM   1222 C CG  . PRO A 1 167 ? 11.01700  43.06900  87.94500  1.000 29.43250 ? 167 PRO A CG  1 
ATOM   1223 C CD  . PRO A 1 167 ? 10.28500  41.96400  87.21100  1.000 26.63935 ? 167 PRO A CD  1 
ATOM   1224 N N   . LEU A 1 168 ? 10.07800  40.61600  90.48800  1.000 26.61460 ? 168 LEU A N   1 
ATOM   1225 C CA  . LEU A 1 168 ? 9.51200   40.72900  91.82900  1.000 34.09644 ? 168 LEU A CA  1 
ATOM   1226 C C   . LEU A 1 168 ? 9.66100   39.46500  92.67200  1.000 30.40682 ? 168 LEU A C   1 
ATOM   1227 O O   . LEU A 1 168 ? 9.25400   39.47000  93.83600  1.000 28.62001 ? 168 LEU A O   1 
ATOM   1228 C CB  . LEU A 1 168 ? 8.03700   41.11700  91.73400  1.000 31.74398 ? 168 LEU A CB  1 
ATOM   1229 C CG  . LEU A 1 168 ? 7.78200   42.35500  90.87100  1.000 33.09700 ? 168 LEU A CG  1 
ATOM   1230 C CD1 . LEU A 1 168 ? 6.31000   42.73900  90.92600  1.000 35.57647 ? 168 LEU A CD1 1 
ATOM   1231 C CD2 . LEU A 1 168 ? 8.66800   43.51900  91.31200  1.000 27.58298 ? 168 LEU A CD2 1 
ATOM   1232 N N   . THR A 1 169 ? 10.24800  38.39900  92.12500  1.000 30.26034 ? 169 THR A N   1 
ATOM   1233 C CA  . THR A 1 169 ? 10.45800  37.13300  92.83500  1.000 26.78294 ? 169 THR A CA  1 
ATOM   1234 C C   . THR A 1 169 ? 9.14600   36.51800  93.32500  1.000 27.08675 ? 169 THR A C   1 
ATOM   1235 O O   . THR A 1 169 ? 9.12300   35.79000  94.32100  1.000 30.65752 ? 169 THR A O   1 
ATOM   1236 C CB  . THR A 1 169 ? 11.43900  37.28500  94.00500  1.000 28.61794 ? 169 THR A CB  1 
ATOM   1237 O OG1 . THR A 1 169 ? 10.79700  37.95700  95.09600  1.000 29.86825 ? 169 THR A OG1 1 
ATOM   1238 C CG2 . THR A 1 169 ? 12.67300  38.06700  93.57900  1.000 27.20557 ? 169 THR A CG2 1 
ATOM   1239 N N   . GLU A 1 170 ? 8.05000   36.77900  92.62400  1.000 26.82611 ? 170 GLU A N   1 
ATOM   1240 C CA  . GLU A 1 170 ? 6.79800   36.10800  92.94200  1.000 29.51984 ? 170 GLU A CA  1 
ATOM   1241 C C   . GLU A 1 170 ? 6.92500   34.61100  92.67000  1.000 28.62402 ? 170 GLU A C   1 
ATOM   1242 O O   . GLU A 1 170 ? 7.75200   34.16800  91.87100  1.000 31.65783 ? 170 GLU A O   1 
ATOM   1243 C CB  . GLU A 1 170 ? 5.65700   36.71200  92.13000  1.000 28.16888 ? 170 GLU A CB  1 
ATOM   1244 C CG  . GLU A 1 170 ? 5.72400   38.23200  92.06400  1.000 34.42155 ? 170 GLU A CG  1 
ATOM   1245 C CD  . GLU A 1 170 ? 4.62500   38.82900  91.21200  1.000 34.93981 ? 170 GLU A CD  1 
ATOM   1246 O OE1 . GLU A 1 170 ? 3.44600   38.69600  91.59400  1.000 41.46234 ? 170 GLU A OE1 1 
ATOM   1247 O OE2 . GLU A 1 170 ? 4.93600   39.42000  90.15400  1.000 39.75640 ? 170 GLU A OE2 1 
ATOM   1248 N N   . ILE A 1 171 ? 6.10600   33.82400  93.36000  1.000 26.72307 ? 171 ILE A N   1 
ATOM   1249 C CA  . ILE A 1 171 ? 6.22300   32.37000  93.33500  1.000 24.21164 ? 171 ILE A CA  1 
ATOM   1250 C C   . ILE A 1 171 ? 5.02700   31.76700  92.61300  1.000 29.42275 ? 171 ILE A C   1 
ATOM   1251 O O   . ILE A 1 171 ? 3.91900   32.31600  92.62600  1.000 31.12772 ? 171 ILE A O   1 
ATOM   1252 C CB  . ILE A 1 171 ? 6.34600   31.79700  94.76100  1.000 28.30979 ? 171 ILE A CB  1 
ATOM   1253 C CG1 . ILE A 1 171 ? 7.40100   32.57200  95.55000  1.000 27.55767 ? 171 ILE A CG1 1 
ATOM   1254 C CG2 . ILE A 1 171 ? 6.70600   30.31600  94.72400  1.000 24.86691 ? 171 ILE A CG2 1 
ATOM   1255 C CD1 . ILE A 1 171 ? 8.78500   32.49700  94.94100  1.000 26.19301 ? 171 ILE A CD1 1 
ATOM   1256 N N   . GLY A 1 172 ? 5.26000   30.62600  91.97500  1.000 26.19395 ? 172 GLY A N   1 
ATOM   1257 C CA  . GLY A 1 172 ? 4.20600   29.84000  91.35200  1.000 24.79396 ? 172 GLY A CA  1 
ATOM   1258 C C   . GLY A 1 172 ? 4.01200   28.54300  92.11800  1.000 28.14961 ? 172 GLY A C   1 
ATOM   1259 O O   . GLY A 1 172 ? 4.97900   27.95100  92.60700  1.000 27.14175 ? 172 GLY A O   1 
ATOM   1260 N N   . ASP A 1 173 ? 2.75400   28.11900  92.23400  1.000 31.49302 ? 173 ASP A N   1 
ATOM   1261 C CA  . ASP A 1 173 ? 2.41200   26.87500  92.92300  1.000 29.47793 ? 173 ASP A CA  1 
ATOM   1262 C C   . ASP A 1 173 ? 2.55100   25.74100  91.91300  1.000 31.66626 ? 173 ASP A C   1 
ATOM   1263 O O   . ASP A 1 173 ? 1.62000   25.41000  91.17600  1.000 28.09175 ? 173 ASP A O   1 
ATOM   1264 C CB  . ASP A 1 173 ? 1.00600   26.95300  93.51100  1.000 33.45529 ? 173 ASP A CB  1 
ATOM   1265 C CG  . ASP A 1 173 ? 0.71800   25.82700  94.50600  1.000 40.81040 ? 173 ASP A CG  1 
ATOM   1266 O OD1 . ASP A 1 173 ? 1.30200   24.73100  94.35700  1.000 36.15157 ? 173 ASP A OD1 1 
ATOM   1267 O OD2 . ASP A 1 173 ? -0.09500  26.03900  95.43600  1.000 42.02258 ? 173 ASP A OD2 1 
ATOM   1268 N N   . MET A 1 174 ? 3.74100   25.13800  91.88200  1.000 30.74718 ? 174 MET A N   1 
ATOM   1269 C CA  . MET A 1 174 ? 4.05700   24.17500  90.83300  1.000 30.03212 ? 174 MET A CA  1 
ATOM   1270 C C   . MET A 1 174 ? 3.16800   22.94100  90.92300  1.000 34.76065 ? 174 MET A C   1 
ATOM   1271 O O   . MET A 1 174 ? 2.63600   22.46900  89.90900  1.000 29.94707 ? 174 MET A O   1 
ATOM   1272 C CB  . MET A 1 174 ? 5.53500   23.78600  90.91100  1.000 31.31472 ? 174 MET A CB  1 
ATOM   1273 C CG  . MET A 1 174 ? 6.49600   24.86800  90.42100  1.000 30.43291 ? 174 MET A CG  1 
ATOM   1274 S SD  . MET A 1 174 ? 8.19400   24.27200  90.26400  1.000 28.03558 ? 174 MET A SD  1 
ATOM   1275 C CE  . MET A 1 174 ? 8.65700   24.08200  91.98000  1.000 20.50689 ? 174 MET A CE  1 
ATOM   1276 N N   . GLN A 1 175 ? 2.99000   22.40300  92.13200  1.000 36.08023 ? 175 GLN A N   1 
ATOM   1277 C CA  . GLN A 1 175 ? 2.20600   21.18100  92.27400  1.000 30.83041 ? 175 GLN A CA  1 
ATOM   1278 C C   . GLN A 1 175 ? 0.74100   21.42400  91.93800  1.000 33.16808 ? 175 GLN A C   1 
ATOM   1279 O O   . GLN A 1 175 ? 0.09700   20.57600  91.31100  1.000 34.35565 ? 175 GLN A O   1 
ATOM   1280 C CB  . GLN A 1 175 ? 2.34900   20.61600  93.68500  1.000 32.76575 ? 175 GLN A CB  1 
ATOM   1281 C CG  . GLN A 1 175 ? 1.72800   19.24200  93.85200  1.000 33.84269 ? 175 GLN A CG  1 
ATOM   1282 C CD  . GLN A 1 175 ? 2.40100   18.18900  92.98700  1.000 35.11385 ? 175 GLN A CD  1 
ATOM   1283 O OE1 . GLN A 1 175 ? 3.48600   17.70700  93.30900  1.000 35.01117 ? 175 GLN A OE1 1 
ATOM   1284 N NE2 . GLN A 1 175 ? 1.75700   17.82900  91.88100  1.000 32.62717 ? 175 GLN A NE2 1 
ATOM   1285 N N   . ALA A 1 176 ? 0.19600   22.57300  92.34500  1.000 27.57178 ? 176 ALA A N   1 
ATOM   1286 C CA  . ALA A 1 176 ? -1.19100  22.87700  92.00500  1.000 29.52752 ? 176 ALA A CA  1 
ATOM   1287 C C   . ALA A 1 176 ? -1.36500  23.04000  90.50200  1.000 32.53677 ? 176 ALA A C   1 
ATOM   1288 O O   . ALA A 1 176 ? -2.35500  22.56800  89.92800  1.000 34.67779 ? 176 ALA A O   1 
ATOM   1289 C CB  . ALA A 1 176 ? -1.65300  24.13700  92.73500  1.000 27.50113 ? 176 ALA A CB  1 
ATOM   1290 N N   . LEU A 1 177 ? -0.41400  23.70800  89.84900  1.000 32.76093 ? 177 LEU A N   1 
ATOM   1291 C CA  . LEU A 1 177 ? -0.51200  23.93800  88.41300  1.000 28.20577 ? 177 LEU A CA  1 
ATOM   1292 C C   . LEU A 1 177 ? -0.17700  22.68800  87.60900  1.000 25.76167 ? 177 LEU A C   1 
ATOM   1293 O O   . LEU A 1 177 ? -0.66000  22.53700  86.48100  1.000 28.12428 ? 177 LEU A O   1 
ATOM   1294 C CB  . LEU A 1 177 ? 0.39200   25.10500  88.02000  1.000 26.81730 ? 177 LEU A CB  1 
ATOM   1295 C CG  . LEU A 1 177 ? -0.12000  26.41000  88.63500  1.000 33.40110 ? 177 LEU A CG  1 
ATOM   1296 C CD1 . LEU A 1 177 ? 0.80800   27.58700  88.35800  1.000 29.67791 ? 177 LEU A CD1 1 
ATOM   1297 C CD2 . LEU A 1 177 ? -1.53200  26.69300  88.12800  1.000 30.41882 ? 177 LEU A CD2 1 
ATOM   1298 N N   . ALA A 1 178 ? 0.64500   21.79300  88.15800  1.000 25.92114 ? 178 ALA A N   1 
ATOM   1299 C CA  . ALA A 1 178 ? 0.83600   20.49100  87.53000  1.000 29.71611 ? 178 ALA A CA  1 
ATOM   1300 C C   . ALA A 1 178 ? -0.46200  19.69700  87.53300  1.000 32.87277 ? 178 ALA A C   1 
ATOM   1301 O O   . ALA A 1 178 ? -0.86500  19.13600  86.50600  1.000 24.16930 ? 178 ALA A O   1 
ATOM   1302 C CB  . ALA A 1 178 ? 1.93900   19.71800  88.24900  1.000 27.82551 ? 178 ALA A CB  1 
ATOM   1303 N N   . ASP A 1 179 ? -1.13500  19.65100  88.68900  1.000 35.87670 ? 179 ASP A N   1 
ATOM   1304 C CA  . ASP A 1 179 ? -2.42100  18.96900  88.78100  1.000 34.64722 ? 179 ASP A CA  1 
ATOM   1305 C C   . ASP A 1 179 ? -3.44100  19.61000  87.85600  1.000 32.18035 ? 179 ASP A C   1 
ATOM   1306 O O   . ASP A 1 179 ? -4.19800  18.91000  87.17500  1.000 33.18801 ? 179 ASP A O   1 
ATOM   1307 C CB  . ASP A 1 179 ? -2.93400  18.99500  90.21900  1.000 30.52203 ? 179 ASP A CB  1 
ATOM   1308 C CG  . ASP A 1 179 ? -2.00500  18.29400  91.18500  1.000 35.62987 ? 179 ASP A CG  1 
ATOM   1309 O OD1 . ASP A 1 179 ? -1.20300  17.44300  90.74000  1.000 35.44281 ? 179 ASP A OD1 1 
ATOM   1310 O OD2 . ASP A 1 179 ? -2.08800  18.59300  92.39500  1.000 38.23732 ? 179 ASP A OD2 1 
ATOM   1311 N N   . LEU A 1 180 ? -3.47200  20.94400  87.81700  1.000 25.18367 ? 180 LEU A N   1 
ATOM   1312 C CA  . LEU A 1 180 ? -4.42000  21.63700  86.95300  1.000 25.97868 ? 180 LEU A CA  1 
ATOM   1313 C C   . LEU A 1 180 ? -4.17800  21.28400  85.49300  1.000 36.50714 ? 180 LEU A C   1 
ATOM   1314 O O   . LEU A 1 180 ? -5.12000  20.97800  84.75100  1.000 36.98696 ? 180 LEU A O   1 
ATOM   1315 C CB  . LEU A 1 180 ? -4.31300  23.14500  87.16600  1.000 25.02695 ? 180 LEU A CB  1 
ATOM   1316 C CG  . LEU A 1 180 ? -5.33700  23.99700  86.41500  1.000 37.44370 ? 180 LEU A CG  1 
ATOM   1317 C CD1 . LEU A 1 180 ? -6.71800  23.90000  87.07200  1.000 35.85586 ? 180 LEU A CD1 1 
ATOM   1318 C CD2 . LEU A 1 180 ? -4.87100  25.44600  86.30800  1.000 28.35068 ? 180 LEU A CD2 1 
ATOM   1319 N N   . ALA A 1 181 ? -2.91000  21.30400  85.06800  1.000 31.98839 ? 181 ALA A N   1 
ATOM   1320 C CA  . ALA A 1 181 ? -2.58800  20.98900  83.68100  1.000 31.70040 ? 181 ALA A CA  1 
ATOM   1321 C C   . ALA A 1 181 ? -2.92800  19.54000  83.35100  1.000 30.15177 ? 181 ALA A C   1 
ATOM   1322 O O   . ALA A 1 181 ? -3.58100  19.25800  82.34000  1.000 30.30523 ? 181 ALA A O   1 
ATOM   1323 C CB  . ALA A 1 181 ? -1.10900  21.27500  83.41400  1.000 34.22450 ? 181 ALA A CB  1 
ATOM   1324 N N   . HIS A 1 182 ? -2.52000  18.60900  84.21600  1.000 31.30284 ? 182 HIS A N   1 
ATOM   1325 C CA  . HIS A 1 182 ? -2.67600  17.18800  83.92200  1.000 32.50930 ? 182 HIS A CA  1 
ATOM   1326 C C   . HIS A 1 182 ? -4.13900  16.75600  83.88500  1.000 36.18199 ? 182 HIS A C   1 
ATOM   1327 O O   . HIS A 1 182 ? -4.49800  15.87800  83.09200  1.000 40.49066 ? 182 HIS A O   1 
ATOM   1328 C CB  . HIS A 1 182 ? -1.88800  16.37400  84.94000  1.000 29.68108 ? 182 HIS A CB  1 
ATOM   1329 C CG  . HIS A 1 182 ? -0.42400  16.68100  84.92900  1.000 33.56814 ? 182 HIS A CG  1 
ATOM   1330 N ND1 . HIS A 1 182 ? 0.43700   16.25600  85.91700  1.000 32.35410 ? 182 HIS A ND1 1 
ATOM   1331 C CD2 . HIS A 1 182 ? 0.32900   17.38500  84.05000  1.000 26.30323 ? 182 HIS A CD2 1 
ATOM   1332 C CE1 . HIS A 1 182 ? 1.65900   16.67700  85.64200  1.000 34.65756 ? 182 HIS A CE1 1 
ATOM   1333 N NE2 . HIS A 1 182 ? 1.62000   17.36500  84.51500  1.000 26.78508 ? 182 HIS A NE2 1 
ATOM   1334 N N   . VAL A 1 183 ? -4.99100  17.35200  84.72400  1.000 34.27441 ? 183 VAL A N   1 
ATOM   1335 C CA  . VAL A 1 183 ? -6.42600  17.08400  84.64600  1.000 36.17552 ? 183 VAL A CA  1 
ATOM   1336 C C   . VAL A 1 183 ? -6.95400  17.44000  83.26200  1.000 34.86105 ? 183 VAL A C   1 
ATOM   1337 O O   . VAL A 1 183 ? -7.79100  16.72600  82.69700  1.000 42.62905 ? 183 VAL A O   1 
ATOM   1338 C CB  . VAL A 1 183 ? -7.17700  17.85100  85.75100  1.000 39.32595 ? 183 VAL A CB  1 
ATOM   1339 C CG1 . VAL A 1 183 ? -8.65600  17.97900  85.40900  1.000 40.67205 ? 183 VAL A CG1 1 
ATOM   1340 C CG2 . VAL A 1 183 ? -6.99200  17.16600  87.09900  1.000 36.82356 ? 183 VAL A CG2 1 
ATOM   1341 N N   . HIS A 1 184 ? -6.46300  18.54000  82.69100  1.000 38.00198 ? 184 HIS A N   1 
ATOM   1342 C CA  . HIS A 1 184 ? -6.87400  19.00000  81.37200  1.000 38.37676 ? 184 HIS A CA  1 
ATOM   1343 C C   . HIS A 1 184 ? -5.95700  18.50200  80.26000  1.000 35.52554 ? 184 HIS A C   1 
ATOM   1344 O O   . HIS A 1 184 ? -5.91400  19.11800  79.18800  1.000 37.70910 ? 184 HIS A O   1 
ATOM   1345 C CB  . HIS A 1 184 ? -6.94800  20.52800  81.34600  1.000 33.58727 ? 184 HIS A CB  1 
ATOM   1346 C CG  . HIS A 1 184 ? -7.95200  21.09800  82.29800  1.000 37.78955 ? 184 HIS A CG  1 
ATOM   1347 N ND1 . HIS A 1 184 ? -7.82400  20.99100  83.66600  1.000 36.56498 ? 184 HIS A ND1 1 
ATOM   1348 C CD2 . HIS A 1 184 ? -9.10300  21.77700  82.08000  1.000 38.74520 ? 184 HIS A CD2 1 
ATOM   1349 C CE1 . HIS A 1 184 ? -8.85100  21.58200  84.25000  1.000 39.71787 ? 184 HIS A CE1 1 
ATOM   1350 N NE2 . HIS A 1 184 ? -9.64200  22.06700  83.31000  1.000 41.09650 ? 184 HIS A NE2 1 
ATOM   1351 N N   . ASP A 1 185 ? -5.22100  17.41300  80.50000  1.000 35.89252 ? 185 ASP A N   1 
ATOM   1352 C CA  . ASP A 1 185 ? -4.39600  16.76600  79.47800  1.000 37.80277 ? 185 ASP A CA  1 
ATOM   1353 C C   . ASP A 1 185 ? -3.44200  17.76200  78.82400  1.000 37.83778 ? 185 ASP A C   1 
ATOM   1354 O O   . ASP A 1 185 ? -3.29000  17.81200  77.60100  1.000 35.69775 ? 185 ASP A O   1 
ATOM   1355 C CB  . ASP A 1 185 ? -5.27500  16.06600  78.44400  1.000 39.64074 ? 185 ASP A CB  1 
ATOM   1356 C CG  . ASP A 1 185 ? -6.14300  14.99200  79.07000  1.000 44.81970 ? 185 ASP A CG  1 
ATOM   1357 O OD1 . ASP A 1 185 ? -5.58300  14.07300  79.70600  1.000 39.35213 ? 185 ASP A OD1 1 
ATOM   1358 O OD2 . ASP A 1 185 ? -7.38300  15.08800  78.95300  1.000 46.70889 ? 185 ASP A OD2 1 
ATOM   1359 N N   . ALA A 1 186 ? -2.81200  18.57800  79.66200  1.000 33.50743 ? 186 ALA A N   1 
ATOM   1360 C CA  . ALA A 1 186 ? -1.83900  19.56800  79.24500  1.000 29.05631 ? 186 ALA A CA  1 
ATOM   1361 C C   . ALA A 1 186 ? -0.54300  19.34500  80.01200  1.000 33.44767 ? 186 ALA A C   1 
ATOM   1362 O O   . ALA A 1 186 ? -0.52100  18.69500  81.06200  1.000 31.60164 ? 186 ALA A O   1 
ATOM   1363 C CB  . ALA A 1 186 ? -2.35600  20.99200  79.47800  1.000 25.33950 ? 186 ALA A CB  1 
ATOM   1364 N N   . TRP A 1 187 ? 0.54300   19.88200  79.46700  1.000 30.68000 ? 187 TRP A N   1 
ATOM   1365 C CA  . TRP A 1 187 ? 1.85600   19.77000  80.07900  1.000 28.88950 ? 187 TRP A CA  1 
ATOM   1366 C C   . TRP A 1 187 ? 2.17500   21.01400  80.89800  1.000 24.71219 ? 187 TRP A C   1 
ATOM   1367 O O   . TRP A 1 187 ? 1.76800   22.12600  80.55500  1.000 24.74491 ? 187 TRP A O   1 
ATOM   1368 C CB  . TRP A 1 187 ? 2.93300   19.56300  79.01500  1.000 27.69757 ? 187 TRP A CB  1 
ATOM   1369 C CG  . TRP A 1 187 ? 2.89100   18.22100  78.36700  1.000 29.07205 ? 187 TRP A CG  1 
ATOM   1370 C CD1 . TRP A 1 187 ? 3.29400   17.03500  78.91300  1.000 30.06074 ? 187 TRP A CD1 1 
ATOM   1371 C CD2 . TRP A 1 187 ? 2.43800   17.92000  77.04400  1.000 28.02854 ? 187 TRP A CD2 1 
ATOM   1372 N NE1 . TRP A 1 187 ? 3.11500   16.01500  78.01100  1.000 34.32251 ? 187 TRP A NE1 1 
ATOM   1373 C CE2 . TRP A 1 187 ? 2.59000   16.53200  76.85600  1.000 31.48583 ? 187 TRP A CE2 1 
ATOM   1374 C CE3 . TRP A 1 187 ? 1.91100   18.68800  76.00200  1.000 32.85671 ? 187 TRP A CE3 1 
ATOM   1375 C CZ2 . TRP A 1 187 ? 2.23800   15.89600  75.66500  1.000 40.94735 ? 187 TRP A CZ2 1 
ATOM   1376 C CZ3 . TRP A 1 187 ? 1.56000   18.05200  74.81600  1.000 39.36414 ? 187 TRP A CZ3 1 
ATOM   1377 C CH2 . TRP A 1 187 ? 1.72900   16.67200  74.65700  1.000 37.66652 ? 187 TRP A CH2 1 
ATOM   1378 N N   . LEU A 1 188 ? 2.90700   20.80900  81.99400  1.000 26.21218 ? 188 LEU A N   1 
ATOM   1379 C CA  . LEU A 1 188 ? 3.47200   21.89900  82.78000  1.000 27.30019 ? 188 LEU A CA  1 
ATOM   1380 C C   . LEU A 1 188 ? 4.94600   22.05200  82.42700  1.000 25.17244 ? 188 LEU A C   1 
ATOM   1381 O O   . LEU A 1 188 ? 5.72400   21.09900  82.55200  1.000 24.47599 ? 188 LEU A O   1 
ATOM   1382 C CB  . LEU A 1 188 ? 3.32100   21.65200  84.27900  1.000 22.85322 ? 188 LEU A CB  1 
ATOM   1383 C CG  . LEU A 1 188 ? 3.97000   22.73900  85.13700  1.000 25.04897 ? 188 LEU A CG  1 
ATOM   1384 C CD1 . LEU A 1 188 ? 3.28900   24.08600  84.91300  1.000 21.22133 ? 188 LEU A CD1 1 
ATOM   1385 C CD2 . LEU A 1 188 ? 3.96300   22.36300  86.61800  1.000 24.87354 ? 188 LEU A CD2 1 
ATOM   1386 N N   . VAL A 1 189 ? 5.32500   23.24900  81.99900  1.000 25.81819 ? 189 VAL A N   1 
ATOM   1387 C CA  . VAL A 1 189 ? 6.69900   23.55700  81.62700  1.000 25.44440 ? 189 VAL A CA  1 
ATOM   1388 C C   . VAL A 1 189 ? 7.18800   24.66900  82.54300  1.000 25.04297 ? 189 VAL A C   1 
ATOM   1389 O O   . VAL A 1 189 ? 6.59800   25.75600  82.58000  1.000 23.54295 ? 189 VAL A O   1 
ATOM   1390 C CB  . VAL A 1 189 ? 6.80800   23.96700  80.15000  1.000 25.75027 ? 189 VAL A CB  1 
ATOM   1391 C CG1 . VAL A 1 189 ? 8.23800   24.35300  79.81800  1.000 24.38025 ? 189 VAL A CG1 1 
ATOM   1392 C CG2 . VAL A 1 189 ? 6.31600   22.83600  79.24000  1.000 22.82324 ? 189 VAL A CG2 1 
ATOM   1393 N N   . VAL A 1 190 ? 8.26100   24.40600  83.27800  1.000 22.45817 ? 190 VAL A N   1 
ATOM   1394 C CA  . VAL A 1 190 ? 8.81500   25.36900  84.21900  1.000 22.51677 ? 190 VAL A CA  1 
ATOM   1395 C C   . VAL A 1 190 ? 10.19200  25.79500  83.73300  1.000 24.39479 ? 190 VAL A C   1 
ATOM   1396 O O   . VAL A 1 190 ? 11.04800  24.95100  83.44000  1.000 26.65199 ? 190 VAL A O   1 
ATOM   1397 C CB  . VAL A 1 190 ? 8.88600   24.79200  85.64000  1.000 20.36111 ? 190 VAL A CB  1 
ATOM   1398 C CG1 . VAL A 1 190 ? 9.48700   25.81400  86.58400  1.000 20.24048 ? 190 VAL A CG1 1 
ATOM   1399 C CG2 . VAL A 1 190 ? 7.49900   24.37200  86.10500  1.000 21.99481 ? 190 VAL A CG2 1 
ATOM   1400 N N   . ASP A 1 191 ? 10.39200  27.10300  83.63700  1.000 22.96604 ? 191 ASP A N   1 
ATOM   1401 C CA  . ASP A 1 191 ? 11.69500  27.69800  83.37200  1.000 23.64589 ? 191 ASP A CA  1 
ATOM   1402 C C   . ASP A 1 191 ? 12.41400  27.86200  84.70900  1.000 20.56916 ? 191 ASP A C   1 
ATOM   1403 O O   . ASP A 1 191 ? 11.96800  28.63500  85.56000  1.000 22.40308 ? 191 ASP A O   1 
ATOM   1404 C CB  . ASP A 1 191 ? 11.50200  29.03900  82.65700  1.000 24.55228 ? 191 ASP A CB  1 
ATOM   1405 C CG  . ASP A 1 191 ? 12.81100  29.68400  82.21200  1.000 27.94206 ? 191 ASP A CG  1 
ATOM   1406 O OD1 . ASP A 1 191 ? 13.83000  29.52100  82.90900  1.000 29.86736 ? 191 ASP A OD1 1 
ATOM   1407 O OD2 . ASP A 1 191 ? 12.81300  30.37500  81.16800  1.000 24.39348 ? 191 ASP A OD2 1 
ATOM   1408 N N   . ASN A 1 192 ? 13.52600  27.14700  84.89400  1.000 20.08089 ? 192 ASN A N   1 
ATOM   1409 C CA  . ASN A 1 192 ? 14.17000  27.02400  86.20000  1.000 23.27042 ? 192 ASN A CA  1 
ATOM   1410 C C   . ASN A 1 192 ? 15.43400  27.88200  86.33200  1.000 24.39145 ? 192 ASN A C   1 
ATOM   1411 O O   . ASN A 1 192 ? 16.32000  27.55400  87.13200  1.000 22.57953 ? 192 ASN A O   1 
ATOM   1412 C CB  . ASN A 1 192 ? 14.49100  25.55200  86.48200  1.000 18.61966 ? 192 ASN A CB  1 
ATOM   1413 C CG  . ASN A 1 192 ? 14.66600  25.25200  87.96900  1.000 22.77322 ? 192 ASN A CG  1 
ATOM   1414 O OD1 . ASN A 1 192 ? 14.13900  25.96100  88.82600  1.000 22.13489 ? 192 ASN A OD1 1 
ATOM   1415 N ND2 . ASN A 1 192 ? 15.41500  24.19700  88.27700  1.000 23.07386 ? 192 ASN A ND2 1 
ATOM   1416 N N   . CYS A 1 193 ? 15.53000  28.98700  85.57800  1.000 23.14799 ? 193 CYS A N   1 
ATOM   1417 C CA  . CYS A 1 193 ? 16.74600  29.80400  85.60100  1.000 23.63197 ? 193 CYS A CA  1 
ATOM   1418 C C   . CYS A 1 193 ? 16.98500  30.43300  86.96500  1.000 22.89695 ? 193 CYS A C   1 
ATOM   1419 O O   . CYS A 1 193 ? 18.13400  30.54800  87.40900  1.000 21.47452 ? 193 CYS A O   1 
ATOM   1420 C CB  . CYS A 1 193 ? 16.67700  30.91300  84.55700  1.000 24.24692 ? 193 CYS A CB  1 
ATOM   1421 S SG  . CYS A 1 193 ? 16.66600  30.36300  82.87400  1.000 30.24878 ? 193 CYS A SG  1 
ATOM   1422 N N   . PHE A 1 194 ? 15.91800  30.88400  87.62300  1.000 21.13213 ? 194 PHE A N   1 
ATOM   1423 C CA  . PHE A 1 194 ? 16.07000  31.63300  88.86600  1.000 22.91760 ? 194 PHE A CA  1 
ATOM   1424 C C   . PHE A 1 194 ? 16.80800  30.81300  89.92100  1.000 23.60507 ? 194 PHE A C   1 
ATOM   1425 O O   . PHE A 1 194 ? 17.74500  31.30400  90.56300  1.000 22.97568 ? 194 PHE A O   1 
ATOM   1426 C CB  . PHE A 1 194 ? 14.68900  32.06100  89.37400  1.000 24.71450 ? 194 PHE A CB  1 
ATOM   1427 C CG  . PHE A 1 194 ? 14.72300  33.12200  90.44500  1.000 20.24852 ? 194 PHE A CG  1 
ATOM   1428 C CD1 . PHE A 1 194 ? 15.08400  32.81000  91.74600  1.000 23.51803 ? 194 PHE A CD1 1 
ATOM   1429 C CD2 . PHE A 1 194 ? 14.36300  34.42800  90.15300  1.000 23.20451 ? 194 PHE A CD2 1 
ATOM   1430 C CE1 . PHE A 1 194 ? 15.10400  33.78400  92.73000  1.000 24.54243 ? 194 PHE A CE1 1 
ATOM   1431 C CE2 . PHE A 1 194 ? 14.38000  35.40200  91.13100  1.000 24.61783 ? 194 PHE A CE2 1 
ATOM   1432 C CZ  . PHE A 1 194 ? 14.75200  35.07900  92.42100  1.000 23.24553 ? 194 PHE A CZ  1 
ATOM   1433 N N   . CYS A 1 195 ? 16.40800  29.55300  90.10300  1.000 23.22391 ? 195 CYS A N   1 
ATOM   1434 C CA  . CYS A 1 195 ? 16.89900  28.73000  91.20300  1.000 21.40806 ? 195 CYS A CA  1 
ATOM   1435 C C   . CYS A 1 195 ? 18.01300  27.77000  90.81600  1.000 22.89791 ? 195 CYS A C   1 
ATOM   1436 O O   . CYS A 1 195 ? 18.89800  27.51600  91.64000  1.000 23.70574 ? 195 CYS A O   1 
ATOM   1437 C CB  . CYS A 1 195 ? 15.75400  27.91300  91.80400  1.000 25.22938 ? 195 CYS A CB  1 
ATOM   1438 S SG  . CYS A 1 195 ? 14.67900  28.84500  92.89700  1.000 31.56749 ? 195 CYS A SG  1 
ATOM   1439 N N   . THR A 1 196 ? 17.98300  27.22700  89.58500  1.000 23.73291 ? 196 THR A N   1 
ATOM   1440 C CA  . THR A 1 196 ? 18.83200  26.13900  89.09200  1.000 26.16850 ? 196 THR A CA  1 
ATOM   1441 C C   . THR A 1 196 ? 18.51000  24.84400  89.83500  1.000 23.37107 ? 196 THR A C   1 
ATOM   1442 O O   . THR A 1 196 ? 17.90700  24.88700  90.91500  1.000 23.40387 ? 196 THR A O   1 
ATOM   1443 C CB  . THR A 1 196 ? 20.32600  26.46800  89.23300  1.000 20.44328 ? 196 THR A CB  1 
ATOM   1444 O OG1 . THR A 1 196 ? 20.74300  26.22300  90.57900  1.000 27.24810 ? 196 THR A OG1 1 
ATOM   1445 C CG2 . THR A 1 196 ? 20.59400  27.90100  88.88400  1.000 17.94145 ? 196 THR A CG2 1 
ATOM   1446 N N   . PRO A 1 197 ? 18.89100  23.67500  89.30200  1.000 25.84944 ? 197 PRO A N   1 
ATOM   1447 C CA  . PRO A 1 197 ? 18.62500  22.41700  90.02700  1.000 24.95354 ? 197 PRO A CA  1 
ATOM   1448 C C   . PRO A 1 197 ? 19.33900  22.31000  91.37000  1.000 25.99155 ? 197 PRO A C   1 
ATOM   1449 O O   . PRO A 1 197 ? 18.98900  21.42700  92.16600  1.000 30.12452 ? 197 PRO A O   1 
ATOM   1450 C CB  . PRO A 1 197 ? 19.10500  21.33200  89.04900  1.000 25.77970 ? 197 PRO A CB  1 
ATOM   1451 C CG  . PRO A 1 197 ? 20.05000  22.04100  88.11300  1.000 22.75567 ? 197 PRO A CG  1 
ATOM   1452 C CD  . PRO A 1 197 ? 19.48000  23.42300  87.97400  1.000 24.91067 ? 197 PRO A CD  1 
ATOM   1453 N N   . ALA A 1 198 ? 20.33200  23.15700  91.64300  1.000 19.09227 ? 198 ALA A N   1 
ATOM   1454 C CA  . ALA A 1 198 ? 20.92900  23.17700  92.97100  1.000 22.05444 ? 198 ALA A CA  1 
ATOM   1455 C C   . ALA A 1 198 ? 19.93800  23.61300  94.04300  1.000 23.76410 ? 198 ALA A C   1 
ATOM   1456 O O   . ALA A 1 198 ? 20.14400  23.31000  95.22200  1.000 23.39646 ? 198 ALA A O   1 
ATOM   1457 C CB  . ALA A 1 198 ? 22.15000  24.10100  92.99000  1.000 21.01544 ? 198 ALA A CB  1 
ATOM   1458 N N   . LEU A 1 199 ? 18.87300  24.31700  93.67100  1.000 21.93360 ? 199 LEU A N   1 
ATOM   1459 C CA  . LEU A 1 199 ? 17.91200  24.81900  94.64400  1.000 23.96288 ? 199 LEU A CA  1 
ATOM   1460 C C   . LEU A 1 199 ? 16.49100  24.32800  94.42400  1.000 24.91871 ? 199 LEU A C   1 
ATOM   1461 O O   . LEU A 1 199 ? 15.73900  24.22800  95.39400  1.000 30.99045 ? 199 LEU A O   1 
ATOM   1462 C CB  . LEU A 1 199 ? 17.89700  26.35900  94.64700  1.000 25.07119 ? 199 LEU A CB  1 
ATOM   1463 C CG  . LEU A 1 199 ? 19.22300  27.07900  94.90000  1.000 20.91309 ? 199 LEU A CG  1 
ATOM   1464 C CD1 . LEU A 1 199 ? 19.02200  28.58800  94.95600  1.000 20.10960 ? 199 LEU A CD1 1 
ATOM   1465 C CD2 . LEU A 1 199 ? 19.86500  26.57000  96.17200  1.000 24.01347 ? 199 LEU A CD2 1 
ATOM   1466 N N   . GLN A 1 200 ? 16.10500  24.01700  93.18800  1.000 24.82851 ? 200 GLN A N   1 
ATOM   1467 C CA  . GLN A 1 200 ? 14.72500  23.67700  92.87500  1.000 28.95792 ? 200 GLN A CA  1 
ATOM   1468 C C   . GLN A 1 200 ? 14.70300  22.65500  91.74600  1.000 28.80401 ? 200 GLN A C   1 
ATOM   1469 O O   . GLN A 1 200 ? 15.42500  22.80200  90.75700  1.000 24.36198 ? 200 GLN A O   1 
ATOM   1470 C CB  . GLN A 1 200 ? 13.93500  24.93200  92.48400  1.000 26.00500 ? 200 GLN A CB  1 
ATOM   1471 C CG  . GLN A 1 200 ? 12.46400  24.70300  92.19300  1.000 26.39691 ? 200 GLN A CG  1 
ATOM   1472 C CD  . GLN A 1 200 ? 11.71400  26.00400  91.95000  1.000 28.23940 ? 200 GLN A CD  1 
ATOM   1473 O OE1 . GLN A 1 200 ? 10.92100  26.43700  92.78600  1.000 29.07102 ? 200 GLN A OE1 1 
ATOM   1474 N NE2 . GLN A 1 200 ? 11.95700  26.62900  90.79800  1.000 24.61230 ? 200 GLN A NE2 1 
ATOM   1475 N N   . GLN A 1 201 ? 13.87600  21.61900  91.90000  1.000 26.19293 ? 201 GLN A N   1 
ATOM   1476 C CA  . GLN A 1 201 ? 13.73200  20.56600  90.89500  1.000 27.77759 ? 201 GLN A CA  1 
ATOM   1477 C C   . GLN A 1 201 ? 12.25700  20.43600  90.54000  1.000 29.96242 ? 201 GLN A C   1 
ATOM   1478 O O   . GLN A 1 201 ? 11.52800  19.63800  91.14500  1.000 28.02545 ? 201 GLN A O   1 
ATOM   1479 C CB  . GLN A 1 201 ? 14.30400  19.23900  91.38700  1.000 28.24609 ? 201 GLN A CB  1 
ATOM   1480 C CG  . GLN A 1 201 ? 15.78000  19.29400  91.73000  1.000 29.79325 ? 201 GLN A CG  1 
ATOM   1481 C CD  . GLN A 1 201 ? 16.02100  19.33900  93.22600  1.000 40.19585 ? 201 GLN A CD  1 
ATOM   1482 O OE1 . GLN A 1 201 ? 15.53300  18.48300  93.96900  1.000 45.02972 ? 201 GLN A OE1 1 
ATOM   1483 N NE2 . GLN A 1 201 ? 16.77200  20.34300  93.67900  1.000 37.64380 ? 201 GLN A NE2 1 
ATOM   1484 N N   . PRO A 1 202 ? 11.78800  21.19400  89.54300  1.000 27.76074 ? 202 PRO A N   1 
ATOM   1485 C CA  . PRO A 1 202 ? 10.34600  21.23200  89.26000  1.000 23.00516 ? 202 PRO A CA  1 
ATOM   1486 C C   . PRO A 1 202 ? 9.73800   19.88300  88.94700  1.000 29.39391 ? 202 PRO A C   1 
ATOM   1487 O O   . PRO A 1 202 ? 8.52200   19.72300  89.11800  1.000 26.82412 ? 202 PRO A O   1 
ATOM   1488 C CB  . PRO A 1 202 ? 10.25600  22.17700  88.05600  1.000 22.06490 ? 202 PRO A CB  1 
ATOM   1489 C CG  . PRO A 1 202 ? 11.42200  23.09700  88.23900  1.000 24.65533 ? 202 PRO A CG  1 
ATOM   1490 C CD  . PRO A 1 202 ? 12.52600  22.22300  88.79000  1.000 26.92109 ? 202 PRO A CD  1 
ATOM   1491 N N   . LEU A 1 203 ? 10.53500  18.90600  88.50300  1.000 28.66525 ? 203 LEU A N   1 
ATOM   1492 C CA  . LEU A 1 203 ? 9.98600   17.58000  88.23300  1.000 26.74474 ? 203 LEU A CA  1 
ATOM   1493 C C   . LEU A 1 203 ? 9.40900   16.94400  89.48700  1.000 32.76572 ? 203 LEU A C   1 
ATOM   1494 O O   . LEU A 1 203 ? 8.45200   16.16600  89.40100  1.000 31.11415 ? 203 LEU A O   1 
ATOM   1495 C CB  . LEU A 1 203 ? 11.05400  16.66700  87.63400  1.000 29.62640 ? 203 LEU A CB  1 
ATOM   1496 C CG  . LEU A 1 203 ? 11.56500  17.02500  86.24100  1.000 33.10486 ? 203 LEU A CG  1 
ATOM   1497 C CD1 . LEU A 1 203 ? 12.31900  15.84600  85.67500  1.000 31.96093 ? 203 LEU A CD1 1 
ATOM   1498 C CD2 . LEU A 1 203 ? 10.42300  17.42800  85.32100  1.000 30.26785 ? 203 LEU A CD2 1 
ATOM   1499 N N   . LYS A 1 204 ? 9.97200   17.25900  90.65900  1.000 32.09864 ? 204 LYS A N   1 
ATOM   1500 C CA  . LYS A 1 204 ? 9.44500   16.74900  91.91900  1.000 33.88156 ? 204 LYS A CA  1 
ATOM   1501 C C   . LYS A 1 204 ? 8.11300   17.37800  92.28900  1.000 33.72414 ? 204 LYS A C   1 
ATOM   1502 O O   . LYS A 1 204 ? 7.52300   16.99100  93.30300  1.000 37.31593 ? 204 LYS A O   1 
ATOM   1503 C CB  . LYS A 1 204 ? 10.45800  16.97100  93.04500  1.000 31.61216 ? 204 LYS A CB  1 
ATOM   1504 C CG  . LYS A 1 204 ? 11.73400  16.17200  92.86900  1.000 31.66270 ? 204 LYS A CG  1 
ATOM   1505 C CD  . LYS A 1 204 ? 12.74100  16.45900  93.96300  1.000 36.12717 ? 204 LYS A CD  1 
ATOM   1506 C CE  . LYS A 1 204 ? 13.98200  15.60700  93.76300  1.000 45.72634 ? 204 LYS A CE  1 
ATOM   1507 N NZ  . LYS A 1 204 ? 15.06600  15.96000  94.71700  1.000 52.83230 ? 204 LYS A NZ  1 
ATOM   1508 N N   . PHE A 1 205 ? 7.63600   18.33600  91.49300  1.000 34.11832 ? 205 PHE A N   1 
ATOM   1509 C CA  . PHE A 1 205 ? 6.35900   18.99900  91.72100  1.000 31.18549 ? 205 PHE A CA  1 
ATOM   1510 C C   . PHE A 1 205 ? 5.41300   18.82500  90.53900  1.000 29.43759 ? 205 PHE A C   1 
ATOM   1511 O O   . PHE A 1 205 ? 4.48600   19.62200  90.36800  1.000 33.01726 ? 205 PHE A O   1 
ATOM   1512 C CB  . PHE A 1 205 ? 6.58500   20.48100  92.02900  1.000 27.90888 ? 205 PHE A CB  1 
ATOM   1513 C CG  . PHE A 1 205 ? 7.32300   20.71500  93.31900  1.000 33.14902 ? 205 PHE A CG  1 
ATOM   1514 C CD1 . PHE A 1 205 ? 8.70300   20.59500  93.37500  1.000 33.13763 ? 205 PHE A CD1 1 
ATOM   1515 C CD2 . PHE A 1 205 ? 6.63500   21.02700  94.47900  1.000 32.60495 ? 205 PHE A CD2 1 
ATOM   1516 C CE1 . PHE A 1 205 ? 9.38300   20.79200  94.56300  1.000 29.65665 ? 205 PHE A CE1 1 
ATOM   1517 C CE2 . PHE A 1 205 ? 7.30800   21.22800  95.67000  1.000 32.37138 ? 205 PHE A CE2 1 
ATOM   1518 C CZ  . PHE A 1 205 ? 8.68400   21.10900  95.71100  1.000 33.05119 ? 205 PHE A CZ  1 
ATOM   1519 N N   . GLY A 1 206 ? 5.63000   17.79800  89.71900  1.000 30.50455 ? 206 GLY A N   1 
ATOM   1520 C CA  . GLY A 1 206 ? 4.72400   17.46400  88.63700  1.000 30.42742 ? 206 GLY A CA  1 
ATOM   1521 C C   . GLY A 1 206 ? 5.00300   18.11900  87.29700  1.000 36.02898 ? 206 GLY A C   1 
ATOM   1522 O O   . GLY A 1 206 ? 4.29300   17.81800  86.32500  1.000 27.57259 ? 206 GLY A O   1 
ATOM   1523 N N   . ALA A 1 207 ? 6.00300   18.99700  87.20400  1.000 28.13344 ? 207 ALA A N   1 
ATOM   1524 C CA  . ALA A 1 207 ? 6.36500   19.56500  85.91300  1.000 23.77531 ? 207 ALA A CA  1 
ATOM   1525 C C   . ALA A 1 207 ? 6.73500   18.45700  84.93600  1.000 26.56861 ? 207 ALA A C   1 
ATOM   1526 O O   . ALA A 1 207 ? 7.24500   17.40100  85.31900  1.000 24.86848 ? 207 ALA A O   1 
ATOM   1527 C CB  . ALA A 1 207 ? 7.53000   20.54000  86.06000  1.000 23.14997 ? 207 ALA A CB  1 
ATOM   1528 N N   . ASP A 1 208 ? 6.44000   18.68900  83.66200  1.000 24.43126 ? 208 ASP A N   1 
ATOM   1529 C CA  . ASP A 1 208 ? 6.78500   17.72600  82.62600  1.000 26.62691 ? 208 ASP A CA  1 
ATOM   1530 C C   . ASP A 1 208 ? 8.05000   18.09800  81.86900  1.000 24.85646 ? 208 ASP A C   1 
ATOM   1531 O O   . ASP A 1 208 ? 8.77100   17.20300  81.42400  1.000 26.46750 ? 208 ASP A O   1 
ATOM   1532 C CB  . ASP A 1 208 ? 5.61800   17.57400  81.64500  1.000 28.77171 ? 208 ASP A CB  1 
ATOM   1533 C CG  . ASP A 1 208 ? 4.36700   17.03900  82.32100  1.000 30.53573 ? 208 ASP A CG  1 
ATOM   1534 O OD1 . ASP A 1 208 ? 4.29500   15.81400  82.54800  1.000 28.31759 ? 208 ASP A OD1 1 
ATOM   1535 O OD2 . ASP A 1 208 ? 3.47800   17.85000  82.66100  1.000 29.45018 ? 208 ASP A OD2 1 
ATOM   1536 N N   . LEU A 1 209 ? 8.34300   19.39300  81.73200  1.000 24.86125 ? 209 LEU A N   1 
ATOM   1537 C CA  . LEU A 1 209 ? 9.57600   19.87100  81.12000  1.000 25.43537 ? 209 LEU A CA  1 
ATOM   1538 C C   . LEU A 1 209 ? 10.18000  20.98600  81.96200  1.000 23.80485 ? 209 LEU A C   1 
ATOM   1539 O O   . LEU A 1 209 ? 9.47600   21.90100  82.39800  1.000 23.77132 ? 209 LEU A O   1 
ATOM   1540 C CB  . LEU A 1 209 ? 9.33800   20.38200  79.69800  1.000 21.94821 ? 209 LEU A CB  1 
ATOM   1541 C CG  . LEU A 1 209 ? 8.98300   19.33300  78.65000  1.000 22.98197 ? 209 LEU A CG  1 
ATOM   1542 C CD1 . LEU A 1 209 ? 8.74500   20.00300  77.30900  1.000 21.71116 ? 209 LEU A CD1 1 
ATOM   1543 C CD2 . LEU A 1 209 ? 10.09200  18.30100  78.55700  1.000 20.08662 ? 209 LEU A CD2 1 
ATOM   1544 N N   . VAL A 1 210 ? 11.48900  20.91000  82.17400  1.000 23.55187 ? 210 VAL A N   1 
ATOM   1545 C CA  . VAL A 1 210 ? 12.24700  21.95000  82.85600  1.000 23.02108 ? 210 VAL A CA  1 
ATOM   1546 C C   . VAL A 1 210 ? 13.15400  22.61900  81.83300  1.000 22.48807 ? 210 VAL A C   1 
ATOM   1547 O O   . VAL A 1 210 ? 13.91200  21.94200  81.12800  1.000 23.88634 ? 210 VAL A O   1 
ATOM   1548 C CB  . VAL A 1 210 ? 13.06000  21.38000  84.03000  1.000 20.85053 ? 210 VAL A CB  1 
ATOM   1549 C CG1 . VAL A 1 210 ? 13.71500  22.51000  84.80700  1.000 22.31113 ? 210 VAL A CG1 1 
ATOM   1550 C CG2 . VAL A 1 210 ? 12.16300  20.56500  84.93500  1.000 26.73722 ? 210 VAL A CG2 1 
ATOM   1551 N N   . ILE A 1 211 ? 13.06100  23.94100  81.74100  1.000 24.33897 ? 211 ILE A N   1 
ATOM   1552 C CA  . ILE A 1 211 ? 13.79000  24.73200  80.75800  1.000 22.18915 ? 211 ILE A CA  1 
ATOM   1553 C C   . ILE A 1 211 ? 14.91500  25.45500  81.48000  1.000 25.21941 ? 211 ILE A C   1 
ATOM   1554 O O   . ILE A 1 211 ? 14.72800  25.95300  82.59700  1.000 21.77722 ? 211 ILE A O   1 
ATOM   1555 C CB  . ILE A 1 211 ? 12.87000  25.73700  80.03900  1.000 23.55004 ? 211 ILE A CB  1 
ATOM   1556 C CG1 . ILE A 1 211 ? 11.68400  25.02000  79.40000  1.000 22.83220 ? 211 ILE A CG1 1 
ATOM   1557 C CG2 . ILE A 1 211 ? 13.64400  26.55000  79.00900  1.000 21.38549 ? 211 ILE A CG2 1 
ATOM   1558 C CD1 . ILE A 1 211 ? 12.06000  23.80300  78.61200  1.000 26.57887 ? 211 ILE A CD1 1 
ATOM   1559 N N   . HIS A 1 212 ? 16.08800  25.49100  80.85700  1.000 20.65442 ? 212 HIS A N   1 
ATOM   1560 C CA  . HIS A 1 212 ? 17.23700  26.16200  81.44200  1.000 21.16442 ? 212 HIS A CA  1 
ATOM   1561 C C   . HIS A 1 212 ? 17.85300  27.12400  80.44800  1.000 22.88145 ? 212 HIS A C   1 
ATOM   1562 O O   . HIS A 1 212 ? 17.88100  26.86000  79.24200  1.000 25.32896 ? 212 HIS A O   1 
ATOM   1563 C CB  . HIS A 1 212 ? 18.29500  25.16500  81.90800  1.000 18.74658 ? 212 HIS A CB  1 
ATOM   1564 C CG  . HIS A 1 212 ? 17.95900  24.52200  83.21300  1.000 26.75413 ? 212 HIS A CG  1 
ATOM   1565 N ND1 . HIS A 1 212 ? 17.87100  25.23900  84.38700  1.000 23.20786 ? 212 HIS A ND1 1 
ATOM   1566 C CD2 . HIS A 1 212 ? 17.66400  23.24000  83.53000  1.000 18.61547 ? 212 HIS A CD2 1 
ATOM   1567 C CE1 . HIS A 1 212 ? 17.54300  24.42500  85.37300  1.000 23.45201 ? 212 HIS A CE1 1 
ATOM   1568 N NE2 . HIS A 1 212 ? 17.41700  23.20500  84.88100  1.000 27.51064 ? 212 HIS A NE2 1 
ATOM   1569 N N   . SER A 1 213 ? 18.32000  28.24900  80.96700  1.000 22.40976 ? 213 SER A N   1 
ATOM   1570 C CA  . SER A 1 213 ? 19.29600  29.08700  80.28500  1.000 21.42577 ? 213 SER A CA  1 
ATOM   1571 C C   . SER A 1 213 ? 20.63000  28.77300  80.94800  1.000 22.62409 ? 213 SER A C   1 
ATOM   1572 O O   . SER A 1 213 ? 20.89300  29.21200  82.07100  1.000 23.85215 ? 213 SER A O   1 
ATOM   1573 C CB  . SER A 1 213 ? 18.93600  30.56500  80.39600  1.000 22.30623 ? 213 SER A CB  1 
ATOM   1574 O OG  . SER A 1 213 ? 19.93600  31.39300  79.82300  1.000 25.01653 ? 213 SER A OG  1 
ATOM   1575 N N   . ALA A 1 214 ? 21.46400  27.97800  80.26800  1.000 21.34952 ? 214 ALA A N   1 
ATOM   1576 C CA  . ALA A 1 214 ? 22.81100  27.74200  80.77600  1.000 18.07054 ? 214 ALA A CA  1 
ATOM   1577 C C   . ALA A 1 214 ? 23.61000  29.03200  80.81000  1.000 20.32320 ? 214 ALA A C   1 
ATOM   1578 O O   . ALA A 1 214 ? 24.61300  29.12200  81.52500  1.000 19.61985 ? 214 ALA A O   1 
ATOM   1579 C CB  . ALA A 1 214 ? 23.52300  26.69000  79.92700  1.000 15.50048 ? 214 ALA A CB  1 
ATOM   1580 N N   . THR A 1 215 ? 23.15100  30.03500  80.06000  1.000 20.76148 ? 215 THR A N   1 
ATOM   1581 C CA  . THR A 1 215 ? 23.76600  31.35100  80.03400  1.000 18.05040 ? 215 THR A CA  1 
ATOM   1582 C C   . THR A 1 215 ? 23.89900  31.95300  81.42500  1.000 21.49295 ? 215 THR A C   1 
ATOM   1583 O O   . THR A 1 215 ? 24.86100  32.68200  81.70400  1.000 17.57689 ? 215 THR A O   1 
ATOM   1584 C CB  . THR A 1 215 ? 22.91900  32.27100  79.15900  1.000 20.14421 ? 215 THR A CB  1 
ATOM   1585 O OG1 . THR A 1 215 ? 22.63900  31.62200  77.91200  1.000 18.85289 ? 215 THR A OG1 1 
ATOM   1586 C CG2 . THR A 1 215 ? 23.62100  33.57900  78.91800  1.000 20.96258 ? 215 THR A CG2 1 
ATOM   1587 N N   . LYS A 1 216 ? 22.91300  31.72100  82.29400  1.000 21.05456 ? 216 LYS A N   1 
ATOM   1588 C CA  . LYS A 1 216 ? 22.93400  32.46900  83.54000  1.000 22.43437 ? 216 LYS A CA  1 
ATOM   1589 C C   . LYS A 1 216 ? 23.78700  31.81100  84.61900  1.000 21.17897 ? 216 LYS A C   1 
ATOM   1590 O O   . LYS A 1 216 ? 24.97700  32.11500  84.73000  1.000 25.41107 ? 216 LYS A O   1 
ATOM   1591 C CB  . LYS A 1 216 ? 21.50000  32.65800  84.04000  1.000 25.14499 ? 216 LYS A CB  1 
ATOM   1592 C CG  . LYS A 1 216 ? 20.55400  33.27600  83.01000  1.000 20.84160 ? 216 LYS A CG  1 
ATOM   1593 C CD  . LYS A 1 216 ? 21.14600  34.54700  82.42300  1.000 25.69400 ? 216 LYS A CD  1 
ATOM   1594 C CE  . LYS A 1 216 ? 20.06700  35.54300  81.99900  1.000 29.97929 ? 216 LYS A CE  1 
ATOM   1595 N NZ  . LYS A 1 216 ? 19.02500  34.94700  81.12300  1.000 28.09083 ? 216 LYS A NZ  1 
ATOM   1596 N N   . TYR A 1 217 ? 23.26100  30.79500  85.29700  1.000 22.72450 ? 217 TYR A N   1 
ATOM   1597 C CA  . TYR A 1 217 ? 23.93000  30.28600  86.48900  1.000 19.03911 ? 217 TYR A CA  1 
ATOM   1598 C C   . TYR A 1 217 ? 24.72400  29.01900  86.23600  1.000 17.89175 ? 217 TYR A C   1 
ATOM   1599 O O   . TYR A 1 217 ? 25.72800  28.78800  86.91700  1.000 16.00949 ? 217 TYR A O   1 
ATOM   1600 C CB  . TYR A 1 217 ? 22.92700  29.99700  87.60600  1.000 26.53920 ? 217 TYR A CB  1 
ATOM   1601 C CG  . TYR A 1 217 ? 22.48500  31.17500  88.44700  1.000 23.13719 ? 217 TYR A CG  1 
ATOM   1602 C CD1 . TYR A 1 217 ? 23.36700  31.81400  89.31000  1.000 21.80215 ? 217 TYR A CD1 1 
ATOM   1603 C CD2 . TYR A 1 217 ? 21.16700  31.61400  88.41200  1.000 25.73380 ? 217 TYR A CD2 1 
ATOM   1604 C CE1 . TYR A 1 217 ? 22.95100  32.88200  90.09700  1.000 25.28863 ? 217 TYR A CE1 1 
ATOM   1605 C CE2 . TYR A 1 217 ? 20.73900  32.67500  89.19100  1.000 24.65666 ? 217 TYR A CE2 1 
ATOM   1606 C CZ  . TYR A 1 217 ? 21.63100  33.30700  90.02900  1.000 28.94475 ? 217 TYR A CZ  1 
ATOM   1607 O OH  . TYR A 1 217 ? 21.19100  34.36100  90.79600  1.000 26.83382 ? 217 TYR A OH  1 
ATOM   1608 N N   . LEU A 1 218 ? 24.28400  28.18700  85.29100  1.000 17.71367 ? 218 LEU A N   1 
ATOM   1609 C CA  . LEU A 1 218 ? 25.03600  26.98400  84.95900  1.000 19.54353 ? 218 LEU A CA  1 
ATOM   1610 C C   . LEU A 1 218 ? 26.43200  27.34600  84.46800  1.000 21.52939 ? 218 LEU A C   1 
ATOM   1611 O O   . LEU A 1 218 ? 27.43300  26.77200  84.91800  1.000 17.90999 ? 218 LEU A O   1 
ATOM   1612 C CB  . LEU A 1 218 ? 24.27500  26.17100  83.91100  1.000 15.40684 ? 218 LEU A CB  1 
ATOM   1613 C CG  . LEU A 1 218 ? 22.78100  25.96000  84.19000  1.000 19.16609 ? 218 LEU A CG  1 
ATOM   1614 C CD1 . LEU A 1 218 ? 22.13700  25.04300  83.13100  1.000 14.88726 ? 218 LEU A CD1 1 
ATOM   1615 C CD2 . LEU A 1 218 ? 22.54400  25.42700  85.61400  1.000 16.43138 ? 218 LEU A CD2 1 
ATOM   1616 N N   . ASP A 1 219 ? 26.51800  28.30600  83.54300  1.000 18.07888 ? 219 ASP A N   1 
ATOM   1617 C CA  . ASP A 1 219 ? 27.80000  28.94500  83.26200  1.000 18.24575 ? 219 ASP A CA  1 
ATOM   1618 C C   . ASP A 1 219 ? 28.29100  29.68200  84.49900  1.000 19.82815 ? 219 ASP A C   1 
ATOM   1619 O O   . ASP A 1 219 ? 29.41200  29.45700  84.97000  1.000 21.34617 ? 219 ASP A O   1 
ATOM   1620 C CB  . ASP A 1 219 ? 27.65200  29.89900  82.06700  1.000 17.18727 ? 219 ASP A CB  1 
ATOM   1621 C CG  . ASP A 1 219 ? 28.97000  30.56900  81.64500  1.000 20.78328 ? 219 ASP A CG  1 
ATOM   1622 O OD1 . ASP A 1 219 ? 29.70200  31.12100  82.49900  1.000 17.01580 ? 219 ASP A OD1 1 
ATOM   1623 O OD2 . ASP A 1 219 ? 29.26000  30.56100  80.42800  1.000 23.07546 ? 219 ASP A OD2 1 
ATOM   1624 N N   . GLY A 1 220 ? 27.44500  30.55200  85.05200  1.000 20.00806 ? 220 GLY A N   1 
ATOM   1625 C CA  . GLY A 1 220 ? 27.72100  31.23800  86.29300  1.000 17.02421 ? 220 GLY A CA  1 
ATOM   1626 C C   . GLY A 1 220 ? 28.73700  32.35100  86.20700  1.000 20.36725 ? 220 GLY A C   1 
ATOM   1627 O O   . GLY A 1 220 ? 29.01000  32.99200  87.23000  1.000 14.74675 ? 220 GLY A O   1 
ATOM   1628 N N   . GLN A 1 221 ? 29.31900  32.60000  85.02400  1.000 21.73628 ? 221 GLN A N   1 
ATOM   1629 C CA  . GLN A 1 221 ? 30.35900  33.61700  84.90800  1.000 20.75363 ? 221 GLN A CA  1 
ATOM   1630 C C   . GLN A 1 221 ? 30.24300  34.43100  83.62000  1.000 19.01174 ? 221 GLN A C   1 
ATOM   1631 O O   . GLN A 1 221 ? 31.22000  35.07700  83.21500  1.000 17.72314 ? 221 GLN A O   1 
ATOM   1632 C CB  . GLN A 1 221 ? 31.74400  32.97300  85.03300  1.000 18.00100 ? 221 GLN A CB  1 
ATOM   1633 C CG  . GLN A 1 221 ? 32.09900  32.65400  86.48000  1.000 19.52454 ? 221 GLN A CG  1 
ATOM   1634 C CD  . GLN A 1 221 ? 33.36800  31.83600  86.63000  1.000 20.83161 ? 221 GLN A CD  1 
ATOM   1635 O OE1 . GLN A 1 221 ? 33.39400  30.64700  86.32100  1.000 23.02797 ? 221 GLN A OE1 1 
ATOM   1636 N NE2 . GLN A 1 221 ? 34.42800  32.47300  87.11500  1.000 17.16162 ? 221 GLN A NE2 1 
ATOM   1637 N N   . GLY A 1 222 ? 29.07600  34.41900  82.97700  1.000 17.07570 ? 222 GLY A N   1 
ATOM   1638 C CA  . GLY A 1 222 ? 28.77800  35.36100  81.91600  1.000 20.67531 ? 222 GLY A CA  1 
ATOM   1639 C C   . GLY A 1 222 ? 29.49900  35.11500  80.61300  1.000 24.64905 ? 222 GLY A C   1 
ATOM   1640 O O   . GLY A 1 222 ? 29.58800  36.02800  79.78700  1.000 23.17337 ? 222 GLY A O   1 
ATOM   1641 N N   . ARG A 1 223 ? 29.99100  33.89700  80.38800  1.000 20.26781 ? 223 ARG A N   1 
ATOM   1642 C CA  . ARG A 1 223 ? 30.87700  33.63700  79.26300  1.000 19.82382 ? 223 ARG A CA  1 
ATOM   1643 C C   . ARG A 1 223 ? 30.13900  33.21900  77.99700  1.000 20.40506 ? 223 ARG A C   1 
ATOM   1644 O O   . ARG A 1 223 ? 30.55900  33.57800  76.89500  1.000 20.09049 ? 223 ARG A O   1 
ATOM   1645 C CB  . ARG A 1 223 ? 31.89200  32.55600  79.64300  1.000 20.06121 ? 223 ARG A CB  1 
ATOM   1646 C CG  . ARG A 1 223 ? 32.90700  33.00200  80.68400  1.000 23.86534 ? 223 ARG A CG  1 
ATOM   1647 C CD  . ARG A 1 223 ? 33.56600  31.81600  81.38200  1.000 23.70695 ? 223 ARG A CD  1 
ATOM   1648 N NE  . ARG A 1 223 ? 32.59400  31.00500  82.10300  1.000 19.75102 ? 223 ARG A NE  1 
ATOM   1649 C CZ  . ARG A 1 223 ? 32.89200  29.91400  82.79400  1.000 22.77574 ? 223 ARG A CZ  1 
ATOM   1650 N NH1 . ARG A 1 223 ? 34.13900  29.48500  82.90500  1.000 18.08440 ? 223 ARG A NH1 1 
ATOM   1651 N NH2 . ARG A 1 223 ? 31.91300  29.23500  83.38800  1.000 18.94929 ? 223 ARG A NH2 1 
ATOM   1652 N N   . THR A 1 224 ? 29.06100  32.44900  78.11500  1.000 21.62107 ? 224 THR A N   1 
ATOM   1653 C CA  . THR A 1 224 ? 28.51200  31.75500  76.95700  1.000 20.19995 ? 224 THR A CA  1 
ATOM   1654 C C   . THR A 1 224 ? 26.99200  31.78100  76.97700  1.000 20.47386 ? 224 THR A C   1 
ATOM   1655 O O   . THR A 1 224 ? 26.35900  31.99300  78.01500  1.000 20.91559 ? 224 THR A O   1 
ATOM   1656 C CB  . THR A 1 224 ? 28.96800  30.29400  76.90500  1.000 19.28441 ? 224 THR A CB  1 
ATOM   1657 O OG1 . THR A 1 224 ? 28.58700  29.64700  78.12500  1.000 19.41624 ? 224 THR A OG1 1 
ATOM   1658 C CG2 . THR A 1 224 ? 30.47800  30.19500  76.71900  1.000 16.99100 ? 224 THR A CG2 1 
ATOM   1659 N N   . LEU A 1 225 ? 26.41900  31.54700  75.80100  1.000 19.84706 ? 225 LEU A N   1 
ATOM   1660 C CA  . LEU A 1 225 ? 24.99000  31.31900  75.65200  1.000 21.17262 ? 225 LEU A CA  1 
ATOM   1661 C C   . LEU A 1 225 ? 24.73200  29.82400  75.58700  1.000 16.85096 ? 225 LEU A C   1 
ATOM   1662 O O   . LEU A 1 225 ? 25.50500  29.07700  74.98200  1.000 16.84702 ? 225 LEU A O   1 
ATOM   1663 C CB  . LEU A 1 225 ? 24.43800  31.98800  74.39200  1.000 21.72889 ? 225 LEU A CB  1 
ATOM   1664 C CG  . LEU A 1 225 ? 23.89800  33.41300  74.50500  1.000 27.25233 ? 225 LEU A CG  1 
ATOM   1665 C CD1 . LEU A 1 225 ? 24.92000  34.32900  75.13400  1.000 24.82718 ? 225 LEU A CD1 1 
ATOM   1666 C CD2 . LEU A 1 225 ? 23.51600  33.91800  73.12100  1.000 27.72055 ? 225 LEU A CD2 1 
ATOM   1667 N N   . GLY A 1 226 ? 23.65000  29.39600  76.22000  1.000 19.52349 ? 226 GLY A N   1 
ATOM   1668 C CA  . GLY A 1 226 ? 23.23300  28.01000  76.14100  1.000 18.80290 ? 226 GLY A CA  1 
ATOM   1669 C C   . GLY A 1 226 ? 21.88600  27.82600  76.79900  1.000 18.07860 ? 226 GLY A C   1 
ATOM   1670 O O   . GLY A 1 226 ? 21.44300  28.66000  77.59900  1.000 19.68367 ? 226 GLY A O   1 
ATOM   1671 N N   . GLY A 1 227 ? 21.23700  26.71300  76.44800  1.000 14.50077 ? 227 GLY A N   1 
ATOM   1672 C CA  . GLY A 1 227 ? 19.96600  26.35000  77.03900  1.000 18.63470 ? 227 GLY A CA  1 
ATOM   1673 C C   . GLY A 1 227 ? 19.80300  24.84700  77.04400  1.000 20.91295 ? 227 GLY A C   1 
ATOM   1674 O O   . GLY A 1 227 ? 20.62100  24.11200  76.48700  1.000 19.31161 ? 227 GLY A O   1 
ATOM   1675 N N   . ALA A 1 228 ? 18.73200  24.39000  77.69000  1.000 21.72111 ? 228 ALA A N   1 
ATOM   1676 C CA  . ALA A 1 228 ? 18.45700  22.96100  77.73300  1.000 19.35277 ? 228 ALA A CA  1 
ATOM   1677 C C   . ALA A 1 228 ? 16.98900  22.73200  78.05700  1.000 21.75188 ? 228 ALA A C   1 
ATOM   1678 O O   . ALA A 1 228 ? 16.31300  23.59800  78.61900  1.000 20.28554 ? 228 ALA A O   1 
ATOM   1679 C CB  . ALA A 1 228 ? 19.34900  22.24900  78.75400  1.000 17.08927 ? 228 ALA A CB  1 
ATOM   1680 N N   . VAL A 1 229 ? 16.51300  21.54300  77.68700  1.000 19.89496 ? 229 VAL A N   1 
ATOM   1681 C CA  . VAL A 1 229 ? 15.16700  21.06800  77.98900  1.000 22.07621 ? 229 VAL A CA  1 
ATOM   1682 C C   . VAL A 1 229 ? 15.29500  19.70100  78.64500  1.000 23.20799 ? 229 VAL A C   1 
ATOM   1683 O O   . VAL A 1 229 ? 15.84300  18.77300  78.03800  1.000 23.24548 ? 229 VAL A O   1 
ATOM   1684 C CB  . VAL A 1 229 ? 14.29300  20.96900  76.72800  1.000 22.66493 ? 229 VAL A CB  1 
ATOM   1685 C CG1 . VAL A 1 229 ? 12.88800  20.50200  77.09500  1.000 20.41377 ? 229 VAL A CG1 1 
ATOM   1686 C CG2 . VAL A 1 229 ? 14.26300  22.30300  75.99200  1.000 19.74115 ? 229 VAL A CG2 1 
ATOM   1687 N N   . CYS A 1 230 ? 14.77100  19.56800  79.86400  1.000 20.21810 ? 230 CYS A N   1 
ATOM   1688 C CA  . CYS A 1 230 ? 14.86200  18.33800  80.63800  1.000 23.52405 ? 230 CYS A CA  1 
ATOM   1689 C C   . CYS A 1 230 ? 13.47900  17.73700  80.86400  1.000 26.57295 ? 230 CYS A C   1 
ATOM   1690 O O   . CYS A 1 230 ? 12.48800  18.45800  81.02200  1.000 22.04149 ? 230 CYS A O   1 
ATOM   1691 C CB  . CYS A 1 230 ? 15.52900  18.58300  81.99600  1.000 19.87631 ? 230 CYS A CB  1 
ATOM   1692 S SG  . CYS A 1 230 ? 17.17800  19.26000  81.87900  1.000 27.51010 ? 230 CYS A SG  1 
ATOM   1693 N N   . GLY A 1 231 ? 13.43200  16.40900  80.90400  1.000 23.93432 ? 231 GLY A N   1 
ATOM   1694 C CA  . GLY A 1 231 ? 12.18400  15.69900  81.09700  1.000 23.22586 ? 231 GLY A CA  1 
ATOM   1695 C C   . GLY A 1 231 ? 12.38400  14.20900  80.89400  1.000 24.97645 ? 231 GLY A C   1 
ATOM   1696 O O   . GLY A 1 231 ? 13.51300  13.71000  80.86500  1.000 22.29983 ? 231 GLY A O   1 
ATOM   1697 N N   . SER A 1 232 ? 11.26400  13.50600  80.75200  1.000 22.14065 ? 232 SER A N   1 
ATOM   1698 C CA  . SER A 1 232 ? 11.32200  12.06200  80.56800  1.000 25.75894 ? 232 SER A CA  1 
ATOM   1699 C C   . SER A 1 232 ? 11.86200  11.71800  79.18300  1.000 23.30875 ? 232 SER A C   1 
ATOM   1700 O O   . SER A 1 232 ? 11.76500  12.50600  78.23900  1.000 22.63975 ? 232 SER A O   1 
ATOM   1701 C CB  . SER A 1 232 ? 9.94100   11.43600  80.75800  1.000 21.96508 ? 232 SER A CB  1 
ATOM   1702 O OG  . SER A 1 232 ? 9.11700   11.65400  79.62200  1.000 23.43164 ? 232 SER A OG  1 
ATOM   1703 N N   . THR A 1 233 ? 12.44900  10.52500  79.07600  1.000 22.48548 ? 233 THR A N   1 
ATOM   1704 C CA  . THR A 1 233 ? 12.92400  10.05300  77.78100  1.000 22.23583 ? 233 THR A CA  1 
ATOM   1705 C C   . THR A 1 233 ? 11.79100  10.03500  76.76500  1.000 28.83429 ? 233 THR A C   1 
ATOM   1706 O O   . THR A 1 233 ? 11.97800  10.41700  75.60400  1.000 29.83949 ? 233 THR A O   1 
ATOM   1707 C CB  . THR A 1 233 ? 13.53700  8.65800   77.91900  1.000 24.29037 ? 233 THR A CB  1 
ATOM   1708 O OG1 . THR A 1 233 ? 14.77100  8.74100   78.63900  1.000 21.38118 ? 233 THR A OG1 1 
ATOM   1709 C CG2 . THR A 1 233 ? 13.79500  8.03500   76.55000  1.000 24.94265 ? 233 THR A CG2 1 
ATOM   1710 N N   . GLU A 1 234 ? 10.60400  9.60200   77.19100  1.000 29.15607 ? 234 GLU A N   1 
ATOM   1711 C CA  . GLU A 1 234 ? 9.47700   9.49800   76.27300  1.000 31.17360 ? 234 GLU A CA  1 
ATOM   1712 C C   . GLU A 1 234 ? 9.00800   10.86900  75.80000  1.000 26.88664 ? 234 GLU A C   1 
ATOM   1713 O O   . GLU A 1 234 ? 8.69800   11.04800  74.61700  1.000 31.49803 ? 234 GLU A O   1 
ATOM   1714 C CB  . GLU A 1 234 ? 8.33800   8.73400   76.94800  1.000 36.53388 ? 234 GLU A CB  1 
ATOM   1715 C CG  . GLU A 1 234 ? 7.03300   8.72000   76.17700  1.000 35.77734 ? 234 GLU A CG  1 
ATOM   1716 C CD  . GLU A 1 234 ? 5.97000   7.90200   76.87900  1.000 42.96555 ? 234 GLU A CD  1 
ATOM   1717 O OE1 . GLU A 1 234 ? 6.10100   6.65900   76.89700  1.000 49.35227 ? 234 GLU A OE1 1 
ATOM   1718 O OE2 . GLU A 1 234 ? 5.01900   8.50000   77.43100  1.000 40.90324 ? 234 GLU A OE2 1 
ATOM   1719 N N   . LEU A 1 235 ? 8.93800   11.84800  76.70600  1.000 26.72455 ? 235 LEU A N   1 
ATOM   1720 C CA  . LEU A 1 235 ? 8.46100   13.17000  76.30600  1.000 23.79030 ? 235 LEU A CA  1 
ATOM   1721 C C   . LEU A 1 235 ? 9.45500   13.86200  75.38100  1.000 26.46003 ? 235 LEU A C   1 
ATOM   1722 O O   . LEU A 1 235 ? 9.05600   14.48500  74.39100  1.000 22.52888 ? 235 LEU A O   1 
ATOM   1723 C CB  . LEU A 1 235 ? 8.18000   14.03200  77.53600  1.000 20.12871 ? 235 LEU A CB  1 
ATOM   1724 C CG  . LEU A 1 235 ? 7.48500   15.36100  77.22400  1.000 22.96246 ? 235 LEU A CG  1 
ATOM   1725 C CD1 . LEU A 1 235 ? 6.21600   15.11000  76.43000  1.000 23.82717 ? 235 LEU A CD1 1 
ATOM   1726 C CD2 . LEU A 1 235 ? 7.16600   16.14400  78.48600  1.000 22.36739 ? 235 LEU A CD2 1 
ATOM   1727 N N   . LEU A 1 236 ? 10.75400  13.76000  75.67800  1.000 23.77275 ? 236 LEU A N   1 
ATOM   1728 C CA  . LEU A 1 236 ? 11.74500  14.41900  74.83500  1.000 24.81803 ? 236 LEU A CA  1 
ATOM   1729 C C   . LEU A 1 236 ? 11.86800  13.73700  73.47900  1.000 28.99381 ? 236 LEU A C   1 
ATOM   1730 O O   . LEU A 1 236 ? 12.26900  14.37600  72.49900  1.000 25.38438 ? 236 LEU A O   1 
ATOM   1731 C CB  . LEU A 1 236 ? 13.10400  14.46200  75.54000  1.000 23.89969 ? 236 LEU A CB  1 
ATOM   1732 C CG  . LEU A 1 236 ? 13.46500  15.75900  76.27700  1.000 27.07557 ? 236 LEU A CG  1 
ATOM   1733 C CD1 . LEU A 1 236 ? 12.59700  15.97200  77.49300  1.000 24.27761 ? 236 LEU A CD1 1 
ATOM   1734 C CD2 . LEU A 1 236 ? 14.91900  15.75400  76.68400  1.000 30.39460 ? 236 LEU A CD2 1 
ATOM   1735 N N   . ASN A 1 237 ? 11.52700  12.45400  73.39800  1.000 26.48899 ? 237 ASN A N   1 
ATOM   1736 C CA  . ASN A 1 237 ? 11.55400  11.72800  72.13800  1.000 25.14707 ? 237 ASN A CA  1 
ATOM   1737 C C   . ASN A 1 237 ? 10.26100  11.86100  71.34900  1.000 26.48746 ? 237 ASN A C   1 
ATOM   1738 O O   . ASN A 1 237 ? 10.15100  11.27400  70.27000  1.000 28.06729 ? 237 ASN A O   1 
ATOM   1739 C CB  . ASN A 1 237 ? 11.85000  10.24900  72.38500  1.000 26.78681 ? 237 ASN A CB  1 
ATOM   1740 C CG  . ASN A 1 237 ? 13.29400  10.00400  72.75100  1.000 35.42675 ? 237 ASN A CG  1 
ATOM   1741 O OD1 . ASN A 1 237 ? 14.15300  10.86500  72.54500  1.000 32.23112 ? 237 ASN A OD1 1 
ATOM   1742 N ND2 . ASN A 1 237 ? 13.57600  8.82100   73.28800  1.000 34.84004 ? 237 ASN A ND2 1 
ATOM   1743 N N   . SER A 1 238 ? 9.28300   12.61000  71.85700  1.000 25.37125 ? 238 SER A N   1 
ATOM   1744 C CA  . SER A 1 238 ? 8.02900   12.84400  71.15600  1.000 25.94698 ? 238 SER A CA  1 
ATOM   1745 C C   . SER A 1 238 ? 8.02400   14.17900  70.42000  1.000 30.96291 ? 238 SER A C   1 
ATOM   1746 O O   . SER A 1 238 ? 6.95200   14.74400  70.17700  1.000 33.54547 ? 238 SER A O   1 
ATOM   1747 C CB  . SER A 1 238 ? 6.85400   12.77600  72.12900  1.000 28.46979 ? 238 SER A CB  1 
ATOM   1748 O OG  . SER A 1 238 ? 6.70300   14.00700  72.82000  1.000 35.29078 ? 238 SER A OG  1 
ATOM   1749 N N   . GLY A 1 239 ? 9.19900   14.69400  70.06000  1.000 24.97192 ? 239 GLY A N   1 
ATOM   1750 C CA  . GLY A 1 239 ? 9.28500   15.88700  69.25300  1.000 23.37523 ? 239 GLY A CA  1 
ATOM   1751 C C   . GLY A 1 239 ? 10.35000  16.90200  69.63700  1.000 29.12856 ? 239 GLY A C   1 
ATOM   1752 O O   . GLY A 1 239 ? 10.99200  17.48200  68.75100  1.000 25.25264 ? 239 GLY A O   1 
ATOM   1753 N N   . PRO A 1 240 ? 10.60100  17.12200  70.93800  1.000 23.28229 ? 240 PRO A N   1 
ATOM   1754 C CA  . PRO A 1 240 ? 11.66100  18.09000  71.30100  1.000 23.45810 ? 240 PRO A CA  1 
ATOM   1755 C C   . PRO A 1 240 ? 13.03900  17.72300  70.77000  1.000 24.61899 ? 240 PRO A C   1 
ATOM   1756 O O   . PRO A 1 240 ? 13.71700  18.58400  70.19400  1.000 24.15126 ? 240 PRO A O   1 
ATOM   1757 C CB  . PRO A 1 240 ? 11.61500  18.09500  72.83600  1.000 26.21321 ? 240 PRO A CB  1 
ATOM   1758 C CG  . PRO A 1 240 ? 10.20000  17.78100  73.15800  1.000 24.36186 ? 240 PRO A CG  1 
ATOM   1759 C CD  . PRO A 1 240 ? 9.75100   16.79700  72.09900  1.000 25.93647 ? 240 PRO A CD  1 
ATOM   1760 N N   . ARG A 1 241 ? 13.47500  16.46900  70.94700  1.000 24.52705 ? 241 ARG A N   1 
ATOM   1761 C CA  . ARG A 1 241 ? 14.76400  16.04500  70.40300  1.000 22.97069 ? 241 ARG A CA  1 
ATOM   1762 C C   . ARG A 1 241 ? 14.78200  16.14800  68.88700  1.000 25.61454 ? 241 ARG A C   1 
ATOM   1763 O O   . ARG A 1 241 ? 15.75600  16.63700  68.30100  1.000 25.49736 ? 241 ARG A O   1 
ATOM   1764 C CB  . ARG A 1 241 ? 15.07800  14.60600  70.81000  1.000 27.71998 ? 241 ARG A CB  1 
ATOM   1765 C CG  . ARG A 1 241 ? 15.32000  14.38600  72.27900  1.000 33.95994 ? 241 ARG A CG  1 
ATOM   1766 C CD  . ARG A 1 241 ? 16.75300  14.02500  72.53500  1.000 34.45702 ? 241 ARG A CD  1 
ATOM   1767 N NE  . ARG A 1 241 ? 16.89100  13.25700  73.76300  1.000 37.43820 ? 241 ARG A NE  1 
ATOM   1768 C CZ  . ARG A 1 241 ? 17.96100  13.29700  74.54200  1.000 39.17989 ? 241 ARG A CZ  1 
ATOM   1769 N NH1 . ARG A 1 241 ? 18.97800  14.10600  74.27500  1.000 32.34613 ? 241 ARG A NH1 1 
ATOM   1770 N NH2 . ARG A 1 241 ? 18.01200  12.51200  75.61500  1.000 35.53889 ? 241 ARG A NH2 1 
ATOM   1771 N N   . ASN A 1 242 ? 13.71500  15.67900  68.23300  1.000 24.72927 ? 242 ASN A N   1 
ATOM   1772 C CA  . ASN A 1 242 ? 13.65400  15.75400  66.78000  1.000 23.21329 ? 242 ASN A CA  1 
ATOM   1773 C C   . ASN A 1 242 ? 13.72400  17.19700  66.30600  1.000 22.20348 ? 242 ASN A C   1 
ATOM   1774 O O   . ASN A 1 242 ? 14.32800  17.48500  65.27000  1.000 22.39195 ? 242 ASN A O   1 
ATOM   1775 C CB  . ASN A 1 242 ? 12.38300  15.08200  66.26400  1.000 22.77887 ? 242 ASN A CB  1 
ATOM   1776 C CG  . ASN A 1 242 ? 12.20400  15.25500  64.76300  1.000 25.88594 ? 242 ASN A CG  1 
ATOM   1777 O OD1 . ASN A 1 242 ? 11.42300  16.09400  64.31100  1.000 30.42817 ? 242 ASN A OD1 1 
ATOM   1778 N ND2 . ASN A 1 242 ? 12.94600  14.48100  63.98700  1.000 20.60542 ? 242 ASN A ND2 1 
ATOM   1779 N N   . PHE A 1 243 ? 13.11500  18.12200  67.05200  1.000 23.04582 ? 243 PHE A N   1 
ATOM   1780 C CA  . PHE A 1 243 ? 13.17700  19.52400  66.65800  1.000 22.22535 ? 243 PHE A CA  1 
ATOM   1781 C C   . PHE A 1 243 ? 14.60900  20.04100  66.67700  1.000 23.49123 ? 243 PHE A C   1 
ATOM   1782 O O   . PHE A 1 243 ? 15.03600  20.73000  65.74600  1.000 24.40134 ? 243 PHE A O   1 
ATOM   1783 C CB  . PHE A 1 243 ? 12.29800  20.37800  67.56600  1.000 23.11503 ? 243 PHE A CB  1 
ATOM   1784 C CG  . PHE A 1 243 ? 12.29700  21.83500  67.20200  1.000 24.55516 ? 243 PHE A CG  1 
ATOM   1785 C CD1 . PHE A 1 243 ? 11.49600  22.30200  66.17500  1.000 21.08789 ? 243 PHE A CD1 1 
ATOM   1786 C CD2 . PHE A 1 243 ? 13.10500  22.73700  67.87700  1.000 25.63536 ? 243 PHE A CD2 1 
ATOM   1787 C CE1 . PHE A 1 243 ? 11.49900  23.64200  65.82900  1.000 22.19991 ? 243 PHE A CE1 1 
ATOM   1788 C CE2 . PHE A 1 243 ? 13.10700  24.08300  67.53500  1.000 21.23806 ? 243 PHE A CE2 1 
ATOM   1789 C CZ  . PHE A 1 243 ? 12.30100  24.53200  66.51100  1.000 19.02841 ? 243 PHE A CZ  1 
ATOM   1790 N N   . VAL A 1 244 ? 15.36700  19.71900  67.72600  1.000 23.34112 ? 244 VAL A N   1 
ATOM   1791 C CA  . VAL A 1 244 ? 16.73300  20.23200  67.82900  1.000 21.24257 ? 244 VAL A CA  1 
ATOM   1792 C C   . VAL A 1 244 ? 17.59800  19.67900  66.70300  1.000 25.63463 ? 244 VAL A C   1 
ATOM   1793 O O   . VAL A 1 244 ? 18.39900  20.40600  66.09800  1.000 23.04397 ? 244 VAL A O   1 
ATOM   1794 C CB  . VAL A 1 244 ? 17.32200  19.91400  69.21700  1.000 22.40697 ? 244 VAL A CB  1 
ATOM   1795 C CG1 . VAL A 1 244 ? 18.82000  20.20300  69.25100  1.000 19.51171 ? 244 VAL A CG1 1 
ATOM   1796 C CG2 . VAL A 1 244 ? 16.60400  20.72600  70.28200  1.000 17.82201 ? 244 VAL A CG2 1 
ATOM   1797 N N   . ARG A 1 245 ? 17.44100  18.38900  66.39200  1.000 21.12290 ? 245 ARG A N   1 
ATOM   1798 C CA  A ARG A 1 245 ? 18.25000  17.80800  65.32900  0.490 23.87800 ? 245 ARG A CA  1 
ATOM   1799 C CA  B ARG A 1 245 ? 18.21500  17.76700  65.32100  0.510 23.85753 ? 245 ARG A CA  1 
ATOM   1800 C C   . ARG A 1 245 ? 17.83500  18.31500  63.95200  1.000 20.62052 ? 245 ARG A C   1 
ATOM   1801 O O   . ARG A 1 245 ? 18.68500  18.41800  63.06100  1.000 22.81386 ? 245 ARG A O   1 
ATOM   1802 C CB  A ARG A 1 245 ? 18.18200  16.28200  65.38800  0.490 26.68011 ? 245 ARG A CB  1 
ATOM   1803 C CB  B ARG A 1 245 ? 18.01300  16.25000  65.34200  0.510 26.59099 ? 245 ARG A CB  1 
ATOM   1804 C CG  A ARG A 1 245 ? 16.85200  15.69100  65.00300  0.490 24.68988 ? 245 ARG A CG  1 
ATOM   1805 C CG  B ARG A 1 245 ? 18.58200  15.54600  66.56800  0.510 28.99829 ? 245 ARG A CG  1 
ATOM   1806 C CD  A ARG A 1 245 ? 16.76300  14.24100  65.42900  0.490 29.52213 ? 245 ARG A CD  1 
ATOM   1807 C CD  B ARG A 1 245 ? 18.02200  14.13800  66.70400  0.510 28.41980 ? 245 ARG A CD  1 
ATOM   1808 N NE  A ARG A 1 245 ? 17.72700  13.38800  64.74600  0.490 31.70106 ? 245 ARG A NE  1 
ATOM   1809 N NE  B ARG A 1 245 ? 18.52100  13.46600  67.89800  0.510 31.86182 ? 245 ARG A NE  1 
ATOM   1810 C CZ  A ARG A 1 245 ? 17.51400  12.82100  63.56700  0.490 33.35253 ? 245 ARG A CZ  1 
ATOM   1811 C CZ  B ARG A 1 245 ? 19.33600  12.42000  67.88500  0.510 33.24107 ? 245 ARG A CZ  1 
ATOM   1812 N NH1 A ARG A 1 245 ? 16.39000  13.01800  62.89800  0.490 30.69791 ? 245 ARG A NH1 1 
ATOM   1813 N NH1 B ARG A 1 245 ? 19.74500  11.87600  66.75000  0.510 32.31532 ? 245 ARG A NH1 1 
ATOM   1814 N NH2 A ARG A 1 245 ? 18.45200  12.03400  63.04700  0.490 37.16996 ? 245 ARG A NH2 1 
ATOM   1815 N NH2 B ARG A 1 245 ? 19.74200  11.90100  69.03900  0.510 34.95577 ? 245 ARG A NH2 1 
ATOM   1816 N N   . THR A 1 246 ? 16.56200  18.65500  63.76300  1.000 19.60543 ? 246 THR A N   1 
ATOM   1817 C CA  . THR A 1 246 ? 16.03900  19.04200  62.45700  1.000 19.81571 ? 246 THR A CA  1 
ATOM   1818 C C   . THR A 1 246 ? 16.09300  20.55000  62.21900  1.000 21.52212 ? 246 THR A C   1 
ATOM   1819 O O   . THR A 1 246 ? 16.55400  20.99300  61.16500  1.000 18.90096 ? 246 THR A O   1 
ATOM   1820 C CB  . THR A 1 246 ? 14.60000  18.53400  62.30600  1.000 18.82718 ? 246 THR A CB  1 
ATOM   1821 O OG1 . THR A 1 246 ? 14.57700  17.11300  62.49300  1.000 20.20105 ? 246 THR A OG1 1 
ATOM   1822 C CG2 . THR A 1 246 ? 14.05600  18.85400  60.93100  1.000 15.03476 ? 246 THR A CG2 1 
ATOM   1823 N N   . ALA A 1 247 ? 15.61100  21.35000  63.17100  1.000 18.16540 ? 247 ALA A N   1 
ATOM   1824 C CA  . ALA A 1 247 ? 15.69400  22.79800  63.05300  1.000 16.57919 ? 247 ALA A CA  1 
ATOM   1825 C C   . ALA A 1 247 ? 17.05600  23.34800  63.45600  1.000 18.10630 ? 247 ALA A C   1 
ATOM   1826 O O   . ALA A 1 247 ? 17.32100  24.53000  63.21800  1.000 17.64410 ? 247 ALA A O   1 
ATOM   1827 C CB  . ALA A 1 247 ? 14.59900  23.46300  63.89300  1.000 17.01798 ? 247 ALA A CB  1 
ATOM   1828 N N   . GLY A 1 248 ? 17.90500  22.53600  64.08100  1.000 17.85160 ? 248 GLY A N   1 
ATOM   1829 C CA  . GLY A 1 248 ? 19.27900  22.89000  64.36800  1.000 16.70550 ? 248 GLY A CA  1 
ATOM   1830 C C   . GLY A 1 248 ? 19.59200  24.08500  65.26400  1.000 16.68545 ? 248 GLY A C   1 
ATOM   1831 O O   . GLY A 1 248 ? 20.57900  24.78900  65.02300  1.000 16.15974 ? 248 GLY A O   1 
ATOM   1832 N N   . PRO A 1 249 ? 18.81400  24.33300  66.34300  1.000 15.62789 ? 249 PRO A N   1 
ATOM   1833 C CA  . PRO A 1 249 ? 19.29300  25.31300  67.33900  1.000 15.05858 ? 249 PRO A CA  1 
ATOM   1834 C C   . PRO A 1 249 ? 20.28000  24.68000  68.31400  1.000 17.76134 ? 249 PRO A C   1 
ATOM   1835 O O   . PRO A 1 249 ? 20.07800  24.67300  69.53000  1.000 19.12118 ? 249 PRO A O   1 
ATOM   1836 C CB  . PRO A 1 249 ? 17.99100  25.73600  68.02700  1.000 17.47030 ? 249 PRO A CB  1 
ATOM   1837 C CG  . PRO A 1 249 ? 17.21200  24.46600  68.06600  1.000 15.64012 ? 249 PRO A CG  1 
ATOM   1838 C CD  . PRO A 1 249 ? 17.51200  23.77000  66.74800  1.000 16.44725 ? 249 PRO A CD  1 
ATOM   1839 N N   . SER A 1 250 ? 21.35500  24.11400  67.77600  1.000 13.22768 ? 250 SER A N   1 
ATOM   1840 C CA  . SER A 1 250 ? 22.20100  23.24600  68.57700  1.000 18.49130 ? 250 SER A CA  1 
ATOM   1841 C C   . SER A 1 250 ? 23.26900  24.04000  69.33200  1.000 20.47997 ? 250 SER A C   1 
ATOM   1842 O O   . SER A 1 250 ? 23.57800  25.19000  69.01400  1.000 20.89680 ? 250 SER A O   1 
ATOM   1843 C CB  . SER A 1 250 ? 22.84700  22.16800  67.70500  1.000 20.99578 ? 250 SER A CB  1 
ATOM   1844 O OG  . SER A 1 250 ? 23.49400  22.73400  66.58900  1.000 22.48910 ? 250 SER A OG  1 
ATOM   1845 N N   . LEU A 1 251 ? 23.82900  23.39600  70.35100  1.000 17.52277 ? 251 LEU A N   1 
ATOM   1846 C CA  . LEU A 1 251 ? 24.79500  24.00900  71.24800  1.000 17.05723 ? 251 LEU A CA  1 
ATOM   1847 C C   . LEU A 1 251 ? 26.20600  23.65800  70.79500  1.000 16.08471 ? 251 LEU A C   1 
ATOM   1848 O O   . LEU A 1 251 ? 26.49600  22.49800  70.47800  1.000 15.02343 ? 251 LEU A O   1 
ATOM   1849 C CB  . LEU A 1 251 ? 24.55800  23.53800  72.68500  1.000 15.28196 ? 251 LEU A CB  1 
ATOM   1850 C CG  . LEU A 1 251 ? 25.48400  24.04800  73.78700  1.000 15.52281 ? 251 LEU A CG  1 
ATOM   1851 C CD1 . LEU A 1 251 ? 25.36900  25.55300  73.91500  1.000 14.47582 ? 251 LEU A CD1 1 
ATOM   1852 C CD2 . LEU A 1 251 ? 25.16300  23.35900  75.11400  1.000 19.19203 ? 251 LEU A CD2 1 
ATOM   1853 N N   . SER A 1 252 ? 27.07300  24.66200  70.75300  1.000 18.56674 ? 252 SER A N   1 
ATOM   1854 C CA  . SER A 1 252 ? 28.44900  24.43600  70.36000  1.000 15.05019 ? 252 SER A CA  1 
ATOM   1855 C C   . SER A 1 252 ? 29.16800  23.57900  71.40100  1.000 19.43939 ? 252 SER A C   1 
ATOM   1856 O O   . SER A 1 252 ? 28.88000  23.67100  72.59900  1.000 15.36346 ? 252 SER A O   1 
ATOM   1857 C CB  . SER A 1 252 ? 29.17500  25.76100  70.20100  1.000 17.30840 ? 252 SER A CB  1 
ATOM   1858 O OG  . SER A 1 252 ? 30.56900  25.55600  70.13100  1.000 19.94894 ? 252 SER A OG  1 
ATOM   1859 N N   . PRO A 1 253 ? 30.08900  22.71600  70.96200  1.000 16.01422 ? 253 PRO A N   1 
ATOM   1860 C CA  . PRO A 1 253 ? 30.87400  21.93300  71.92900  1.000 16.48333 ? 253 PRO A CA  1 
ATOM   1861 C C   . PRO A 1 253 ? 31.69200  22.79500  72.87200  1.000 20.56231 ? 253 PRO A C   1 
ATOM   1862 O O   . PRO A 1 253 ? 31.86000  22.43000  74.04600  1.000 16.69568 ? 253 PRO A O   1 
ATOM   1863 C CB  . PRO A 1 253 ? 31.77800  21.07000  71.03500  1.000 17.53725 ? 253 PRO A CB  1 
ATOM   1864 C CG  . PRO A 1 253 ? 31.13700  21.07600  69.69500  1.000 20.25238 ? 253 PRO A CG  1 
ATOM   1865 C CD  . PRO A 1 253 ? 30.41400  22.37800  69.56700  1.000 18.03117 ? 253 PRO A CD  1 
ATOM   1866 N N   . PHE A 1 254 ? 32.22700  23.92200  72.38400  1.000 14.59884 ? 254 PHE A N   1 
ATOM   1867 C CA  . PHE A 1 254 ? 32.96800  24.82300  73.25700  1.000 17.27649 ? 254 PHE A CA  1 
ATOM   1868 C C   . PHE A 1 254 ? 32.06800  25.35800  74.36000  1.000 16.21752 ? 254 PHE A C   1 
ATOM   1869 O O   . PHE A 1 254 ? 32.45500  25.38700  75.53300  1.000 16.05691 ? 254 PHE A O   1 
ATOM   1870 C CB  . PHE A 1 254 ? 33.56200  25.98200  72.45500  1.000 16.14697 ? 254 PHE A CB  1 
ATOM   1871 C CG  . PHE A 1 254 ? 34.54800  25.56000  71.40900  1.000 18.13987 ? 254 PHE A CG  1 
ATOM   1872 C CD1 . PHE A 1 254 ? 35.86100  25.29200  71.74700  1.000 24.46712 ? 254 PHE A CD1 1 
ATOM   1873 C CD2 . PHE A 1 254 ? 34.16200  25.43800  70.08200  1.000 21.88986 ? 254 PHE A CD2 1 
ATOM   1874 C CE1 . PHE A 1 254 ? 36.77500  24.89900  70.78100  1.000 26.64284 ? 254 PHE A CE1 1 
ATOM   1875 C CE2 . PHE A 1 254 ? 35.06700  25.05400  69.11500  1.000 23.02806 ? 254 PHE A CE2 1 
ATOM   1876 C CZ  . PHE A 1 254 ? 36.37600  24.78300  69.46600  1.000 24.73550 ? 254 PHE A CZ  1 
ATOM   1877 N N   . ASN A 1 255 ? 30.85700  25.79100  73.99600  1.000 15.26023 ? 255 ASN A N   1 
ATOM   1878 C CA  . ASN A 1 255 ? 29.92000  26.30200  74.99000  1.000 16.93189 ? 255 ASN A CA  1 
ATOM   1879 C C   . ASN A 1 255 ? 29.51400  25.20800  75.96300  1.000 14.96411 ? 255 ASN A C   1 
ATOM   1880 O O   . ASN A 1 255 ? 29.41100  25.44600  77.17100  1.000 15.87289 ? 255 ASN A O   1 
ATOM   1881 C CB  . ASN A 1 255 ? 28.67900  26.88400  74.31000  1.000 12.25049 ? 255 ASN A CB  1 
ATOM   1882 C CG  . ASN A 1 255 ? 28.96700  28.16900  73.56800  1.000 16.33109 ? 255 ASN A CG  1 
ATOM   1883 O OD1 . ASN A 1 255 ? 30.02100  28.32500  72.96000  1.000 15.51504 ? 255 ASN A OD1 1 
ATOM   1884 N ND2 . ASN A 1 255 ? 28.02400  29.10100  73.61600  1.000 17.93813 ? 255 ASN A ND2 1 
ATOM   1885 N N   . ALA A 1 256 ? 29.27200  24.00500  75.44800  1.000 11.29630 ? 256 ALA A N   1 
ATOM   1886 C CA  . ALA A 1 256 ? 28.90900  22.89100  76.31100  1.000 14.62226 ? 256 ALA A CA  1 
ATOM   1887 C C   . ALA A 1 256 ? 30.01700  22.60500  77.31000  1.000 15.62251 ? 256 ALA A C   1 
ATOM   1888 O O   . ALA A 1 256 ? 29.75300  22.39600  78.50000  1.000 14.25658 ? 256 ALA A O   1 
ATOM   1889 C CB  . ALA A 1 256 ? 28.60400  21.65600  75.46400  1.000 14.91219 ? 256 ALA A CB  1 
ATOM   1890 N N   . TRP A 1 257 ? 31.26900  22.62900  76.84500  1.000 15.98913 ? 257 TRP A N   1 
ATOM   1891 C CA  . TRP A 1 257 ? 32.41100  22.37400  77.71800  1.000 14.89154 ? 257 TRP A CA  1 
ATOM   1892 C C   . TRP A 1 257 ? 32.50100  23.41600  78.82200  1.000 16.46842 ? 257 TRP A C   1 
ATOM   1893 O O   . TRP A 1 257 ? 32.71400  23.07300  79.99100  1.000 18.18591 ? 257 TRP A O   1 
ATOM   1894 C CB  . TRP A 1 257 ? 33.69300  22.34200  76.88400  1.000 14.92578 ? 257 TRP A CB  1 
ATOM   1895 C CG  . TRP A 1 257 ? 34.94900  22.25800  77.67300  1.000 14.15096 ? 257 TRP A CG  1 
ATOM   1896 C CD1 . TRP A 1 257 ? 35.46800  21.15000  78.27600  1.000 13.81006 ? 257 TRP A CD1 1 
ATOM   1897 C CD2 . TRP A 1 257 ? 35.87100  23.32600  77.93000  1.000 17.12223 ? 257 TRP A CD2 1 
ATOM   1898 N NE1 . TRP A 1 257 ? 36.65500  21.46100  78.90000  1.000 13.28861 ? 257 TRP A NE1 1 
ATOM   1899 C CE2 . TRP A 1 257 ? 36.92500  22.79100  78.70200  1.000 16.98755 ? 257 TRP A CE2 1 
ATOM   1900 C CE3 . TRP A 1 257 ? 35.90800  24.68400  77.58200  1.000 18.00977 ? 257 TRP A CE3 1 
ATOM   1901 C CZ2 . TRP A 1 257 ? 38.00600  23.56600  79.13100  1.000 17.01180 ? 257 TRP A CZ2 1 
ATOM   1902 C CZ3 . TRP A 1 257 ? 36.98200  25.45500  78.01200  1.000 15.91474 ? 257 TRP A CZ3 1 
ATOM   1903 C CH2 . TRP A 1 257 ? 38.01500  24.89300  78.77800  1.000 16.22832 ? 257 TRP A CH2 1 
ATOM   1904 N N   . VAL A 1 258 ? 32.31700  24.69300  78.47600  1.000 14.61454 ? 258 VAL A N   1 
ATOM   1905 C CA  . VAL A 1 258 ? 32.28300  25.73700  79.49600  1.000 16.80849 ? 258 VAL A CA  1 
ATOM   1906 C C   . VAL A 1 258 ? 31.17400  25.45500  80.50200  1.000 15.23913 ? 258 VAL A C   1 
ATOM   1907 O O   . VAL A 1 258 ? 31.37600  25.54200  81.71700  1.000 14.62738 ? 258 VAL A O   1 
ATOM   1908 C CB  . VAL A 1 258 ? 32.10700  27.12400  78.84100  1.000 19.32670 ? 258 VAL A CB  1 
ATOM   1909 C CG1 . VAL A 1 258 ? 31.84700  28.19700  79.90300  1.000 16.44648 ? 258 VAL A CG1 1 
ATOM   1910 C CG2 . VAL A 1 258 ? 33.32100  27.48800  77.98900  1.000 17.97623 ? 258 VAL A CG2 1 
ATOM   1911 N N   . GLN A 1 259 ? 29.99400  25.09000  80.01200  1.000 16.61387 ? 259 GLN A N   1 
ATOM   1912 C CA  . GLN A 1 259 ? 28.83500  24.96300  80.88300  1.000 14.16122 ? 259 GLN A CA  1 
ATOM   1913 C C   . GLN A 1 259 ? 28.89000  23.69300  81.72800  1.000 16.55028 ? 259 GLN A C   1 
ATOM   1914 O O   . GLN A 1 259 ? 28.54900  23.72600  82.91600  1.000 14.76732 ? 259 GLN A O   1 
ATOM   1915 C CB  . GLN A 1 259 ? 27.56300  25.03100  80.03800  1.000 15.21803 ? 259 GLN A CB  1 
ATOM   1916 C CG  . GLN A 1 259 ? 27.36800  26.41100  79.39600  1.000 17.37186 ? 259 GLN A CG  1 
ATOM   1917 C CD  . GLN A 1 259 ? 26.49200  26.37000  78.15300  1.000 20.07852 ? 259 GLN A CD  1 
ATOM   1918 O OE1 . GLN A 1 259 ? 25.90700  25.34000  77.82500  1.000 21.22356 ? 259 GLN A OE1 1 
ATOM   1919 N NE2 . GLN A 1 259 ? 26.40400  27.49300  77.45600  1.000 15.92164 ? 259 GLN A NE2 1 
ATOM   1920 N N   . LEU A 1 260 ? 29.33600  22.57000  81.15700  1.000 15.95842 ? 260 LEU A N   1 
ATOM   1921 C CA  . LEU A 1 260 ? 29.41600  21.35300  81.95600  1.000 16.22165 ? 260 LEU A CA  1 
ATOM   1922 C C   . LEU A 1 260 ? 30.43600  21.50400  83.08100  1.000 15.85673 ? 260 LEU A C   1 
ATOM   1923 O O   . LEU A 1 260 ? 30.22800  20.99300  84.18600  1.000 13.64437 ? 260 LEU A O   1 
ATOM   1924 C CB  . LEU A 1 260 ? 29.72800  20.14100  81.07000  1.000 17.22683 ? 260 LEU A CB  1 
ATOM   1925 C CG  . LEU A 1 260 ? 31.09600  19.94500  80.41500  1.000 15.78610 ? 260 LEU A CG  1 
ATOM   1926 C CD1 . LEU A 1 260 ? 32.06100  19.23400  81.35100  1.000 15.06273 ? 260 LEU A CD1 1 
ATOM   1927 C CD2 . LEU A 1 260 ? 30.93700  19.16600  79.11800  1.000 12.02228 ? 260 LEU A CD2 1 
ATOM   1928 N N   . LYS A 1 261 ? 31.54300  22.21000  82.82700  1.000 13.79659 ? 261 LYS A N   1 
ATOM   1929 C CA  . LYS A 1 261 ? 32.44600  22.52900  83.92600  1.000 17.06148 ? 261 LYS A CA  1 
ATOM   1930 C C   . LYS A 1 261 ? 31.80500  23.51200  84.89800  1.000 17.60716 ? 261 LYS A C   1 
ATOM   1931 O O   . LYS A 1 261 ? 32.06000  23.44300  86.10300  1.000 15.70998 ? 261 LYS A O   1 
ATOM   1932 C CB  . LYS A 1 261 ? 33.76800  23.08000  83.39800  1.000 18.23539 ? 261 LYS A CB  1 
ATOM   1933 C CG  . LYS A 1 261 ? 34.51700  22.11600  82.47100  1.000 21.79745 ? 261 LYS A CG  1 
ATOM   1934 C CD  . LYS A 1 261 ? 34.76500  20.75400  83.11000  1.000 17.18125 ? 261 LYS A CD  1 
ATOM   1935 C CE  . LYS A 1 261 ? 36.05800  20.70900  83.89700  1.000 16.13003 ? 261 LYS A CE  1 
ATOM   1936 N NZ  . LYS A 1 261 ? 36.50000  19.30700  84.16500  1.000 16.37966 ? 261 LYS A NZ  1 
ATOM   1937 N N   . GLY A 1 262 ? 30.96300  24.42000  84.40300  1.000 19.49145 ? 262 GLY A N   1 
ATOM   1938 C CA  . GLY A 1 262 ? 30.28400  25.34200  85.29800  1.000 19.74441 ? 262 GLY A CA  1 
ATOM   1939 C C   . GLY A 1 262 ? 29.36900  24.63500  86.27600  1.000 15.69094 ? 262 GLY A C   1 
ATOM   1940 O O   . GLY A 1 262 ? 29.24500  25.05400  87.42900  1.000 15.20605 ? 262 GLY A O   1 
ATOM   1941 N N   . LEU A 1 263 ? 28.72900  23.54700  85.83500  1.000 14.32181 ? 263 LEU A N   1 
ATOM   1942 C CA  . LEU A 1 263 ? 27.86400  22.77300  86.71600  1.000 16.60394 ? 263 LEU A CA  1 
ATOM   1943 C C   . LEU A 1 263 ? 28.62600  22.20100  87.90900  1.000 18.67641 ? 263 LEU A C   1 
ATOM   1944 O O   . LEU A 1 263 ? 28.02800  21.96200  88.96300  1.000 20.88158 ? 263 LEU A O   1 
ATOM   1945 C CB  . LEU A 1 263 ? 27.20000  21.64200  85.92900  1.000 14.00662 ? 263 LEU A CB  1 
ATOM   1946 C CG  . LEU A 1 263 ? 26.24400  22.02400  84.79400  1.000 17.46327 ? 263 LEU A CG  1 
ATOM   1947 C CD1 . LEU A 1 263 ? 25.72200  20.77700  84.09800  1.000 16.22856 ? 263 LEU A CD1 1 
ATOM   1948 C CD2 . LEU A 1 263 ? 25.08700  22.86200  85.31000  1.000 11.99380 ? 263 LEU A CD2 1 
ATOM   1949 N N   . GLU A 1 264 ? 29.93600  21.97200  87.76600  1.000 19.18958 ? 264 GLU A N   1 
ATOM   1950 C CA  . GLU A 1 264 ? 30.70200  21.31000  88.81900  1.000 18.50775 ? 264 GLU A CA  1 
ATOM   1951 C C   . GLU A 1 264 ? 30.76100  22.12100  90.10800  1.000 18.29085 ? 264 GLU A C   1 
ATOM   1952 O O   . GLU A 1 264 ? 30.98000  21.54400  91.18100  1.000 20.42476 ? 264 GLU A O   1 
ATOM   1953 C CB  . GLU A 1 264 ? 32.12400  21.01400  88.33200  1.000 18.45238 ? 264 GLU A CB  1 
ATOM   1954 C CG  . GLU A 1 264 ? 32.18000  19.99000  87.21700  1.000 19.47825 ? 264 GLU A CG  1 
ATOM   1955 C CD  . GLU A 1 264 ? 33.59400  19.60100  86.83000  1.000 20.02401 ? 264 GLU A CD  1 
ATOM   1956 O OE1 . GLU A 1 264 ? 34.54900  20.16600  87.40300  1.000 23.79097 ? 264 GLU A OE1 1 
ATOM   1957 O OE2 . GLU A 1 264 ? 33.75000  18.72600  85.94700  1.000 23.27127 ? 264 GLU A OE2 1 
ATOM   1958 N N   . THR A 1 265 ? 30.58200  23.43900  90.02800  1.000 17.06302 ? 265 THR A N   1 
ATOM   1959 C CA  . THR A 1 265 ? 30.62300  24.31500  91.18900  1.000 17.14893 ? 265 THR A CA  1 
ATOM   1960 C C   . THR A 1 265 ? 29.28400  24.98800  91.46500  1.000 17.33770 ? 265 THR A C   1 
ATOM   1961 O O   . THR A 1 265 ? 29.23000  25.91800  92.27600  1.000 18.90368 ? 265 THR A O   1 
ATOM   1962 C CB  . THR A 1 265 ? 31.70000  25.38700  91.01000  1.000 18.31985 ? 265 THR A CB  1 
ATOM   1963 O OG1 . THR A 1 265 ? 31.34800  26.23500  89.90900  1.000 19.73424 ? 265 THR A OG1 1 
ATOM   1964 C CG2 . THR A 1 265 ? 33.05600  24.75700  90.75800  1.000 18.09943 ? 265 THR A CG2 1 
ATOM   1965 N N   . LEU A 1 266 ? 28.20400  24.54500  90.81400  1.000 19.06189 ? 266 LEU A N   1 
ATOM   1966 C CA  . LEU A 1 266 ? 26.92400  25.24200  90.93100  1.000 20.52160 ? 266 LEU A CA  1 
ATOM   1967 C C   . LEU A 1 266 ? 26.44700  25.29000  92.37700  1.000 22.24013 ? 266 LEU A C   1 
ATOM   1968 O O   . LEU A 1 266 ? 26.03800  26.34700  92.87000  1.000 19.02375 ? 266 LEU A O   1 
ATOM   1969 C CB  . LEU A 1 266 ? 25.86900  24.57100  90.05300  1.000 17.71248 ? 266 LEU A CB  1 
ATOM   1970 C CG  . LEU A 1 266 ? 24.46000  25.17500  90.13300  1.000 20.35025 ? 266 LEU A CG  1 
ATOM   1971 C CD1 . LEU A 1 266 ? 24.43100  26.59500  89.58700  1.000 17.51686 ? 266 LEU A CD1 1 
ATOM   1972 C CD2 . LEU A 1 266 ? 23.44700  24.30600  89.40000  1.000 16.65686 ? 266 LEU A CD2 1 
ATOM   1973 N N   . GLY A 1 267 ? 26.51500  24.15600  93.07900  1.000 19.74108 ? 267 GLY A N   1 
ATOM   1974 C CA  . GLY A 1 267 ? 26.00700  24.11700  94.43800  1.000 19.23357 ? 267 GLY A CA  1 
ATOM   1975 C C   . GLY A 1 267 ? 26.70100  25.11100  95.34900  1.000 21.48111 ? 267 GLY A C   1 
ATOM   1976 O O   . GLY A 1 267 ? 26.04900  25.91300  96.02300  1.000 20.46030 ? 267 GLY A O   1 
ATOM   1977 N N   . LEU A 1 268 ? 28.03400  25.10700  95.35100  1.000 17.07073 ? 268 LEU A N   1 
ATOM   1978 C CA  . LEU A 1 268 ? 28.72900  25.98800  96.27700  1.000 21.42397 ? 268 LEU A CA  1 
ATOM   1979 C C   . LEU A 1 268 ? 28.65400  27.44300  95.84100  1.000 23.88326 ? 268 LEU A C   1 
ATOM   1980 O O   . LEU A 1 268 ? 28.76700  28.33700  96.69000  1.000 20.39472 ? 268 LEU A O   1 
ATOM   1981 C CB  . LEU A 1 268 ? 30.18100  25.53800  96.46600  1.000 25.25405 ? 268 LEU A CB  1 
ATOM   1982 C CG  . LEU A 1 268 ? 31.21600  25.57600  95.34400  1.000 25.74890 ? 268 LEU A CG  1 
ATOM   1983 C CD1 . LEU A 1 268 ? 31.86000  26.94100  95.23700  1.000 21.46505 ? 268 LEU A CD1 1 
ATOM   1984 C CD2 . LEU A 1 268 ? 32.27100  24.51000  95.60500  1.000 26.77186 ? 268 LEU A CD2 1 
ATOM   1985 N N   . ARG A 1 269 ? 28.45400  27.70200  94.54400  1.000 19.68420 ? 269 ARG A N   1 
ATOM   1986 C CA  . ARG A 1 269 ? 28.25000  29.07500  94.09700  1.000 18.68722 ? 269 ARG A CA  1 
ATOM   1987 C C   . ARG A 1 269 ? 26.88500  29.59700  94.52900  1.000 20.14315 ? 269 ARG A C   1 
ATOM   1988 O O   . ARG A 1 269 ? 26.76800  30.73900  94.99100  1.000 18.90120 ? 269 ARG A O   1 
ATOM   1989 C CB  . ARG A 1 269 ? 28.41100  29.17100  92.57800  1.000 19.24096 ? 269 ARG A CB  1 
ATOM   1990 C CG  . ARG A 1 269 ? 29.85500  29.04800  92.09900  1.000 18.15288 ? 269 ARG A CG  1 
ATOM   1991 C CD  . ARG A 1 269 ? 30.00000  29.39600  90.62400  1.000 16.33293 ? 269 ARG A CD  1 
ATOM   1992 N NE  . ARG A 1 269 ? 29.51800  28.33300  89.74700  1.000 18.55800 ? 269 ARG A NE  1 
ATOM   1993 C CZ  . ARG A 1 269 ? 28.35700  28.35300  89.10300  1.000 20.07363 ? 269 ARG A CZ  1 
ATOM   1994 N NH1 . ARG A 1 269 ? 27.51000  29.36400  89.23200  1.000 20.49559 ? 269 ARG A NH1 1 
ATOM   1995 N NH2 . ARG A 1 269 ? 28.04100  27.33800  88.30400  1.000 17.49482 ? 269 ARG A NH2 1 
ATOM   1996 N N   . MET A 1 270 ? 25.84100  28.77800  94.39100  1.000 17.38514 ? 270 MET A N   1 
ATOM   1997 C CA  . MET A 1 270 ? 24.50700  29.23100  94.77300  1.000 22.63349 ? 270 MET A CA  1 
ATOM   1998 C C   . MET A 1 270 ? 24.41200  29.48500  96.27500  1.000 20.66683 ? 270 MET A C   1 
ATOM   1999 O O   . MET A 1 270 ? 23.69800  30.40100  96.70000  1.000 21.76111 ? 270 MET A O   1 
ATOM   2000 C CB  . MET A 1 270 ? 23.45100  28.21800  94.32100  1.000 17.78188 ? 270 MET A CB  1 
ATOM   2001 C CG  . MET A 1 270 ? 23.36100  28.04000  92.80400  1.000 19.29786 ? 270 MET A CG  1 
ATOM   2002 S SD  . MET A 1 270 ? 23.15900  29.58500  91.88200  1.000 21.84678 ? 270 MET A SD  1 
ATOM   2003 C CE  . MET A 1 270 ? 21.49700  30.04600  92.36600  1.000 22.52175 ? 270 MET A CE  1 
ATOM   2004 N N   . GLU A 1 271 ? 25.12000  28.69800  97.08700  1.000 20.49144 ? 271 GLU A N   1 
ATOM   2005 C CA  A GLU A 1 271 ? 25.12600  28.93500  98.52800  0.499 23.86403 ? 271 GLU A CA  1 
ATOM   2006 C CA  B GLU A 1 271 ? 25.12200  28.93500  98.52600  0.501 23.87942 ? 271 GLU A CA  1 
ATOM   2007 C C   . GLU A 1 271 ? 25.68400  30.31400  98.85000  1.000 22.51751 ? 271 GLU A C   1 
ATOM   2008 O O   . GLU A 1 271 ? 25.09800  31.06700  99.63700  1.000 26.41294 ? 271 GLU A O   1 
ATOM   2009 C CB  A GLU A 1 271 ? 25.93600  27.84900  99.24200  0.499 23.88480 ? 271 GLU A CB  1 
ATOM   2010 C CB  B GLU A 1 271 ? 25.91700  27.83400  99.23300  0.501 23.88758 ? 271 GLU A CB  1 
ATOM   2011 C CG  A GLU A 1 271 ? 25.13700  26.61100  99.63300  0.499 27.20008 ? 271 GLU A CG  1 
ATOM   2012 C CG  B GLU A 1 271 ? 25.29200  26.45300  99.07800  0.501 26.87519 ? 271 GLU A CG  1 
ATOM   2013 C CD  A GLU A 1 271 ? 24.30600  26.81000  100.89400 0.499 30.20522 ? 271 GLU A CD  1 
ATOM   2014 C CD  B GLU A 1 271 ? 26.17700  25.33000  99.58900  0.501 29.52464 ? 271 GLU A CD  1 
ATOM   2015 O OE1 A GLU A 1 271 ? 24.62400  27.72000  101.69200 0.499 31.81872 ? 271 GLU A OE1 1 
ATOM   2016 O OE1 B GLU A 1 271 ? 27.22800  25.62300  100.20200 0.501 30.05701 ? 271 GLU A OE1 1 
ATOM   2017 O OE2 A GLU A 1 271 ? 23.33300  26.05400  101.08600 0.499 28.01992 ? 271 GLU A OE2 1 
ATOM   2018 O OE2 B GLU A 1 271 ? 25.81600  24.15200  99.37000  0.501 28.95378 ? 271 GLU A OE2 1 
ATOM   2019 N N   . ARG A 1 272 ? 26.81500  30.67100  98.24000  1.000 21.06384 ? 272 ARG A N   1 
ATOM   2020 C CA  . ARG A 1 272 ? 27.37200  31.99800  98.46900  1.000 18.96980 ? 272 ARG A CA  1 
ATOM   2021 C C   . ARG A 1 272 ? 26.49800  33.07400  97.83800  1.000 24.22262 ? 272 ARG A C   1 
ATOM   2022 O O   . ARG A 1 272 ? 26.27100  34.12700  98.44500  1.000 19.30382 ? 272 ARG A O   1 
ATOM   2023 C CB  . ARG A 1 272 ? 28.79700  32.07600  97.93200  1.000 20.02862 ? 272 ARG A CB  1 
ATOM   2024 C CG  . ARG A 1 272 ? 29.45100  33.41500  98.18500  1.000 21.90068 ? 272 ARG A CG  1 
ATOM   2025 C CD  . ARG A 1 272 ? 29.36900  33.76800  99.66000  1.000 29.60417 ? 272 ARG A CD  1 
ATOM   2026 N NE  . ARG A 1 272 ? 30.13000  32.81900  100.46100 1.000 28.82060 ? 272 ARG A NE  1 
ATOM   2027 C CZ  . ARG A 1 272 ? 31.41200  32.96600  100.75700 1.000 33.76965 ? 272 ARG A CZ  1 
ATOM   2028 N NH1 . ARG A 1 272 ? 32.08500  34.04300  100.38400 1.000 30.44284 ? 272 ARG A NH1 1 
ATOM   2029 N NH2 . ARG A 1 272 ? 32.04000  32.00000  101.42200 1.000 35.21309 ? 272 ARG A NH2 1 
ATOM   2030 N N   . HIS A 1 273 ? 25.99700  32.82200  96.62200  1.000 22.31637 ? 273 HIS A N   1 
ATOM   2031 C CA  . HIS A 1 273 ? 25.04400  33.73000  95.98700  1.000 19.07545 ? 273 HIS A CA  1 
ATOM   2032 C C   . HIS A 1 273 ? 23.88000  34.03700  96.91700  1.000 20.56435 ? 273 HIS A C   1 
ATOM   2033 O O   . HIS A 1 273 ? 23.49600  35.19800  97.09700  1.000 17.51683 ? 273 HIS A O   1 
ATOM   2034 C CB  . HIS A 1 273 ? 24.50300  33.11200  94.69200  1.000 20.06012 ? 273 HIS A CB  1 
ATOM   2035 C CG  . HIS A 1 273 ? 25.34800  33.35400  93.47800  1.000 19.11079 ? 273 HIS A CG  1 
ATOM   2036 N ND1 . HIS A 1 273 ? 25.66100  34.61600  93.02200  1.000 18.94339 ? 273 HIS A ND1 1 
ATOM   2037 C CD2 . HIS A 1 273 ? 25.89800  32.48900  92.59200  1.000 20.00811 ? 273 HIS A CD2 1 
ATOM   2038 C CE1 . HIS A 1 273 ? 26.38600  34.51900  91.92200  1.000 18.38738 ? 273 HIS A CE1 1 
ATOM   2039 N NE2 . HIS A 1 273 ? 26.54500  33.23800  91.63900  1.000 16.34180 ? 273 HIS A NE2 1 
ATOM   2040 N N   . CYS A 1 274 ? 23.29500  32.99200  97.50600  1.000 20.75844 ? 274 CYS A N   1 
ATOM   2041 C CA  . CYS A 1 274 ? 22.10300  33.16800  98.32600  1.000 24.22219 ? 274 CYS A CA  1 
ATOM   2042 C C   . CYS A 1 274 ? 22.43300  33.78200  99.68100  1.000 23.62861 ? 274 CYS A C   1 
ATOM   2043 O O   . CYS A 1 274 ? 21.67800  34.62400  100.17900 1.000 25.42078 ? 274 CYS A O   1 
ATOM   2044 C CB  . CYS A 1 274 ? 21.38500  31.82900  98.49000  1.000 20.89760 ? 274 CYS A CB  1 
ATOM   2045 S SG  . CYS A 1 274 ? 20.63100  31.23800  96.95200  1.000 21.30136 ? 274 CYS A SG  1 
ATOM   2046 N N   . ALA A 1 275 ? 23.55700  33.39000  100.28700 1.000 21.77628 ? 275 ALA A N   1 
ATOM   2047 C CA  . ALA A 1 275 ? 23.93400  33.98500  101.56500 1.000 22.62351 ? 275 ALA A CA  1 
ATOM   2048 C C   . ALA A 1 275 ? 24.16100  35.48700  101.42700 1.000 24.23491 ? 275 ALA A C   1 
ATOM   2049 O O   . ALA A 1 275 ? 23.67900  36.27000  102.25400 1.000 21.74182 ? 275 ALA A O   1 
ATOM   2050 C CB  . ALA A 1 275 ? 25.17600  33.29200  102.12500 1.000 20.21099 ? 275 ALA A CB  1 
ATOM   2051 N N   . ASN A 1 276 ? 24.86400  35.90900  100.36800 1.000 21.04539 ? 276 ASN A N   1 
ATOM   2052 C CA  . ASN A 1 276 ? 25.04100  37.33700  100.11200 1.000 19.38635 ? 276 ASN A CA  1 
ATOM   2053 C C   . ASN A 1 276 ? 23.70200  38.02000  99.86200  1.000 23.49353 ? 276 ASN A C   1 
ATOM   2054 O O   . ASN A 1 276 ? 23.48200  39.15900  100.29600 1.000 20.71728 ? 276 ASN A O   1 
ATOM   2055 C CB  . ASN A 1 276 ? 25.96700  37.55700  98.91200  1.000 21.67101 ? 276 ASN A CB  1 
ATOM   2056 C CG  . ASN A 1 276 ? 27.43400  37.37100  99.25000  1.000 22.99988 ? 276 ASN A CG  1 
ATOM   2057 O OD1 . ASN A 1 276 ? 27.80800  37.28800  100.41600 1.000 25.88776 ? 276 ASN A OD1 1 
ATOM   2058 N ND2 . ASN A 1 276 ? 28.27900  37.31600  98.21800  1.000 27.14122 ? 276 ASN A ND2 1 
ATOM   2059 N N   . ALA A 1 277 ? 22.80200  37.34500  99.14200  1.000 20.25218 ? 277 ALA A N   1 
ATOM   2060 C CA  . ALA A 1 277 ? 21.49300  37.92000  98.85900  1.000 20.85212 ? 277 ALA A CA  1 
ATOM   2061 C C   . ALA A 1 277 ? 20.69800  38.14500  100.14100 1.000 26.98279 ? 277 ALA A C   1 
ATOM   2062 O O   . ALA A 1 277 ? 20.02600  39.17300  100.29000 1.000 25.69846 ? 277 ALA A O   1 
ATOM   2063 C CB  . ALA A 1 277 ? 20.72500  37.01400  97.90100  1.000 17.85814 ? 277 ALA A CB  1 
ATOM   2064 N N   . GLN A 1 278 ? 20.76500  37.19100  101.07800 1.000 26.66468 ? 278 GLN A N   1 
ATOM   2065 C CA  . GLN A 1 278 ? 20.01100  37.30400  102.32500 1.000 26.26298 ? 278 GLN A CA  1 
ATOM   2066 C C   . GLN A 1 278 ? 20.46100  38.51200  103.14100 1.000 27.76152 ? 278 GLN A C   1 
ATOM   2067 O O   . GLN A 1 278 ? 19.62800  39.26000  103.66700 1.000 25.66053 ? 278 GLN A O   1 
ATOM   2068 C CB  . GLN A 1 278 ? 20.15700  36.01600  103.14300 1.000 22.77640 ? 278 GLN A CB  1 
ATOM   2069 C CG  . GLN A 1 278 ? 19.23500  35.91300  104.36700 1.000 21.40120 ? 278 GLN A CG  1 
ATOM   2070 C CD  . GLN A 1 278 ? 17.79300  35.60100  103.99900 1.000 24.66034 ? 278 GLN A CD  1 
ATOM   2071 O OE1 . GLN A 1 278 ? 17.50800  34.62000  103.30700 1.000 29.95986 ? 278 GLN A OE1 1 
ATOM   2072 N NE2 . GLN A 1 278 ? 16.87600  36.44100  104.45700 1.000 25.19211 ? 278 GLN A NE2 1 
ATOM   2073 N N   . LYS A 1 279 ? 21.77600  38.72200  103.25800 1.000 24.12581 ? 279 LYS A N   1 
ATOM   2074 C CA  . LYS A 1 279 ? 22.26900  39.88200  103.99600 1.000 26.71413 ? 279 LYS A CA  1 
ATOM   2075 C C   . LYS A 1 279 ? 21.83500  41.18100  103.32900 1.000 25.31509 ? 279 LYS A C   1 
ATOM   2076 O O   . LYS A 1 279 ? 21.32700  42.09200  103.98900 1.000 29.79956 ? 279 LYS A O   1 
ATOM   2077 C CB  . LYS A 1 279 ? 23.79200  39.83200  104.11100 1.000 25.10872 ? 279 LYS A CB  1 
ATOM   2078 C CG  . LYS A 1 279 ? 24.32000  38.72000  104.98800 1.000 31.79391 ? 279 LYS A CG  1 
ATOM   2079 C CD  . LYS A 1 279 ? 25.82600  38.84000  105.16700 1.000 35.10041 ? 279 LYS A CD  1 
ATOM   2080 C CE  . LYS A 1 279 ? 26.40500  37.56300  105.76000 1.000 47.31354 ? 279 LYS A CE  1 
ATOM   2081 N NZ  . LYS A 1 279 ? 27.87300  37.66700  105.98800 1.000 63.31769 ? 279 LYS A NZ  1 
ATOM   2082 N N   . ILE A 1 280 ? 22.02100  41.27600  102.01300 1.000 23.15049 ? 280 ILE A N   1 
ATOM   2083 C CA  . ILE A 1 280 ? 21.73200  42.51700  101.30500 1.000 24.72889 ? 280 ILE A CA  1 
ATOM   2084 C C   . ILE A 1 280 ? 20.24200  42.84000  101.34800 1.000 23.45440 ? 280 ILE A C   1 
ATOM   2085 O O   . ILE A 1 280 ? 19.85400  44.00000  101.52600 1.000 22.78371 ? 280 ILE A O   1 
ATOM   2086 C CB  . ILE A 1 280 ? 22.26200  42.42900  99.86300  1.000 24.37800 ? 280 ILE A CB  1 
ATOM   2087 C CG1 . ILE A 1 280 ? 23.78600  42.53900  99.86100  1.000 25.03141 ? 280 ILE A CG1 1 
ATOM   2088 C CG2 . ILE A 1 280 ? 21.65700  43.50400  98.98900  1.000 16.99630 ? 280 ILE A CG2 1 
ATOM   2089 C CD1 . ILE A 1 280 ? 24.38900  42.32900  98.49400  1.000 33.01442 ? 280 ILE A CD1 1 
ATOM   2090 N N   . ALA A 1 281 ? 19.38400  41.83200  101.17900 1.000 20.00735 ? 281 ALA A N   1 
ATOM   2091 C CA  . ALA A 1 281 ? 17.94500  42.08200  101.21100 1.000 25.73564 ? 281 ALA A CA  1 
ATOM   2092 C C   . ALA A 1 281 ? 17.51400  42.66200  102.55600 1.000 27.57885 ? 281 ALA A C   1 
ATOM   2093 O O   . ALA A 1 281 ? 16.80200  43.67100  102.60900 1.000 26.27728 ? 281 ALA A O   1 
ATOM   2094 C CB  . ALA A 1 281 ? 17.17700  40.79300  100.91000 1.000 20.63455 ? 281 ALA A CB  1 
ATOM   2095 N N   . GLU A 1 282 ? 17.94800  42.04000  103.65600 1.000 21.92487 ? 282 GLU A N   1 
ATOM   2096 C CA  . GLU A 1 282 ? 17.56600  42.51800  104.98100 1.000 27.24914 ? 282 GLU A CA  1 
ATOM   2097 C C   . GLU A 1 282 ? 18.12600  43.91000  105.24700 1.000 30.68223 ? 282 GLU A C   1 
ATOM   2098 O O   . GLU A 1 282 ? 17.40800  44.79900  105.72000 1.000 28.26325 ? 282 GLU A O   1 
ATOM   2099 C CB  . GLU A 1 282 ? 18.04000  41.53100  106.04800 1.000 24.65448 ? 282 GLU A CB  1 
ATOM   2100 C CG  . GLU A 1 282 ? 17.39200  40.15900  105.94300 1.000 27.05975 ? 282 GLU A CG  1 
ATOM   2101 C CD  . GLU A 1 282 ? 17.95200  39.16100  106.93600 1.000 26.91463 ? 282 GLU A CD  1 
ATOM   2102 O OE1 . GLU A 1 282 ? 18.97700  39.46400  107.58300 1.000 31.91679 ? 282 GLU A OE1 1 
ATOM   2103 O OE2 . GLU A 1 282 ? 17.36500  38.06900  107.07000 1.000 31.78707 ? 282 GLU A OE2 1 
ATOM   2104 N N   . TRP A 1 283 ? 19.40500  44.12300  104.92600 1.000 27.51363 ? 283 TRP A N   1 
ATOM   2105 C CA  . TRP A 1 283 ? 20.00800  45.44000  105.11500 1.000 27.34743 ? 283 TRP A CA  1 
ATOM   2106 C C   . TRP A 1 283 ? 19.29800  46.49500  104.27500 1.000 32.54342 ? 283 TRP A C   1 
ATOM   2107 O O   . TRP A 1 283 ? 19.12200  47.63900  104.71500 1.000 32.45849 ? 283 TRP A O   1 
ATOM   2108 C CB  . TRP A 1 283 ? 21.49700  45.38500  104.77200 1.000 25.23476 ? 283 TRP A CB  1 
ATOM   2109 C CG  . TRP A 1 283 ? 22.16500  46.72700  104.73400 1.000 30.80530 ? 283 TRP A CG  1 
ATOM   2110 C CD1 . TRP A 1 283 ? 22.67600  47.41700  105.79200 1.000 29.55170 ? 283 TRP A CD1 1 
ATOM   2111 C CD2 . TRP A 1 283 ? 22.40300  47.53700  103.57300 1.000 31.14227 ? 283 TRP A CD2 1 
ATOM   2112 N NE1 . TRP A 1 283 ? 23.21500  48.60600  105.36500 1.000 34.56244 ? 283 TRP A NE1 1 
ATOM   2113 C CE2 . TRP A 1 283 ? 23.06000  48.70500  104.00800 1.000 28.98959 ? 283 TRP A CE2 1 
ATOM   2114 C CE3 . TRP A 1 283 ? 22.12300  47.38600  102.21000 1.000 28.81900 ? 283 TRP A CE3 1 
ATOM   2115 C CZ2 . TRP A 1 283 ? 23.44400  49.71900  103.13000 1.000 32.96886 ? 283 TRP A CZ2 1 
ATOM   2116 C CZ3 . TRP A 1 283 ? 22.50500  48.39300  101.33600 1.000 27.83437 ? 283 TRP A CZ3 1 
ATOM   2117 C CH2 . TRP A 1 283 ? 23.15900  49.54500  101.80100 1.000 32.38648 ? 283 TRP A CH2 1 
ATOM   2118 N N   . LEU A 1 284 ? 18.88400  46.12700  103.05900 1.000 29.30111 ? 284 LEU A N   1 
ATOM   2119 C CA  . LEU A 1 284 ? 18.12200  47.04800  102.22200 1.000 28.32405 ? 284 LEU A CA  1 
ATOM   2120 C C   . LEU A 1 284 ? 16.78800  47.40700  102.85900 1.000 28.89896 ? 284 LEU A C   1 
ATOM   2121 O O   . LEU A 1 284 ? 16.33200  48.55200  102.75400 1.000 33.88339 ? 284 LEU A O   1 
ATOM   2122 C CB  . LEU A 1 284 ? 17.89200  46.43700  100.84400 1.000 24.42020 ? 284 LEU A CB  1 
ATOM   2123 C CG  . LEU A 1 284 ? 18.99700  46.69300  99.83000  1.000 30.69106 ? 284 LEU A CG  1 
ATOM   2124 C CD1 . LEU A 1 284 ? 18.74600  45.86800  98.57200  1.000 25.73624 ? 284 LEU A CD1 1 
ATOM   2125 C CD2 . LEU A 1 284 ? 19.04800  48.18300  99.52000  1.000 27.57142 ? 284 LEU A CD2 1 
ATOM   2126 N N   . GLU A 1 285 ? 16.13300  46.43600  103.49900 1.000 28.27751 ? 285 GLU A N   1 
ATOM   2127 C CA  . GLU A 1 285 ? 14.78500  46.67000  104.00400 1.000 35.64994 ? 285 GLU A CA  1 
ATOM   2128 C C   . GLU A 1 285 ? 14.77100  47.69400  105.13100 1.000 29.04718 ? 285 GLU A C   1 
ATOM   2129 O O   . GLU A 1 285 ? 13.78000  48.41100  105.29900 1.000 35.49113 ? 285 GLU A O   1 
ATOM   2130 C CB  . GLU A 1 285 ? 14.15800  45.35600  104.46900 1.000 33.85134 ? 285 GLU A CB  1 
ATOM   2131 C CG  . GLU A 1 285 ? 12.64000  45.40200  104.49600 1.000 32.97166 ? 285 GLU A CG  1 
ATOM   2132 C CD  . GLU A 1 285 ? 12.00600  44.03100  104.60900 1.000 35.91195 ? 285 GLU A CD  1 
ATOM   2133 O OE1 . GLU A 1 285 ? 12.46200  43.22500  105.45000 1.000 35.04460 ? 285 GLU A OE1 1 
ATOM   2134 O OE2 . GLU A 1 285 ? 11.04800  43.76400  103.85000 1.000 33.51421 ? 285 GLU A OE2 1 
ATOM   2135 N N   . ALA A 1 286 ? 15.85500  47.79000  105.89300 1.000 29.40936 ? 286 ALA A N   1 
ATOM   2136 C CA  . ALA A 1 286 ? 15.95000  48.72400  107.00500 1.000 34.27589 ? 286 ALA A CA  1 
ATOM   2137 C C   . ALA A 1 286 ? 16.44400  50.10500  106.58700 1.000 37.26547 ? 286 ALA A C   1 
ATOM   2138 O O   . ALA A 1 286 ? 16.62000  50.97100  107.45100 1.000 35.29692 ? 286 ALA A O   1 
ATOM   2139 C CB  . ALA A 1 286 ? 16.86800  48.15200  108.09200 1.000 29.73740 ? 286 ALA A CB  1 
ATOM   2140 N N   . ARG A 1 287 ? 16.69100  50.32600  105.29300 1.000 30.82532 ? 287 ARG A N   1 
ATOM   2141 C CA  . ARG A 1 287 ? 17.13400  51.63700  104.83800 1.000 35.76678 ? 287 ARG A CA  1 
ATOM   2142 C C   . ARG A 1 287 ? 15.94300  52.58700  104.71000 1.000 36.48289 ? 287 ARG A C   1 
ATOM   2143 O O   . ARG A 1 287 ? 14.89000  52.19900  104.19400 1.000 35.61305 ? 287 ARG A O   1 
ATOM   2144 C CB  . ARG A 1 287 ? 17.85800  51.52600  103.49600 1.000 34.42108 ? 287 ARG A CB  1 
ATOM   2145 C CG  . ARG A 1 287 ? 19.18100  50.78500  103.56700 1.000 31.86253 ? 287 ARG A CG  1 
ATOM   2146 C CD  . ARG A 1 287 ? 20.21900  51.57500  104.34900 1.000 35.86996 ? 287 ARG A CD  1 
ATOM   2147 N NE  . ARG A 1 287 ? 20.41600  52.90600  103.78400 1.000 39.96373 ? 287 ARG A NE  1 
ATOM   2148 C CZ  . ARG A 1 287 ? 21.49700  53.65200  103.97100 1.000 36.09101 ? 287 ARG A CZ  1 
ATOM   2149 N NH1 . ARG A 1 287 ? 22.52100  53.21800  104.68800 1.000 34.83273 ? 287 ARG A NH1 1 
ATOM   2150 N NH2 . ARG A 1 287 ? 21.55400  54.86000  103.42000 1.000 33.54828 ? 287 ARG A NH2 1 
ATOM   2151 N N   . PRO A 1 288 ? 16.08400  53.83100  105.17700 1.000 37.70698 ? 288 PRO A N   1 
ATOM   2152 C CA  . PRO A 1 288 ? 14.97700  54.79500  105.04300 1.000 33.42170 ? 288 PRO A CA  1 
ATOM   2153 C C   . PRO A 1 288 ? 14.59400  55.09100  103.60200 1.000 34.42324 ? 288 PRO A C   1 
ATOM   2154 O O   . PRO A 1 288 ? 13.42800  55.41200  103.33200 1.000 29.44890 ? 288 PRO A O   1 
ATOM   2155 C CB  . PRO A 1 288 ? 15.51600  56.05000  105.74900 1.000 33.45414 ? 288 PRO A CB  1 
ATOM   2156 C CG  . PRO A 1 288 ? 16.63200  55.56200  106.62500 1.000 38.77071 ? 288 PRO A CG  1 
ATOM   2157 C CD  . PRO A 1 288 ? 17.23500  54.39600  105.90200 1.000 35.81321 ? 288 PRO A CD  1 
ATOM   2158 N N   . GLU A 1 289 ? 15.54000  55.00000  102.66500 1.000 31.80222 ? 289 GLU A N   1 
ATOM   2159 C CA  . GLU A 1 289 ? 15.28100  55.35700  101.27700 1.000 29.74049 ? 289 GLU A CA  1 
ATOM   2160 C C   . GLU A 1 289 ? 14.54200  54.27100  100.50700 1.000 33.22041 ? 289 GLU A C   1 
ATOM   2161 O O   . GLU A 1 289 ? 14.16200  54.51000  99.35500  1.000 27.84863 ? 289 GLU A O   1 
ATOM   2162 C CB  . GLU A 1 289 ? 16.59600  55.67300  100.55800 1.000 32.56966 ? 289 GLU A CB  1 
ATOM   2163 C CG  . GLU A 1 289 ? 17.50800  56.65700  101.28000 1.000 28.76314 ? 289 GLU A CG  1 
ATOM   2164 C CD  . GLU A 1 289 ? 18.45500  55.97900  102.25300 1.000 31.87051 ? 289 GLU A CD  1 
ATOM   2165 O OE1 . GLU A 1 289 ? 18.10000  54.91700  102.80700 1.000 30.93199 ? 289 GLU A OE1 1 
ATOM   2166 O OE2 . GLU A 1 289 ? 19.56400  56.51000  102.46300 1.000 38.21758 ? 289 GLU A OE2 1 
ATOM   2167 N N   . VAL A 1 290 ? 14.32900  53.09900  101.10700 1.000 28.64821 ? 290 VAL A N   1 
ATOM   2168 C CA  . VAL A 1 290 ? 13.76700  51.93800  100.42400 1.000 32.56445 ? 290 VAL A CA  1 
ATOM   2169 C C   . VAL A 1 290 ? 12.35100  51.69800  100.94000 1.000 32.04543 ? 290 VAL A C   1 
ATOM   2170 O O   . VAL A 1 290 ? 12.14600  51.46100  102.13700 1.000 30.15164 ? 290 VAL A O   1 
ATOM   2171 C CB  . VAL A 1 290 ? 14.64300  50.69000  100.62400 1.000 30.75942 ? 290 VAL A CB  1 
ATOM   2172 C CG1 . VAL A 1 290 ? 14.02600  49.49300  99.92300  1.000 32.40539 ? 290 VAL A CG1 1 
ATOM   2173 C CG2 . VAL A 1 290 ? 16.05900  50.94300  100.11900 1.000 29.37823 ? 290 VAL A CG2 1 
ATOM   2174 N N   . ALA A 1 291 ? 11.37600  51.74400  100.03000 1.000 33.40754 ? 291 ALA A N   1 
ATOM   2175 C CA  . ALA A 1 291 ? 9.98500   51.51000  100.40800 1.000 36.86705 ? 291 ALA A CA  1 
ATOM   2176 C C   . ALA A 1 291 ? 9.68700   50.02900  100.61000 1.000 36.79486 ? 291 ALA A C   1 
ATOM   2177 O O   . ALA A 1 291 ? 8.89300   49.67000  101.48900 1.000 42.15486 ? 291 ALA A O   1 
ATOM   2178 C CB  . ALA A 1 291 ? 9.04600   52.09200  99.35200  1.000 34.48568 ? 291 ALA A CB  1 
ATOM   2179 N N   . ARG A 1 292 ? 10.29300  49.16000  99.80100  1.000 34.61236 ? 292 ARG A N   1 
ATOM   2180 C CA  . ARG A 1 292 ? 9.99700   47.73400  99.84700  1.000 30.76800 ? 292 ARG A CA  1 
ATOM   2181 C C   . ARG A 1 292 ? 11.13000  46.95800  99.18400  1.000 32.77716 ? 292 ARG A C   1 
ATOM   2182 O O   . ARG A 1 292 ? 11.79200  47.45600  98.27000  1.000 30.62397 ? 292 ARG A O   1 
ATOM   2183 C CB  . ARG A 1 292 ? 8.66300   47.41900  99.15600  1.000 26.57044 ? 292 ARG A CB  1 
ATOM   2184 C CG  . ARG A 1 292 ? 8.18800   45.99700  99.36300  1.000 30.32352 ? 292 ARG A CG  1 
ATOM   2185 C CD  . ARG A 1 292 ? 6.91500   45.70100  98.60100  1.000 33.20182 ? 292 ARG A CD  1 
ATOM   2186 N NE  . ARG A 1 292 ? 6.61400   44.27400  98.61100  1.000 36.69611 ? 292 ARG A NE  1 
ATOM   2187 C CZ  . ARG A 1 292 ? 5.54400   43.72500  98.05000  1.000 40.78264 ? 292 ARG A CZ  1 
ATOM   2188 N NH1 . ARG A 1 292 ? 4.62500   44.46300  97.44600  1.000 33.16285 ? 292 ARG A NH1 1 
ATOM   2189 N NH2 . ARG A 1 292 ? 5.39800   42.40200  98.09000  1.000 34.73180 ? 292 ARG A NH2 1 
ATOM   2190 N N   . VAL A 1 293 ? 11.33600  45.73000  99.65200  1.000 30.64194 ? 293 VAL A N   1 
ATOM   2191 C CA  . VAL A 1 293 ? 12.29700  44.80400  99.06900  1.000 29.85981 ? 293 VAL A CA  1 
ATOM   2192 C C   . VAL A 1 293 ? 11.55800  43.53100  98.68300  1.000 31.81968 ? 293 VAL A C   1 
ATOM   2193 O O   . VAL A 1 293 ? 10.73800  43.02100  99.45700  1.000 30.37333 ? 293 VAL A O   1 
ATOM   2194 C CB  . VAL A 1 293 ? 13.45600  44.49400  100.03800 1.000 25.64126 ? 293 VAL A CB  1 
ATOM   2195 C CG1 . VAL A 1 293 ? 14.43300  43.51700  99.40100  1.000 24.87189 ? 293 VAL A CG1 1 
ATOM   2196 C CG2 . VAL A 1 293 ? 14.16400  45.77400  100.44200 1.000 26.60656 ? 293 VAL A CG2 1 
ATOM   2197 N N   . TYR A 1 294 ? 11.83900  43.02900  97.48100  1.000 29.03788 ? 294 TYR A N   1 
ATOM   2198 C CA  . TYR A 1 294 ? 11.24300  41.79800  96.96300  1.000 27.59852 ? 294 TYR A CA  1 
ATOM   2199 C C   . TYR A 1 294 ? 12.30300  40.69700  96.97800  1.000 26.80127 ? 294 TYR A C   1 
ATOM   2200 O O   . TYR A 1 294 ? 13.16600  40.64500  96.09700  1.000 22.98639 ? 294 TYR A O   1 
ATOM   2201 C CB  . TYR A 1 294 ? 10.70000  42.00600  95.55200  1.000 27.43531 ? 294 TYR A CB  1 
ATOM   2202 C CG  . TYR A 1 294 ? 9.75300   43.17800  95.41000  1.000 33.37249 ? 294 TYR A CG  1 
ATOM   2203 C CD1 . TYR A 1 294 ? 10.23700  44.46800  95.20300  1.000 32.73570 ? 294 TYR A CD1 1 
ATOM   2204 C CD2 . TYR A 1 294 ? 8.37500   42.99600  95.47000  1.000 29.46437 ? 294 TYR A CD2 1 
ATOM   2205 C CE1 . TYR A 1 294 ? 9.37800   45.54200  95.06700  1.000 32.47835 ? 294 TYR A CE1 1 
ATOM   2206 C CE2 . TYR A 1 294 ? 7.50700   44.06400  95.33200  1.000 30.54733 ? 294 TYR A CE2 1 
ATOM   2207 C CZ  . TYR A 1 294 ? 8.01500   45.33600  95.13200  1.000 33.97156 ? 294 TYR A CZ  1 
ATOM   2208 O OH  . TYR A 1 294 ? 7.15800   46.40600  94.99500  1.000 37.48427 ? 294 TYR A OH  1 
ATOM   2209 N N   . TYR A 1 295 ? 12.22300  39.80800  97.96600  1.000 25.46503 ? 295 TYR A N   1 
ATOM   2210 C CA  . TYR A 1 295 ? 13.14700  38.68400  98.05400  1.000 22.68675 ? 295 TYR A CA  1 
ATOM   2211 C C   . TYR A 1 295 ? 12.50800  37.52500  98.81700  1.000 25.70961 ? 295 TYR A C   1 
ATOM   2212 O O   . TYR A 1 295 ? 12.02700  37.71300  99.94300  1.000 26.90874 ? 295 TYR A O   1 
ATOM   2213 C CB  . TYR A 1 295 ? 14.45200  39.12500  98.71900  1.000 23.60478 ? 295 TYR A CB  1 
ATOM   2214 C CG  . TYR A 1 295 ? 15.45200  38.01000  98.87700  1.000 25.77809 ? 295 TYR A CG  1 
ATOM   2215 C CD1 . TYR A 1 295 ? 16.04800  37.42500  97.76700  1.000 22.24886 ? 295 TYR A CD1 1 
ATOM   2216 C CD2 . TYR A 1 295 ? 15.79900  37.54200  100.13500 1.000 24.29041 ? 295 TYR A CD2 1 
ATOM   2217 C CE1 . TYR A 1 295 ? 16.96000  36.40100  97.90800  1.000 22.52536 ? 295 TYR A CE1 1 
ATOM   2218 C CE2 . TYR A 1 295 ? 16.71000  36.52800  100.29000 1.000 25.57576 ? 295 TYR A CE2 1 
ATOM   2219 C CZ  . TYR A 1 295 ? 17.28800  35.95500  99.17300  1.000 28.95799 ? 295 TYR A CZ  1 
ATOM   2220 O OH  . TYR A 1 295 ? 18.19900  34.93400  99.32800  1.000 29.61307 ? 295 TYR A OH  1 
ATOM   2221 N N   . PRO A 1 296 ? 12.50200  36.31200  98.25000  1.000 28.55724 ? 296 PRO A N   1 
ATOM   2222 C CA  . PRO A 1 296 ? 11.76500  35.19600  98.87800  1.000 27.74724 ? 296 PRO A CA  1 
ATOM   2223 C C   . PRO A 1 296 ? 12.25700  34.81000  100.26500 1.000 25.74906 ? 296 PRO A C   1 
ATOM   2224 O O   . PRO A 1 296 ? 11.55700  34.06000  100.95700 1.000 26.06696 ? 296 PRO A O   1 
ATOM   2225 C CB  . PRO A 1 296 ? 11.96200  34.04000  97.88400  1.000 27.44289 ? 296 PRO A CB  1 
ATOM   2226 C CG  . PRO A 1 296 ? 12.23900  34.71800  96.57500  1.000 24.85639 ? 296 PRO A CG  1 
ATOM   2227 C CD  . PRO A 1 296 ? 13.04100  35.93800  96.93100  1.000 23.48862 ? 296 PRO A CD  1 
ATOM   2228 N N   . GLY A 1 297 ? 13.43400  35.26100  100.68100 1.000 25.93737 ? 297 GLY A N   1 
ATOM   2229 C CA  . GLY A 1 297 ? 13.93200  34.97200  102.00800 1.000 24.12287 ? 297 GLY A CA  1 
ATOM   2230 C C   . GLY A 1 297 ? 13.54300  35.96700  103.07700 1.000 29.33220 ? 297 GLY A C   1 
ATOM   2231 O O   . GLY A 1 297 ? 14.01200  35.85000  104.21400 1.000 27.80929 ? 297 GLY A O   1 
ATOM   2232 N N   . LEU A 1 298 ? 12.70900  36.95400  102.75200 1.000 25.41041 ? 298 LEU A N   1 
ATOM   2233 C CA  . LEU A 1 298 ? 12.21700  37.91900  103.72900 1.000 31.43280 ? 298 LEU A CA  1 
ATOM   2234 C C   . LEU A 1 298 ? 10.86100  37.48100  104.26300 1.000 31.54639 ? 298 LEU A C   1 
ATOM   2235 O O   . LEU A 1 298 ? 10.03600  36.93200  103.52300 1.000 26.09359 ? 298 LEU A O   1 
ATOM   2236 C CB  . LEU A 1 298 ? 12.09300  39.31700  103.12000 1.000 27.10762 ? 298 LEU A CB  1 
ATOM   2237 C CG  . LEU A 1 298 ? 13.37900  40.02600  102.69600 1.000 28.88404 ? 298 LEU A CG  1 
ATOM   2238 C CD1 . LEU A 1 298 ? 13.05400  41.32700  101.97900 1.000 27.18605 ? 298 LEU A CD1 1 
ATOM   2239 C CD2 . LEU A 1 298 ? 14.27500  40.27900  103.89900 1.000 26.79731 ? 298 LEU A CD2 1 
ATOM   2240 N N   . ASP A 1 299 ? 10.63700  37.72500  105.55900 1.000 34.43839 ? 299 ASP A N   1 
ATOM   2241 C CA  . ASP A 1 299 ? 9.31200   37.49800  106.13000 1.000 32.63953 ? 299 ASP A CA  1 
ATOM   2242 C C   . ASP A 1 299 ? 8.26700   38.36200  105.44300 1.000 26.05955 ? 299 ASP A C   1 
ATOM   2243 O O   . ASP A 1 299 ? 7.10800   37.95600  105.31800 1.000 31.37025 ? 299 ASP A O   1 
ATOM   2244 C CB  . ASP A 1 299 ? 9.31800   37.78000  107.63500 1.000 34.11874 ? 299 ASP A CB  1 
ATOM   2245 C CG  . ASP A 1 299 ? 10.23200  36.85000  108.40100 1.000 35.00200 ? 299 ASP A CG  1 
ATOM   2246 O OD1 . ASP A 1 299 ? 10.54000  35.75400  107.88700 1.000 40.30866 ? 299 ASP A OD1 1 
ATOM   2247 O OD2 . ASP A 1 299 ? 10.63600  37.21400  109.52300 1.000 39.39200 ? 299 ASP A OD2 1 
ATOM   2248 N N   . SER A 1 300 ? 8.66600   39.54200  104.96800 1.000 26.83991 ? 300 SER A N   1 
ATOM   2249 C CA  . SER A 1 300 ? 7.76800   40.44900  104.26600 1.000 32.27202 ? 300 SER A CA  1 
ATOM   2250 C C   . SER A 1 300 ? 7.34000   39.93200  102.89600 1.000 26.98723 ? 300 SER A C   1 
ATOM   2251 O O   . SER A 1 300 ? 6.47300   40.54700  102.26600 1.000 28.53940 ? 300 SER A O   1 
ATOM   2252 C CB  . SER A 1 300 ? 8.44100   41.81200  104.11100 1.000 32.35838 ? 300 SER A CB  1 
ATOM   2253 O OG  . SER A 1 300 ? 9.67800   41.67100  103.43300 1.000 30.37809 ? 300 SER A OG  1 
ATOM   2254 N N   . HIS A 1 301 ? 7.93200   38.85300  102.40500 1.000 27.88884 ? 301 HIS A N   1 
ATOM   2255 C CA  . HIS A 1 301 ? 7.53100   38.30900  101.11200 1.000 29.63792 ? 301 HIS A CA  1 
ATOM   2256 C C   . HIS A 1 301 ? 6.21100   37.56200  101.25700 1.000 27.55763 ? 301 HIS A C   1 
ATOM   2257 O O   . HIS A 1 301 ? 6.12900   36.62300  102.05800 1.000 25.67480 ? 301 HIS A O   1 
ATOM   2258 C CB  . HIS A 1 301 ? 8.60500   37.38100  100.56000 1.000 27.05835 ? 301 HIS A CB  1 
ATOM   2259 C CG  . HIS A 1 301 ? 8.40800   37.02300  99.12000  1.000 28.58394 ? 301 HIS A CG  1 
ATOM   2260 N ND1 . HIS A 1 301 ? 7.38500   36.20600  98.68800  1.000 26.25759 ? 301 HIS A ND1 1 
ATOM   2261 C CD2 . HIS A 1 301 ? 9.10300   37.37400  98.01300  1.000 23.57277 ? 301 HIS A CD2 1 
ATOM   2262 C CE1 . HIS A 1 301 ? 7.45900   36.06800  97.37700  1.000 29.33901 ? 301 HIS A CE1 1 
ATOM   2263 N NE2 . HIS A 1 301 ? 8.49200   36.76700  96.94300  1.000 27.94225 ? 301 HIS A NE2 1 
ATOM   2264 N N   . PRO A 1 302 ? 5.17400   37.92200  100.49600 1.000 29.25071 ? 302 PRO A N   1 
ATOM   2265 C CA  . PRO A 1 302 ? 3.84300   37.33300  100.73100 1.000 29.41110 ? 302 PRO A CA  1 
ATOM   2266 C C   . PRO A 1 302 ? 3.77500   35.83600  100.49700 1.000 29.87161 ? 302 PRO A C   1 
ATOM   2267 O O   . PRO A 1 302 ? 2.82300   35.19900  100.96400 1.000 31.52010 ? 302 PRO A O   1 
ATOM   2268 C CB  . PRO A 1 302 ? 2.94300   38.09300  99.74600  1.000 30.86031 ? 302 PRO A CB  1 
ATOM   2269 C CG  . PRO A 1 302 ? 3.87700   38.59700  98.68400  1.000 29.69481 ? 302 PRO A CG  1 
ATOM   2270 C CD  . PRO A 1 302 ? 5.17100   38.89200  99.38600  1.000 30.14451 ? 302 PRO A CD  1 
ATOM   2271 N N   . GLN A 1 303 ? 4.73200   35.25300  99.77900  1.000 26.86580 ? 303 GLN A N   1 
ATOM   2272 C CA  . GLN A 1 303 ? 4.73800   33.82000  99.51200  1.000 28.32557 ? 303 GLN A CA  1 
ATOM   2273 C C   . GLN A 1 303 ? 6.00500   33.15400  100.02800 1.000 24.98902 ? 303 GLN A C   1 
ATOM   2274 O O   . GLN A 1 303 ? 6.50200   32.20300  99.42700  1.000 27.44191 ? 303 GLN A O   1 
ATOM   2275 C CB  . GLN A 1 303 ? 4.57900   33.54900  98.02300  1.000 29.38449 ? 303 GLN A CB  1 
ATOM   2276 C CG  . GLN A 1 303 ? 3.53100   34.38700  97.36500  1.000 27.08150 ? 303 GLN A CG  1 
ATOM   2277 C CD  . GLN A 1 303 ? 3.51700   34.15200  95.89700  1.000 30.73681 ? 303 GLN A CD  1 
ATOM   2278 O OE1 . GLN A 1 303 ? 4.06900   34.93900  95.12600  1.000 32.03229 ? 303 GLN A OE1 1 
ATOM   2279 N NE2 . GLN A 1 303 ? 2.91200   33.04500  95.48800  1.000 27.83596 ? 303 GLN A NE2 1 
ATOM   2280 N N   . GLN A 1 304 ? 6.53400   33.64800  101.14400 1.000 27.81241 ? 304 GLN A N   1 
ATOM   2281 C CA  . GLN A 1 304 ? 7.74500   33.06700  101.70900 1.000 29.01354 ? 304 GLN A CA  1 
ATOM   2282 C C   . GLN A 1 304 ? 7.59700   31.56300  101.92300 1.000 24.53190 ? 304 GLN A C   1 
ATOM   2283 O O   . GLN A 1 304 ? 8.54000   30.79800  101.69800 1.000 25.23803 ? 304 GLN A O   1 
ATOM   2284 C CB  . GLN A 1 304 ? 8.07400   33.77600  103.02100 1.000 28.67635 ? 304 GLN A CB  1 
ATOM   2285 C CG  . GLN A 1 304 ? 9.37300   33.35500  103.66200 1.000 30.41129 ? 304 GLN A CG  1 
ATOM   2286 C CD  . GLN A 1 304 ? 9.56000   33.99500  105.02200 1.000 37.14664 ? 304 GLN A CD  1 
ATOM   2287 O OE1 . GLN A 1 304 ? 8.58500   34.30100  105.71500 1.000 33.85902 ? 304 GLN A OE1 1 
ATOM   2288 N NE2 . GLN A 1 304 ? 10.81400  34.21500  105.40800 1.000 34.60377 ? 304 GLN A NE2 1 
ATOM   2289 N N   . ALA A 1 305 ? 6.41100   31.11800  102.34200 1.000 24.49176 ? 305 ALA A N   1 
ATOM   2290 C CA  . ALA A 1 305 ? 6.23500   29.71500  102.70900 1.000 26.71190 ? 305 ALA A CA  1 
ATOM   2291 C C   . ALA A 1 305 ? 6.20700   28.80400  101.48500 1.000 25.34324 ? 305 ALA A C   1 
ATOM   2292 O O   . ALA A 1 305 ? 6.80800   27.72200  101.49900 1.000 25.36427 ? 305 ALA A O   1 
ATOM   2293 C CB  . ALA A 1 305 ? 4.96000   29.55100  103.53200 1.000 26.20174 ? 305 ALA A CB  1 
ATOM   2294 N N   . LEU A 1 306 ? 5.50400   29.20900  100.42100 1.000 26.95120 ? 306 LEU A N   1 
ATOM   2295 C CA  . LEU A 1 306 ? 5.52100   28.41100  99.19800  1.000 29.02065 ? 306 LEU A CA  1 
ATOM   2296 C C   . LEU A 1 306 ? 6.93000   28.33300  98.61900  1.000 29.22046 ? 306 LEU A C   1 
ATOM   2297 O O   . LEU A 1 306 ? 7.34500   27.28300  98.11500  1.000 26.61710 ? 306 LEU A O   1 
ATOM   2298 C CB  . LEU A 1 306 ? 4.54500   28.98300  98.16800  1.000 28.01148 ? 306 LEU A CB  1 
ATOM   2299 C CG  . LEU A 1 306 ? 4.43600   28.21800  96.84000  1.000 30.03037 ? 306 LEU A CG  1 
ATOM   2300 C CD1 . LEU A 1 306 ? 4.08800   26.75600  97.07200  1.000 30.57531 ? 306 LEU A CD1 1 
ATOM   2301 C CD2 . LEU A 1 306 ? 3.41700   28.86400  95.90400  1.000 25.63582 ? 306 LEU A CD2 1 
ATOM   2302 N N   . ALA A 1 307 ? 7.68100   29.43600  98.69400  1.000 26.06563 ? 307 ALA A N   1 
ATOM   2303 C CA  . ALA A 1 307 ? 9.05200   29.43700  98.19500  1.000 27.57827 ? 307 ALA A CA  1 
ATOM   2304 C C   . ALA A 1 307 ? 9.92900   28.45500  98.96400  1.000 27.94160 ? 307 ALA A C   1 
ATOM   2305 O O   . ALA A 1 307 ? 10.71800  27.71900  98.36200  1.000 27.88417 ? 307 ALA A O   1 
ATOM   2306 C CB  . ALA A 1 307 ? 9.63400   30.85000  98.26700  1.000 27.46427 ? 307 ALA A CB  1 
ATOM   2307 N N   . ALA A 1 308 ? 9.80800   28.42500  100.29600 1.000 25.80872 ? 308 ALA A N   1 
ATOM   2308 C CA  . ALA A 1 308 ? 10.60800  27.49000  101.08700 1.000 27.31982 ? 308 ALA A CA  1 
ATOM   2309 C C   . ALA A 1 308 ? 10.17000  26.04600  100.86800 1.000 26.91419 ? 308 ALA A C   1 
ATOM   2310 O O   . ALA A 1 308 ? 10.98200  25.12400  101.01000 1.000 30.10288 ? 308 ALA A O   1 
ATOM   2311 C CB  . ALA A 1 308 ? 10.53500  27.85000  102.57100 1.000 24.85398 ? 308 ALA A CB  1 
ATOM   2312 N N   A ARG A 1 309 ? 8.89300   25.82600  100.54500 0.429 28.68597 ? 309 ARG A N   1 
ATOM   2313 N N   B ARG A 1 309 ? 8.89600   25.83300  100.53700 0.571 28.67827 ? 309 ARG A N   1 
ATOM   2314 C CA  A ARG A 1 309 ? 8.43300   24.47800  100.22400 0.429 30.69550 ? 309 ARG A CA  1 
ATOM   2315 C CA  B ARG A 1 309 ? 8.41400   24.49400  100.21800 0.571 30.76064 ? 309 ARG A CA  1 
ATOM   2316 C C   A ARG A 1 309 ? 9.09200   23.95600  98.95100  0.429 30.68669 ? 309 ARG A C   1 
ATOM   2317 C C   B ARG A 1 309 ? 9.06400   23.95700  98.94700  0.571 30.71845 ? 309 ARG A C   1 
ATOM   2318 O O   A ARG A 1 309 ? 9.45700   22.77700  98.87300  0.429 29.29866 ? 309 ARG A O   1 
ATOM   2319 O O   B ARG A 1 309 ? 9.39000   22.76700  98.86500  0.571 29.27691 ? 309 ARG A O   1 
ATOM   2320 C CB  A ARG A 1 309 ? 6.90700   24.46000  100.08900 0.429 30.51081 ? 309 ARG A CB  1 
ATOM   2321 C CB  B ARG A 1 309 ? 6.89100   24.52200  100.07500 0.571 30.53620 ? 309 ARG A CB  1 
ATOM   2322 C CG  A ARG A 1 309 ? 6.33200   23.16200  99.52000  0.429 30.54549 ? 309 ARG A CG  1 
ATOM   2323 C CG  B ARG A 1 309 ? 6.20100   23.16700  100.00900 0.571 30.57940 ? 309 ARG A CG  1 
ATOM   2324 C CD  A ARG A 1 309 ? 4.83200   23.27800  99.26700  0.429 30.44585 ? 309 ARG A CD  1 
ATOM   2325 C CD  B ARG A 1 309 ? 4.70600   23.38100  100.16000 0.571 32.32387 ? 309 ARG A CD  1 
ATOM   2326 N NE  A ARG A 1 309 ? 4.42300   22.53000  98.08400  0.429 33.84595 ? 309 ARG A NE  1 
ATOM   2327 N NE  B ARG A 1 309 ? 4.45500   24.51000  101.05100 0.571 34.70964 ? 309 ARG A NE  1 
ATOM   2328 C CZ  A ARG A 1 309 ? 3.81800   21.35000  98.10500  0.429 30.97413 ? 309 ARG A CZ  1 
ATOM   2329 C CZ  B ARG A 1 309 ? 3.26400   25.03800  101.29400 0.571 26.90079 ? 309 ARG A CZ  1 
ATOM   2330 N NH1 A ARG A 1 309 ? 3.49100   20.75900  99.24200  0.429 29.18509 ? 309 ARG A NH1 1 
ATOM   2331 N NH1 B ARG A 1 309 ? 2.16400   24.53600  100.75900 0.571 30.19579 ? 309 ARG A NH1 1 
ATOM   2332 N NH2 A ARG A 1 309 ? 3.53300   20.74900  96.95400  0.429 28.51089 ? 309 ARG A NH2 1 
ATOM   2333 N NH2 B ARG A 1 309 ? 3.17900   26.10400  102.08300 0.571 19.37489 ? 309 ARG A NH2 1 
ATOM   2334 N N   . GLN A 1 310 ? 9.25800   24.81800  97.94500  1.000 29.73513 ? 310 GLN A N   1 
ATOM   2335 C CA  . GLN A 1 310 ? 9.76700   24.39300  96.64600  1.000 31.51490 ? 310 GLN A CA  1 
ATOM   2336 C C   . GLN A 1 310 ? 11.27800  24.53300  96.49200  1.000 31.78086 ? 310 GLN A C   1 
ATOM   2337 O O   . GLN A 1 310 ? 11.85200  23.90300  95.59500  1.000 27.49337 ? 310 GLN A O   1 
ATOM   2338 C CB  . GLN A 1 310 ? 9.06300   25.18100  95.53200  1.000 25.05293 ? 310 GLN A CB  1 
ATOM   2339 C CG  . GLN A 1 310 ? 7.59600   24.79600  95.36000  1.000 28.68930 ? 310 GLN A CG  1 
ATOM   2340 C CD  . GLN A 1 310 ? 6.81700   25.70400  94.41500  1.000 24.81376 ? 310 GLN A CD  1 
ATOM   2341 O OE1 . GLN A 1 310 ? 5.76600   25.31900  93.89500  1.000 27.10647 ? 310 GLN A OE1 1 
ATOM   2342 N NE2 . GLN A 1 310 ? 7.31700   26.91300  94.20200  1.000 23.16027 ? 310 GLN A NE2 1 
ATOM   2343 N N   . GLN A 1 311 ? 11.93900  25.31500  97.34400  1.000 30.14984 ? 311 GLN A N   1 
ATOM   2344 C CA  . GLN A 1 311 ? 13.32800  25.69600  97.12600  1.000 28.54888 ? 311 GLN A CA  1 
ATOM   2345 C C   . GLN A 1 311 ? 14.17000  25.38000  98.35100  1.000 32.23311 ? 311 GLN A C   1 
ATOM   2346 O O   . GLN A 1 311 ? 13.72400  25.56100  99.48800  1.000 37.02182 ? 311 GLN A O   1 
ATOM   2347 C CB  . GLN A 1 311 ? 13.43200  27.18600  96.79800  1.000 23.87616 ? 311 GLN A CB  1 
ATOM   2348 C CG  . GLN A 1 311 ? 12.48800  27.61700  95.69500  1.000 24.04175 ? 311 GLN A CG  1 
ATOM   2349 C CD  . GLN A 1 311 ? 12.36000  29.11400  95.60500  1.000 24.99803 ? 311 GLN A CD  1 
ATOM   2350 O OE1 . GLN A 1 311 ? 11.40200  29.63000  95.03300  1.000 25.19030 ? 311 GLN A OE1 1 
ATOM   2351 N NE2 . GLN A 1 311 ? 13.33000  29.82700  96.17400  1.000 23.46111 ? 311 GLN A NE2 1 
ATOM   2352 N N   . ARG A 1 312 ? 15.39400  24.90400  98.11300  1.000 27.81778 ? 312 ARG A N   1 
ATOM   2353 C CA  . ARG A 1 312 ? 16.31300  24.66400  99.21800  1.000 31.05077 ? 312 ARG A CA  1 
ATOM   2354 C C   . ARG A 1 312 ? 16.80800  25.97200  99.82200  1.000 30.46269 ? 312 ARG A C   1 
ATOM   2355 O O   . ARG A 1 312 ? 17.03300  26.04500  101.03500 1.000 29.56669 ? 312 ARG A O   1 
ATOM   2356 C CB  . ARG A 1 312 ? 17.49200  23.80700  98.75200  1.000 30.39215 ? 312 ARG A CB  1 
ATOM   2357 C CG  . ARG A 1 312 ? 18.48200  23.46700  99.86000  1.000 32.20438 ? 312 ARG A CG  1 
ATOM   2358 C CD  . ARG A 1 312 ? 19.50400  22.41800  99.41900  1.000 37.58190 ? 312 ARG A CD  1 
ATOM   2359 N NE  . ARG A 1 312 ? 20.31600  22.86200  98.29000  1.000 31.65006 ? 312 ARG A NE  1 
ATOM   2360 C CZ  . ARG A 1 312 ? 21.43700  23.56200  98.39900  1.000 32.95974 ? 312 ARG A CZ  1 
ATOM   2361 N NH1 . ARG A 1 312 ? 21.89900  23.95000  99.57800  1.000 34.80616 ? 312 ARG A NH1 1 
ATOM   2362 N NH2 . ARG A 1 312 ? 22.11300  23.88100  97.29800  1.000 35.34825 ? 312 ARG A NH2 1 
ATOM   2363 N N   . LEU A 1 313 ? 16.99300  26.99600  98.99800  1.000 24.11918 ? 313 LEU A N   1 
ATOM   2364 C CA  . LEU A 1 313 ? 17.42200  28.32300  99.40800  1.000 25.24072 ? 313 LEU A CA  1 
ATOM   2365 C C   . LEU A 1 313 ? 16.58700  29.34700  98.65700  1.000 26.84659 ? 313 LEU A C   1 
ATOM   2366 O O   . LEU A 1 313 ? 16.03200  29.04300  97.59600  1.000 25.26213 ? 313 LEU A O   1 
ATOM   2367 C CB  . LEU A 1 313 ? 18.91500  28.55200  99.13300  1.000 26.22789 ? 313 LEU A CB  1 
ATOM   2368 C CG  . LEU A 1 313 ? 19.91900  27.80900  100.01700 1.000 29.41776 ? 313 LEU A CG  1 
ATOM   2369 C CD1 . LEU A 1 313 ? 21.33700  28.22300  99.66600  1.000 28.18195 ? 313 LEU A CD1 1 
ATOM   2370 C CD2 . LEU A 1 313 ? 19.64400  28.06400  101.49000 1.000 28.61989 ? 313 LEU A CD2 1 
ATOM   2371 N N   . PRO A 1 314 ? 16.45700  30.56600  99.19300  1.000 24.87381 ? 314 PRO A N   1 
ATOM   2372 C CA  . PRO A 1 314 ? 15.53600  31.53900  98.58000  1.000 24.97972 ? 314 PRO A CA  1 
ATOM   2373 C C   . PRO A 1 314 ? 15.89800  31.95900  97.16500  1.000 26.00795 ? 314 PRO A C   1 
ATOM   2374 O O   . PRO A 1 314 ? 14.99700  32.30600  96.39000  1.000 24.42763 ? 314 PRO A O   1 
ATOM   2375 C CB  . PRO A 1 314 ? 15.59600  32.73100  99.55000  1.000 23.17552 ? 314 PRO A CB  1 
ATOM   2376 C CG  . PRO A 1 314 ? 15.98000  32.13300  100.85200 1.000 21.90517 ? 314 PRO A CG  1 
ATOM   2377 C CD  . PRO A 1 314 ? 16.93700  31.02500  100.50700 1.000 24.88585 ? 314 PRO A CD  1 
ATOM   2378 N N   . GLY A 1 315 ? 17.17500  31.95700  96.80400  1.000 22.71174 ? 315 GLY A N   1 
ATOM   2379 C CA  . GLY A 1 315 ? 17.63200  32.54700  95.56100  1.000 20.03253 ? 315 GLY A CA  1 
ATOM   2380 C C   . GLY A 1 315 ? 18.58200  33.70300  95.81300  1.000 23.25151 ? 315 GLY A C   1 
ATOM   2381 O O   . GLY A 1 315 ? 18.89200  34.05700  96.95000  1.000 21.87773 ? 315 GLY A O   1 
ATOM   2382 N N   . ALA A 1 316 ? 19.05100  34.29600  94.71100  1.000 18.57650 ? 316 ALA A N   1 
ATOM   2383 C CA  . ALA A 1 316 ? 20.06600  35.34100  94.78600  1.000 19.11939 ? 316 ALA A CA  1 
ATOM   2384 C C   . ALA A 1 316 ? 19.69100  36.58800  93.99700  1.000 19.00236 ? 316 ALA A C   1 
ATOM   2385 O O   . ALA A 1 316 ? 20.53000  37.48300  93.82600  1.000 18.64274 ? 316 ALA A O   1 
ATOM   2386 C CB  . ALA A 1 316 ? 21.42000  34.81300  94.30500  1.000 19.23929 ? 316 ALA A CB  1 
ATOM   2387 N N   . ILE A 1 317 ? 18.46400  36.66800  93.50500  1.000 20.67059 ? 317 ILE A N   1 
ATOM   2388 C CA  . ILE A 1 317 ? 17.95800  37.84100  92.80900  1.000 22.03438 ? 317 ILE A CA  1 
ATOM   2389 C C   . ILE A 1 317 ? 16.97200  38.54700  93.73000  1.000 22.80711 ? 317 ILE A C   1 
ATOM   2390 O O   . ILE A 1 317 ? 16.09100  37.90500  94.31600  1.000 19.64823 ? 317 ILE A O   1 
ATOM   2391 C CB  . ILE A 1 317 ? 17.30300  37.45000  91.47400  1.000 20.05574 ? 317 ILE A CB  1 
ATOM   2392 C CG1 . ILE A 1 317 ? 18.37700  36.92900  90.51200  1.000 23.11920 ? 317 ILE A CG1 1 
ATOM   2393 C CG2 . ILE A 1 317 ? 16.55200  38.63100  90.87600  1.000 20.46236 ? 317 ILE A CG2 1 
ATOM   2394 C CD1 . ILE A 1 317 ? 17.82500  36.11900  89.36000  1.000 23.65151 ? 317 ILE A CD1 1 
ATOM   2395 N N   . LEU A 1 318 ? 17.13900  39.86100  93.88000  1.000 22.83749 ? 318 LEU A N   1 
ATOM   2396 C CA  . LEU A 1 318 ? 16.20400  40.68100  94.63500  1.000 21.12555 ? 318 LEU A CA  1 
ATOM   2397 C C   . LEU A 1 318 ? 15.89900  41.94700  93.84800  1.000 24.57526 ? 318 LEU A C   1 
ATOM   2398 O O   . LEU A 1 318 ? 16.66800  42.36800  92.98000  1.000 24.37919 ? 318 LEU A O   1 
ATOM   2399 C CB  . LEU A 1 318 ? 16.75100  41.04000  96.02600  1.000 22.45593 ? 318 LEU A CB  1 
ATOM   2400 C CG  . LEU A 1 318 ? 18.03800  41.87600  96.09700  1.000 20.56881 ? 318 LEU A CG  1 
ATOM   2401 C CD1 . LEU A 1 318 ? 17.74800  43.37300  96.08900  1.000 17.62969 ? 318 LEU A CD1 1 
ATOM   2402 C CD2 . LEU A 1 318 ? 18.86100  41.49100  97.32400  1.000 20.50394 ? 318 LEU A CD2 1 
ATOM   2403 N N   . SER A 1 319 ? 14.75700  42.54900  94.16400  1.000 24.72057 ? 319 SER A N   1 
ATOM   2404 C CA  . SER A 1 319 ? 14.40500  43.87100  93.67700  1.000 24.81109 ? 319 SER A CA  1 
ATOM   2405 C C   . SER A 1 319 ? 13.99200  44.72500  94.86500  1.000 29.20345 ? 319 SER A C   1 
ATOM   2406 O O   . SER A 1 319 ? 13.59100  44.20900  95.91200  1.000 28.72286 ? 319 SER A O   1 
ATOM   2407 C CB  . SER A 1 319 ? 13.27700  43.82100  92.63400  1.000 25.53820 ? 319 SER A CB  1 
ATOM   2408 O OG  . SER A 1 319 ? 13.71000  43.21700  91.42300  1.000 20.93340 ? 319 SER A OG  1 
ATOM   2409 N N   . PHE A 1 320 ? 14.11300  46.04100  94.70800  1.000 26.43114 ? 320 PHE A N   1 
ATOM   2410 C CA  . PHE A 1 320 ? 13.68800  46.94300  95.76700  1.000 28.59574 ? 320 PHE A CA  1 
ATOM   2411 C C   . PHE A 1 320 ? 13.20100  48.25500  95.16500  1.000 31.00553 ? 320 PHE A C   1 
ATOM   2412 O O   . PHE A 1 320 ? 13.68700  48.70000  94.12000  1.000 29.98053 ? 320 PHE A O   1 
ATOM   2413 C CB  . PHE A 1 320 ? 14.80700  47.18200  96.79600  1.000 26.06611 ? 320 PHE A CB  1 
ATOM   2414 C CG  . PHE A 1 320 ? 16.02300  47.88500  96.24700  1.000 27.90745 ? 320 PHE A CG  1 
ATOM   2415 C CD1 . PHE A 1 320 ? 16.98500  47.18900  95.53000  1.000 27.48498 ? 320 PHE A CD1 1 
ATOM   2416 C CD2 . PHE A 1 320 ? 16.22200  49.23400  96.48300  1.000 27.39299 ? 320 PHE A CD2 1 
ATOM   2417 C CE1 . PHE A 1 320 ? 18.11000  47.83100  95.03600  1.000 24.77375 ? 320 PHE A CE1 1 
ATOM   2418 C CE2 . PHE A 1 320 ? 17.34600  49.88400  95.99500  1.000 28.37069 ? 320 PHE A CE2 1 
ATOM   2419 C CZ  . PHE A 1 320 ? 18.29100  49.17900  95.26800  1.000 28.51284 ? 320 PHE A CZ  1 
ATOM   2420 N N   . ASP A 1 321 ? 12.20600  48.84500  95.82500  1.000 29.12659 ? 321 ASP A N   1 
ATOM   2421 C CA  . ASP A 1 321 ? 11.65900  50.14800  95.46300  1.000 31.74976 ? 321 ASP A CA  1 
ATOM   2422 C C   . ASP A 1 321 ? 12.26900  51.20800  96.36900  1.000 33.03506 ? 321 ASP A C   1 
ATOM   2423 O O   . ASP A 1 321 ? 12.19300  51.09900  97.59800  1.000 31.97737 ? 321 ASP A O   1 
ATOM   2424 C CB  . ASP A 1 321 ? 10.13500  50.17900  95.61500  1.000 30.58153 ? 321 ASP A CB  1 
ATOM   2425 C CG  . ASP A 1 321 ? 9.41000   49.36000  94.56300  1.000 35.74048 ? 321 ASP A CG  1 
ATOM   2426 O OD1 . ASP A 1 321 ? 9.74200   49.47700  93.36300  1.000 35.22720 ? 321 ASP A OD1 1 
ATOM   2427 O OD2 . ASP A 1 321 ? 8.48300   48.61100  94.94100  1.000 39.38366 ? 321 ASP A OD2 1 
ATOM   2428 N N   . LEU A 1 322 ? 12.85900  52.23400  95.77400  1.000 27.69090 ? 322 LEU A N   1 
ATOM   2429 C CA  . LEU A 1 322 ? 13.34300  53.36200  96.55100  1.000 37.90982 ? 322 LEU A CA  1 
ATOM   2430 C C   . LEU A 1 322 ? 12.38500  54.53500  96.38500  1.000 36.73350 ? 322 LEU A C   1 
ATOM   2431 O O   . LEU A 1 322 ? 11.78100  54.71200  95.32100  1.000 30.55331 ? 322 LEU A O   1 
ATOM   2432 C CB  . LEU A 1 322 ? 14.77100  53.75800  96.15200  1.000 33.85799 ? 322 LEU A CB  1 
ATOM   2433 C CG  . LEU A 1 322 ? 15.28100  53.42700  94.75300  1.000 36.68639 ? 322 LEU A CG  1 
ATOM   2434 C CD1 . LEU A 1 322 ? 14.59200  54.29500  93.71400  1.000 39.45862 ? 322 LEU A CD1 1 
ATOM   2435 C CD2 . LEU A 1 322 ? 16.79600  53.59300  94.68700  1.000 32.90129 ? 322 LEU A CD2 1 
ATOM   2436 N N   . HIS A 1 323 ? 12.19700  55.29100  97.46700  1.000 33.95821 ? 323 HIS A N   1 
ATOM   2437 C CA  . HIS A 1 323 ? 11.42600  56.52200  97.37600  1.000 35.29276 ? 323 HIS A CA  1 
ATOM   2438 C C   . HIS A 1 323 ? 12.13400  57.48000  96.42900  1.000 37.38776 ? 323 HIS A C   1 
ATOM   2439 O O   . HIS A 1 323 ? 13.36200  57.61800  96.46000  1.000 38.43733 ? 323 HIS A O   1 
ATOM   2440 C CB  . HIS A 1 323 ? 11.26400  57.17700  98.75100  1.000 26.18875 ? 323 HIS A CB  1 
ATOM   2441 C CG  . HIS A 1 323 ? 10.68600  56.27900  99.80100  1.000 33.61164 ? 323 HIS A CG  1 
ATOM   2442 N ND1 . HIS A 1 323 ? 9.36800   55.87700  99.79600  1.000 30.00952 ? 323 HIS A ND1 1 
ATOM   2443 C CD2 . HIS A 1 323 ? 11.24200  55.73200  100.90900 1.000 33.63878 ? 323 HIS A CD2 1 
ATOM   2444 C CE1 . HIS A 1 323 ? 9.14000   55.10800  100.84600 1.000 29.47301 ? 323 HIS A CE1 1 
ATOM   2445 N NE2 . HIS A 1 323 ? 10.26100  55.00300  101.53700 1.000 34.95558 ? 323 HIS A NE2 1 
ATOM   2446 N N   . GLY A 1 324 ? 11.35700  58.14000  95.57900  1.000 31.03742 ? 324 GLY A N   1 
ATOM   2447 C CA  . GLY A 1 324 ? 11.91400  59.04600  94.59800  1.000 27.05705 ? 324 GLY A CA  1 
ATOM   2448 C C   . GLY A 1 324 ? 11.79800  58.56800  93.17300  1.000 28.37554 ? 324 GLY A C   1 
ATOM   2449 O O   . GLY A 1 324 ? 12.22500  59.29000  92.26400  1.000 29.07757 ? 324 GLY A O   1 
ATOM   2450 N N   . GLY A 1 325 ? 11.24900  57.37700  92.94700  1.000 26.93984 ? 325 GLY A N   1 
ATOM   2451 C CA  . GLY A 1 325 ? 10.95700  56.92700  91.60000  1.000 28.01870 ? 325 GLY A CA  1 
ATOM   2452 C C   . GLY A 1 325 ? 12.20200  56.80200  90.74100  1.000 30.71522 ? 325 GLY A C   1 
ATOM   2453 O O   . GLY A 1 325 ? 13.30800  56.51500  91.21900  1.000 30.65746 ? 325 GLY A O   1 
ATOM   2454 N N   . GLN A 1 326 ? 12.01900  57.05400  89.44200  1.000 28.05635 ? 326 GLN A N   1 
ATOM   2455 C CA  . GLN A 1 326 ? 13.09800  56.84800  88.48300  1.000 29.12086 ? 326 GLN A CA  1 
ATOM   2456 C C   . GLN A 1 326 ? 14.27300  57.77400  88.75000  1.000 29.27330 ? 326 GLN A C   1 
ATOM   2457 O O   . GLN A 1 326 ? 15.43100  57.37200  88.59300  1.000 30.93292 ? 326 GLN A O   1 
ATOM   2458 C CB  . GLN A 1 326 ? 12.58900  57.03800  87.05700  1.000 25.89931 ? 326 GLN A CB  1 
ATOM   2459 C CG  . GLN A 1 326 ? 13.67300  56.81000  86.02800  1.000 29.44340 ? 326 GLN A CG  1 
ATOM   2460 C CD  . GLN A 1 326 ? 13.15000  56.78000  84.60900  1.000 34.18481 ? 326 GLN A CD  1 
ATOM   2461 O OE1 . GLN A 1 326 ? 12.33800  55.92500  84.24600  1.000 30.21074 ? 326 GLN A OE1 1 
ATOM   2462 N NE2 . GLN A 1 326 ? 13.62100  57.71500  83.79300  1.000 25.59773 ? 326 GLN A NE2 1 
ATOM   2463 N N   . LYS A 1 327 ? 14.00200  59.02100  89.14000  1.000 27.71582 ? 327 LYS A N   1 
ATOM   2464 C CA  . LYS A 1 327 ? 15.09200  59.95500  89.40100  1.000 29.09209 ? 327 LYS A CA  1 
ATOM   2465 C C   . LYS A 1 327 ? 16.01900  59.42400  90.48500  1.000 28.98867 ? 327 LYS A C   1 
ATOM   2466 O O   . LYS A 1 327 ? 17.24700  59.49400  90.35200  1.000 26.83409 ? 327 LYS A O   1 
ATOM   2467 C CB  . LYS A 1 327 ? 14.53600  61.32000  89.80000  1.000 34.36196 ? 327 LYS A CB  1 
ATOM   2468 C CG  . LYS A 1 327 ? 15.60600  62.35300  90.13400  1.000 32.52389 ? 327 LYS A CG  1 
ATOM   2469 C CD  . LYS A 1 327 ? 14.98300  63.60800  90.72700  1.000 32.03039 ? 327 LYS A CD  1 
ATOM   2470 C CE  . LYS A 1 327 ? 16.03500  64.65700  91.03400  1.000 39.11922 ? 327 LYS A CE  1 
ATOM   2471 N NZ  . LYS A 1 327 ? 16.64200  65.19900  89.79100  1.000 38.11568 ? 327 LYS A NZ  1 
ATOM   2472 N N   . ALA A 1 328 ? 15.44900  58.88500  91.56400  1.000 27.67557 ? 328 ALA A N   1 
ATOM   2473 C CA  . ALA A 1 328 ? 16.27200  58.30500  92.61900  1.000 27.09839 ? 328 ALA A CA  1 
ATOM   2474 C C   . ALA A 1 328 ? 16.99700  57.04900  92.13800  1.000 27.72739 ? 328 ALA A C   1 
ATOM   2475 O O   . ALA A 1 328 ? 18.17400  56.84800  92.45500  1.000 29.12345 ? 328 ALA A O   1 
ATOM   2476 C CB  . ALA A 1 328 ? 15.40900  58.00100  93.84200  1.000 25.53061 ? 328 ALA A CB  1 
ATOM   2477 N N   . ALA A 1 329 ? 16.31600  56.19600  91.36900  1.000 27.37290 ? 329 ALA A N   1 
ATOM   2478 C CA  . ALA A 1 329 ? 16.93200  54.94700  90.92800  1.000 29.30453 ? 329 ALA A CA  1 
ATOM   2479 C C   . ALA A 1 329 ? 18.11600  55.20800  90.00300  1.000 29.79563 ? 329 ALA A C   1 
ATOM   2480 O O   . ALA A 1 329 ? 19.14200  54.52000  90.08700  1.000 25.60470 ? 329 ALA A O   1 
ATOM   2481 C CB  . ALA A 1 329 ? 15.89500  54.06100  90.23900  1.000 27.41334 ? 329 ALA A CB  1 
ATOM   2482 N N   . TRP A 1 330 ? 17.99300  56.19400  89.11300  1.000 26.96272 ? 330 TRP A N   1 
ATOM   2483 C CA  . TRP A 1 330 ? 19.09300  56.50200  88.20600  1.000 29.17412 ? 330 TRP A CA  1 
ATOM   2484 C C   . TRP A 1 330 ? 20.26100  57.14600  88.94300  1.000 29.33856 ? 330 TRP A C   1 
ATOM   2485 O O   . TRP A 1 330 ? 21.42300  56.82300  88.67200  1.000 30.83947 ? 330 TRP A O   1 
ATOM   2486 C CB  . TRP A 1 330 ? 18.60600  57.39400  87.06900  1.000 24.01170 ? 330 TRP A CB  1 
ATOM   2487 C CG  . TRP A 1 330 ? 17.83400  56.63200  86.04500  1.000 24.43313 ? 330 TRP A CG  1 
ATOM   2488 C CD1 . TRP A 1 330 ? 17.32000  55.37800  86.17800  1.000 25.05942 ? 330 TRP A CD1 1 
ATOM   2489 C CD2 . TRP A 1 330 ? 17.50300  57.06500  84.72000  1.000 27.67365 ? 330 TRP A CD2 1 
ATOM   2490 N NE1 . TRP A 1 330 ? 16.68100  55.00100  85.01900  1.000 25.12129 ? 330 TRP A NE1 1 
ATOM   2491 C CE2 . TRP A 1 330 ? 16.78000  56.01800  84.10800  1.000 23.14646 ? 330 TRP A CE2 1 
ATOM   2492 C CE3 . TRP A 1 330 ? 17.74600  58.23700  83.99200  1.000 26.97719 ? 330 TRP A CE3 1 
ATOM   2493 C CZ2 . TRP A 1 330 ? 16.29100  56.10800  82.80400  1.000 28.62626 ? 330 TRP A CZ2 1 
ATOM   2494 C CZ3 . TRP A 1 330 ? 17.26300  58.32600  82.69900  1.000 26.82302 ? 330 TRP A CZ3 1 
ATOM   2495 C CH2 . TRP A 1 330 ? 16.54400  57.26400  82.11500  1.000 30.97675 ? 330 TRP A CH2 1 
ATOM   2496 N N   . ALA A 1 331 ? 19.97900  58.05000  89.88200  1.000 27.24127 ? 331 ALA A N   1 
ATOM   2497 C CA  . ALA A 1 331 ? 21.05600  58.63300  90.67300  1.000 29.90527 ? 331 ALA A CA  1 
ATOM   2498 C C   . ALA A 1 331 ? 21.77000  57.56400  91.49300  1.000 30.06741 ? 331 ALA A C   1 
ATOM   2499 O O   . ALA A 1 331 ? 23.00000  57.58600  91.62300  1.000 26.51676 ? 331 ALA A O   1 
ATOM   2500 C CB  . ALA A 1 331 ? 20.50700  59.73400  91.57800  1.000 26.74658 ? 331 ALA A CB  1 
ATOM   2501 N N   . PHE A 1 332 ? 21.00900  56.61000  92.03900  1.000 27.87428 ? 332 PHE A N   1 
ATOM   2502 C CA  . PHE A 1 332 ? 21.59000  55.53400  92.83700  1.000 27.08953 ? 332 PHE A CA  1 
ATOM   2503 C C   . PHE A 1 332 ? 22.58200  54.70900  92.02300  1.000 25.04266 ? 332 PHE A C   1 
ATOM   2504 O O   . PHE A 1 332 ? 23.72800  54.51000  92.43800  1.000 22.15652 ? 332 PHE A O   1 
ATOM   2505 C CB  . PHE A 1 332 ? 20.46700  54.65100  93.38200  1.000 23.59784 ? 332 PHE A CB  1 
ATOM   2506 C CG  . PHE A 1 332 ? 20.93800  53.49300  94.21500  1.000 25.88933 ? 332 PHE A CG  1 
ATOM   2507 C CD1 . PHE A 1 332 ? 21.25700  52.27600  93.62800  1.000 27.92318 ? 332 PHE A CD1 1 
ATOM   2508 C CD2 . PHE A 1 332 ? 21.02300  53.60800  95.58900  1.000 26.44826 ? 332 PHE A CD2 1 
ATOM   2509 C CE1 . PHE A 1 332 ? 21.67600  51.20700  94.39800  1.000 25.61311 ? 332 PHE A CE1 1 
ATOM   2510 C CE2 . PHE A 1 332 ? 21.44400  52.54600  96.36500  1.000 26.86516 ? 332 PHE A CE2 1 
ATOM   2511 C CZ  . PHE A 1 332 ? 21.76700  51.34200  95.77000  1.000 28.36174 ? 332 PHE A CZ  1 
ATOM   2512 N N   . VAL A 1 333 ? 22.16200  54.22500  90.85200  1.000 22.88407 ? 333 VAL A N   1 
ATOM   2513 C CA  . VAL A 1 333 ? 23.03500  53.34400  90.08400  1.000 27.11657 ? 333 VAL A CA  1 
ATOM   2514 C C   . VAL A 1 333 ? 24.22600  54.11700  89.53100  1.000 27.86073 ? 333 VAL A C   1 
ATOM   2515 O O   . VAL A 1 333 ? 25.34700  53.59500  89.47800  1.000 26.02998 ? 333 VAL A O   1 
ATOM   2516 C CB  . VAL A 1 333 ? 22.25000  52.62300  88.97200  1.000 26.86652 ? 333 VAL A CB  1 
ATOM   2517 C CG1 . VAL A 1 333 ? 21.11500  51.80700  89.56600  1.000 22.72201 ? 333 VAL A CG1 1 
ATOM   2518 C CG2 . VAL A 1 333 ? 21.72400  53.60200  87.95600  1.000 26.57676 ? 333 VAL A CG2 1 
ATOM   2519 N N   . ASP A 1 334 ? 24.01000  55.37600  89.13100  1.000 27.05284 ? 334 ASP A N   1 
ATOM   2520 C CA  . ASP A 1 334 ? 25.07300  56.16800  88.52300  1.000 26.88310 ? 334 ASP A CA  1 
ATOM   2521 C C   . ASP A 1 334 ? 26.21500  56.44100  89.49200  1.000 24.94748 ? 334 ASP A C   1 
ATOM   2522 O O   . ASP A 1 334 ? 27.33000  56.73800  89.05200  1.000 32.26178 ? 334 ASP A O   1 
ATOM   2523 C CB  . ASP A 1 334 ? 24.50800  57.49200  87.98700  1.000 28.52346 ? 334 ASP A CB  1 
ATOM   2524 C CG  . ASP A 1 334 ? 23.70600  57.31800  86.69400  1.000 29.51370 ? 334 ASP A CG  1 
ATOM   2525 O OD1 . ASP A 1 334 ? 23.63700  56.19000  86.15800  1.000 28.45546 ? 334 ASP A OD1 1 
ATOM   2526 O OD2 . ASP A 1 334 ? 23.14400  58.32100  86.20700  1.000 32.93340 ? 334 ASP A OD2 1 
ATOM   2527 N N   . ALA A 1 335 ? 25.96800  56.34600  90.79500  1.000 24.52950 ? 335 ALA A N   1 
ATOM   2528 C CA  . ALA A 1 335 ? 27.02100  56.51900  91.78400  1.000 24.43925 ? 335 ALA A CA  1 
ATOM   2529 C C   . ALA A 1 335 ? 27.76600  55.22700  92.10000  1.000 23.31531 ? 335 ALA A C   1 
ATOM   2530 O O   . ALA A 1 335 ? 28.79400  55.27700  92.78100  1.000 26.92348 ? 335 ALA A O   1 
ATOM   2531 C CB  . ALA A 1 335 ? 26.44000  57.10100  93.07800  1.000 24.18729 ? 335 ALA A CB  1 
ATOM   2532 N N   . LEU A 1 336 ? 27.29000  54.08100  91.62900  1.000 26.06443 ? 336 LEU A N   1 
ATOM   2533 C CA  . LEU A 1 336 ? 27.96500  52.82500  91.93200  1.000 27.80408 ? 336 LEU A CA  1 
ATOM   2534 C C   . LEU A 1 336 ? 29.31100  52.75000  91.21700  1.000 25.53142 ? 336 LEU A C   1 
ATOM   2535 O O   . LEU A 1 336 ? 29.45400  53.20100  90.07800  1.000 29.56409 ? 336 LEU A O   1 
ATOM   2536 C CB  . LEU A 1 336 ? 27.08800  51.63900  91.53300  1.000 24.35871 ? 336 LEU A CB  1 
ATOM   2537 C CG  . LEU A 1 336 ? 25.67600  51.61600  92.12700  1.000 27.38882 ? 336 LEU A CG  1 
ATOM   2538 C CD1 . LEU A 1 336 ? 24.90300  50.42000  91.59400  1.000 24.01337 ? 336 LEU A CD1 1 
ATOM   2539 C CD2 . LEU A 1 336 ? 25.70700  51.61100  93.65100  1.000 23.68907 ? 336 LEU A CD2 1 
ATOM   2540 N N   . ARG A 1 337 ? 30.30500  52.18100  91.90200  1.000 25.33248 ? 337 ARG A N   1 
ATOM   2541 C CA  . ARG A 1 337 ? 31.62600  51.97400  91.32900  1.000 26.14917 ? 337 ARG A CA  1 
ATOM   2542 C C   . ARG A 1 337 ? 31.99600  50.50800  91.17000  1.000 30.56786 ? 337 ARG A C   1 
ATOM   2543 O O   . ARG A 1 337 ? 32.96300  50.20500  90.46100  1.000 25.70246 ? 337 ARG A O   1 
ATOM   2544 C CB  . ARG A 1 337 ? 32.69800  52.65300  92.19000  1.000 29.05065 ? 337 ARG A CB  1 
ATOM   2545 C CG  . ARG A 1 337 ? 32.46400  54.12600  92.45200  1.000 33.78151 ? 337 ARG A CG  1 
ATOM   2546 C CD  . ARG A 1 337 ? 33.74300  54.78200  92.94400  1.000 43.96266 ? 337 ARG A CD  1 
ATOM   2547 N NE  . ARG A 1 337 ? 33.49500  56.00800  93.69200  1.000 57.48322 ? 337 ARG A NE  1 
ATOM   2548 C CZ  . ARG A 1 337 ? 34.44700  56.79700  94.17300  1.000 58.12347 ? 337 ARG A CZ  1 
ATOM   2549 N NH1 . ARG A 1 337 ? 35.72900  56.53400  93.97600  1.000 54.32696 ? 337 ARG A NH1 1 
ATOM   2550 N NH2 . ARG A 1 337 ? 34.10400  57.87500  94.87200  1.000 59.24437 ? 337 ARG A NH2 1 
ATOM   2551 N N   . LEU A 1 338 ? 31.26000  49.60000  91.80900  1.000 26.77532 ? 338 LEU A N   1 
ATOM   2552 C CA  . LEU A 1 338 ? 31.57500  48.17900  91.80900  1.000 25.16030 ? 338 LEU A CA  1 
ATOM   2553 C C   . LEU A 1 338 ? 30.54400  47.34200  91.06700  1.000 27.69692 ? 338 LEU A C   1 
ATOM   2554 O O   . LEU A 1 338 ? 30.91100  46.50400  90.23600  1.000 23.59307 ? 338 LEU A O   1 
ATOM   2555 C CB  . LEU A 1 338 ? 31.70400  47.68300  93.25600  1.000 23.17974 ? 338 LEU A CB  1 
ATOM   2556 C CG  . LEU A 1 338 ? 32.16700  46.24100  93.43100  1.000 23.38496 ? 338 LEU A CG  1 
ATOM   2557 C CD1 . LEU A 1 338 ? 33.53000  46.04900  92.77700  1.000 26.21193 ? 338 LEU A CD1 1 
ATOM   2558 C CD2 . LEU A 1 338 ? 32.20900  45.86700  94.90100  1.000 22.48873 ? 338 LEU A CD2 1 
ATOM   2559 N N   . LEU A 1 339 ? 29.25900  47.54500  91.34900  1.000 25.29633 ? 339 LEU A N   1 
ATOM   2560 C CA  . LEU A 1 339 ? 28.21900  46.74800  90.71600  1.000 25.02504 ? 339 LEU A CA  1 
ATOM   2561 C C   . LEU A 1 339 ? 28.17100  47.01300  89.21400  1.000 25.55699 ? 339 LEU A C   1 
ATOM   2562 O O   . LEU A 1 339 ? 28.40900  48.13000  88.75100  1.000 26.38901 ? 339 LEU A O   1 
ATOM   2563 C CB  . LEU A 1 339 ? 26.85500  47.04800  91.34000  1.000 27.09895 ? 339 LEU A CB  1 
ATOM   2564 C CG  . LEU A 1 339 ? 26.47300  46.30800  92.62500  1.000 28.47291 ? 339 LEU A CG  1 
ATOM   2565 C CD1 . LEU A 1 339 ? 27.28700  46.78300  93.81500  1.000 24.79334 ? 339 LEU A CD1 1 
ATOM   2566 C CD2 . LEU A 1 339 ? 24.97300  46.42800  92.89500  1.000 23.94921 ? 339 LEU A CD2 1 
ATOM   2567 N N   . SER A 1 340 ? 27.84800  45.96400  88.45700  1.000 20.70565 ? 340 SER A N   1 
ATOM   2568 C CA  . SER A 1 340 ? 27.78000  46.03000  87.00300  1.000 22.58865 ? 340 SER A CA  1 
ATOM   2569 C C   . SER A 1 340 ? 26.41900  46.55600  86.55600  1.000 23.05977 ? 340 SER A C   1 
ATOM   2570 O O   . SER A 1 340 ? 25.38300  45.98200  86.90400  1.000 21.86497 ? 340 SER A O   1 
ATOM   2571 C CB  . SER A 1 340 ? 28.02300  44.64900  86.39700  1.000 20.69814 ? 340 SER A CB  1 
ATOM   2572 O OG  . SER A 1 340 ? 29.31800  44.17400  86.69900  1.000 20.55543 ? 340 SER A OG  1 
ATOM   2573 N N   . LEU A 1 341 ? 26.42700  47.62900  85.76900  1.000 24.24924 ? 341 LEU A N   1 
ATOM   2574 C CA  . LEU A 1 341 ? 25.21800  48.13600  85.11900  1.000 25.42760 ? 341 LEU A CA  1 
ATOM   2575 C C   . LEU A 1 341 ? 25.01300  47.33700  83.84100  1.000 27.96803 ? 341 LEU A C   1 
ATOM   2576 O O   . LEU A 1 341 ? 25.53300  47.67400  82.77600  1.000 23.75820 ? 341 LEU A O   1 
ATOM   2577 C CB  . LEU A 1 341 ? 25.33200  49.62500  84.81700  1.000 26.68620 ? 341 LEU A CB  1 
ATOM   2578 C CG  . LEU A 1 341 ? 25.53100  50.59800  85.97600  1.000 31.17263 ? 341 LEU A CG  1 
ATOM   2579 C CD1 . LEU A 1 341 ? 25.53300  52.03300  85.46400  1.000 34.59430 ? 341 LEU A CD1 1 
ATOM   2580 C CD2 . LEU A 1 341 ? 24.44800  50.40700  87.01400  1.000 36.06516 ? 341 LEU A CD2 1 
ATOM   2581 N N   . THR A 1 342 ? 24.24700  46.25900  83.94400  1.000 24.51412 ? 342 THR A N   1 
ATOM   2582 C CA  . THR A 1 342 ? 24.08000  45.38100  82.79900  1.000 28.72569 ? 342 THR A CA  1 
ATOM   2583 C C   . THR A 1 342 ? 22.79100  44.59700  82.97500  1.000 26.76958 ? 342 THR A C   1 
ATOM   2584 O O   . THR A 1 342 ? 22.35200  44.34100  84.09900  1.000 30.42594 ? 342 THR A O   1 
ATOM   2585 C CB  . THR A 1 342 ? 25.29000  44.44700  82.63700  1.000 26.17352 ? 342 THR A CB  1 
ATOM   2586 O OG1 . THR A 1 342 ? 25.13400  43.63200  81.46800  1.000 26.11755 ? 342 THR A OG1 1 
ATOM   2587 C CG2 . THR A 1 342 ? 25.44000  43.55600  83.85400  1.000 24.60215 ? 342 THR A CG2 1 
ATOM   2588 N N   . ALA A 1 343 ? 22.18000  44.23900  81.84700  1.000 31.38178 ? 343 ALA A N   1 
ATOM   2589 C CA  . ALA A 1 343 ? 20.89200  43.54500  81.84300  1.000 31.85331 ? 343 ALA A CA  1 
ATOM   2590 C C   . ALA A 1 343 ? 21.13300  42.03400  81.77700  1.000 33.36564 ? 343 ALA A C   1 
ATOM   2591 O O   . ALA A 1 343 ? 20.93200  41.36800  80.75600  1.000 32.55678 ? 343 ALA A O   1 
ATOM   2592 C CB  . ALA A 1 343 ? 20.03000  44.03600  80.68700  1.000 26.03377 ? 343 ALA A CB  1 
ATOM   2593 N N   . ASN A 1 344 ? 21.58200  41.49900  82.90700  1.000 23.31404 ? 344 ASN A N   1 
ATOM   2594 C CA  . ASN A 1 344 ? 21.94100  40.09200  82.98900  1.000 28.93349 ? 344 ASN A CA  1 
ATOM   2595 C C   . ASN A 1 344 ? 21.86700  39.66400  84.44400  1.000 23.47809 ? 344 ASN A C   1 
ATOM   2596 O O   . ASN A 1 344 ? 21.89500  40.49400  85.35500  1.000 27.34194 ? 344 ASN A O   1 
ATOM   2597 C CB  . ASN A 1 344 ? 23.34500  39.83400  82.42400  1.000 25.45560 ? 344 ASN A CB  1 
ATOM   2598 C CG  . ASN A 1 344 ? 23.51100  38.41800  81.89100  1.000 28.40449 ? 344 ASN A CG  1 
ATOM   2599 O OD1 . ASN A 1 344 ? 22.70900  37.53100  82.18700  1.000 31.89161 ? 344 ASN A OD1 1 
ATOM   2600 N ND2 . ASN A 1 344 ? 24.55600  38.20300  81.09900  1.000 27.02973 ? 344 ASN A ND2 1 
ATOM   2601 N N   . LEU A 1 345 ? 21.77600  38.35500  84.64900  1.000 24.19737 ? 345 LEU A N   1 
ATOM   2602 C CA  . LEU A 1 345 ? 21.82200  37.77400  85.98200  1.000 23.95863 ? 345 LEU A CA  1 
ATOM   2603 C C   . LEU A 1 345 ? 22.66500  36.50900  85.93100  1.000 20.83741 ? 345 LEU A C   1 
ATOM   2604 O O   . LEU A 1 345 ? 23.08800  36.06000  84.86300  1.000 21.94888 ? 345 LEU A O   1 
ATOM   2605 C CB  . LEU A 1 345 ? 20.41100  37.48200  86.51700  1.000 22.41717 ? 345 LEU A CB  1 
ATOM   2606 C CG  . LEU A 1 345 ? 19.51400  36.59100  85.65300  1.000 22.95413 ? 345 LEU A CG  1 
ATOM   2607 C CD1 . LEU A 1 345 ? 19.61800  35.13700  86.10200  1.000 27.59898 ? 345 LEU A CD1 1 
ATOM   2608 C CD2 . LEU A 1 345 ? 18.06100  37.06000  85.66600  1.000 21.75028 ? 345 LEU A CD2 1 
ATOM   2609 N N   . GLY A 1 346 ? 22.91600  35.94000  87.10700  1.000 20.57959 ? 346 GLY A N   1 
ATOM   2610 C CA  . GLY A 1 346 ? 23.59900  34.66500  87.18800  1.000 24.22444 ? 346 GLY A CA  1 
ATOM   2611 C C   . GLY A 1 346 ? 25.10100  34.71200  87.03500  1.000 25.92103 ? 346 GLY A C   1 
ATOM   2612 O O   . GLY A 1 346 ? 25.70400  33.70300  86.65700  1.000 22.29320 ? 346 GLY A O   1 
ATOM   2613 N N   . ASP A 1 347 ? 25.73100  35.84400  87.32500  1.000 16.69584 ? 347 ASP A N   1 
ATOM   2614 C CA  . ASP A 1 347 ? 27.17300  35.97600  87.20800  1.000 15.42874 ? 347 ASP A CA  1 
ATOM   2615 C C   . ASP A 1 347 ? 27.80800  36.09200  88.58800  1.000 19.70621 ? 347 ASP A C   1 
ATOM   2616 O O   . ASP A 1 347 ? 27.16900  36.52300  89.55400  1.000 16.25450 ? 347 ASP A O   1 
ATOM   2617 C CB  . ASP A 1 347 ? 27.53800  37.20500  86.36800  1.000 17.98947 ? 347 ASP A CB  1 
ATOM   2618 C CG  . ASP A 1 347 ? 28.95400  37.13800  85.80900  1.000 21.95264 ? 347 ASP A CG  1 
ATOM   2619 O OD1 . ASP A 1 347 ? 29.86600  36.64500  86.51200  1.000 17.93486 ? 347 ASP A OD1 1 
ATOM   2620 O OD2 . ASP A 1 347 ? 29.15500  37.58600  84.65600  1.000 22.23601 ? 347 ASP A OD2 1 
ATOM   2621 N N   . ALA A 1 348 ? 29.07800  35.69200  88.67100  1.000 15.94315 ? 348 ALA A N   1 
ATOM   2622 C CA  . ALA A 1 348 ? 29.86300  36.01800  89.85200  1.000 16.58392 ? 348 ALA A CA  1 
ATOM   2623 C C   . ALA A 1 348 ? 29.89900  37.51900  90.07100  1.000 17.88965 ? 348 ALA A C   1 
ATOM   2624 O O   . ALA A 1 348 ? 29.91200  37.98000  91.21700  1.000 18.98469 ? 348 ALA A O   1 
ATOM   2625 C CB  . ALA A 1 348 ? 31.28200  35.46600  89.72400  1.000 14.56783 ? 348 ALA A CB  1 
ATOM   2626 N N   . LYS A 1 349 ? 29.90200  38.29400  88.98800  1.000 17.90043 ? 349 LYS A N   1 
ATOM   2627 C CA  . LYS A 1 349 ? 29.84200  39.74600  89.08500  1.000 18.01932 ? 349 LYS A CA  1 
ATOM   2628 C C   . LYS A 1 349 ? 28.41500  40.16900  89.41100  1.000 19.72210 ? 349 LYS A C   1 
ATOM   2629 O O   . LYS A 1 349 ? 27.48900  39.88200  88.64300  1.000 17.04128 ? 349 LYS A O   1 
ATOM   2630 C CB  . LYS A 1 349 ? 30.29900  40.39500  87.78000  1.000 20.77477 ? 349 LYS A CB  1 
ATOM   2631 C CG  . LYS A 1 349 ? 31.63700  39.90300  87.24700  1.000 19.33582 ? 349 LYS A CG  1 
ATOM   2632 C CD  . LYS A 1 349 ? 32.16300  40.84100  86.16400  1.000 20.22158 ? 349 LYS A CD  1 
ATOM   2633 C CE  . LYS A 1 349 ? 33.18500  40.15800  85.26100  1.000 22.38777 ? 349 LYS A CE  1 
ATOM   2634 N NZ  . LYS A 1 349 ? 34.25600  39.42800  86.00500  1.000 22.04863 ? 349 LYS A NZ  1 
ATOM   2635 N N   . THR A 1 350 ? 28.23800  40.85000  90.54500  1.000 19.52988 ? 350 THR A N   1 
ATOM   2636 C CA  . THR A 1 350 ? 26.93400  41.40700  90.88500  1.000 18.54353 ? 350 THR A CA  1 
ATOM   2637 C C   . THR A 1 350 ? 26.48400  42.36800  89.79100  1.000 19.41439 ? 350 THR A C   1 
ATOM   2638 O O   . THR A 1 350 ? 27.26600  43.19800  89.32300  1.000 17.23480 ? 350 THR A O   1 
ATOM   2639 C CB  . THR A 1 350 ? 26.99600  42.13600  92.23300  1.000 20.97722 ? 350 THR A CB  1 
ATOM   2640 O OG1 . THR A 1 350 ? 27.30600  41.20600  93.28100  1.000 19.05641 ? 350 THR A OG1 1 
ATOM   2641 C CG2 . THR A 1 350 ? 25.66500  42.80900  92.54900  1.000 19.88395 ? 350 THR A CG2 1 
ATOM   2642 N N   . THR A 1 351 ? 25.22800  42.24300  89.36800  1.000 17.49266 ? 351 THR A N   1 
ATOM   2643 C CA  . THR A 1 351 ? 24.65900  43.14600  88.37900  1.000 19.44285 ? 351 THR A CA  1 
ATOM   2644 C C   . THR A 1 351 ? 23.46700  43.88700  88.96900  1.000 22.36633 ? 351 THR A C   1 
ATOM   2645 O O   . THR A 1 351 ? 22.82000  43.41700  89.91100  1.000 20.42781 ? 351 THR A O   1 
ATOM   2646 C CB  . THR A 1 351 ? 24.20400  42.41100  87.11000  1.000 20.09010 ? 351 THR A CB  1 
ATOM   2647 O OG1 . THR A 1 351 ? 22.98400  41.71100  87.38200  1.000 20.27021 ? 351 THR A OG1 1 
ATOM   2648 C CG2 . THR A 1 351 ? 25.26800  41.42300  86.63700  1.000 18.82578 ? 351 THR A CG2 1 
ATOM   2649 N N   . ILE A 1 352 ? 23.18500  45.05500  88.40400  1.000 24.46631 ? 352 ILE A N   1 
ATOM   2650 C CA  . ILE A 1 352 ? 22.01800  45.84100  88.77500  1.000 24.47074 ? 352 ILE A CA  1 
ATOM   2651 C C   . ILE A 1 352 ? 21.44700  46.46300  87.50800  1.000 27.84727 ? 352 ILE A C   1 
ATOM   2652 O O   . ILE A 1 352 ? 22.18200  46.78500  86.56900  1.000 26.99915 ? 352 ILE A O   1 
ATOM   2653 C CB  . ILE A 1 352 ? 22.36600  46.91300  89.83200  1.000 21.67293 ? 352 ILE A CB  1 
ATOM   2654 C CG1 . ILE A 1 352 ? 21.10500  47.62200  90.33500  1.000 23.18529 ? 352 ILE A CG1 1 
ATOM   2655 C CG2 . ILE A 1 352 ? 23.38700  47.89400  89.28400  1.000 20.61804 ? 352 ILE A CG2 1 
ATOM   2656 C CD1 . ILE A 1 352 ? 21.34000  48.47400  91.57200  1.000 18.99227 ? 352 ILE A CD1 1 
ATOM   2657 N N   . THR A 1 353 ? 20.12200  46.60200  87.47200  1.000 27.08496 ? 353 THR A N   1 
ATOM   2658 C CA  . THR A 1 353 ? 19.46800  47.20700  86.32400  1.000 26.18302 ? 353 THR A CA  1 
ATOM   2659 C C   . THR A 1 353 ? 18.15000  47.82800  86.76400  1.000 29.54411 ? 353 THR A C   1 
ATOM   2660 O O   . THR A 1 353 ? 17.60100  47.49100  87.81700  1.000 25.15468 ? 353 THR A O   1 
ATOM   2661 C CB  . THR A 1 353 ? 19.24100  46.18400  85.21000  1.000 26.06551 ? 353 THR A CB  1 
ATOM   2662 O OG1 . THR A 1 353 ? 18.89400  46.86600  83.99900  1.000 36.36474 ? 353 THR A OG1 1 
ATOM   2663 C CG2 . THR A 1 353 ? 18.13100  45.23000  85.59200  1.000 26.32820 ? 353 THR A CG2 1 
ATOM   2664 N N   . HIS A 1 354 ? 17.65400  48.75500  85.93900  1.000 27.63314 ? 354 HIS A N   1 
ATOM   2665 C CA  . HIS A 1 354 ? 16.41600  49.49100  86.18500  1.000 28.06085 ? 354 HIS A CA  1 
ATOM   2666 C C   . HIS A 1 354 ? 15.37100  49.00200  85.19300  1.000 28.94126 ? 354 HIS A C   1 
ATOM   2667 O O   . HIS A 1 354 ? 15.29900  49.50600  84.06300  1.000 29.42920 ? 354 HIS A O   1 
ATOM   2668 C CB  . HIS A 1 354 ? 16.63600  50.99900  86.04200  1.000 23.32158 ? 354 HIS A CB  1 
ATOM   2669 C CG  . HIS A 1 354 ? 15.39900  51.81200  86.26500  1.000 28.29259 ? 354 HIS A CG  1 
ATOM   2670 N ND1 . HIS A 1 354 ? 14.72800  52.44500  85.24000  1.000 29.91915 ? 354 HIS A ND1 1 
ATOM   2671 C CD2 . HIS A 1 354 ? 14.70700  52.08800  87.39600  1.000 26.64052 ? 354 HIS A CD2 1 
ATOM   2672 C CE1 . HIS A 1 354 ? 13.67800  53.07900  85.73100  1.000 32.61923 ? 354 HIS A CE1 1 
ATOM   2673 N NE2 . HIS A 1 354 ? 13.64300  52.88000  87.03800  1.000 31.75762 ? 354 HIS A NE2 1 
ATOM   2674 N N   . PRO A 1 355 ? 14.54700  48.01900  85.56200  1.000 27.54111 ? 355 PRO A N   1 
ATOM   2675 C CA  . PRO A 1 355 ? 13.71400  47.33700  84.55700  1.000 27.20874 ? 355 PRO A CA  1 
ATOM   2676 C C   . PRO A 1 355 ? 12.73400  48.24200  83.83300  1.000 33.12299 ? 355 PRO A C   1 
ATOM   2677 O O   . PRO A 1 355 ? 12.47100  48.01900  82.64300  1.000 30.23093 ? 355 PRO A O   1 
ATOM   2678 C CB  . PRO A 1 355 ? 12.98700  46.26800  85.38200  1.000 29.30831 ? 355 PRO A CB  1 
ATOM   2679 C CG  . PRO A 1 355 ? 13.85500  46.05700  86.57800  1.000 24.26656 ? 355 PRO A CG  1 
ATOM   2680 C CD  . PRO A 1 355 ? 14.43600  47.39500  86.89000  1.000 25.86570 ? 355 PRO A CD  1 
ATOM   2681 N N   . ALA A 1 356 ? 12.19500  49.26200  84.50800  1.000 32.09972 ? 356 ALA A N   1 
ATOM   2682 C CA  . ALA A 1 356 ? 11.16800  50.10200  83.89500  1.000 36.50076 ? 356 ALA A CA  1 
ATOM   2683 C C   . ALA A 1 356 ? 11.68900  50.83500  82.66700  1.000 34.87768 ? 356 ALA A C   1 
ATOM   2684 O O   . ALA A 1 356 ? 10.91400  51.12800  81.75000  1.000 40.01492 ? 356 ALA A O   1 
ATOM   2685 C CB  . ALA A 1 356 ? 10.61700  51.10200  84.91400  1.000 31.81544 ? 356 ALA A CB  1 
ATOM   2686 N N   . SER A 1 357 ? 12.98700  51.13600  82.61800  1.000 30.35738 ? 357 SER A N   1 
ATOM   2687 C CA  . SER A 1 357 ? 13.54000  51.83500  81.46600  1.000 32.34969 ? 357 SER A CA  1 
ATOM   2688 C C   . SER A 1 357 ? 14.36200  50.93900  80.55000  1.000 32.57683 ? 357 SER A C   1 
ATOM   2689 O O   . SER A 1 357 ? 14.77400  51.39500  79.47800  1.000 33.20298 ? 357 SER A O   1 
ATOM   2690 C CB  . SER A 1 357 ? 14.40000  53.02600  81.91600  1.000 32.40700 ? 357 SER A CB  1 
ATOM   2691 O OG  . SER A 1 357 ? 15.54700  52.60600  82.63100  1.000 30.21216 ? 357 SER A OG  1 
ATOM   2692 N N   . THR A 1 358 ? 14.63800  49.69200  80.93900  1.000 32.61261 ? 358 THR A N   1 
ATOM   2693 C CA  . THR A 1 358 ? 15.40200  48.79900  80.07100  1.000 31.84701 ? 358 THR A CA  1 
ATOM   2694 C C   . THR A 1 358 ? 14.60900  47.56800  79.65000  1.000 33.02377 ? 358 THR A C   1 
ATOM   2695 O O   . THR A 1 358 ? 14.19000  47.48800  78.49500  1.000 41.23545 ? 358 THR A O   1 
ATOM   2696 C CB  . THR A 1 358 ? 16.69300  48.39500  80.78300  1.000 29.22410 ? 358 THR A CB  1 
ATOM   2697 O OG1 . THR A 1 358 ? 16.36500  47.64400  81.95800  1.000 32.20744 ? 358 THR A OG1 1 
ATOM   2698 C CG2 . THR A 1 358 ? 17.49900  49.63400  81.18000  1.000 27.52374 ? 358 THR A CG2 1 
ATOM   2699 N N   . THR A 1 359 ? 14.29000  46.65900  80.56600  1.000 34.72991 ? 359 THR A N   1 
ATOM   2700 C CA  . THR A 1 359 ? 13.72500  45.37800  80.16100  1.000 35.58194 ? 359 THR A CA  1 
ATOM   2701 C C   . THR A 1 359 ? 12.20800  45.40400  80.09300  1.000 38.91147 ? 359 THR A C   1 
ATOM   2702 O O   . THR A 1 359 ? 11.61100  44.54600  79.42900  1.000 33.72895 ? 359 THR A O   1 
ATOM   2703 C CB  . THR A 1 359 ? 14.17700  44.26800  81.11800  1.000 31.81387 ? 359 THR A CB  1 
ATOM   2704 O OG1 . THR A 1 359 ? 13.77100  44.58700  82.45200  1.000 31.64487 ? 359 THR A OG1 1 
ATOM   2705 C CG2 . THR A 1 359 ? 15.68300  44.13000  81.09100  1.000 33.10918 ? 359 THR A CG2 1 
ATOM   2706 N N   . HIS A 1 360 ? 11.58000  46.37600  80.75400  1.000 35.28080 ? 360 HIS A N   1 
ATOM   2707 C CA  . HIS A 1 360 ? 10.13300  46.54000  80.75600  1.000 36.93940 ? 360 HIS A CA  1 
ATOM   2708 C C   . HIS A 1 360 ? 9.71600   47.87500  80.14400  1.000 39.66883 ? 360 HIS A C   1 
ATOM   2709 O O   . HIS A 1 360 ? 8.61200   48.35800  80.41300  1.000 42.46431 ? 360 HIS A O   1 
ATOM   2710 C CB  . HIS A 1 360 ? 9.59400   46.41400  82.18400  1.000 36.30648 ? 360 HIS A CB  1 
ATOM   2711 C CG  . HIS A 1 360 ? 9.75500   45.04800  82.77600  1.000 31.83981 ? 360 HIS A CG  1 
ATOM   2712 N ND1 . HIS A 1 360 ? 10.98200  44.43400  82.91700  1.000 31.37084 ? 360 HIS A ND1 1 
ATOM   2713 C CD2 . HIS A 1 360 ? 8.84000   44.17600  83.26300  1.000 30.19250 ? 360 HIS A CD2 1 
ATOM   2714 C CE1 . HIS A 1 360 ? 10.81500  43.24300  83.46300  1.000 31.75876 ? 360 HIS A CE1 1 
ATOM   2715 N NE2 . HIS A 1 360 ? 9.52500   43.06200  83.68300  1.000 31.41510 ? 360 HIS A NE2 1 
ATOM   2716 N N   . SER A 1 361 ? 10.58300  48.48300  79.33000  1.000 36.73317 ? 361 SER A N   1 
ATOM   2717 C CA  . SER A 1 361 ? 10.32100  49.82300  78.81300  1.000 45.87376 ? 361 SER A CA  1 
ATOM   2718 C C   . SER A 1 361 ? 9.27700   49.82700  77.70100  1.000 50.69054 ? 361 SER A C   1 
ATOM   2719 O O   . SER A 1 361 ? 8.56300   50.82300  77.53300  1.000 51.38282 ? 361 SER A O   1 
ATOM   2720 C CB  . SER A 1 361 ? 11.62000  50.45600  78.31300  1.000 39.31234 ? 361 SER A CB  1 
ATOM   2721 O OG  . SER A 1 361 ? 12.22100  49.64700  77.32100  1.000 39.05134 ? 361 SER A OG  1 
ATOM   2722 N N   . ARG A 1 362 ? 9.17500   48.74100  76.93400  1.000 48.87055 ? 362 ARG A N   1 
ATOM   2723 C CA  . ARG A 1 362 ? 8.16000   48.63600  75.89400  1.000 50.83348 ? 362 ARG A CA  1 
ATOM   2724 C C   . ARG A 1 362 ? 6.79300   48.27300  76.45900  1.000 48.67744 ? 362 ARG A C   1 
ATOM   2725 O O   . ARG A 1 362 ? 5.79400   48.35300  75.73800  1.000 51.43396 ? 362 ARG A O   1 
ATOM   2726 C CB  . ARG A 1 362 ? 8.57800   47.60300  74.83600  1.000 52.37304 ? 362 ARG A CB  1 
ATOM   2727 C CG  . ARG A 1 362 ? 10.03900  47.13100  74.91400  1.000 59.24329 ? 362 ARG A CG  1 
ATOM   2728 C CD  . ARG A 1 362 ? 11.05500  48.21500  74.52500  1.000 65.21372 ? 362 ARG A CD  1 
ATOM   2729 N NE  . ARG A 1 362 ? 11.05300  48.52800  73.10000  1.000 70.87238 ? 362 ARG A NE  1 
ATOM   2730 C CZ  . ARG A 1 362 ? 11.94600  48.07600  72.22900  1.000 74.26650 ? 362 ARG A CZ  1 
ATOM   2731 N NH1 . ARG A 1 362 ? 12.93200  47.27600  72.60000  1.000 78.35623 ? 362 ARG A NH1 1 
ATOM   2732 N NH2 . ARG A 1 362 ? 11.84800  48.43800  70.95200  1.000 69.54686 ? 362 ARG A NH2 1 
ATOM   2733 N N   . VAL A 1 363 ? 6.73300   47.88300  77.71900  1.000 48.65585 ? 363 VAL A N   1 
ATOM   2734 C CA  . VAL A 1 363 ? 5.47300   47.60300  78.39500  1.000 50.18729 ? 363 VAL A CA  1 
ATOM   2735 C C   . VAL A 1 363 ? 4.78100   48.92000  78.73500  1.000 54.25872 ? 363 VAL A C   1 
ATOM   2736 O O   . VAL A 1 363 ? 5.42500   49.96400  78.89700  1.000 53.06656 ? 363 VAL A O   1 
ATOM   2737 C CB  . VAL A 1 363 ? 5.74300   46.74500  79.65000  1.000 45.01101 ? 363 VAL A CB  1 
ATOM   2738 C CG1 . VAL A 1 363 ? 4.46200   46.36300  80.35200  1.000 42.57886 ? 363 VAL A CG1 1 
ATOM   2739 C CG2 . VAL A 1 363 ? 6.53400   45.49300  79.27600  1.000 48.79052 ? 363 VAL A CG2 1 
ATOM   2740 N N   . SER A 1 364 ? 3.44100   48.87800  78.81900  1.000 43.37198 ? 364 SER A N   1 
ATOM   2741 C CA  . SER A 1 364 ? 2.63200   50.03200  79.17100  1.000 45.04519 ? 364 SER A CA  1 
ATOM   2742 C C   . SER A 1 364 ? 2.74000   50.33400  80.66600  1.000 50.71349 ? 364 SER A C   1 
ATOM   2743 O O   . SER A 1 364 ? 2.97300   49.42900  81.47700  1.000 44.92562 ? 364 SER A O   1 
ATOM   2744 C CB  . SER A 1 364 ? 1.16900   49.78800  78.80900  1.000 41.57683 ? 364 SER A CB  1 
ATOM   2745 O OG  . SER A 1 364 ? 0.50900   49.05500  79.83300  1.000 40.09055 ? 364 SER A OG  1 
ATOM   2746 N N   . PRO A 1 365 ? 2.57400   51.60300  81.05500  1.000 42.86233 ? 365 PRO A N   1 
ATOM   2747 C CA  . PRO A 1 365 ? 2.59600   51.92700  82.49200  1.000 44.30292 ? 365 PRO A CA  1 
ATOM   2748 C C   . PRO A 1 365 ? 1.54600   51.17400  83.29200  1.000 44.03814 ? 365 PRO A C   1 
ATOM   2749 O O   . PRO A 1 365 ? 1.82400   50.72600  84.41300  1.000 40.63689 ? 365 PRO A O   1 
ATOM   2750 C CB  . PRO A 1 365 ? 2.35400   53.44400  82.50700  1.000 48.46911 ? 365 PRO A CB  1 
ATOM   2751 C CG  . PRO A 1 365 ? 2.81700   53.91600  81.15500  1.000 39.91825 ? 365 PRO A CG  1 
ATOM   2752 C CD  . PRO A 1 365 ? 2.48200   52.80600  80.20800  1.000 40.40401 ? 365 PRO A CD  1 
ATOM   2753 N N   . GLU A 1 366 ? 0.34400   51.00400  82.73700  1.000 46.10374 ? 366 GLU A N   1 
ATOM   2754 C CA  . GLU A 1 366 ? -0.70500  50.27600  83.44600  1.000 46.20396 ? 366 GLU A CA  1 
ATOM   2755 C C   . GLU A 1 366 ? -0.35200  48.79900  83.59100  1.000 44.26339 ? 366 GLU A C   1 
ATOM   2756 O O   . GLU A 1 366 ? -0.59500  48.19500  84.64500  1.000 41.67155 ? 366 GLU A O   1 
ATOM   2757 C CB  . GLU A 1 366 ? -2.04500  50.44400  82.72400  1.000 45.11770 ? 366 GLU A CB  1 
ATOM   2758 C CG  . GLU A 1 366 ? -2.40100  51.88400  82.37000  1.000 41.82325 ? 366 GLU A CG  1 
ATOM   2759 C CD  . GLU A 1 366 ? -1.74300  52.36500  81.07800  1.000 47.70632 ? 366 GLU A CD  1 
ATOM   2760 O OE1 . GLU A 1 366 ? -0.72500  51.76400  80.65000  1.000 40.29421 ? 366 GLU A OE1 1 
ATOM   2761 O OE2 . GLU A 1 366 ? -2.25100  53.34600  80.48800  1.000 46.59327 ? 366 GLU A OE2 1 
ATOM   2762 N N   . ALA A 1 367 ? 0.21600   48.19800  82.54200  1.000 43.61059 ? 367 ALA A N   1 
ATOM   2763 C CA  . ALA A 1 367 ? 0.66700   46.81400  82.64900  1.000 42.80708 ? 367 ALA A CA  1 
ATOM   2764 C C   . ALA A 1 367 ? 1.77600   46.68100  83.68200  1.000 41.98451 ? 367 ALA A C   1 
ATOM   2765 O O   . ALA A 1 367 ? 1.77800   45.73800  84.48400  1.000 39.15820 ? 367 ALA A O   1 
ATOM   2766 C CB  . ALA A 1 367 ? 1.12800   46.30400  81.28700  1.000 37.71920 ? 367 ALA A CB  1 
ATOM   2767 N N   . ARG A 1 368 ? 2.72400   47.62400  83.68800  1.000 42.46766 ? 368 ARG A N   1 
ATOM   2768 C CA  . ARG A 1 368 ? 3.74800   47.62700  84.72900  1.000 39.85013 ? 368 ARG A CA  1 
ATOM   2769 C C   . ARG A 1 368 ? 3.12300   47.83800  86.10400  1.000 39.87955 ? 368 ARG A C   1 
ATOM   2770 O O   . ARG A 1 368 ? 3.51300   47.18400  87.08000  1.000 39.06648 ? 368 ARG A O   1 
ATOM   2771 C CB  . ARG A 1 368 ? 4.80000   48.70200  84.44000  1.000 39.74138 ? 368 ARG A CB  1 
ATOM   2772 C CG  . ARG A 1 368 ? 5.63200   48.44800  83.18800  1.000 42.46504 ? 368 ARG A CG  1 
ATOM   2773 C CD  . ARG A 1 368 ? 6.95000   49.21500  83.22000  1.000 41.60851 ? 368 ARG A CD  1 
ATOM   2774 N NE  . ARG A 1 368 ? 6.77200   50.65100  83.03600  1.000 44.73519 ? 368 ARG A NE  1 
ATOM   2775 C CZ  . ARG A 1 368 ? 6.84300   51.26800  81.86400  1.000 46.93274 ? 368 ARG A CZ  1 
ATOM   2776 N NH1 . ARG A 1 368 ? 7.09000   50.60300  80.74700  1.000 46.35020 ? 368 ARG A NH1 1 
ATOM   2777 N NH2 . ARG A 1 368 ? 6.66400   52.58400  81.81000  1.000 50.30000 ? 368 ARG A NH2 1 
ATOM   2778 N N   . ALA A 1 369 ? 2.13800   48.73800  86.19300  1.000 41.14052 ? 369 ALA A N   1 
ATOM   2779 C CA  . ALA A 1 369 ? 1.43900   48.95900  87.45600  1.000 41.58253 ? 369 ALA A CA  1 
ATOM   2780 C C   . ALA A 1 369 ? 0.69100   47.70900  87.90800  1.000 42.81002 ? 369 ALA A C   1 
ATOM   2781 O O   . ALA A 1 369 ? 0.68700   47.37700  89.10000  1.000 40.72402 ? 369 ALA A O   1 
ATOM   2782 C CB  . ALA A 1 369 ? 0.47700   50.13700  87.32100  1.000 40.35942 ? 369 ALA A CB  1 
ATOM   2783 N N   . ALA A 1 370 ? 0.03900   47.01100  86.97400  1.000 41.74937 ? 370 ALA A N   1 
ATOM   2784 C CA  . ALA A 1 370 ? -0.63700  45.76400  87.32400  1.000 44.61063 ? 370 ALA A CA  1 
ATOM   2785 C C   . ALA A 1 370 ? 0.36100   44.72700  87.82700  1.000 47.04335 ? 370 ALA A C   1 
ATOM   2786 O O   . ALA A 1 370 ? 0.15100   44.10000  88.87400  1.000 38.86698 ? 370 ALA A O   1 
ATOM   2787 C CB  . ALA A 1 370 ? -1.40800  45.22600  86.11800  1.000 38.73009 ? 370 ALA A CB  1 
ATOM   2788 N N   . ALA A 1 371 ? 1.46500   44.54500  87.09400  1.000 43.33447 ? 371 ALA A N   1 
ATOM   2789 C CA  . ALA A 1 371 ? 2.50700   43.62700  87.54200  1.000 39.84460 ? 371 ALA A CA  1 
ATOM   2790 C C   . ALA A 1 371 ? 3.12400   44.10300  88.84900  1.000 40.16542 ? 371 ALA A C   1 
ATOM   2791 O O   . ALA A 1 371 ? 3.41100   43.29700  89.74100  1.000 35.83486 ? 371 ALA A O   1 
ATOM   2792 C CB  . ALA A 1 371 ? 3.57700   43.47700  86.46000  1.000 38.21316 ? 371 ALA A CB  1 
ATOM   2793 N N   . GLY A 1 372 ? 3.31100   45.41000  88.99100  1.000 42.61557 ? 372 GLY A N   1 
ATOM   2794 C CA  . GLY A 1 372 ? 3.96200   45.96600  90.15400  1.000 35.24116 ? 372 GLY A CA  1 
ATOM   2795 C C   . GLY A 1 372 ? 5.40100   46.37300  89.93900  1.000 33.62679 ? 372 GLY A C   1 
ATOM   2796 O O   . GLY A 1 372 ? 6.15500   46.44000  90.91500  1.000 36.09939 ? 372 GLY A O   1 
ATOM   2797 N N   . VAL A 1 373 ? 5.80300   46.63700  88.69900  1.000 29.49672 ? 373 VAL A N   1 
ATOM   2798 C CA  . VAL A 1 373 ? 7.17300   47.03000  88.37400  1.000 35.11432 ? 373 VAL A CA  1 
ATOM   2799 C C   . VAL A 1 373 ? 7.17500   48.55400  88.30400  1.000 33.20417 ? 373 VAL A C   1 
ATOM   2800 O O   . VAL A 1 373 ? 6.92100   49.15800  87.25900  1.000 34.78799 ? 373 VAL A O   1 
ATOM   2801 C CB  . VAL A 1 373 ? 7.65900   46.37900  87.07900  1.000 35.72651 ? 373 VAL A CB  1 
ATOM   2802 C CG1 . VAL A 1 373 ? 9.07800   46.82400  86.74900  1.000 30.81465 ? 373 VAL A CG1 1 
ATOM   2803 C CG2 . VAL A 1 373 ? 7.58900   44.85900  87.19600  1.000 27.21968 ? 373 VAL A CG2 1 
ATOM   2804 N N   . GLY A 1 374 ? 7.46300   49.18900  89.44300  1.000 35.52274 ? 374 GLY A N   1 
ATOM   2805 C CA  . GLY A 1 374 ? 7.41300   50.63200  89.53000  1.000 32.52437 ? 374 GLY A CA  1 
ATOM   2806 C C   . GLY A 1 374 ? 8.63300   51.31200  88.94000  1.000 31.58507 ? 374 GLY A C   1 
ATOM   2807 O O   . GLY A 1 374 ? 9.61600   50.68100  88.55200  1.000 27.37044 ? 374 GLY A O   1 
ATOM   2808 N N   . ASP A 1 375 ? 8.55500   52.64300  88.87700  1.000 32.94447 ? 375 ASP A N   1 
ATOM   2809 C CA  . ASP A 1 375 ? 9.65100   53.43800  88.34400  1.000 26.72366 ? 375 ASP A CA  1 
ATOM   2810 C C   . ASP A 1 375 ? 10.80600  53.57700  89.32400  1.000 29.37791 ? 375 ASP A C   1 
ATOM   2811 O O   . ASP A 1 375 ? 11.89700  53.99100  88.92000  1.000 29.64968 ? 375 ASP A O   1 
ATOM   2812 C CB  . ASP A 1 375 ? 9.14900   54.82500  87.94600  1.000 34.86685 ? 375 ASP A CB  1 
ATOM   2813 C CG  . ASP A 1 375 ? 8.06700   54.76700  86.89000  1.000 39.69020 ? 375 ASP A CG  1 
ATOM   2814 O OD1 . ASP A 1 375 ? 8.06400   53.80400  86.09300  1.000 38.14352 ? 375 ASP A OD1 1 
ATOM   2815 O OD2 . ASP A 1 375 ? 7.21800   55.68400  86.86000  1.000 46.15876 ? 375 ASP A OD2 1 
ATOM   2816 N N   . GLY A 1 376 ? 10.59200  53.25500  90.59500  1.000 27.47768 ? 376 GLY A N   1 
ATOM   2817 C CA  . GLY A 1 376 ? 11.66400  53.29800  91.56600  1.000 31.88878 ? 376 GLY A CA  1 
ATOM   2818 C C   . GLY A 1 376 ? 12.23200  51.92200  91.83900  1.000 28.83305 ? 376 GLY A C   1 
ATOM   2819 O O   . GLY A 1 376 ? 12.90000  51.71200  92.85400  1.000 30.13550 ? 376 GLY A O   1 
ATOM   2820 N N   . LEU A 1 377 ? 11.97400  50.97600  90.94000  1.000 26.59900 ? 377 LEU A N   1 
ATOM   2821 C CA  . LEU A 1 377 ? 12.38300  49.58900  91.13100  1.000 29.67434 ? 377 LEU A CA  1 
ATOM   2822 C C   . LEU A 1 377 ? 13.76400  49.34100  90.53600  1.000 25.53449 ? 377 LEU A C   1 
ATOM   2823 O O   . LEU A 1 377 ? 14.00700  49.64200  89.36500  1.000 24.82769 ? 377 LEU A O   1 
ATOM   2824 C CB  . LEU A 1 377 ? 11.37500  48.63500  90.49100  1.000 28.12781 ? 377 LEU A CB  1 
ATOM   2825 C CG  . LEU A 1 377 ? 11.67500  47.15800  90.75100  1.000 32.74896 ? 377 LEU A CG  1 
ATOM   2826 C CD1 . LEU A 1 377 ? 11.38200  46.82900  92.19100  1.000 31.69688 ? 377 LEU A CD1 1 
ATOM   2827 C CD2 . LEU A 1 377 ? 10.87800  46.25900  89.83000  1.000 34.42698 ? 377 LEU A CD2 1 
ATOM   2828 N N   . LEU A 1 378 ? 14.65400  48.77100  91.34200  1.000 26.17968 ? 378 LEU A N   1 
ATOM   2829 C CA  . LEU A 1 378 ? 15.95200  48.29300  90.89100  1.000 23.73323 ? 378 LEU A CA  1 
ATOM   2830 C C   . LEU A 1 378 ? 16.05100  46.79400  91.14400  1.000 29.13722 ? 378 LEU A C   1 
ATOM   2831 O O   . LEU A 1 378 ? 15.62900  46.30300  92.19700  1.000 23.14849 ? 378 LEU A O   1 
ATOM   2832 C CB  . LEU A 1 378 ? 17.09200  49.02300  91.60700  1.000 23.44139 ? 378 LEU A CB  1 
ATOM   2833 C CG  . LEU A 1 378 ? 17.25800  50.49700  91.23800  1.000 24.22872 ? 378 LEU A CG  1 
ATOM   2834 C CD1 . LEU A 1 378 ? 18.35500  51.14100  92.06400  1.000 18.78784 ? 378 LEU A CD1 1 
ATOM   2835 C CD2 . LEU A 1 378 ? 17.55200  50.62900  89.74500  1.000 22.69213 ? 378 LEU A CD2 1 
ATOM   2836 N N   . ARG A 1 379 ? 16.59800  46.06600  90.17600  1.000 26.93420 ? 379 ARG A N   1 
ATOM   2837 C CA  . ARG A 1 379 ? 16.82300  44.63500  90.31200  1.000 23.71098 ? 379 ARG A CA  1 
ATOM   2838 C C   . ARG A 1 379 ? 18.31300  44.37000  90.44500  1.000 26.08177 ? 379 ARG A C   1 
ATOM   2839 O O   . ARG A 1 379 ? 19.11000  44.86900  89.64400  1.000 27.34454 ? 379 ARG A O   1 
ATOM   2840 C CB  . ARG A 1 379 ? 16.27100  43.86100  89.11900  1.000 24.17949 ? 379 ARG A CB  1 
ATOM   2841 C CG  . ARG A 1 379 ? 16.35800  42.36100  89.32200  1.000 23.07475 ? 379 ARG A CG  1 
ATOM   2842 C CD  . ARG A 1 379 ? 16.29600  41.61600  88.01100  1.000 29.62822 ? 379 ARG A CD  1 
ATOM   2843 N NE  . ARG A 1 379 ? 17.47500  41.84900  87.18400  1.000 27.24495 ? 379 ARG A NE  1 
ATOM   2844 C CZ  . ARG A 1 379 ? 17.68200  41.27100  86.00900  1.000 27.27897 ? 379 ARG A CZ  1 
ATOM   2845 N NH1 . ARG A 1 379 ? 16.80700  40.42100  85.49500  1.000 25.31034 ? 379 ARG A NH1 1 
ATOM   2846 N NH2 . ARG A 1 379 ? 18.79600  41.54700  85.33700  1.000 27.85031 ? 379 ARG A NH2 1 
ATOM   2847 N N   . ILE A 1 380 ? 18.68500  43.58500  91.44800  1.000 20.90889 ? 380 ILE A N   1 
ATOM   2848 C CA  . ILE A 1 380 ? 20.07500  43.22200  91.68200  1.000 20.57583 ? 380 ILE A CA  1 
ATOM   2849 C C   . ILE A 1 380 ? 20.20000  41.71300  91.57700  1.000 21.11795 ? 380 ILE A C   1 
ATOM   2850 O O   . ILE A 1 380 ? 19.47100  40.97600  92.25000  1.000 20.37124 ? 380 ILE A O   1 
ATOM   2851 C CB  . ILE A 1 380 ? 20.57600  43.70700  93.05300  1.000 20.28164 ? 380 ILE A CB  1 
ATOM   2852 C CG1 . ILE A 1 380 ? 20.63900  45.22800  93.08800  1.000 21.30137 ? 380 ILE A CG1 1 
ATOM   2853 C CG2 . ILE A 1 380 ? 21.94400  43.10700  93.36700  1.000 18.75561 ? 380 ILE A CG2 1 
ATOM   2854 C CD1 . ILE A 1 380 ? 21.18900  45.76200  94.37800  1.000 23.97544 ? 380 ILE A CD1 1 
ATOM   2855 N N   . SER A 1 381 ? 21.10600  41.26000  90.71500  1.000 21.98320 ? 381 SER A N   1 
ATOM   2856 C CA  . SER A 1 381 ? 21.56200  39.87600  90.71700  1.000 19.18827 ? 381 SER A CA  1 
ATOM   2857 C C   . SER A 1 381 ? 22.80000  39.82900  91.60100  1.000 16.86202 ? 381 SER A C   1 
ATOM   2858 O O   . SER A 1 381 ? 23.85700  40.34800  91.22900  1.000 21.27643 ? 381 SER A O   1 
ATOM   2859 C CB  . SER A 1 381 ? 21.85900  39.38900  89.30200  1.000 17.71870 ? 381 SER A CB  1 
ATOM   2860 O OG  . SER A 1 381 ? 22.40600  38.07900  89.31300  1.000 20.17168 ? 381 SER A OG  1 
ATOM   2861 N N   . VAL A 1 382 ? 22.66000  39.24300  92.78300  1.000 18.43365 ? 382 VAL A N   1 
ATOM   2862 C CA  . VAL A 1 382 ? 23.70400  39.31500  93.79700  1.000 19.38312 ? 382 VAL A CA  1 
ATOM   2863 C C   . VAL A 1 382 ? 24.79600  38.31400  93.44100  1.000 17.59272 ? 382 VAL A C   1 
ATOM   2864 O O   . VAL A 1 382 ? 24.53400  37.11500  93.30200  1.000 15.23624 ? 382 VAL A O   1 
ATOM   2865 C CB  . VAL A 1 382 ? 23.13200  39.05100  95.19800  1.000 20.51846 ? 382 VAL A CB  1 
ATOM   2866 C CG1 . VAL A 1 382 ? 24.22200  39.13600  96.24200  1.000 22.06061 ? 382 VAL A CG1 1 
ATOM   2867 C CG2 . VAL A 1 382 ? 22.01900  40.04400  95.51100  1.000 20.81501 ? 382 VAL A CG2 1 
ATOM   2868 N N   . GLY A 1 383 ? 26.01900  38.80800  93.28800  1.000 19.25343 ? 383 GLY A N   1 
ATOM   2869 C CA  . GLY A 1 383 ? 27.14700  37.98900  92.90100  1.000 15.69142 ? 383 GLY A CA  1 
ATOM   2870 C C   . GLY A 1 383 ? 27.88200  37.39800  94.08700  1.000 18.58105 ? 383 GLY A C   1 
ATOM   2871 O O   . GLY A 1 383 ? 27.33900  37.23600  95.18200  1.000 19.80416 ? 383 GLY A O   1 
ATOM   2872 N N   . LEU A 1 384 ? 29.15000  37.07400  93.85300  1.000 19.86230 ? 384 LEU A N   1 
ATOM   2873 C CA  . LEU A 1 384 ? 29.96000  36.31800  94.79200  1.000 17.62342 ? 384 LEU A CA  1 
ATOM   2874 C C   . LEU A 1 384 ? 31.03200  37.16500  95.44900  1.000 17.86922 ? 384 LEU A C   1 
ATOM   2875 O O   . LEU A 1 384 ? 31.87400  36.62600  96.17400  1.000 20.95355 ? 384 LEU A O   1 
ATOM   2876 C CB  . LEU A 1 384 ? 30.61300  35.12800  94.08600  1.000 16.80938 ? 384 LEU A CB  1 
ATOM   2877 C CG  . LEU A 1 384 ? 29.63300  34.16300  93.42700  1.000 20.60717 ? 384 LEU A CG  1 
ATOM   2878 C CD1 . LEU A 1 384 ? 30.38600  33.09300  92.65500  1.000 11.43238 ? 384 LEU A CD1 1 
ATOM   2879 C CD2 . LEU A 1 384 ? 28.70500  33.55500  94.47800  1.000 19.80347 ? 384 LEU A CD2 1 
ATOM   2880 N N   . GLU A 1 385 ? 31.04500  38.46700  95.19800  1.000 16.30012 ? 385 GLU A N   1 
ATOM   2881 C CA  . GLU A 1 385 ? 32.03600  39.29300  95.85800  1.000 19.64042 ? 385 GLU A CA  1 
ATOM   2882 C C   . GLU A 1 385 ? 31.65500  39.46900  97.32700  1.000 21.82789 ? 385 GLU A C   1 
ATOM   2883 O O   . GLU A 1 385 ? 30.58400  39.04400  97.77700  1.000 19.34065 ? 385 GLU A O   1 
ATOM   2884 C CB  . GLU A 1 385 ? 32.19400  40.63000  95.12900  1.000 22.91743 ? 385 GLU A CB  1 
ATOM   2885 C CG  . GLU A 1 385 ? 30.91000  41.28600  94.70400  1.000 25.15914 ? 385 GLU A CG  1 
ATOM   2886 C CD  . GLU A 1 385 ? 30.45200  40.92200  93.29400  1.000 19.45202 ? 385 GLU A CD  1 
ATOM   2887 O OE1 . GLU A 1 385 ? 30.93400  41.52600  92.31400  1.000 16.87854 ? 385 GLU A OE1 1 
ATOM   2888 O OE2 . GLU A 1 385 ? 29.58200  40.04200  93.17100  1.000 22.01116 ? 385 GLU A OE2 1 
ATOM   2889 N N   . HIS A 1 386 ? 32.56600  40.05300  98.09800  1.000 21.85447 ? 386 HIS A N   1 
ATOM   2890 C CA  . HIS A 1 386 ? 32.32000  40.17300  99.52700  1.000 21.82910 ? 386 HIS A CA  1 
ATOM   2891 C C   . HIS A 1 386 ? 31.16100  41.12600  99.77100  1.000 26.77421 ? 386 HIS A C   1 
ATOM   2892 O O   . HIS A 1 386 ? 31.13400  42.24000  99.23400  1.000 25.65497 ? 386 HIS A O   1 
ATOM   2893 C CB  . HIS A 1 386 ? 33.56200  40.65900  100.26400 1.000 19.92363 ? 386 HIS A CB  1 
ATOM   2894 C CG  . HIS A 1 386 ? 33.56500  40.29600  101.71800 1.000 28.22385 ? 386 HIS A CG  1 
ATOM   2895 N ND1 . HIS A 1 386 ? 32.74700  40.91300  102.64000 1.000 28.49998 ? 386 HIS A ND1 1 
ATOM   2896 C CD2 . HIS A 1 386 ? 34.26400  39.35900  102.40300 1.000 23.69120 ? 386 HIS A CD2 1 
ATOM   2897 C CE1 . HIS A 1 386 ? 32.95300  40.38100  103.83200 1.000 31.04441 ? 386 HIS A CE1 1 
ATOM   2898 N NE2 . HIS A 1 386 ? 33.86900  39.43700  103.71600 1.000 23.81588 ? 386 HIS A NE2 1 
ATOM   2899 N N   . ALA A 1 387 ? 30.20700  40.68000  100.59400 1.000 22.55356 ? 387 ALA A N   1 
ATOM   2900 C CA  . ALA A 1 387 ? 29.02100  41.48100  100.87300 1.000 27.03619 ? 387 ALA A CA  1 
ATOM   2901 C C   . ALA A 1 387 ? 29.38400  42.85500  101.42200 1.000 28.59842 ? 387 ALA A C   1 
ATOM   2902 O O   . ALA A 1 387 ? 28.71600  43.84500  101.10200 1.000 25.84098 ? 387 ALA A O   1 
ATOM   2903 C CB  . ALA A 1 387 ? 28.10600  40.73500  101.84600 1.000 25.59275 ? 387 ALA A CB  1 
ATOM   2904 N N   . ASP A 1 388 ? 30.44700  42.94500  102.22500 1.000 28.90146 ? 388 ASP A N   1 
ATOM   2905 C CA  . ASP A 1 388 ? 30.87300  44.24500  102.73200 1.000 27.26814 ? 388 ASP A CA  1 
ATOM   2906 C C   . ASP A 1 388 ? 31.17800  45.19700  101.58600 1.000 27.92462 ? 388 ASP A C   1 
ATOM   2907 O O   . ASP A 1 388 ? 30.74600  46.35400  101.59500 1.000 26.94565 ? 388 ASP A O   1 
ATOM   2908 C CB  . ASP A 1 388 ? 32.10000  44.09500  103.63300 1.000 32.85070 ? 388 ASP A CB  1 
ATOM   2909 C CG  . ASP A 1 388 ? 31.77800  43.44900  104.97300 1.000 36.51879 ? 388 ASP A CG  1 
ATOM   2910 O OD1 . ASP A 1 388 ? 30.60500  43.08600  105.21400 1.000 32.16284 ? 388 ASP A OD1 1 
ATOM   2911 O OD2 . ASP A 1 388 ? 32.71700  43.30600  105.78600 1.000 37.96396 ? 388 ASP A OD2 1 
ATOM   2912 N N   . ASP A 1 389 ? 31.91300  44.72000  100.57800 1.000 28.11482 ? 389 ASP A N   1 
ATOM   2913 C CA  . ASP A 1 389 ? 32.20800  45.56600  99.42500  1.000 26.32774 ? 389 ASP A CA  1 
ATOM   2914 C C   . ASP A 1 389 ? 30.93600  45.92500  98.67000  1.000 26.59079 ? 389 ASP A C   1 
ATOM   2915 O O   . ASP A 1 389 ? 30.77000  47.06500  98.22300  1.000 26.24226 ? 389 ASP A O   1 
ATOM   2916 C CB  . ASP A 1 389 ? 33.20700  44.87300  98.50100  1.000 24.54722 ? 389 ASP A CB  1 
ATOM   2917 C CG  . ASP A 1 389 ? 34.56100  44.67800  99.15200  1.000 25.95458 ? 389 ASP A CG  1 
ATOM   2918 O OD1 . ASP A 1 389 ? 35.06100  45.62600  99.79100  1.000 29.85350 ? 389 ASP A OD1 1 
ATOM   2919 O OD2 . ASP A 1 389 ? 35.11900  43.57100  99.03500  1.000 25.96221 ? 389 ASP A OD2 1 
ATOM   2920 N N   . LEU A 1 390 ? 30.02600  44.96300  98.51100  1.000 22.35647 ? 390 LEU A N   1 
ATOM   2921 C CA  . LEU A 1 390 ? 28.75000  45.26800  97.87900  1.000 22.85037 ? 390 LEU A CA  1 
ATOM   2922 C C   . LEU A 1 390 ? 27.95500  46.27500  98.70300  1.000 27.27330 ? 390 LEU A C   1 
ATOM   2923 O O   . LEU A 1 390 ? 27.35600  47.20600  98.14900  1.000 26.94173 ? 390 LEU A O   1 
ATOM   2924 C CB  . LEU A 1 390 ? 27.95500  43.98100  97.67400  1.000 23.04855 ? 390 LEU A CB  1 
ATOM   2925 C CG  . LEU A 1 390 ? 28.53200  43.00400  96.64600  1.000 22.94078 ? 390 LEU A CG  1 
ATOM   2926 C CD1 . LEU A 1 390 ? 27.71100  41.72900  96.61500  1.000 22.10207 ? 390 LEU A CD1 1 
ATOM   2927 C CD2 . LEU A 1 390 ? 28.57900  43.64600  95.26300  1.000 17.80321 ? 390 LEU A CD2 1 
ATOM   2928 N N   A ARG A 1 391 ? 27.93300  46.10300  100.02900 0.520 26.33396 ? 391 ARG A N   1 
ATOM   2929 N N   B ARG A 1 391 ? 27.94500  46.10500  100.02700 0.480 26.34431 ? 391 ARG A N   1 
ATOM   2930 C CA  A ARG A 1 391 ? 27.20300  47.03000  100.89100 0.520 26.21670 ? 391 ARG A CA  1 
ATOM   2931 C CA  B ARG A 1 391 ? 27.20500  47.01100  100.89900 0.480 26.23355 ? 391 ARG A CA  1 
ATOM   2932 C C   A ARG A 1 391 ? 27.76200  48.44200  100.77200 0.520 27.47591 ? 391 ARG A C   1 
ATOM   2933 C C   B ARG A 1 391 ? 27.75900  48.43200  100.82300 0.480 27.46921 ? 391 ARG A C   1 
ATOM   2934 O O   A ARG A 1 391 ? 27.01200  49.40900  100.59700 0.520 26.82018 ? 391 ARG A O   1 
ATOM   2935 O O   B ARG A 1 391 ? 26.99600  49.39900  100.71700 0.480 26.87642 ? 391 ARG A O   1 
ATOM   2936 C CB  A ARG A 1 391 ? 27.25900  46.55500  102.34600 0.520 26.09567 ? 391 ARG A CB  1 
ATOM   2937 C CB  B ARG A 1 391 ? 27.24300  46.47500  102.33300 0.480 26.15892 ? 391 ARG A CB  1 
ATOM   2938 C CG  A ARG A 1 391 ? 26.50100  47.45600  103.32100 0.520 29.39378 ? 391 ARG A CG  1 
ATOM   2939 C CG  B ARG A 1 391 ? 26.40700  47.24000  103.34500 0.480 29.44670 ? 391 ARG A CG  1 
ATOM   2940 C CD  A ARG A 1 391 ? 26.74900  47.08700  104.78600 0.520 26.25606 ? 391 ARG A CD  1 
ATOM   2941 C CD  B ARG A 1 391 ? 25.56600  46.30400  104.23200 0.480 29.18008 ? 391 ARG A CD  1 
ATOM   2942 N NE  A ARG A 1 391 ? 28.10100  47.43000  105.21500 0.520 27.86082 ? 391 ARG A NE  1 
ATOM   2943 N NE  B ARG A 1 391 ? 26.16700  44.98900  104.44700 0.480 31.71155 ? 391 ARG A NE  1 
ATOM   2944 C CZ  A ARG A 1 391 ? 29.06200  46.55000  105.45800 0.520 28.41276 ? 391 ARG A CZ  1 
ATOM   2945 C CZ  B ARG A 1 391 ? 25.68100  43.84900  103.97000 0.480 26.70354 ? 391 ARG A CZ  1 
ATOM   2946 N NH1 A ARG A 1 391 ? 28.84600  45.24800  105.37400 0.520 30.90909 ? 391 ARG A NH1 1 
ATOM   2947 N NH1 B ARG A 1 391 ? 24.57900  43.81700  103.24000 0.480 22.05521 ? 391 ARG A NH1 1 
ATOM   2948 N NH2 A ARG A 1 391 ? 30.27100  46.98800  105.79700 0.520 31.77156 ? 391 ARG A NH2 1 
ATOM   2949 N NH2 B ARG A 1 391 ? 26.31200  42.71100  104.24000 0.480 28.89645 ? 391 ARG A NH2 1 
ATOM   2950 N N   . GLU A 1 392 ? 29.08700  48.57500  100.84400 1.000 26.37335 ? 392 GLU A N   1 
ATOM   2951 C CA  . GLU A 1 392 ? 29.69500  49.89900  100.79300 1.000 27.02995 ? 392 GLU A CA  1 
ATOM   2952 C C   . GLU A 1 392 ? 29.45700  50.57900  99.45300  1.000 28.19401 ? 392 GLU A C   1 
ATOM   2953 O O   . GLU A 1 392 ? 29.30600  51.80600  99.40100  1.000 29.87427 ? 392 GLU A O   1 
ATOM   2954 C CB  . GLU A 1 392 ? 31.18800  49.79800  101.09100 1.000 27.76738 ? 392 GLU A CB  1 
ATOM   2955 C CG  . GLU A 1 392 ? 31.48800  49.32300  102.50700 1.000 30.65161 ? 392 GLU A CG  1 
ATOM   2956 C CD  . GLU A 1 392 ? 32.97200  49.13600  102.76800 1.000 42.09156 ? 392 GLU A CD  1 
ATOM   2957 O OE1 . GLU A 1 392 ? 33.79300  49.58400  101.93300 1.000 41.61528 ? 392 GLU A OE1 1 
ATOM   2958 O OE2 . GLU A 1 392 ? 33.31400  48.53500  103.80900 1.000 38.81646 ? 392 GLU A OE2 1 
ATOM   2959 N N   . ASP A 1 393 ? 29.43500  49.81100  98.36200  1.000 27.77801 ? 393 ASP A N   1 
ATOM   2960 C CA  . ASP A 1 393 ? 29.13500  50.40400  97.06400  1.000 26.50708 ? 393 ASP A CA  1 
ATOM   2961 C C   . ASP A 1 393 ? 27.69700  50.89800  97.00900  1.000 28.35614 ? 393 ASP A C   1 
ATOM   2962 O O   . ASP A 1 393 ? 27.42700  51.98300  96.48100  1.000 29.51924 ? 393 ASP A O   1 
ATOM   2963 C CB  . ASP A 1 393 ? 29.39900  49.40000  95.94200  1.000 24.45603 ? 393 ASP A CB  1 
ATOM   2964 C CG  . ASP A 1 393 ? 29.48200  50.06500  94.58000  1.000 28.04068 ? 393 ASP A CG  1 
ATOM   2965 O OD1 . ASP A 1 393 ? 30.05700  51.17200  94.50500  1.000 24.44541 ? 393 ASP A OD1 1 
ATOM   2966 O OD2 . ASP A 1 393 ? 28.99000  49.48000  93.58700  1.000 31.24370 ? 393 ASP A OD2 1 
ATOM   2967 N N   . MET A 1 394 ? 26.75900  50.11400  97.54700  1.000 23.22626 ? 394 MET A N   1 
ATOM   2968 C CA  . MET A 1 394 ? 25.36700  50.54700  97.56700  1.000 30.29321 ? 394 MET A CA  1 
ATOM   2969 C C   . MET A 1 394 ? 25.17200  51.77200  98.45400  1.000 30.93891 ? 394 MET A C   1 
ATOM   2970 O O   . MET A 1 394 ? 24.29000  52.59500  98.18500  1.000 29.15776 ? 394 MET A O   1 
ATOM   2971 C CB  . MET A 1 394 ? 24.47000  49.39700  98.01500  1.000 27.76771 ? 394 MET A CB  1 
ATOM   2972 C CG  . MET A 1 394 ? 24.46500  48.23100  97.03600  1.000 27.92118 ? 394 MET A CG  1 
ATOM   2973 S SD  . MET A 1 394 ? 23.41300  46.85500  97.53500  1.000 32.61046 ? 394 MET A SD  1 
ATOM   2974 C CE  . MET A 1 394 ? 21.79800  47.59600  97.36000  1.000 35.62270 ? 394 MET A CE  1 
ATOM   2975 N N   . GLU A 1 395 ? 25.98800  51.91600  99.50200  1.000 27.13090 ? 395 GLU A N   1 
ATOM   2976 C CA  . GLU A 1 395 ? 25.95000  53.13000  100.30900 1.000 29.34126 ? 395 GLU A CA  1 
ATOM   2977 C C   . GLU A 1 395 ? 26.37700  54.35500  99.50300  1.000 32.58597 ? 395 GLU A C   1 
ATOM   2978 O O   . GLU A 1 395 ? 25.92700  55.47100  99.78900  1.000 34.80645 ? 395 GLU A O   1 
ATOM   2979 C CB  . GLU A 1 395 ? 26.82600  52.95900  101.55400 1.000 27.64679 ? 395 GLU A CB  1 
ATOM   2980 C CG  . GLU A 1 395 ? 26.26000  51.96600  102.56300 1.000 30.66509 ? 395 GLU A CG  1 
ATOM   2981 C CD  . GLU A 1 395 ? 27.22800  51.64000  103.68900 1.000 36.85708 ? 395 GLU A CD  1 
ATOM   2982 O OE1 . GLU A 1 395 ? 28.43100  51.95500  103.55500 1.000 35.57556 ? 395 GLU A OE1 1 
ATOM   2983 O OE2 . GLU A 1 395 ? 26.78400  51.06600  104.70800 1.000 32.39741 ? 395 GLU A OE2 1 
ATOM   2984 N N   . ARG A 1 396 ? 27.24000  54.17500  98.49800  1.000 31.55869 ? 396 ARG A N   1 
ATOM   2985 C CA  . ARG A 1 396 ? 27.51700  55.27300  97.57600  1.000 32.78094 ? 396 ARG A CA  1 
ATOM   2986 C C   . ARG A 1 396 ? 26.25700  55.67500  96.82100  1.000 31.88536 ? 396 ARG A C   1 
ATOM   2987 O O   . ARG A 1 396 ? 26.00000  56.86600  96.61400  1.000 39.39868 ? 396 ARG A O   1 
ATOM   2988 C CB  . ARG A 1 396 ? 28.62500  54.88800  96.59300  1.000 30.76384 ? 396 ARG A CB  1 
ATOM   2989 C CG  . ARG A 1 396 ? 29.95400  54.57800  97.25000  1.000 34.62098 ? 396 ARG A CG  1 
ATOM   2990 C CD  . ARG A 1 396 ? 31.05300  54.29900  96.22400  1.000 35.48158 ? 396 ARG A CD  1 
ATOM   2991 N NE  . ARG A 1 396 ? 32.29700  53.93900  96.89100  1.000 39.39125 ? 396 ARG A NE  1 
ATOM   2992 C CZ  . ARG A 1 396 ? 32.72600  52.69600  97.06400  1.000 34.92696 ? 396 ARG A CZ  1 
ATOM   2993 N NH1 . ARG A 1 396 ? 32.09600  51.66500  96.52400  1.000 29.79580 ? 396 ARG A NH1 1 
ATOM   2994 N NH2 . ARG A 1 396 ? 33.81000  52.48100  97.80400  1.000 34.25933 ? 396 ARG A NH2 1 
ATOM   2995 N N   . GLY A 1 397 ? 25.45900  54.69400  96.40100  1.000 29.28730 ? 397 GLY A N   1 
ATOM   2996 C CA  . GLY A 1 397 ? 24.21300  55.01100  95.72500  1.000 33.66183 ? 397 GLY A CA  1 
ATOM   2997 C C   . GLY A 1 397 ? 23.24000  55.76100  96.61300  1.000 31.28383 ? 397 GLY A C   1 
ATOM   2998 O O   . GLY A 1 397 ? 22.55700  56.68300  96.16300  1.000 33.70605 ? 397 GLY A O   1 
ATOM   2999 N N   . PHE A 1 398 ? 23.15300  55.36700  97.88500  1.000 30.89188 ? 398 PHE A N   1 
ATOM   3000 C CA  . PHE A 1 398 ? 22.26300  56.05900  98.81200  1.000 36.04316 ? 398 PHE A CA  1 
ATOM   3001 C C   . PHE A 1 398 ? 22.76700  57.45700  99.14000  1.000 35.24606 ? 398 PHE A C   1 
ATOM   3002 O O   . PHE A 1 398 ? 21.96200  58.37600  99.32500  1.000 36.45383 ? 398 PHE A O   1 
ATOM   3003 C CB  . PHE A 1 398 ? 22.09800  55.23700  100.08700 1.000 31.14113 ? 398 PHE A CB  1 
ATOM   3004 C CG  . PHE A 1 398 ? 21.22300  54.03800  99.91300  1.000 31.90979 ? 398 PHE A CG  1 
ATOM   3005 C CD1 . PHE A 1 398 ? 19.98900  54.15300  99.29400  1.000 30.34537 ? 398 PHE A CD1 1 
ATOM   3006 C CD2 . PHE A 1 398 ? 21.63900  52.78900  100.34800 1.000 29.39620 ? 398 PHE A CD2 1 
ATOM   3007 C CE1 . PHE A 1 398 ? 19.17800  53.05100  99.12700  1.000 30.21326 ? 398 PHE A CE1 1 
ATOM   3008 C CE2 . PHE A 1 398 ? 20.82900  51.68000  100.18300 1.000 26.12890 ? 398 PHE A CE2 1 
ATOM   3009 C CZ  . PHE A 1 398 ? 19.59800  51.81000  99.57400  1.000 27.14121 ? 398 PHE A CZ  1 
ATOM   3010 N N   . ALA A 1 399 ? 24.08700  57.63800  99.21800  1.000 36.36199 ? 399 ALA A N   1 
ATOM   3011 C CA  . ALA A 1 399 ? 24.63300  58.96900  99.44900  1.000 34.29421 ? 399 ALA A CA  1 
ATOM   3012 C C   . ALA A 1 399 ? 24.27000  59.92000  98.31800  1.000 35.61505 ? 399 ALA A C   1 
ATOM   3013 O O   . ALA A 1 399 ? 24.13000  61.12600  98.54200  1.000 37.70778 ? 399 ALA A O   1 
ATOM   3014 C CB  . ALA A 1 399 ? 26.15000  58.89100  99.61300  1.000 30.53018 ? 399 ALA A CB  1 
ATOM   3015 N N   . ALA A 1 400 ? 24.10100  59.39500  97.10300  1.000 34.29675 ? 400 ALA A N   1 
ATOM   3016 C CA  . ALA A 1 400 ? 23.75900  60.21900  95.95400  1.000 34.00925 ? 400 ALA A CA  1 
ATOM   3017 C C   . ALA A 1 400 ? 22.34300  60.77200  96.02000  1.000 38.24770 ? 400 ALA A C   1 
ATOM   3018 O O   . ALA A 1 400 ? 22.01300  61.67200  95.24100  1.000 40.48010 ? 400 ALA A O   1 
ATOM   3019 C CB  . ALA A 1 400 ? 23.93800  59.41500  94.66700  1.000 36.39311 ? 400 ALA A CB  1 
ATOM   3020 N N   . LEU A 1 401 ? 21.50200  60.25000  96.90900  1.000 43.12559 ? 401 LEU A N   1 
ATOM   3021 C CA  . LEU A 1 401 ? 20.14200  60.74800  97.07300  1.000 40.72409 ? 401 LEU A CA  1 
ATOM   3022 C C   . LEU A 1 401 ? 20.06100  61.94300  98.01300  1.000 45.17447 ? 401 LEU A C   1 
ATOM   3023 O O   . LEU A 1 401 ? 18.97600  62.51400  98.17100  1.000 53.55449 ? 401 LEU A O   1 
ATOM   3024 C CB  . LEU A 1 401 ? 19.23500  59.62700  97.58200  1.000 37.31189 ? 401 LEU A CB  1 
ATOM   3025 C CG  . LEU A 1 401 ? 19.28500  58.34700  96.75000  1.000 32.31996 ? 401 LEU A CG  1 
ATOM   3026 C CD1 . LEU A 1 401 ? 18.29400  57.31900  97.27400  1.000 27.54252 ? 401 LEU A CD1 1 
ATOM   3027 C CD2 . LEU A 1 401 ? 19.02500  58.66800  95.28900  1.000 30.13994 ? 401 LEU A CD2 1 
ATOM   3028 N N   . VAL A 1 402 ? 21.17000  62.33200  98.63300  1.000 44.15522 ? 402 VAL A N   1 
ATOM   3029 C CA  . VAL A 1 402 ? 21.18100  63.44100  99.57400  1.000 48.38771 ? 402 VAL A CA  1 
ATOM   3030 C C   . VAL A 1 402 ? 21.66600  64.71000  98.88200  1.000 52.82138 ? 402 VAL A C   1 
ATOM   3031 O O   . VAL A 1 402 ? 21.94800  64.70800  97.68100  1.000 56.38546 ? 402 VAL A O   1 
ATOM   3032 C CB  . VAL A 1 402 ? 22.05300  63.11600  100.79900 1.000 50.84662 ? 402 VAL A CB  1 
ATOM   3033 C CG1 . VAL A 1 402 ? 21.91000  64.20100  101.85400 1.000 60.36860 ? 402 VAL A CG1 1 
ATOM   3034 C CG2 . VAL A 1 402 ? 21.67800  61.75900  101.37300 1.000 45.72496 ? 402 VAL A CG2 1 
ATOM   3035 N N   . ASP B 1 9   ? 35.65600  54.79500  50.79500  1.000 62.64013 ? 9   ASP B N   1 
ATOM   3036 C CA  . ASP B 1 9   ? 35.51200  54.89400  49.34600  1.000 62.05873 ? 9   ASP B CA  1 
ATOM   3037 C C   . ASP B 1 9   ? 36.39400  53.87000  48.63000  1.000 58.99800 ? 9   ASP B C   1 
ATOM   3038 O O   . ASP B 1 9   ? 35.93800  53.15800  47.73200  1.000 54.38596 ? 9   ASP B O   1 
ATOM   3039 C CB  . ASP B 1 9   ? 35.85300  56.31300  48.86900  1.000 67.41043 ? 9   ASP B CB  1 
ATOM   3040 C CG  . ASP B 1 9   ? 36.79700  57.04600  49.82000  1.000 71.69598 ? 9   ASP B CG  1 
ATOM   3041 O OD1 . ASP B 1 9   ? 36.46600  57.16500  51.02100  1.000 67.62912 ? 9   ASP B OD1 1 
ATOM   3042 O OD2 . ASP B 1 9   ? 37.87100  57.50100  49.36400  1.000 68.88681 ? 9   ASP B OD2 1 
ATOM   3043 N N   . TRP B 1 10  ? 37.66000  53.80600  49.05000  1.000 58.62620 ? 10  TRP B N   1 
ATOM   3044 C CA  . TRP B 1 10  ? 38.63100  52.92800  48.40200  1.000 54.16397 ? 10  TRP B CA  1 
ATOM   3045 C C   . TRP B 1 10  ? 38.24000  51.46100  48.53500  1.000 47.28259 ? 10  TRP B C   1 
ATOM   3046 O O   . TRP B 1 10  ? 38.47100  50.66500  47.61600  1.000 43.35065 ? 10  TRP B O   1 
ATOM   3047 C CB  . TRP B 1 10  ? 40.01700  53.16100  49.00500  1.000 50.10384 ? 10  TRP B CB  1 
ATOM   3048 C CG  . TRP B 1 10  ? 40.06400  52.89100  50.48400  1.000 44.66732 ? 10  TRP B CG  1 
ATOM   3049 C CD1 . TRP B 1 10  ? 39.58600  53.69400  51.48000  1.000 41.75207 ? 10  TRP B CD1 1 
ATOM   3050 C CD2 . TRP B 1 10  ? 40.61900  51.73600  51.13000  1.000 39.59659 ? 10  TRP B CD2 1 
ATOM   3051 N NE1 . TRP B 1 10  ? 39.80900  53.11000  52.70700  1.000 46.21045 ? 10  TRP B NE1 1 
ATOM   3052 C CE2 . TRP B 1 10  ? 40.44100  51.90800  52.51900  1.000 42.12361 ? 10  TRP B CE2 1 
ATOM   3053 C CE3 . TRP B 1 10  ? 41.25100  50.57600  50.66900  1.000 36.94529 ? 10  TRP B CE3 1 
ATOM   3054 C CZ2 . TRP B 1 10  ? 40.87000  50.96000  53.45300  1.000 38.41611 ? 10  TRP B CZ2 1 
ATOM   3055 C CZ3 . TRP B 1 10  ? 41.67400  49.63300  51.59600  1.000 36.45084 ? 10  TRP B CZ3 1 
ATOM   3056 C CH2 . TRP B 1 10  ? 41.48100  49.83200  52.97300  1.000 35.61804 ? 10  TRP B CH2 1 
ATOM   3057 N N   . ALA B 1 11  ? 37.65000  51.08500  49.67300  1.000 45.91863 ? 11  ALA B N   1 
ATOM   3058 C CA  . ALA B 1 11  ? 37.36900  49.68100  49.94900  1.000 45.16171 ? 11  ALA B CA  1 
ATOM   3059 C C   . ALA B 1 11  ? 36.34400  49.08200  48.99500  1.000 44.98103 ? 11  ALA B C   1 
ATOM   3060 O O   . ALA B 1 11  ? 36.23700  47.85400  48.91600  1.000 45.39353 ? 11  ALA B O   1 
ATOM   3061 C CB  . ALA B 1 11  ? 36.89200  49.51900  51.39300  1.000 43.14111 ? 11  ALA B CB  1 
ATOM   3062 N N   . ASP B 1 12  ? 35.59500  49.91300  48.26900  1.000 48.58560 ? 12  ASP B N   1 
ATOM   3063 C CA  . ASP B 1 12  ? 34.56600  49.39600  47.37300  1.000 49.52115 ? 12  ASP B CA  1 
ATOM   3064 C C   . ASP B 1 12  ? 35.15600  48.57400  46.23300  1.000 48.33479 ? 12  ASP B C   1 
ATOM   3065 O O   . ASP B 1 12  ? 34.51600  47.62700  45.76100  1.000 51.02906 ? 12  ASP B O   1 
ATOM   3066 C CB  . ASP B 1 12  ? 33.73200  50.55000  46.81500  1.000 56.47058 ? 12  ASP B CB  1 
ATOM   3067 C CG  . ASP B 1 12  ? 32.98400  51.30700  47.89600  1.000 58.19810 ? 12  ASP B CG  1 
ATOM   3068 O OD1 . ASP B 1 12  ? 33.04800  50.89100  49.07300  1.000 57.38401 ? 12  ASP B OD1 1 
ATOM   3069 O OD2 . ASP B 1 12  ? 32.33400  52.32100  47.56700  1.000 67.64434 ? 12  ASP B OD2 1 
ATOM   3070 N N   . ARG B 1 13  ? 36.36300  48.90700  45.78100  1.000 41.52091 ? 13  ARG B N   1 
ATOM   3071 C CA  . ARG B 1 13  ? 36.95700  48.24200  44.63100  1.000 40.37060 ? 13  ARG B CA  1 
ATOM   3072 C C   . ARG B 1 13  ? 37.80500  47.03200  45.01400  1.000 35.62482 ? 13  ARG B C   1 
ATOM   3073 O O   . ARG B 1 13  ? 38.44600  46.44000  44.13900  1.000 34.11500 ? 13  ARG B O   1 
ATOM   3074 C CB  . ARG B 1 13  ? 37.79000  49.23900  43.81900  1.000 46.90724 ? 13  ARG B CB  1 
ATOM   3075 C CG  . ARG B 1 13  ? 39.17700  49.53100  44.36800  1.000 47.47189 ? 13  ARG B CG  1 
ATOM   3076 C CD  . ARG B 1 13  ? 39.88100  50.59600  43.52000  1.000 53.73371 ? 13  ARG B CD  1 
ATOM   3077 N NE  . ARG B 1 13  ? 39.24500  51.90300  43.65500  1.000 60.46698 ? 13  ARG B NE  1 
ATOM   3078 C CZ  . ARG B 1 13  ? 39.74100  52.91400  44.35800  1.000 61.64387 ? 13  ARG B CZ  1 
ATOM   3079 N NH1 . ARG B 1 13  ? 40.92000  52.83100  44.95600  1.000 53.93872 ? 13  ARG B NH1 1 
ATOM   3080 N NH2 . ARG B 1 13  ? 39.03600  54.03900  44.46400  1.000 65.28521 ? 13  ARG B NH2 1 
ATOM   3081 N N   . LEU B 1 14  ? 37.81600  46.64800  46.28800  1.000 34.72445 ? 14  LEU B N   1 
ATOM   3082 C CA  . LEU B 1 14  ? 38.61300  45.50900  46.72200  1.000 30.98198 ? 14  LEU B CA  1 
ATOM   3083 C C   . LEU B 1 14  ? 38.07500  44.21100  46.13000  1.000 26.89476 ? 14  LEU B C   1 
ATOM   3084 O O   . LEU B 1 14  ? 36.86300  44.00100  46.05200  1.000 28.58967 ? 14  LEU B O   1 
ATOM   3085 C CB  . LEU B 1 14  ? 38.62600  45.42100  48.24700  1.000 27.84945 ? 14  LEU B CB  1 
ATOM   3086 C CG  . LEU B 1 14  ? 39.22400  46.61300  48.99800  1.000 30.84351 ? 14  LEU B CG  1 
ATOM   3087 C CD1 . LEU B 1 14  ? 39.07500  46.43200  50.49900  1.000 23.54406 ? 14  LEU B CD1 1 
ATOM   3088 C CD2 . LEU B 1 14  ? 40.68600  46.79900  48.62300  1.000 28.86296 ? 14  LEU B CD2 1 
ATOM   3089 N N   . ARG B 1 15  ? 38.99000  43.34100  45.71200  1.000 25.41137 ? 15  ARG B N   1 
ATOM   3090 C CA  . ARG B 1 15  ? 38.64700  42.04300  45.15000  1.000 25.20920 ? 15  ARG B CA  1 
ATOM   3091 C C   . ARG B 1 15  ? 38.22000  41.07200  46.25000  1.000 24.12565 ? 15  ARG B C   1 
ATOM   3092 O O   . ARG B 1 15  ? 38.57700  41.24900  47.41700  1.000 22.22521 ? 15  ARG B O   1 
ATOM   3093 C CB  . ARG B 1 15  ? 39.83700  41.46800  44.38300  1.000 25.80158 ? 15  ARG B CB  1 
ATOM   3094 C CG  . ARG B 1 15  ? 40.06300  42.06600  43.00400  1.000 27.65850 ? 15  ARG B CG  1 
ATOM   3095 C CD  . ARG B 1 15  ? 40.73500  43.41700  43.10700  1.000 30.28422 ? 15  ARG B CD  1 
ATOM   3096 N NE  . ARG B 1 15  ? 41.05400  43.98600  41.80600  1.000 38.12781 ? 15  ARG B NE  1 
ATOM   3097 C CZ  . ARG B 1 15  ? 41.43700  45.24100  41.62200  1.000 40.17126 ? 15  ARG B CZ  1 
ATOM   3098 N NH1 . ARG B 1 15  ? 41.51900  46.09200  42.63200  1.000 37.62430 ? 15  ARG B NH1 1 
ATOM   3099 N NH2 . ARG B 1 15  ? 41.74400  45.65300  40.39500  1.000 48.45545 ? 15  ARG B NH2 1 
ATOM   3100 N N   . PRO B 1 16  ? 37.47100  40.01900  45.89600  1.000 24.30851 ? 16  PRO B N   1 
ATOM   3101 C CA  . PRO B 1 16  ? 36.97600  39.09000  46.93000  1.000 25.76206 ? 16  PRO B CA  1 
ATOM   3102 C C   . PRO B 1 16  ? 38.05600  38.50600  47.83000  1.000 23.07196 ? 16  PRO B C   1 
ATOM   3103 O O   . PRO B 1 16  ? 37.82400  38.39700  49.04000  1.000 23.65665 ? 16  PRO B O   1 
ATOM   3104 C CB  . PRO B 1 16  ? 36.28300  38.00100  46.10100  1.000 26.30121 ? 16  PRO B CB  1 
ATOM   3105 C CG  . PRO B 1 16  ? 35.80900  38.72000  44.89000  1.000 27.55590 ? 16  PRO B CG  1 
ATOM   3106 C CD  . PRO B 1 16  ? 36.87900  39.73400  44.57600  1.000 25.87816 ? 16  PRO B CD  1 
ATOM   3107 N N   . GLU B 1 17  ? 39.22800  38.14900  47.29000  1.000 19.55810 ? 17  GLU B N   1 
ATOM   3108 C CA  . GLU B 1 17  ? 40.29500  37.60400  48.12900  1.000 20.59918 ? 17  GLU B CA  1 
ATOM   3109 C C   . GLU B 1 17  ? 40.66400  38.57400  49.24300  1.000 22.61175 ? 17  GLU B C   1 
ATOM   3110 O O   . GLU B 1 17  ? 40.86300  38.16700  50.39500  1.000 20.15156 ? 17  GLU B O   1 
ATOM   3111 C CB  . GLU B 1 17  ? 41.53900  37.29200  47.29000  1.000 25.04314 ? 17  GLU B CB  1 
ATOM   3112 C CG  . GLU B 1 17  ? 41.42200  36.10500  46.34100  1.000 26.78450 ? 17  GLU B CG  1 
ATOM   3113 C CD  . GLU B 1 17  ? 40.86000  36.48900  44.98200  1.000 32.00589 ? 17  GLU B CD  1 
ATOM   3114 O OE1 . GLU B 1 17  ? 40.39600  37.63900  44.83100  1.000 26.92084 ? 17  GLU B OE1 1 
ATOM   3115 O OE2 . GLU B 1 17  ? 40.88600  35.63800  44.06200  1.000 36.73819 ? 17  GLU B OE2 1 
ATOM   3116 N N   . THR B 1 18  ? 40.77400  39.86000  48.91000  1.000 22.64470 ? 18  THR B N   1 
ATOM   3117 C CA  . THR B 1 18  ? 41.10900  40.87100  49.90700  1.000 20.90637 ? 18  THR B CA  1 
ATOM   3118 C C   . THR B 1 18  ? 39.96900  41.07000  50.89600  1.000 21.80757 ? 18  THR B C   1 
ATOM   3119 O O   . THR B 1 18  ? 40.20300  41.21500  52.10400  1.000 21.90785 ? 18  THR B O   1 
ATOM   3120 C CB  . THR B 1 18  ? 41.45300  42.18200  49.20400  1.000 21.82814 ? 18  THR B CB  1 
ATOM   3121 O OG1 . THR B 1 18  ? 42.51400  41.94800  48.27000  1.000 20.20860 ? 18  THR B OG1 1 
ATOM   3122 C CG2 . THR B 1 18  ? 41.88500  43.24200  50.20600  1.000 17.99630 ? 18  THR B CG2 1 
ATOM   3123 N N   . ILE B 1 19  ? 38.72900  41.06400  50.40100  1.000 19.06066 ? 19  ILE B N   1 
ATOM   3124 C CA  . ILE B 1 19  ? 37.56400  41.24300  51.26400  1.000 22.49663 ? 19  ILE B CA  1 
ATOM   3125 C C   . ILE B 1 19  ? 37.49900  40.13800  52.31200  1.000 21.23642 ? 19  ILE B C   1 
ATOM   3126 O O   . ILE B 1 19  ? 37.22800  40.39300  53.49400  1.000 20.85929 ? 19  ILE B O   1 
ATOM   3127 C CB  . ILE B 1 19  ? 36.28000  41.28700  50.41300  1.000 20.16083 ? 19  ILE B CB  1 
ATOM   3128 C CG1 . ILE B 1 19  ? 36.22200  42.57700  49.59800  1.000 25.11052 ? 19  ILE B CG1 1 
ATOM   3129 C CG2 . ILE B 1 19  ? 35.05800  41.15400  51.28600  1.000 20.89043 ? 19  ILE B CG2 1 
ATOM   3130 C CD1 . ILE B 1 19  ? 35.09500  42.60700  48.57400  1.000 28.45084 ? 19  ILE B CD1 1 
ATOM   3131 N N   . ALA B 1 20  ? 37.74800  38.89500  51.89600  1.000 15.63454 ? 20  ALA B N   1 
ATOM   3132 C CA  . ALA B 1 20  ? 37.64900  37.76200  52.80700  1.000 19.09717 ? 20  ALA B CA  1 
ATOM   3133 C C   . ALA B 1 20  ? 38.66700  37.83600  53.93300  1.000 21.06445 ? 20  ALA B C   1 
ATOM   3134 O O   . ALA B 1 20  ? 38.49100  37.17100  54.95800  1.000 16.24116 ? 20  ALA B O   1 
ATOM   3135 C CB  . ALA B 1 20  ? 37.82400  36.45400  52.03600  1.000 17.14739 ? 20  ALA B CB  1 
ATOM   3136 N N   . ILE B 1 21  ? 39.72700  38.62200  53.76500  1.000 19.92073 ? 21  ILE B N   1 
ATOM   3137 C CA  . ILE B 1 21  ? 40.78600  38.71400  54.76100  1.000 20.70782 ? 21  ILE B CA  1 
ATOM   3138 C C   . ILE B 1 21  ? 40.66000  39.97100  55.62100  1.000 19.60284 ? 21  ILE B C   1 
ATOM   3139 O O   . ILE B 1 21  ? 41.15300  39.98000  56.76100  1.000 21.33813 ? 21  ILE B O   1 
ATOM   3140 C CB  . ILE B 1 21  ? 42.16000  38.63800  54.05500  1.000 20.31873 ? 21  ILE B CB  1 
ATOM   3141 C CG1 . ILE B 1 21  ? 42.27400  37.29600  53.32700  1.000 19.48135 ? 21  ILE B CG1 1 
ATOM   3142 C CG2 . ILE B 1 21  ? 43.32100  38.80700  55.02200  1.000 19.41907 ? 21  ILE B CG2 1 
ATOM   3143 C CD1 . ILE B 1 21  ? 43.53600  37.12500  52.52100  1.000 22.14369 ? 21  ILE B CD1 1 
ATOM   3144 N N   . ARG B 1 22  ? 39.95600  41.00000  55.14100  1.000 17.91921 ? 22  ARG B N   1 
ATOM   3145 C CA  . ARG B 1 22  ? 39.93600  42.30300  55.78500  1.000 22.21646 ? 22  ARG B CA  1 
ATOM   3146 C C   . ARG B 1 22  ? 38.55100  42.81100  56.16200  1.000 20.63319 ? 22  ARG B C   1 
ATOM   3147 O O   . ARG B 1 22  ? 38.46000  43.69900  57.01600  1.000 24.05953 ? 22  ARG B O   1 
ATOM   3148 C CB  . ARG B 1 22  ? 40.60200  43.34900  54.87600  1.000 20.55050 ? 22  ARG B CB  1 
ATOM   3149 C CG  . ARG B 1 22  ? 42.02200  43.00500  54.47900  1.000 21.37587 ? 22  ARG B CG  1 
ATOM   3150 C CD  . ARG B 1 22  ? 42.97400  43.14200  55.65700  1.000 24.18592 ? 22  ARG B CD  1 
ATOM   3151 N NE  . ARG B 1 22  ? 44.36700  42.95400  55.26200  1.000 24.74294 ? 22  ARG B NE  1 
ATOM   3152 C CZ  . ARG B 1 22  ? 45.40600  43.26200  56.02700  1.000 26.21297 ? 22  ARG B CZ  1 
ATOM   3153 N NH1 . ARG B 1 22  ? 45.24500  43.78600  57.23000  1.000 24.59094 ? 22  ARG B NH1 1 
ATOM   3154 N NH2 . ARG B 1 22  ? 46.63600  43.04100  55.57100  1.000 24.03146 ? 22  ARG B NH2 1 
ATOM   3155 N N   . ALA B 1 23  ? 37.48400  42.30300  55.55400  1.000 17.78880 ? 23  ALA B N   1 
ATOM   3156 C CA  . ALA B 1 23  ? 36.15700  42.83100  55.84000  1.000 17.92059 ? 23  ALA B CA  1 
ATOM   3157 C C   . ALA B 1 23  ? 35.71100  42.45600  57.24800  1.000 19.20646 ? 23  ALA B C   1 
ATOM   3158 O O   . ALA B 1 23  ? 36.12200  41.43200  57.80400  1.000 21.59883 ? 23  ALA B O   1 
ATOM   3159 C CB  . ALA B 1 23  ? 35.13800  42.31700  54.82600  1.000 16.57362 ? 23  ALA B CB  1 
ATOM   3160 N N   . GLY B 1 24  ? 34.87100  43.31400  57.83100  1.000 18.74694 ? 24  GLY B N   1 
ATOM   3161 C CA  . GLY B 1 24  ? 34.26300  43.07500  59.12400  1.000 20.23369 ? 24  GLY B CA  1 
ATOM   3162 C C   . GLY B 1 24  ? 35.13400  43.35300  60.33100  1.000 18.96871 ? 24  GLY B C   1 
ATOM   3163 O O   . GLY B 1 24  ? 34.69800  43.09400  61.45800  1.000 20.08851 ? 24  GLY B O   1 
ATOM   3164 N N   . ILE B 1 25  ? 36.33800  43.87700  60.14700  1.000 20.44350 ? 25  ILE B N   1 
ATOM   3165 C CA  . ILE B 1 25  ? 37.25500  44.05900  61.26600  1.000 19.14700 ? 25  ILE B CA  1 
ATOM   3166 C C   . ILE B 1 25  ? 36.95100  45.38000  61.95900  1.000 22.55566 ? 25  ILE B C   1 
ATOM   3167 O O   . ILE B 1 25  ? 36.82200  46.42500  61.31000  1.000 23.72957 ? 25  ILE B O   1 
ATOM   3168 C CB  . ILE B 1 25  ? 38.71400  43.99700  60.78800  1.000 23.47667 ? 25  ILE B CB  1 
ATOM   3169 C CG1 . ILE B 1 25  ? 39.01500  42.60900  60.20700  1.000 23.44346 ? 25  ILE B CG1 1 
ATOM   3170 C CG2 . ILE B 1 25  ? 39.66700  44.33300  61.92900  1.000 21.68819 ? 25  ILE B CG2 1 
ATOM   3171 C CD1 . ILE B 1 25  ? 40.44100  42.43400  59.72100  1.000 22.97990 ? 25  ILE B CD1 1 
ATOM   3172 N N   . HIS B 1 26  ? 36.80100  45.32600  63.28400  1.000 23.44921 ? 26  HIS B N   1 
ATOM   3173 C CA  . HIS B 1 26  ? 36.63000  46.51300  64.12700  1.000 25.54693 ? 26  HIS B CA  1 
ATOM   3174 C C   . HIS B 1 26  ? 37.54200  46.31600  65.33600  1.000 28.22897 ? 26  HIS B C   1 
ATOM   3175 O O   . HIS B 1 26  ? 37.10300  45.81700  66.37800  1.000 25.11839 ? 26  HIS B O   1 
ATOM   3176 C CB  . HIS B 1 26  ? 35.17800  46.69800  64.54300  1.000 27.75077 ? 26  HIS B CB  1 
ATOM   3177 C CG  . HIS B 1 26  ? 34.21200  46.62600  63.40500  1.000 29.89304 ? 26  HIS B CG  1 
ATOM   3178 N ND1 . HIS B 1 26  ? 33.98700  47.68500  62.55100  1.000 28.39045 ? 26  HIS B ND1 1 
ATOM   3179 C CD2 . HIS B 1 26  ? 33.41200  45.62000  62.97700  1.000 25.72748 ? 26  HIS B CD2 1 
ATOM   3180 C CE1 . HIS B 1 26  ? 33.09100  47.33300  61.64600  1.000 26.11528 ? 26  HIS B CE1 1 
ATOM   3181 N NE2 . HIS B 1 26  ? 32.72600  46.08500  61.88300  1.000 25.34724 ? 26  HIS B NE2 1 
ATOM   3182 N N   . ARG B 1 27  ? 38.80200  46.72400  65.19400  1.000 28.91343 ? 27  ARG B N   1 
ATOM   3183 C CA  . ARG B 1 27  ? 39.78500  46.47800  66.24100  1.000 26.11016 ? 27  ARG B CA  1 
ATOM   3184 C C   . ARG B 1 27  ? 39.43300  47.25100  67.50400  1.000 26.41957 ? 27  ARG B C   1 
ATOM   3185 O O   . ARG B 1 27  ? 38.91100  48.36800  67.44900  1.000 25.41693 ? 27  ARG B O   1 
ATOM   3186 C CB  . ARG B 1 27  ? 41.18900  46.86300  65.76500  1.000 25.32317 ? 27  ARG B CB  1 
ATOM   3187 C CG  . ARG B 1 27  ? 41.73300  45.95500  64.69000  1.000 26.37551 ? 27  ARG B CG  1 
ATOM   3188 C CD  . ARG B 1 27  ? 43.20900  46.16800  64.42300  1.000 24.01181 ? 27  ARG B CD  1 
ATOM   3189 N NE  . ARG B 1 27  ? 43.69900  45.10700  63.55200  1.000 29.14655 ? 27  ARG B NE  1 
ATOM   3190 C CZ  . ARG B 1 27  ? 43.64300  45.13800  62.22700  1.000 32.58958 ? 27  ARG B CZ  1 
ATOM   3191 N NH1 . ARG B 1 27  ? 43.19700  46.20000  61.57800  1.000 30.76220 ? 27  ARG B NH1 1 
ATOM   3192 N NH2 . ARG B 1 27  ? 44.04300  44.07400  61.53400  1.000 31.52288 ? 27  ARG B NH2 1 
ATOM   3193 N N   . THR B 1 28  ? 39.70800  46.63600  68.64800  1.000 25.05551 ? 28  THR B N   1 
ATOM   3194 C CA  . THR B 1 28  ? 39.56100  47.31400  69.92300  1.000 24.26794 ? 28  THR B CA  1 
ATOM   3195 C C   . THR B 1 28  ? 40.73800  48.25900  70.12800  1.000 26.38926 ? 28  THR B C   1 
ATOM   3196 O O   . THR B 1 28  ? 41.67400  48.31500  69.32200  1.000 25.47598 ? 28  THR B O   1 
ATOM   3197 C CB  . THR B 1 28  ? 39.48400  46.30400  71.06400  1.000 26.83186 ? 28  THR B CB  1 
ATOM   3198 O OG1 . THR B 1 28  ? 40.81100  45.87600  71.40200  1.000 24.31143 ? 28  THR B OG1 1 
ATOM   3199 C CG2 . THR B 1 28  ? 38.63800  45.08700  70.66000  1.000 21.15872 ? 28  THR B CG2 1 
ATOM   3200 N N   . GLN B 1 29  ? 40.71100  48.99700  71.23700  1.000 23.04498 ? 29  GLN B N   1 
ATOM   3201 C CA  . GLN B 1 29  ? 41.82400  49.87900  71.55500  1.000 28.52666 ? 29  GLN B CA  1 
ATOM   3202 C C   . GLN B 1 29  ? 43.10200  49.11000  71.87700  1.000 26.84718 ? 29  GLN B C   1 
ATOM   3203 O O   . GLN B 1 29  ? 44.17000  49.72900  71.94700  1.000 27.28341 ? 29  GLN B O   1 
ATOM   3204 C CB  . GLN B 1 29  ? 41.44900  50.80800  72.71600  1.000 26.38602 ? 29  GLN B CB  1 
ATOM   3205 C CG  . GLN B 1 29  ? 40.97900  50.09000  73.97100  1.000 31.64225 ? 29  GLN B CG  1 
ATOM   3206 C CD  . GLN B 1 29  ? 39.82000  50.79700  74.66100  1.000 43.22723 ? 29  GLN B CD  1 
ATOM   3207 O OE1 . GLN B 1 29  ? 39.32800  51.82600  74.18700  1.000 46.70838 ? 29  GLN B OE1 1 
ATOM   3208 N NE2 . GLN B 1 29  ? 39.37400  50.24100  75.78600  1.000 39.60501 ? 29  GLN B NE2 1 
ATOM   3209 N N   . GLU B 1 30  ? 43.02500  47.78900  72.07200  1.000 24.25887 ? 30  GLU B N   1 
ATOM   3210 C CA  . GLU B 1 30  ? 44.23200  46.98300  72.23000  1.000 25.05744 ? 30  GLU B CA  1 
ATOM   3211 C C   . GLU B 1 30  ? 45.00900  46.83300  70.92600  1.000 24.76535 ? 30  GLU B C   1 
ATOM   3212 O O   . GLU B 1 30  ? 46.15100  46.35800  70.95900  1.000 21.44675 ? 30  GLU B O   1 
ATOM   3213 C CB  . GLU B 1 30  ? 43.88500  45.59500  72.78400  1.000 23.69000 ? 30  GLU B CB  1 
ATOM   3214 C CG  . GLU B 1 30  ? 43.06500  45.60600  74.07500  1.000 22.86246 ? 30  GLU B CG  1 
ATOM   3215 C CD  . GLU B 1 30  ? 43.89200  45.96300  75.29900  1.000 27.30516 ? 30  GLU B CD  1 
ATOM   3216 O OE1 . GLU B 1 30  ? 45.11900  46.15700  75.15700  1.000 25.59902 ? 30  GLU B OE1 1 
ATOM   3217 O OE2 . GLU B 1 30  ? 43.31400  46.04200  76.40600  1.000 29.82914 ? 30  GLU B OE2 1 
ATOM   3218 N N   . GLN B 1 31  ? 44.41300  47.21400  69.79400  1.000 21.04270 ? 31  GLN B N   1 
ATOM   3219 C CA  . GLN B 1 31  ? 45.06800  47.17900  68.48600  1.000 23.47788 ? 31  GLN B CA  1 
ATOM   3220 C C   . GLN B 1 31  ? 45.49200  45.76400  68.09800  1.000 23.60680 ? 31  GLN B C   1 
ATOM   3221 O O   . GLN B 1 31  ? 46.50000  45.57400  67.41200  1.000 22.72912 ? 31  GLN B O   1 
ATOM   3222 C CB  . GLN B 1 31  ? 46.26700  48.13200  68.44700  1.000 26.97677 ? 31  GLN B CB  1 
ATOM   3223 C CG  . GLN B 1 31  ? 45.90700  49.59100  68.70000  1.000 30.36131 ? 31  GLN B CG  1 
ATOM   3224 C CD  . GLN B 1 31  ? 47.11100  50.51000  68.60800  1.000 37.50801 ? 31  GLN B CD  1 
ATOM   3225 O OE1 . GLN B 1 31  ? 48.10300  50.31800  69.30600  1.000 36.93205 ? 31  GLN B OE1 1 
ATOM   3226 N NE2 . GLN B 1 31  ? 47.03100  51.50900  67.73700  1.000 39.22745 ? 31  GLN B NE2 1 
ATOM   3227 N N   . GLU B 1 32  ? 44.72500  44.76400  68.53500  1.000 21.99753 ? 32  GLU B N   1 
ATOM   3228 C CA  . GLU B 1 32  ? 45.02600  43.37900  68.19500  1.000 23.16087 ? 32  GLU B CA  1 
ATOM   3229 C C   . GLU B 1 32  ? 45.05600  43.19800  66.68300  1.000 22.50772 ? 32  GLU B C   1 
ATOM   3230 O O   . GLU B 1 32  ? 44.15400  43.65100  65.97200  1.000 20.90077 ? 32  GLU B O   1 
ATOM   3231 C CB  . GLU B 1 32  ? 43.99200  42.43900  68.82500  1.000 22.25501 ? 32  GLU B CB  1 
ATOM   3232 C CG  . GLU B 1 32  ? 42.57000  42.54300  68.26000  1.000 24.32978 ? 32  GLU B CG  1 
ATOM   3233 C CD  . GLU B 1 32  ? 41.78700  43.74600  68.76900  1.000 24.47009 ? 32  GLU B CD  1 
ATOM   3234 O OE1 . GLU B 1 32  ? 42.33800  44.53400  69.57000  1.000 22.25727 ? 32  GLU B OE1 1 
ATOM   3235 O OE2 . GLU B 1 32  ? 40.60700  43.89000  68.37300  1.000 25.00663 ? 32  GLU B OE2 1 
ATOM   3236 N N   . HIS B 1 33  ? 46.11800  42.56000  66.18600  1.000 24.28322 ? 33  HIS B N   1 
ATOM   3237 C CA  . HIS B 1 33  ? 46.21000  42.31100  64.75200  1.000 22.42615 ? 33  HIS B CA  1 
ATOM   3238 C C   . HIS B 1 33  ? 45.15000  41.31700  64.29600  1.000 24.66352 ? 33  HIS B C   1 
ATOM   3239 O O   . HIS B 1 33  ? 44.54400  41.49400  63.23300  1.000 28.20315 ? 33  HIS B O   1 
ATOM   3240 C CB  . HIS B 1 33  ? 47.60600  41.81200  64.38400  1.000 23.58488 ? 33  HIS B CB  1 
ATOM   3241 C CG  . HIS B 1 33  ? 47.82500  41.68400  62.90900  1.000 23.29888 ? 33  HIS B CG  1 
ATOM   3242 N ND1 . HIS B 1 33  ? 47.27200  42.55700  61.99900  1.000 26.27742 ? 33  HIS B ND1 1 
ATOM   3243 C CD2 . HIS B 1 33  ? 48.52800  40.78200  62.18500  1.000 21.15168 ? 33  HIS B CD2 1 
ATOM   3244 C CE1 . HIS B 1 33  ? 47.62000  42.19500  60.77700  1.000 23.92057 ? 33  HIS B CE1 1 
ATOM   3245 N NE2 . HIS B 1 33  ? 48.38700  41.12500  60.86300  1.000 20.83064 ? 33  HIS B NE2 1 
ATOM   3246 N N   . SER B 1 34  ? 44.91100  40.27200  65.08500  1.000 20.88789 ? 34  SER B N   1 
ATOM   3247 C CA  . SER B 1 34  ? 43.97600  39.21600  64.72400  1.000 23.21620 ? 34  SER B CA  1 
ATOM   3248 C C   . SER B 1 34  ? 42.66800  39.37400  65.49400  1.000 20.87254 ? 34  SER B C   1 
ATOM   3249 O O   . SER B 1 34  ? 42.63600  39.91800  66.59900  1.000 22.19721 ? 34  SER B O   1 
ATOM   3250 C CB  . SER B 1 34  ? 44.58300  37.84000  64.99000  1.000 18.68593 ? 34  SER B CB  1 
ATOM   3251 O OG  . SER B 1 34  ? 43.90000  36.83800  64.25700  1.000 19.68049 ? 34  SER B OG  1 
ATOM   3252 N N   . GLU B 1 35  ? 41.58700  38.88000  64.89600  1.000 21.10278 ? 35  GLU B N   1 
ATOM   3253 C CA  . GLU B 1 35  ? 40.25000  39.10300  65.43000  1.000 19.35615 ? 35  GLU B CA  1 
ATOM   3254 C C   . GLU B 1 35  ? 40.08400  38.44500  66.79700  1.000 20.45528 ? 35  GLU B C   1 
ATOM   3255 O O   . GLU B 1 35  ? 40.49400  37.30300  67.01500  1.000 19.70369 ? 35  GLU B O   1 
ATOM   3256 C CB  . GLU B 1 35  ? 39.20200  38.56600  64.44900  1.000 21.69463 ? 35  GLU B CB  1 
ATOM   3257 C CG  . GLU B 1 35  ? 39.15600  39.28400  63.09100  1.000 21.87106 ? 35  GLU B CG  1 
ATOM   3258 C CD  . GLU B 1 35  ? 40.27300  38.86000  62.13000  1.000 25.45142 ? 35  GLU B CD  1 
ATOM   3259 O OE1 . GLU B 1 35  ? 41.14000  38.05200  62.52400  1.000 24.87218 ? 35  GLU B OE1 1 
ATOM   3260 O OE2 . GLU B 1 35  ? 40.28400  39.34000  60.97400  1.000 23.57476 ? 35  GLU B OE2 1 
ATOM   3261 N N   . ALA B 1 36  ? 39.47100  39.17400  67.72000  1.000 19.75524 ? 36  ALA B N   1 
ATOM   3262 C CA  . ALA B 1 36  ? 39.31700  38.70900  69.09000  1.000 20.74127 ? 36  ALA B CA  1 
ATOM   3263 C C   . ALA B 1 36  ? 38.05600  37.86300  69.24600  1.000 16.88165 ? 36  ALA B C   1 
ATOM   3264 O O   . ALA B 1 36  ? 37.11900  37.93900  68.45100  1.000 17.96870 ? 36  ALA B O   1 
ATOM   3265 C CB  . ALA B 1 36  ? 39.26500  39.89400  70.05600  1.000 17.09657 ? 36  ALA B CB  1 
ATOM   3266 N N   . ILE B 1 37  ? 38.03900  37.05700  70.30100  1.000 17.19286 ? 37  ILE B N   1 
ATOM   3267 C CA  . ILE B 1 37  ? 36.86700  36.27800  70.67400  1.000 17.05627 ? 37  ILE B CA  1 
ATOM   3268 C C   . ILE B 1 37  ? 36.20000  36.96700  71.85500  1.000 17.90606 ? 37  ILE B C   1 
ATOM   3269 O O   . ILE B 1 37  ? 36.85900  37.28300  72.85300  1.000 16.26042 ? 37  ILE B O   1 
ATOM   3270 C CB  . ILE B 1 37  ? 37.24200  34.82700  71.01900  1.000 18.64047 ? 37  ILE B CB  1 
ATOM   3271 C CG1 . ILE B 1 37  ? 38.05600  34.19800  69.88800  1.000 17.87762 ? 37  ILE B CG1 1 
ATOM   3272 C CG2 . ILE B 1 37  ? 35.98600  34.00600  71.27800  1.000 21.13386 ? 37  ILE B CG2 1 
ATOM   3273 C CD1 . ILE B 1 37  ? 38.58700  32.82900  70.20600  1.000 13.99146 ? 37  ILE B CD1 1 
ATOM   3274 N N   . PHE B 1 38  ? 34.90300  37.22100  71.73700  1.000 16.53798 ? 38  PHE B N   1 
ATOM   3275 C CA  . PHE B 1 38  ? 34.16800  37.83400  72.83200  1.000 15.98768 ? 38  PHE B CA  1 
ATOM   3276 C C   . PHE B 1 38  ? 33.19900  36.81800  73.41800  1.000 19.40671 ? 38  PHE B C   1 
ATOM   3277 O O   . PHE B 1 38  ? 32.02300  36.78600  73.03700  1.000 19.63756 ? 38  PHE B O   1 
ATOM   3278 C CB  . PHE B 1 38  ? 33.42600  39.09100  72.36900  1.000 15.22235 ? 38  PHE B CB  1 
ATOM   3279 C CG  . PHE B 1 38  ? 34.33000  40.27900  72.12200  1.000 16.17496 ? 38  PHE B CG  1 
ATOM   3280 C CD1 . PHE B 1 38  ? 34.97300  40.44100  70.90500  1.000 14.01367 ? 38  PHE B CD1 1 
ATOM   3281 C CD2 . PHE B 1 38  ? 34.53000  41.23100  73.10700  1.000 21.45430 ? 38  PHE B CD2 1 
ATOM   3282 C CE1 . PHE B 1 38  ? 35.79700  41.52300  70.67000  1.000 15.87306 ? 38  PHE B CE1 1 
ATOM   3283 C CE2 . PHE B 1 38  ? 35.35900  42.32200  72.88200  1.000 20.27631 ? 38  PHE B CE2 1 
ATOM   3284 C CZ  . PHE B 1 38  ? 35.99300  42.46400  71.65800  1.000 20.82865 ? 38  PHE B CZ  1 
ATOM   3285 N N   . PRO B 1 39  ? 33.65500  35.96100  74.33000  1.000 19.23025 ? 39  PRO B N   1 
ATOM   3286 C CA  . PRO B 1 39  ? 32.71700  35.11100  75.06300  1.000 18.82815 ? 39  PRO B CA  1 
ATOM   3287 C C   . PRO B 1 39  ? 32.09100  35.89700  76.20300  1.000 19.48221 ? 39  PRO B C   1 
ATOM   3288 O O   . PRO B 1 39  ? 32.58000  35.89200  77.33500  1.000 19.92314 ? 39  PRO B O   1 
ATOM   3289 C CB  . PRO B 1 39  ? 33.59500  33.95200  75.55500  1.000 19.07425 ? 39  PRO B CB  1 
ATOM   3290 C CG  . PRO B 1 39  ? 34.94900  34.56000  75.70900  1.000 20.87116 ? 39  PRO B CG  1 
ATOM   3291 C CD  . PRO B 1 39  ? 35.04600  35.74000  74.76300  1.000 18.36984 ? 39  PRO B CD  1 
ATOM   3292 N N   . THR B 1 40  ? 31.03200  36.63000  75.89500  1.000 20.38929 ? 40  THR B N   1 
ATOM   3293 C CA  . THR B 1 40  ? 30.31300  37.39500  76.90000  1.000 23.59052 ? 40  THR B CA  1 
ATOM   3294 C C   . THR B 1 40  ? 28.83800  37.33200  76.54100  1.000 24.47431 ? 40  THR B C   1 
ATOM   3295 O O   . THR B 1 40  ? 28.49100  37.30000  75.35900  1.000 24.17365 ? 40  THR B O   1 
ATOM   3296 C CB  . THR B 1 40  ? 30.80700  38.85100  76.95900  1.000 23.65061 ? 40  THR B CB  1 
ATOM   3297 O OG1 . THR B 1 40  ? 30.15500  39.54700  78.02900  1.000 18.72416 ? 40  THR B OG1 1 
ATOM   3298 C CG2 . THR B 1 40  ? 30.55100  39.57000  75.63500  1.000 20.87002 ? 40  THR B CG2 1 
ATOM   3299 N N   . SER B 1 41  ? 27.97300  37.27400  77.55000  1.000 20.73599 ? 41  SER B N   1 
ATOM   3300 C CA  A SER B 1 41  ? 26.54700  37.24300  77.26700  0.868 23.79112 ? 41  SER B CA  1 
ATOM   3301 C CA  B SER B 1 41  ? 26.53600  37.23600  77.31800  0.132 23.80590 ? 41  SER B CA  1 
ATOM   3302 C C   . SER B 1 41  ? 25.87300  38.60500  77.37700  1.000 25.69190 ? 41  SER B C   1 
ATOM   3303 O O   . SER B 1 41  ? 24.78000  38.77100  76.82900  1.000 30.00360 ? 41  SER B O   1 
ATOM   3304 C CB  A SER B 1 41  ? 25.83700  36.24900  78.18900  0.868 21.20258 ? 41  SER B CB  1 
ATOM   3305 C CB  B SER B 1 41  ? 25.85400  36.31900  78.33600  0.132 21.55742 ? 41  SER B CB  1 
ATOM   3306 O OG  A SER B 1 41  ? 26.09600  36.55200  79.54100  0.868 21.21849 ? 41  SER B OG  1 
ATOM   3307 O OG  B SER B 1 41  ? 24.45000  36.49200  78.29300  0.132 25.05313 ? 41  SER B OG  1 
ATOM   3308 N N   . SER B 1 42  ? 26.49100  39.58100  78.04300  1.000 21.32822 ? 42  SER B N   1 
ATOM   3309 C CA  . SER B 1 42  ? 25.89700  40.90700  78.17800  1.000 26.46679 ? 42  SER B CA  1 
ATOM   3310 C C   . SER B 1 42  ? 26.99100  41.96500  78.09600  1.000 25.12131 ? 42  SER B C   1 
ATOM   3311 O O   . SER B 1 42  ? 28.17500  41.66000  77.92200  1.000 23.25343 ? 42  SER B O   1 
ATOM   3312 C CB  . SER B 1 42  ? 25.09500  41.03400  79.48200  1.000 22.20567 ? 42  SER B CB  1 
ATOM   3313 O OG  . SER B 1 42  ? 25.92000  40.86300  80.62100  1.000 23.33135 ? 42  SER B OG  1 
ATOM   3314 N N   . PHE B 1 43  ? 26.57900  43.22700  78.22100  1.000 26.86468 ? 43  PHE B N   1 
ATOM   3315 C CA  . PHE B 1 43  ? 27.48100  44.36000  78.07800  1.000 26.94519 ? 43  PHE B CA  1 
ATOM   3316 C C   . PHE B 1 43  ? 27.16000  45.41100  79.13400  1.000 27.65397 ? 43  PHE B C   1 
ATOM   3317 O O   . PHE B 1 43  ? 26.00800  45.56400  79.55500  1.000 30.97722 ? 43  PHE B O   1 
ATOM   3318 C CB  . PHE B 1 43  ? 27.38900  44.95500  76.66500  1.000 29.59748 ? 43  PHE B CB  1 
ATOM   3319 C CG  . PHE B 1 43  ? 27.65800  43.95700  75.57200  1.000 32.00152 ? 43  PHE B CG  1 
ATOM   3320 C CD1 . PHE B 1 43  ? 26.63600  43.14600  75.08300  1.000 35.59297 ? 43  PHE B CD1 1 
ATOM   3321 C CD2 . PHE B 1 43  ? 28.93000  43.82200  75.03500  1.000 27.99856 ? 43  PHE B CD2 1 
ATOM   3322 C CE1 . PHE B 1 43  ? 26.87800  42.22000  74.07800  1.000 31.77239 ? 43  PHE B CE1 1 
ATOM   3323 C CE2 . PHE B 1 43  ? 29.18000  42.89800  74.02400  1.000 28.52185 ? 43  PHE B CE2 1 
ATOM   3324 C CZ  . PHE B 1 43  ? 28.15200  42.09900  73.54600  1.000 31.79094 ? 43  PHE B CZ  1 
ATOM   3325 N N   . VAL B 1 44  ? 28.19000  46.13600  79.56100  1.000 27.02310 ? 44  VAL B N   1 
ATOM   3326 C CA  . VAL B 1 44  ? 28.09000  47.06900  80.67800  1.000 26.97883 ? 44  VAL B CA  1 
ATOM   3327 C C   . VAL B 1 44  ? 27.86600  48.47100  80.13400  1.000 31.00549 ? 44  VAL B C   1 
ATOM   3328 O O   . VAL B 1 44  ? 28.54800  48.89900  79.19300  1.000 33.81836 ? 44  VAL B O   1 
ATOM   3329 C CB  . VAL B 1 44  ? 29.34700  47.02200  81.56400  1.000 28.38401 ? 44  VAL B CB  1 
ATOM   3330 C CG1 . VAL B 1 44  ? 29.17500  47.92900  82.77800  1.000 33.02754 ? 44  VAL B CG1 1 
ATOM   3331 C CG2 . VAL B 1 44  ? 29.62500  45.60300  82.00800  1.000 26.93389 ? 44  VAL B CG2 1 
ATOM   3332 N N   . PHE B 1 45  ? 26.91000  49.18300  80.72600  1.000 28.93813 ? 45  PHE B N   1 
ATOM   3333 C CA  . PHE B 1 45  ? 26.60900  50.56400  80.38200  1.000 30.62525 ? 45  PHE B CA  1 
ATOM   3334 C C   . PHE B 1 45  ? 27.28200  51.50800  81.37100  1.000 31.53540 ? 45  PHE B C   1 
ATOM   3335 O O   . PHE B 1 45  ? 27.47100  51.17400  82.54300  1.000 34.05289 ? 45  PHE B O   1 
ATOM   3336 C CB  . PHE B 1 45  ? 25.09900  50.80000  80.37300  1.000 28.48629 ? 45  PHE B CB  1 
ATOM   3337 C CG  . PHE B 1 45  ? 24.32500  49.71600  79.67700  1.000 31.85600 ? 45  PHE B CG  1 
ATOM   3338 C CD1 . PHE B 1 45  ? 24.43200  49.54100  78.30700  1.000 31.94108 ? 45  PHE B CD1 1 
ATOM   3339 C CD2 . PHE B 1 45  ? 23.49900  48.86600  80.39300  1.000 31.19601 ? 45  PHE B CD2 1 
ATOM   3340 C CE1 . PHE B 1 45  ? 23.72500  48.54200  77.66600  1.000 36.97919 ? 45  PHE B CE1 1 
ATOM   3341 C CE2 . PHE B 1 45  ? 22.78500  47.86700  79.75700  1.000 31.38992 ? 45  PHE B CE2 1 
ATOM   3342 C CZ  . PHE B 1 45  ? 22.89900  47.70400  78.39300  1.000 37.52308 ? 45  PHE B CZ  1 
ATOM   3343 N N   . ASP B 1 46  ? 27.65200  52.69400  80.87900  1.000 34.22579 ? 46  ASP B N   1 
ATOM   3344 C CA  . ASP B 1 46  ? 28.35100  53.66600  81.71900  1.000 34.59067 ? 46  ASP B CA  1 
ATOM   3345 C C   . ASP B 1 46  ? 27.41300  54.33900  82.71300  1.000 32.31146 ? 46  ASP B C   1 
ATOM   3346 O O   . ASP B 1 46  ? 27.85400  54.77900  83.78200  1.000 32.03828 ? 46  ASP B O   1 
ATOM   3347 C CB  . ASP B 1 46  ? 29.03300  54.72400  80.84500  1.000 42.26555 ? 46  ASP B CB  1 
ATOM   3348 C CG  . ASP B 1 46  ? 29.97200  54.11800  79.81100  1.000 50.88835 ? 46  ASP B CG  1 
ATOM   3349 O OD1 . ASP B 1 46  ? 30.77100  53.22200  80.16800  1.000 47.94142 ? 46  ASP B OD1 1 
ATOM   3350 O OD2 . ASP B 1 46  ? 29.90700  54.53800  78.63500  1.000 55.25103 ? 46  ASP B OD2 1 
ATOM   3351 N N   . SER B 1 47  ? 26.12500  54.43000  82.38300  1.000 33.31365 ? 47  SER B N   1 
ATOM   3352 C CA  . SER B 1 47  ? 25.16900  55.14500  83.21400  1.000 30.79259 ? 47  SER B CA  1 
ATOM   3353 C C   . SER B 1 47  ? 23.78100  54.56800  82.99900  1.000 28.87390 ? 47  SER B C   1 
ATOM   3354 O O   . SER B 1 47  ? 23.52700  53.85000  82.02700  1.000 27.49801 ? 47  SER B O   1 
ATOM   3355 C CB  . SER B 1 47  ? 25.15700  56.64300  82.89900  1.000 31.03024 ? 47  SER B CB  1 
ATOM   3356 O OG  . SER B 1 47  ? 24.68400  56.86600  81.57900  1.000 29.57935 ? 47  SER B OG  1 
ATOM   3357 N N   . ALA B 1 48  ? 22.87600  54.90500  83.92200  1.000 29.88864 ? 48  ALA B N   1 
ATOM   3358 C CA  . ALA B 1 48  ? 21.47700  54.53200  83.74800  1.000 29.54782 ? 48  ALA B CA  1 
ATOM   3359 C C   . ALA B 1 48  ? 20.91700  55.10300  82.45500  1.000 26.17300 ? 48  ALA B C   1 
ATOM   3360 O O   . ALA B 1 48  ? 20.15400  54.42900  81.75300  1.000 28.32621 ? 48  ALA B O   1 
ATOM   3361 C CB  . ALA B 1 48  ? 20.64800  55.01500  84.93700  1.000 24.37877 ? 48  ALA B CB  1 
ATOM   3362 N N   . GLU B 1 49  ? 21.28700  56.34800  82.12600  1.000 29.57082 ? 49  GLU B N   1 
ATOM   3363 C CA  A GLU B 1 49  ? 20.76700  56.99000  80.92100  0.499 31.07487 ? 49  GLU B CA  1 
ATOM   3364 C CA  B GLU B 1 49  ? 20.75100  56.98000  80.92400  0.501 31.10873 ? 49  GLU B CA  1 
ATOM   3365 C C   . GLU B 1 49  ? 21.18700  56.23800  79.66500  1.000 35.10392 ? 49  GLU B C   1 
ATOM   3366 O O   . GLU B 1 49  ? 20.37000  56.00700  78.76500  1.000 35.83785 ? 49  GLU B O   1 
ATOM   3367 C CB  A GLU B 1 49  ? 21.24300  58.44300  80.85200  0.499 31.35636 ? 49  GLU B CB  1 
ATOM   3368 C CB  B GLU B 1 49  ? 21.15900  58.45700  80.85800  0.501 31.36303 ? 49  GLU B CB  1 
ATOM   3369 C CG  A GLU B 1 49  ? 20.14600  59.47200  81.06300  0.499 33.08173 ? 49  GLU B CG  1 
ATOM   3370 C CG  B GLU B 1 49  ? 22.26300  58.90900  81.81700  0.501 31.20020 ? 49  GLU B CG  1 
ATOM   3371 C CD  A GLU B 1 49  ? 20.09900  60.51100  79.95800  0.499 33.33073 ? 49  GLU B CD  1 
ATOM   3372 C CD  B GLU B 1 49  ? 21.81500  58.97600  83.26600  0.501 32.24462 ? 49  GLU B CD  1 
ATOM   3373 O OE1 A GLU B 1 49  ? 21.17300  61.00100  79.54800  0.499 32.37947 ? 49  GLU B OE1 1 
ATOM   3374 O OE1 B GLU B 1 49  ? 21.75900  57.91000  83.90700  0.501 27.98799 ? 49  GLU B OE1 1 
ATOM   3375 O OE2 A GLU B 1 49  ? 18.98600  60.82800  79.49100  0.499 33.76173 ? 49  GLU B OE2 1 
ATOM   3376 O OE2 B GLU B 1 49  ? 21.51300  60.08500  83.76100  0.501 34.87077 ? 49  GLU B OE2 1 
ATOM   3377 N N   . GLU B 1 50  ? 22.46300  55.84200  79.58600  1.000 27.66048 ? 50  GLU B N   1 
ATOM   3378 C CA  . GLU B 1 50  ? 22.92300  55.11700  78.40400  1.000 32.27046 ? 50  GLU B CA  1 
ATOM   3379 C C   . GLU B 1 50  ? 22.20900  53.77700  78.27200  1.000 36.31574 ? 50  GLU B C   1 
ATOM   3380 O O   . GLU B 1 50  ? 21.91900  53.32400  77.15700  1.000 37.43463 ? 50  GLU B O   1 
ATOM   3381 C CB  . GLU B 1 50  ? 24.44000  54.92000  78.44900  1.000 31.64959 ? 50  GLU B CB  1 
ATOM   3382 C CG  . GLU B 1 50  ? 24.95300  53.93400  77.40000  1.000 37.00073 ? 50  GLU B CG  1 
ATOM   3383 C CD  . GLU B 1 50  ? 26.46700  53.85500  77.33000  1.000 41.16461 ? 50  GLU B CD  1 
ATOM   3384 O OE1 . GLU B 1 50  ? 27.09200  54.79900  76.80100  1.000 46.67690 ? 50  GLU B OE1 1 
ATOM   3385 O OE2 . GLU B 1 50  ? 27.03200  52.84400  77.80300  1.000 40.94832 ? 50  GLU B OE2 1 
ATOM   3386 N N   . ALA B 1 51  ? 21.91600  53.12800  79.40300  1.000 35.27523 ? 51  ALA B N   1 
ATOM   3387 C CA  . ALA B 1 51  ? 21.18500  51.86700  79.36800  1.000 29.53658 ? 51  ALA B CA  1 
ATOM   3388 C C   . ALA B 1 51  ? 19.78400  52.05700  78.80200  1.000 35.79964 ? 51  ALA B C   1 
ATOM   3389 O O   . ALA B 1 51  ? 19.31900  51.25100  77.98500  1.000 36.92039 ? 51  ALA B O   1 
ATOM   3390 C CB  . ALA B 1 51  ? 21.11800  51.26800  80.77100  1.000 31.22456 ? 51  ALA B CB  1 
ATOM   3391 N N   . ALA B 1 52  ? 19.08800  53.11000  79.23600  1.000 33.81739 ? 52  ALA B N   1 
ATOM   3392 C CA  . ALA B 1 52  ? 17.75800  53.38300  78.70400  1.000 36.24945 ? 52  ALA B CA  1 
ATOM   3393 C C   . ALA B 1 52  ? 17.81900  53.73300  77.22200  1.000 37.29996 ? 52  ALA B C   1 
ATOM   3394 O O   . ALA B 1 52  ? 17.00000  53.25100  76.42900  1.000 33.71774 ? 52  ALA B O   1 
ATOM   3395 C CB  . ALA B 1 52  ? 17.09900  54.50800  79.50000  1.000 33.49975 ? 52  ALA B CB  1 
ATOM   3396 N N   . ASP B 1 53  ? 18.79100  54.56400  76.83100  1.000 33.17445 ? 53  ASP B N   1 
ATOM   3397 C CA  . ASP B 1 53  ? 18.91000  54.95400  75.43000  1.000 38.94411 ? 53  ASP B CA  1 
ATOM   3398 C C   . ASP B 1 53  ? 19.20900  53.75300  74.54900  1.000 41.33681 ? 53  ASP B C   1 
ATOM   3399 O O   . ASP B 1 53  ? 18.65000  53.62100  73.45400  1.000 44.46133 ? 53  ASP B O   1 
ATOM   3400 C CB  . ASP B 1 53  ? 19.99500  56.01700  75.26800  1.000 43.87037 ? 53  ASP B CB  1 
ATOM   3401 C CG  . ASP B 1 53  ? 19.56000  57.37500  75.78200  1.000 47.56403 ? 53  ASP B CG  1 
ATOM   3402 O OD1 . ASP B 1 53  ? 18.41000  57.49100  76.25500  1.000 43.52199 ? 53  ASP B OD1 1 
ATOM   3403 O OD2 . ASP B 1 53  ? 20.36500  58.32700  75.71100  1.000 52.01890 ? 53  ASP B OD2 1 
ATOM   3404 N N   . ARG B 1 54  ? 20.09100  52.86500  75.00500  1.000 41.41043 ? 54  ARG B N   1 
ATOM   3405 C CA  . ARG B 1 54  ? 20.44300  51.71200  74.18700  1.000 44.45251 ? 54  ARG B CA  1 
ATOM   3406 C C   . ARG B 1 54  ? 19.26200  50.75700  74.03900  1.000 43.38176 ? 54  ARG B C   1 
ATOM   3407 O O   . ARG B 1 54  ? 19.03900  50.20200  72.95600  1.000 43.86292 ? 54  ARG B O   1 
ATOM   3408 C CB  . ARG B 1 54  ? 21.66000  51.00600  74.77900  1.000 44.06892 ? 54  ARG B CB  1 
ATOM   3409 C CG  . ARG B 1 54  ? 22.40600  50.15500  73.77400  1.000 48.19170 ? 54  ARG B CG  1 
ATOM   3410 C CD  . ARG B 1 54  ? 23.85500  49.96600  74.17700  1.000 50.54432 ? 54  ARG B CD  1 
ATOM   3411 N NE  . ARG B 1 54  ? 24.64800  51.16800  73.95700  1.000 47.81298 ? 54  ARG B NE  1 
ATOM   3412 C CZ  . ARG B 1 54  ? 25.92400  51.29100  74.29500  1.000 45.31048 ? 54  ARG B CZ  1 
ATOM   3413 N NH1 . ARG B 1 54  ? 26.57700  50.30600  74.89000  1.000 39.65179 ? 54  ARG B NH1 1 
ATOM   3414 N NH2 . ARG B 1 54  ? 26.55800  52.43000  74.03400  1.000 50.31263 ? 54  ARG B NH2 1 
ATOM   3415 N N   . PHE B 1 55  ? 18.48400  50.56200  75.10800  1.000 41.62316 ? 55  PHE B N   1 
ATOM   3416 C CA  . PHE B 1 55  ? 17.30300  49.70800  75.01000  1.000 41.04002 ? 55  PHE B CA  1 
ATOM   3417 C C   . PHE B 1 55  ? 16.22000  50.32900  74.13600  1.000 46.53952 ? 55  PHE B C   1 
ATOM   3418 O O   . PHE B 1 55  ? 15.48600  49.60400  73.45500  1.000 48.47802 ? 55  PHE B O   1 
ATOM   3419 C CB  . PHE B 1 55  ? 16.75000  49.40100  76.40100  1.000 40.30889 ? 55  PHE B CB  1 
ATOM   3420 C CG  . PHE B 1 55  ? 17.29200  48.13700  76.99000  1.000 38.25756 ? 55  PHE B CG  1 
ATOM   3421 C CD1 . PHE B 1 55  ? 16.65400  46.93000  76.77000  1.000 34.37052 ? 55  PHE B CD1 1 
ATOM   3422 C CD2 . PHE B 1 55  ? 18.45600  48.15000  77.74200  1.000 40.98389 ? 55  PHE B CD2 1 
ATOM   3423 C CE1 . PHE B 1 55  ? 17.15200  45.75800  77.30500  1.000 36.30062 ? 55  PHE B CE1 1 
ATOM   3424 C CE2 . PHE B 1 55  ? 18.96300  46.98000  78.28200  1.000 38.18635 ? 55  PHE B CE2 1 
ATOM   3425 C CZ  . PHE B 1 55  ? 18.31100  45.78300  78.06200  1.000 37.15761 ? 55  PHE B CZ  1 
ATOM   3426 N N   . ALA B 1 56  ? 16.09600  51.65500  74.14600  1.000 45.70317 ? 56  ALA B N   1 
ATOM   3427 C CA  . ALA B 1 56  ? 15.13200  52.31800  73.28000  1.000 46.34334 ? 56  ALA B CA  1 
ATOM   3428 C C   . ALA B 1 56  ? 15.61300  52.43800  71.83700  1.000 48.96023 ? 56  ALA B C   1 
ATOM   3429 O O   . ALA B 1 56  ? 14.80000  52.74100  70.95700  1.000 52.02439 ? 56  ALA B O   1 
ATOM   3430 C CB  . ALA B 1 56  ? 14.79600  53.70500  73.83300  1.000 42.61953 ? 56  ALA B CB  1 
ATOM   3431 N N   . GLY B 1 57  ? 16.89700  52.19400  71.57100  1.000 50.62323 ? 57  GLY B N   1 
ATOM   3432 C CA  . GLY B 1 57  ? 17.43400  52.32500  70.22900  1.000 48.99033 ? 57  GLY B CA  1 
ATOM   3433 C C   . GLY B 1 57  ? 17.85600  53.72400  69.83800  1.000 52.07457 ? 57  GLY B C   1 
ATOM   3434 O O   . GLY B 1 57  ? 18.04500  53.98400  68.64400  1.000 52.45372 ? 57  GLY B O   1 
ATOM   3435 N N   . ARG B 1 58  ? 18.00000  54.63400  70.80800  1.000 53.11455 ? 58  ARG B N   1 
ATOM   3436 C CA  . ARG B 1 58  ? 18.41100  56.00500  70.51000  1.000 50.81665 ? 58  ARG B CA  1 
ATOM   3437 C C   . ARG B 1 58  ? 19.88600  56.08800  70.14200  1.000 56.92744 ? 58  ARG B C   1 
ATOM   3438 O O   . ARG B 1 58  ? 20.28500  56.98200  69.38600  1.000 59.79023 ? 58  ARG B O   1 
ATOM   3439 C CB  . ARG B 1 58  ? 18.13000  56.91500  71.70700  1.000 50.03101 ? 58  ARG B CB  1 
ATOM   3440 C CG  . ARG B 1 58  ? 16.74700  57.55500  71.73100  1.000 51.97900 ? 58  ARG B CG  1 
ATOM   3441 C CD  . ARG B 1 58  ? 15.63100  56.52700  71.77400  1.000 53.42242 ? 58  ARG B CD  1 
ATOM   3442 N NE  . ARG B 1 58  ? 14.34400  57.13800  72.07900  1.000 57.39066 ? 58  ARG B NE  1 
ATOM   3443 C CZ  . ARG B 1 58  ? 13.88700  57.33400  73.30800  1.000 65.88103 ? 58  ARG B CZ  1 
ATOM   3444 N NH1 . ARG B 1 58  ? 14.58400  56.96100  74.37200  1.000 50.23719 ? 58  ARG B NH1 1 
ATOM   3445 N NH2 . ARG B 1 58  ? 12.70500  57.92100  73.47400  1.000 69.35470 ? 58  ARG B NH2 1 
ATOM   3446 N N   . VAL B 1 59  ? 20.70400  55.18400  70.67300  1.000 56.25476 ? 59  VAL B N   1 
ATOM   3447 C CA  . VAL B 1 59  ? 22.14300  55.18900  70.42500  1.000 61.73687 ? 59  VAL B CA  1 
ATOM   3448 C C   . VAL B 1 59  ? 22.56900  53.80300  69.95100  1.000 57.84138 ? 59  VAL B C   1 
ATOM   3449 O O   . VAL B 1 59  ? 21.90800  52.80500  70.27300  1.000 51.07927 ? 59  VAL B O   1 
ATOM   3450 C CB  . VAL B 1 59  ? 22.92800  55.60900  71.68100  1.000 58.11777 ? 59  VAL B CB  1 
ATOM   3451 C CG1 . VAL B 1 59  ? 22.51200  57.00000  72.14100  1.000 53.52246 ? 59  VAL B CG1 1 
ATOM   3452 C CG2 . VAL B 1 59  ? 22.73600  54.58900  72.79400  1.000 51.79322 ? 59  VAL B CG2 1 
ATOM   3453 N N   . PRO B 1 60  ? 23.64400  53.69500  69.17600  1.000 61.72948 ? 60  PRO B N   1 
ATOM   3454 C CA  . PRO B 1 60  ? 24.17700  52.37600  68.82900  1.000 62.07136 ? 60  PRO B CA  1 
ATOM   3455 C C   . PRO B 1 60  ? 25.03100  51.80400  69.95000  1.000 60.94392 ? 60  PRO B C   1 
ATOM   3456 O O   . PRO B 1 60  ? 25.68100  52.53200  70.70600  1.000 61.59763 ? 60  PRO B O   1 
ATOM   3457 C CB  . PRO B 1 60  ? 25.02400  52.66200  67.58400  1.000 63.47840 ? 60  PRO B CB  1 
ATOM   3458 C CG  . PRO B 1 60  ? 25.50800  54.06700  67.80600  1.000 62.17384 ? 60  PRO B CG  1 
ATOM   3459 C CD  . PRO B 1 60  ? 24.38000  54.78600  68.50800  1.000 58.50644 ? 60  PRO B CD  1 
ATOM   3460 N N   . GLY B 1 61  ? 25.02300  50.48200  70.05000  1.000 58.68816 ? 61  GLY B N   1 
ATOM   3461 C CA  . GLY B 1 61  ? 25.83800  49.80500  71.03900  1.000 52.39275 ? 61  GLY B CA  1 
ATOM   3462 C C   . GLY B 1 61  ? 25.35400  48.39700  71.29300  1.000 47.56808 ? 61  GLY B C   1 
ATOM   3463 O O   . GLY B 1 61  ? 24.31900  47.96100  70.78900  1.000 47.72928 ? 61  GLY B O   1 
ATOM   3464 N N   . ASN B 1 62  ? 26.12900  47.68800  72.11100  1.000 39.24241 ? 62  ASN B N   1 
ATOM   3465 C CA  . ASN B 1 62  ? 25.86700  46.29200  72.43000  1.000 40.90221 ? 62  ASN B CA  1 
ATOM   3466 C C   . ASN B 1 62  ? 24.94800  46.18200  73.64500  1.000 42.30477 ? 62  ASN B C   1 
ATOM   3467 O O   . ASN B 1 62  ? 25.07000  46.95000  74.60400  1.000 39.00019 ? 62  ASN B O   1 
ATOM   3468 C CB  . ASN B 1 62  ? 27.18200  45.55300  72.69200  1.000 36.05458 ? 62  ASN B CB  1 
ATOM   3469 C CG  . ASN B 1 62  ? 28.13700  45.59200  71.49900  1.000 40.34196 ? 62  ASN B CG  1 
ATOM   3470 O OD1 . ASN B 1 62  ? 27.73700  45.35500  70.35700  1.000 33.89875 ? 62  ASN B OD1 1 
ATOM   3471 N ND2 . ASN B 1 62  ? 29.40800  45.88900  71.76700  1.000 25.80219 ? 62  ASN B ND2 1 
ATOM   3472 N N   . ILE B 1 63  ? 24.02200  45.22000  73.59600  1.000 39.42846 ? 63  ILE B N   1 
ATOM   3473 C CA  . ILE B 1 63  ? 23.04400  45.01600  74.66400  1.000 38.80350 ? 63  ILE B CA  1 
ATOM   3474 C C   . ILE B 1 63  ? 23.17100  43.60900  75.23300  1.000 37.35622 ? 63  ILE B C   1 
ATOM   3475 O O   . ILE B 1 63  ? 23.41600  43.42500  76.43300  1.000 30.75235 ? 63  ILE B O   1 
ATOM   3476 C CB  . ILE B 1 63  ? 21.60700  45.25500  74.16300  1.000 41.58818 ? 63  ILE B CB  1 
ATOM   3477 C CG1 . ILE B 1 63  ? 21.39500  46.72200  73.78700  1.000 42.56427 ? 63  ILE B CG1 1 
ATOM   3478 C CG2 . ILE B 1 63  ? 20.59700  44.80800  75.21700  1.000 40.95575 ? 63  ILE B CG2 1 
ATOM   3479 C CD1 . ILE B 1 63  ? 19.99300  47.03100  73.30500  1.000 40.21472 ? 63  ILE B CD1 1 
ATOM   3480 N N   . TYR B 1 64  ? 22.98500  42.60900  74.37300  1.000 35.78184 ? 64  TYR B N   1 
ATOM   3481 C CA  . TYR B 1 64  ? 23.00800  41.21000  74.76900  1.000 39.80461 ? 64  TYR B CA  1 
ATOM   3482 C C   . TYR B 1 64  ? 23.56400  40.39300  73.60800  1.000 38.64107 ? 64  TYR B C   1 
ATOM   3483 O O   . TYR B 1 64  ? 23.33800  40.71700  72.43900  1.000 39.48919 ? 64  TYR B O   1 
ATOM   3484 C CB  . TYR B 1 64  ? 21.60300  40.73700  75.17300  1.000 37.63207 ? 64  TYR B CB  1 
ATOM   3485 C CG  . TYR B 1 64  ? 21.55700  39.48600  76.02700  1.000 41.39844 ? 64  TYR B CG  1 
ATOM   3486 C CD1 . TYR B 1 64  ? 21.74800  39.55000  77.40700  1.000 33.08410 ? 64  TYR B CD1 1 
ATOM   3487 C CD2 . TYR B 1 64  ? 21.29200  38.24300  75.45700  1.000 41.57875 ? 64  TYR B CD2 1 
ATOM   3488 C CE1 . TYR B 1 64  ? 21.69400  38.40300  78.19300  1.000 33.75585 ? 64  TYR B CE1 1 
ATOM   3489 C CE2 . TYR B 1 64  ? 21.23500  37.09300  76.23200  1.000 38.60148 ? 64  TYR B CE2 1 
ATOM   3490 C CZ  . TYR B 1 64  ? 21.43400  37.17700  77.59600  1.000 34.66514 ? 64  TYR B CZ  1 
ATOM   3491 O OH  . TYR B 1 64  ? 21.37300  36.02800  78.35300  1.000 33.56627 ? 64  TYR B OH  1 
ATOM   3492 N N   . ALA B 1 65  ? 24.30200  39.33100  73.94500  1.000 39.63118 ? 65  ALA B N   1 
ATOM   3493 C CA  . ALA B 1 65  ? 25.03200  38.56400  72.93900  1.000 40.01564 ? 65  ALA B CA  1 
ATOM   3494 C C   . ALA B 1 65  ? 24.12300  37.81900  71.97000  1.000 40.42255 ? 65  ALA B C   1 
ATOM   3495 O O   . ALA B 1 65  ? 24.57400  37.45700  70.87700  1.000 43.37434 ? 65  ALA B O   1 
ATOM   3496 C CB  . ALA B 1 65  ? 25.97200  37.56900  73.61800  1.000 34.29467 ? 65  ALA B CB  1 
ATOM   3497 N N   . ARG B 1 66  ? 22.86300  37.57400  72.33700  1.000 41.32434 ? 66  ARG B N   1 
ATOM   3498 C CA  . ARG B 1 66  ? 21.96000  36.84300  71.45600  1.000 43.75303 ? 66  ARG B CA  1 
ATOM   3499 C C   . ARG B 1 66  ? 21.57400  37.64000  70.21300  1.000 43.72979 ? 66  ARG B C   1 
ATOM   3500 O O   . ARG B 1 66  ? 21.02700  37.05600  69.27200  1.000 38.01574 ? 66  ARG B O   1 
ATOM   3501 C CB  . ARG B 1 66  ? 20.70700  36.42000  72.23200  1.000 38.93894 ? 66  ARG B CB  1 
ATOM   3502 C CG  . ARG B 1 66  ? 20.05600  35.13200  71.74100  1.000 34.91862 ? 66  ARG B CG  1 
ATOM   3503 C CD  . ARG B 1 66  ? 18.93200  34.67600  72.67800  1.000 31.66327 ? 66  ARG B CD  1 
ATOM   3504 N NE  . ARG B 1 66  ? 17.98100  35.75100  72.93900  1.000 37.27953 ? 66  ARG B NE  1 
ATOM   3505 C CZ  . ARG B 1 66  ? 17.81600  36.34600  74.11200  1.000 34.03845 ? 66  ARG B CZ  1 
ATOM   3506 N NH1 . ARG B 1 66  ? 18.47300  35.94900  75.19000  1.000 31.68317 ? 66  ARG B NH1 1 
ATOM   3507 N NH2 . ARG B 1 66  ? 16.96500  37.36400  74.20900  1.000 39.06804 ? 66  ARG B NH2 1 
ATOM   3508 N N   . PHE B 1 67  ? 21.84100  38.95000  70.18000  1.000 48.81772 ? 67  PHE B N   1 
ATOM   3509 C CA  . PHE B 1 67  ? 21.62100  39.73800  68.97300  1.000 48.50604 ? 67  PHE B CA  1 
ATOM   3510 C C   . PHE B 1 67  ? 22.75800  40.68800  68.60900  1.000 42.37589 ? 67  PHE B C   1 
ATOM   3511 O O   . PHE B 1 67  ? 22.75200  41.20600  67.48600  1.000 43.59950 ? 67  PHE B O   1 
ATOM   3512 C CB  . PHE B 1 67  ? 20.29800  40.53100  69.05400  1.000 50.09732 ? 67  PHE B CB  1 
ATOM   3513 C CG  . PHE B 1 67  ? 19.97000  41.10600  70.42200  1.000 52.23205 ? 67  PHE B CG  1 
ATOM   3514 C CD1 . PHE B 1 67  ? 19.42800  40.30700  71.42700  1.000 50.44738 ? 67  PHE B CD1 1 
ATOM   3515 C CD2 . PHE B 1 67  ? 20.13400  42.46300  70.67300  1.000 50.71711 ? 67  PHE B CD2 1 
ATOM   3516 C CE1 . PHE B 1 67  ? 19.09600  40.84400  72.66900  1.000 49.29106 ? 67  PHE B CE1 1 
ATOM   3517 C CE2 . PHE B 1 67  ? 19.80600  43.00500  71.91500  1.000 51.02669 ? 67  PHE B CE2 1 
ATOM   3518 C CZ  . PHE B 1 67  ? 19.28600  42.19400  72.91200  1.000 47.23468 ? 67  PHE B CZ  1 
ATOM   3519 N N   . THR B 1 68  ? 23.73300  40.91900  69.49100  1.000 38.85465 ? 68  THR B N   1 
ATOM   3520 C CA  . THR B 1 68  ? 24.91700  41.71700  69.16000  1.000 37.50080 ? 68  THR B CA  1 
ATOM   3521 C C   . THR B 1 68  ? 26.12500  41.11700  69.86300  1.000 34.35301 ? 68  THR B C   1 
ATOM   3522 O O   . THR B 1 68  ? 26.26500  41.24800  71.08300  1.000 39.63356 ? 68  THR B O   1 
ATOM   3523 C CB  . THR B 1 68  ? 24.75300  43.18500  69.56700  1.000 43.34768 ? 68  THR B CB  1 
ATOM   3524 O OG1 . THR B 1 68  ? 24.12500  43.26200  70.85700  1.000 42.62526 ? 68  THR B OG1 1 
ATOM   3525 C CG2 . THR B 1 68  ? 23.94300  43.95800  68.53100  1.000 44.92104 ? 68  THR B CG2 1 
ATOM   3526 N N   . ASN B 1 69  ? 27.00100  40.47100  69.10000  1.000 27.02668 ? 69  ASN B N   1 
ATOM   3527 C CA  . ASN B 1 69  ? 28.27700  40.00000  69.61200  1.000 23.50605 ? 69  ASN B CA  1 
ATOM   3528 C C   . ASN B 1 69  ? 29.34600  40.39400  68.60100  1.000 20.55070 ? 69  ASN B C   1 
ATOM   3529 O O   . ASN B 1 69  ? 29.20400  40.08200  67.40600  1.000 17.05246 ? 69  ASN B O   1 
ATOM   3530 C CB  . ASN B 1 69  ? 28.28900  38.47800  69.84300  1.000 21.98611 ? 69  ASN B CB  1 
ATOM   3531 C CG  . ASN B 1 69  ? 29.64800  37.97300  70.29000  1.000 19.92996 ? 69  ASN B CG  1 
ATOM   3532 O OD1 . ASN B 1 69  ? 30.56200  37.82100  69.47700  1.000 19.32929 ? 69  ASN B OD1 1 
ATOM   3533 N ND2 . ASN B 1 69  ? 29.79400  37.72500  71.59000  1.000 21.61369 ? 69  ASN B ND2 1 
ATOM   3534 N N   . PRO B 1 70  ? 30.41600  41.07700  69.03100  1.000 21.96231 ? 70  PRO B N   1 
ATOM   3535 C CA  . PRO B 1 70  ? 31.40100  41.59100  68.06000  1.000 19.96281 ? 70  PRO B CA  1 
ATOM   3536 C C   . PRO B 1 70  ? 32.04100  40.51500  67.19800  1.000 20.79604 ? 70  PRO B C   1 
ATOM   3537 O O   . PRO B 1 70  ? 32.29500  40.75700  66.01100  1.000 18.91726 ? 70  PRO B O   1 
ATOM   3538 C CB  . PRO B 1 70  ? 32.44400  42.28800  68.95300  1.000 19.12353 ? 70  PRO B CB  1 
ATOM   3539 C CG  . PRO B 1 70  ? 31.73800  42.55300  70.25000  1.000 20.32459 ? 70  PRO B CG  1 
ATOM   3540 C CD  . PRO B 1 70  ? 30.74300  41.45300  70.41900  1.000 19.93447 ? 70  PRO B CD  1 
ATOM   3541 N N   . THR B 1 71  ? 32.32700  39.33600  67.76200  1.000 19.48384 ? 71  THR B N   1 
ATOM   3542 C CA  . THR B 1 71  ? 32.93900  38.27500  66.96800  1.000 16.08640 ? 71  THR B CA  1 
ATOM   3543 C C   . THR B 1 71  ? 31.97400  37.76500  65.90600  1.000 18.74045 ? 71  THR B C   1 
ATOM   3544 O O   . THR B 1 71  ? 32.36500  37.56200  64.75000  1.000 12.56108 ? 71  THR B O   1 
ATOM   3545 C CB  . THR B 1 71  ? 33.40100  37.12700  67.87200  1.000 16.26357 ? 71  THR B CB  1 
ATOM   3546 O OG1 . THR B 1 71  ? 34.25600  37.63700  68.90200  1.000 16.75753 ? 71  THR B OG1 1 
ATOM   3547 C CG2 . THR B 1 71  ? 34.16800  36.07300  67.06600  1.000 12.86861 ? 71  THR B CG2 1 
ATOM   3548 N N   . VAL B 1 72  ? 30.70500  37.56600  66.28100  1.000 16.54331 ? 72  VAL B N   1 
ATOM   3549 C CA  . VAL B 1 72  ? 29.69100  37.13500  65.31900  1.000 16.76734 ? 72  VAL B CA  1 
ATOM   3550 C C   . VAL B 1 72  ? 29.49500  38.19800  64.24700  1.000 16.55296 ? 72  VAL B C   1 
ATOM   3551 O O   . VAL B 1 72  ? 29.32800  37.88600  63.06200  1.000 14.08106 ? 72  VAL B O   1 
ATOM   3552 C CB  . VAL B 1 72  ? 28.36800  36.81300  66.04100  1.000 14.02242 ? 72  VAL B CB  1 
ATOM   3553 C CG1 . VAL B 1 72  ? 27.27300  36.44900  65.03900  1.000 10.48115 ? 72  VAL B CG1 1 
ATOM   3554 C CG2 . VAL B 1 72  ? 28.56800  35.69800  67.04800  1.000 14.71715 ? 72  VAL B CG2 1 
ATOM   3555 N N   . ARG B 1 73  ? 29.51900  39.47100  64.65100  1.000 17.55210 ? 73  ARG B N   1 
ATOM   3556 C CA  . ARG B 1 73  ? 29.31800  40.57100  63.71300  1.000 16.67113 ? 73  ARG B CA  1 
ATOM   3557 C C   . ARG B 1 73  ? 30.39400  40.58400  62.63600  1.000 19.87752 ? 73  ARG B C   1 
ATOM   3558 O O   . ARG B 1 73  ? 30.11100  40.87800  61.46700  1.000 20.88235 ? 73  ARG B O   1 
ATOM   3559 C CB  . ARG B 1 73  ? 29.29700  41.89500  64.47600  1.000 19.51165 ? 73  ARG B CB  1 
ATOM   3560 C CG  . ARG B 1 73  ? 29.30800  43.12700  63.60800  1.000 24.38024 ? 73  ARG B CG  1 
ATOM   3561 C CD  . ARG B 1 73  ? 29.76100  44.33400  64.40900  1.000 23.00228 ? 73  ARG B CD  1 
ATOM   3562 N NE  . ARG B 1 73  ? 29.88800  45.51600  63.56700  1.000 30.64864 ? 73  ARG B NE  1 
ATOM   3563 C CZ  . ARG B 1 73  ? 30.26700  46.71100  64.00000  1.000 36.38535 ? 73  ARG B CZ  1 
ATOM   3564 N NH1 . ARG B 1 73  ? 30.59700  46.91700  65.26600  1.000 33.05268 ? 73  ARG B NH1 1 
ATOM   3565 N NH2 . ARG B 1 73  ? 30.30800  47.72800  63.14300  1.000 37.99141 ? 73  ARG B NH2 1 
ATOM   3566 N N   . THR B 1 74  ? 31.63800  40.27900  63.00900  1.000 16.53849 ? 74  THR B N   1 
ATOM   3567 C CA  . THR B 1 74  ? 32.70600  40.22100  62.01500  1.000 18.03788 ? 74  THR B CA  1 
ATOM   3568 C C   . THR B 1 74  ? 32.44100  39.12000  60.99300  1.000 18.50133 ? 74  THR B C   1 
ATOM   3569 O O   . THR B 1 74  ? 32.63000  39.32100  59.78800  1.000 19.04924 ? 74  THR B O   1 
ATOM   3570 C CB  . THR B 1 74  ? 34.05700  40.01900  62.70900  1.000 16.90289 ? 74  THR B CB  1 
ATOM   3571 O OG1 . THR B 1 74  ? 34.37400  41.17400  63.49800  1.000 21.09900 ? 74  THR B OG1 1 
ATOM   3572 C CG2 . THR B 1 74  ? 35.15900  39.79400  61.70000  1.000 13.82016 ? 74  THR B CG2 1 
ATOM   3573 N N   . PHE B 1 75  ? 31.98700  37.95300  61.45400  1.000 16.23590 ? 75  PHE B N   1 
ATOM   3574 C CA  . PHE B 1 75  ? 31.65600  36.87200  60.53000  1.000 15.38326 ? 75  PHE B CA  1 
ATOM   3575 C C   . PHE B 1 75  ? 30.53100  37.27900  59.58400  1.000 15.29105 ? 75  PHE B C   1 
ATOM   3576 O O   . PHE B 1 75  ? 30.63700  37.09900  58.36400  1.000 15.92057 ? 75  PHE B O   1 
ATOM   3577 C CB  . PHE B 1 75  ? 31.27600  35.62100  61.31600  1.000 15.35917 ? 75  PHE B CB  1 
ATOM   3578 C CG  . PHE B 1 75  ? 30.69000  34.53200  60.47300  1.000 16.17497 ? 75  PHE B CG  1 
ATOM   3579 C CD1 . PHE B 1 75  ? 31.47700  33.84200  59.56700  1.000 13.20138 ? 75  PHE B CD1 1 
ATOM   3580 C CD2 . PHE B 1 75  ? 29.35100  34.19500  60.59100  1.000 13.95760 ? 75  PHE B CD2 1 
ATOM   3581 C CE1 . PHE B 1 75  ? 30.94400  32.83600  58.79000  1.000 14.08784 ? 75  PHE B CE1 1 
ATOM   3582 C CE2 . PHE B 1 75  ? 28.80600  33.18600  59.82500  1.000 16.59481 ? 75  PHE B CE2 1 
ATOM   3583 C CZ  . PHE B 1 75  ? 29.60500  32.50200  58.92000  1.000 17.67195 ? 75  PHE B CZ  1 
ATOM   3584 N N   . GLU B 1 76  ? 29.45600  37.85900  60.12700  1.000 15.56663 ? 76  GLU B N   1 
ATOM   3585 C CA  . GLU B 1 76  ? 28.30900  38.24000  59.30200  1.000 15.50631 ? 76  GLU B CA  1 
ATOM   3586 C C   . GLU B 1 76  ? 28.69900  39.25900  58.23800  1.000 18.48425 ? 76  GLU B C   1 
ATOM   3587 O O   . GLU B 1 76  ? 28.39800  39.08400  57.05000  1.000 18.08859 ? 76  GLU B O   1 
ATOM   3588 C CB  . GLU B 1 76  ? 27.19300  38.80200  60.18400  1.000 14.89243 ? 76  GLU B CB  1 
ATOM   3589 C CG  . GLU B 1 76  ? 26.55400  37.79000  61.10800  1.000 16.03449 ? 76  GLU B CG  1 
ATOM   3590 C CD  . GLU B 1 76  ? 25.62900  38.43900  62.12000  1.000 18.53061 ? 76  GLU B CD  1 
ATOM   3591 O OE1 . GLU B 1 76  ? 25.74400  39.66100  62.33100  1.000 19.11523 ? 76  GLU B OE1 1 
ATOM   3592 O OE2 . GLU B 1 76  ? 24.78100  37.73100  62.70000  1.000 19.12981 ? 76  GLU B OE2 1 
ATOM   3593 N N   . GLU B 1 77  ? 29.37500  40.33500  58.64700  1.000 15.77812 ? 77  GLU B N   1 
ATOM   3594 C CA  . GLU B 1 77  ? 29.75900  41.37000  57.69400  1.000 19.89658 ? 77  GLU B CA  1 
ATOM   3595 C C   . GLU B 1 77  ? 30.71300  40.82000  56.64000  1.000 16.44534 ? 77  GLU B C   1 
ATOM   3596 O O   . GLU B 1 77  ? 30.60700  41.16200  55.45800  1.000 19.62486 ? 77  GLU B O   1 
ATOM   3597 C CB  . GLU B 1 77  ? 30.38700  42.55500  58.43300  1.000 17.03360 ? 77  GLU B CB  1 
ATOM   3598 C CG  . GLU B 1 77  ? 29.42300  43.26800  59.37100  1.000 20.08789 ? 77  GLU B CG  1 
ATOM   3599 C CD  . GLU B 1 77  ? 30.06400  44.42800  60.10900  1.000 25.03627 ? 77  GLU B CD  1 
ATOM   3600 O OE1 . GLU B 1 77  ? 31.27300  44.68100  59.90400  1.000 24.98712 ? 77  GLU B OE1 1 
ATOM   3601 O OE2 . GLU B 1 77  ? 29.35600  45.08400  60.89900  1.000 26.80741 ? 77  GLU B OE2 1 
ATOM   3602 N N   . ARG B 1 78  ? 31.64600  39.96100  57.05000  1.000 15.46188 ? 78  ARG B N   1 
ATOM   3603 C CA  . ARG B 1 78  ? 32.59100  39.38400  56.10000  1.000 17.92747 ? 78  ARG B CA  1 
ATOM   3604 C C   . ARG B 1 78  ? 31.88200  38.48700  55.09100  1.000 17.29919 ? 78  ARG B C   1 
ATOM   3605 O O   . ARG B 1 78  ? 32.11600  38.59200  53.87900  1.000 16.89671 ? 78  ARG B O   1 
ATOM   3606 C CB  . ARG B 1 78  ? 33.67200  38.61200  56.85300  1.000 13.87387 ? 78  ARG B CB  1 
ATOM   3607 C CG  . ARG B 1 78  ? 34.78900  38.07200  55.97500  1.000 17.94343 ? 78  ARG B CG  1 
ATOM   3608 C CD  . ARG B 1 78  ? 35.93800  37.54400  56.82800  1.000 17.38881 ? 78  ARG B CD  1 
ATOM   3609 N NE  . ARG B 1 78  ? 36.59100  38.61500  57.57400  1.000 18.46209 ? 78  ARG B NE  1 
ATOM   3610 C CZ  . ARG B 1 78  ? 37.68500  38.46000  58.30700  1.000 20.94581 ? 78  ARG B CZ  1 
ATOM   3611 N NH1 . ARG B 1 78  ? 38.27100  37.27600  58.43800  1.000 15.65944 ? 78  ARG B NH1 1 
ATOM   3612 N NH2 . ARG B 1 78  ? 38.20800  39.51800  58.92100  1.000 19.23532 ? 78  ARG B NH2 1 
ATOM   3613 N N   . LEU B 1 79  ? 31.00400  37.60100  55.57100  1.000 16.84874 ? 79  LEU B N   1 
ATOM   3614 C CA  . LEU B 1 79  ? 30.28100  36.71700  54.66300  1.000 14.90604 ? 79  LEU B CA  1 
ATOM   3615 C C   . LEU B 1 79  ? 29.34700  37.51000  53.75700  1.000 17.09877 ? 79  LEU B C   1 
ATOM   3616 O O   . LEU B 1 79  ? 29.29900  37.26800  52.54600  1.000 15.55116 ? 79  LEU B O   1 
ATOM   3617 C CB  . LEU B 1 79  ? 29.50800  35.66700  55.46100  1.000 14.25202 ? 79  LEU B CB  1 
ATOM   3618 C CG  . LEU B 1 79  ? 28.65800  34.65500  54.68900  1.000 16.24710 ? 79  LEU B CG  1 
ATOM   3619 C CD1 . LEU B 1 79  ? 29.49400  33.90800  53.68700  1.000 10.07624 ? 79  LEU B CD1 1 
ATOM   3620 C CD2 . LEU B 1 79  ? 27.99800  33.67700  55.64700  1.000 16.59875 ? 79  LEU B CD2 1 
ATOM   3621 N N   . ALA B 1 80  ? 28.62700  38.48500  54.32300  1.000 18.13513 ? 80  ALA B N   1 
ATOM   3622 C CA  . ALA B 1 80  ? 27.76600  39.34700  53.51800  1.000 18.39665 ? 80  ALA B CA  1 
ATOM   3623 C C   . ALA B 1 80  ? 28.54700  39.99400  52.38600  1.000 18.86737 ? 80  ALA B C   1 
ATOM   3624 O O   . ALA B 1 80  ? 28.11400  39.98100  51.22700  1.000 15.08732 ? 80  ALA B O   1 
ATOM   3625 C CB  . ALA B 1 80  ? 27.12500  40.42200  54.39700  1.000 15.62718 ? 80  ALA B CB  1 
ATOM   3626 N N   . ALA B 1 81  ? 29.71800  40.55000  52.70300  1.000 20.55540 ? 81  ALA B N   1 
ATOM   3627 C CA  . ALA B 1 81  ? 30.52300  41.20300  51.67900  1.000 19.59119 ? 81  ALA B CA  1 
ATOM   3628 C C   . ALA B 1 81  ? 30.95800  40.22000  50.60400  1.000 16.83010 ? 81  ALA B C   1 
ATOM   3629 O O   . ALA B 1 81  ? 31.12500  40.60600  49.44400  1.000 23.16225 ? 81  ALA B O   1 
ATOM   3630 C CB  . ALA B 1 81  ? 31.73800  41.87900  52.31700  1.000 16.46991 ? 81  ALA B CB  1 
ATOM   3631 N N   . LEU B 1 82  ? 31.14500  38.94900  50.96200  1.000 18.53165 ? 82  LEU B N   1 
ATOM   3632 C CA  . LEU B 1 82  ? 31.52100  37.96400  49.95500  1.000 18.56711 ? 82  LEU B CA  1 
ATOM   3633 C C   . LEU B 1 82  ? 30.34400  37.55900  49.08100  1.000 15.41059 ? 82  LEU B C   1 
ATOM   3634 O O   . LEU B 1 82  ? 30.54800  37.10800  47.94900  1.000 20.86257 ? 82  LEU B O   1 
ATOM   3635 C CB  . LEU B 1 82  ? 32.12900  36.73500  50.61900  1.000 14.21755 ? 82  LEU B CB  1 
ATOM   3636 C CG  . LEU B 1 82  ? 33.51100  37.00500  51.20800  1.000 22.17779 ? 82  LEU B CG  1 
ATOM   3637 C CD1 . LEU B 1 82  ? 34.08200  35.74100  51.81700  1.000 18.40364 ? 82  LEU B CD1 1 
ATOM   3638 C CD2 . LEU B 1 82  ? 34.44600  37.56800  50.13900  1.000 16.93973 ? 82  LEU B CD2 1 
ATOM   3639 N N   . GLU B 1 83  ? 29.12200  37.68700  49.58300  1.000 14.59395 ? 83  GLU B N   1 
ATOM   3640 C CA  . GLU B 1 83  ? 27.93300  37.42100  48.78700  1.000 18.64897 ? 83  GLU B CA  1 
ATOM   3641 C C   . GLU B 1 83  ? 27.41700  38.66000  48.06700  1.000 19.07757 ? 83  GLU B C   1 
ATOM   3642 O O   . GLU B 1 83  ? 26.47500  38.55200  47.27600  1.000 23.75911 ? 83  GLU B O   1 
ATOM   3643 C CB  . GLU B 1 83  ? 26.82200  36.83400  49.67400  1.000 19.78164 ? 83  GLU B CB  1 
ATOM   3644 C CG  . GLU B 1 83  ? 27.01800  35.36100  50.07100  1.000 17.98703 ? 83  GLU B CG  1 
ATOM   3645 C CD  . GLU B 1 83  ? 26.64500  34.38500  48.95600  1.000 22.04730 ? 83  GLU B CD  1 
ATOM   3646 O OE1 . GLU B 1 83  ? 26.12000  34.83300  47.91400  1.000 18.92863 ? 83  GLU B OE1 1 
ATOM   3647 O OE2 . GLU B 1 83  ? 26.87900  33.16700  49.12100  1.000 19.76781 ? 83  GLU B OE2 1 
ATOM   3648 N N   . GLY B 1 84  ? 28.01300  39.82800  48.30600  1.000 20.43619 ? 84  GLY B N   1 
ATOM   3649 C CA  . GLY B 1 84  ? 27.47600  41.04700  47.73700  1.000 18.73767 ? 84  GLY B CA  1 
ATOM   3650 C C   . GLY B 1 84  ? 26.17200  41.47700  48.35800  1.000 19.17105 ? 84  GLY B C   1 
ATOM   3651 O O   . GLY B 1 84  ? 25.43300  42.26300  47.75700  1.000 24.21201 ? 84  GLY B O   1 
ATOM   3652 N N   . ALA B 1 85  ? 25.87000  40.97600  49.55000  1.000 19.24697 ? 85  ALA B N   1 
ATOM   3653 C CA  . ALA B 1 85  ? 24.64000  41.28100  50.25700  1.000 15.82184 ? 85  ALA B CA  1 
ATOM   3654 C C   . ALA B 1 85  ? 24.82900  42.49100  51.15900  1.000 21.80257 ? 85  ALA B C   1 
ATOM   3655 O O   . ALA B 1 85  ? 25.94300  42.80300  51.58900  1.000 21.55160 ? 85  ALA B O   1 
ATOM   3656 C CB  . ALA B 1 85  ? 24.19400  40.07700  51.09000  1.000 17.80363 ? 85  ALA B CB  1 
ATOM   3657 N N   . GLU B 1 86  ? 23.72100  43.17800  51.44200  1.000 20.63324 ? 86  GLU B N   1 
ATOM   3658 C CA  . GLU B 1 86  ? 23.78200  44.30200  52.36900  1.000 19.01501 ? 86  GLU B CA  1 
ATOM   3659 C C   . GLU B 1 86  ? 23.93900  43.82300  53.80200  1.000 23.37570 ? 86  GLU B C   1 
ATOM   3660 O O   . GLU B 1 86  ? 24.61900  44.46800  54.60900  1.000 24.83248 ? 86  GLU B O   1 
ATOM   3661 C CB  . GLU B 1 86  ? 22.52900  45.16500  52.24300  1.000 19.77084 ? 86  GLU B CB  1 
ATOM   3662 C CG  . GLU B 1 86  ? 22.40100  45.87700  50.92000  1.000 25.11727 ? 86  GLU B CG  1 
ATOM   3663 C CD  . GLU B 1 86  ? 21.08100  46.59900  50.78300  1.000 24.03116 ? 86  GLU B CD  1 
ATOM   3664 O OE1 . GLU B 1 86  ? 20.22200  46.44400  51.67500  1.000 18.65685 ? 86  GLU B OE1 1 
ATOM   3665 O OE2 . GLU B 1 86  ? 20.90000  47.32100  49.77900  1.000 32.75688 ? 86  GLU B OE2 1 
ATOM   3666 N N   . ALA B 1 87  ? 23.31000  42.70000  54.13900  1.000 21.96684 ? 87  ALA B N   1 
ATOM   3667 C CA  . ALA B 1 87  ? 23.20900  42.26300  55.52000  1.000 21.62525 ? 87  ALA B CA  1 
ATOM   3668 C C   . ALA B 1 87  ? 23.32000  40.74800  55.59600  1.000 21.55614 ? 87  ALA B C   1 
ATOM   3669 O O   . ALA B 1 87  ? 23.06700  40.02800  54.62800  1.000 18.07107 ? 87  ALA B O   1 
ATOM   3670 C CB  . ALA B 1 87  ? 21.89200  42.72200  56.15900  1.000 19.19264 ? 87  ALA B CB  1 
ATOM   3671 N N   . CYS B 1 88  ? 23.70500  40.27800  56.77800  1.000 22.34752 ? 88  CYS B N   1 
ATOM   3672 C CA  . CYS B 1 88  ? 23.76300  38.85900  57.07500  1.000 18.29680 ? 88  CYS B CA  1 
ATOM   3673 C C   . CYS B 1 88  ? 23.49100  38.67800  58.55900  1.000 18.30928 ? 88  CYS B C   1 
ATOM   3674 O O   . CYS B 1 88  ? 23.87900  39.52600  59.36900  1.000 19.50361 ? 88  CYS B O   1 
ATOM   3675 C CB  . CYS B 1 88  ? 25.12400  38.27300  56.69500  1.000 18.93206 ? 88  CYS B CB  1 
ATOM   3676 S SG  . CYS B 1 88  ? 25.37700  36.59300  57.24900  1.000 20.15480 ? 88  CYS B SG  1 
ATOM   3677 N N   . VAL B 1 89  ? 22.80800  37.59300  58.91300  1.000 16.43206 ? 89  VAL B N   1 
ATOM   3678 C CA  . VAL B 1 89  ? 22.60000  37.23400  60.31300  1.000 19.27176 ? 89  VAL B CA  1 
ATOM   3679 C C   . VAL B 1 89  ? 22.99500  35.77600  60.50100  1.000 16.59906 ? 89  VAL B C   1 
ATOM   3680 O O   . VAL B 1 89  ? 22.59600  34.90900  59.71500  1.000 16.87337 ? 89  VAL B O   1 
ATOM   3681 C CB  . VAL B 1 89  ? 21.15400  37.48800  60.78600  1.000 18.39148 ? 89  VAL B CB  1 
ATOM   3682 C CG1 . VAL B 1 89  ? 20.13900  36.71200  59.95000  1.000 16.10793 ? 89  VAL B CG1 1 
ATOM   3683 C CG2 . VAL B 1 89  ? 21.02000  37.16300  62.28400  1.000 16.75052 ? 89  VAL B CG2 1 
ATOM   3684 N N   . ALA B 1 90  ? 23.80500  35.51600  61.51700  1.000 13.30421 ? 90  ALA B N   1 
ATOM   3685 C CA  . ALA B 1 90  ? 24.37900  34.20100  61.73100  1.000 15.14338 ? 90  ALA B CA  1 
ATOM   3686 C C   . ALA B 1 90  ? 23.46800  33.36000  62.61000  1.000 17.11176 ? 90  ALA B C   1 
ATOM   3687 O O   . ALA B 1 90  ? 22.71200  33.88100  63.43400  1.000 15.12784 ? 90  ALA B O   1 
ATOM   3688 C CB  . ALA B 1 90  ? 25.76400  34.31400  62.37200  1.000 13.10959 ? 90  ALA B CB  1 
ATOM   3689 N N   . THR B 1 91  ? 23.56400  32.04300  62.43400  1.000 16.32770 ? 91  THR B N   1 
ATOM   3690 C CA  . THR B 1 91  ? 22.73000  31.08000  63.13400  1.000 16.98237 ? 91  THR B CA  1 
ATOM   3691 C C   . THR B 1 91  ? 23.58800  29.93700  63.65900  1.000 15.28712 ? 91  THR B C   1 
ATOM   3692 O O   . THR B 1 91  ? 24.73500  29.74700  63.24600  1.000 17.82595 ? 91  THR B O   1 
ATOM   3693 C CB  . THR B 1 91  ? 21.64100  30.51100  62.22100  1.000 16.38185 ? 91  THR B CB  1 
ATOM   3694 O OG1 . THR B 1 91  ? 22.26300  29.87200  61.09800  1.000 16.83506 ? 91  THR B OG1 1 
ATOM   3695 C CG2 . THR B 1 91  ? 20.71400  31.61300  61.72800  1.000 15.42293 ? 91  THR B CG2 1 
ATOM   3696 N N   . ALA B 1 92  ? 23.00100  29.15900  64.56900  1.000 15.16362 ? 92  ALA B N   1 
ATOM   3697 C CA  . ALA B 1 92  ? 23.72800  28.07600  65.21900  1.000 16.31029 ? 92  ALA B CA  1 
ATOM   3698 C C   . ALA B 1 92  ? 24.14400  26.98200  64.25000  1.000 14.88186 ? 92  ALA B C   1 
ATOM   3699 O O   . ALA B 1 92  ? 25.09900  26.25300  64.53600  1.000 14.41142 ? 92  ALA B O   1 
ATOM   3700 C CB  . ALA B 1 92  ? 22.87900  27.47100  66.33700  1.000 15.17229 ? 92  ALA B CB  1 
ATOM   3701 N N   . SER B 1 93  ? 23.44600  26.84400  63.12500  1.000 12.68139 ? 93  SER B N   1 
ATOM   3702 C CA  . SER B 1 93  ? 23.72800  25.80600  62.14500  1.000 13.55949 ? 93  SER B CA  1 
ATOM   3703 C C   . SER B 1 93  ? 23.06600  26.20200  60.83400  1.000 14.11822 ? 93  SER B C   1 
ATOM   3704 O O   . SER B 1 93  ? 22.26300  27.13800  60.77800  1.000 15.07541 ? 93  SER B O   1 
ATOM   3705 C CB  . SER B 1 93  ? 23.22900  24.43500  62.61500  1.000 10.73616 ? 93  SER B CB  1 
ATOM   3706 O OG  . SER B 1 93  ? 21.82200  24.45900  62.77400  1.000 15.37916 ? 93  SER B OG  1 
ATOM   3707 N N   . GLY B 1 94  ? 23.42400  25.47800  59.77200  1.000 13.34043 ? 94  GLY B N   1 
ATOM   3708 C CA  . GLY B 1 94  ? 22.77000  25.69500  58.49200  1.000 15.46812 ? 94  GLY B CA  1 
ATOM   3709 C C   . GLY B 1 94  ? 21.27800  25.42300  58.55900  1.000 16.67096 ? 94  GLY B C   1 
ATOM   3710 O O   . GLY B 1 94  ? 20.47400  26.16900  57.99200  1.000 15.25415 ? 94  GLY B O   1 
ATOM   3711 N N   . MET B 1 95  ? 20.88800  24.35600  59.26200  1.000 13.43661 ? 95  MET B N   1 
ATOM   3712 C CA  . MET B 1 95  ? 19.46900  24.09000  59.47000  1.000 15.87057 ? 95  MET B CA  1 
ATOM   3713 C C   . MET B 1 95  ? 18.79900  25.23500  60.21400  1.000 14.48274 ? 95  MET B C   1 
ATOM   3714 O O   . MET B 1 95  ? 17.67300  25.62000  59.88700  1.000 16.25622 ? 95  MET B O   1 
ATOM   3715 C CB  . MET B 1 95  ? 19.27200  22.77600  60.23100  1.000 14.47853 ? 95  MET B CB  1 
ATOM   3716 C CG  . MET B 1 95  ? 19.55700  21.51800  59.41800  1.000 14.66483 ? 95  MET B CG  1 
ATOM   3717 S SD  . MET B 1 95  ? 18.86300  21.54600  57.74500  1.000 18.29921 ? 95  MET B SD  1 
ATOM   3718 C CE  . MET B 1 95  ? 17.15600  21.98800  58.04600  1.000 12.55933 ? 95  MET B CE  1 
ATOM   3719 N N   . ALA B 1 96  ? 19.47100  25.79200  61.22200  1.000 12.79458 ? 96  ALA B N   1 
ATOM   3720 C CA  . ALA B 1 96  ? 18.89600  26.94400  61.90200  1.000 15.47452 ? 96  ALA B CA  1 
ATOM   3721 C C   . ALA B 1 96  ? 18.79900  28.14500  60.96900  1.000 15.57894 ? 96  ALA B C   1 
ATOM   3722 O O   . ALA B 1 96  ? 17.93100  29.00300  61.15700  1.000 15.79431 ? 96  ALA B O   1 
ATOM   3723 C CB  . ALA B 1 96  ? 19.70700  27.28600  63.15300  1.000 12.31207 ? 96  ALA B CB  1 
ATOM   3724 N N   . ALA B 1 97  ? 19.67500  28.22800  59.96300  1.000 15.96782 ? 97  ALA B N   1 
ATOM   3725 C CA  . ALA B 1 97  ? 19.52500  29.27000  58.95300  1.000 15.35253 ? 97  ALA B CA  1 
ATOM   3726 C C   . ALA B 1 97  ? 18.29200  29.02100  58.09000  1.000 15.09596 ? 97  ALA B C   1 
ATOM   3727 O O   . ALA B 1 97  ? 17.57700  29.96500  57.73400  1.000 14.54181 ? 97  ALA B O   1 
ATOM   3728 C CB  . ALA B 1 97  ? 20.78500  29.36100  58.08800  1.000 15.25622 ? 97  ALA B CB  1 
ATOM   3729 N N   . CYS B 1 98  ? 18.03200  27.76000  57.73300  1.000 13.66958 ? 98  CYS B N   1 
ATOM   3730 C CA  . CYS B 1 98  ? 16.79000  27.43100  57.04100  1.000 14.47913 ? 98  CYS B CA  1 
ATOM   3731 C C   . CYS B 1 98  ? 15.58600  27.74700  57.91500  1.000 18.78004 ? 98  CYS B C   1 
ATOM   3732 O O   . CYS B 1 98  ? 14.61200  28.35800  57.45600  1.000 15.45013 ? 98  CYS B O   1 
ATOM   3733 C CB  . CYS B 1 98  ? 16.78200  25.95900  56.63800  1.000 17.26826 ? 98  CYS B CB  1 
ATOM   3734 S SG  . CYS B 1 98  ? 18.03000  25.51100  55.41000  1.000 18.46807 ? 98  CYS B SG  1 
ATOM   3735 N N   . LEU B 1 99  ? 15.64800  27.35900  59.19300  1.000 13.36842 ? 99  LEU B N   1 
ATOM   3736 C CA  . LEU B 1 99  ? 14.57400  27.69800  60.11900  1.000 14.70813 ? 99  LEU B CA  1 
ATOM   3737 C C   . LEU B 1 99  ? 14.33600  29.20300  60.14800  1.000 17.84022 ? 99  LEU B C   1 
ATOM   3738 O O   . LEU B 1 99  ? 13.18900  29.66200  60.10700  1.000 16.58987 ? 99  LEU B O   1 
ATOM   3739 C CB  . LEU B 1 99  ? 14.91600  27.18000  61.51500  1.000 16.95648 ? 99  LEU B CB  1 
ATOM   3740 C CG  . LEU B 1 99  ? 13.92900  27.50300  62.63600  1.000 16.49828 ? 99  LEU B CG  1 
ATOM   3741 C CD1 . LEU B 1 99  ? 12.67900  26.64300  62.51000  1.000 18.14503 ? 99  LEU B CD1 1 
ATOM   3742 C CD2 . LEU B 1 99  ? 14.58200  27.32000  63.98900  1.000 15.64346 ? 99  LEU B CD2 1 
ATOM   3743 N N   . THR B 1 100 ? 15.41800  29.98800  60.18100  1.000 20.37750 ? 100 THR B N   1 
ATOM   3744 C CA  . THR B 1 100 ? 15.29800  31.44200  60.25200  1.000 19.69146 ? 100 THR B CA  1 
ATOM   3745 C C   . THR B 1 100 ? 14.64900  32.01900  58.99500  1.000 18.54140 ? 100 THR B C   1 
ATOM   3746 O O   . THR B 1 100 ? 13.76600  32.88100  59.08400  1.000 15.39225 ? 100 THR B O   1 
ATOM   3747 C CB  . THR B 1 100 ? 16.68000  32.05700  60.49100  1.000 16.48347 ? 100 THR B CB  1 
ATOM   3748 O OG1 . THR B 1 100 ? 17.19000  31.59000  61.74700  1.000 17.72051 ? 100 THR B OG1 1 
ATOM   3749 C CG2 . THR B 1 100 ? 16.61200  33.58700  60.50800  1.000 13.44413 ? 100 THR B CG2 1 
ATOM   3750 N N   . ALA B 1 101 ? 15.06700  31.55800  57.81500  1.000 18.33845 ? 101 ALA B N   1 
ATOM   3751 C CA  . ALA B 1 101 ? 14.47300  32.07200  56.58600  1.000 18.27730 ? 101 ALA B CA  1 
ATOM   3752 C C   . ALA B 1 101 ? 12.98600  31.74900  56.51600  1.000 20.69014 ? 101 ALA B C   1 
ATOM   3753 O O   . ALA B 1 101 ? 12.17800  32.60100  56.13400  1.000 20.66811 ? 101 ALA B O   1 
ATOM   3754 C CB  . ALA B 1 101 ? 15.19600  31.50700  55.36600  1.000 14.05068 ? 101 ALA B CB  1 
ATOM   3755 N N   . PHE B 1 102 ? 12.60600  30.52200  56.88300  1.000 18.76856 ? 102 PHE B N   1 
ATOM   3756 C CA  . PHE B 1 102 ? 11.20600  30.11600  56.80800  1.000 16.79886 ? 102 PHE B CA  1 
ATOM   3757 C C   . PHE B 1 102 ? 10.36200  30.85600  57.83600  1.000 18.79128 ? 102 PHE B C   1 
ATOM   3758 O O   . PHE B 1 102 ? 9.35500   31.48200  57.49800  1.000 20.61859 ? 102 PHE B O   1 
ATOM   3759 C CB  . PHE B 1 102 ? 11.07700  28.60700  57.02900  1.000 19.14423 ? 102 PHE B CB  1 
ATOM   3760 C CG  . PHE B 1 102 ? 11.83000  27.77200  56.03800  1.000 19.45684 ? 102 PHE B CG  1 
ATOM   3761 C CD1 . PHE B 1 102 ? 11.98000  28.18800  54.72600  1.000 21.52274 ? 102 PHE B CD1 1 
ATOM   3762 C CD2 . PHE B 1 102 ? 12.38500  26.56300  56.42000  1.000 15.54525 ? 102 PHE B CD2 1 
ATOM   3763 C CE1 . PHE B 1 102 ? 12.66900  27.41000  53.81400  1.000 23.74975 ? 102 PHE B CE1 1 
ATOM   3764 C CE2 . PHE B 1 102 ? 13.08200  25.78700  55.51600  1.000 19.17509 ? 102 PHE B CE2 1 
ATOM   3765 C CZ  . PHE B 1 102 ? 13.22300  26.20800  54.21300  1.000 19.03027 ? 102 PHE B CZ  1 
ATOM   3766 N N   . MET B 1 103 ? 10.74700  30.77600  59.11000  1.000 14.91578 ? 103 MET B N   1 
ATOM   3767 C CA  . MET B 1 103 ? 9.91300   31.36500  60.14700  1.000 20.57309 ? 103 MET B CA  1 
ATOM   3768 C C   . MET B 1 103 ? 10.03200  32.88000  60.18600  1.000 20.26769 ? 103 MET B C   1 
ATOM   3769 O O   . MET B 1 103 ? 9.10000   33.56000  60.63300  1.000 18.30152 ? 103 MET B O   1 
ATOM   3770 C CB  . MET B 1 103 ? 10.25700  30.75800  61.50700  1.000 17.12131 ? 103 MET B CB  1 
ATOM   3771 C CG  . MET B 1 103 ? 9.87400   29.29400  61.59500  1.000 20.59114 ? 103 MET B CG  1 
ATOM   3772 S SD  . MET B 1 103 ? 9.78400   28.69000  63.27800  1.000 28.62507 ? 103 MET B SD  1 
ATOM   3773 C CE  . MET B 1 103 ? 8.29000   29.50400  63.83700  1.000 23.87794 ? 103 MET B CE  1 
ATOM   3774 N N   . GLY B 1 104 ? 11.16000  33.43000  59.73600  1.000 16.38461 ? 104 GLY B N   1 
ATOM   3775 C CA  . GLY B 1 104 ? 11.25800  34.87400  59.67900  1.000 20.28186 ? 104 GLY B CA  1 
ATOM   3776 C C   . GLY B 1 104 ? 10.41100  35.48500  58.58900  1.000 23.34325 ? 104 GLY B C   1 
ATOM   3777 O O   . GLY B 1 104 ? 10.02300  36.65100  58.69900  1.000 30.72127 ? 104 GLY B O   1 
ATOM   3778 N N   . ILE B 1 105 ? 10.09100  34.71300  57.55500  1.000 19.08623 ? 105 ILE B N   1 
ATOM   3779 C CA  . ILE B 1 105 ? 9.45900   35.23100  56.35400  1.000 25.53905 ? 105 ILE B CA  1 
ATOM   3780 C C   . ILE B 1 105 ? 8.02500   34.73700  56.20800  1.000 26.10502 ? 105 ILE B C   1 
ATOM   3781 O O   . ILE B 1 105 ? 7.15000   35.48300  55.76400  1.000 26.10019 ? 105 ILE B O   1 
ATOM   3782 C CB  . ILE B 1 105 ? 10.30300  34.86200  55.11400  1.000 26.51153 ? 105 ILE B CB  1 
ATOM   3783 C CG1 . ILE B 1 105 ? 11.53600  35.76000  55.02700  1.000 29.90521 ? 105 ILE B CG1 1 
ATOM   3784 C CG2 . ILE B 1 105 ? 9.49300   34.93900  53.85700  1.000 28.19192 ? 105 ILE B CG2 1 
ATOM   3785 C CD1 . ILE B 1 105 ? 11.22400  37.22200  55.19000  1.000 27.55156 ? 105 ILE B CD1 1 
ATOM   3786 N N   . LEU B 1 106 ? 7.76100   33.49300  56.58500  1.000 21.00819 ? 106 LEU B N   1 
ATOM   3787 C CA  . LEU B 1 106 ? 6.46100   32.90000  56.34700  1.000 22.08463 ? 106 LEU B CA  1 
ATOM   3788 C C   . LEU B 1 106 ? 5.55300   33.09100  57.55600  1.000 24.92558 ? 106 LEU B C   1 
ATOM   3789 O O   . LEU B 1 106 ? 5.93200   33.67200  58.57700  1.000 25.99876 ? 106 LEU B O   1 
ATOM   3790 C CB  . LEU B 1 106 ? 6.60700   31.41700  56.01200  1.000 16.80017 ? 106 LEU B CB  1 
ATOM   3791 C CG  . LEU B 1 106 ? 7.57400   31.08300  54.87700  1.000 23.52486 ? 106 LEU B CG  1 
ATOM   3792 C CD1 . LEU B 1 106 ? 7.75600   29.57700  54.77500  1.000 16.07335 ? 106 LEU B CD1 1 
ATOM   3793 C CD2 . LEU B 1 106 ? 7.09800   31.68200  53.55700  1.000 20.24225 ? 106 LEU B CD2 1 
ATOM   3794 N N   . LYS B 1 107 ? 4.32800   32.59200  57.42300  1.000 26.26758 ? 107 LYS B N   1 
ATOM   3795 C CA  . LYS B 1 107 ? 3.37600   32.50500  58.51800  1.000 28.10993 ? 107 LYS B CA  1 
ATOM   3796 C C   . LYS B 1 107 ? 2.42800   31.35500  58.21100  1.000 26.83972 ? 107 LYS B C   1 
ATOM   3797 O O   . LYS B 1 107 ? 2.45700   30.77600  57.12100  1.000 23.31802 ? 107 LYS B O   1 
ATOM   3798 C CB  . LYS B 1 107 ? 2.61300   33.81900  58.71000  1.000 21.60637 ? 107 LYS B CB  1 
ATOM   3799 C CG  . LYS B 1 107 ? 1.76200   34.20500  57.51900  1.000 20.76880 ? 107 LYS B CG  1 
ATOM   3800 C CD  . LYS B 1 107 ? 1.04100   35.52500  57.75700  1.000 28.92419 ? 107 LYS B CD  1 
ATOM   3801 C CE  . LYS B 1 107 ? 0.21500   35.92500  56.54600  1.000 26.98616 ? 107 LYS B CE  1 
ATOM   3802 N NZ  . LYS B 1 107 ? 1.04700   35.90100  55.30800  1.000 27.22726 ? 107 LYS B NZ  1 
ATOM   3803 N N   . ALA B 1 108 ? 1.58700   31.01900  59.18800  1.000 27.55755 ? 108 ALA B N   1 
ATOM   3804 C CA  . ALA B 1 108 ? 0.60200   29.96700  58.97100  1.000 26.04490 ? 108 ALA B CA  1 
ATOM   3805 C C   . ALA B 1 108 ? -0.29700  30.33800  57.80100  1.000 23.85394 ? 108 ALA B C   1 
ATOM   3806 O O   . ALA B 1 108 ? -0.80900  31.45900  57.72600  1.000 22.71972 ? 108 ALA B O   1 
ATOM   3807 C CB  . ALA B 1 108 ? -0.23100  29.73900  60.23100  1.000 24.29069 ? 108 ALA B CB  1 
ATOM   3808 N N   . GLY B 1 109 ? -0.48500  29.39200  56.88600  1.000 26.42685 ? 109 GLY B N   1 
ATOM   3809 C CA  . GLY B 1 109 ? -1.28600  29.61100  55.70200  1.000 23.99713 ? 109 GLY B CA  1 
ATOM   3810 C C   . GLY B 1 109 ? -0.49200  29.87400  54.44200  1.000 27.79488 ? 109 GLY B C   1 
ATOM   3811 O O   . GLY B 1 109 ? -1.08600  29.91400  53.35600  1.000 29.30720 ? 109 GLY B O   1 
ATOM   3812 N N   . ASP B 1 110 ? 0.82300   30.06200  54.55300  1.000 26.21200 ? 110 ASP B N   1 
ATOM   3813 C CA  . ASP B 1 110 ? 1.68200   30.24400  53.39300  1.000 26.38850 ? 110 ASP B CA  1 
ATOM   3814 C C   . ASP B 1 110 ? 2.04800   28.89200  52.78800  1.000 23.39497 ? 110 ASP B C   1 
ATOM   3815 O O   . ASP B 1 110 ? 1.95600   27.84700  53.43400  1.000 23.00345 ? 110 ASP B O   1 
ATOM   3816 C CB  . ASP B 1 110 ? 2.95900   31.00600  53.76700  1.000 26.96418 ? 110 ASP B CB  1 
ATOM   3817 C CG  . ASP B 1 110 ? 2.68800   32.44400  54.19400  1.000 25.77983 ? 110 ASP B CG  1 
ATOM   3818 O OD1 . ASP B 1 110 ? 1.62000   32.99000  53.83700  1.000 27.63312 ? 110 ASP B OD1 1 
ATOM   3819 O OD2 . ASP B 1 110 ? 3.55300   33.02800  54.88600  1.000 26.09657 ? 110 ASP B OD2 1 
ATOM   3820 N N   . HIS B 1 111 ? 2.46500   28.92600  51.52700  1.000 21.22491 ? 111 HIS B N   1 
ATOM   3821 C CA  . HIS B 1 111 ? 2.84700   27.72700  50.80100  1.000 22.86374 ? 111 HIS B CA  1 
ATOM   3822 C C   . HIS B 1 111 ? 4.23900   27.90800  50.21300  1.000 25.88305 ? 111 HIS B C   1 
ATOM   3823 O O   . HIS B 1 111 ? 4.61600   29.00900  49.79900  1.000 23.18984 ? 111 HIS B O   1 
ATOM   3824 C CB  . HIS B 1 111 ? 1.83300   27.40900  49.68900  1.000 24.22505 ? 111 HIS B CB  1 
ATOM   3825 C CG  . HIS B 1 111 ? 2.25800   26.30000  48.77700  1.000 26.38123 ? 111 HIS B CG  1 
ATOM   3826 N ND1 . HIS B 1 111 ? 2.71400   26.52500  47.49500  1.000 25.00535 ? 111 HIS B ND1 1 
ATOM   3827 C CD2 . HIS B 1 111 ? 2.28700   24.95800  48.95600  1.000 24.74843 ? 111 HIS B CD2 1 
ATOM   3828 C CE1 . HIS B 1 111 ? 3.00700   25.37000  46.92400  1.000 23.47925 ? 111 HIS B CE1 1 
ATOM   3829 N NE2 . HIS B 1 111 ? 2.75400   24.40300  47.78900  1.000 28.88834 ? 111 HIS B NE2 1 
ATOM   3830 N N   . VAL B 1 112 ? 4.99400   26.81300  50.16800  1.000 25.00026 ? 112 VAL B N   1 
ATOM   3831 C CA  . VAL B 1 112 ? 6.37500   26.81000  49.69700  1.000 22.76297 ? 112 VAL B CA  1 
ATOM   3832 C C   . VAL B 1 112 ? 6.50700   25.79600  48.57200  1.000 22.92644 ? 112 VAL B C   1 
ATOM   3833 O O   . VAL B 1 112 ? 6.02700   24.66400  48.69200  1.000 24.23643 ? 112 VAL B O   1 
ATOM   3834 C CB  . VAL B 1 112 ? 7.36000   26.47100  50.83200  1.000 22.40693 ? 112 VAL B CB  1 
ATOM   3835 C CG1 . VAL B 1 112 ? 8.74400   26.20700  50.26800  1.000 20.45038 ? 112 VAL B CG1 1 
ATOM   3836 C CG2 . VAL B 1 112 ? 7.40300   27.58600  51.84200  1.000 23.61441 ? 112 VAL B CG2 1 
ATOM   3837 N N   . VAL B 1 113 ? 7.15600   26.20100  47.48300  1.000 21.92843 ? 113 VAL B N   1 
ATOM   3838 C CA  . VAL B 1 113 ? 7.62000   25.27400  46.45800  1.000 19.89836 ? 113 VAL B CA  1 
ATOM   3839 C C   . VAL B 1 113 ? 9.11800   25.09800  46.64600  1.000 23.18519 ? 113 VAL B C   1 
ATOM   3840 O O   . VAL B 1 113 ? 9.86600   26.08500  46.68400  1.000 22.35575 ? 113 VAL B O   1 
ATOM   3841 C CB  . VAL B 1 113 ? 7.29800   25.77900  45.04300  1.000 19.41512 ? 113 VAL B CB  1 
ATOM   3842 C CG1 . VAL B 1 113 ? 7.67000   24.72500  44.02100  1.000 20.30160 ? 113 VAL B CG1 1 
ATOM   3843 C CG2 . VAL B 1 113 ? 5.82900   26.14700  44.92300  1.000 22.90333 ? 113 VAL B CG2 1 
ATOM   3844 N N   . ALA B 1 114 ? 9.55800   23.84900  46.78200  1.000 19.90463 ? 114 ALA B N   1 
ATOM   3845 C CA  . ALA B 1 114 ? 10.94800  23.54900  47.08200  1.000 19.78042 ? 114 ALA B CA  1 
ATOM   3846 C C   . ALA B 1 114 ? 11.45300  22.45200  46.16100  1.000 22.14726 ? 114 ALA B C   1 
ATOM   3847 O O   . ALA B 1 114 ? 10.70900  21.54500  45.78400  1.000 23.67246 ? 114 ALA B O   1 
ATOM   3848 C CB  . ALA B 1 114 ? 11.13000  23.12100  48.54200  1.000 19.29269 ? 114 ALA B CB  1 
ATOM   3849 N N   . SER B 1 115 ? 12.72900  22.55100  45.79400  1.000 18.09755 ? 115 SER B N   1 
ATOM   3850 C CA  . SER B 1 115 ? 13.34600  21.49700  45.00700  1.000 20.51155 ? 115 SER B CA  1 
ATOM   3851 C C   . SER B 1 115 ? 13.31700  20.19400  45.79000  1.000 21.45115 ? 115 SER B C   1 
ATOM   3852 O O   . SER B 1 115 ? 13.62900  20.16200  46.98300  1.000 21.24627 ? 115 SER B O   1 
ATOM   3853 C CB  . SER B 1 115 ? 14.78500  21.86300  44.64400  1.000 18.08666 ? 115 SER B CB  1 
ATOM   3854 O OG  . SER B 1 115 ? 15.45700  20.74200  44.09200  1.000 19.05203 ? 115 SER B OG  1 
ATOM   3855 N N   . ARG B 1 116 ? 12.93600  19.11600  45.10400  1.000 24.71590 ? 116 ARG B N   1 
ATOM   3856 C CA  . ARG B 1 116 ? 12.80000  17.81400  45.74900  1.000 25.46721 ? 116 ARG B CA  1 
ATOM   3857 C C   . ARG B 1 116 ? 14.12800  17.31400  46.29700  1.000 18.80672 ? 116 ARG B C   1 
ATOM   3858 O O   . ARG B 1 116 ? 14.15100  16.54700  47.26800  1.000 21.74471 ? 116 ARG B O   1 
ATOM   3859 C CB  . ARG B 1 116 ? 12.20700  16.81500  44.74800  1.000 25.33772 ? 116 ARG B CB  1 
ATOM   3860 C CG  . ARG B 1 116 ? 12.32000  15.33800  45.13100  1.000 37.81413 ? 116 ARG B CG  1 
ATOM   3861 C CD  . ARG B 1 116 ? 10.95500  14.64000  45.29500  1.000 38.54757 ? 116 ARG B CD  1 
ATOM   3862 N NE  . ARG B 1 116 ? 9.89600   15.21800  44.47000  1.000 42.16953 ? 116 ARG B NE  1 
ATOM   3863 C CZ  . ARG B 1 116 ? 9.78900   15.06500  43.15500  1.000 46.03344 ? 116 ARG B CZ  1 
ATOM   3864 N NH1 . ARG B 1 116 ? 10.67800  14.36700  42.46200  1.000 49.22348 ? 116 ARG B NH1 1 
ATOM   3865 N NH2 . ARG B 1 116 ? 8.77000   15.63600  42.51700  1.000 42.24481 ? 116 ARG B NH2 1 
ATOM   3866 N N   . SER B 1 117 ? 15.23900  17.76100  45.71900  1.000 19.81052 ? 117 SER B N   1 
ATOM   3867 C CA  . SER B 1 117 ? 16.55700  17.22900  46.04100  1.000 20.15994 ? 117 SER B CA  1 
ATOM   3868 C C   . SER B 1 117 ? 17.27300  17.99300  47.15200  1.000 19.31582 ? 117 SER B C   1 
ATOM   3869 O O   . SER B 1 117 ? 18.45200  17.71400  47.40600  1.000 20.80590 ? 117 SER B O   1 
ATOM   3870 C CB  . SER B 1 117 ? 17.43400  17.21200  44.78600  1.000 20.58735 ? 117 SER B CB  1 
ATOM   3871 O OG  . SER B 1 117 ? 17.51600  18.50400  44.21100  1.000 23.74060 ? 117 SER B OG  1 
ATOM   3872 N N   . ILE B 1 118 ? 16.60400  18.94400  47.81500  1.000 15.12599 ? 118 ILE B N   1 
ATOM   3873 C CA  . ILE B 1 118 ? 17.28400  19.70400  48.86300  1.000 16.98424 ? 118 ILE B CA  1 
ATOM   3874 C C   . ILE B 1 118 ? 17.71500  18.77400  49.99600  1.000 18.03028 ? 118 ILE B C   1 
ATOM   3875 O O   . ILE B 1 118 ? 17.23500  17.64200  50.13400  1.000 15.52182 ? 118 ILE B O   1 
ATOM   3876 C CB  . ILE B 1 118 ? 16.41400  20.84400  49.41700  1.000 19.32926 ? 118 ILE B CB  1 
ATOM   3877 C CG1 . ILE B 1 118 ? 15.17000  20.28200  50.10800  1.000 17.54071 ? 118 ILE B CG1 1 
ATOM   3878 C CG2 . ILE B 1 118 ? 16.05900  21.85700  48.32300  1.000 15.79871 ? 118 ILE B CG2 1 
ATOM   3879 C CD1 . ILE B 1 118 ? 14.25800  21.34300  50.64900  1.000 14.05935 ? 118 ILE B CD1 1 
ATOM   3880 N N   . PHE B 1 119 ? 18.65300  19.26800  50.80400  1.000 21.08281 ? 119 PHE B N   1 
ATOM   3881 C CA  . PHE B 1 119 ? 19.15800  18.56300  51.97600  1.000 20.44698 ? 119 PHE B CA  1 
ATOM   3882 C C   . PHE B 1 119 ? 18.03700  17.81600  52.68700  1.000 19.09060 ? 119 PHE B C   1 
ATOM   3883 O O   . PHE B 1 119 ? 16.97600  18.38100  52.97000  1.000 16.89232 ? 119 PHE B O   1 
ATOM   3884 C CB  . PHE B 1 119 ? 19.81500  19.57500  52.92300  1.000 18.77910 ? 119 PHE B CB  1 
ATOM   3885 C CG  . PHE B 1 119 ? 20.73900  18.96300  53.94100  1.000 15.40840 ? 119 PHE B CG  1 
ATOM   3886 C CD1 . PHE B 1 119 ? 21.87300  18.26700  53.54300  1.000 17.03757 ? 119 PHE B CD1 1 
ATOM   3887 C CD2 . PHE B 1 119 ? 20.49700  19.12400  55.29900  1.000 16.37813 ? 119 PHE B CD2 1 
ATOM   3888 C CE1 . PHE B 1 119 ? 22.73900  17.71600  54.48700  1.000 16.95643 ? 119 PHE B CE1 1 
ATOM   3889 C CE2 . PHE B 1 119 ? 21.35500  18.58200  56.24800  1.000 14.85678 ? 119 PHE B CE2 1 
ATOM   3890 C CZ  . PHE B 1 119 ? 22.47800  17.87900  55.84500  1.000 15.49615 ? 119 PHE B CZ  1 
ATOM   3891 N N   . GLY B 1 120 ? 18.27400  16.53000  52.95200  1.000 17.67223 ? 120 GLY B N   1 
ATOM   3892 C CA  . GLY B 1 120 ? 17.21200  15.68500  53.47800  1.000 20.68053 ? 120 GLY B CA  1 
ATOM   3893 C C   . GLY B 1 120 ? 16.61100  16.21800  54.76400  1.000 20.33797 ? 120 GLY B C   1 
ATOM   3894 O O   . GLY B 1 120 ? 15.39900  16.12400  54.98100  1.000 18.25669 ? 120 GLY B O   1 
ATOM   3895 N N   . THR B 1 121 ? 17.44700  16.79600  55.63100  1.000 17.29593 ? 121 THR B N   1 
ATOM   3896 C CA  . THR B 1 121 ? 16.93300  17.38300  56.86400  1.000 19.63493 ? 121 THR B CA  1 
ATOM   3897 C C   . THR B 1 121 ? 16.05700  18.59800  56.58100  1.000 19.11419 ? 121 THR B C   1 
ATOM   3898 O O   . THR B 1 121 ? 15.07800  18.83700  57.29700  1.000 18.13356 ? 121 THR B O   1 
ATOM   3899 C CB  . THR B 1 121 ? 18.09400  17.75300  57.78700  1.000 18.40382 ? 121 THR B CB  1 
ATOM   3900 O OG1 . THR B 1 121 ? 18.92600  16.60700  57.96900  1.000 17.96272 ? 121 THR B OG1 1 
ATOM   3901 C CG2 . THR B 1 121 ? 17.58300  18.20700  59.13800  1.000 15.54683 ? 121 THR B CG2 1 
ATOM   3902 N N   . THR B 1 122 ? 16.38600  19.37600  55.54900  1.000 16.42584 ? 122 THR B N   1 
ATOM   3903 C CA  . THR B 1 122 ? 15.52700  20.49700  55.18500  1.000 18.71550 ? 122 THR B CA  1 
ATOM   3904 C C   . THR B 1 122 ? 14.16100  20.01100  54.71500  1.000 18.37676 ? 122 THR B C   1 
ATOM   3905 O O   . THR B 1 122 ? 13.13700  20.63700  55.01900  1.000 17.19931 ? 122 THR B O   1 
ATOM   3906 C CB  . THR B 1 122 ? 16.19400  21.35800  54.10800  1.000 17.42318 ? 122 THR B CB  1 
ATOM   3907 O OG1 . THR B 1 122 ? 17.54500  21.65100  54.48900  1.000 14.37287 ? 122 THR B OG1 1 
ATOM   3908 C CG2 . THR B 1 122 ? 15.43200  22.66300  53.94100  1.000 14.92589 ? 122 THR B CG2 1 
ATOM   3909 N N   . VAL B 1 123 ? 14.12900  18.89900  53.96800  1.000 19.90115 ? 123 VAL B N   1 
ATOM   3910 C CA  . VAL B 1 123 ? 12.85800  18.28600  53.58000  1.000 20.20236 ? 123 VAL B CA  1 
ATOM   3911 C C   . VAL B 1 123 ? 12.02000  17.99300  54.81800  1.000 19.99396 ? 123 VAL B C   1 
ATOM   3912 O O   . VAL B 1 123 ? 10.82500  18.30400  54.86700  1.000 21.69979 ? 123 VAL B O   1 
ATOM   3913 C CB  . VAL B 1 123 ? 13.10100  17.00500  52.75500  1.000 20.72683 ? 123 VAL B CB  1 
ATOM   3914 C CG1 . VAL B 1 123 ? 11.79800  16.23500  52.54800  1.000 20.57976 ? 123 VAL B CG1 1 
ATOM   3915 C CG2 . VAL B 1 123 ? 13.71600  17.33500  51.41900  1.000 15.65745 ? 123 VAL B CG2 1 
ATOM   3916 N N   . GLN B 1 124 ? 12.64800  17.41300  55.84700  1.000 20.62053 ? 124 GLN B N   1 
ATOM   3917 C CA  . GLN B 1 124 ? 11.93900  17.11800  57.08900  1.000 20.81557 ? 124 GLN B CA  1 
ATOM   3918 C C   . GLN B 1 124 ? 11.50300  18.39000  57.80900  1.000 21.53520 ? 124 GLN B C   1 
ATOM   3919 O O   . GLN B 1 124 ? 10.39900  18.44100  58.36200  1.000 22.26118 ? 124 GLN B O   1 
ATOM   3920 C CB  . GLN B 1 124 ? 12.81200  16.25400  58.00200  1.000 23.43977 ? 124 GLN B CB  1 
ATOM   3921 C CG  . GLN B 1 124 ? 13.02600  14.82800  57.49000  1.000 22.80555 ? 124 GLN B CG  1 
ATOM   3922 C CD  . GLN B 1 124 ? 11.73700  14.19900  56.98100  1.000 30.06978 ? 124 GLN B CD  1 
ATOM   3923 O OE1 . GLN B 1 124 ? 10.76100  14.06600  57.72300  1.000 39.11049 ? 124 GLN B OE1 1 
ATOM   3924 N NE2 . GLN B 1 124 ? 11.72200  13.82800  55.70100  1.000 31.23953 ? 124 GLN B NE2 1 
ATOM   3925 N N   . LEU B 1 125 ? 12.35300  19.42300  57.82400  1.000 20.05159 ? 125 LEU B N   1 
ATOM   3926 C CA  . LEU B 1 125 ? 11.99000  20.66200  58.51100  1.000 19.08129 ? 125 LEU B CA  1 
ATOM   3927 C C   . LEU B 1 125 ? 10.74700  21.28600  57.89300  1.000 22.54448 ? 125 LEU B C   1 
ATOM   3928 O O   . LEU B 1 125 ? 9.84500   21.73800  58.60900  1.000 24.80308 ? 125 LEU B O   1 
ATOM   3929 C CB  . LEU B 1 125 ? 13.15500  21.65100  58.47900  1.000 19.64095 ? 125 LEU B CB  1 
ATOM   3930 C CG  . LEU B 1 125 ? 12.89900  23.06600  59.02400  1.000 21.69255 ? 125 LEU B CG  1 
ATOM   3931 C CD1 . LEU B 1 125 ? 12.55800  23.03200  60.50100  1.000 18.89402 ? 125 LEU B CD1 1 
ATOM   3932 C CD2 . LEU B 1 125 ? 14.09700  23.98300  58.77600  1.000 18.79232 ? 125 LEU B CD2 1 
ATOM   3933 N N   . LEU B 1 126 ? 10.68200  21.31600  56.56300  1.000 21.07721 ? 126 LEU B N   1 
ATOM   3934 C CA  . LEU B 1 126 ? 9.48900   21.81100  55.89000  1.000 22.19746 ? 126 LEU B CA  1 
ATOM   3935 C C   . LEU B 1 126 ? 8.34100   20.81600  56.01200  1.000 24.97085 ? 126 LEU B C   1 
ATOM   3936 O O   . LEU B 1 126 ? 7.26300   21.15000  56.51900  1.000 27.75400 ? 126 LEU B O   1 
ATOM   3937 C CB  . LEU B 1 126 ? 9.80500   22.09500  54.41900  1.000 18.61152 ? 126 LEU B CB  1 
ATOM   3938 C CG  . LEU B 1 126 ? 10.54400  23.39000  54.08100  1.000 20.28583 ? 126 LEU B CG  1 
ATOM   3939 C CD1 . LEU B 1 126 ? 11.13100  23.31100  52.68400  1.000 17.41434 ? 126 LEU B CD1 1 
ATOM   3940 C CD2 . LEU B 1 126 ? 9.60300   24.58000  54.18600  1.000 20.65788 ? 126 LEU B CD2 1 
ATOM   3941 N N   . GLY B 1 127 ? 8.56300   19.57600  55.56600  1.000 22.78464 ? 127 GLY B N   1 
ATOM   3942 C CA  . GLY B 1 127 ? 7.47900   18.61500  55.43800  1.000 23.69896 ? 127 GLY B CA  1 
ATOM   3943 C C   . GLY B 1 127 ? 6.94600   18.06400  56.74800  1.000 27.74157 ? 127 GLY B C   1 
ATOM   3944 O O   . GLY B 1 127 ? 5.78500   17.64600  56.80200  1.000 31.23334 ? 127 GLY B O   1 
ATOM   3945 N N   . ASN B 1 128 ? 7.75100   18.05500  57.80400  1.000 30.06576 ? 128 ASN B N   1 
ATOM   3946 C CA  . ASN B 1 128 ? 7.31700   17.44800  59.05500  1.000 30.49382 ? 128 ASN B CA  1 
ATOM   3947 C C   . ASN B 1 128 ? 7.19600   18.42400  60.21600  1.000 27.60068 ? 128 ASN B C   1 
ATOM   3948 O O   . ASN B 1 128 ? 6.32500   18.23500  61.06600  1.000 27.19526 ? 128 ASN B O   1 
ATOM   3949 C CB  . ASN B 1 128 ? 8.27100   16.30700  59.45300  1.000 32.55152 ? 128 ASN B CB  1 
ATOM   3950 C CG  . ASN B 1 128 ? 7.66100   15.36100  60.48100  1.000 44.70427 ? 128 ASN B CG  1 
ATOM   3951 O OD1 . ASN B 1 128 ? 7.77300   15.57800  61.69300  1.000 46.64307 ? 128 ASN B OD1 1 
ATOM   3952 N ND2 . ASN B 1 128 ? 7.01900   14.30000  60.00000  1.000 45.41980 ? 128 ASN B ND2 1 
ATOM   3953 N N   . ILE B 1 129 ? 8.03500   19.45400  60.28500  1.000 25.68618 ? 129 ILE B N   1 
ATOM   3954 C CA  . ILE B 1 129 ? 7.99100   20.38300  61.40900  1.000 23.49159 ? 129 ILE B CA  1 
ATOM   3955 C C   . ILE B 1 129 ? 7.06200   21.54700  61.08700  1.000 24.58574 ? 129 ILE B C   1 
ATOM   3956 O O   . ILE B 1 129 ? 6.04600   21.75000  61.76100  1.000 27.47241 ? 129 ILE B O   1 
ATOM   3957 C CB  . ILE B 1 129 ? 9.39900   20.89000  61.76800  1.000 28.27670 ? 129 ILE B CB  1 
ATOM   3958 C CG1 . ILE B 1 129 ? 10.32900  19.71700  62.08900  1.000 24.91703 ? 129 ILE B CG1 1 
ATOM   3959 C CG2 . ILE B 1 129 ? 9.33100   21.85600  62.94200  1.000 19.33563 ? 129 ILE B CG2 1 
ATOM   3960 C CD1 . ILE B 1 129 ? 10.07100  19.10100  63.42000  1.000 26.39260 ? 129 ILE B CD1 1 
ATOM   3961 N N   . LEU B 1 130 ? 7.39500   22.32200  60.05200  1.000 22.71467 ? 130 LEU B N   1 
ATOM   3962 C CA  . LEU B 1 130 ? 6.60200   23.51000  59.75900  1.000 21.44661 ? 130 LEU B CA  1 
ATOM   3963 C C   . LEU B 1 130 ? 5.20500   23.16200  59.25900  1.000 23.07649 ? 130 LEU B C   1 
ATOM   3964 O O   . LEU B 1 130 ? 4.28400   23.96700  59.42400  1.000 18.09221 ? 130 LEU B O   1 
ATOM   3965 C CB  . LEU B 1 130 ? 7.34300   24.38700  58.75300  1.000 20.47973 ? 130 LEU B CB  1 
ATOM   3966 C CG  . LEU B 1 130 ? 8.66700   24.92900  59.30700  1.000 25.64869 ? 130 LEU B CG  1 
ATOM   3967 C CD1 . LEU B 1 130 ? 9.41900   25.73300  58.27000  1.000 18.57310 ? 130 LEU B CD1 1 
ATOM   3968 C CD2 . LEU B 1 130 ? 8.43100   25.76100  60.56500  1.000 18.44372 ? 130 LEU B CD2 1 
ATOM   3969 N N   . SER B 1 131 ? 5.02600   21.97600  58.67000  1.000 24.30967 ? 131 SER B N   1 
ATOM   3970 C CA  . SER B 1 131 ? 3.69200   21.53200  58.28200  1.000 21.55864 ? 131 SER B CA  1 
ATOM   3971 C C   . SER B 1 131 ? 2.74300   21.53600  59.47200  1.000 21.60641 ? 131 SER B C   1 
ATOM   3972 O O   . SER B 1 131 ? 1.56300   21.87100  59.33300  1.000 27.66195 ? 131 SER B O   1 
ATOM   3973 C CB  . SER B 1 131 ? 3.76800   20.13600  57.66900  1.000 23.64143 ? 131 SER B CB  1 
ATOM   3974 O OG  . SER B 1 131 ? 4.23200   19.20200  58.63100  1.000 30.99605 ? 131 SER B OG  1 
ATOM   3975 N N   . ARG B 1 132 ? 3.24400   21.18300  60.65500  1.000 24.76858 ? 132 ARG B N   1 
ATOM   3976 C CA  . ARG B 1 132 ? 2.42000   21.22100  61.85500  1.000 27.48050 ? 132 ARG B CA  1 
ATOM   3977 C C   . ARG B 1 132 ? 2.13500   22.64100  62.32400  1.000 28.55817 ? 132 ARG B C   1 
ATOM   3978 O O   . ARG B 1 132 ? 1.35600   22.81600  63.26800  1.000 30.50379 ? 132 ARG B O   1 
ATOM   3979 C CB  . ARG B 1 132 ? 3.08400   20.42700  62.98400  1.000 25.28536 ? 132 ARG B CB  1 
ATOM   3980 C CG  . ARG B 1 132 ? 3.46500   18.99800  62.60900  1.000 33.27490 ? 132 ARG B CG  1 
ATOM   3981 C CD  . ARG B 1 132 ? 4.02600   18.20000  63.80400  1.000 41.66693 ? 132 ARG B CD  1 
ATOM   3982 N NE  . ARG B 1 132 ? 5.34400   18.64300  64.25700  1.000 39.80188 ? 132 ARG B NE  1 
ATOM   3983 C CZ  . ARG B 1 132 ? 5.56200   19.39100  65.33300  1.000 40.02750 ? 132 ARG B CZ  1 
ATOM   3984 N NH1 . ARG B 1 132 ? 4.56300   19.84100  66.07700  1.000 29.61106 ? 132 ARG B NH1 1 
ATOM   3985 N NH2 . ARG B 1 132 ? 6.81600   19.68900  65.67700  1.000 32.75011 ? 132 ARG B NH2 1 
ATOM   3986 N N   . PHE B 1 133 ? 2.74900   23.65500  61.71100  1.000 24.85520 ? 133 PHE B N   1 
ATOM   3987 C CA  . PHE B 1 133 ? 2.50700   25.04300  62.08700  1.000 24.32934 ? 133 PHE B CA  1 
ATOM   3988 C C   . PHE B 1 133 ? 1.92900   25.84600  60.92900  1.000 24.75796 ? 133 PHE B C   1 
ATOM   3989 O O   . PHE B 1 133 ? 2.14500   27.05400  60.82900  1.000 27.94107 ? 133 PHE B O   1 
ATOM   3990 C CB  . PHE B 1 133 ? 3.78300   25.68200  62.63500  1.000 21.74847 ? 133 PHE B CB  1 
ATOM   3991 C CG  . PHE B 1 133 ? 4.16900   25.14700  63.98400  1.000 26.25050 ? 133 PHE B CG  1 
ATOM   3992 C CD1 . PHE B 1 133 ? 3.60500   25.67100  65.13600  1.000 24.66943 ? 133 PHE B CD1 1 
ATOM   3993 C CD2 . PHE B 1 133 ? 5.04500   24.08100  64.10000  1.000 23.60202 ? 133 PHE B CD2 1 
ATOM   3994 C CE1 . PHE B 1 133 ? 3.92800   25.16100  66.37800  1.000 24.81001 ? 133 PHE B CE1 1 
ATOM   3995 C CE2 . PHE B 1 133 ? 5.37300   23.57300  65.34000  1.000 23.95230 ? 133 PHE B CE2 1 
ATOM   3996 C CZ  . PHE B 1 133 ? 4.81300   24.11400  66.48000  1.000 22.50448 ? 133 PHE B CZ  1 
ATOM   3997 N N   . GLY B 1 134 ? 1.17500   25.18200  60.05700  1.000 26.46373 ? 134 GLY B N   1 
ATOM   3998 C CA  . GLY B 1 134 ? 0.40800   25.85500  59.03100  1.000 23.05913 ? 134 GLY B CA  1 
ATOM   3999 C C   . GLY B 1 134 ? 1.13300   26.14700  57.73800  1.000 22.95005 ? 134 GLY B C   1 
ATOM   4000 O O   . GLY B 1 134 ? 0.57900   26.85900  56.89200  1.000 24.62855 ? 134 GLY B O   1 
ATOM   4001 N N   . VAL B 1 135 ? 2.34200   25.62800  57.54900  1.000 21.24666 ? 135 VAL B N   1 
ATOM   4002 C CA  . VAL B 1 135 ? 3.11800   25.87700  56.34000  1.000 21.44966 ? 135 VAL B CA  1 
ATOM   4003 C C   . VAL B 1 135 ? 2.99600   24.66400  55.42900  1.000 21.50592 ? 135 VAL B C   1 
ATOM   4004 O O   . VAL B 1 135 ? 3.35900   23.54900  55.81700  1.000 23.14313 ? 135 VAL B O   1 
ATOM   4005 C CB  . VAL B 1 135 ? 4.58900   26.17900  56.66600  1.000 25.09051 ? 135 VAL B CB  1 
ATOM   4006 C CG1 . VAL B 1 135 ? 5.38800   26.39600  55.37500  1.000 21.91140 ? 135 VAL B CG1 1 
ATOM   4007 C CG2 . VAL B 1 135 ? 4.69500   27.39900  57.58200  1.000 20.03161 ? 135 VAL B CG2 1 
ATOM   4008 N N   . GLU B 1 136 ? 2.50300   24.88200  54.21300  1.000 23.45820 ? 136 GLU B N   1 
ATOM   4009 C CA  . GLU B 1 136 ? 2.35500   23.83000  53.21900  1.000 21.69099 ? 136 GLU B CA  1 
ATOM   4010 C C   . GLU B 1 136 ? 3.52600   23.87500  52.24500  1.000 27.13268 ? 136 GLU B C   1 
ATOM   4011 O O   . GLU B 1 136 ? 3.99400   24.95500  51.87300  1.000 26.06841 ? 136 GLU B O   1 
ATOM   4012 C CB  . GLU B 1 136 ? 1.03700   23.98500  52.46000  1.000 27.41496 ? 136 GLU B CB  1 
ATOM   4013 C CG  . GLU B 1 136 ? -0.17900  24.16600  53.35800  1.000 33.11827 ? 136 GLU B CG  1 
ATOM   4014 C CD  . GLU B 1 136 ? -1.30300  24.92600  52.67200  1.000 37.90705 ? 136 GLU B CD  1 
ATOM   4015 O OE1 . GLU B 1 136 ? -1.49600  24.75200  51.44700  1.000 38.47654 ? 136 GLU B OE1 1 
ATOM   4016 O OE2 . GLU B 1 136 ? -1.98600  25.71100  53.36000  1.000 36.62435 ? 136 GLU B OE2 1 
ATOM   4017 N N   . THR B 1 137 ? 4.00000   22.69800  51.83800  1.000 23.77237 ? 137 THR B N   1 
ATOM   4018 C CA  . THR B 1 137 ? 5.15200   22.58700  50.95600  1.000 22.61358 ? 137 THR B CA  1 
ATOM   4019 C C   . THR B 1 137 ? 4.85300   21.61500  49.82300  1.000 25.96336 ? 137 THR B C   1 
ATOM   4020 O O   . THR B 1 137 ? 4.25900   20.55600  50.04100  1.000 31.67270 ? 137 THR B O   1 
ATOM   4021 C CB  . THR B 1 137 ? 6.40500   22.12100  51.72100  1.000 22.63435 ? 137 THR B CB  1 
ATOM   4022 O OG1 . THR B 1 137 ? 6.65300   22.99600  52.83100  1.000 24.40490 ? 137 THR B OG1 1 
ATOM   4023 C CG2 . THR B 1 137 ? 7.62400   22.12600  50.81000  1.000 20.82830 ? 137 THR B CG2 1 
ATOM   4024 N N   . SER B 1 138 ? 5.26500   21.98500  48.61400  1.000 22.02272 ? 138 SER B N   1 
ATOM   4025 C CA  . SER B 1 138 ? 5.25600   21.10000  47.45800  1.000 25.29820 ? 138 SER B CA  1 
ATOM   4026 C C   . SER B 1 138 ? 6.67600   20.97900  46.92100  1.000 23.87804 ? 138 SER B C   1 
ATOM   4027 O O   . SER B 1 138 ? 7.42900   21.95800  46.91000  1.000 22.44354 ? 138 SER B O   1 
ATOM   4028 C CB  . SER B 1 138 ? 4.31600   21.62400  46.36000  1.000 22.39165 ? 138 SER B CB  1 
ATOM   4029 O OG  . SER B 1 138 ? 3.01200   21.85700  46.87000  1.000 30.32911 ? 138 SER B OG  1 
ATOM   4030 N N   . PHE B 1 139 ? 7.04300   19.77800  46.48100  1.000 22.18470 ? 139 PHE B N   1 
ATOM   4031 C CA  . PHE B 1 139 ? 8.39400   19.49000  46.01800  1.000 22.34808 ? 139 PHE B CA  1 
ATOM   4032 C C   . PHE B 1 139 ? 8.37900   19.15700  44.53100  1.000 29.14587 ? 139 PHE B C   1 
ATOM   4033 O O   . PHE B 1 139 ? 7.56400   18.34400  44.08000  1.000 30.24277 ? 139 PHE B O   1 
ATOM   4034 C CB  . PHE B 1 139 ? 9.00900   18.33900  46.82000  1.000 26.09489 ? 139 PHE B CB  1 
ATOM   4035 C CG  . PHE B 1 139 ? 9.24300   18.66600  48.27300  1.000 24.34119 ? 139 PHE B CG  1 
ATOM   4036 C CD1 . PHE B 1 139 ? 10.38200  19.34700  48.67000  1.000 20.90691 ? 139 PHE B CD1 1 
ATOM   4037 C CD2 . PHE B 1 139 ? 8.32600   18.28600  49.24000  1.000 24.17468 ? 139 PHE B CD2 1 
ATOM   4038 C CE1 . PHE B 1 139 ? 10.59800  19.65100  50.00300  1.000 22.58894 ? 139 PHE B CE1 1 
ATOM   4039 C CE2 . PHE B 1 139 ? 8.53900   18.58000  50.57900  1.000 19.82480 ? 139 PHE B CE2 1 
ATOM   4040 C CZ  . PHE B 1 139 ? 9.67600   19.26000  50.96100  1.000 21.51993 ? 139 PHE B CZ  1 
ATOM   4041 N N   . VAL B 1 140 ? 9.29000   19.77200  43.78000  1.000 24.86243 ? 140 VAL B N   1 
ATOM   4042 C CA  . VAL B 1 140 ? 9.33800   19.63000  42.32500  1.000 23.38908 ? 140 VAL B CA  1 
ATOM   4043 C C   . VAL B 1 140 ? 10.76400  19.28900  41.91400  1.000 23.77415 ? 140 VAL B C   1 
ATOM   4044 O O   . VAL B 1 140 ? 11.71200  19.50200  42.68300  1.000 25.48896 ? 140 VAL B O   1 
ATOM   4045 C CB  . VAL B 1 140 ? 8.86600   20.91600  41.61000  1.000 23.60928 ? 140 VAL B CB  1 
ATOM   4046 C CG1 . VAL B 1 140 ? 7.49200   21.32400  42.09300  1.000 23.11682 ? 140 VAL B CG1 1 
ATOM   4047 C CG2 . VAL B 1 140 ? 9.87700   22.03300  41.82800  1.000 24.95818 ? 140 VAL B CG2 1 
ATOM   4048 N N   . PRO B 1 141 ? 10.94800  18.73500  40.71200  1.000 28.18192 ? 141 PRO B N   1 
ATOM   4049 C CA  . PRO B 1 141 ? 12.31000  18.52500  40.20200  1.000 28.42066 ? 141 PRO B CA  1 
ATOM   4050 C C   . PRO B 1 141 ? 13.01800  19.85100  39.97000  1.000 24.24437 ? 141 PRO B C   1 
ATOM   4051 O O   . PRO B 1 141 ? 12.41900  20.82000  39.50400  1.000 23.70508 ? 141 PRO B O   1 
ATOM   4052 C CB  . PRO B 1 141 ? 12.08800  17.77100  38.88400  1.000 25.98844 ? 141 PRO B CB  1 
ATOM   4053 C CG  . PRO B 1 141 ? 10.71800  17.20500  38.98600  1.000 25.29445 ? 141 PRO B CG  1 
ATOM   4054 C CD  . PRO B 1 141 ? 9.93300   18.18100  39.80000  1.000 28.55742 ? 141 PRO B CD  1 
ATOM   4055 N N   . LEU B 1 142 ? 14.31900  19.87200  40.26500  1.000 25.14570 ? 142 LEU B N   1 
ATOM   4056 C CA  . LEU B 1 142 ? 15.05600  21.13400  40.29600  1.000 24.33568 ? 142 LEU B CA  1 
ATOM   4057 C C   . LEU B 1 142 ? 15.09000  21.80900  38.92600  1.000 24.33149 ? 142 LEU B C   1 
ATOM   4058 O O   . LEU B 1 142 ? 14.79600  23.00400  38.80300  1.000 22.07594 ? 142 LEU B O   1 
ATOM   4059 C CB  . LEU B 1 142 ? 16.47400  20.89100  40.81000  1.000 23.63818 ? 142 LEU B CB  1 
ATOM   4060 C CG  . LEU B 1 142 ? 17.36700  22.13200  40.82600  1.000 20.90870 ? 142 LEU B CG  1 
ATOM   4061 C CD1 . LEU B 1 142 ? 16.79500  23.20400  41.75000  1.000 17.00804 ? 142 LEU B CD1 1 
ATOM   4062 C CD2 . LEU B 1 142 ? 18.77700  21.74000  41.24100  1.000 21.70509 ? 142 LEU B CD2 1 
ATOM   4063 N N   . ALA B 1 143 ? 15.44100  21.06200  37.88100  1.000 27.09257 ? 143 ALA B N   1 
ATOM   4064 C CA  . ALA B 1 143 ? 15.65000  21.67200  36.57200  1.000 23.39941 ? 143 ALA B CA  1 
ATOM   4065 C C   . ALA B 1 143 ? 14.36400  21.86500  35.78100  1.000 28.63904 ? 143 ALA B C   1 
ATOM   4066 O O   . ALA B 1 143 ? 14.39400  22.53900  34.74600  1.000 30.16417 ? 143 ALA B O   1 
ATOM   4067 C CB  . ALA B 1 143 ? 16.63200  20.83500  35.75000  1.000 22.84113 ? 143 ALA B CB  1 
ATOM   4068 N N   . ASP B 1 144 ? 13.24200  21.31700  36.24300  1.000 29.34943 ? 144 ASP B N   1 
ATOM   4069 C CA  . ASP B 1 144 ? 11.97800  21.36500  35.50800  1.000 27.19262 ? 144 ASP B CA  1 
ATOM   4070 C C   . ASP B 1 144 ? 11.25300  22.65900  35.85600  1.000 25.73909 ? 144 ASP B C   1 
ATOM   4071 O O   . ASP B 1 144 ? 10.41600  22.70100  36.75800  1.000 27.07146 ? 144 ASP B O   1 
ATOM   4072 C CB  . ASP B 1 144 ? 11.13100  20.14100  35.84100  1.000 31.30059 ? 144 ASP B CB  1 
ATOM   4073 C CG  . ASP B 1 144 ? 9.94900   19.96300  34.89600  1.000 34.28629 ? 144 ASP B CG  1 
ATOM   4074 O OD1 . ASP B 1 144 ? 9.53600   20.94300  34.24200  1.000 30.83711 ? 144 ASP B OD1 1 
ATOM   4075 O OD2 . ASP B 1 144 ? 9.42500   18.83200  34.81100  1.000 40.17702 ? 144 ASP B OD2 1 
ATOM   4076 N N   . VAL B 1 145 ? 11.56500  23.73300  35.11900  1.000 27.44957 ? 145 VAL B N   1 
ATOM   4077 C CA  . VAL B 1 145 ? 10.88000  25.01200  35.35000  1.000 24.38720 ? 145 VAL B CA  1 
ATOM   4078 C C   . VAL B 1 145 ? 9.37200   24.89700  35.17900  1.000 28.09030 ? 145 VAL B C   1 
ATOM   4079 O O   . VAL B 1 145 ? 8.63500   25.48800  35.98600  1.000 30.42727 ? 145 VAL B O   1 
ATOM   4080 C CB  . VAL B 1 145 ? 11.50400  26.11300  34.48000  1.000 28.90728 ? 145 VAL B CB  1 
ATOM   4081 C CG1 . VAL B 1 145 ? 10.73800  27.42300  34.65300  1.000 19.88081 ? 145 VAL B CG1 1 
ATOM   4082 C CG2 . VAL B 1 145 ? 12.97500  26.30500  34.83000  1.000 25.72610 ? 145 VAL B CG2 1 
ATOM   4083 N N   . PRO B 1 146 ? 8.83300   24.19800  34.16800  1.000 27.16018 ? 146 PRO B N   1 
ATOM   4084 C CA  . PRO B 1 146 ? 7.36700   24.03400  34.11400  1.000 28.37066 ? 146 PRO B CA  1 
ATOM   4085 C C   . PRO B 1 146 ? 6.77500   23.40500  35.36400  1.000 28.53467 ? 146 PRO B C   1 
ATOM   4086 O O   . PRO B 1 146 ? 5.68600   23.80900  35.79400  1.000 28.86132 ? 146 PRO B O   1 
ATOM   4087 C CB  . PRO B 1 146 ? 7.16100   23.13900  32.88100  1.000 30.13526 ? 146 PRO B CB  1 
ATOM   4088 C CG  . PRO B 1 146 ? 8.32000   23.45100  32.00000  1.000 31.05480 ? 146 PRO B CG  1 
ATOM   4089 C CD  . PRO B 1 146 ? 9.48000   23.74400  32.91700  1.000 29.17590 ? 146 PRO B CD  1 
ATOM   4090 N N   . ALA B 1 147 ? 7.45700   22.42500  35.96200  1.000 26.09504 ? 147 ALA B N   1 
ATOM   4091 C CA  . ALA B 1 147 ? 6.93700   21.81000  37.18000  1.000 23.65564 ? 147 ALA B CA  1 
ATOM   4092 C C   . ALA B 1 147 ? 6.88500   22.81500  38.32600  1.000 27.97400 ? 147 ALA B C   1 
ATOM   4093 O O   . ALA B 1 147 ? 5.93600   22.81500  39.11800  1.000 25.98093 ? 147 ALA B O   1 
ATOM   4094 C CB  . ALA B 1 147 ? 7.78000   20.59400  37.55900  1.000 24.33402 ? 147 ALA B CB  1 
ATOM   4095 N N   . TRP B 1 148 ? 7.89800   23.68200  38.42900  1.000 23.86422 ? 148 TRP B N   1 
ATOM   4096 C CA  . TRP B 1 148 ? 7.85100   24.76400  39.41000  1.000 26.08263 ? 148 TRP B CA  1 
ATOM   4097 C C   . TRP B 1 148 ? 6.59100   25.60700  39.23100  1.000 25.86899 ? 148 TRP B C   1 
ATOM   4098 O O   . TRP B 1 148 ? 5.86400   25.87000  40.19600  1.000 24.75530 ? 148 TRP B O   1 
ATOM   4099 C CB  . TRP B 1 148 ? 9.09500   25.64600  39.28500  1.000 20.77859 ? 148 TRP B CB  1 
ATOM   4100 C CG  . TRP B 1 148 ? 10.35900  25.09400  39.86500  1.000 21.77083 ? 148 TRP B CG  1 
ATOM   4101 C CD1 . TRP B 1 148 ? 11.28600  24.32600  39.22800  1.000 25.18074 ? 148 TRP B CD1 1 
ATOM   4102 C CD2 . TRP B 1 148 ? 10.86400  25.31500  41.19000  1.000 17.59031 ? 148 TRP B CD2 1 
ATOM   4103 N NE1 . TRP B 1 148 ? 12.32900  24.03700  40.07600  1.000 22.98715 ? 148 TRP B NE1 1 
ATOM   4104 C CE2 . TRP B 1 148 ? 12.09400  24.63400  41.28700  1.000 23.28120 ? 148 TRP B CE2 1 
ATOM   4105 C CE3 . TRP B 1 148 ? 10.39200  26.01600  42.30200  1.000 20.38440 ? 148 TRP B CE3 1 
ATOM   4106 C CZ2 . TRP B 1 148 ? 12.85700  24.62500  42.46100  1.000 19.11237 ? 148 TRP B CZ2 1 
ATOM   4107 C CZ3 . TRP B 1 148 ? 11.15400  26.00900  43.46900  1.000 21.21634 ? 148 TRP B CZ3 1 
ATOM   4108 C CH2 . TRP B 1 148 ? 12.37200  25.31600  43.53500  1.000 16.76069 ? 148 TRP B CH2 1 
ATOM   4109 N N   . ARG B 1 149 ? 6.30700   26.01600  37.98600  1.000 26.91254 ? 149 ARG B N   1 
ATOM   4110 C CA  . ARG B 1 149 ? 5.17000   26.89700  37.72200  1.000 25.04684 ? 149 ARG B CA  1 
ATOM   4111 C C   . ARG B 1 149 ? 3.84700   26.22200  38.05700  1.000 24.46276 ? 149 ARG B C   1 
ATOM   4112 O O   . ARG B 1 149 ? 2.93600   26.85900  38.59800  1.000 24.64393 ? 149 ARG B O   1 
ATOM   4113 C CB  . ARG B 1 149 ? 5.18200   27.34300  36.25900  1.000 30.43096 ? 149 ARG B CB  1 
ATOM   4114 C CG  . ARG B 1 149 ? 4.21200   28.47900  35.94100  1.000 31.27157 ? 149 ARG B CG  1 
ATOM   4115 C CD  . ARG B 1 149 ? 4.19300   28.80400  34.44800  1.000 34.42979 ? 149 ARG B CD  1 
ATOM   4116 N NE  . ARG B 1 149 ? 5.33700   28.23300  33.74300  1.000 39.67323 ? 149 ARG B NE  1 
ATOM   4117 C CZ  . ARG B 1 149 ? 6.45300   28.89100  33.45700  1.000 33.96830 ? 149 ARG B CZ  1 
ATOM   4118 N NH1 . ARG B 1 149 ? 6.60800   30.16400  33.78900  1.000 31.47850 ? 149 ARG B NH1 1 
ATOM   4119 N NH2 . ARG B 1 149 ? 7.43900   28.25500  32.82700  1.000 28.24772 ? 149 ARG B NH2 1 
ATOM   4120 N N   . ALA B 1 150 ? 3.72100   24.93200  37.73900  1.000 23.88510 ? 150 ALA B N   1 
ATOM   4121 C CA  . ALA B 1 150 ? 2.48300   24.21100  38.02100  1.000 24.12264 ? 150 ALA B CA  1 
ATOM   4122 C C   . ALA B 1 150 ? 2.23000   24.06100  39.52000  1.000 28.54637 ? 150 ALA B C   1 
ATOM   4123 O O   . ALA B 1 150 ? 1.07000   24.05300  39.95200  1.000 27.56062 ? 150 ALA B O   1 
ATOM   4124 C CB  . ALA B 1 150 ? 2.51500   22.83800  37.34600  1.000 27.13561 ? 150 ALA B CB  1 
ATOM   4125 N N   . ALA B 1 151 ? 3.28700   23.93400  40.32800  1.000 28.87936 ? 151 ALA B N   1 
ATOM   4126 C CA  . ALA B 1 151 ? 3.11200   23.77500  41.76900  1.000 24.77674 ? 151 ALA B CA  1 
ATOM   4127 C C   . ALA B 1 151 ? 2.74800   25.07600  42.47200  1.000 25.53765 ? 151 ALA B C   1 
ATOM   4128 O O   . ALA B 1 151 ? 2.38900   25.04300  43.65500  1.000 28.06499 ? 151 ALA B O   1 
ATOM   4129 C CB  . ALA B 1 151 ? 4.37700   23.19200  42.40100  1.000 21.02495 ? 151 ALA B CB  1 
ATOM   4130 N N   . LEU B 1 152 ? 2.83100   26.20900  41.78100  1.000 26.39985 ? 152 LEU B N   1 
ATOM   4131 C CA  . LEU B 1 152 ? 2.45000   27.47900  42.38300  1.000 28.09391 ? 152 LEU B CA  1 
ATOM   4132 C C   . LEU B 1 152 ? 0.99100   27.44900  42.82700  1.000 28.68562 ? 152 LEU B C   1 
ATOM   4133 O O   . LEU B 1 152 ? 0.12900   26.87300  42.15800  1.000 29.07194 ? 152 LEU B O   1 
ATOM   4134 C CB  . LEU B 1 152 ? 2.67800   28.61900  41.38900  1.000 23.93997 ? 152 LEU B CB  1 
ATOM   4135 C CG  . LEU B 1 152 ? 3.94000   29.47200  41.53200  1.000 30.34668 ? 152 LEU B CG  1 
ATOM   4136 C CD1 . LEU B 1 152 ? 5.15600   28.61500  41.81500  1.000 28.67758 ? 152 LEU B CD1 1 
ATOM   4137 C CD2 . LEU B 1 152 ? 4.15900   30.30600  40.27000  1.000 30.41985 ? 152 LEU B CD2 1 
ATOM   4138 N N   . ARG B 1 153 ? 0.72600   28.05600  43.97600  1.000 29.26464 ? 153 ARG B N   1 
ATOM   4139 C CA  . ARG B 1 153 ? -0.60400  28.26700  44.52000  1.000 27.02383 ? 153 ARG B CA  1 
ATOM   4140 C C   . ARG B 1 153 ? -0.80600  29.75600  44.75900  1.000 29.00718 ? 153 ARG B C   1 
ATOM   4141 O O   . ARG B 1 153 ? 0.16000   30.52600  44.75100  1.000 30.89364 ? 153 ARG B O   1 
ATOM   4142 C CB  . ARG B 1 153 ? -0.80200  27.49800  45.83500  1.000 24.41769 ? 153 ARG B CB  1 
ATOM   4143 C CG  . ARG B 1 153 ? -0.78300  25.98800  45.68800  1.000 29.52769 ? 153 ARG B CG  1 
ATOM   4144 C CD  . ARG B 1 153 ? -1.07400  25.30400  47.01500  1.000 32.39017 ? 153 ARG B CD  1 
ATOM   4145 N NE  . ARG B 1 153 ? -0.83100  23.86900  46.94700  1.000 38.11797 ? 153 ARG B NE  1 
ATOM   4146 C CZ  . ARG B 1 153 ? -0.95400  23.04000  47.97400  1.000 41.97584 ? 153 ARG B CZ  1 
ATOM   4147 N NH1 . ARG B 1 153 ? -1.32300  23.47200  49.17000  1.000 44.58486 ? 153 ARG B NH1 1 
ATOM   4148 N NH2 . ARG B 1 153 ? -0.69600  21.74600  47.79800  1.000 46.95978 ? 153 ARG B NH2 1 
ATOM   4149 N N   . PRO B 1 154 ? -2.05100  30.20600  44.94400  1.000 32.95904 ? 154 PRO B N   1 
ATOM   4150 C CA  . PRO B 1 154 ? -2.25500  31.62300  45.29400  1.000 32.08355 ? 154 PRO B CA  1 
ATOM   4151 C C   . PRO B 1 154 ? -1.56300  32.03700  46.58400  1.000 30.49216 ? 154 PRO B C   1 
ATOM   4152 O O   . PRO B 1 154 ? -1.17800  33.20600  46.71400  1.000 31.86684 ? 154 PRO B O   1 
ATOM   4153 C CB  . PRO B 1 154 ? -3.78400  31.74900  45.40100  1.000 30.21534 ? 154 PRO B CB  1 
ATOM   4154 C CG  . PRO B 1 154 ? -4.30100  30.34300  45.45800  1.000 35.54294 ? 154 PRO B CG  1 
ATOM   4155 C CD  . PRO B 1 154 ? -3.32600  29.51500  44.69000  1.000 31.96534 ? 154 PRO B CD  1 
ATOM   4156 N N   . ASN B 1 155 ? -1.37900  31.12300  47.53700  1.000 26.49082 ? 155 ASN B N   1 
ATOM   4157 C CA  . ASN B 1 155 ? -0.73900  31.44600  48.80600  1.000 27.87944 ? 155 ASN B CA  1 
ATOM   4158 C C   . ASN B 1 155 ? 0.74600   31.09700  48.82900  1.000 28.21156 ? 155 ASN B C   1 
ATOM   4159 O O   . ASN B 1 155 ? 1.34800   31.08400  49.91000  1.000 26.63691 ? 155 ASN B O   1 
ATOM   4160 C CB  . ASN B 1 155 ? -1.46300  30.75000  49.96600  1.000 24.60344 ? 155 ASN B CB  1 
ATOM   4161 C CG  . ASN B 1 155 ? -1.38100  29.23500  49.88800  1.000 29.66289 ? 155 ASN B CG  1 
ATOM   4162 O OD1 . ASN B 1 155 ? -1.27900  28.65600  48.80200  1.000 28.17688 ? 155 ASN B OD1 1 
ATOM   4163 N ND2 . ASN B 1 155 ? -1.42300  28.58400  51.04600  1.000 24.41170 ? 155 ASN B ND2 1 
ATOM   4164 N N   . THR B 1 156 ? 1.34800   30.81500  47.66800  1.000 25.49161 ? 156 THR B N   1 
ATOM   4165 C CA  . THR B 1 156 ? 2.78500   30.55700  47.59900  1.000 26.16822 ? 156 THR B CA  1 
ATOM   4166 C C   . THR B 1 156 ? 3.56100   31.83700  47.88200  1.000 28.36493 ? 156 THR B C   1 
ATOM   4167 O O   . THR B 1 156 ? 3.39300   32.84000  47.18000  1.000 28.73748 ? 156 THR B O   1 
ATOM   4168 C CB  . THR B 1 156 ? 3.18100   30.01700  46.22800  1.000 20.43559 ? 156 THR B CB  1 
ATOM   4169 O OG1 . THR B 1 156 ? 2.50900   28.78100  45.97600  1.000 24.90961 ? 156 THR B OG1 1 
ATOM   4170 C CG2 . THR B 1 156 ? 4.67700   29.77800  46.18500  1.000 20.25452 ? 156 THR B CG2 1 
ATOM   4171 N N   . ARG B 1 157 ? 4.43100   31.79800  48.89100  1.000 25.69628 ? 157 ARG B N   1 
ATOM   4172 C CA  . ARG B 1 157 ? 5.23400   32.95600  49.24700  1.000 21.73789 ? 157 ARG B CA  1 
ATOM   4173 C C   . ARG B 1 157 ? 6.72800   32.74100  49.07100  1.000 23.03489 ? 157 ARG B C   1 
ATOM   4174 O O   . ARG B 1 157 ? 7.48500   33.71700  49.15200  1.000 24.51252 ? 157 ARG B O   1 
ATOM   4175 C CB  . ARG B 1 157 ? 4.96100   33.37500  50.70000  1.000 20.45288 ? 157 ARG B CB  1 
ATOM   4176 C CG  . ARG B 1 157 ? 3.50700   33.70700  51.00400  1.000 27.50781 ? 157 ARG B CG  1 
ATOM   4177 C CD  . ARG B 1 157 ? 3.17500   35.17200  50.72500  1.000 30.98451 ? 157 ARG B CD  1 
ATOM   4178 N NE  . ARG B 1 157 ? 3.06900   35.46800  49.29900  1.000 40.05228 ? 157 ARG B NE  1 
ATOM   4179 C CZ  . ARG B 1 157 ? 1.98100   35.25600  48.56700  1.000 44.18762 ? 157 ARG B CZ  1 
ATOM   4180 N NH1 . ARG B 1 157 ? 0.89100   34.71100  49.08900  1.000 35.33994 ? 157 ARG B NH1 1 
ATOM   4181 N NH2 . ARG B 1 157 ? 1.98800   35.59800  47.27900  1.000 35.80468 ? 157 ARG B NH2 1 
ATOM   4182 N N   . MET B 1 158 ? 7.17700   31.51400  48.81400  1.000 21.70840 ? 158 MET B N   1 
ATOM   4183 C CA  . MET B 1 158 ? 8.60400   31.24000  48.76200  1.000 21.56743 ? 158 MET B CA  1 
ATOM   4184 C C   . MET B 1 158 ? 8.88800   30.10300  47.79700  1.000 17.71710 ? 158 MET B C   1 
ATOM   4185 O O   . MET B 1 158 ? 8.13300   29.13200  47.72400  1.000 19.46205 ? 158 MET B O   1 
ATOM   4186 C CB  . MET B 1 158 ? 9.16300   30.88800  50.14900  1.000 20.27816 ? 158 MET B CB  1 
ATOM   4187 C CG  . MET B 1 158 ? 10.64100  30.51500  50.14400  1.000 15.60146 ? 158 MET B CG  1 
ATOM   4188 S SD  . MET B 1 158 ? 11.33800  30.11800  51.76200  1.000 21.53064 ? 158 MET B SD  1 
ATOM   4189 C CE  . MET B 1 158 ? 11.10600  31.66500  52.63900  1.000 14.19193 ? 158 MET B CE  1 
ATOM   4190 N N   . LEU B 1 159 ? 9.98400   30.24300  47.06100  1.000 18.80896 ? 159 LEU B N   1 
ATOM   4191 C CA  . LEU B 1 159 ? 10.59300  29.16800  46.29700  1.000 16.67897 ? 159 LEU B CA  1 
ATOM   4192 C C   . LEU B 1 159 ? 11.96300  28.88200  46.90000  1.000 19.53283 ? 159 LEU B C   1 
ATOM   4193 O O   . LEU B 1 159 ? 12.78900  29.79300  47.03000  1.000 20.62644 ? 159 LEU B O   1 
ATOM   4194 C CB  . LEU B 1 159 ? 10.73200  29.54600  44.81900  1.000 16.00005 ? 159 LEU B CB  1 
ATOM   4195 C CG  . LEU B 1 159 ? 9.53700   29.42000  43.86600  1.000 18.68674 ? 159 LEU B CG  1 
ATOM   4196 C CD1 . LEU B 1 159 ? 8.36700   30.28800  44.28900  1.000 14.44916 ? 159 LEU B CD1 1 
ATOM   4197 C CD2 . LEU B 1 159 ? 9.98000   29.76100  42.44600  1.000 17.18725 ? 159 LEU B CD2 1 
ATOM   4198 N N   . PHE B 1 160 ? 12.20700  27.62600  47.26500  1.000 20.80683 ? 160 PHE B N   1 
ATOM   4199 C CA  . PHE B 1 160 ? 13.43400  27.23800  47.94900  1.000 17.48892 ? 160 PHE B CA  1 
ATOM   4200 C C   . PHE B 1 160 ? 14.17600  26.18700  47.13700  1.000 17.36681 ? 160 PHE B C   1 
ATOM   4201 O O   . PHE B 1 160 ? 13.57100  25.22700  46.65400  1.000 20.85885 ? 160 PHE B O   1 
ATOM   4202 C CB  . PHE B 1 160 ? 13.12500  26.69800  49.34800  1.000 21.40104 ? 160 PHE B CB  1 
ATOM   4203 C CG  . PHE B 1 160 ? 14.35000  26.36700  50.15500  1.000 19.34113 ? 160 PHE B CG  1 
ATOM   4204 C CD1 . PHE B 1 160 ? 14.94700  25.11900  50.05700  1.000 18.43355 ? 160 PHE B CD1 1 
ATOM   4205 C CD2 . PHE B 1 160 ? 14.89800  27.30300  51.01700  1.000 18.15338 ? 160 PHE B CD2 1 
ATOM   4206 C CE1 . PHE B 1 160 ? 16.07600  24.81100  50.79900  1.000 18.56518 ? 160 PHE B CE1 1 
ATOM   4207 C CE2 . PHE B 1 160 ? 16.02300  27.00500  51.76400  1.000 20.63271 ? 160 PHE B CE2 1 
ATOM   4208 C CZ  . PHE B 1 160 ? 16.61500  25.75800  51.65600  1.000 18.70186 ? 160 PHE B CZ  1 
ATOM   4209 N N   . LEU B 1 161 ? 15.48800  26.35300  47.00000  1.000 15.64156 ? 161 LEU B N   1 
ATOM   4210 C CA  . LEU B 1 161 ? 16.26900  25.36700  46.26800  1.000 16.38161 ? 161 LEU B CA  1 
ATOM   4211 C C   . LEU B 1 161 ? 17.73600  25.45600  46.65800  1.000 19.26565 ? 161 LEU B C   1 
ATOM   4212 O O   . LEU B 1 161 ? 18.19200  26.44300  47.24400  1.000 17.48024 ? 161 LEU B O   1 
ATOM   4213 C CB  . LEU B 1 161 ? 16.13000  25.55400  44.75500  1.000 16.93466 ? 161 LEU B CB  1 
ATOM   4214 C CG  . LEU B 1 161 ? 16.69900  26.87800  44.23800  1.000 23.19707 ? 161 LEU B CG  1 
ATOM   4215 C CD1 . LEU B 1 161 ? 18.00900  26.66500  43.50400  1.000 19.64512 ? 161 LEU B CD1 1 
ATOM   4216 C CD2 . LEU B 1 161 ? 15.69300  27.57600  43.34500  1.000 24.18294 ? 161 LEU B CD2 1 
ATOM   4217 N N   . GLU B 1 162 ? 18.46500  24.40300  46.30800  1.000 14.97020 ? 162 GLU B N   1 
ATOM   4218 C CA  . GLU B 1 162 ? 19.91600  24.41300  46.25300  1.000 16.47429 ? 162 GLU B CA  1 
ATOM   4219 C C   . GLU B 1 162 ? 20.34300  24.22500  44.80600  1.000 17.41018 ? 162 GLU B C   1 
ATOM   4220 O O   . GLU B 1 162 ? 19.67200  23.53200  44.03900  1.000 18.97187 ? 162 GLU B O   1 
ATOM   4221 C CB  . GLU B 1 162 ? 20.51800  23.29800  47.11800  1.000 17.63673 ? 162 GLU B CB  1 
ATOM   4222 C CG  . GLU B 1 162 ? 19.90500  23.18400  48.50000  1.000 18.18559 ? 162 GLU B CG  1 
ATOM   4223 C CD  . GLU B 1 162 ? 20.27500  21.88600  49.21600  1.000 18.55775 ? 162 GLU B CD  1 
ATOM   4224 O OE1 . GLU B 1 162 ? 21.05800  21.07800  48.66300  1.000 16.16148 ? 162 GLU B OE1 1 
ATOM   4225 O OE2 . GLU B 1 162 ? 19.76600  21.67400  50.33600  1.000 15.69493 ? 162 GLU B OE2 1 
ATOM   4226 N N   . THR B 1 163 ? 21.45400  24.86600  44.42500  1.000 21.70631 ? 163 THR B N   1 
ATOM   4227 C CA  . THR B 1 163 ? 22.05500  24.59100  43.11400  1.000 17.94298 ? 163 THR B CA  1 
ATOM   4228 C C   . THR B 1 163 ? 23.56100  24.82500  43.20000  1.000 18.89620 ? 163 THR B C   1 
ATOM   4229 O O   . THR B 1 163 ? 23.98300  25.85400  43.74900  1.000 18.92640 ? 163 THR B O   1 
ATOM   4230 C CB  . THR B 1 163 ? 21.46000  25.43500  41.97800  1.000 16.00383 ? 163 THR B CB  1 
ATOM   4231 O OG1 . THR B 1 163 ? 22.12600  25.11000  40.75400  1.000 16.59274 ? 163 THR B OG1 1 
ATOM   4232 C CG2 . THR B 1 163 ? 21.60000  26.94000  42.23800  1.000 14.18179 ? 163 THR B CG2 1 
ATOM   4233 N N   . PRO B 1 164 ? 24.39500  23.88300  42.73000  1.000 18.65307 ? 164 PRO B N   1 
ATOM   4234 C CA  . PRO B 1 164 ? 24.07300  22.52800  42.25600  1.000 17.03420 ? 164 PRO B CA  1 
ATOM   4235 C C   . PRO B 1 164 ? 23.41500  21.69300  43.34500  1.000 22.47494 ? 164 PRO B C   1 
ATOM   4236 O O   . PRO B 1 164 ? 23.56700  21.97300  44.53600  1.000 18.05676 ? 164 PRO B O   1 
ATOM   4237 C CB  . PRO B 1 164 ? 25.44500  21.95600  41.87100  1.000 19.33441 ? 164 PRO B CB  1 
ATOM   4238 C CG  . PRO B 1 164 ? 26.27300  23.15400  41.52400  1.000 18.66542 ? 164 PRO B CG  1 
ATOM   4239 C CD  . PRO B 1 164 ? 25.80600  24.22500  42.47700  1.000 19.72369 ? 164 PRO B CD  1 
ATOM   4240 N N   . SER B 1 165 ? 22.66200  20.67300  42.95200  1.000 17.45639 ? 165 SER B N   1 
ATOM   4241 C CA  . SER B 1 165 ? 21.96300  19.83600  43.90400  1.000 14.93937 ? 165 SER B CA  1 
ATOM   4242 C C   . SER B 1 165 ? 22.88200  18.73400  44.41900  1.000 19.97998 ? 165 SER B C   1 
ATOM   4243 O O   . SER B 1 165 ? 23.94900  18.45800  43.86800  1.000 18.17344 ? 165 SER B O   1 
ATOM   4244 C CB  . SER B 1 165 ? 20.72700  19.21200  43.26800  1.000 19.77583 ? 165 SER B CB  1 
ATOM   4245 O OG  . SER B 1 165 ? 21.10700  18.07300  42.52000  1.000 18.94980 ? 165 SER B OG  1 
ATOM   4246 N N   . ASN B 1 166 ? 22.44600  18.09800  45.50000  1.000 19.76844 ? 166 ASN B N   1 
ATOM   4247 C CA  . ASN B 1 166 ? 23.10200  16.92100  46.02400  1.000 22.44830 ? 166 ASN B CA  1 
ATOM   4248 C C   . ASN B 1 166 ? 22.16400  15.72500  45.91800  1.000 19.44820 ? 166 ASN B C   1 
ATOM   4249 O O   . ASN B 1 166 ? 20.98400  15.84000  46.26600  1.000 21.64229 ? 166 ASN B O   1 
ATOM   4250 C CB  . ASN B 1 166 ? 23.51000  17.13200  47.49200  1.000 20.65996 ? 166 ASN B CB  1 
ATOM   4251 C CG  . ASN B 1 166 ? 23.82300  15.83000  48.20200  1.000 21.38133 ? 166 ASN B CG  1 
ATOM   4252 O OD1 . ASN B 1 166 ? 24.92800  15.29900  48.09200  1.000 19.63832 ? 166 ASN B OD1 1 
ATOM   4253 N ND2 . ASN B 1 166 ? 22.84300  15.30400  48.92900  1.000 21.26358 ? 166 ASN B ND2 1 
ATOM   4254 N N   . PRO B 1 167 ? 22.65400  14.55900  45.47200  1.000 19.08964 ? 167 PRO B N   1 
ATOM   4255 C CA  . PRO B 1 167 ? 24.02800  14.24600  45.07100  1.000 19.19528 ? 167 PRO B CA  1 
ATOM   4256 C C   . PRO B 1 167 ? 24.25800  14.24800  43.55800  1.000 20.16040 ? 167 PRO B C   1 
ATOM   4257 O O   . PRO B 1 167 ? 25.35100  13.91200  43.11300  1.000 21.49020 ? 167 PRO B O   1 
ATOM   4258 C CB  . PRO B 1 167 ? 24.21900  12.84700  45.66100  1.000 18.61911 ? 167 PRO B CB  1 
ATOM   4259 C CG  . PRO B 1 167 ? 22.85400  12.20600  45.47700  1.000 18.94990 ? 167 PRO B CG  1 
ATOM   4260 C CD  . PRO B 1 167 ? 21.83900  13.33100  45.57100  1.000 21.95966 ? 167 PRO B CD  1 
ATOM   4261 N N   . LEU B 1 168 ? 23.27500  14.62000  42.74000  1.000 19.75864 ? 168 LEU B N   1 
ATOM   4262 C CA  . LEU B 1 168 ? 23.41400  14.52700  41.29000  1.000 22.46947 ? 168 LEU B CA  1 
ATOM   4263 C C   . LEU B 1 168 ? 24.00800  15.77500  40.65600  1.000 23.15704 ? 168 LEU B C   1 
ATOM   4264 O O   . LEU B 1 168 ? 24.25600  15.77300  39.44600  1.000 23.65280 ? 168 LEU B O   1 
ATOM   4265 C CB  . LEU B 1 168 ? 22.05800  14.23500  40.64400  1.000 20.02793 ? 168 LEU B CB  1 
ATOM   4266 C CG  . LEU B 1 168 ? 21.36900  12.96300  41.13600  1.000 24.44708 ? 168 LEU B CG  1 
ATOM   4267 C CD1 . LEU B 1 168 ? 20.15500  12.62700  40.26500  1.000 23.18836 ? 168 LEU B CD1 1 
ATOM   4268 C CD2 . LEU B 1 168 ? 22.36600  11.81400  41.16400  1.000 19.88250 ? 168 LEU B CD2 1 
ATOM   4269 N N   . THR B 1 169 ? 24.25000  16.82700  41.43900  1.000 22.17153 ? 169 THR B N   1 
ATOM   4270 C CA  . THR B 1 169 ? 24.75500  18.10600  40.93000  1.000 20.15352 ? 169 THR B CA  1 
ATOM   4271 C C   . THR B 1 169 ? 23.87600  18.63600  39.80200  1.000 22.47358 ? 169 THR B C   1 
ATOM   4272 O O   . THR B 1 169 ? 24.35900  19.18500  38.80900  1.000 26.41515 ? 169 THR B O   1 
ATOM   4273 C CB  . THR B 1 169 ? 26.21100  18.00100  40.47600  1.000 19.86605 ? 169 THR B CB  1 
ATOM   4274 O OG1 . THR B 1 169 ? 26.26500  17.44300  39.15600  1.000 18.06512 ? 169 THR B OG1 1 
ATOM   4275 C CG2 . THR B 1 169 ? 27.01700  17.13600  41.43500  1.000 19.24147 ? 169 THR B CG2 1 
ATOM   4276 N N   . GLU B 1 170 ? 22.56900  18.45800  39.94800  1.000 21.24596 ? 170 GLU B N   1 
ATOM   4277 C CA  . GLU B 1 170 ? 21.64300  19.07800  39.01900  1.000 22.40754 ? 170 GLU B CA  1 
ATOM   4278 C C   . GLU B 1 170 ? 21.61400  20.58600  39.26000  1.000 20.40264 ? 170 GLU B C   1 
ATOM   4279 O O   . GLU B 1 170 ? 21.95000  21.07100  40.34200  1.000 18.38938 ? 170 GLU B O   1 
ATOM   4280 C CB  . GLU B 1 170 ? 20.25500  18.45700  39.17200  1.000 19.85176 ? 170 GLU B CB  1 
ATOM   4281 C CG  . GLU B 1 170 ? 20.24700  16.96400  38.88400  1.000 27.01676 ? 170 GLU B CG  1 
ATOM   4282 C CD  . GLU B 1 170 ? 19.05000  16.24800  39.48000  1.000 33.19406 ? 170 GLU B CD  1 
ATOM   4283 O OE1 . GLU B 1 170 ? 18.84900  16.33200  40.71200  1.000 32.01954 ? 170 GLU B OE1 1 
ATOM   4284 O OE2 . GLU B 1 170 ? 18.31200  15.59600  38.71300  1.000 42.09717 ? 170 GLU B OE2 1 
ATOM   4285 N N   . ILE B 1 171 ? 21.22700  21.33500  38.23000  1.000 20.82161 ? 171 ILE B N   1 
ATOM   4286 C CA  . ILE B 1 171 ? 21.34200  22.79000  38.23600  1.000 19.69905 ? 171 ILE B CA  1 
ATOM   4287 C C   . ILE B 1 171 ? 19.95000  23.40000  38.19700  1.000 19.65589 ? 171 ILE B C   1 
ATOM   4288 O O   . ILE B 1 171 ? 19.07300  22.93200  37.46300  1.000 19.59011 ? 171 ILE B O   1 
ATOM   4289 C CB  . ILE B 1 171 ? 22.19700  23.30100  37.05800  1.000 18.68766 ? 171 ILE B CB  1 
ATOM   4290 C CG1 . ILE B 1 171 ? 23.54800  22.59400  37.02600  1.000 20.20558 ? 171 ILE B CG1 1 
ATOM   4291 C CG2 . ILE B 1 171 ? 22.42200  24.79600  37.17400  1.000 19.04946 ? 171 ILE B CG2 1 
ATOM   4292 C CD1 . ILE B 1 171 ? 24.41300  22.88800  38.22700  1.000 16.73737 ? 171 ILE B CD1 1 
ATOM   4293 N N   . GLY B 1 172 ? 19.74600  24.43300  39.01000  1.000 17.95419 ? 172 GLY B N   1 
ATOM   4294 C CA  . GLY B 1 172 ? 18.52200  25.21200  38.99800  1.000 16.65682 ? 172 GLY B CA  1 
ATOM   4295 C C   . GLY B 1 172 ? 18.77400  26.55300  38.32700  1.000 20.96254 ? 172 GLY B C   1 
ATOM   4296 O O   . GLY B 1 172 ? 19.77800  27.21500  38.60100  1.000 19.27188 ? 172 GLY B O   1 
ATOM   4297 N N   . ASP B 1 173 ? 17.85300  26.92800  37.43700  1.000 25.07393 ? 173 ASP B N   1 
ATOM   4298 C CA  . ASP B 1 173 ? 17.91100  28.19100  36.70000  1.000 18.44460 ? 173 ASP B CA  1 
ATOM   4299 C C   . ASP B 1 173 ? 17.46100  29.29700  37.64100  1.000 19.90745 ? 173 ASP B C   1 
ATOM   4300 O O   . ASP B 1 173 ? 16.27600  29.62400  37.73400  1.000 19.82452 ? 173 ASP B O   1 
ATOM   4301 C CB  . ASP B 1 173 ? 17.03500  28.12000  35.45500  1.000 24.90882 ? 173 ASP B CB  1 
ATOM   4302 C CG  . ASP B 1 173 ? 17.25900  29.28600  34.50700  1.000 27.24138 ? 173 ASP B CG  1 
ATOM   4303 O OD1 . ASP B 1 173 ? 17.64800  30.39100  34.96400  1.000 25.58581 ? 173 ASP B OD1 1 
ATOM   4304 O OD2 . ASP B 1 173 ? 17.03400  29.09000  33.29400  1.000 28.44911 ? 173 ASP B OD2 1 
ATOM   4305 N N   . MET B 1 174 ? 18.43200  29.89100  38.33600  1.000 19.94283 ? 174 MET B N   1 
ATOM   4306 C CA  . MET B 1 174 ? 18.11700  30.85000  39.38800  1.000 18.05541 ? 174 MET B CA  1 
ATOM   4307 C C   . MET B 1 174 ? 17.34400  32.04600  38.84700  1.000 22.34685 ? 174 MET B C   1 
ATOM   4308 O O   . MET B 1 174 ? 16.33400  32.46300  39.43000  1.000 21.10245 ? 174 MET B O   1 
ATOM   4309 C CB  . MET B 1 174 ? 19.40500  31.30500  40.06900  1.000 18.41474 ? 174 MET B CB  1 
ATOM   4310 C CG  . MET B 1 174 ? 20.02300  30.23500  40.94900  1.000 25.54265 ? 174 MET B CG  1 
ATOM   4311 S SD  . MET B 1 174 ? 21.33900  30.88100  41.98700  1.000 22.70056 ? 174 MET B SD  1 
ATOM   4312 C CE  . MET B 1 174 ? 22.68000  30.95300  40.80100  1.000 15.48628 ? 174 MET B CE  1 
ATOM   4313 N N   . GLN B 1 175 ? 17.80300  32.61500  37.73000  1.000 20.25750 ? 175 GLN B N   1 
ATOM   4314 C CA  . GLN B 1 175 ? 17.15400  33.81300  37.20600  1.000 23.56057 ? 175 GLN B CA  1 
ATOM   4315 C C   . GLN B 1 175 ? 15.70800  33.52100  36.81900  1.000 22.29299 ? 175 GLN B C   1 
ATOM   4316 O O   . GLN B 1 175 ? 14.79000  34.27000  37.18100  1.000 20.61611 ? 175 GLN B O   1 
ATOM   4317 C CB  . GLN B 1 175 ? 17.94100  34.35700  36.01200  1.000 20.15379 ? 175 GLN B CB  1 
ATOM   4318 C CG  . GLN B 1 175 ? 17.47300  35.72200  35.54000  1.000 22.18634 ? 175 GLN B CG  1 
ATOM   4319 C CD  . GLN B 1 175 ? 17.54800  36.76600  36.63900  1.000 26.49799 ? 175 GLN B CD  1 
ATOM   4320 O OE1 . GLN B 1 175 ? 18.63600  37.17000  37.05800  1.000 24.28726 ? 175 GLN B OE1 1 
ATOM   4321 N NE2 . GLN B 1 175 ? 16.39000  37.20200  37.11900  1.000 22.04832 ? 175 GLN B NE2 1 
ATOM   4322 N N   . ALA B 1 176 ? 15.48400  32.40300  36.11900  1.000 23.56618 ? 176 ALA B N   1 
ATOM   4323 C CA  . ALA B 1 176 ? 14.13100  32.04500  35.70200  1.000 22.28737 ? 176 ALA B CA  1 
ATOM   4324 C C   . ALA B 1 176 ? 13.22900  31.81900  36.90500  1.000 22.79613 ? 176 ALA B C   1 
ATOM   4325 O O   . ALA B 1 176 ? 12.06100  32.23100  36.90500  1.000 19.58529 ? 176 ALA B O   1 
ATOM   4326 C CB  . ALA B 1 176 ? 14.16600  30.79700  34.81900  1.000 18.37859 ? 176 ALA B CB  1 
ATOM   4327 N N   . LEU B 1 177 ? 13.75400  31.16900  37.94600  1.000 19.24516 ? 177 LEU B N   1 
ATOM   4328 C CA  . LEU B 1 177 ? 12.94600  30.92700  39.13600  1.000 20.82924 ? 177 LEU B CA  1 
ATOM   4329 C C   . LEU B 1 177 ? 12.74800  32.20400  39.94200  1.000 22.38775 ? 177 LEU B C   1 
ATOM   4330 O O   . LEU B 1 177 ? 11.68800  32.39200  40.55400  1.000 20.36005 ? 177 LEU B O   1 
ATOM   4331 C CB  . LEU B 1 177 ? 13.58800  29.82200  39.97600  1.000 20.30632 ? 177 LEU B CB  1 
ATOM   4332 C CG  . LEU B 1 177 ? 13.58400  28.47400  39.24200  1.000 23.33026 ? 177 LEU B CG  1 
ATOM   4333 C CD1 . LEU B 1 177 ? 14.39700  27.42100  39.97700  1.000 21.02522 ? 177 LEU B CD1 1 
ATOM   4334 C CD2 . LEU B 1 177 ? 12.14900  27.99500  39.03400  1.000 20.09532 ? 177 LEU B CD2 1 
ATOM   4335 N N   . ALA B 1 178 ? 13.74500  33.09500  39.94800  1.000 22.97205 ? 178 ALA B N   1 
ATOM   4336 C CA  . ALA B 1 178 ? 13.55400  34.40900  40.55200  1.000 21.60101 ? 178 ALA B CA  1 
ATOM   4337 C C   . ALA B 1 178 ? 12.41800  35.15200  39.86500  1.000 21.36928 ? 178 ALA B C   1 
ATOM   4338 O O   . ALA B 1 178 ? 11.52800  35.70400  40.52600  1.000 21.63343 ? 178 ALA B O   1 
ATOM   4339 C CB  . ALA B 1 178 ? 14.85000  35.22000  40.47600  1.000 21.12848 ? 178 ALA B CB  1 
ATOM   4340 N N   . ASP B 1 179 ? 12.42400  35.15700  38.52700  1.000 22.54881 ? 179 ASP B N   1 
ATOM   4341 C CA  . ASP B 1 179 ? 11.34800  35.80300  37.78400  1.000 25.18511 ? 179 ASP B CA  1 
ATOM   4342 C C   . ASP B 1 179 ? 10.00400  35.15100  38.09100  1.000 22.02333 ? 179 ASP B C   1 
ATOM   4343 O O   . ASP B 1 179 ? 9.00100   35.84400  38.30000  1.000 23.22840 ? 179 ASP B O   1 
ATOM   4344 C CB  . ASP B 1 179 ? 11.64500  35.75900  36.28200  1.000 25.76672 ? 179 ASP B CB  1 
ATOM   4345 C CG  . ASP B 1 179 ? 12.87700  36.58500  35.89500  1.000 29.96623 ? 179 ASP B CG  1 
ATOM   4346 O OD1 . ASP B 1 179 ? 13.26500  37.48600  36.67300  1.000 21.81431 ? 179 ASP B OD1 1 
ATOM   4347 O OD2 . ASP B 1 179 ? 13.45000  36.33500  34.80400  1.000 25.65943 ? 179 ASP B OD2 1 
ATOM   4348 N N   . LEU B 1 180 ? 9.97100   33.81900  38.14500  1.000 19.64595 ? 180 LEU B N   1 
ATOM   4349 C CA  . LEU B 1 180 ? 8.73800   33.11400  38.48100  1.000 19.85196 ? 180 LEU B CA  1 
ATOM   4350 C C   . LEU B 1 180 ? 8.22700   33.53300  39.85300  1.000 20.09394 ? 180 LEU B C   1 
ATOM   4351 O O   . LEU B 1 180 ? 7.04400   33.85600  40.01600  1.000 19.99438 ? 180 LEU B O   1 
ATOM   4352 C CB  . LEU B 1 180 ? 8.97600   31.60300  38.42900  1.000 18.60608 ? 180 LEU B CB  1 
ATOM   4353 C CG  . LEU B 1 180 ? 7.77400   30.67700  38.62000  1.000 26.96858 ? 180 LEU B CG  1 
ATOM   4354 C CD1 . LEU B 1 180 ? 6.67500   31.00900  37.61700  1.000 25.10074 ? 180 LEU B CD1 1 
ATOM   4355 C CD2 . LEU B 1 180 ? 8.20700   29.21800  38.48400  1.000 23.09401 ? 180 LEU B CD2 1 
ATOM   4356 N N   . ALA B 1 181 ? 9.11900   33.56400  40.84800  1.000 20.80742 ? 181 ALA B N   1 
ATOM   4357 C CA  . ALA B 1 181 ? 8.70900   33.92300  42.20200  1.000 21.43500 ? 181 ALA B CA  1 
ATOM   4358 C C   . ALA B 1 181 ? 8.20400   35.35800  42.27100  1.000 21.73246 ? 181 ALA B C   1 
ATOM   4359 O O   . ALA B 1 181 ? 7.18200   35.63900  42.91000  1.000 24.37243 ? 181 ALA B O   1 
ATOM   4360 C CB  . ALA B 1 181 ? 9.87600   33.72700  43.17000  1.000 22.59452 ? 181 ALA B CB  1 
ATOM   4361 N N   . HIS B 1 182 ? 8.90700   36.27900  41.61600  1.000 21.32382 ? 182 HIS B N   1 
ATOM   4362 C CA  . HIS B 1 182 ? 8.61500   37.69600  41.78800  1.000 22.83195 ? 182 HIS B CA  1 
ATOM   4363 C C   . HIS B 1 182 ? 7.32300   38.10200  41.09200  1.000 23.53188 ? 182 HIS B C   1 
ATOM   4364 O O   . HIS B 1 182 ? 6.59100   38.95500  41.60400  1.000 26.40289 ? 182 HIS B O   1 
ATOM   4365 C CB  . HIS B 1 182 ? 9.80200   38.51500  41.28800  1.000 21.81989 ? 182 HIS B CB  1 
ATOM   4366 C CG  . HIS B 1 182 ? 11.05700  38.26300  42.06000  1.000 20.25065 ? 182 HIS B CG  1 
ATOM   4367 N ND1 . HIS B 1 182 ? 12.30900  38.31700  41.48900  1.000 20.53433 ? 182 HIS B ND1 1 
ATOM   4368 C CD2 . HIS B 1 182 ? 11.25000  37.94400  43.36300  1.000 20.29043 ? 182 HIS B CD2 1 
ATOM   4369 C CE1 . HIS B 1 182 ? 13.22000  38.04500  42.40600  1.000 20.37598 ? 182 HIS B CE1 1 
ATOM   4370 N NE2 . HIS B 1 182 ? 12.60300  37.81300  43.55100  1.000 20.12210 ? 182 HIS B NE2 1 
ATOM   4371 N N   . VAL B 1 183 ? 7.01900   37.49500  39.94200  1.000 26.12604 ? 183 VAL B N   1 
ATOM   4372 C CA  . VAL B 1 183 ? 5.74000   37.74800  39.28500  1.000 25.65082 ? 183 VAL B CA  1 
ATOM   4373 C C   . VAL B 1 183 ? 4.57700   37.33200  40.18100  1.000 31.55279 ? 183 VAL B C   1 
ATOM   4374 O O   . VAL B 1 183 ? 3.49300   37.92600  40.12100  1.000 33.01027 ? 183 VAL B O   1 
ATOM   4375 C CB  . VAL B 1 183 ? 5.69800   37.02800  37.92300  1.000 27.20988 ? 183 VAL B CB  1 
ATOM   4376 C CG1 . VAL B 1 183 ? 4.32200   37.14300  37.29700  1.000 34.99007 ? 183 VAL B CG1 1 
ATOM   4377 C CG2 . VAL B 1 183 ? 6.74300   37.61000  36.99100  1.000 26.45982 ? 183 VAL B CG2 1 
ATOM   4378 N N   . HIS B 1 184 ? 4.77600   36.32400  41.03400  1.000 23.81140 ? 184 HIS B N   1 
ATOM   4379 C CA  . HIS B 1 184 ? 3.72800   35.84100  41.92200  1.000 25.79831 ? 184 HIS B CA  1 
ATOM   4380 C C   . HIS B 1 184 ? 3.92300   36.30300  43.35900  1.000 25.94303 ? 184 HIS B C   1 
ATOM   4381 O O   . HIS B 1 184 ? 3.41500   35.65900  44.28300  1.000 26.80389 ? 184 HIS B O   1 
ATOM   4382 C CB  . HIS B 1 184 ? 3.63900   34.31500  41.85900  1.000 25.91205 ? 184 HIS B CB  1 
ATOM   4383 C CG  . HIS B 1 184 ? 3.32400   33.78900  40.49300  1.000 32.89114 ? 184 HIS B CG  1 
ATOM   4384 N ND1 . HIS B 1 184 ? 4.24700   33.77900  39.46800  1.000 34.50714 ? 184 HIS B ND1 1 
ATOM   4385 C CD2 . HIS B 1 184 ? 2.18600   33.26700  39.97900  1.000 31.52504 ? 184 HIS B CD2 1 
ATOM   4386 C CE1 . HIS B 1 184 ? 3.69200   33.27300  38.38100  1.000 32.97640 ? 184 HIS B CE1 1 
ATOM   4387 N NE2 . HIS B 1 184 ? 2.44100   32.95400  38.66400  1.000 36.32777 ? 184 HIS B NE2 1 
ATOM   4388 N N   . ASP B 1 185 ? 4.65500   37.40000  43.56300  1.000 25.73814 ? 185 ASP B N   1 
ATOM   4389 C CA  . ASP B 1 185 ? 4.80800   38.02200  44.88100  1.000 28.52994 ? 185 ASP B CA  1 
ATOM   4390 C C   . ASP B 1 185 ? 5.34300   37.03200  45.91600  1.000 27.17890 ? 185 ASP B C   1 
ATOM   4391 O O   . ASP B 1 185 ? 4.90400   37.00100  47.06800  1.000 26.22024 ? 185 ASP B O   1 
ATOM   4392 C CB  . ASP B 1 185 ? 3.49300   38.65400  45.34300  1.000 31.76975 ? 185 ASP B CB  1 
ATOM   4393 C CG  . ASP B 1 185 ? 3.19100   39.96000  44.61600  1.000 43.13130 ? 185 ASP B CG  1 
ATOM   4394 O OD1 . ASP B 1 185 ? 4.05000   40.87000  44.64400  1.000 42.75234 ? 185 ASP B OD1 1 
ATOM   4395 O OD2 . ASP B 1 185 ? 2.10800   40.07100  44.00300  1.000 47.32356 ? 185 ASP B OD2 1 
ATOM   4396 N N   . ALA B 1 186 ? 6.30800   36.22000  45.49400  1.000 25.62323 ? 186 ALA B N   1 
ATOM   4397 C CA  . ALA B 1 186 ? 7.00800   35.28300  46.35500  1.000 25.21022 ? 186 ALA B CA  1 
ATOM   4398 C C   . ALA B 1 186 ? 8.50300   35.57000  46.30100  1.000 27.55484 ? 186 ALA B C   1 
ATOM   4399 O O   . ALA B 1 186 ? 9.00300   36.19500  45.36100  1.000 23.42527 ? 186 ALA B O   1 
ATOM   4400 C CB  . ALA B 1 186 ? 6.73600   33.83300  45.93700  1.000 21.26225 ? 186 ALA B CB  1 
ATOM   4401 N N   . TRP B 1 187 ? 9.21300   35.11200  47.32700  1.000 22.73113 ? 187 TRP B N   1 
ATOM   4402 C CA  . TRP B 1 187 ? 10.65600  35.27600  47.40700  1.000 20.36911 ? 187 TRP B CA  1 
ATOM   4403 C C   . TRP B 1 187 ? 11.35500  34.02200  46.90100  1.000 20.08489 ? 187 TRP B C   1 
ATOM   4404 O O   . TRP B 1 187 ? 10.84000  32.90700  47.02200  1.000 21.76885 ? 187 TRP B O   1 
ATOM   4405 C CB  . TRP B 1 187 ? 11.10100  35.57400  48.84300  1.000 19.73808 ? 187 TRP B CB  1 
ATOM   4406 C CG  . TRP B 1 187 ? 10.66000  36.91200  49.35200  1.000 22.82724 ? 187 TRP B CG  1 
ATOM   4407 C CD1 . TRP B 1 187 ? 11.20800  38.12800  49.05100  1.000 26.15000 ? 187 TRP B CD1 1 
ATOM   4408 C CD2 . TRP B 1 187 ? 9.58800   37.17100  50.26400  1.000 22.71037 ? 187 TRP B CD2 1 
ATOM   4409 N NE1 . TRP B 1 187 ? 10.53600  39.12800  49.71500  1.000 32.71630 ? 187 TRP B NE1 1 
ATOM   4410 C CE2 . TRP B 1 187 ? 9.53700   38.56500  50.46500  1.000 27.98292 ? 187 TRP B CE2 1 
ATOM   4411 C CE3 . TRP B 1 187 ? 8.66000   36.36100  50.92200  1.000 31.00667 ? 187 TRP B CE3 1 
ATOM   4412 C CZ2 . TRP B 1 187 ? 8.59800   39.16300  51.30000  1.000 37.48911 ? 187 TRP B CZ2 1 
ATOM   4413 C CZ3 . TRP B 1 187 ? 7.72500   36.95900  51.75400  1.000 36.72282 ? 187 TRP B CZ3 1 
ATOM   4414 C CH2 . TRP B 1 187 ? 7.70400   38.34400  51.93700  1.000 37.51634 ? 187 TRP B CH2 1 
ATOM   4415 N N   . LEU B 1 188 ? 12.53300  34.21800  46.32000  1.000 18.95437 ? 188 LEU B N   1 
ATOM   4416 C CA  . LEU B 1 188 ? 13.41200  33.12000  45.94500  1.000 19.94201 ? 188 LEU B CA  1 
ATOM   4417 C C   . LEU B 1 188 ? 14.50000  33.00000  47.00400  1.000 19.76795 ? 188 LEU B C   1 
ATOM   4418 O O   . LEU B 1 188 ? 15.20000  33.97800  47.29200  1.000 20.17217 ? 188 LEU B O   1 
ATOM   4419 C CB  . LEU B 1 188 ? 14.03000  33.34400  44.56800  1.000 16.58820 ? 188 LEU B CB  1 
ATOM   4420 C CG  . LEU B 1 188 ? 15.03800  32.26700  44.15400  1.000 21.96001 ? 188 LEU B CG  1 
ATOM   4421 C CD1 . LEU B 1 188 ? 14.34400  30.93900  43.93600  1.000 19.45343 ? 188 LEU B CD1 1 
ATOM   4422 C CD2 . LEU B 1 188 ? 15.81500  32.68000  42.90800  1.000 17.36296 ? 188 LEU B CD2 1 
ATOM   4423 N N   . VAL B 1 189 ? 14.63200  31.81100  47.58400  1.000 21.69244 ? 189 VAL B N   1 
ATOM   4424 C CA  . VAL B 1 189 ? 15.61400  31.53200  48.62600  1.000 16.26328 ? 189 VAL B CA  1 
ATOM   4425 C C   . VAL B 1 189 ? 16.51500  30.41800  48.11700  1.000 18.74063 ? 189 VAL B C   1 
ATOM   4426 O O   . VAL B 1 189 ? 16.03100  29.33600  47.76200  1.000 20.87877 ? 189 VAL B O   1 
ATOM   4427 C CB  . VAL B 1 189 ? 14.94300  31.14000  49.95000  1.000 16.43350 ? 189 VAL B CB  1 
ATOM   4428 C CG1 . VAL B 1 189 ? 15.98400  30.73700  50.97700  1.000 20.38336 ? 189 VAL B CG1 1 
ATOM   4429 C CG2 . VAL B 1 189 ? 14.08800  32.28900  50.47500  1.000 17.62312 ? 189 VAL B CG2 1 
ATOM   4430 N N   . VAL B 1 190 ? 17.81900  30.67800  48.07900  1.000 16.65042 ? 190 VAL B N   1 
ATOM   4431 C CA  . VAL B 1 190 ? 18.79100  29.74500  47.52700  1.000 14.85554 ? 190 VAL B CA  1 
ATOM   4432 C C   . VAL B 1 190 ? 19.77500  29.34600  48.61800  1.000 17.37898 ? 190 VAL B C   1 
ATOM   4433 O O   . VAL B 1 190 ? 20.40600  30.20600  49.24500  1.000 16.29768 ? 190 VAL B O   1 
ATOM   4434 C CB  . VAL B 1 190 ? 19.53700  30.34200  46.32100  1.000 14.52971 ? 190 VAL B CB  1 
ATOM   4435 C CG1 . VAL B 1 190 ? 20.50400  29.32200  45.76600  1.000 12.83086 ? 190 VAL B CG1 1 
ATOM   4436 C CG2 . VAL B 1 190 ? 18.54700  30.78600  45.24800  1.000 13.02187 ? 190 VAL B CG2 1 
ATOM   4437 N N   . ASP B 1 191 ? 19.90400  28.04000  48.82800  1.000 16.87072 ? 191 ASP B N   1 
ATOM   4438 C CA  . ASP B 1 191 ? 20.89900  27.46200  49.71600  1.000 15.65106 ? 191 ASP B CA  1 
ATOM   4439 C C   . ASP B 1 191 ? 22.17900  27.26700  48.90600  1.000 18.23673 ? 191 ASP B C   1 
ATOM   4440 O O   . ASP B 1 191 ? 22.18900  26.51600  47.92500  1.000 14.93718 ? 191 ASP B O   1 
ATOM   4441 C CB  . ASP B 1 191 ? 20.36000  26.14600  50.28400  1.000 15.51458 ? 191 ASP B CB  1 
ATOM   4442 C CG  . ASP B 1 191 ? 21.32900  25.43700  51.22200  1.000 16.27156 ? 191 ASP B CG  1 
ATOM   4443 O OD1 . ASP B 1 191 ? 22.55800  25.52600  51.03100  1.000 16.56564 ? 191 ASP B OD1 1 
ATOM   4444 O OD2 . ASP B 1 191 ? 20.84100  24.74900  52.14800  1.000 18.64347 ? 191 ASP B OD2 1 
ATOM   4445 N N   . ASN B 1 192 ? 23.25700  27.93200  49.32500  1.000 16.98149 ? 192 ASN B N   1 
ATOM   4446 C CA  . ASN B 1 192 ? 24.46300  28.08400  48.52100  1.000 16.80366 ? 192 ASN B CA  1 
ATOM   4447 C C   . ASN B 1 192 ? 25.65400  27.29900  49.08400  1.000 17.31032 ? 192 ASN B C   1 
ATOM   4448 O O   . ASN B 1 192 ? 26.80700  27.68300  48.87300  1.000 17.78677 ? 192 ASN B O   1 
ATOM   4449 C CB  . ASN B 1 192 ? 24.79800  29.57500  48.39400  1.000 14.23330 ? 192 ASN B CB  1 
ATOM   4450 C CG  . ASN B 1 192 ? 25.78100  29.87500  47.27100  1.000 16.91186 ? 192 ASN B CG  1 
ATOM   4451 O OD1 . ASN B 1 192 ? 25.95500  29.08000  46.34500  1.000 16.54156 ? 192 ASN B OD1 1 
ATOM   4452 N ND2 . ASN B 1 192 ? 26.43300  31.02800  47.35300  1.000 15.08730 ? 192 ASN B ND2 1 
ATOM   4453 N N   . CYS B 1 193 ? 25.39500  26.18700  49.78500  1.000 19.04119 ? 193 CYS B N   1 
ATOM   4454 C CA  . CYS B 1 193 ? 26.47700  25.41600  50.40800  1.000 15.73939 ? 193 CYS B CA  1 
ATOM   4455 C C   . CYS B 1 193 ? 27.40000  24.77900  49.37800  1.000 17.69579 ? 193 CYS B C   1 
ATOM   4456 O O   . CYS B 1 193 ? 28.61100  24.67700  49.60500  1.000 16.67082 ? 193 CYS B O   1 
ATOM   4457 C CB  . CYS B 1 193 ? 25.91200  24.32000  51.30800  1.000 16.06596 ? 193 CYS B CB  1 
ATOM   4458 S SG  . CYS B 1 193 ? 24.97200  24.90500  52.70800  1.000 21.99301 ? 193 CYS B SG  1 
ATOM   4459 N N   . PHE B 1 194 ? 26.84300  24.31100  48.26100  1.000 15.99716 ? 194 PHE B N   1 
ATOM   4460 C CA  . PHE B 1 194 ? 27.62400  23.55300  47.28800  1.000 12.70336 ? 194 PHE B CA  1 
ATOM   4461 C C   . PHE B 1 194 ? 28.76400  24.39500  46.71400  1.000 15.82456 ? 194 PHE B C   1 
ATOM   4462 O O   . PHE B 1 194 ? 29.89500  23.90700  46.56700  1.000 14.80328 ? 194 PHE B O   1 
ATOM   4463 C CB  . PHE B 1 194 ? 26.67700  23.05700  46.18800  1.000 15.83770 ? 194 PHE B CB  1 
ATOM   4464 C CG  . PHE B 1 194 ? 27.25500  22.00700  45.26800  1.000 16.02620 ? 194 PHE B CG  1 
ATOM   4465 C CD1 . PHE B 1 194 ? 28.19300  22.33800  44.30300  1.000 13.68471 ? 194 PHE B CD1 1 
ATOM   4466 C CD2 . PHE B 1 194 ? 26.79200  20.70200  45.31800  1.000 16.24734 ? 194 PHE B CD2 1 
ATOM   4467 C CE1 . PHE B 1 194 ? 28.69500  21.38500  43.43900  1.000 14.59651 ? 194 PHE B CE1 1 
ATOM   4468 C CE2 . PHE B 1 194 ? 27.28800  19.74800  44.46000  1.000 18.78687 ? 194 PHE B CE2 1 
ATOM   4469 C CZ  . PHE B 1 194 ? 28.24600  20.09100  43.51500  1.000 19.73705 ? 194 PHE B CZ  1 
ATOM   4470 N N   . CYS B 1 195 ? 28.49300  25.66300  46.39800  1.000 14.84604 ? 195 CYS B N   1 
ATOM   4471 C CA  . CYS B 1 195 ? 29.46400  26.51600  45.71500  1.000 17.75020 ? 195 CYS B CA  1 
ATOM   4472 C C   . CYS B 1 195 ? 30.16600  27.52300  46.61600  1.000 16.89070 ? 195 CYS B C   1 
ATOM   4473 O O   . CYS B 1 195 ? 31.33800  27.82000  46.36900  1.000 17.84183 ? 195 CYS B O   1 
ATOM   4474 C CB  . CYS B 1 195 ? 28.78900  27.27900  44.57300  1.000 19.05665 ? 195 CYS B CB  1 
ATOM   4475 S SG  . CYS B 1 195 ? 28.48400  26.26500  43.11800  1.000 21.00564 ? 195 CYS B SG  1 
ATOM   4476 N N   . THR B 1 196 ? 29.49000  28.05200  47.65500  1.000 16.22546 ? 196 THR B N   1 
ATOM   4477 C CA  . THR B 1 196 ? 29.96100  29.14300  48.52100  1.000 20.02758 ? 196 THR B CA  1 
ATOM   4478 C C   . THR B 1 196 ? 30.00400  30.45200  47.73600  1.000 18.85974 ? 196 THR B C   1 
ATOM   4479 O O   . THR B 1 196 ? 29.94900  30.42600  46.50100  1.000 20.16955 ? 196 THR B O   1 
ATOM   4480 C CB  . THR B 1 196 ? 31.35000  28.86500  49.11800  1.000 19.66767 ? 196 THR B CB  1 
ATOM   4481 O OG1 . THR B 1 196 ? 32.35800  29.15800  48.14100  1.000 18.19332 ? 196 THR B OG1 1 
ATOM   4482 C CG2 . THR B 1 196 ? 31.48600  27.42400  49.56400  1.000 17.55891 ? 196 THR B CG2 1 
ATOM   4483 N N   . PRO B 1 197 ? 30.11300  31.61300  48.39500  1.000 19.58809 ? 197 PRO B N   1 
ATOM   4484 C CA  . PRO B 1 197 ? 30.21200  32.87400  47.63600  1.000 19.12256 ? 197 PRO B CA  1 
ATOM   4485 C C   . PRO B 1 197 ? 31.47700  33.00300  46.80300  1.000 17.22456 ? 197 PRO B C   1 
ATOM   4486 O O   . PRO B 1 197 ? 31.54400  33.90600  45.96000  1.000 19.96626 ? 197 PRO B O   1 
ATOM   4487 C CB  . PRO B 1 197 ? 30.15500  33.95300  48.72900  1.000 17.18125 ? 197 PRO B CB  1 
ATOM   4488 C CG  . PRO B 1 197 ? 30.56100  33.24800  49.98300  1.000 18.61852 ? 197 PRO B CG  1 
ATOM   4489 C CD  . PRO B 1 197 ? 30.01200  31.86200  49.84500  1.000 17.84726 ? 197 PRO B CD  1 
ATOM   4490 N N   . ALA B 1 198 ? 32.48500  32.15300  47.01300  1.000 17.26634 ? 198 ALA B N   1 
ATOM   4491 C CA  . ALA B 1 198 ? 33.67100  32.20500  46.16800  1.000 16.21385 ? 198 ALA B CA  1 
ATOM   4492 C C   . ALA B 1 198 ? 33.39200  31.74000  44.74600  1.000 21.46914 ? 198 ALA B C   1 
ATOM   4493 O O   . ALA B 1 198 ? 34.14200  32.10300  43.83400  1.000 22.29930 ? 198 ALA B O   1 
ATOM   4494 C CB  . ALA B 1 198 ? 34.79700  31.36600  46.77100  1.000 14.13047 ? 198 ALA B CB  1 
ATOM   4495 N N   . LEU B 1 199 ? 32.33800  30.94800  44.53400  1.000 17.11162 ? 199 LEU B N   1 
ATOM   4496 C CA  . LEU B 1 199 ? 32.01400  30.42900  43.21100  1.000 19.14651 ? 199 LEU B CA  1 
ATOM   4497 C C   . LEU B 1 199 ? 30.68300  30.91700  42.66100  1.000 18.33069 ? 199 LEU B C   1 
ATOM   4498 O O   . LEU B 1 199 ? 30.52000  30.96000  41.44200  1.000 18.96701 ? 199 LEU B O   1 
ATOM   4499 C CB  . LEU B 1 199 ? 31.99400  28.89200  43.22600  1.000 17.32419 ? 199 LEU B CB  1 
ATOM   4500 C CG  . LEU B 1 199 ? 33.25000  28.18600  43.74000  1.000 16.89962 ? 199 LEU B CG  1 
ATOM   4501 C CD1 . LEU B 1 199 ? 33.10500  26.68300  43.59200  1.000 17.09117 ? 199 LEU B CD1 1 
ATOM   4502 C CD2 . LEU B 1 199 ? 34.49400  28.68300  43.01400  1.000 21.46778 ? 199 LEU B CD2 1 
ATOM   4503 N N   . GLN B 1 200 ? 29.73000  31.27600  43.51500  1.000 19.05609 ? 200 GLN B N   1 
ATOM   4504 C CA  . GLN B 1 200 ? 28.38500  31.59500  43.06000  1.000 21.60956 ? 200 GLN B CA  1 
ATOM   4505 C C   . GLN B 1 200 ? 27.78100  32.64800  43.97400  1.000 20.84768 ? 200 GLN B C   1 
ATOM   4506 O O   . GLN B 1 200 ? 27.93500  32.57500  45.19600  1.000 15.27144 ? 200 GLN B O   1 
ATOM   4507 C CB  . GLN B 1 200 ? 27.50400  30.33900  43.04000  1.000 19.54414 ? 200 GLN B CB  1 
ATOM   4508 C CG  . GLN B 1 200 ? 26.07500  30.56300  42.57400  1.000 19.78941 ? 200 GLN B CG  1 
ATOM   4509 C CD  . GLN B 1 200 ? 25.31400  29.25400  42.42000  1.000 21.09848 ? 200 GLN B CD  1 
ATOM   4510 O OE1 . GLN B 1 200 ? 25.08300  28.78500  41.30600  1.000 22.88847 ? 200 GLN B OE1 1 
ATOM   4511 N NE2 . GLN B 1 200 ? 24.93200  28.65500  43.54200  1.000 17.42723 ? 200 GLN B NE2 1 
ATOM   4512 N N   . GLN B 1 201 ? 27.10100  33.62700  43.37800  1.000 17.74615 ? 201 GLN B N   1 
ATOM   4513 C CA  . GLN B 1 201 ? 26.42800  34.68900  44.12600  1.000 20.59037 ? 201 GLN B CA  1 
ATOM   4514 C C   . GLN B 1 201 ? 24.98000  34.75000  43.66400  1.000 20.36922 ? 201 GLN B C   1 
ATOM   4515 O O   . GLN B 1 201 ? 24.64600  35.47200  42.71500  1.000 23.67742 ? 201 GLN B O   1 
ATOM   4516 C CB  . GLN B 1 201 ? 27.13200  36.03200  43.94800  1.000 21.14247 ? 201 GLN B CB  1 
ATOM   4517 C CG  . GLN B 1 201 ? 28.54800  36.05100  44.49700  1.000 26.31965 ? 201 GLN B CG  1 
ATOM   4518 C CD  . GLN B 1 201 ? 29.31000  37.30600  44.11000  1.000 36.26622 ? 201 GLN B CD  1 
ATOM   4519 O OE1 . GLN B 1 201 ? 29.67400  37.49200  42.94700  1.000 40.86122 ? 201 GLN B OE1 1 
ATOM   4520 N NE2 . GLN B 1 201 ? 29.56200  38.17200  45.08900  1.000 32.64732 ? 201 GLN B NE2 1 
ATOM   4521 N N   . PRO B 1 202 ? 24.08700  34.01000  44.32300  1.000 20.40845 ? 202 PRO B N   1 
ATOM   4522 C CA  . PRO B 1 202 ? 22.69300  33.95500  43.85900  1.000 16.89487 ? 202 PRO B CA  1 
ATOM   4523 C C   . PRO B 1 202 ? 21.99000  35.30300  43.84300  1.000 20.19379 ? 202 PRO B C   1 
ATOM   4524 O O   . PRO B 1 202 ? 20.98700  35.44200  43.13300  1.000 20.78506 ? 202 PRO B O   1 
ATOM   4525 C CB  . PRO B 1 202 ? 22.03400  32.99000  44.85400  1.000 17.92248 ? 202 PRO B CB  1 
ATOM   4526 C CG  . PRO B 1 202 ? 23.16500  32.15200  45.36300  1.000 20.24689 ? 202 PRO B CG  1 
ATOM   4527 C CD  . PRO B 1 202 ? 24.33700  33.08400  45.44000  1.000 18.22867 ? 202 PRO B CD  1 
ATOM   4528 N N   . LEU B 1 203 ? 22.47300  36.30100  44.59200  1.000 22.11578 ? 203 LEU B N   1 
ATOM   4529 C CA  . LEU B 1 203 ? 21.84200  37.61700  44.53100  1.000 21.56619 ? 203 LEU B CA  1 
ATOM   4530 C C   . LEU B 1 203 ? 21.93900  38.22100  43.13700  1.000 20.06164 ? 203 LEU B C   1 
ATOM   4531 O O   . LEU B 1 203 ? 21.05100  38.97600  42.73400  1.000 18.91601 ? 203 LEU B O   1 
ATOM   4532 C CB  . LEU B 1 203 ? 22.46100  38.56900  45.55300  1.000 21.90117 ? 203 LEU B CB  1 
ATOM   4533 C CG  . LEU B 1 203 ? 22.21700  38.22200  47.02300  1.000 27.55115 ? 203 LEU B CG  1 
ATOM   4534 C CD1 . LEU B 1 203 ? 22.70000  39.35100  47.91300  1.000 21.43610 ? 203 LEU B CD1 1 
ATOM   4535 C CD2 . LEU B 1 203 ? 20.75200  37.92600  47.27300  1.000 21.96127 ? 203 LEU B CD2 1 
ATOM   4536 N N   . LYS B 1 204 ? 22.99900  37.89900  42.39000  1.000 16.04077 ? 204 LYS B N   1 
ATOM   4537 C CA  . LYS B 1 204 ? 23.15800  38.40600  41.03400  1.000 19.57505 ? 204 LYS B CA  1 
ATOM   4538 C C   . LYS B 1 204 ? 22.18500  37.77900  40.05300  1.000 22.15810 ? 204 LYS B C   1 
ATOM   4539 O O   . LYS B 1 204 ? 22.09300  38.24800  38.91500  1.000 25.68968 ? 204 LYS B O   1 
ATOM   4540 C CB  . LYS B 1 204 ? 24.58500  38.17500  40.54500  1.000 19.46660 ? 204 LYS B CB  1 
ATOM   4541 C CG  . LYS B 1 204 ? 25.61100  39.04200  41.25000  1.000 24.69043 ? 204 LYS B CG  1 
ATOM   4542 C CD  . LYS B 1 204 ? 27.01200  38.71900  40.77400  1.000 30.91983 ? 204 LYS B CD  1 
ATOM   4543 C CE  . LYS B 1 204 ? 28.03800  39.63700  41.41200  1.000 32.79424 ? 204 LYS B CE  1 
ATOM   4544 N NZ  . LYS B 1 204 ? 29.40400  39.07700  41.21800  1.000 35.64033 ? 204 LYS B NZ  1 
ATOM   4545 N N   . PHE B 1 205 ? 21.47700  36.72400  40.45500  1.000 23.34885 ? 205 PHE B N   1 
ATOM   4546 C CA  . PHE B 1 205 ? 20.48300  36.07800  39.60900  1.000 19.88914 ? 205 PHE B CA  1 
ATOM   4547 C C   . PHE B 1 205 ? 19.08800  36.19300  40.20100  1.000 20.09198 ? 205 PHE B C   1 
ATOM   4548 O O   . PHE B 1 205 ? 18.22300  35.36100  39.90600  1.000 21.27440 ? 205 PHE B O   1 
ATOM   4549 C CB  . PHE B 1 205 ? 20.84600  34.61300  39.37100  1.000 16.38119 ? 205 PHE B CB  1 
ATOM   4550 C CG  . PHE B 1 205 ? 22.16000  34.42700  38.68100  1.000 20.10786 ? 205 PHE B CG  1 
ATOM   4551 C CD1 . PHE B 1 205 ? 23.34700  34.51000  39.38800  1.000 20.36685 ? 205 PHE B CD1 1 
ATOM   4552 C CD2 . PHE B 1 205 ? 22.21200  34.17100  37.32400  1.000 21.07891 ? 205 PHE B CD2 1 
ATOM   4553 C CE1 . PHE B 1 205 ? 24.55700  34.34600  38.75600  1.000 22.26449 ? 205 PHE B CE1 1 
ATOM   4554 C CE2 . PHE B 1 205 ? 23.42000  34.00800  36.68500  1.000 23.97437 ? 205 PHE B CE2 1 
ATOM   4555 C CZ  . PHE B 1 205 ? 24.59600  34.09500  37.40200  1.000 24.78203 ? 205 PHE B CZ  1 
ATOM   4556 N N   . GLY B 1 206 ? 18.86100  37.19500  41.05100  1.000 18.96505 ? 206 GLY B N   1 
ATOM   4557 C CA  . GLY B 1 206 ? 17.53400  37.51900  41.53200  1.000 19.01338 ? 206 GLY B CA  1 
ATOM   4558 C C   . GLY B 1 206 ? 17.10700  36.86500  42.83300  1.000 22.53087 ? 206 GLY B C   1 
ATOM   4559 O O   . GLY B 1 206 ? 15.95400  37.05700  43.24600  1.000 20.29841 ? 206 GLY B O   1 
ATOM   4560 N N   . ALA B 1 207 ? 17.97800  36.09800  43.48900  1.000 19.75968 ? 207 ALA B N   1 
ATOM   4561 C CA  . ALA B 1 207 ? 17.63700  35.54600  44.79600  1.000 17.48907 ? 207 ALA B CA  1 
ATOM   4562 C C   . ALA B 1 207 ? 17.36800  36.66600  45.79200  1.000 15.94970 ? 207 ALA B C   1 
ATOM   4563 O O   . ALA B 1 207 ? 17.96100  37.74300  45.72300  1.000 18.88826 ? 207 ALA B O   1 
ATOM   4564 C CB  . ALA B 1 207 ? 18.76300  34.65000  45.31700  1.000 18.14436 ? 207 ALA B CB  1 
ATOM   4565 N N   . ASP B 1 208 ? 16.44200  36.41200  46.71500  1.000 20.43551 ? 208 ASP B N   1 
ATOM   4566 C CA  . ASP B 1 208 ? 16.12000  37.35400  47.78000  1.000 19.52860 ? 208 ASP B CA  1 
ATOM   4567 C C   . ASP B 1 208 ? 16.84500  37.04200  49.08100  1.000 21.12285 ? 208 ASP B C   1 
ATOM   4568 O O   . ASP B 1 208 ? 17.26000  37.96500  49.78600  1.000 20.73953 ? 208 ASP B O   1 
ATOM   4569 C CB  . ASP B 1 208 ? 14.60900  37.37400  48.02400  1.000 20.32699 ? 208 ASP B CB  1 
ATOM   4570 C CG  . ASP B 1 208 ? 13.83500  37.83800  46.80700  1.000 22.90393 ? 208 ASP B CG  1 
ATOM   4571 O OD1 . ASP B 1 208 ? 13.84500  39.05600  46.52600  1.000 24.59582 ? 208 ASP B OD1 1 
ATOM   4572 O OD2 . ASP B 1 208 ? 13.24600  36.98100  46.11300  1.000 20.89568 ? 208 ASP B OD2 1 
ATOM   4573 N N   . LEU B 1 209 ? 17.00800  35.76000  49.40900  1.000 20.94102 ? 209 LEU B N   1 
ATOM   4574 C CA  . LEU B 1 209 ? 17.81200  35.32200  50.54300  1.000 19.91492 ? 209 LEU B CA  1 
ATOM   4575 C C   . LEU B 1 209 ? 18.78600  34.24500  50.08600  1.000 20.78779 ? 209 LEU B C   1 
ATOM   4576 O O   . LEU B 1 209 ? 18.45300  33.40800  49.23900  1.000 17.13772 ? 209 LEU B O   1 
ATOM   4577 C CB  . LEU B 1 209 ? 16.94400  34.77600  51.68100  1.000 18.39716 ? 209 LEU B CB  1 
ATOM   4578 C CG  . LEU B 1 209 ? 16.05500  35.77800  52.40500  1.000 18.55675 ? 209 LEU B CG  1 
ATOM   4579 C CD1 . LEU B 1 209 ? 15.21500  35.05800  53.43800  1.000 19.66033 ? 209 LEU B CD1 1 
ATOM   4580 C CD2 . LEU B 1 209 ? 16.90200  36.84500  53.05700  1.000 20.20954 ? 209 LEU B CD2 1 
ATOM   4581 N N   . VAL B 1 210 ? 19.98900  34.27300  50.64900  1.000 20.49010 ? 210 VAL B N   1 
ATOM   4582 C CA  . VAL B 1 210 ? 20.99300  33.24100  50.42300  1.000 17.56753 ? 210 VAL B CA  1 
ATOM   4583 C C   . VAL B 1 210 ? 21.26500  32.56300  51.75900  1.000 17.97300 ? 210 VAL B C   1 
ATOM   4584 O O   . VAL B 1 210 ? 21.59700  33.23400  52.74500  1.000 16.99459 ? 210 VAL B O   1 
ATOM   4585 C CB  . VAL B 1 210 ? 22.28300  33.81600  49.82500  1.000 16.71331 ? 210 VAL B CB  1 
ATOM   4586 C CG1 . VAL B 1 210 ? 23.26100  32.69100  49.52600  1.000 18.72172 ? 210 VAL B CG1 1 
ATOM   4587 C CG2 . VAL B 1 210 ? 21.97100  34.60100  48.57200  1.000 18.33954 ? 210 VAL B CG2 1 
ATOM   4588 N N   . ILE B 1 211 ? 21.11300  31.24200  51.79400  1.000 17.53901 ? 211 ILE B N   1 
ATOM   4589 C CA  . ILE B 1 211 ? 21.26800  30.45700  53.01400  1.000 16.76208 ? 211 ILE B CA  1 
ATOM   4590 C C   . ILE B 1 211 ? 22.63100  29.79100  52.97600  1.000 17.85337 ? 211 ILE B C   1 
ATOM   4591 O O   . ILE B 1 211 ? 23.06600  29.30800  51.92200  1.000 15.64943 ? 211 ILE B O   1 
ATOM   4592 C CB  . ILE B 1 211 ? 20.14800  29.40800  53.15200  1.000 19.49260 ? 211 ILE B CB  1 
ATOM   4593 C CG1 . ILE B 1 211 ? 18.77900  30.07400  53.09100  1.000 16.74854 ? 211 ILE B CG1 1 
ATOM   4594 C CG2 . ILE B 1 211 ? 20.29800  28.61000  54.45000  1.000 16.38917 ? 211 ILE B CG2 1 
ATOM   4595 C CD1 . ILE B 1 211 ? 18.57200  31.11400  54.14900  1.000 20.91802 ? 211 ILE B CD1 1 
ATOM   4596 N N   . HIS B 1 212 ? 23.31600  29.77000  54.11700  1.000 12.90120 ? 212 HIS B N   1 
ATOM   4597 C CA  . HIS B 1 212 ? 24.62100  29.13900  54.20600  1.000 13.63004 ? 212 HIS B CA  1 
ATOM   4598 C C   . HIS B 1 212 ? 24.68400  28.21100  55.40200  1.000 15.58975 ? 212 HIS B C   1 
ATOM   4599 O O   . HIS B 1 212 ? 24.11200  28.49400  56.45800  1.000 18.51787 ? 212 HIS B O   1 
ATOM   4600 C CB  . HIS B 1 212 ? 25.75100  30.16600  54.31300  1.000 16.07518 ? 212 HIS B CB  1 
ATOM   4601 C CG  . HIS B 1 212 ? 26.19800  30.69900  52.98900  1.000 17.07672 ? 212 HIS B CG  1 
ATOM   4602 N ND1 . HIS B 1 212 ? 26.91300  29.94000  52.08700  1.000 19.54660 ? 212 HIS B ND1 1 
ATOM   4603 C CD2 . HIS B 1 212 ? 26.02000  31.90800  52.40800  1.000 15.93509 ? 212 HIS B CD2 1 
ATOM   4604 C CE1 . HIS B 1 212 ? 27.15000  30.65700  51.00400  1.000 19.95256 ? 212 HIS B CE1 1 
ATOM   4605 N NE2 . HIS B 1 212 ? 26.62700  31.85800  51.17600  1.000 20.42235 ? 212 HIS B NE2 1 
ATOM   4606 N N   . SER B 1 213 ? 25.37300  27.09900  55.21500  1.000 13.63955 ? 213 SER B N   1 
ATOM   4607 C CA  . SER B 1 213 ? 25.86900  26.27900  56.30500  1.000 16.27475 ? 213 SER B CA  1 
ATOM   4608 C C   . SER B 1 213 ? 27.35400  26.58700  56.44400  1.000 15.16560 ? 213 SER B C   1 
ATOM   4609 O O   . SER B 1 213 ? 28.15700  26.19500  55.59400  1.000 15.53471 ? 213 SER B O   1 
ATOM   4610 C CB  . SER B 1 213 ? 25.63000  24.79400  56.03100  1.000 17.57375 ? 213 SER B CB  1 
ATOM   4611 O OG  . SER B 1 213 ? 26.33400  23.98000  56.94900  1.000 17.86407 ? 213 SER B OG  1 
ATOM   4612 N N   . ALA B 1 214 ? 27.71400  27.31400  57.50400  1.000 13.70129 ? 214 ALA B N   1 
ATOM   4613 C CA  . ALA B 1 214 ? 29.12300  27.55200  57.79000  1.000 13.72785 ? 214 ALA B CA  1 
ATOM   4614 C C   . ALA B 1 214 ? 29.83900  26.25200  58.11300  1.000 15.60342 ? 214 ALA B C   1 
ATOM   4615 O O   . ALA B 1 214 ? 31.07200  26.18500  58.03000  1.000 16.03420 ? 214 ALA B O   1 
ATOM   4616 C CB  . ALA B 1 214 ? 29.26600  28.54700  58.94200  1.000 11.70856 ? 214 ALA B CB  1 
ATOM   4617 N N   . THR B 1 215 ? 29.07400  25.21900  58.46300  1.000 15.02812 ? 215 THR B N   1 
ATOM   4618 C CA  . THR B 1 215 ? 29.62500  23.90700  58.76000  1.000 15.51566 ? 215 THR B CA  1 
ATOM   4619 C C   . THR B 1 215 ? 30.42600  23.33900  57.59600  1.000 16.49364 ? 215 THR B C   1 
ATOM   4620 O O   . THR B 1 215 ? 31.37600  22.57700  57.81800  1.000 15.44107 ? 215 THR B O   1 
ATOM   4621 C CB  . THR B 1 215 ? 28.47900  22.96000  59.11800  1.000 16.43298 ? 215 THR B CB  1 
ATOM   4622 O OG1 . THR B 1 215 ? 27.63500  23.57900  60.09500  1.000 13.77722 ? 215 THR B OG1 1 
ATOM   4623 C CG2 . THR B 1 215 ? 29.00300  21.64800  59.64500  1.000 14.60947 ? 215 THR B CG2 1 
ATOM   4624 N N   . LYS B 1 216 ? 30.07600  23.68500  56.35300  1.000 18.32620 ? 216 LYS B N   1 
ATOM   4625 C CA  . LYS B 1 216 ? 30.68000  22.91100  55.28000  1.000 18.14776 ? 216 LYS B CA  1 
ATOM   4626 C C   . LYS B 1 216 ? 31.97300  23.51400  54.74300  1.000 17.61860 ? 216 LYS B C   1 
ATOM   4627 O O   . LYS B 1 216 ? 33.04100  23.18600  55.26300  1.000 26.75233 ? 216 LYS B O   1 
ATOM   4628 C CB  . LYS B 1 216 ? 29.66900  22.76200  54.13900  1.000 21.45150 ? 216 LYS B CB  1 
ATOM   4629 C CG  . LYS B 1 216 ? 28.33700  22.15300  54.56700  1.000 17.40604 ? 216 LYS B CG  1 
ATOM   4630 C CD  . LYS B 1 216 ? 28.55000  20.83300  55.29700  1.000 20.33525 ? 216 LYS B CD  1 
ATOM   4631 C CE  . LYS B 1 216 ? 27.36800  19.87900  55.11600  1.000 23.32888 ? 216 LYS B CE  1 
ATOM   4632 N NZ  . LYS B 1 216 ? 26.04400  20.53000  55.29200  1.000 20.56191 ? 216 LYS B NZ  1 
ATOM   4633 N N   . TYR B 1 217 ? 31.90600  24.51300  53.86300  1.000 18.15034 ? 217 TYR B N   1 
ATOM   4634 C CA  . TYR B 1 217 ? 33.12400  25.00300  53.21300  1.000 15.75551 ? 217 TYR B CA  1 
ATOM   4635 C C   . TYR B 1 217 ? 33.64700  26.28700  53.83800  1.000 15.92583 ? 217 TYR B C   1 
ATOM   4636 O O   . TYR B 1 217 ? 34.84900  26.55800  53.76100  1.000 15.40667 ? 217 TYR B O   1 
ATOM   4637 C CB  . TYR B 1 217 ? 32.90800  25.26600  51.71300  1.000 19.01705 ? 217 TYR B CB  1 
ATOM   4638 C CG  . TYR B 1 217 ? 32.91500  24.07400  50.76500  1.000 15.54518 ? 217 TYR B CG  1 
ATOM   4639 C CD1 . TYR B 1 217 ? 34.08200  23.36400  50.49500  1.000 18.22538 ? 217 TYR B CD1 1 
ATOM   4640 C CD2 . TYR B 1 217 ? 31.75600  23.69200  50.10200  1.000 14.35185 ? 217 TYR B CD2 1 
ATOM   4641 C CE1 . TYR B 1 217 ? 34.08500  22.27700  49.60900  1.000 16.93256 ? 217 TYR B CE1 1 
ATOM   4642 C CE2 . TYR B 1 217 ? 31.74300  22.61200  49.22200  1.000 15.65965 ? 217 TYR B CE2 1 
ATOM   4643 C CZ  . TYR B 1 217 ? 32.90700  21.91000  48.97800  1.000 17.45262 ? 217 TYR B CZ  1 
ATOM   4644 O OH  . TYR B 1 217 ? 32.88400  20.84600  48.10200  1.000 18.55928 ? 217 TYR B OH  1 
ATOM   4645 N N   . LEU B 1 218 ? 32.77000  27.08600  54.44400  1.000 12.03463 ? 218 LEU B N   1 
ATOM   4646 C CA  . LEU B 1 218 ? 33.23100  28.30100  55.10200  1.000 15.38858 ? 218 LEU B CA  1 
ATOM   4647 C C   . LEU B 1 218 ? 34.18800  27.96200  56.24200  1.000 15.62131 ? 218 LEU B C   1 
ATOM   4648 O O   . LEU B 1 218 ? 35.28800  28.52600  56.33100  1.000 15.24539 ? 218 LEU B O   1 
ATOM   4649 C CB  . LEU B 1 218 ? 32.03400  29.11300  55.59200  1.000 10.85624 ? 218 LEU B CB  1 
ATOM   4650 C CG  . LEU B 1 218 ? 30.89600  29.33600  54.58200  1.000 16.80972 ? 218 LEU B CG  1 
ATOM   4651 C CD1 . LEU B 1 218 ? 29.89900  30.37200  55.09800  1.000 9.89580  ? 218 LEU B CD1 1 
ATOM   4652 C CD2 . LEU B 1 218 ? 31.41600  29.72300  53.20300  1.000 12.94544 ? 218 LEU B CD2 1 
ATOM   4653 N N   . ASP B 1 219 ? 33.78700  27.03500  57.12200  1.000 14.73011 ? 219 ASP B N   1 
ATOM   4654 C CA  . ASP B 1 219 ? 34.73700  26.43100  58.05300  1.000 13.39409 ? 219 ASP B CA  1 
ATOM   4655 C C   . ASP B 1 219 ? 35.82400  25.70700  57.28100  1.000 14.83889 ? 219 ASP B C   1 
ATOM   4656 O O   . ASP B 1 219 ? 37.01700  25.96800  57.46700  1.000 15.40260 ? 219 ASP B O   1 
ATOM   4657 C CB  . ASP B 1 219 ? 34.00300  25.46600  58.99900  1.000 14.73103 ? 219 ASP B CB  1 
ATOM   4658 C CG  . ASP B 1 219 ? 34.92600  24.77500  60.02300  1.000 16.64490 ? 219 ASP B CG  1 
ATOM   4659 O OD1 . ASP B 1 219 ? 36.04300  24.31600  59.67400  1.000 12.65565 ? 219 ASP B OD1 1 
ATOM   4660 O OD2 . ASP B 1 219 ? 34.50600  24.66300  61.20000  1.000 16.06781 ? 219 ASP B OD2 1 
ATOM   4661 N N   . GLY B 1 220 ? 35.42000  24.80500  56.38600  1.000 18.76711 ? 220 GLY B N   1 
ATOM   4662 C CA  . GLY B 1 220 ? 36.33100  24.13500  55.49000  1.000 13.16367 ? 220 GLY B CA  1 
ATOM   4663 C C   . GLY B 1 220 ? 37.10000  22.98400  56.08700  1.000 14.50059 ? 220 GLY B C   1 
ATOM   4664 O O   . GLY B 1 220 ? 37.81800  22.29700  55.34800  1.000 16.91776 ? 220 GLY B O   1 
ATOM   4665 N N   . GLN B 1 221 ? 36.99300  22.74100  57.40100  1.000 20.18527 ? 221 GLN B N   1 
ATOM   4666 C CA  . GLN B 1 221 ? 37.82800  21.70900  58.00700  1.000 15.40165 ? 221 GLN B CA  1 
ATOM   4667 C C   . GLN B 1 221 ? 37.09100  20.86700  59.04800  1.000 18.22572 ? 221 GLN B C   1 
ATOM   4668 O O   . GLN B 1 221 ? 37.74100  20.25000  59.90400  1.000 17.11068 ? 221 GLN B O   1 
ATOM   4669 C CB  . GLN B 1 221 ? 39.08400  22.34600  58.60400  1.000 17.24021 ? 221 GLN B CB  1 
ATOM   4670 C CG  . GLN B 1 221 ? 39.99900  22.94600  57.53200  1.000 21.37141 ? 221 GLN B CG  1 
ATOM   4671 C CD  . GLN B 1 221 ? 41.23400  23.61000  58.08600  1.000 19.00886 ? 221 GLN B CD  1 
ATOM   4672 O OE1 . GLN B 1 221 ? 41.25800  24.82000  58.30700  1.000 22.83038 ? 221 GLN B OE1 1 
ATOM   4673 N NE2 . GLN B 1 221 ? 42.27600  22.82400  58.30200  1.000 19.26874 ? 221 GLN B NE2 1 
ATOM   4674 N N   . GLY B 1 222 ? 35.76000  20.81200  58.98900  1.000 16.23615 ? 222 GLY B N   1 
ATOM   4675 C CA  . GLY B 1 222 ? 34.99600  19.85900  59.77800  1.000 16.55091 ? 222 GLY B CA  1 
ATOM   4676 C C   . GLY B 1 222 ? 34.92400  20.13500  61.26500  1.000 20.65654 ? 222 GLY B C   1 
ATOM   4677 O O   . GLY B 1 222 ? 34.61000  19.22400  62.03700  1.000 17.18900 ? 222 GLY B O   1 
ATOM   4678 N N   . ARG B 1 223 ? 35.17100  21.37300  61.69300  1.000 16.09810 ? 223 ARG B N   1 
ATOM   4679 C CA  . ARG B 1 223 ? 35.34300  21.64100  63.11600  1.000 17.84087 ? 223 ARG B CA  1 
ATOM   4680 C C   . ARG B 1 223 ? 34.05500  22.06400  63.81300  1.000 15.49344 ? 223 ARG B C   1 
ATOM   4681 O O   . ARG B 1 223 ? 33.81500  21.66700  64.95300  1.000 15.20762 ? 223 ARG B O   1 
ATOM   4682 C CB  . ARG B 1 223 ? 36.41800  22.71400  63.31500  1.000 14.56830 ? 223 ARG B CB  1 
ATOM   4683 C CG  . ARG B 1 223 ? 37.80800  22.25900  62.87400  1.000 18.01150 ? 223 ARG B CG  1 
ATOM   4684 C CD  . ARG B 1 223 ? 38.75000  23.42900  62.63700  1.000 19.43515 ? 223 ARG B CD  1 
ATOM   4685 N NE  . ARG B 1 223 ? 38.30600  24.26300  61.52900  1.000 17.95512 ? 223 ARG B NE  1 
ATOM   4686 C CZ  . ARG B 1 223 ? 38.90600  25.37900  61.13800  1.000 17.36577 ? 223 ARG B CZ  1 
ATOM   4687 N NH1 . ARG B 1 223 ? 39.99800  25.82400  61.73700  1.000 17.90754 ? 223 ARG B NH1 1 
ATOM   4688 N NH2 . ARG B 1 223 ? 38.39200  26.07300  60.12600  1.000 16.35818 ? 223 ARG B NH2 1 
ATOM   4689 N N   . THR B 1 224 ? 33.21600  22.86600  63.17000  1.000 17.43324 ? 224 THR B N   1 
ATOM   4690 C CA  . THR B 1 224 ? 32.14500  23.54500  63.88100  1.000 16.12432 ? 224 THR B CA  1 
ATOM   4691 C C   . THR B 1 224 ? 30.84600  23.47200  63.09300  1.000 18.35895 ? 224 THR B C   1 
ATOM   4692 O O   . THR B 1 224 ? 30.82200  23.12300  61.90900  1.000 16.25210 ? 224 THR B O   1 
ATOM   4693 C CB  . THR B 1 224 ? 32.49500  25.01200  64.14000  1.000 17.41367 ? 224 THR B CB  1 
ATOM   4694 O OG1 . THR B 1 224 ? 32.75300  25.65700  62.88400  1.000 17.56776 ? 224 THR B OG1 1 
ATOM   4695 C CG2 . THR B 1 224 ? 33.72100  25.12700  65.04400  1.000 10.88668 ? 224 THR B CG2 1 
ATOM   4696 N N   . LEU B 1 225 ? 29.75900  23.80200  63.78600  1.000 17.63842 ? 225 LEU B N   1 
ATOM   4697 C CA  . LEU B 1 225 ? 28.45100  24.02200  63.18800  1.000 15.19114 ? 225 LEU B CA  1 
ATOM   4698 C C   . LEU B 1 225 ? 28.16000  25.51600  63.13600  1.000 15.36948 ? 225 LEU B C   1 
ATOM   4699 O O   . LEU B 1 225 ? 28.49100  26.25900  64.06600  1.000 14.68954 ? 225 LEU B O   1 
ATOM   4700 C CB  . LEU B 1 225 ? 27.34700  23.32100  63.98700  1.000 11.63013 ? 225 LEU B CB  1 
ATOM   4701 C CG  . LEU B 1 225 ? 26.92700  21.89100  63.63700  1.000 19.46171 ? 225 LEU B CG  1 
ATOM   4702 C CD1 . LEU B 1 225 ? 28.11700  21.00600  63.36200  1.000 19.95670 ? 225 LEU B CD1 1 
ATOM   4703 C CD2 . LEU B 1 225 ? 26.08700  21.30600  64.77300  1.000 16.67864 ? 225 LEU B CD2 1 
ATOM   4704 N N   . GLY B 1 226 ? 27.54300  25.95100  62.04500  1.000 16.05962 ? 226 GLY B N   1 
ATOM   4705 C CA  . GLY B 1 226 ? 27.11100  27.33000  61.93800  1.000 13.25256 ? 226 GLY B CA  1 
ATOM   4706 C C   . GLY B 1 226 ? 26.32800  27.53600  60.66500  1.000 13.23045 ? 226 GLY B C   1 
ATOM   4707 O O   . GLY B 1 226 ? 26.45500  26.77000  59.70400  1.000 12.95915 ? 226 GLY B O   1 
ATOM   4708 N N   . GLY B 1 227 ? 25.51800  28.59500  60.66600  1.000 13.88496 ? 227 GLY B N   1 
ATOM   4709 C CA  . GLY B 1 227 ? 24.76700  28.97400  59.48800  1.000 15.06266 ? 227 GLY B CA  1 
ATOM   4710 C C   . GLY B 1 227 ? 24.66600  30.48300  59.36200  1.000 18.61456 ? 227 GLY B C   1 
ATOM   4711 O O   . GLY B 1 227 ? 25.12200  31.23100  60.23200  1.000 13.04574 ? 227 GLY B O   1 
ATOM   4712 N N   . ALA B 1 228 ? 24.05800  30.91700  58.25800  1.000 12.74284 ? 228 ALA B N   1 
ATOM   4713 C CA  . ALA B 1 228 ? 23.87300  32.33900  58.01500  1.000 15.93337 ? 228 ALA B CA  1 
ATOM   4714 C C   . ALA B 1 228 ? 22.80300  32.54900  56.95300  1.000 18.39971 ? 228 ALA B C   1 
ATOM   4715 O O   . ALA B 1 228 ? 22.61200  31.71700  56.06100  1.000 14.67767 ? 228 ALA B O   1 
ATOM   4716 C CB  . ALA B 1 228 ? 25.18100  33.00500  57.58100  1.000 14.89499 ? 228 ALA B CB  1 
ATOM   4717 N N   . VAL B 1 229 ? 22.12100  33.68200  57.06500  1.000 14.89416 ? 229 VAL B N   1 
ATOM   4718 C CA  . VAL B 1 229 ? 21.12500  34.13000  56.10500  1.000 15.82577 ? 229 VAL B CA  1 
ATOM   4719 C C   . VAL B 1 229 ? 21.59800  35.47600  55.57200  1.000 17.77029 ? 229 VAL B C   1 
ATOM   4720 O O   . VAL B 1 229 ? 21.84300  36.40200  56.35200  1.000 23.51770 ? 229 VAL B O   1 
ATOM   4721 C CB  . VAL B 1 229 ? 19.73500  34.24500  56.75100  1.000 16.90206 ? 229 VAL B CB  1 
ATOM   4722 C CG1 . VAL B 1 229 ? 18.73000  34.81300  55.76700  1.000 16.67778 ? 229 VAL B CG1 1 
ATOM   4723 C CG2 . VAL B 1 229 ? 19.27600  32.87600  57.28500  1.000 16.58834 ? 229 VAL B CG2 1 
ATOM   4724 N N   . CYS B 1 230 ? 21.73700  35.58300  54.25600  1.000 15.92281 ? 230 CYS B N   1 
ATOM   4725 C CA  . CYS B 1 230 ? 22.21700  36.79800  53.61300  1.000 19.52371 ? 230 CYS B CA  1 
ATOM   4726 C C   . CYS B 1 230 ? 21.12200  37.39500  52.73900  1.000 21.51885 ? 230 CYS B C   1 
ATOM   4727 O O   . CYS B 1 230 ? 20.38800  36.66400  52.06600  1.000 18.92565 ? 230 CYS B O   1 
ATOM   4728 C CB  . CYS B 1 230 ? 23.46500  36.52300  52.76700  1.000 19.08803 ? 230 CYS B CB  1 
ATOM   4729 S SG  . CYS B 1 230 ? 24.92900  36.09400  53.73200  1.000 28.11197 ? 230 CYS B SG  1 
ATOM   4730 N N   . GLY B 1 231 ? 21.02500  38.72100  52.75200  1.000 21.69817 ? 231 GLY B N   1 
ATOM   4731 C CA  . GLY B 1 231 ? 20.02300  39.40800  51.95900  1.000 21.24715 ? 231 GLY B CA  1 
ATOM   4732 C C   . GLY B 1 231 ? 20.09100  40.90300  52.18600  1.000 21.75771 ? 231 GLY B C   1 
ATOM   4733 O O   . GLY B 1 231 ? 21.02000  41.41700  52.81600  1.000 18.71063 ? 231 GLY B O   1 
ATOM   4734 N N   . SER B 1 232 ? 19.08800  41.59800  51.65800  1.000 18.96226 ? 232 SER B N   1 
ATOM   4735 C CA  . SER B 1 232 ? 18.99900  43.04100  51.83200  1.000 20.88404 ? 232 SER B CA  1 
ATOM   4736 C C   . SER B 1 232 ? 18.78300  43.39100  53.29900  1.000 18.69699 ? 232 SER B C   1 
ATOM   4737 O O   . SER B 1 232 ? 18.21900  42.61000  54.06900  1.000 21.82959 ? 232 SER B O   1 
ATOM   4738 C CB  . SER B 1 232 ? 17.85100  43.60700  50.99900  1.000 20.54736 ? 232 SER B CB  1 
ATOM   4739 O OG  . SER B 1 232 ? 16.60000  43.24900  51.56700  1.000 21.38203 ? 232 SER B OG  1 
ATOM   4740 N N   . THR B 1 233 ? 19.24300  44.58200  53.68600  1.000 18.00540 ? 233 THR B N   1 
ATOM   4741 C CA  . THR B 1 233 ? 18.96400  45.08300  55.03000  1.000 22.69331 ? 233 THR B CA  1 
ATOM   4742 C C   . THR B 1 233 ? 17.46900  45.06900  55.31800  1.000 23.05283 ? 233 THR B C   1 
ATOM   4743 O O   . THR B 1 233 ? 17.03600  44.66100  56.40300  1.000 23.11067 ? 233 THR B O   1 
ATOM   4744 C CB  . THR B 1 233 ? 19.51600  46.50800  55.18900  1.000 22.76605 ? 233 THR B CB  1 
ATOM   4745 O OG1 . THR B 1 233 ? 20.94600  46.47200  55.24200  1.000 23.32650 ? 233 THR B OG1 1 
ATOM   4746 C CG2 . THR B 1 233 ? 18.98100  47.17600  56.46200  1.000 15.52378 ? 233 THR B CG2 1 
ATOM   4747 N N   . GLU B 1 234 ? 16.66700  45.50600  54.34500  1.000 25.32438 ? 234 GLU B N   1 
ATOM   4748 C CA  . GLU B 1 234 ? 15.22800  45.63500  54.53400  1.000 24.71347 ? 234 GLU B CA  1 
ATOM   4749 C C   . GLU B 1 234 ? 14.56000  44.28300  54.75600  1.000 23.59260 ? 234 GLU B C   1 
ATOM   4750 O O   . GLU B 1 234 ? 13.67300  44.15700  55.61200  1.000 22.31943 ? 234 GLU B O   1 
ATOM   4751 C CB  . GLU B 1 234 ? 14.62200  46.34600  53.32600  1.000 25.58837 ? 234 GLU B CB  1 
ATOM   4752 C CG  . GLU B 1 234 ? 13.16000  46.03600  53.07800  1.000 35.37784 ? 234 GLU B CG  1 
ATOM   4753 C CD  . GLU B 1 234 ? 12.50800  47.03000  52.13300  1.000 42.35207 ? 234 GLU B CD  1 
ATOM   4754 O OE1 . GLU B 1 234 ? 12.18000  48.14700  52.58900  1.000 41.05101 ? 234 GLU B OE1 1 
ATOM   4755 O OE2 . GLU B 1 234 ? 12.33200  46.69600  50.93900  1.000 43.17895 ? 234 GLU B OE2 1 
ATOM   4756 N N   . LEU B 1 235 ? 14.95400  43.26400  53.98700  1.000 19.50506 ? 235 LEU B N   1 
ATOM   4757 C CA  . LEU B 1 235 ? 14.30500  41.96100  54.12300  1.000 24.67557 ? 235 LEU B CA  1 
ATOM   4758 C C   . LEU B 1 235 ? 14.71700  41.26800  55.41800  1.000 23.72471 ? 235 LEU B C   1 
ATOM   4759 O O   . LEU B 1 235 ? 13.86300  40.74600  56.14400  1.000 23.63820 ? 235 LEU B O   1 
ATOM   4760 C CB  . LEU B 1 235 ? 14.60900  41.08100  52.90500  1.000 20.72625 ? 235 LEU B CB  1 
ATOM   4761 C CG  . LEU B 1 235 ? 13.75600  39.81300  52.75100  1.000 21.90442 ? 235 LEU B CG  1 
ATOM   4762 C CD1 . LEU B 1 235 ? 12.27700  40.16300  52.62700  1.000 18.37077 ? 235 LEU B CD1 1 
ATOM   4763 C CD2 . LEU B 1 235 ? 14.20100  38.96900  51.56600  1.000 17.63009 ? 235 LEU B CD2 1 
ATOM   4764 N N   . LEU B 1 236 ? 16.01300  41.27800  55.74600  1.000 23.08703 ? 236 LEU B N   1 
ATOM   4765 C CA  . LEU B 1 236 ? 16.44700  40.68900  57.01000  1.000 22.53721 ? 236 LEU B CA  1 
ATOM   4766 C C   . LEU B 1 236 ? 15.81800  41.39200  58.20300  1.000 25.00329 ? 236 LEU B C   1 
ATOM   4767 O O   . LEU B 1 236 ? 15.61500  40.76900  59.25200  1.000 25.29677 ? 236 LEU B O   1 
ATOM   4768 C CB  . LEU B 1 236 ? 17.96800  40.72900  57.13300  1.000 22.64746 ? 236 LEU B CB  1 
ATOM   4769 C CG  . LEU B 1 236 ? 18.75200  39.74000  56.27400  1.000 21.44804 ? 236 LEU B CG  1 
ATOM   4770 C CD1 . LEU B 1 236 ? 20.15000  39.60400  56.82200  1.000 24.02782 ? 236 LEU B CD1 1 
ATOM   4771 C CD2 . LEU B 1 236 ? 18.06500  38.40100  56.25400  1.000 23.86863 ? 236 LEU B CD2 1 
ATOM   4772 N N   . ASN B 1 237 ? 15.50800  42.68100  58.06800  1.000 22.81607 ? 237 ASN B N   1 
ATOM   4773 C CA  . ASN B 1 237 ? 14.86200  43.43400  59.13400  1.000 23.99127 ? 237 ASN B CA  1 
ATOM   4774 C C   . ASN B 1 237 ? 13.36500  43.19800  59.18900  1.000 25.82637 ? 237 ASN B C   1 
ATOM   4775 O O   . ASN B 1 237 ? 12.70600  43.72600  60.09000  1.000 24.51694 ? 237 ASN B O   1 
ATOM   4776 C CB  . ASN B 1 237 ? 15.12800  44.93800  58.97700  1.000 26.25368 ? 237 ASN B CB  1 
ATOM   4777 C CG  . ASN B 1 237 ? 16.53100  45.34100  59.41800  1.000 31.72496 ? 237 ASN B CG  1 
ATOM   4778 O OD1 . ASN B 1 237 ? 17.22200  44.59300  60.11300  1.000 24.27751 ? 237 ASN B OD1 1 
ATOM   4779 N ND2 . ASN B 1 237 ? 16.95000  46.53700  59.01900  1.000 37.60917 ? 237 ASN B ND2 1 
ATOM   4780 N N   . SER B 1 238 ? 12.81300  42.44000  58.24100  1.000 22.67772 ? 238 SER B N   1 
ATOM   4781 C CA  . SER B 1 238 ? 11.39100  42.14200  58.21000  1.000 25.88714 ? 238 SER B CA  1 
ATOM   4782 C C   . SER B 1 238 ? 11.05800  40.81200  58.88500  1.000 25.81933 ? 238 SER B C   1 
ATOM   4783 O O   . SER B 1 238 ? 10.03000  40.20700  58.56800  1.000 28.06679 ? 238 SER B O   1 
ATOM   4784 C CB  . SER B 1 238 ? 10.88100  42.14500  56.76800  1.000 27.91795 ? 238 SER B CB  1 
ATOM   4785 O OG  . SER B 1 238 ? 11.15800  40.90500  56.13300  1.000 31.11731 ? 238 SER B OG  1 
ATOM   4786 N N   . GLY B 1 239 ? 11.89600  40.34800  59.80900  1.000 22.43610 ? 239 GLY B N   1 
ATOM   4787 C CA  . GLY B 1 239 ? 11.58300  39.16500  60.58100  1.000 23.86308 ? 239 GLY B CA  1 
ATOM   4788 C C   . GLY B 1 239 ? 12.70300  38.16400  60.81700  1.000 19.07566 ? 239 GLY B C   1 
ATOM   4789 O O   . GLY B 1 239 ? 12.78800  37.58500  61.90200  1.000 20.43797 ? 239 GLY B O   1 
ATOM   4790 N N   . PRO B 1 240 ? 13.59200  37.94100  59.84000  1.000 18.84380 ? 240 PRO B N   1 
ATOM   4791 C CA  . PRO B 1 240 ? 14.70700  37.00800  60.10200  1.000 18.59443 ? 240 PRO B CA  1 
ATOM   4792 C C   . PRO B 1 240 ? 15.57700  37.41400  61.28000  1.000 24.97242 ? 240 PRO B C   1 
ATOM   4793 O O   . PRO B 1 240 ? 15.84600  36.58400  62.16300  1.000 17.64734 ? 240 PRO B O   1 
ATOM   4794 C CB  . PRO B 1 240 ? 15.47800  37.01800  58.77700  1.000 19.44734 ? 240 PRO B CB  1 
ATOM   4795 C CG  . PRO B 1 240 ? 14.42400  37.26500  57.75900  1.000 20.30347 ? 240 PRO B CG  1 
ATOM   4796 C CD  . PRO B 1 240 ? 13.47300  38.24300  58.40000  1.000 19.66117 ? 240 PRO B CD  1 
ATOM   4797 N N   . ARG B 1 241 ? 16.01300  38.67700  61.33000  1.000 22.44980 ? 241 ARG B N   1 
ATOM   4798 C CA  . ARG B 1 241 ? 16.86700  39.11800  62.42900  1.000 20.77919 ? 241 ARG B CA  1 
ATOM   4799 C C   . ARG B 1 241 ? 16.14000  39.04900  63.76300  1.000 22.36606 ? 241 ARG B C   1 
ATOM   4800 O O   . ARG B 1 241 ? 16.71100  38.60500  64.76600  1.000 20.29591 ? 241 ARG B O   1 
ATOM   4801 C CB  . ARG B 1 241 ? 17.37100  40.53400  62.17100  1.000 24.21360 ? 241 ARG B CB  1 
ATOM   4802 C CG  . ARG B 1 241 ? 18.75300  40.56300  61.56500  1.000 33.06412 ? 241 ARG B CG  1 
ATOM   4803 C CD  . ARG B 1 241 ? 19.09800  41.93200  61.02800  1.000 25.86695 ? 241 ARG B CD  1 
ATOM   4804 N NE  . ARG B 1 241 ? 20.47600  41.98100  60.56200  1.000 26.46850 ? 241 ARG B NE  1 
ATOM   4805 C CZ  . ARG B 1 241 ? 20.94400  42.89800  59.72900  1.000 32.91044 ? 241 ARG B CZ  1 
ATOM   4806 N NH1 . ARG B 1 241 ? 20.15600  43.83500  59.22400  1.000 32.21478 ? 241 ARG B NH1 1 
ATOM   4807 N NH2 . ARG B 1 241 ? 22.23300  42.87500  59.39400  1.000 30.37257 ? 241 ARG B NH2 1 
ATOM   4808 N N   . ASN B 1 242 ? 14.88100  39.48500  63.80000  1.000 24.10126 ? 242 ASN B N   1 
ATOM   4809 C CA  . ASN B 1 242 ? 14.12500  39.39600  65.04200  1.000 25.70857 ? 242 ASN B CA  1 
ATOM   4810 C C   . ASN B 1 242 ? 13.97100  37.94500  65.48000  1.000 21.44143 ? 242 ASN B C   1 
ATOM   4811 O O   . ASN B 1 242 ? 14.06000  37.64000  66.67600  1.000 22.47603 ? 242 ASN B O   1 
ATOM   4812 C CB  . ASN B 1 242 ? 12.76000  40.06200  64.88400  1.000 24.73202 ? 242 ASN B CB  1 
ATOM   4813 C CG  . ASN B 1 242 ? 12.04400  40.23000  66.21000  1.000 32.95354 ? 242 ASN B CG  1 
ATOM   4814 O OD1 . ASN B 1 242 ? 12.34100  41.14900  66.97000  1.000 39.43298 ? 242 ASN B OD1 1 
ATOM   4815 N ND2 . ASN B 1 242 ? 11.10000  39.33700  66.49700  1.000 34.34134 ? 242 ASN B ND2 1 
ATOM   4816 N N   . PHE B 1 243 ? 13.75700  37.03600  64.52500  1.000 19.94647 ? 243 PHE B N   1 
ATOM   4817 C CA  . PHE B 1 243 ? 13.62700  35.62000  64.86300  1.000 23.12062 ? 243 PHE B CA  1 
ATOM   4818 C C   . PHE B 1 243 ? 14.87400  35.10200  65.57100  1.000 19.69557 ? 243 PHE B C   1 
ATOM   4819 O O   . PHE B 1 243 ? 14.78000  34.44600  66.61300  1.000 19.69632 ? 243 PHE B O   1 
ATOM   4820 C CB  . PHE B 1 243 ? 13.35700  34.79200  63.60800  1.000 17.93727 ? 243 PHE B CB  1 
ATOM   4821 C CG  . PHE B 1 243 ? 13.20000  33.32600  63.88700  1.000 19.58669 ? 243 PHE B CG  1 
ATOM   4822 C CD1 . PHE B 1 243 ? 12.01400  32.83300  64.41900  1.000 18.98872 ? 243 PHE B CD1 1 
ATOM   4823 C CD2 . PHE B 1 243 ? 14.24000  32.44100  63.64400  1.000 19.25562 ? 243 PHE B CD2 1 
ATOM   4824 C CE1 . PHE B 1 243 ? 11.86200  31.48500  64.69500  1.000 16.62774 ? 243 PHE B CE1 1 
ATOM   4825 C CE2 . PHE B 1 243 ? 14.09500  31.08400  63.91300  1.000 19.80302 ? 243 PHE B CE2 1 
ATOM   4826 C CZ  . PHE B 1 243 ? 12.90400  30.60600  64.44100  1.000 19.01052 ? 243 PHE B CZ  1 
ATOM   4827 N N   . VAL B 1 244 ? 16.05500  35.38500  65.01100  1.000 21.34796 ? 244 VAL B N   1 
ATOM   4828 C CA  . VAL B 1 244 ? 17.30400  34.95300  65.63400  1.000 20.81929 ? 244 VAL B CA  1 
ATOM   4829 C C   . VAL B 1 244 ? 17.43200  35.54900  67.02800  1.000 23.07834 ? 244 VAL B C   1 
ATOM   4830 O O   . VAL B 1 244 ? 17.83200  34.86500  67.97800  1.000 22.73835 ? 244 VAL B O   1 
ATOM   4831 C CB  . VAL B 1 244 ? 18.50400  35.33100  64.74500  1.000 17.62636 ? 244 VAL B CB  1 
ATOM   4832 C CG1 . VAL B 1 244 ? 19.83300  35.02600  65.45500  1.000 16.98347 ? 244 VAL B CG1 1 
ATOM   4833 C CG2 . VAL B 1 244 ? 18.42900  34.59900  63.41900  1.000 17.97137 ? 244 VAL B CG2 1 
ATOM   4834 N N   . ARG B 1 245 ? 17.07800  36.82800  67.17300  1.000 21.57801 ? 245 ARG B N   1 
ATOM   4835 C CA  . ARG B 1 245 ? 17.16800  37.50300  68.46500  1.000 26.63899 ? 245 ARG B CA  1 
ATOM   4836 C C   . ARG B 1 245 ? 16.19900  36.90800  69.48300  1.000 25.02739 ? 245 ARG B C   1 
ATOM   4837 O O   . ARG B 1 245 ? 16.53300  36.78700  70.66800  1.000 25.33500 ? 245 ARG B O   1 
ATOM   4838 C CB  . ARG B 1 245 ? 16.90600  39.00200  68.28700  1.000 27.77161 ? 245 ARG B CB  1 
ATOM   4839 C CG  . ARG B 1 245 ? 16.67100  39.74300  69.59600  1.000 44.61714 ? 245 ARG B CG  1 
ATOM   4840 C CD  . ARG B 1 245 ? 16.61000  41.26100  69.42200  1.000 49.79846 ? 245 ARG B CD  1 
ATOM   4841 N NE  . ARG B 1 245 ? 15.28000  41.73900  69.06200  1.000 52.94126 ? 245 ARG B NE  1 
ATOM   4842 C CZ  . ARG B 1 245 ? 14.26000  41.83100  69.90700  1.000 57.89268 ? 245 ARG B CZ  1 
ATOM   4843 N NH1 . ARG B 1 245 ? 14.36700  41.43600  71.16600  1.000 61.61279 ? 245 ARG B NH1 1 
ATOM   4844 N NH2 . ARG B 1 245 ? 13.10200  42.32700  69.47700  1.000 47.47658 ? 245 ARG B NH2 1 
ATOM   4845 N N   . THR B 1 246 ? 15.00000  36.52900  69.04500  1.000 20.38416 ? 246 THR B N   1 
ATOM   4846 C CA  . THR B 1 246 ? 13.92200  36.13900  69.94600  1.000 20.55649 ? 246 THR B CA  1 
ATOM   4847 C C   . THR B 1 246 ? 13.82700  34.63100  70.14500  1.000 19.21832 ? 246 THR B C   1 
ATOM   4848 O O   . THR B 1 246 ? 13.68100  34.17300  71.27800  1.000 20.68265 ? 246 THR B O   1 
ATOM   4849 C CB  . THR B 1 246 ? 12.58700  36.68300  69.42400  1.000 22.58643 ? 246 THR B CB  1 
ATOM   4850 O OG1 . THR B 1 246 ? 12.74000  38.06600  69.08700  1.000 23.98946 ? 246 THR B OG1 1 
ATOM   4851 C CG2 . THR B 1 246 ? 11.50300  36.54600  70.47600  1.000 18.69763 ? 246 THR B CG2 1 
ATOM   4852 N N   . ALA B 1 247 ? 13.88600  33.84600  69.06900  1.000 19.98686 ? 247 ALA B N   1 
ATOM   4853 C CA  . ALA B 1 247 ? 13.89200  32.39300  69.20100  1.000 19.44431 ? 247 ALA B CA  1 
ATOM   4854 C C   . ALA B 1 247 ? 15.27100  31.84600  69.54300  1.000 20.27869 ? 247 ALA B C   1 
ATOM   4855 O O   . ALA B 1 247 ? 15.38100  30.67100  69.90600  1.000 17.70671 ? 247 ALA B O   1 
ATOM   4856 C CB  . ALA B 1 247 ? 13.38400  31.73500  67.91400  1.000 16.87659 ? 247 ALA B CB  1 
ATOM   4857 N N   . GLY B 1 248 ? 16.31800  32.65800  69.39600  1.000 20.14446 ? 248 GLY B N   1 
ATOM   4858 C CA  . GLY B 1 248 ? 17.64900  32.35400  69.88200  1.000 19.78505 ? 248 GLY B CA  1 
ATOM   4859 C C   . GLY B 1 248 ? 18.45600  31.20500  69.28800  1.000 17.91061 ? 248 GLY B C   1 
ATOM   4860 O O   . GLY B 1 248 ? 19.22800  30.56700  70.01200  1.000 17.06323 ? 248 GLY B O   1 
ATOM   4861 N N   . PRO B 1 249 ? 18.35400  30.91900  67.96700  1.000 15.75146 ? 249 PRO B N   1 
ATOM   4862 C CA  . PRO B 1 249 ? 19.33100  29.97200  67.39800  1.000 14.56971 ? 249 PRO B CA  1 
ATOM   4863 C C   . PRO B 1 249 ? 20.63900  30.66700  67.03800  1.000 17.48070 ? 249 PRO B C   1 
ATOM   4864 O O   . PRO B 1 249 ? 21.08000  30.67200  65.88700  1.000 18.80707 ? 249 PRO B O   1 
ATOM   4865 C CB  . PRO B 1 249 ? 18.59100  29.43800  66.16700  1.000 13.78096 ? 249 PRO B CB  1 
ATOM   4866 C CG  . PRO B 1 249 ? 17.84000  30.62000  65.69300  1.000 18.23859 ? 249 PRO B CG  1 
ATOM   4867 C CD  . PRO B 1 249 ? 17.39700  31.36400  66.93600  1.000 14.94912 ? 249 PRO B CD  1 
ATOM   4868 N N   . SER B 1 250 ? 21.26600  31.28100  68.03400  1.000 17.97109 ? 250 SER B N   1 
ATOM   4869 C CA  . SER B 1 250 ? 22.38900  32.15500  67.75500  1.000 17.71233 ? 250 SER B CA  1 
ATOM   4870 C C   . SER B 1 250 ? 23.69200  31.36500  67.65200  1.000 17.82245 ? 250 SER B C   1 
ATOM   4871 O O   . SER B 1 250 ? 23.80400  30.21800  68.09200  1.000 19.64848 ? 250 SER B O   1 
ATOM   4872 C CB  . SER B 1 250 ? 22.49600  33.24300  68.82100  1.000 24.00082 ? 250 SER B CB  1 
ATOM   4873 O OG  . SER B 1 250 ? 22.36100  32.69600  70.11200  1.000 25.63917 ? 250 SER B OG  1 
ATOM   4874 N N   . LEU B 1 251 ? 24.68300  32.00300  67.04300  1.000 13.64215 ? 251 LEU B N   1 
ATOM   4875 C CA  . LEU B 1 251 ? 25.96600  31.38300  66.75900  1.000 14.59904 ? 251 LEU B CA  1 
ATOM   4876 C C   . LEU B 1 251 ? 26.93700  31.71000  67.88300  1.000 16.10971 ? 251 LEU B C   1 
ATOM   4877 O O   . LEU B 1 251 ? 27.03600  32.86500  68.30800  1.000 15.93432 ? 251 LEU B O   1 
ATOM   4878 C CB  . LEU B 1 251 ? 26.52000  31.87200  65.42100  1.000 13.32705 ? 251 LEU B CB  1 
ATOM   4879 C CG  . LEU B 1 251 ? 27.86400  31.28600  64.99300  1.000 15.51628 ? 251 LEU B CG  1 
ATOM   4880 C CD1 . LEU B 1 251 ? 27.72900  29.79200  64.78700  1.000 13.82104 ? 251 LEU B CD1 1 
ATOM   4881 C CD2 . LEU B 1 251 ? 28.38000  31.97100  63.73600  1.000 14.63239 ? 251 LEU B CD2 1 
ATOM   4882 N N   . SER B 1 252 ? 27.63200  30.69100  68.36600  1.000 17.33405 ? 252 SER B N   1 
ATOM   4883 C CA  . SER B 1 252 ? 28.63000  30.89500  69.39800  1.000 15.00634 ? 252 SER B CA  1 
ATOM   4884 C C   . SER B 1 252 ? 29.79800  31.71200  68.85000  1.000 15.38195 ? 252 SER B C   1 
ATOM   4885 O O   . SER B 1 252 ? 30.22500  31.49800  67.71000  1.000 13.48265 ? 252 SER B O   1 
ATOM   4886 C CB  . SER B 1 252 ? 29.14400  29.55500  69.91200  1.000 13.87154 ? 252 SER B CB  1 
ATOM   4887 O OG  . SER B 1 252 ? 30.22800  29.75700  70.79900  1.000 17.57807 ? 252 SER B OG  1 
ATOM   4888 N N   . PRO B 1 253 ? 30.33600  32.65000  69.63700  1.000 14.83615 ? 253 PRO B N   1 
ATOM   4889 C CA  . PRO B 1 253 ? 31.52300  33.39200  69.18100  1.000 14.08753 ? 253 PRO B CA  1 
ATOM   4890 C C   . PRO B 1 253 ? 32.73300  32.51000  68.92100  1.000 13.21465 ? 253 PRO B C   1 
ATOM   4891 O O   . PRO B 1 253 ? 33.53700  32.83500  68.03500  1.000 13.80663 ? 253 PRO B O   1 
ATOM   4892 C CB  . PRO B 1 253 ? 31.77800  34.39400  70.31900  1.000 15.04083 ? 253 PRO B CB  1 
ATOM   4893 C CG  . PRO B 1 253 ? 31.01300  33.88200  71.48300  1.000 16.15946 ? 253 PRO B CG  1 
ATOM   4894 C CD  . PRO B 1 253 ? 29.83700  33.13700  70.93000  1.000 15.71220 ? 253 PRO B CD  1 
ATOM   4895 N N   . PHE B 1 254 ? 32.89800  31.40900  69.66000  1.000 13.83733 ? 254 PHE B N   1 
ATOM   4896 C CA  . PHE B 1 254 ? 33.96500  30.46800  69.33400  1.000 15.79247 ? 254 PHE B CA  1 
ATOM   4897 C C   . PHE B 1 254 ? 33.80100  29.94700  67.91300  1.000 15.14496 ? 254 PHE B C   1 
ATOM   4898 O O   . PHE B 1 254 ? 34.75300  29.94900  67.12300  1.000 16.09602 ? 254 PHE B O   1 
ATOM   4899 C CB  . PHE B 1 254 ? 33.98200  29.30400  70.32600  1.000 18.07203 ? 254 PHE B CB  1 
ATOM   4900 C CG  . PHE B 1 254 ? 34.31000  29.70700  71.73300  1.000 26.38109 ? 254 PHE B CG  1 
ATOM   4901 C CD1 . PHE B 1 254 ? 35.61700  29.97700  72.10000  1.000 30.12801 ? 254 PHE B CD1 1 
ATOM   4902 C CD2 . PHE B 1 254 ? 33.31300  29.80200  72.69400  1.000 26.27671 ? 254 PHE B CD2 1 
ATOM   4903 C CE1 . PHE B 1 254 ? 35.92600  30.35100  73.39700  1.000 30.06976 ? 254 PHE B CE1 1 
ATOM   4904 C CE2 . PHE B 1 254 ? 33.61600  30.16900  73.99600  1.000 25.04859 ? 254 PHE B CE2 1 
ATOM   4905 C CZ  . PHE B 1 254 ? 34.92400  30.44600  74.34600  1.000 24.69018 ? 254 PHE B CZ  1 
ATOM   4906 N N   . ASN B 1 255 ? 32.58700  29.50800  67.56800  1.000 12.86746 ? 255 ASN B N   1 
ATOM   4907 C CA  . ASN B 1 255 ? 32.32000  29.02200  66.21800  1.000 12.59357 ? 255 ASN B CA  1 
ATOM   4908 C C   . ASN B 1 255 ? 32.47100  30.13600  65.19100  1.000 14.15166 ? 255 ASN B C   1 
ATOM   4909 O O   . ASN B 1 255 ? 33.06700  29.93200  64.12500  1.000 12.48649 ? 255 ASN B O   1 
ATOM   4910 C CB  . ASN B 1 255 ? 30.91800  28.41500  66.15300  1.000 13.10345 ? 255 ASN B CB  1 
ATOM   4911 C CG  . ASN B 1 255 ? 30.78800  27.15200  66.99400  1.000 14.59962 ? 255 ASN B CG  1 
ATOM   4912 O OD1 . ASN B 1 255 ? 31.47600  26.99100  67.99900  1.000 14.27804 ? 255 ASN B OD1 1 
ATOM   4913 N ND2 . ASN B 1 255 ? 29.90500  26.24700  66.57800  1.000 15.44561 ? 255 ASN B ND2 1 
ATOM   4914 N N   . ALA B 1 256 ? 31.94600  31.32600  65.49900  1.000 12.09741 ? 256 ALA B N   1 
ATOM   4915 C CA  . ALA B 1 256 ? 32.06300  32.44600  64.57100  1.000 12.55187 ? 256 ALA B CA  1 
ATOM   4916 C C   . ALA B 1 256 ? 33.52200  32.77600  64.29800  1.000 13.79507 ? 256 ALA B C   1 
ATOM   4917 O O   . ALA B 1 256 ? 33.89300  33.09100  63.16200  1.000 12.14108 ? 256 ALA B O   1 
ATOM   4918 C CB  . ALA B 1 256 ? 31.33000  33.66900  65.12300  1.000 13.43884 ? 256 ALA B CB  1 
ATOM   4919 N N   . TRP B 1 257 ? 34.36600  32.69800  65.33400  1.000 12.52587 ? 257 TRP B N   1 
ATOM   4920 C CA  . TRP B 1 257 ? 35.79300  32.96800  65.17500  1.000 12.49982 ? 257 TRP B CA  1 
ATOM   4921 C C   . TRP B 1 257 ? 36.45600  31.94500  64.25900  1.000 14.49980 ? 257 TRP B C   1 
ATOM   4922 O O   . TRP B 1 257 ? 37.23900  32.30700  63.37200  1.000 16.09733 ? 257 TRP B O   1 
ATOM   4923 C CB  . TRP B 1 257 ? 36.45600  32.98400  66.55600  1.000 15.65482 ? 257 TRP B CB  1 
ATOM   4924 C CG  . TRP B 1 257 ? 37.95200  33.03200  66.55900  1.000 16.49046 ? 257 TRP B CG  1 
ATOM   4925 C CD1 . TRP B 1 257 ? 38.74000  34.12500  66.33200  1.000 18.40207 ? 257 TRP B CD1 1 
ATOM   4926 C CD2 . TRP B 1 257 ? 38.84300  31.94500  66.83500  1.000 14.99553 ? 257 TRP B CD2 1 
ATOM   4927 N NE1 . TRP B 1 257 ? 40.06600  33.78200  66.44500  1.000 15.94353 ? 257 TRP B NE1 1 
ATOM   4928 C CE2 . TRP B 1 257 ? 40.15500  32.44900  66.75400  1.000 15.40308 ? 257 TRP B CE2 1 
ATOM   4929 C CE3 . TRP B 1 257 ? 38.65600  30.59400  67.14600  1.000 14.85130 ? 257 TRP B CE3 1 
ATOM   4930 C CZ2 . TRP B 1 257 ? 41.27500  31.64900  66.96700  1.000 17.14495 ? 257 TRP B CZ2 1 
ATOM   4931 C CZ3 . TRP B 1 257 ? 39.77000  29.80100  67.35600  1.000 17.09338 ? 257 TRP B CZ3 1 
ATOM   4932 C CH2 . TRP B 1 257 ? 41.06300  30.33100  67.26300  1.000 20.06325 ? 257 TRP B CH2 1 
ATOM   4933 N N   . VAL B 1 258 ? 36.14600  30.66200  64.44900  1.000 16.35097 ? 258 VAL B N   1 
ATOM   4934 C CA  . VAL B 1 258 ? 36.65700  29.63300  63.54800  1.000 12.78276 ? 258 VAL B CA  1 
ATOM   4935 C C   . VAL B 1 258 ? 36.21100  29.91500  62.12100  1.000 13.01003 ? 258 VAL B C   1 
ATOM   4936 O O   . VAL B 1 258 ? 37.00000  29.82400  61.17300  1.000 13.73909 ? 258 VAL B O   1 
ATOM   4937 C CB  . VAL B 1 258 ? 36.18500  28.24200  64.01300  1.000 15.26001 ? 258 VAL B CB  1 
ATOM   4938 C CG1 . VAL B 1 258 ? 36.56600  27.18200  62.99200  1.000 12.62889 ? 258 VAL B CG1 1 
ATOM   4939 C CG2 . VAL B 1 258 ? 36.74500  27.91300  65.39600  1.000 12.97553 ? 258 VAL B CG2 1 
ATOM   4940 N N   . GLN B 1 259 ? 34.94100  30.27100  61.94900  1.000 12.78901 ? 259 GLN B N   1 
ATOM   4941 C CA  . GLN B 1 259 ? 34.36900  30.39800  60.61500  1.000 13.59184 ? 259 GLN B CA  1 
ATOM   4942 C C   . GLN B 1 259 ? 34.84000  31.66700  59.90900  1.000 12.59862 ? 259 GLN B C   1 
ATOM   4943 O O   . GLN B 1 259 ? 35.12600  31.63900  58.70800  1.000 13.39026 ? 259 GLN B O   1 
ATOM   4944 C CB  . GLN B 1 259 ? 32.84000  30.33000  60.71400  1.000 11.98949 ? 259 GLN B CB  1 
ATOM   4945 C CG  . GLN B 1 259 ? 32.36900  28.93300  61.16300  1.000 12.25870 ? 259 GLN B CG  1 
ATOM   4946 C CD  . GLN B 1 259 ? 31.03100  28.92700  61.88500  1.000 15.05704 ? 259 GLN B CD  1 
ATOM   4947 O OE1 . GLN B 1 259 ? 30.29800  29.91800  61.88700  1.000 13.75484 ? 259 GLN B OE1 1 
ATOM   4948 N NE2 . GLN B 1 259 ? 30.70600  27.79600  62.50100  1.000 11.79436 ? 259 GLN B NE2 1 
ATOM   4949 N N   . LEU B 1 260 ? 34.95300  32.78200  60.62900  1.000 13.34670 ? 260 LEU B N   1 
ATOM   4950 C CA  . LEU B 1 260 ? 35.45400  33.99300  59.99100  1.000 15.35661 ? 260 LEU B CA  1 
ATOM   4951 C C   . LEU B 1 260 ? 36.90500  33.81800  59.55600  1.000 14.91048 ? 260 LEU B C   1 
ATOM   4952 O O   . LEU B 1 260 ? 37.31400  34.33600  58.51300  1.000 17.10834 ? 260 LEU B O   1 
ATOM   4953 C CB  . LEU B 1 260 ? 35.28600  35.19900  60.92300  1.000 13.05492 ? 260 LEU B CB  1 
ATOM   4954 C CG  . LEU B 1 260 ? 36.14000  35.40300  62.17500  1.000 16.96767 ? 260 LEU B CG  1 
ATOM   4955 C CD1 . LEU B 1 260 ? 37.46700  36.09500  61.84800  1.000 16.24514 ? 260 LEU B CD1 1 
ATOM   4956 C CD2 . LEU B 1 260 ? 35.35100  36.21200  63.20100  1.000 13.18437 ? 260 LEU B CD2 1 
ATOM   4957 N N   . LYS B 1 261 ? 37.69800  33.08300  60.33900  1.000 16.18481 ? 261 LYS B N   1 
ATOM   4958 C CA  . LYS B 1 261 ? 39.05600  32.76600  59.91000  1.000 16.83651 ? 261 LYS B CA  1 
ATOM   4959 C C   . LYS B 1 261 ? 39.05400  31.81300  58.72400  1.000 13.64922 ? 261 LYS B C   1 
ATOM   4960 O O   . LYS B 1 261 ? 39.91400  31.91200  57.84300  1.000 12.29720 ? 261 LYS B O   1 
ATOM   4961 C CB  . LYS B 1 261 ? 39.85800  32.17500  61.06900  1.000 14.69848 ? 261 LYS B CB  1 
ATOM   4962 C CG  . LYS B 1 261 ? 40.38400  33.22000  62.04100  1.000 21.26432 ? 261 LYS B CG  1 
ATOM   4963 C CD  . LYS B 1 261 ? 41.33900  34.18400  61.34300  1.000 20.45157 ? 261 LYS B CD  1 
ATOM   4964 C CE  . LYS B 1 261 ? 42.05500  35.05400  62.34800  1.000 21.10143 ? 261 LYS B CE  1 
ATOM   4965 N NZ  . LYS B 1 261 ? 42.97800  36.03800  61.71400  1.000 19.45454 ? 261 LYS B NZ  1 
ATOM   4966 N N   . GLY B 1 262 ? 38.10900  30.87000  58.69000  1.000 16.55557 ? 262 GLY B N   1 
ATOM   4967 C CA  . GLY B 1 262 ? 38.00300  29.99200  57.53500  1.000 16.46678 ? 262 GLY B CA  1 
ATOM   4968 C C   . GLY B 1 262 ? 37.70600  30.75100  56.25300  1.000 13.28615 ? 262 GLY B C   1 
ATOM   4969 O O   . GLY B 1 262 ? 38.21400  30.40600  55.18500  1.000 15.04999 ? 262 GLY B O   1 
ATOM   4970 N N   . LEU B 1 263 ? 36.88900  31.80400  56.34800  1.000 14.65769 ? 263 LEU B N   1 
ATOM   4971 C CA  . LEU B 1 263 ? 36.57800  32.61700  55.17700  1.000 15.24120 ? 263 LEU B CA  1 
ATOM   4972 C C   . LEU B 1 263 ? 37.83300  33.18800  54.53100  1.000 17.38126 ? 263 LEU B C   1 
ATOM   4973 O O   . LEU B 1 263 ? 37.86100  33.38200  53.31200  1.000 18.24817 ? 263 LEU B O   1 
ATOM   4974 C CB  . LEU B 1 263 ? 35.62700  33.75400  55.56100  1.000 13.00789 ? 263 LEU B CB  1 
ATOM   4975 C CG  . LEU B 1 263 ? 34.21800  33.34900  55.99000  1.000 16.32887 ? 263 LEU B CG  1 
ATOM   4976 C CD1 . LEU B 1 263 ? 33.35500  34.58200  56.25200  1.000 12.71686 ? 263 LEU B CD1 1 
ATOM   4977 C CD2 . LEU B 1 263 ? 33.57700  32.44600  54.93700  1.000 11.53288 ? 263 LEU B CD2 1 
ATOM   4978 N N   . GLU B 1 264 ? 38.88400  33.44700  55.32100  1.000 15.71543 ? 264 GLU B N   1 
ATOM   4979 C CA  . GLU B 1 264 ? 40.07100  34.10700  54.78800  1.000 18.91038 ? 264 GLU B CA  1 
ATOM   4980 C C   . GLU B 1 264 ? 40.75900  33.28700  53.70300  1.000 20.02412 ? 264 GLU B C   1 
ATOM   4981 O O   . GLU B 1 264 ? 41.46400  33.85800  52.86700  1.000 18.54958 ? 264 GLU B O   1 
ATOM   4982 C CB  . GLU B 1 264 ? 41.06400  34.41100  55.91200  1.000 16.74186 ? 264 GLU B CB  1 
ATOM   4983 C CG  . GLU B 1 264 ? 40.53100  35.39100  56.94200  1.000 19.69616 ? 264 GLU B CG  1 
ATOM   4984 C CD  . GLU B 1 264 ? 41.55000  35.76000  58.00300  1.000 19.84822 ? 264 GLU B CD  1 
ATOM   4985 O OE1 . GLU B 1 264 ? 42.72600  35.35300  57.87600  1.000 20.27496 ? 264 GLU B OE1 1 
ATOM   4986 O OE2 . GLU B 1 264 ? 41.16700  36.46000  58.96800  1.000 19.77819 ? 264 GLU B OE2 1 
ATOM   4987 N N   . THR B 1 265 ? 40.57600  31.96800  53.70000  1.000 17.18317 ? 265 THR B N   1 
ATOM   4988 C CA  . THR B 1 265 ? 41.20400  31.09700  52.71400  1.000 20.19346 ? 265 THR B CA  1 
ATOM   4989 C C   . THR B 1 265 ? 40.18600  30.42300  51.80200  1.000 19.83321 ? 265 THR B C   1 
ATOM   4990 O O   . THR B 1 265 ? 40.54000  29.47800  51.09000  1.000 17.61270 ? 265 THR B O   1 
ATOM   4991 C CB  . THR B 1 265 ? 42.04800  30.03300  53.41500  1.000 16.44991 ? 265 THR B CB  1 
ATOM   4992 O OG1 . THR B 1 265 ? 41.19400  29.23700  54.24900  1.000 21.56596 ? 265 THR B OG1 1 
ATOM   4993 C CG2 . THR B 1 265 ? 43.12400  30.68500  54.27300  1.000 16.56724 ? 265 THR B CG2 1 
ATOM   4994 N N   . LEU B 1 266 ? 38.93500  30.89000  51.80200  1.000 16.11853 ? 266 LEU B N   1 
ATOM   4995 C CA  . LEU B 1 266 ? 37.87500  30.18800  51.08700  1.000 17.31916 ? 266 LEU B CA  1 
ATOM   4996 C C   . LEU B 1 266 ? 38.17400  30.08800  49.59600  1.000 18.97770 ? 266 LEU B C   1 
ATOM   4997 O O   . LEU B 1 266 ? 38.02600  29.01200  48.99900  1.000 18.55558 ? 266 LEU B O   1 
ATOM   4998 C CB  . LEU B 1 266 ? 36.53600  30.88800  51.32700  1.000 15.06695 ? 266 LEU B CB  1 
ATOM   4999 C CG  . LEU B 1 266 ? 35.34500  30.36000  50.52100  1.000 21.48441 ? 266 LEU B CG  1 
ATOM   5000 C CD1 . LEU B 1 266 ? 35.04000  28.92200  50.89800  1.000 17.02075 ? 266 LEU B CD1 1 
ATOM   5001 C CD2 . LEU B 1 266 ? 34.12000  31.23600  50.71500  1.000 15.64396 ? 266 LEU B CD2 1 
ATOM   5002 N N   . GLY B 1 267 ? 38.62100  31.19000  48.98500  1.000 17.25139 ? 267 GLY B N   1 
ATOM   5003 C CA  . GLY B 1 267 ? 38.88100  31.18600  47.55100  1.000 13.89878 ? 267 GLY B CA  1 
ATOM   5004 C C   . GLY B 1 267 ? 40.01000  30.25100  47.15600  1.000 22.75209 ? 267 GLY B C   1 
ATOM   5005 O O   . GLY B 1 267 ? 39.89400  29.49000  46.19100  1.000 22.68359 ? 267 GLY B O   1 
ATOM   5006 N N   . LEU B 1 268 ? 41.12200  30.29600  47.89600  1.000 17.57388 ? 268 LEU B N   1 
ATOM   5007 C CA  . LEU B 1 268 ? 42.23200  29.39200  47.61000  1.000 18.10057 ? 268 LEU B CA  1 
ATOM   5008 C C   . LEU B 1 268 ? 41.81700  27.94200  47.79200  1.000 20.83409 ? 268 LEU B C   1 
ATOM   5009 O O   . LEU B 1 268 ? 42.22400  27.07000  47.01700  1.000 17.87826 ? 268 LEU B O   1 
ATOM   5010 C CB  . LEU B 1 268 ? 43.41900  29.68700  48.52300  1.000 21.93405 ? 268 LEU B CB  1 
ATOM   5011 C CG  . LEU B 1 268 ? 43.86700  31.12300  48.72300  1.000 27.71674 ? 268 LEU B CG  1 
ATOM   5012 C CD1 . LEU B 1 268 ? 45.01200  31.14100  49.72700  1.000 22.31510 ? 268 LEU B CD1 1 
ATOM   5013 C CD2 . LEU B 1 268 ? 44.27200  31.72400  47.38000  1.000 32.61343 ? 268 LEU B CD2 1 
ATOM   5014 N N   . ARG B 1 269 ? 41.04100  27.66100  48.84400  1.000 19.34324 ? 269 ARG B N   1 
ATOM   5015 C CA  . ARG B 1 269 ? 40.62800  26.29000  49.11700  1.000 21.78346 ? 269 ARG B CA  1 
ATOM   5016 C C   . ARG B 1 269 ? 39.68600  25.77100  48.03900  1.000 19.97563 ? 269 ARG B C   1 
ATOM   5017 O O   . ARG B 1 269 ? 39.83900  24.63400  47.57800  1.000 21.36731 ? 269 ARG B O   1 
ATOM   5018 C CB  . ARG B 1 269 ? 39.98000  26.19700  50.50000  1.000 16.83977 ? 269 ARG B CB  1 
ATOM   5019 C CG  . ARG B 1 269 ? 40.97600  26.28900  51.64700  1.000 13.37043 ? 269 ARG B CG  1 
ATOM   5020 C CD  . ARG B 1 269 ? 40.32000  26.03800  53.00600  1.000 16.97491 ? 269 ARG B CD  1 
ATOM   5021 N NE  . ARG B 1 269 ? 39.44700  27.12500  53.43500  1.000 15.00156 ? 269 ARG B NE  1 
ATOM   5022 C CZ  . ARG B 1 269 ? 38.12100  27.09000  53.40300  1.000 18.42016 ? 269 ARG B CZ  1 
ATOM   5023 N NH1 . ARG B 1 269 ? 37.46400  26.03300  52.94400  1.000 15.33088 ? 269 ARG B NH1 1 
ATOM   5024 N NH2 . ARG B 1 269 ? 37.43300  28.13600  53.85800  1.000 16.34582 ? 269 ARG B NH2 1 
ATOM   5025 N N   . MET B 1 270 ? 38.71000  26.58500  47.61900  1.000 19.62201 ? 270 MET B N   1 
ATOM   5026 C CA  . MET B 1 270 ? 37.79400  26.13900  46.57200  1.000 21.70797 ? 270 MET B CA  1 
ATOM   5027 C C   . MET B 1 270 ? 38.52400  25.89400  45.25800  1.000 23.23279 ? 270 MET B C   1 
ATOM   5028 O O   . MET B 1 270 ? 38.14100  24.99800  44.49400  1.000 19.96567 ? 270 MET B O   1 
ATOM   5029 C CB  . MET B 1 270 ? 36.66800  27.15400  46.36000  1.000 15.31787 ? 270 MET B CB  1 
ATOM   5030 C CG  . MET B 1 270 ? 35.74200  27.33800  47.55500  1.000 20.17953 ? 270 MET B CG  1 
ATOM   5031 S SD  . MET B 1 270 ? 35.12000  25.80100  48.27200  1.000 19.21856 ? 270 MET B SD  1 
ATOM   5032 C CE  . MET B 1 270 ? 34.09500  25.17200  46.93900  1.000 15.69952 ? 270 MET B CE  1 
ATOM   5033 N N   . GLU B 1 271 ? 39.57100  26.67300  44.97100  1.000 20.28624 ? 271 GLU B N   1 
ATOM   5034 C CA  . GLU B 1 271 ? 40.30000  26.47100  43.72200  1.000 26.27199 ? 271 GLU B CA  1 
ATOM   5035 C C   . GLU B 1 271 ? 40.98800  25.11200  43.69700  1.000 21.08610 ? 271 GLU B C   1 
ATOM   5036 O O   . GLU B 1 271 ? 40.95000  24.41200  42.67900  1.000 22.36556 ? 271 GLU B O   1 
ATOM   5037 C CB  . GLU B 1 271 ? 41.30900  27.59900  43.50100  1.000 22.94702 ? 271 GLU B CB  1 
ATOM   5038 C CG  . GLU B 1 271 ? 40.71300  28.79000  42.75900  1.000 38.16426 ? 271 GLU B CG  1 
ATOM   5039 C CD  . GLU B 1 271 ? 41.45600  30.08800  43.01800  1.000 41.82895 ? 271 GLU B CD  1 
ATOM   5040 O OE1 . GLU B 1 271 ? 42.69400  30.04800  43.18900  1.000 45.41987 ? 271 GLU B OE1 1 
ATOM   5041 O OE2 . GLU B 1 271 ? 40.79600  31.14900  43.05700  1.000 37.77789 ? 271 GLU B OE2 1 
ATOM   5042 N N   . ARG B 1 272 ? 41.62200  24.71800  44.80300  1.000 20.85744 ? 272 ARG B N   1 
ATOM   5043 C CA  . ARG B 1 272 ? 42.22700  23.39100  44.85000  1.000 19.96048 ? 272 ARG B CA  1 
ATOM   5044 C C   . ARG B 1 272 ? 41.15900  22.30600  44.93600  1.000 21.77078 ? 272 ARG B C   1 
ATOM   5045 O O   . ARG B 1 272 ? 41.29100  21.25300  44.29900  1.000 21.07997 ? 272 ARG B O   1 
ATOM   5046 C CB  . ARG B 1 272 ? 43.20400  23.29700  46.01900  1.000 22.26650 ? 272 ARG B CB  1 
ATOM   5047 C CG  . ARG B 1 272 ? 43.84900  21.93200  46.16800  1.000 20.72421 ? 272 ARG B CG  1 
ATOM   5048 C CD  . ARG B 1 272 ? 44.66200  21.56500  44.94300  1.000 29.17457 ? 272 ARG B CD  1 
ATOM   5049 N NE  . ARG B 1 272 ? 45.66200  22.57800  44.63300  1.000 30.20072 ? 272 ARG B NE  1 
ATOM   5050 C CZ  . ARG B 1 272 ? 46.83400  22.69000  45.24300  1.000 35.73223 ? 272 ARG B CZ  1 
ATOM   5051 N NH1 . ARG B 1 272 ? 47.18800  21.86800  46.21800  1.000 37.02073 ? 272 ARG B NH1 1 
ATOM   5052 N NH2 . ARG B 1 272 ? 47.67100  23.65500  44.86800  1.000 33.86665 ? 272 ARG B NH2 1 
ATOM   5053 N N   . HIS B 1 273 ? 40.08900  22.55500  45.70300  1.000 17.32255 ? 273 HIS B N   1 
ATOM   5054 C CA  . HIS B 1 273 ? 38.95100  21.63900  45.74100  1.000 19.75375 ? 273 HIS B CA  1 
ATOM   5055 C C   . HIS B 1 273 ? 38.44500  21.34500  44.33700  1.000 21.41375 ? 273 HIS B C   1 
ATOM   5056 O O   . HIS B 1 273 ? 38.31600  20.18200  43.93900  1.000 20.39402 ? 273 HIS B O   1 
ATOM   5057 C CB  . HIS B 1 273 ? 37.80600  22.23900  46.56600  1.000 15.87923 ? 273 HIS B CB  1 
ATOM   5058 C CG  . HIS B 1 273 ? 37.89600  21.98600  48.03800  1.000 21.58300 ? 273 HIS B CG  1 
ATOM   5059 N ND1 . HIS B 1 273 ? 37.90600  20.71800  48.57600  1.000 17.33816 ? 273 HIS B ND1 1 
ATOM   5060 C CD2 . HIS B 1 273 ? 37.93100  22.84300  49.08900  1.000 16.72037 ? 273 HIS B CD2 1 
ATOM   5061 C CE1 . HIS B 1 273 ? 37.96700  20.80400  49.89500  1.000 19.20606 ? 273 HIS B CE1 1 
ATOM   5062 N NE2 . HIS B 1 273 ? 37.98600  22.08200  50.23100  1.000 15.98963 ? 273 HIS B NE2 1 
ATOM   5063 N N   . CYS B 1 274 ? 38.16200  22.39900  43.56600  1.000 19.19053 ? 274 CYS B N   1 
ATOM   5064 C CA  . CYS B 1 274 ? 37.55900  22.21000  42.25000  1.000 21.99566 ? 274 CYS B CA  1 
ATOM   5065 C C   . CYS B 1 274 ? 38.55200  21.60800  41.26800  1.000 19.70055 ? 274 CYS B C   1 
ATOM   5066 O O   . CYS B 1 274 ? 38.17600  20.78700  40.42500  1.000 19.31500 ? 274 CYS B O   1 
ATOM   5067 C CB  . CYS B 1 274 ? 37.01400  23.53600  41.72400  1.000 15.76302 ? 274 CYS B CB  1 
ATOM   5068 S SG  . CYS B 1 274 ? 35.61900  24.19400  42.67600  1.000 19.93834 ? 274 CYS B SG  1 
ATOM   5069 N N   . ALA B 1 275 ? 39.82300  22.00400  41.35900  1.000 18.33813 ? 275 ALA B N   1 
ATOM   5070 C CA  . ALA B 1 275 ? 40.83600  21.41400  40.49000  1.000 24.58687 ? 275 ALA B CA  1 
ATOM   5071 C C   . ALA B 1 275 ? 40.96100  19.91900  40.73900  1.000 22.53335 ? 275 ALA B C   1 
ATOM   5072 O O   . ALA B 1 275 ? 41.04900  19.13100  39.79000  1.000 26.26246 ? 275 ALA B O   1 
ATOM   5073 C CB  . ALA B 1 275 ? 42.18500  22.10700  40.69700  1.000 24.73923 ? 275 ALA B CB  1 
ATOM   5074 N N   . ASN B 1 276 ? 40.95600  19.50700  42.01100  1.000 21.09553 ? 276 ASN B N   1 
ATOM   5075 C CA  . ASN B 1 276 ? 40.99200  18.08100  42.32600  1.000 23.20942 ? 276 ASN B CA  1 
ATOM   5076 C C   . ASN B 1 276 ? 39.75900  17.36500  41.78800  1.000 21.89364 ? 276 ASN B C   1 
ATOM   5077 O O   . ASN B 1 276 ? 39.86700  16.28700  41.19400  1.000 21.30915 ? 276 ASN B O   1 
ATOM   5078 C CB  . ASN B 1 276 ? 41.10300  17.87400  43.83800  1.000 20.44852 ? 276 ASN B CB  1 
ATOM   5079 C CG  . ASN B 1 276 ? 42.52900  17.96200  44.34300  1.000 24.43791 ? 276 ASN B CG  1 
ATOM   5080 O OD1 . ASN B 1 276 ? 43.48000  17.93200  43.55900  1.000 21.29082 ? 276 ASN B OD1 1 
ATOM   5081 N ND2 . ASN B 1 276 ? 42.68800  18.05800  45.66600  1.000 21.88799 ? 276 ASN B ND2 1 
ATOM   5082 N N   . ALA B 1 277 ? 38.57700  17.95800  41.97900  1.000 18.46728 ? 277 ALA B N   1 
ATOM   5083 C CA  . ALA B 1 277 ? 37.34200  17.31200  41.55000  1.000 20.42290 ? 277 ALA B CA  1 
ATOM   5084 C C   . ALA B 1 277 ? 37.30300  17.12400  40.03300  1.000 25.11788 ? 277 ALA B C   1 
ATOM   5085 O O   . ALA B 1 277 ? 36.87600  16.07100  39.54100  1.000 20.88976 ? 277 ALA B O   1 
ATOM   5086 C CB  . ALA B 1 277 ? 36.14100  18.12600  42.02500  1.000 14.91355 ? 277 ALA B CB  1 
ATOM   5087 N N   . GLN B 1 278 ? 37.74700  18.13100  39.27500  1.000 20.88607 ? 278 GLN B N   1 
ATOM   5088 C CA  . GLN B 1 278 ? 37.74000  18.00900  37.82200  1.000 21.18567 ? 278 GLN B CA  1 
ATOM   5089 C C   . GLN B 1 278 ? 38.62500  16.85100  37.35900  1.000 24.90756 ? 278 GLN B C   1 
ATOM   5090 O O   . GLN B 1 278 ? 38.21300  16.04800  36.51100  1.000 23.83008 ? 278 GLN B O   1 
ATOM   5091 C CB  . GLN B 1 278 ? 38.18200  19.33000  37.19100  1.000 21.23665 ? 278 GLN B CB  1 
ATOM   5092 C CG  . GLN B 1 278 ? 38.17300  19.34300  35.66200  1.000 20.77313 ? 278 GLN B CG  1 
ATOM   5093 C CD  . GLN B 1 278 ? 36.77600  19.44500  35.08600  1.000 22.76332 ? 278 GLN B CD  1 
ATOM   5094 O OE1 . GLN B 1 278 ? 35.92300  20.17100  35.60700  1.000 22.21967 ? 278 GLN B OE1 1 
ATOM   5095 N NE2 . GLN B 1 278 ? 36.53000  18.71000  34.00900  1.000 21.75975 ? 278 GLN B NE2 1 
ATOM   5096 N N   . LYS B 1 279 ? 39.83200  16.73000  37.92700  1.000 19.60511 ? 279 LYS B N   1 
ATOM   5097 C CA  . LYS B 1 279 ? 40.70600  15.61200  37.57900  1.000 24.33243 ? 279 LYS B CA  1 
ATOM   5098 C C   . LYS B 1 279 ? 40.06500  14.27700  37.93300  1.000 27.33724 ? 279 LYS B C   1 
ATOM   5099 O O   . LYS B 1 279 ? 40.12500  13.32000  37.15100  1.000 27.61838 ? 279 LYS B O   1 
ATOM   5100 C CB  . LYS B 1 279 ? 42.05500  15.73600  38.29700  1.000 26.63965 ? 279 LYS B CB  1 
ATOM   5101 C CG  . LYS B 1 279 ? 42.88300  16.96500  37.94500  1.000 33.73465 ? 279 LYS B CG  1 
ATOM   5102 C CD  . LYS B 1 279 ? 44.28900  16.86400  38.53700  1.000 35.07653 ? 279 LYS B CD  1 
ATOM   5103 C CE  . LYS B 1 279 ? 44.94800  18.23500  38.65600  1.000 37.77077 ? 279 LYS B CE  1 
ATOM   5104 N NZ  . LYS B 1 279 ? 44.28200  19.09000  39.69300  1.000 44.99689 ? 279 LYS B NZ  1 
ATOM   5105 N N   . ILE B 1 280 ? 39.46900  14.18500  39.12200  1.000 26.54925 ? 280 ILE B N   1 
ATOM   5106 C CA  . ILE B 1 280 ? 38.91200  12.91400  39.56600  1.000 25.19150 ? 280 ILE B CA  1 
ATOM   5107 C C   . ILE B 1 280 ? 37.66600  12.56100  38.76300  1.000 22.07432 ? 280 ILE B C   1 
ATOM   5108 O O   . ILE B 1 280 ? 37.45300  11.39600  38.40800  1.000 22.38875 ? 280 ILE B O   1 
ATOM   5109 C CB  . ILE B 1 280 ? 38.63600  12.96100  41.07800  1.000 24.93223 ? 280 ILE B CB  1 
ATOM   5110 C CG1 . ILE B 1 280 ? 39.96200  13.03500  41.83800  1.000 20.81020 ? 280 ILE B CG1 1 
ATOM   5111 C CG2 . ILE B 1 280 ? 37.81300  11.75700  41.51700  1.000 17.58050 ? 280 ILE B CG2 1 
ATOM   5112 C CD1 . ILE B 1 280 ? 39.78600  13.24600  43.30900  1.000 28.64547 ? 280 ILE B CD1 1 
ATOM   5113 N N   . ALA B 1 281 ? 36.82900  13.55700  38.45400  1.000 19.63218 ? 281 ALA B N   1 
ATOM   5114 C CA  . ALA B 1 281 ? 35.60100  13.28000  37.71500  1.000 24.67188 ? 281 ALA B CA  1 
ATOM   5115 C C   . ALA B 1 281 ? 35.90900  12.70000  36.33700  1.000 25.69631 ? 281 ALA B C   1 
ATOM   5116 O O   . ALA B 1 281 ? 35.30600  11.70100  35.92400  1.000 25.22775 ? 281 ALA B O   1 
ATOM   5117 C CB  . ALA B 1 281 ? 34.75600  14.55000  37.59500  1.000 20.01149 ? 281 ALA B CB  1 
ATOM   5118 N N   . GLU B 1 282 ? 36.86800  13.30000  35.62300  1.000 23.33915 ? 282 GLU B N   1 
ATOM   5119 C CA  . GLU B 1 282 ? 37.22900  12.80600  34.29400  1.000 30.94069 ? 282 GLU B CA  1 
ATOM   5120 C C   . GLU B 1 282 ? 37.87200  11.42600  34.36500  1.000 25.74954 ? 282 GLU B C   1 
ATOM   5121 O O   . GLU B 1 282 ? 37.57900  10.55700  33.53800  1.000 23.60327 ? 282 GLU B O   1 
ATOM   5122 C CB  . GLU B 1 282 ? 38.16500  13.79300  33.59700  1.000 26.67050 ? 282 GLU B CB  1 
ATOM   5123 C CG  . GLU B 1 282 ? 37.53400  15.14300  33.27800  1.000 27.19546 ? 282 GLU B CG  1 
ATOM   5124 C CD  . GLU B 1 282 ? 38.52400  16.10500  32.64600  1.000 29.75525 ? 282 GLU B CD  1 
ATOM   5125 O OE1 . GLU B 1 282 ? 39.61300  15.64800  32.24400  1.000 34.41748 ? 282 GLU B OE1 1 
ATOM   5126 O OE2 . GLU B 1 282 ? 38.22200  17.31400  32.55900  1.000 29.21344 ? 282 GLU B OE2 1 
ATOM   5127 N N   . TRP B 1 283 ? 38.74600  11.20400  35.34500  1.000 24.71440 ? 283 TRP B N   1 
ATOM   5128 C CA  . TRP B 1 283 ? 39.36000  9.88900   35.50400  1.000 24.89025 ? 283 TRP B CA  1 
ATOM   5129 C C   . TRP B 1 283 ? 38.31600  8.81800   35.82300  1.000 29.57067 ? 283 TRP B C   1 
ATOM   5130 O O   . TRP B 1 283 ? 38.40000  7.68800   35.32200  1.000 29.93354 ? 283 TRP B O   1 
ATOM   5131 C CB  . TRP B 1 283 ? 40.43100  9.95000   36.59300  1.000 22.44881 ? 283 TRP B CB  1 
ATOM   5132 C CG  . TRP B 1 283 ? 41.00900  8.62000   36.94800  1.000 27.48902 ? 283 TRP B CG  1 
ATOM   5133 C CD1 . TRP B 1 283 ? 41.94100  7.91700   36.24300  1.000 30.70689 ? 283 TRP B CD1 1 
ATOM   5134 C CD2 . TRP B 1 283 ? 40.70200  7.83300   38.10500  1.000 27.78102 ? 283 TRP B CD2 1 
ATOM   5135 N NE1 . TRP B 1 283 ? 42.23000  6.73700   36.88800  1.000 28.63848 ? 283 TRP B NE1 1 
ATOM   5136 C CE2 . TRP B 1 283 ? 41.48200  6.66200   38.03200  1.000 27.06414 ? 283 TRP B CE2 1 
ATOM   5137 C CE3 . TRP B 1 283 ? 39.83900  8.00400   39.19400  1.000 27.31042 ? 283 TRP B CE3 1 
ATOM   5138 C CZ2 . TRP B 1 283 ? 41.42700  5.66900   39.00600  1.000 30.75547 ? 283 TRP B CZ2 1 
ATOM   5139 C CZ3 . TRP B 1 283 ? 39.78700  7.01900   40.15800  1.000 25.62648 ? 283 TRP B CZ3 1 
ATOM   5140 C CH2 . TRP B 1 283 ? 40.57600  5.86500   40.05900  1.000 25.82110 ? 283 TRP B CH2 1 
ATOM   5141 N N   . LEU B 1 284 ? 37.32900  9.15200   36.66100  1.000 26.78959 ? 284 LEU B N   1 
ATOM   5142 C CA  . LEU B 1 284 ? 36.26900  8.20000   36.98500  1.000 24.86604 ? 284 LEU B CA  1 
ATOM   5143 C C   . LEU B 1 284 ? 35.42600  7.86300   35.76200  1.000 24.68470 ? 284 LEU B C   1 
ATOM   5144 O O   . LEU B 1 284 ? 35.03300  6.70700   35.57100  1.000 22.57345 ? 284 LEU B O   1 
ATOM   5145 C CB  . LEU B 1 284 ? 35.37600  8.75800   38.09300  1.000 20.18797 ? 284 LEU B CB  1 
ATOM   5146 C CG  . LEU B 1 284 ? 35.93600  8.72200   39.50900  1.000 24.95991 ? 284 LEU B CG  1 
ATOM   5147 C CD1 . LEU B 1 284 ? 35.06500  9.54600   40.44700  1.000 23.48684 ? 284 LEU B CD1 1 
ATOM   5148 C CD2 . LEU B 1 284 ? 36.01900  7.28400   39.97400  1.000 21.46848 ? 284 LEU B CD2 1 
ATOM   5149 N N   . GLU B 1 285 ? 35.11200  8.86600   34.93800  1.000 24.11332 ? 285 GLU B N   1 
ATOM   5150 C CA  . GLU B 1 285 ? 34.22800  8.63800   33.80000  1.000 30.31592 ? 285 GLU B CA  1 
ATOM   5151 C C   . GLU B 1 285 ? 34.85200  7.68600   32.78600  1.000 28.08140 ? 285 GLU B C   1 
ATOM   5152 O O   . GLU B 1 285 ? 34.13000  7.00400   32.05300  1.000 28.63300 ? 285 GLU B O   1 
ATOM   5153 C CB  . GLU B 1 285 ? 33.86300  9.97400   33.14100  1.000 30.46223 ? 285 GLU B CB  1 
ATOM   5154 C CG  . GLU B 1 285 ? 32.53600  9.95000   32.38400  1.000 27.24475 ? 285 GLU B CG  1 
ATOM   5155 C CD  . GLU B 1 285 ? 32.13100  11.30700  31.83400  1.000 31.05261 ? 285 GLU B CD  1 
ATOM   5156 O OE1 . GLU B 1 285 ? 33.02100  12.09800  31.45100  1.000 30.66126 ? 285 GLU B OE1 1 
ATOM   5157 O OE2 . GLU B 1 285 ? 30.91300  11.58500  31.78400  1.000 29.24725 ? 285 GLU B OE2 1 
ATOM   5158 N N   . ALA B 1 286 ? 36.18200  7.60700   32.74600  1.000 26.65142 ? 286 ALA B N   1 
ATOM   5159 C CA  . ALA B 1 286 ? 36.88100  6.73300   31.81500  1.000 29.58391 ? 286 ALA B CA  1 
ATOM   5160 C C   . ALA B 1 286 ? 37.12700  5.33500   32.36300  1.000 27.04517 ? 286 ALA B C   1 
ATOM   5161 O O   . ALA B 1 286 ? 37.59800  4.47300   31.61500  1.000 33.24556 ? 286 ALA B O   1 
ATOM   5162 C CB  . ALA B 1 286 ? 38.22100  7.35600   31.40600  1.000 22.89368 ? 286 ALA B CB  1 
ATOM   5163 N N   . ARG B 1 287 ? 36.83200  5.08500   33.63400  1.000 26.97840 ? 287 ARG B N   1 
ATOM   5164 C CA  . ARG B 1 287 ? 37.03000  3.74800   34.17700  1.000 29.90390 ? 287 ARG B CA  1 
ATOM   5165 C C   . ARG B 1 287 ? 35.96000  2.79900   33.64000  1.000 30.89110 ? 287 ARG B C   1 
ATOM   5166 O O   . ARG B 1 287 ? 34.80000  3.19300   33.47600  1.000 30.24111 ? 287 ARG B O   1 
ATOM   5167 C CB  . ARG B 1 287 ? 36.99400  3.76800   35.70600  1.000 31.68874 ? 287 ARG B CB  1 
ATOM   5168 C CG  . ARG B 1 287 ? 38.15900  4.50600   36.35600  1.000 29.51807 ? 287 ARG B CG  1 
ATOM   5169 C CD  . ARG B 1 287 ? 39.46200  3.73600   36.21800  1.000 30.69695 ? 287 ARG B CD  1 
ATOM   5170 N NE  . ARG B 1 287 ? 39.38700  2.42500   36.85400  1.000 34.70476 ? 287 ARG B NE  1 
ATOM   5171 C CZ  . ARG B 1 287 ? 40.43900  1.70700   37.22300  1.000 37.58238 ? 287 ARG B CZ  1 
ATOM   5172 N NH1 . ARG B 1 287 ? 41.67400  2.16100   37.07200  1.000 35.25730 ? 287 ARG B NH1 1 
ATOM   5173 N NH2 . ARG B 1 287 ? 40.24900  0.50200   37.75700  1.000 31.47106 ? 287 ARG B NH2 1 
ATOM   5174 N N   . PRO B 1 288 ? 36.31900  1.55300   33.33000  1.000 29.34938 ? 288 PRO B N   1 
ATOM   5175 C CA  . PRO B 1 288 ? 35.29800  0.59800   32.87400  1.000 30.69482 ? 288 PRO B CA  1 
ATOM   5176 C C   . PRO B 1 288 ? 34.25300  0.29200   33.93100  1.000 31.78321 ? 288 PRO B C   1 
ATOM   5177 O O   . PRO B 1 288 ? 33.09800  0.02000   33.58100  1.000 27.00468 ? 288 PRO B O   1 
ATOM   5178 C CB  . PRO B 1 288 ? 36.12000  -0.64700  32.51500  1.000 26.58661 ? 288 PRO B CB  1 
ATOM   5179 C CG  . PRO B 1 288 ? 37.53800  -0.17700  32.41900  1.000 34.64091 ? 288 PRO B CG  1 
ATOM   5180 C CD  . PRO B 1 288 ? 37.65500  0.94300   33.39100  1.000 29.26495 ? 288 PRO B CD  1 
ATOM   5181 N N   . GLU B 1 289 ? 34.62900  0.32800   35.21600  1.000 26.11307 ? 289 GLU B N   1 
ATOM   5182 C CA  . GLU B 1 289 ? 33.72500  -0.02600  36.30600  1.000 27.23275 ? 289 GLU B CA  1 
ATOM   5183 C C   . GLU B 1 289 ? 32.64700  1.01800   36.55600  1.000 27.75035 ? 289 GLU B C   1 
ATOM   5184 O O   . GLU B 1 289 ? 31.71500  0.74300   37.32000  1.000 28.25550 ? 289 GLU B O   1 
ATOM   5185 C CB  . GLU B 1 289 ? 34.50400  -0.24000  37.61100  1.000 27.81728 ? 289 GLU B CB  1 
ATOM   5186 C CG  . GLU B 1 289 ? 35.66500  -1.22400  37.53400  1.000 28.27068 ? 289 GLU B CG  1 
ATOM   5187 C CD  . GLU B 1 289 ? 36.99100  -0.54800  37.21900  1.000 28.24411 ? 289 GLU B CD  1 
ATOM   5188 O OE1 . GLU B 1 289 ? 36.98100  0.52100   36.57500  1.000 27.02613 ? 289 GLU B OE1 1 
ATOM   5189 O OE2 . GLU B 1 289 ? 38.04600  -1.08400  37.62000  1.000 35.00744 ? 289 GLU B OE2 1 
ATOM   5190 N N   . VAL B 1 290 ? 32.74500  2.19500   35.94400  1.000 27.27816 ? 290 VAL B N   1 
ATOM   5191 C CA  . VAL B 1 290 ? 31.87700  3.32500   36.25900  1.000 29.31522 ? 290 VAL B CA  1 
ATOM   5192 C C   . VAL B 1 290 ? 30.87900  3.50400   35.12500  1.000 26.39408 ? 290 VAL B C   1 
ATOM   5193 O O   . VAL B 1 290 ? 31.27200  3.69500   33.96800  1.000 28.83735 ? 290 VAL B O   1 
ATOM   5194 C CB  . VAL B 1 290 ? 32.68700  4.61000   36.48700  1.000 26.11853 ? 290 VAL B CB  1 
ATOM   5195 C CG1 . VAL B 1 290 ? 31.75900  5.77900   36.77000  1.000 23.55373 ? 290 VAL B CG1 1 
ATOM   5196 C CG2 . VAL B 1 290 ? 33.66900  4.41200   37.62200  1.000 25.47178 ? 290 VAL B CG2 1 
ATOM   5197 N N   . ALA B 1 291 ? 29.58600  3.46800   35.46500  1.000 25.67295 ? 291 ALA B N   1 
ATOM   5198 C CA  . ALA B 1 291 ? 28.53300  3.63100   34.46700  1.000 27.08695 ? 291 ALA B CA  1 
ATOM   5199 C C   . ALA B 1 291 ? 28.28100  5.09700   34.13200  1.000 28.25331 ? 291 ALA B C   1 
ATOM   5200 O O   . ALA B 1 291 ? 28.05300  5.43900   32.96700  1.000 29.63504 ? 291 ALA B O   1 
ATOM   5201 C CB  . ALA B 1 291 ? 27.24100  2.98400   34.96100  1.000 21.79065 ? 291 ALA B CB  1 
ATOM   5202 N N   . ARG B 1 292 ? 28.29700  5.97300   35.13300  1.000 26.78656 ? 292 ARG B N   1 
ATOM   5203 C CA  . ARG B 1 292 ? 27.99800  7.38000   34.91000  1.000 27.54886 ? 292 ARG B CA  1 
ATOM   5204 C C   . ARG B 1 292 ? 28.65900  8.20100   36.00700  1.000 26.00358 ? 292 ARG B C   1 
ATOM   5205 O O   . ARG B 1 292 ? 28.83600  7.72800   37.13300  1.000 28.15334 ? 292 ARG B O   1 
ATOM   5206 C CB  . ARG B 1 292 ? 26.48300  7.64500   34.88200  1.000 22.75014 ? 292 ARG B CB  1 
ATOM   5207 C CG  . ARG B 1 292 ? 26.12100  9.08400   34.53500  1.000 27.76860 ? 292 ARG B CG  1 
ATOM   5208 C CD  . ARG B 1 292 ? 24.62100  9.30500   34.41000  1.000 32.56249 ? 292 ARG B CD  1 
ATOM   5209 N NE  . ARG B 1 292 ? 24.31500  10.71500  34.18900  1.000 31.35433 ? 292 ARG B NE  1 
ATOM   5210 C CZ  . ARG B 1 292 ? 23.08900  11.21900  34.14700  1.000 35.12530 ? 292 ARG B CZ  1 
ATOM   5211 N NH1 . ARG B 1 292 ? 22.02000  10.45100  34.28500  1.000 37.12757 ? 292 ARG B NH1 1 
ATOM   5212 N NH2 . ARG B 1 292 ? 22.93200  12.52900  33.97200  1.000 35.25777 ? 292 ARG B NH2 1 
ATOM   5213 N N   . VAL B 1 293 ? 29.03200  9.42800   35.66100  1.000 27.08943 ? 293 VAL B N   1 
ATOM   5214 C CA  . VAL B 1 293 ? 29.58300  10.38500  36.60800  1.000 24.52338 ? 293 VAL B CA  1 
ATOM   5215 C C   . VAL B 1 293 ? 28.73200  11.64300  36.54200  1.000 25.56132 ? 293 VAL B C   1 
ATOM   5216 O O   . VAL B 1 293 ? 28.31300  12.06400  35.45700  1.000 25.09295 ? 293 VAL B O   1 
ATOM   5217 C CB  . VAL B 1 293 ? 31.06700  10.69200  36.31700  1.000 19.76850 ? 293 VAL B CB  1 
ATOM   5218 C CG1 . VAL B 1 293 ? 31.61200  11.68300  37.32100  1.000 21.51452 ? 293 VAL B CG1 1 
ATOM   5219 C CG2 . VAL B 1 293 ? 31.88000  9.41300   36.36000  1.000 22.44917 ? 293 VAL B CG2 1 
ATOM   5220 N N   . TYR B 1 294 ? 28.43600  12.20600  37.71200  1.000 21.60344 ? 294 TYR B N   1 
ATOM   5221 C CA  . TYR B 1 294 ? 27.65000  13.42700  37.85100  1.000 21.04683 ? 294 TYR B CA  1 
ATOM   5222 C C   . TYR B 1 294 ? 28.58000  14.51700  38.37200  1.000 21.43237 ? 294 TYR B C   1 
ATOM   5223 O O   . TYR B 1 294 ? 28.94500  14.51200  39.55200  1.000 22.75897 ? 294 TYR B O   1 
ATOM   5224 C CB  . TYR B 1 294 ? 26.47600  13.22300  38.81000  1.000 22.72625 ? 294 TYR B CB  1 
ATOM   5225 C CG  . TYR B 1 294 ? 25.61800  12.00500  38.54400  1.000 24.31500 ? 294 TYR B CG  1 
ATOM   5226 C CD1 . TYR B 1 294 ? 26.01400  10.74300  38.97400  1.000 23.91813 ? 294 TYR B CD1 1 
ATOM   5227 C CD2 . TYR B 1 294 ? 24.39700  12.12000  37.88800  1.000 22.16382 ? 294 TYR B CD2 1 
ATOM   5228 C CE1 . TYR B 1 294 ? 25.23000  9.62900   38.74200  1.000 23.09737 ? 294 TYR B CE1 1 
ATOM   5229 C CE2 . TYR B 1 294 ? 23.60400  11.01000  37.64900  1.000 24.23872 ? 294 TYR B CE2 1 
ATOM   5230 C CZ  . TYR B 1 294 ? 24.02600  9.76700   38.08000  1.000 28.07886 ? 294 TYR B CZ  1 
ATOM   5231 O OH  . TYR B 1 294 ? 23.24500  8.65300   37.85000  1.000 29.00444 ? 294 TYR B OH  1 
ATOM   5232 N N   . TYR B 1 295 ? 28.96800  15.43800  37.50400  1.000 17.99613 ? 295 TYR B N   1 
ATOM   5233 C CA  . TYR B 1 295 ? 29.81000  16.55000  37.92400  1.000 22.20741 ? 295 TYR B CA  1 
ATOM   5234 C C   . TYR B 1 295 ? 29.64700  17.71800  36.95700  1.000 21.59563 ? 295 TYR B C   1 
ATOM   5235 O O   . TYR B 1 295 ? 29.80400  17.53800  35.74400  1.000 26.21365 ? 295 TYR B O   1 
ATOM   5236 C CB  . TYR B 1 295 ? 31.27200  16.11300  38.01300  1.000 19.44209 ? 295 TYR B CB  1 
ATOM   5237 C CG  . TYR B 1 295 ? 32.19900  17.22900  38.42300  1.000 23.76244 ? 295 TYR B CG  1 
ATOM   5238 C CD1 . TYR B 1 295 ? 32.19100  17.72500  39.72400  1.000 20.51847 ? 295 TYR B CD1 1 
ATOM   5239 C CD2 . TYR B 1 295 ? 33.08400  17.79000  37.51200  1.000 20.60817 ? 295 TYR B CD2 1 
ATOM   5240 C CE1 . TYR B 1 295 ? 33.04000  18.75200  40.10400  1.000 18.64058 ? 295 TYR B CE1 1 
ATOM   5241 C CE2 . TYR B 1 295 ? 33.93400  18.81400  37.88000  1.000 23.13745 ? 295 TYR B CE2 1 
ATOM   5242 C CZ  . TYR B 1 295 ? 33.90700  19.29400  39.17500  1.000 21.68310 ? 295 TYR B CZ  1 
ATOM   5243 O OH  . TYR B 1 295 ? 34.76000  20.31100  39.53600  1.000 25.11966 ? 295 TYR B OH  1 
ATOM   5244 N N   . PRO B 1 296 ? 29.33900  18.92200  37.45000  1.000 22.88022 ? 296 PRO B N   1 
ATOM   5245 C CA  . PRO B 1 296 ? 28.98900  20.03200  36.54000  1.000 21.30950 ? 296 PRO B CA  1 
ATOM   5246 C C   . PRO B 1 296 ? 30.10100  20.45000  35.58900  1.000 22.53593 ? 296 PRO B C   1 
ATOM   5247 O O   . PRO B 1 296 ? 29.81000  21.08900  34.56900  1.000 22.92549 ? 296 PRO B O   1 
ATOM   5248 C CB  . PRO B 1 296 ? 28.62200  21.17100  37.50400  1.000 22.18460 ? 296 PRO B CB  1 
ATOM   5249 C CG  . PRO B 1 296 ? 28.19900  20.46400  38.76500  1.000 22.72940 ? 296 PRO B CG  1 
ATOM   5250 C CD  . PRO B 1 296 ? 29.11600  19.27700  38.86100  1.000 19.68956 ? 296 PRO B CD  1 
ATOM   5251 N N   . GLY B 1 297 ? 31.35400  20.12300  35.88000  1.000 22.36473 ? 297 GLY B N   1 
ATOM   5252 C CA  . GLY B 1 297 ? 32.45300  20.43200  34.99100  1.000 21.32392 ? 297 GLY B CA  1 
ATOM   5253 C C   . GLY B 1 297 ? 32.70500  19.40700  33.91100  1.000 24.76766 ? 297 GLY B C   1 
ATOM   5254 O O   . GLY B 1 297 ? 33.70800  19.50300  33.19400  1.000 29.50640 ? 297 GLY B O   1 
ATOM   5255 N N   . LEU B 1 298 ? 31.83000  18.41700  33.78400  1.000 24.18858 ? 298 LEU B N   1 
ATOM   5256 C CA  . LEU B 1 298 ? 31.96500  17.37300  32.78200  1.000 26.23199 ? 298 LEU B CA  1 
ATOM   5257 C C   . LEU B 1 298 ? 31.15700  17.74000  31.54600  1.000 29.70471 ? 298 LEU B C   1 
ATOM   5258 O O   . LEU B 1 298 ? 30.03100  18.23600  31.65500  1.000 25.24509 ? 298 LEU B O   1 
ATOM   5259 C CB  . LEU B 1 298 ? 31.48400  16.03700  33.34900  1.000 26.60138 ? 298 LEU B CB  1 
ATOM   5260 C CG  . LEU B 1 298 ? 32.49700  14.90200  33.50600  1.000 26.94955 ? 298 LEU B CG  1 
ATOM   5261 C CD1 . LEU B 1 298 ? 33.87300  15.42400  33.88100  1.000 27.16649 ? 298 LEU B CD1 1 
ATOM   5262 C CD2 . LEU B 1 298 ? 31.98900  13.92400  34.54900  1.000 22.20814 ? 298 LEU B CD2 1 
ATOM   5263 N N   . ASP B 1 299 ? 31.74300  17.50300  30.36600  1.000 26.59434 ? 299 ASP B N   1 
ATOM   5264 C CA  . ASP B 1 299 ? 31.01700  17.74500  29.12200  1.000 28.57338 ? 299 ASP B CA  1 
ATOM   5265 C C   . ASP B 1 299 ? 29.73100  16.93200  29.05900  1.000 28.89949 ? 299 ASP B C   1 
ATOM   5266 O O   . ASP B 1 299 ? 28.74100  17.37700  28.46400  1.000 30.75725 ? 299 ASP B O   1 
ATOM   5267 C CB  . ASP B 1 299 ? 31.90200  17.42300  27.91600  1.000 29.74207 ? 299 ASP B CB  1 
ATOM   5268 C CG  . ASP B 1 299 ? 32.97600  18.46800  27.67900  1.000 34.13388 ? 299 ASP B CG  1 
ATOM   5269 O OD1 . ASP B 1 299 ? 33.00600  19.48400  28.40600  1.000 37.04041 ? 299 ASP B OD1 1 
ATOM   5270 O OD2 . ASP B 1 299 ? 33.79500  18.27400  26.75700  1.000 47.35958 ? 299 ASP B OD2 1 
ATOM   5271 N N   . SER B 1 300 ? 29.71800  15.75300  29.68100  1.000 26.42824 ? 300 SER B N   1 
ATOM   5272 C CA  . SER B 1 300 ? 28.52800  14.91200  29.67700  1.000 27.86063 ? 300 SER B CA  1 
ATOM   5273 C C   . SER B 1 300 ? 27.42600  15.43000  30.59000  1.000 27.77353 ? 300 SER B C   1 
ATOM   5274 O O   . SER B 1 300 ? 26.31200  14.89700  30.54600  1.000 31.87332 ? 300 SER B O   1 
ATOM   5275 C CB  . SER B 1 300 ? 28.90300  13.48500  30.07800  1.000 24.63712 ? 300 SER B CB  1 
ATOM   5276 O OG  . SER B 1 300 ? 29.57500  13.47300  31.32500  1.000 35.12765 ? 300 SER B OG  1 
ATOM   5277 N N   . HIS B 1 301 ? 27.69600  16.43100  31.41200  1.000 25.31752 ? 301 HIS B N   1 
ATOM   5278 C CA  . HIS B 1 301 ? 26.66000  16.93800  32.30700  1.000 26.59423 ? 301 HIS B CA  1 
ATOM   5279 C C   . HIS B 1 301 ? 25.61400  17.68200  31.48500  1.000 25.78367 ? 301 HIS B C   1 
ATOM   5280 O O   . HIS B 1 301 ? 25.96300  18.58900  30.72200  1.000 26.83076 ? 301 HIS B O   1 
ATOM   5281 C CB  . HIS B 1 301 ? 27.26600  17.85200  33.37200  1.000 21.99929 ? 301 HIS B CB  1 
ATOM   5282 C CG  . HIS B 1 301 ? 26.31600  18.22300  34.46800  1.000 24.86809 ? 301 HIS B CG  1 
ATOM   5283 N ND1 . HIS B 1 301 ? 25.23500  19.05500  34.26800  1.000 22.27639 ? 301 HIS B ND1 1 
ATOM   5284 C CD2 . HIS B 1 301 ? 26.29000  17.87800  35.77800  1.000 20.65198 ? 301 HIS B CD2 1 
ATOM   5285 C CE1 . HIS B 1 301 ? 24.58100  19.20300  35.40700  1.000 23.62489 ? 301 HIS B CE1 1 
ATOM   5286 N NE2 . HIS B 1 301 ? 25.20200  18.50100  36.34000  1.000 24.19271 ? 301 HIS B NE2 1 
ATOM   5287 N N   . PRO B 1 302 ? 24.33300  17.32300  31.59500  1.000 24.96994 ? 302 PRO B N   1 
ATOM   5288 C CA  . PRO B 1 302 ? 23.32100  17.93000  30.71600  1.000 25.56376 ? 302 PRO B CA  1 
ATOM   5289 C C   . PRO B 1 302 ? 23.08500  19.41600  30.95100  1.000 27.19064 ? 302 PRO B C   1 
ATOM   5290 O O   . PRO B 1 302 ? 22.36500  20.03200  30.15600  1.000 31.26185 ? 302 PRO B O   1 
ATOM   5291 C CB  . PRO B 1 302 ? 22.05500  17.10900  31.01300  1.000 31.19049 ? 302 PRO B CB  1 
ATOM   5292 C CG  . PRO B 1 302 ? 22.32700  16.40500  32.30900  1.000 27.39150 ? 302 PRO B CG  1 
ATOM   5293 C CD  . PRO B 1 302 ? 23.80300  16.16600  32.33500  1.000 27.05750 ? 302 PRO B CD  1 
ATOM   5294 N N   . GLN B 1 303 ? 23.66100  20.01800  31.98800  1.000 24.58320 ? 303 GLN B N   1 
ATOM   5295 C CA  . GLN B 1 303 ? 23.48800  21.44500  32.24500  1.000 24.41821 ? 303 GLN B CA  1 
ATOM   5296 C C   . GLN B 1 303 ? 24.82700  22.12000  32.48100  1.000 24.35670 ? 303 GLN B C   1 
ATOM   5297 O O   . GLN B 1 303 ? 24.94900  23.02400  33.31500  1.000 22.27554 ? 303 GLN B O   1 
ATOM   5298 C CB  . GLN B 1 303 ? 22.56700  21.68500  33.43600  1.000 25.02985 ? 303 GLN B CB  1 
ATOM   5299 C CG  . GLN B 1 303 ? 21.26700  20.94400  33.36600  1.000 24.12028 ? 303 GLN B CG  1 
ATOM   5300 C CD  . GLN B 1 303 ? 20.58500  20.90500  34.69700  1.000 25.54155 ? 303 GLN B CD  1 
ATOM   5301 O OE1 . GLN B 1 303 ? 20.84500  20.01700  35.51200  1.000 25.26566 ? 303 GLN B OE1 1 
ATOM   5302 N NE2 . GLN B 1 303 ? 19.71600  21.88000  34.94500  1.000 25.15701 ? 303 GLN B NE2 1 
ATOM   5303 N N   . GLN B 1 304 ? 25.85100  21.69600  31.74100  1.000 23.92364 ? 304 GLN B N   1 
ATOM   5304 C CA  . GLN B 1 304 ? 27.18100  22.27000  31.91600  1.000 25.64836 ? 304 GLN B CA  1 
ATOM   5305 C C   . GLN B 1 304 ? 27.17600  23.77500  31.66900  1.000 26.97793 ? 304 GLN B C   1 
ATOM   5306 O O   . GLN B 1 304 ? 27.79600  24.53700  32.42300  1.000 27.66505 ? 304 GLN B O   1 
ATOM   5307 C CB  . GLN B 1 304 ? 28.16300  21.57200  30.97700  1.000 26.03366 ? 304 GLN B CB  1 
ATOM   5308 C CG  . GLN B 1 304 ? 29.61700  21.93500  31.20300  1.000 27.40449 ? 304 GLN B CG  1 
ATOM   5309 C CD  . GLN B 1 304 ? 30.51700  21.31000  30.16200  1.000 29.39813 ? 304 GLN B CD  1 
ATOM   5310 O OE1 . GLN B 1 304 ? 30.07200  20.99600  29.05900  1.000 25.66750 ? 304 GLN B OE1 1 
ATOM   5311 N NE2 . GLN B 1 304 ? 31.78700  21.11900  30.50600  1.000 29.52308 ? 304 GLN B NE2 1 
ATOM   5312 N N   . ALA B 1 305 ? 26.47100  24.22200  30.62400  1.000 24.44238 ? 305 ALA B N   1 
ATOM   5313 C CA  . ALA B 1 305 ? 26.46900  25.63900  30.27600  1.000 22.42061 ? 305 ALA B CA  1 
ATOM   5314 C C   . ALA B 1 305 ? 25.74500  26.47000  31.32500  1.000 23.34080 ? 305 ALA B C   1 
ATOM   5315 O O   . ALA B 1 305 ? 26.22200  27.54500  31.70800  1.000 24.58628 ? 305 ALA B O   1 
ATOM   5316 C CB  . ALA B 1 305 ? 25.83100  25.84400  28.89900  1.000 21.96171 ? 305 ALA B CB  1 
ATOM   5317 N N   . LEU B 1 306 ? 24.58300  26.00600  31.79000  1.000 23.63870 ? 306 LEU B N   1 
ATOM   5318 C CA  . LEU B 1 306 ? 23.88500  26.74000  32.83700  1.000 18.89864 ? 306 LEU B CA  1 
ATOM   5319 C C   . LEU B 1 306 ? 24.73600  26.81700  34.09600  1.000 20.65123 ? 306 LEU B C   1 
ATOM   5320 O O   . LEU B 1 306 ? 24.79900  27.86300  34.75000  1.000 20.31218 ? 306 LEU B O   1 
ATOM   5321 C CB  . LEU B 1 306 ? 22.53600  26.09100  33.13800  1.000 24.90238 ? 306 LEU B CB  1 
ATOM   5322 C CG  . LEU B 1 306 ? 21.71000  26.81300  34.20800  1.000 24.99039 ? 306 LEU B CG  1 
ATOM   5323 C CD1 . LEU B 1 306 ? 21.57800  28.29900  33.88300  1.000 23.87860 ? 306 LEU B CD1 1 
ATOM   5324 C CD2 . LEU B 1 306 ? 20.33800  26.17000  34.36500  1.000 21.49016 ? 306 LEU B CD2 1 
ATOM   5325 N N   . ALA B 1 307 ? 25.41100  25.71900  34.43800  1.000 18.50489 ? 307 ALA B N   1 
ATOM   5326 C CA  . ALA B 1 307 ? 26.29100  25.72400  35.59900  1.000 18.11981 ? 307 ALA B CA  1 
ATOM   5327 C C   . ALA B 1 307 ? 27.43900  26.70900  35.41100  1.000 21.98445 ? 307 ALA B C   1 
ATOM   5328 O O   . ALA B 1 307 ? 27.80000  27.43700  36.34100  1.000 17.65922 ? 307 ALA B O   1 
ATOM   5329 C CB  . ALA B 1 307 ? 26.82100  24.31200  35.85000  1.000 15.98612 ? 307 ALA B CB  1 
ATOM   5330 N N   . ALA B 1 308 ? 28.02000  26.75200  34.20700  1.000 22.77652 ? 308 ALA B N   1 
ATOM   5331 C CA  . ALA B 1 308 ? 29.14100  27.65500  33.96000  1.000 24.15188 ? 308 ALA B CA  1 
ATOM   5332 C C   . ALA B 1 308 ? 28.70900  29.11200  33.87400  1.000 22.54984 ? 308 ALA B C   1 
ATOM   5333 O O   . ALA B 1 308 ? 29.54500  30.00100  34.05800  1.000 29.21545 ? 308 ALA B O   1 
ATOM   5334 C CB  . ALA B 1 308 ? 29.87200  27.25600  32.68300  1.000 21.92210 ? 308 ALA B CB  1 
ATOM   5335 N N   . ARG B 1 309 ? 27.43400  29.38200  33.59300  1.000 21.79376 ? 309 ARG B N   1 
ATOM   5336 C CA  . ARG B 1 309 ? 26.95100  30.75800  33.63100  1.000 24.76807 ? 309 ARG B CA  1 
ATOM   5337 C C   . ARG B 1 309 ? 26.75000  31.24800  35.05900  1.000 24.74497 ? 309 ARG B C   1 
ATOM   5338 O O   . ARG B 1 309 ? 26.98700  32.42700  35.34500  1.000 22.50407 ? 309 ARG B O   1 
ATOM   5339 C CB  . ARG B 1 309 ? 25.64100  30.88600  32.85000  1.000 28.80645 ? 309 ARG B CB  1 
ATOM   5340 C CG  . ARG B 1 309 ? 25.22700  32.32300  32.56600  1.000 37.84729 ? 309 ARG B CG  1 
ATOM   5341 C CD  . ARG B 1 309 ? 23.95400  32.39200  31.73300  1.000 49.33236 ? 309 ARG B CD  1 
ATOM   5342 N NE  . ARG B 1 309 ? 22.75100  32.28500  32.55000  1.000 51.63847 ? 309 ARG B NE  1 
ATOM   5343 C CZ  . ARG B 1 309 ? 22.09500  33.32100  33.06000  1.000 49.01401 ? 309 ARG B CZ  1 
ATOM   5344 N NH1 . ARG B 1 309 ? 22.49800  34.56500  32.85100  1.000 51.14749 ? 309 ARG B NH1 1 
ATOM   5345 N NH2 . ARG B 1 309 ? 21.00700  33.10200  33.79500  1.000 42.94400 ? 309 ARG B NH2 1 
ATOM   5346 N N   . GLN B 1 310 ? 26.33100  30.36500  35.96500  1.000 21.93771 ? 310 GLN B N   1 
ATOM   5347 C CA  . GLN B 1 310 ? 26.04800  30.76500  37.33500  1.000 21.01519 ? 310 GLN B CA  1 
ATOM   5348 C C   . GLN B 1 310 ? 27.24800  30.64500  38.26600  1.000 18.89645 ? 310 GLN B C   1 
ATOM   5349 O O   . GLN B 1 310 ? 27.24200  31.25300  39.34000  1.000 21.19642 ? 310 GLN B O   1 
ATOM   5350 C CB  . GLN B 1 310 ? 24.88500  29.93300  37.88700  1.000 18.15819 ? 310 GLN B CB  1 
ATOM   5351 C CG  . GLN B 1 310 ? 23.59500  30.13200  37.11000  1.000 23.95097 ? 310 GLN B CG  1 
ATOM   5352 C CD  . GLN B 1 310 ? 22.41900  29.34800  37.67400  1.000 21.98904 ? 310 GLN B CD  1 
ATOM   5353 O OE1 . GLN B 1 310 ? 21.26700  29.77400  37.56200  1.000 20.83734 ? 310 GLN B OE1 1 
ATOM   5354 N NE2 . GLN B 1 310 ? 22.70100  28.19700  38.27100  1.000 19.63559 ? 310 GLN B NE2 1 
ATOM   5355 N N   . GLN B 1 311 ? 28.27600  29.89500  37.89000  1.000 18.77590 ? 311 GLN B N   1 
ATOM   5356 C CA  . GLN B 1 311 ? 29.35400  29.56600  38.80700  1.000 21.82802 ? 311 GLN B CA  1 
ATOM   5357 C C   . GLN B 1 311 ? 30.70200  29.87900  38.17800  1.000 20.49299 ? 311 GLN B C   1 
ATOM   5358 O O   . GLN B 1 311 ? 30.92500  29.61500  36.99500  1.000 20.27979 ? 311 GLN B O   1 
ATOM   5359 C CB  . GLN B 1 311 ? 29.30000  28.07800  39.21400  1.000 20.72333 ? 311 GLN B CB  1 
ATOM   5360 C CG  . GLN B 1 311 ? 27.91400  27.59700  39.60700  1.000 17.89753 ? 311 GLN B CG  1 
ATOM   5361 C CD  . GLN B 1 311 ? 27.78500  26.09400  39.57600  1.000 17.61672 ? 311 GLN B CD  1 
ATOM   5362 O OE1 . GLN B 1 311 ? 26.67600  25.55700  39.53900  1.000 20.16202 ? 311 GLN B OE1 1 
ATOM   5363 N NE2 . GLN B 1 311 ? 28.91800  25.40000  39.59500  1.000 16.36894 ? 311 GLN B NE2 1 
ATOM   5364 N N   . ARG B 1 312 ? 31.60700  30.42600  38.98700  1.000 24.08558 ? 312 ARG B N   1 
ATOM   5365 C CA  . ARG B 1 312 ? 32.97400  30.62800  38.52500  1.000 25.12179 ? 312 ARG B CA  1 
ATOM   5366 C C   . ARG B 1 312 ? 33.66000  29.29800  38.24000  1.000 26.06155 ? 312 ARG B C   1 
ATOM   5367 O O   . ARG B 1 312 ? 34.43300  29.18300  37.28300  1.000 28.41881 ? 312 ARG B O   1 
ATOM   5368 C CB  . ARG B 1 312 ? 33.76100  31.42800  39.56100  1.000 24.64351 ? 312 ARG B CB  1 
ATOM   5369 C CG  . ARG B 1 312 ? 34.64900  32.49800  38.95900  1.000 39.19342 ? 312 ARG B CG  1 
ATOM   5370 C CD  . ARG B 1 312 ? 36.05900  32.40100  39.50000  1.000 40.45881 ? 312 ARG B CD  1 
ATOM   5371 N NE  . ARG B 1 312 ? 36.08300  32.41500  40.95700  1.000 36.56503 ? 312 ARG B NE  1 
ATOM   5372 C CZ  . ARG B 1 312 ? 37.06100  31.89300  41.68500  1.000 37.48966 ? 312 ARG B CZ  1 
ATOM   5373 N NH1 . ARG B 1 312 ? 38.10500  31.30600  41.12000  1.000 35.03812 ? 312 ARG B NH1 1 
ATOM   5374 N NH2 . ARG B 1 312 ? 36.98500  31.95000  43.01200  1.000 38.06412 ? 312 ARG B NH2 1 
ATOM   5375 N N   . LEU B 1 313 ? 33.40300  28.29000  39.06200  1.000 22.66438 ? 313 LEU B N   1 
ATOM   5376 C CA  . LEU B 1 313 ? 33.98800  26.96600  38.93400  1.000 23.63850 ? 313 LEU B CA  1 
ATOM   5377 C C   . LEU B 1 313 ? 32.90200  25.91700  39.11400  1.000 21.28459 ? 313 LEU B C   1 
ATOM   5378 O O   . LEU B 1 313 ? 31.83700  26.20600  39.66800  1.000 20.65581 ? 313 LEU B O   1 
ATOM   5379 C CB  . LEU B 1 313 ? 35.10800  26.75000  39.96500  1.000 25.70147 ? 313 LEU B CB  1 
ATOM   5380 C CG  . LEU B 1 313 ? 36.37700  27.57300  39.74200  1.000 27.82978 ? 313 LEU B CG  1 
ATOM   5381 C CD1 . LEU B 1 313 ? 37.29100  27.49200  40.95600  1.000 27.50964 ? 313 LEU B CD1 1 
ATOM   5382 C CD2 . LEU B 1 313 ? 37.10700  27.10000  38.49100  1.000 27.37127 ? 313 LEU B CD2 1 
ATOM   5383 N N   . PRO B 1 314 ? 33.12900  24.69300  38.62600  1.000 23.51028 ? 314 PRO B N   1 
ATOM   5384 C CA  . PRO B 1 314 ? 32.07500  23.66200  38.71000  1.000 22.47932 ? 314 PRO B CA  1 
ATOM   5385 C C   . PRO B 1 314 ? 31.64300  23.30900  40.12500  1.000 21.80765 ? 314 PRO B C   1 
ATOM   5386 O O   . PRO B 1 314 ? 30.49100  22.90000  40.32300  1.000 17.83273 ? 314 PRO B O   1 
ATOM   5387 C CB  . PRO B 1 314 ? 32.72000  22.45300  38.01600  1.000 17.75394 ? 314 PRO B CB  1 
ATOM   5388 C CG  . PRO B 1 314 ? 33.72400  23.04100  37.09700  1.000 22.07744 ? 314 PRO B CG  1 
ATOM   5389 C CD  . PRO B 1 314 ? 34.26700  24.25000  37.80100  1.000 20.80525 ? 314 PRO B CD  1 
ATOM   5390 N N   . GLY B 1 315 ? 32.52300  23.43900  41.10900  1.000 19.63041 ? 315 GLY B N   1 
ATOM   5391 C CA  . GLY B 1 315 ? 32.31100  22.86700  42.42300  1.000 15.56521 ? 315 GLY B CA  1 
ATOM   5392 C C   . GLY B 1 315 ? 33.26400  21.70800  42.66000  1.000 17.11173 ? 315 GLY B C   1 
ATOM   5393 O O   . GLY B 1 315 ? 34.13500  21.40200  41.84400  1.000 17.65183 ? 315 GLY B O   1 
ATOM   5394 N N   . ALA B 1 316 ? 33.08500  21.05700  43.80800  1.000 17.67472 ? 316 ALA B N   1 
ATOM   5395 C CA  . ALA B 1 316 ? 34.00600  19.99700  44.19800  1.000 19.50119 ? 316 ALA B CA  1 
ATOM   5396 C C   . ALA B 1 316 ? 33.29800  18.76800  44.75000  1.000 17.91628 ? 316 ALA B C   1 
ATOM   5397 O O   . ALA B 1 316 ? 33.95800  17.91000  45.35200  1.000 20.83362 ? 316 ALA B O   1 
ATOM   5398 C CB  . ALA B 1 316 ? 35.02400  20.51300  45.22100  1.000 17.83510 ? 316 ALA B CB  1 
ATOM   5399 N N   . ILE B 1 317 ? 31.98600  18.65800  44.57800  1.000 20.56502 ? 317 ILE B N   1 
ATOM   5400 C CA  . ILE B 1 317 ? 31.22900  17.46400  44.93200  1.000 19.94902 ? 317 ILE B CA  1 
ATOM   5401 C C   . ILE B 1 317 ? 30.88800  16.72600  43.64400  1.000 22.97316 ? 317 ILE B C   1 
ATOM   5402 O O   . ILE B 1 317 ? 30.50100  17.34800  42.64800  1.000 20.41293 ? 317 ILE B O   1 
ATOM   5403 C CB  . ILE B 1 317 ? 29.95800  17.81500  45.72200  1.000 18.60887 ? 317 ILE B CB  1 
ATOM   5404 C CG1 . ILE B 1 317 ? 30.33500  18.34500  47.10700  1.000 18.57946 ? 317 ILE B CG1 1 
ATOM   5405 C CG2 . ILE B 1 317 ? 29.03800  16.59700  45.83600  1.000 17.90408 ? 317 ILE B CG2 1 
ATOM   5406 C CD1 . ILE B 1 317 ? 29.26900  19.21100  47.73500  1.000 18.11724 ? 317 ILE B CD1 1 
ATOM   5407 N N   . LEU B 1 318 ? 31.05900  15.40600  43.65100  1.000 21.33473 ? 318 LEU B N   1 
ATOM   5408 C CA  . LEU B 1 318 ? 30.65700  14.59100  42.51900  1.000 19.02508 ? 318 LEU B CA  1 
ATOM   5409 C C   . LEU B 1 318 ? 30.05900  13.29100  43.02700  1.000 21.40475 ? 318 LEU B C   1 
ATOM   5410 O O   . LEU B 1 318 ? 30.35100  12.83500  44.13600  1.000 23.73974 ? 318 LEU B O   1 
ATOM   5411 C CB  . LEU B 1 318 ? 31.83500  14.30400  41.57300  1.000 14.91962 ? 318 LEU B CB  1 
ATOM   5412 C CG  . LEU B 1 318 ? 33.05000  13.56900  42.13700  1.000 15.96379 ? 318 LEU B CG  1 
ATOM   5413 C CD1 . LEU B 1 318 ? 32.88700  12.05400  42.03800  1.000 14.85107 ? 318 LEU B CD1 1 
ATOM   5414 C CD2 . LEU B 1 318 ? 34.31500  14.02000  41.43200  1.000 18.23503 ? 318 LEU B CD2 1 
ATOM   5415 N N   . SER B 1 319 ? 29.22000  12.69400  42.19100  1.000 20.04709 ? 319 SER B N   1 
ATOM   5416 C CA  . SER B 1 319 ? 28.72900  11.34700  42.41000  1.000 18.23184 ? 319 SER B CA  1 
ATOM   5417 C C   . SER B 1 319 ? 29.03700  10.51000  41.17700  1.000 24.00936 ? 319 SER B C   1 
ATOM   5418 O O   . SER B 1 319 ? 29.32200  11.04000  40.09800  1.000 23.25407 ? 319 SER B O   1 
ATOM   5419 C CB  . SER B 1 319 ? 27.23300  11.34300  42.70800  1.000 21.01917 ? 319 SER B CB  1 
ATOM   5420 O OG  . SER B 1 319 ? 26.97500  11.99200  43.93900  1.000 20.85835 ? 319 SER B OG  1 
ATOM   5421 N N   . PHE B 1 320 ? 29.00900  9.19100   41.34700  1.000 20.68753 ? 320 PHE B N   1 
ATOM   5422 C CA  . PHE B 1 320 ? 29.17500  8.31000   40.20300  1.000 21.84768 ? 320 PHE B CA  1 
ATOM   5423 C C   . PHE B 1 320 ? 28.47700  6.98200   40.46000  1.000 22.09594 ? 320 PHE B C   1 
ATOM   5424 O O   . PHE B 1 320 ? 28.50300  6.45700   41.57700  1.000 20.17189 ? 320 PHE B O   1 
ATOM   5425 C CB  . PHE B 1 320 ? 30.65900  8.09500   39.86300  1.000 21.74571 ? 320 PHE B CB  1 
ATOM   5426 C CG  . PHE B 1 320 ? 31.44900  7.41400   40.94300  1.000 23.79358 ? 320 PHE B CG  1 
ATOM   5427 C CD1 . PHE B 1 320 ? 31.96600  8.13900   42.00600  1.000 22.45925 ? 320 PHE B CD1 1 
ATOM   5428 C CD2 . PHE B 1 320 ? 31.69700  6.05200   40.88300  1.000 23.76358 ? 320 PHE B CD2 1 
ATOM   5429 C CE1 . PHE B 1 320 ? 32.70200  7.51800   42.99800  1.000 19.79065 ? 320 PHE B CE1 1 
ATOM   5430 C CE2 . PHE B 1 320 ? 32.43300  5.42200   41.87000  1.000 23.91991 ? 320 PHE B CE2 1 
ATOM   5431 C CZ  . PHE B 1 320 ? 32.93600  6.15700   42.93100  1.000 27.58801 ? 320 PHE B CZ  1 
ATOM   5432 N N   . ASP B 1 321 ? 27.83900  6.45600   39.41900  1.000 24.18993 ? 321 ASP B N   1 
ATOM   5433 C CA  . ASP B 1 321 ? 27.22300  5.13800   39.47400  1.000 24.90550 ? 321 ASP B CA  1 
ATOM   5434 C C   . ASP B 1 321 ? 28.26200  4.08000   39.13900  1.000 21.25643 ? 321 ASP B C   1 
ATOM   5435 O O   . ASP B 1 321 ? 29.02200  4.23000   38.17800  1.000 23.56482 ? 321 ASP B O   1 
ATOM   5436 C CB  . ASP B 1 321 ? 26.04700  5.04100   38.50200  1.000 22.47418 ? 321 ASP B CB  1 
ATOM   5437 C CG  . ASP B 1 321 ? 24.89400  5.92700   38.89600  1.000 23.63643 ? 321 ASP B CG  1 
ATOM   5438 O OD1 . ASP B 1 321 ? 24.57900  5.98600   40.10500  1.000 26.02597 ? 321 ASP B OD1 1 
ATOM   5439 O OD2 . ASP B 1 321 ? 24.30900  6.57500   38.00000  1.000 22.76536 ? 321 ASP B OD2 1 
ATOM   5440 N N   . LEU B 1 322 ? 28.30200  3.02500   39.94400  1.000 22.70262 ? 322 LEU B N   1 
ATOM   5441 C CA  . LEU B 1 322 ? 29.11900  1.85700   39.65600  1.000 23.88374 ? 322 LEU B CA  1 
ATOM   5442 C C   . LEU B 1 322 ? 28.28200  0.80600   38.94000  1.000 27.19989 ? 322 LEU B C   1 
ATOM   5443 O O   . LEU B 1 322 ? 27.10900  0.59900   39.27200  1.000 25.94812 ? 322 LEU B O   1 
ATOM   5444 C CB  . LEU B 1 322 ? 29.68700  1.26300   40.94500  1.000 23.82219 ? 322 LEU B CB  1 
ATOM   5445 C CG  . LEU B 1 322 ? 30.91400  1.94500   41.53600  1.000 24.48922 ? 322 LEU B CG  1 
ATOM   5446 C CD1 . LEU B 1 322 ? 31.18500  1.41600   42.92800  1.000 30.26263 ? 322 LEU B CD1 1 
ATOM   5447 C CD2 . LEU B 1 322 ? 32.10500  1.70400   40.64100  1.000 20.92701 ? 322 LEU B CD2 1 
ATOM   5448 N N   . HIS B 1 323 ? 28.88500  0.14700   37.95100  1.000 28.65880 ? 323 HIS B N   1 
ATOM   5449 C CA  . HIS B 1 323 ? 28.25900  -1.04800  37.40100  1.000 26.57003 ? 323 HIS B CA  1 
ATOM   5450 C C   . HIS B 1 323 ? 28.14600  -2.08300  38.50500  1.000 26.59549 ? 323 HIS B C   1 
ATOM   5451 O O   . HIS B 1 323 ? 29.14700  -2.46800  39.11800  1.000 30.80417 ? 323 HIS B O   1 
ATOM   5452 C CB  . HIS B 1 323 ? 29.05700  -1.59800  36.22300  1.000 25.42336 ? 323 HIS B CB  1 
ATOM   5453 C CG  . HIS B 1 323 ? 28.90700  -0.80300  34.96300  1.000 22.16977 ? 323 HIS B CG  1 
ATOM   5454 N ND1 . HIS B 1 323 ? 27.69700  -0.64200  34.32500  1.000 23.46939 ? 323 HIS B ND1 1 
ATOM   5455 C CD2 . HIS B 1 323 ? 29.81800  -0.13400  34.21700  1.000 24.69585 ? 323 HIS B CD2 1 
ATOM   5456 C CE1 . HIS B 1 323 ? 27.86800  0.09400   33.24100  1.000 22.38526 ? 323 HIS B CE1 1 
ATOM   5457 N NE2 . HIS B 1 323 ? 29.14600  0.41600   33.15200  1.000 25.90370 ? 323 HIS B NE2 1 
ATOM   5458 N N   . GLY B 1 324 ? 26.93100  -2.52000  38.76500  1.000 28.74103 ? 324 GLY B N   1 
ATOM   5459 C CA  . GLY B 1 324 ? 26.61800  -3.24700  39.97500  1.000 29.68342 ? 324 GLY B CA  1 
ATOM   5460 C C   . GLY B 1 324 ? 25.73300  -2.40800  40.87800  1.000 32.77751 ? 324 GLY B C   1 
ATOM   5461 O O   . GLY B 1 324 ? 25.34200  -1.28400  40.55700  1.000 36.09327 ? 324 GLY B O   1 
ATOM   5462 N N   . GLY B 1 325 ? 25.41600  -2.97900  42.02600  1.000 28.11980 ? 325 GLY B N   1 
ATOM   5463 C CA  . GLY B 1 325 ? 24.49400  -2.29800  42.90200  1.000 32.95533 ? 325 GLY B CA  1 
ATOM   5464 C C   . GLY B 1 325 ? 25.12700  -1.93000  44.22000  1.000 30.77852 ? 325 GLY B C   1 
ATOM   5465 O O   . GLY B 1 325 ? 26.26900  -1.46100  44.27000  1.000 26.49540 ? 325 GLY B O   1 
ATOM   5466 N N   . GLN B 1 326 ? 24.38200  -2.15700  45.29800  1.000 27.67473 ? 326 GLN B N   1 
ATOM   5467 C CA  . GLN B 1 326 ? 24.89300  -1.84000  46.62000  1.000 27.47683 ? 326 GLN B CA  1 
ATOM   5468 C C   . GLN B 1 326 ? 26.13100  -2.66100  46.94100  1.000 30.89709 ? 326 GLN B C   1 
ATOM   5469 O O   . GLN B 1 326 ? 27.07500  -2.15700  47.56300  1.000 28.17686 ? 326 GLN B O   1 
ATOM   5470 C CB  . GLN B 1 326 ? 23.80800  -2.07300  47.66200  1.000 30.37691 ? 326 GLN B CB  1 
ATOM   5471 C CG  . GLN B 1 326 ? 24.28700  -1.87900  49.07100  1.000 29.52162 ? 326 GLN B CG  1 
ATOM   5472 C CD  . GLN B 1 326 ? 23.14700  -1.86300  50.04200  1.000 31.28813 ? 326 GLN B CD  1 
ATOM   5473 O OE1 . GLN B 1 326 ? 23.05600  -2.72200  50.91500  1.000 38.24814 ? 326 GLN B OE1 1 
ATOM   5474 N NE2 . GLN B 1 326 ? 22.25600  -0.88800  49.89400  1.000 33.23312 ? 326 GLN B NE2 1 
ATOM   5475 N N   . LYS B 1 327 ? 26.15000  -3.92700  46.51500  1.000 28.33635 ? 327 LYS B N   1 
ATOM   5476 C CA  . LYS B 1 327 ? 27.28900  -4.78500  46.81900  1.000 30.07603 ? 327 LYS B CA  1 
ATOM   5477 C C   . LYS B 1 327 ? 28.57400  -4.21500  46.23200  1.000 29.53095 ? 327 LYS B C   1 
ATOM   5478 O O   . LYS B 1 327 ? 29.62400  -4.22600  46.88500  1.000 30.26058 ? 327 LYS B O   1 
ATOM   5479 C CB  . LYS B 1 327 ? 27.03600  -6.19600  46.28700  1.000 35.77293 ? 327 LYS B CB  1 
ATOM   5480 C CG  . LYS B 1 327 ? 27.39600  -7.32100  47.25800  1.000 45.73955 ? 327 LYS B CG  1 
ATOM   5481 C CD  . LYS B 1 327 ? 28.86200  -7.28200  47.68300  1.000 43.86044 ? 327 LYS B CD  1 
ATOM   5482 C CE  . LYS B 1 327 ? 29.01400  -6.89400  49.15800  1.000 43.35492 ? 327 LYS B CE  1 
ATOM   5483 N NZ  . LYS B 1 327 ? 29.62100  -5.54300  49.35500  1.000 27.26913 ? 327 LYS B NZ  1 
ATOM   5484 N N   . ALA B 1 328 ? 28.51200  -3.71800  44.99600  1.000 24.69288 ? 328 ALA B N   1 
ATOM   5485 C CA  . ALA B 1 328 ? 29.69100  -3.12800  44.37100  1.000 27.97632 ? 328 ALA B CA  1 
ATOM   5486 C C   . ALA B 1 328 ? 30.12600  -1.85300  45.08700  1.000 21.85897 ? 328 ALA B C   1 
ATOM   5487 O O   . ALA B 1 328 ? 31.32100  -1.64700  45.32600  1.000 21.67091 ? 328 ALA B O   1 
ATOM   5488 C CB  . ALA B 1 328 ? 29.41000  -2.85000  42.89500  1.000 27.92448 ? 328 ALA B CB  1 
ATOM   5489 N N   . ALA B 1 329 ? 29.17000  -0.99100  45.43900  1.000 24.06794 ? 329 ALA B N   1 
ATOM   5490 C CA  . ALA B 1 329 ? 29.50500  0.23800   46.15100  1.000 22.80960 ? 329 ALA B CA  1 
ATOM   5491 C C   . ALA B 1 329 ? 30.13700  -0.06000  47.50600  1.000 26.82282 ? 329 ALA B C   1 
ATOM   5492 O O   . ALA B 1 329 ? 31.13700  0.56400   47.88200  1.000 25.97858 ? 329 ALA B O   1 
ATOM   5493 C CB  . ALA B 1 329 ? 28.25500  1.10000   46.31700  1.000 18.85502 ? 329 ALA B CB  1 
ATOM   5494 N N   . TRP B 1 330 ? 29.57800  -1.02500  48.24800  1.000 27.71159 ? 330 TRP B N   1 
ATOM   5495 C CA  . TRP B 1 330 ? 30.10000  -1.33500  49.57500  1.000 24.30555 ? 330 TRP B CA  1 
ATOM   5496 C C   . TRP B 1 330 ? 31.46700  -1.99900  49.49100  1.000 26.10016 ? 330 TRP B C   1 
ATOM   5497 O O   . TRP B 1 330 ? 32.35700  -1.70700  50.29900  1.000 27.50462 ? 330 TRP B O   1 
ATOM   5498 C CB  . TRP B 1 330 ? 29.11400  -2.21300  50.34200  1.000 24.21071 ? 330 TRP B CB  1 
ATOM   5499 C CG  . TRP B 1 330 ? 27.90500  -1.47000  50.82300  1.000 24.76396 ? 330 TRP B CG  1 
ATOM   5500 C CD1 . TRP B 1 330 ? 27.48000  -0.23800  50.41200  1.000 25.25721 ? 330 TRP B CD1 1 
ATOM   5501 C CD2 . TRP B 1 330 ? 26.97200  -1.90100  51.82200  1.000 27.00192 ? 330 TRP B CD2 1 
ATOM   5502 N NE1 . TRP B 1 330 ? 26.33500  0.12000   51.08500  1.000 24.09690 ? 330 TRP B NE1 1 
ATOM   5503 C CE2 . TRP B 1 330 ? 26.00500  -0.88200  51.96000  1.000 25.56563 ? 330 TRP B CE2 1 
ATOM   5504 C CE3 . TRP B 1 330 ? 26.86000  -3.05200  52.61300  1.000 25.65447 ? 330 TRP B CE3 1 
ATOM   5505 C CZ2 . TRP B 1 330 ? 24.93400  -0.98200  52.85200  1.000 27.54917 ? 330 TRP B CZ2 1 
ATOM   5506 C CZ3 . TRP B 1 330 ? 25.79900  -3.14700  53.50100  1.000 23.14782 ? 330 TRP B CZ3 1 
ATOM   5507 C CH2 . TRP B 1 330 ? 24.85200  -2.11800  53.61400  1.000 26.68030 ? 330 TRP B CH2 1 
ATOM   5508 N N   . ALA B 1 331 ? 31.65800  -2.89800  48.52500  1.000 26.98164 ? 331 ALA B N   1 
ATOM   5509 C CA  . ALA B 1 331 ? 32.98800  -3.45400  48.31300  1.000 26.82675 ? 331 ALA B CA  1 
ATOM   5510 C C   . ALA B 1 331 ? 33.98000  -2.35300  47.96800  1.000 23.80684 ? 331 ALA B C   1 
ATOM   5511 O O   . ALA B 1 331 ? 35.14700  -2.40400  48.37300  1.000 21.00622 ? 331 ALA B O   1 
ATOM   5512 C CB  . ALA B 1 331 ? 32.94800  -4.50700  47.20500  1.000 25.25786 ? 331 ALA B CB  1 
ATOM   5513 N N   . PHE B 1 332 ? 33.52600  -1.34700  47.22100  1.000 22.83322 ? 332 PHE B N   1 
ATOM   5514 C CA  . PHE B 1 332 ? 34.39600  -0.24300  46.83500  1.000 26.57360 ? 332 PHE B CA  1 
ATOM   5515 C C   . PHE B 1 332 ? 34.84800  0.56100   48.05100  1.000 23.94399 ? 332 PHE B C   1 
ATOM   5516 O O   . PHE B 1 332 ? 36.04700  0.79400   48.24100  1.000 23.53290 ? 332 PHE B O   1 
ATOM   5517 C CB  . PHE B 1 332 ? 33.66900  0.65100   45.83000  1.000 23.38301 ? 332 PHE B CB  1 
ATOM   5518 C CG  . PHE B 1 332 ? 34.50100  1.77900   45.29800  1.000 24.18291 ? 332 PHE B CG  1 
ATOM   5519 C CD1 . PHE B 1 332 ? 34.56000  2.99600   45.96600  1.000 27.48182 ? 332 PHE B CD1 1 
ATOM   5520 C CD2 . PHE B 1 332 ? 35.20900  1.63300   44.11800  1.000 22.97474 ? 332 PHE B CD2 1 
ATOM   5521 C CE1 . PHE B 1 332 ? 35.32600  4.04100   45.47700  1.000 21.58201 ? 332 PHE B CE1 1 
ATOM   5522 C CE2 . PHE B 1 332 ? 35.97700  2.67200   43.62300  1.000 26.79310 ? 332 PHE B CE2 1 
ATOM   5523 C CZ  . PHE B 1 332 ? 36.03400  3.88100   44.30300  1.000 23.56816 ? 332 PHE B CZ  1 
ATOM   5524 N N   . VAL B 1 333 ? 33.90200  1.01100   48.88300  1.000 20.72455 ? 333 VAL B N   1 
ATOM   5525 C CA  . VAL B 1 333 ? 34.30500  1.90000   49.96900  1.000 23.94280 ? 333 VAL B CA  1 
ATOM   5526 C C   . VAL B 1 333 ? 35.06100  1.13100   51.04300  1.000 24.47390 ? 333 VAL B C   1 
ATOM   5527 O O   . VAL B 1 333 ? 35.98800  1.67200   51.65500  1.000 26.57181 ? 333 VAL B O   1 
ATOM   5528 C CB  . VAL B 1 333 ? 33.10600  2.67700   50.56100  1.000 24.32903 ? 333 VAL B CB  1 
ATOM   5529 C CG1 . VAL B 1 333 ? 32.17800  3.18300   49.46600  1.000 22.11657 ? 333 VAL B CG1 1 
ATOM   5530 C CG2 . VAL B 1 333 ? 32.35700  1.86800   51.57300  1.000 20.59070 ? 333 VAL B CG2 1 
ATOM   5531 N N   . ASP B 1 334 ? 34.71200  -0.14300  51.27100  1.000 24.48773 ? 334 ASP B N   1 
ATOM   5532 C CA  . ASP B 1 334 ? 35.34500  -0.90400  52.34200  1.000 20.48085 ? 334 ASP B CA  1 
ATOM   5533 C C   . ASP B 1 334 ? 36.83000  -1.13400  52.09900  1.000 22.51763 ? 334 ASP B C   1 
ATOM   5534 O O   . ASP B 1 334 ? 37.56000  -1.42800  53.05100  1.000 27.19542 ? 334 ASP B O   1 
ATOM   5535 C CB  . ASP B 1 334 ? 34.63600  -2.24700  52.53200  1.000 25.57311 ? 334 ASP B CB  1 
ATOM   5536 C CG  . ASP B 1 334 ? 33.29400  -2.10600  53.23400  1.000 26.13746 ? 334 ASP B CG  1 
ATOM   5537 O OD1 . ASP B 1 334 ? 32.92100  -0.96700  53.58400  1.000 23.74490 ? 334 ASP B OD1 1 
ATOM   5538 O OD2 . ASP B 1 334 ? 32.60900  -3.13300  53.43500  1.000 29.69621 ? 334 ASP B OD2 1 
ATOM   5539 N N   . ALA B 1 335 ? 37.29500  -1.01200  50.85900  1.000 22.48990 ? 335 ALA B N   1 
ATOM   5540 C CA  . ALA B 1 335 ? 38.70800  -1.19300  50.56500  1.000 21.82780 ? 335 ALA B CA  1 
ATOM   5541 C C   . ALA B 1 335 ? 39.50400  0.10400   50.65300  1.000 23.02879 ? 335 ALA B C   1 
ATOM   5542 O O   . ALA B 1 335 ? 40.73800  0.06000   50.61700  1.000 27.70314 ? 335 ALA B O   1 
ATOM   5543 C CB  . ALA B 1 335 ? 38.87900  -1.80800  49.17200  1.000 27.47311 ? 335 ALA B CB  1 
ATOM   5544 N N   . LEU B 1 336 ? 38.83700  1.24600   50.77300  1.000 24.09438 ? 336 LEU B N   1 
ATOM   5545 C CA  . LEU B 1 336 ? 39.53500  2.51900   50.87000  1.000 23.42201 ? 336 LEU B CA  1 
ATOM   5546 C C   . LEU B 1 336 ? 40.23900  2.63400   52.21600  1.000 23.24566 ? 336 LEU B C   1 
ATOM   5547 O O   . LEU B 1 336 ? 39.69900  2.23800   53.25200  1.000 25.79524 ? 336 LEU B O   1 
ATOM   5548 C CB  . LEU B 1 336 ? 38.55000  3.67200   50.68900  1.000 23.39351 ? 336 LEU B CB  1 
ATOM   5549 C CG  . LEU B 1 336 ? 37.67400  3.61100   49.43700  1.000 21.98034 ? 336 LEU B CG  1 
ATOM   5550 C CD1 . LEU B 1 336 ? 36.68000  4.75400   49.41600  1.000 18.58413 ? 336 LEU B CD1 1 
ATOM   5551 C CD2 . LEU B 1 336 ? 38.53200  3.62700   48.18200  1.000 22.81523 ? 336 LEU B CD2 1 
ATOM   5552 N N   . ARG B 1 337 ? 41.46000  3.16500   52.19400  1.000 25.09257 ? 337 ARG B N   1 
ATOM   5553 C CA  . ARG B 1 337 ? 42.21000  3.43800   53.41200  1.000 29.41035 ? 337 ARG B CA  1 
ATOM   5554 C C   . ARG B 1 337 ? 42.47500  4.91700   53.65000  1.000 25.17036 ? 337 ARG B C   1 
ATOM   5555 O O   . ARG B 1 337 ? 42.98500  5.26900   54.72100  1.000 28.75395 ? 337 ARG B O   1 
ATOM   5556 C CB  . ARG B 1 337 ? 43.56100  2.70400   53.40200  1.000 34.19619 ? 337 ARG B CB  1 
ATOM   5557 C CG  . ARG B 1 337 ? 43.49000  1.22000   53.10300  1.000 40.63759 ? 337 ARG B CG  1 
ATOM   5558 C CD  . ARG B 1 337 ? 44.76100  0.52400   53.58200  1.000 55.20245 ? 337 ARG B CD  1 
ATOM   5559 N NE  . ARG B 1 337 ? 44.89200  -0.82400  53.04200  1.000 63.50399 ? 337 ARG B NE  1 
ATOM   5560 C CZ  . ARG B 1 337 ? 45.65900  -1.14500  52.00900  1.000 57.61311 ? 337 ARG B CZ  1 
ATOM   5561 N NH1 . ARG B 1 337 ? 46.40000  -0.24000  51.39000  1.000 58.33917 ? 337 ARG B NH1 1 
ATOM   5562 N NH2 . ARG B 1 337 ? 45.68700  -2.40600  51.58800  1.000 57.78397 ? 337 ARG B NH2 1 
ATOM   5563 N N   . LEU B 1 338 ? 42.16300  5.78800   52.69300  1.000 24.15804 ? 338 LEU B N   1 
ATOM   5564 C CA  . LEU B 1 338 ? 42.44600  7.21300   52.81200  1.000 22.95738 ? 338 LEU B CA  1 
ATOM   5565 C C   . LEU B 1 338 ? 41.19000  8.06200   52.91000  1.000 24.67972 ? 338 LEU B C   1 
ATOM   5566 O O   . LEU B 1 338 ? 41.05600  8.85400   53.84800  1.000 21.00399 ? 338 LEU B O   1 
ATOM   5567 C CB  . LEU B 1 338 ? 43.29400  7.68000   51.62500  1.000 20.95273 ? 338 LEU B CB  1 
ATOM   5568 C CG  . LEU B 1 338 ? 43.73600  9.14200   51.65000  1.000 27.27188 ? 338 LEU B CG  1 
ATOM   5569 C CD1 . LEU B 1 338 ? 44.58400  9.42300   52.87900  1.000 26.82559 ? 338 LEU B CD1 1 
ATOM   5570 C CD2 . LEU B 1 338 ? 44.49600  9.48000   50.37600  1.000 23.05471 ? 338 LEU B CD2 1 
ATOM   5571 N N   . LEU B 1 339 ? 40.25700  7.91600   51.96800  1.000 22.59458 ? 339 LEU B N   1 
ATOM   5572 C CA  . LEU B 1 339 ? 39.06300  8.74800   51.99100  1.000 21.49388 ? 339 LEU B CA  1 
ATOM   5573 C C   . LEU B 1 339 ? 38.27000  8.47900   53.26400  1.000 24.63357 ? 339 LEU B C   1 
ATOM   5574 O O   . LEU B 1 339 ? 38.29700  7.38000   53.82200  1.000 24.90327 ? 339 LEU B O   1 
ATOM   5575 C CB  . LEU B 1 339 ? 38.17100  8.49100   50.76800  1.000 21.88058 ? 339 LEU B CB  1 
ATOM   5576 C CG  . LEU B 1 339 ? 38.67200  8.36400   49.32200  1.000 21.39400 ? 339 LEU B CG  1 
ATOM   5577 C CD1 . LEU B 1 339 ? 37.58400  8.84100   48.37300  1.000 20.43728 ? 339 LEU B CD1 1 
ATOM   5578 C CD2 . LEU B 1 339 ? 39.96300  9.10500   49.04700  1.000 21.88801 ? 339 LEU B CD2 1 
ATOM   5579 N N   . SER B 1 340 ? 37.55900  9.50100   53.72400  1.000 18.89813 ? 340 SER B N   1 
ATOM   5580 C CA  . SER B 1 340 ? 36.77700  9.40800   54.94600  1.000 19.36118 ? 340 SER B CA  1 
ATOM   5581 C C   . SER B 1 340 ? 35.39600  8.84900   54.62900  1.000 20.38838 ? 340 SER B C   1 
ATOM   5582 O O   . SER B 1 340 ? 34.68100  9.39100   53.77800  1.000 20.56678 ? 340 SER B O   1 
ATOM   5583 C CB  . SER B 1 340 ? 36.65800  10.78100  55.60300  1.000 19.67942 ? 340 SER B CB  1 
ATOM   5584 O OG  . SER B 1 340 ? 37.94000  11.33500  55.85500  1.000 18.24334 ? 340 SER B OG  1 
ATOM   5585 N N   . LEU B 1 341 ? 35.02200  7.77300   55.31200  1.000 24.70077 ? 341 LEU B N   1 
ATOM   5586 C CA  . LEU B 1 341 ? 33.65100  7.27100   55.26600  1.000 27.25688 ? 341 LEU B CA  1 
ATOM   5587 C C   . LEU B 1 341 ? 32.84100  8.08000   56.26200  1.000 23.49015 ? 341 LEU B C   1 
ATOM   5588 O O   . LEU B 1 341 ? 32.86600  7.80900   57.46300  1.000 24.01630 ? 341 LEU B O   1 
ATOM   5589 C CB  . LEU B 1 341 ? 33.58700  5.78700   55.60600  1.000 28.27378 ? 341 LEU B CB  1 
ATOM   5590 C CG  . LEU B 1 341 ? 33.86200  4.75000   54.52100  1.000 32.41851 ? 341 LEU B CG  1 
ATOM   5591 C CD1 . LEU B 1 341 ? 35.31100  4.81100   54.05500  1.000 34.55623 ? 341 LEU B CD1 1 
ATOM   5592 C CD2 . LEU B 1 341 ? 33.51400  3.36100   55.04500  1.000 32.45299 ? 341 LEU B CD2 1 
ATOM   5593 N N   . THR B 1 342 ? 32.11800  9.07900   55.76700  1.000 19.11450 ? 342 THR B N   1 
ATOM   5594 C CA  . THR B 1 342 ? 31.36000  9.95200   56.64500  1.000 22.43584 ? 342 THR B CA  1 
ATOM   5595 C C   . THR B 1 342 ? 30.33800  10.70200  55.80800  1.000 19.82861 ? 342 THR B C   1 
ATOM   5596 O O   . THR B 1 342 ? 30.56900  10.98300  54.63000  1.000 25.62216 ? 342 THR B O   1 
ATOM   5597 C CB  . THR B 1 342 ? 32.28300  10.92500  57.39700  1.000 21.50071 ? 342 THR B CB  1 
ATOM   5598 O OG1 . THR B 1 342 ? 31.52700  11.66000  58.36700  1.000 21.17388 ? 342 THR B OG1 1 
ATOM   5599 C CG2 . THR B 1 342 ? 32.94400  11.90100  56.43400  1.000 19.81864 ? 342 THR B CG2 1 
ATOM   5600 N N   . ALA B 1 343 ? 29.19900  11.00700  56.42700  1.000 21.01544 ? 343 ALA B N   1 
ATOM   5601 C CA  . ALA B 1 343 ? 28.12100  11.74700  55.77000  1.000 22.25355 ? 343 ALA B CA  1 
ATOM   5602 C C   . ALA B 1 343 ? 28.37300  13.23600  55.98800  1.000 23.02012 ? 343 ALA B C   1 
ATOM   5603 O O   . ALA B 1 343 ? 27.80700  13.88100  56.87500  1.000 23.89601 ? 343 ALA B O   1 
ATOM   5604 C CB  . ALA B 1 343 ? 26.76200  11.31700  56.30800  1.000 18.16219 ? 343 ALA B CB  1 
ATOM   5605 N N   . ASN B 1 344 ? 29.26100  13.78200  55.16400  1.000 21.18310 ? 344 ASN B N   1 
ATOM   5606 C CA  . ASN B 1 344 ? 29.65100  15.17700  55.29600  1.000 22.82917 ? 344 ASN B CA  1 
ATOM   5607 C C   . ASN B 1 344 ? 30.31400  15.62500  54.00200  1.000 22.87052 ? 344 ASN B C   1 
ATOM   5608 O O   . ASN B 1 344 ? 30.67700  14.81000  53.14800  1.000 19.74712 ? 344 ASN B O   1 
ATOM   5609 C CB  . ASN B 1 344 ? 30.58600  15.38500  56.49500  1.000 20.16147 ? 344 ASN B CB  1 
ATOM   5610 C CG  . ASN B 1 344 ? 30.41700  16.75400  57.12600  1.000 24.50360 ? 344 ASN B CG  1 
ATOM   5611 O OD1 . ASN B 1 344 ? 29.77600  17.63400  56.55200  1.000 21.61302 ? 344 ASN B OD1 1 
ATOM   5612 N ND2 . ASN B 1 344 ? 30.99700  16.94200  58.30700  1.000 22.31915 ? 344 ASN B ND2 1 
ATOM   5613 N N   . LEU B 1 345 ? 30.46900  16.94100  53.87300  1.000 21.69457 ? 345 LEU B N   1 
ATOM   5614 C CA  . LEU B 1 345 ? 31.13400  17.53400  52.72500  1.000 17.60113 ? 345 LEU B CA  1 
ATOM   5615 C C   . LEU B 1 345 ? 31.79100  18.83600  53.16400  1.000 19.03575 ? 345 LEU B C   1 
ATOM   5616 O O   . LEU B 1 345 ? 31.54000  19.34300  54.26100  1.000 17.28451 ? 345 LEU B O   1 
ATOM   5617 C CB  . LEU B 1 345 ? 30.14900  17.75200  51.56900  1.000 18.43782 ? 345 LEU B CB  1 
ATOM   5618 C CG  . LEU B 1 345 ? 28.94000  18.66600  51.76500  1.000 21.17164 ? 345 LEU B CG  1 
ATOM   5619 C CD1 . LEU B 1 345 ? 29.27200  20.09700  51.36500  1.000 19.91489 ? 345 LEU B CD1 1 
ATOM   5620 C CD2 . LEU B 1 345 ? 27.75100  18.15100  50.96800  1.000 20.60800 ? 345 LEU B CD2 1 
ATOM   5621 N N   . GLY B 1 346 ? 32.65400  19.36800  52.29900  1.000 17.60464 ? 346 GLY B N   1 
ATOM   5622 C CA  . GLY B 1 346 ? 33.26500  20.65800  52.55700  1.000 16.91528 ? 346 GLY B CA  1 
ATOM   5623 C C   . GLY B 1 346 ? 34.45200  20.63500  53.48800  1.000 20.32409 ? 346 GLY B C   1 
ATOM   5624 O O   . GLY B 1 346 ? 34.80900  21.68200  54.03900  1.000 16.45415 ? 346 GLY B O   1 
ATOM   5625 N N   . ASP B 1 347 ? 35.05900  19.47700  53.70000  1.000 14.68533 ? 347 ASP B N   1 
ATOM   5626 C CA  . ASP B 1 347 ? 36.25900  19.36400  54.50700  1.000 15.31801 ? 347 ASP B CA  1 
ATOM   5627 C C   . ASP B 1 347 ? 37.48700  19.30100  53.60300  1.000 18.32061 ? 347 ASP B C   1 
ATOM   5628 O O   . ASP B 1 347 ? 37.41000  18.90700  52.43800  1.000 19.41541 ? 347 ASP B O   1 
ATOM   5629 C CB  . ASP B 1 347 ? 36.16900  18.11300  55.38800  1.000 15.49113 ? 347 ASP B CB  1 
ATOM   5630 C CG  . ASP B 1 347 ? 37.11100  18.14900  56.58200  1.000 17.43243 ? 347 ASP B CG  1 
ATOM   5631 O OD1 . ASP B 1 347 ? 38.24700  18.65000  56.44700  1.000 18.36083 ? 347 ASP B OD1 1 
ATOM   5632 O OD2 . ASP B 1 347 ? 36.71300  17.65000  57.66300  1.000 16.44763 ? 347 ASP B OD2 1 
ATOM   5633 N N   . ALA B 1 348 ? 38.63600  19.70200  54.15500  1.000 19.92185 ? 348 ALA B N   1 
ATOM   5634 C CA  . ALA B 1 348 ? 39.90200  19.39100  53.50000  1.000 17.16045 ? 348 ALA B CA  1 
ATOM   5635 C C   . ALA B 1 348 ? 40.08700  17.88700  53.37100  1.000 16.56463 ? 348 ALA B C   1 
ATOM   5636 O O   . ALA B 1 348 ? 40.73500  17.42000  52.42900  1.000 18.34470 ? 348 ALA B O   1 
ATOM   5637 C CB  . ALA B 1 348 ? 41.07300  20.00200  54.27100  1.000 13.78426 ? 348 ALA B CB  1 
ATOM   5638 N N   . LYS B 1 349 ? 39.52400  17.11900  54.30300  1.000 15.53424 ? 349 LYS B N   1 
ATOM   5639 C CA  . LYS B 1 349 ? 39.51100  15.66500  54.20700  1.000 17.55398 ? 349 LYS B CA  1 
ATOM   5640 C C   . LYS B 1 349 ? 38.43700  15.23600  53.21200  1.000 18.28974 ? 349 LYS B C   1 
ATOM   5641 O O   . LYS B 1 349 ? 37.25500  15.55700  53.38900  1.000 15.70823 ? 349 LYS B O   1 
ATOM   5642 C CB  . LYS B 1 349 ? 39.25600  15.04000  55.57600  1.000 17.02179 ? 349 LYS B CB  1 
ATOM   5643 C CG  . LYS B 1 349 ? 40.26100  15.44100  56.65300  1.000 16.28239 ? 349 LYS B CG  1 
ATOM   5644 C CD  . LYS B 1 349 ? 40.05600  14.64700  57.94200  1.000 19.91947 ? 349 LYS B CD  1 
ATOM   5645 C CE  . LYS B 1 349 ? 40.54300  15.41600  59.17200  1.000 19.94987 ? 349 LYS B CE  1 
ATOM   5646 N NZ  . LYS B 1 349 ? 41.89200  16.04100  58.99700  1.000 20.52067 ? 349 LYS B NZ  1 
ATOM   5647 N N   . THR B 1 350 ? 38.85000  14.52400  52.16200  1.000 16.42166 ? 350 THR B N   1 
ATOM   5648 C CA  . THR B 1 350 ? 37.90200  13.98300  51.19300  1.000 16.11888 ? 350 THR B CA  1 
ATOM   5649 C C   . THR B 1 350 ? 36.96000  12.99400  51.87200  1.000 16.21965 ? 350 THR B C   1 
ATOM   5650 O O   . THR B 1 350 ? 37.38900  12.14400  52.65600  1.000 16.17698 ? 350 THR B O   1 
ATOM   5651 C CB  . THR B 1 350 ? 38.65600  13.29600  50.04800  1.000 17.01236 ? 350 THR B CB  1 
ATOM   5652 O OG1 . THR B 1 350 ? 39.43000  14.26500  49.32500  1.000 16.20656 ? 350 THR B OG1 1 
ATOM   5653 C CG2 . THR B 1 350 ? 37.68700  12.60900  49.09000  1.000 15.02140 ? 350 THR B CG2 1 
ATOM   5654 N N   . THR B 1 351 ? 35.67100  13.10900  51.58300  1.000 15.23370 ? 351 THR B N   1 
ATOM   5655 C CA  . THR B 1 351 ? 34.68200  12.22100  52.16500  1.000 16.61316 ? 351 THR B CA  1 
ATOM   5656 C C   . THR B 1 351 ? 33.96400  11.44900  51.07000  1.000 18.52327 ? 351 THR B C   1 
ATOM   5657 O O   . THR B 1 351 ? 33.83300  11.91400  49.93400  1.000 19.12028 ? 351 THR B O   1 
ATOM   5658 C CB  . THR B 1 351 ? 33.64200  12.97400  52.98800  1.000 15.70069 ? 351 THR B CB  1 
ATOM   5659 O OG1 . THR B 1 351 ? 32.70700  13.59500  52.10200  1.000 15.47351 ? 351 THR B OG1 1 
ATOM   5660 C CG2 . THR B 1 351 ? 34.30200  14.03000  53.87100  1.000 13.92573 ? 351 THR B CG2 1 
ATOM   5661 N N   . ILE B 1 352 ? 33.49800  10.25900  51.42600  1.000 16.93521 ? 352 ILE B N   1 
ATOM   5662 C CA  . ILE B 1 352 ? 32.67400  9.46200   50.53100  1.000 21.74159 ? 352 ILE B CA  1 
ATOM   5663 C C   . ILE B 1 352 ? 31.54000  8.86900   51.35300  1.000 21.15343 ? 352 ILE B C   1 
ATOM   5664 O O   . ILE B 1 352 ? 31.69300  8.57300   52.54200  1.000 19.81887 ? 352 ILE B O   1 
ATOM   5665 C CB  . ILE B 1 352 ? 33.49500  8.37000   49.79600  1.000 18.24578 ? 352 ILE B CB  1 
ATOM   5666 C CG1 . ILE B 1 352 ? 32.66000  7.70800   48.69900  1.000 15.83946 ? 352 ILE B CG1 1 
ATOM   5667 C CG2 . ILE B 1 352 ? 34.05300  7.34300   50.78000  1.000 15.64693 ? 352 ILE B CG2 1 
ATOM   5668 C CD1 . ILE B 1 352 ? 33.45600  6.75400   47.84100  1.000 17.48206 ? 352 ILE B CD1 1 
ATOM   5669 N N   . THR B 1 353 ? 30.37900  8.73800   50.72000  1.000 18.46160 ? 353 THR B N   1 
ATOM   5670 C CA  . THR B 1 353 ? 29.23800  8.11800   51.36900  1.000 22.60780 ? 353 THR B CA  1 
ATOM   5671 C C   . THR B 1 353 ? 28.36100  7.47500   50.30300  1.000 22.46612 ? 353 THR B C   1 
ATOM   5672 O O   . THR B 1 353 ? 28.43200  7.81900   49.11900  1.000 19.51953 ? 353 THR B O   1 
ATOM   5673 C CB  . THR B 1 353 ? 28.44700  9.13800   52.18900  1.000 20.13826 ? 353 THR B CB  1 
ATOM   5674 O OG1 . THR B 1 353 ? 27.52900  8.45600   53.05400  1.000 24.39560 ? 353 THR B OG1 1 
ATOM   5675 C CG2 . THR B 1 353 ? 27.68500  10.07300  51.25900  1.000 18.63061 ? 353 THR B CG2 1 
ATOM   5676 N N   . HIS B 1 354 ? 27.53100  6.53000   50.74200  1.000 19.92000 ? 354 HIS B N   1 
ATOM   5677 C CA  . HIS B 1 354 ? 26.63600  5.78600   49.86100  1.000 20.45008 ? 354 HIS B CA  1 
ATOM   5678 C C   . HIS B 1 354 ? 25.21300  6.22200   50.16500  1.000 19.73542 ? 354 HIS B C   1 
ATOM   5679 O O   . HIS B 1 354 ? 24.62000  5.75400   51.14900  1.000 22.21815 ? 354 HIS B O   1 
ATOM   5680 C CB  . HIS B 1 354 ? 26.80300  4.27900   50.08100  1.000 21.37207 ? 354 HIS B CB  1 
ATOM   5681 C CG  . HIS B 1 354 ? 25.87500  3.43300   49.26400  1.000 21.51103 ? 354 HIS B CG  1 
ATOM   5682 N ND1 . HIS B 1 354 ? 24.80200  2.76400   49.81400  1.000 24.16828 ? 354 HIS B ND1 1 
ATOM   5683 C CD2 . HIS B 1 354 ? 25.86900  3.13300   47.94400  1.000 20.12313 ? 354 HIS B CD2 1 
ATOM   5684 C CE1 . HIS B 1 354 ? 24.17100  2.09300   48.86600  1.000 24.17670 ? 354 HIS B CE1 1 
ATOM   5685 N NE2 . HIS B 1 354 ? 24.79700  2.30400   47.72100  1.000 24.09828 ? 354 HIS B NE2 1 
ATOM   5686 N N   . PRO B 1 355 ? 24.63200  7.13500   49.38000  1.000 19.13265 ? 355 PRO B N   1 
ATOM   5687 C CA  . PRO B 1 355 ? 23.37700  7.77400   49.81600  1.000 18.60212 ? 355 PRO B CA  1 
ATOM   5688 C C   . PRO B 1 355 ? 22.21900  6.81200   50.00500  1.000 23.91569 ? 355 PRO B C   1 
ATOM   5689 O O   . PRO B 1 355 ? 21.40400  7.02100   50.91300  1.000 22.92244 ? 355 PRO B O   1 
ATOM   5690 C CB  . PRO B 1 355 ? 23.10200  8.78900   48.70000  1.000 19.20059 ? 355 PRO B CB  1 
ATOM   5691 C CG  . PRO B 1 355 ? 24.44600  9.08600   48.13500  1.000 21.57196 ? 355 PRO B CG  1 
ATOM   5692 C CD  . PRO B 1 355 ? 25.19600  7.78600   48.18600  1.000 19.72563 ? 355 PRO B CD  1 
ATOM   5693 N N   . ALA B 1 356 ? 22.12400  5.76200   49.18000  1.000 23.90686 ? 356 ALA B N   1 
ATOM   5694 C CA  . ALA B 1 356 ? 20.97900  4.85700   49.25700  1.000 26.00215 ? 356 ALA B CA  1 
ATOM   5695 C C   . ALA B 1 356 ? 20.86900  4.20400   50.62700  1.000 27.52610 ? 356 ALA B C   1 
ATOM   5696 O O   . ALA B 1 356 ? 19.75900  3.94000   51.10000  1.000 35.44725 ? 356 ALA B O   1 
ATOM   5697 C CB  . ALA B 1 356 ? 21.07000  3.78800   48.16700  1.000 21.82935 ? 356 ALA B CB  1 
ATOM   5698 N N   . SER B 1 357 ? 21.99800  3.94800   51.28500  1.000 27.87785 ? 357 SER B N   1 
ATOM   5699 C CA  . SER B 1 357 ? 21.98400  3.35400   52.61300  1.000 26.88377 ? 357 SER B CA  1 
ATOM   5700 C C   . SER B 1 357 ? 22.29000  4.33200   53.74000  1.000 26.48522 ? 357 SER B C   1 
ATOM   5701 O O   . SER B 1 357 ? 22.22500  3.92600   54.90700  1.000 28.69254 ? 357 SER B O   1 
ATOM   5702 C CB  . SER B 1 357 ? 22.98600  2.19200   52.69000  1.000 26.15264 ? 357 SER B CB  1 
ATOM   5703 O OG  . SER B 1 357 ? 24.32000  2.67300   52.65300  1.000 23.56224 ? 357 SER B OG  1 
ATOM   5704 N N   . THR B 1 358 ? 22.67900  5.58000   53.45100  1.000 22.34336 ? 358 THR B N   1 
ATOM   5705 C CA  . THR B 1 358 ? 22.92900  6.53200   54.53200  1.000 22.93386 ? 358 THR B CA  1 
ATOM   5706 C C   . THR B 1 358 ? 22.03700  7.76700   54.47300  1.000 25.72972 ? 358 THR B C   1 
ATOM   5707 O O   . THR B 1 358 ? 21.05300  7.83100   55.21100  1.000 28.56990 ? 358 THR B O   1 
ATOM   5708 C CB  . THR B 1 358 ? 24.40100  6.93800   54.49800  1.000 23.46039 ? 358 THR B CB  1 
ATOM   5709 O OG1 . THR B 1 358 ? 24.68200  7.54900   53.23000  1.000 23.17663 ? 358 THR B OG1 1 
ATOM   5710 C CG2 . THR B 1 358 ? 25.30700  5.72400   54.69200  1.000 18.09580 ? 358 THR B CG2 1 
ATOM   5711 N N   . THR B 1 359 ? 22.26200  8.69000   53.53600  1.000 25.42333 ? 359 THR B N   1 
ATOM   5712 C CA  . THR B 1 359 ? 21.58100  9.98000   53.61600  1.000 24.47574 ? 359 THR B CA  1 
ATOM   5713 C C   . THR B 1 359 ? 20.20200  9.95000   52.98500  1.000 27.90842 ? 359 THR B C   1 
ATOM   5714 O O   . THR B 1 359 ? 19.35300  10.77600  53.33400  1.000 25.53181 ? 359 THR B O   1 
ATOM   5715 C CB  . THR B 1 359 ? 22.41100  11.08700  52.95100  1.000 21.22551 ? 359 THR B CB  1 
ATOM   5716 O OG1 . THR B 1 359 ? 22.63900  10.76100  51.57400  1.000 24.32735 ? 359 THR B OG1 1 
ATOM   5717 C CG2 . THR B 1 359 ? 23.74700  11.25100  53.64900  1.000 20.97431 ? 359 THR B CG2 1 
ATOM   5718 N N   . HIS B 1 360 ? 19.96700  9.01800   52.06400  1.000 24.47980 ? 360 HIS B N   1 
ATOM   5719 C CA  . HIS B 1 360 ? 18.66000  8.80200   51.46700  1.000 24.71132 ? 360 HIS B CA  1 
ATOM   5720 C C   . HIS B 1 360 ? 18.06700  7.46600   51.90200  1.000 28.35660 ? 360 HIS B C   1 
ATOM   5721 O O   . HIS B 1 360 ? 17.18000  6.93100   51.22600  1.000 27.85965 ? 360 HIS B O   1 
ATOM   5722 C CB  . HIS B 1 360 ? 18.76800  8.89300   49.94200  1.000 23.98335 ? 360 HIS B CB  1 
ATOM   5723 C CG  . HIS B 1 360 ? 19.19500  10.24300  49.44800  1.000 23.88082 ? 360 HIS B CG  1 
ATOM   5724 N ND1 . HIS B 1 360 ? 20.35100  10.86200  49.87400  1.000 23.33332 ? 360 HIS B ND1 1 
ATOM   5725 C CD2 . HIS B 1 360 ? 18.60900  11.10000  48.57700  1.000 23.27151 ? 360 HIS B CD2 1 
ATOM   5726 C CE1 . HIS B 1 360 ? 20.46100  12.03900  49.28500  1.000 23.77609 ? 360 HIS B CE1 1 
ATOM   5727 N NE2 . HIS B 1 360 ? 19.41700  12.20800  48.49300  1.000 24.29876 ? 360 HIS B NE2 1 
ATOM   5728 N N   . SER B 1 361 ? 18.55200  6.92100   53.02300  1.000 23.80490 ? 361 SER B N   1 
ATOM   5729 C CA  . SER B 1 361 ? 18.12200  5.59700   53.46900  1.000 29.98851 ? 361 SER B CA  1 
ATOM   5730 C C   . SER B 1 361 ? 16.64400  5.58000   53.84300  1.000 30.07743 ? 361 SER B C   1 
ATOM   5731 O O   . SER B 1 361 ? 15.93800  4.60700   53.55800  1.000 37.40308 ? 361 SER B O   1 
ATOM   5732 C CB  . SER B 1 361 ? 18.97700  5.14300   54.65200  1.000 26.93888 ? 361 SER B CB  1 
ATOM   5733 O OG  . SER B 1 361 ? 18.78300  5.99800   55.76600  1.000 33.66607 ? 361 SER B OG  1 
ATOM   5734 N N   . ARG B 1 362 ? 16.16000  6.63900   54.48600  1.000 28.58823 ? 362 ARG B N   1 
ATOM   5735 C CA  . ARG B 1 362 ? 14.76300  6.73200   54.89100  1.000 32.40204 ? 362 ARG B CA  1 
ATOM   5736 C C   . ARG B 1 362 ? 13.86400  7.26700   53.78500  1.000 34.69266 ? 362 ARG B C   1 
ATOM   5737 O O   . ARG B 1 362 ? 12.71800  7.64200   54.05200  1.000 38.26866 ? 362 ARG B O   1 
ATOM   5738 C CB  . ARG B 1 362 ? 14.63700  7.59000   56.14800  1.000 36.02449 ? 362 ARG B CB  1 
ATOM   5739 C CG  . ARG B 1 362 ? 15.19400  6.88900   57.36500  1.000 32.64930 ? 362 ARG B CG  1 
ATOM   5740 C CD  . ARG B 1 362 ? 15.12300  7.72400   58.62200  1.000 32.51043 ? 362 ARG B CD  1 
ATOM   5741 N NE  . ARG B 1 362 ? 15.38800  6.88600   59.78400  1.000 46.14578 ? 362 ARG B NE  1 
ATOM   5742 C CZ  . ARG B 1 362 ? 16.58700  6.43100   60.12400  1.000 45.92149 ? 362 ARG B CZ  1 
ATOM   5743 N NH1 . ARG B 1 362 ? 17.67300  6.76100   59.44000  1.000 44.20158 ? 362 ARG B NH1 1 
ATOM   5744 N NH2 . ARG B 1 362 ? 16.70100  5.62200   61.17500  1.000 43.42387 ? 362 ARG B NH2 1 
ATOM   5745 N N   . VAL B 1 363 ? 14.36400  7.32500   52.56300  1.000 28.92003 ? 363 VAL B N   1 
ATOM   5746 C CA  . VAL B 1 363 ? 13.54500  7.54600   51.38000  1.000 34.35037 ? 363 VAL B CA  1 
ATOM   5747 C C   . VAL B 1 363 ? 13.28000  6.18500   50.75400  1.000 37.19213 ? 363 VAL B C   1 
ATOM   5748 O O   . VAL B 1 363 ? 14.17700  5.33100   50.70600  1.000 35.42219 ? 363 VAL B O   1 
ATOM   5749 C CB  . VAL B 1 363 ? 14.24500  8.50100   50.39000  1.000 31.35320 ? 363 VAL B CB  1 
ATOM   5750 C CG1 . VAL B 1 363 ? 13.43900  8.64500   49.10800  1.000 26.89352 ? 363 VAL B CG1 1 
ATOM   5751 C CG2 . VAL B 1 363 ? 14.49500  9.86500   51.04400  1.000 30.82961 ? 363 VAL B CG2 1 
ATOM   5752 N N   . SER B 1 364 ? 12.04800  5.96900   50.29300  1.000 33.31426 ? 364 SER B N   1 
ATOM   5753 C CA  . SER B 1 364 ? 11.69000  4.67600   49.73100  1.000 36.02951 ? 364 SER B CA  1 
ATOM   5754 C C   . SER B 1 364 ? 12.53600  4.38400   48.49100  1.000 33.04567 ? 364 SER B C   1 
ATOM   5755 O O   . SER B 1 364 ? 12.95800  5.30800   47.78500  1.000 33.28666 ? 364 SER B O   1 
ATOM   5756 C CB  . SER B 1 364 ? 10.20700  4.63900   49.36600  1.000 30.59648 ? 364 SER B CB  1 
ATOM   5757 O OG  . SER B 1 364 ? 9.97100   5.34200   48.15900  1.000 32.47936 ? 364 SER B OG  1 
ATOM   5758 N N   . PRO B 1 365 ? 12.82300  3.10800   48.21700  1.000 34.89436 ? 365 PRO B N   1 
ATOM   5759 C CA  . PRO B 1 365 ? 13.56400  2.77600   46.98700  1.000 33.58796 ? 365 PRO B CA  1 
ATOM   5760 C C   . PRO B 1 365 ? 12.87100  3.25300   45.72500  1.000 33.02917 ? 365 PRO B C   1 
ATOM   5761 O O   . PRO B 1 365 ? 13.54800  3.60200   44.74900  1.000 27.63637 ? 365 PRO B O   1 
ATOM   5762 C CB  . PRO B 1 365 ? 13.66000  1.24500   47.03900  1.000 25.96631 ? 365 PRO B CB  1 
ATOM   5763 C CG  . PRO B 1 365 ? 13.58100  0.92000   48.50100  1.000 31.40949 ? 365 PRO B CG  1 
ATOM   5764 C CD  . PRO B 1 365 ? 12.62400  1.93000   49.08000  1.000 31.97908 ? 365 PRO B CD  1 
ATOM   5765 N N   . GLU B 1 366 ? 11.53700  3.27000   45.71600  1.000 33.28582 ? 366 GLU B N   1 
ATOM   5766 C CA  . GLU B 1 366 ? 10.80400  3.76800   44.55600  1.000 35.92181 ? 366 GLU B CA  1 
ATOM   5767 C C   . GLU B 1 366 ? 11.01900  5.26700   44.36400  1.000 33.08734 ? 366 GLU B C   1 
ATOM   5768 O O   . GLU B 1 366 ? 11.18600  5.73800   43.23200  1.000 30.61506 ? 366 GLU B O   1 
ATOM   5769 C CB  . GLU B 1 366 ? 9.31300   3.44900   44.70600  1.000 32.08880 ? 366 GLU B CB  1 
ATOM   5770 C CG  . GLU B 1 366 ? 8.95800   1.97000   44.53800  1.000 34.88937 ? 366 GLU B CG  1 
ATOM   5771 C CD  . GLU B 1 366 ? 9.54900   1.06900   45.62500  1.000 39.17261 ? 366 GLU B CD  1 
ATOM   5772 O OE1 . GLU B 1 366 ? 9.55700   1.46900   46.81300  1.000 32.97030 ? 366 GLU B OE1 1 
ATOM   5773 O OE2 . GLU B 1 366 ? 10.01000  -0.04500  45.28600  1.000 43.91097 ? 366 GLU B OE2 1 
ATOM   5774 N N   . ALA B 1 367 ? 11.01000  6.03200   45.45800  1.000 33.37535 ? 367 ALA B N   1 
ATOM   5775 C CA  . ALA B 1 367 ? 11.20500  7.47600   45.35000  1.000 33.29408 ? 367 ALA B CA  1 
ATOM   5776 C C   . ALA B 1 367 ? 12.63000  7.81600   44.93200  1.000 30.24440 ? 367 ALA B C   1 
ATOM   5777 O O   . ALA B 1 367 ? 12.84300  8.74500   44.14500  1.000 34.72268 ? 367 ALA B O   1 
ATOM   5778 C CB  . ALA B 1 367 ? 10.85000  8.16000   46.67000  1.000 29.25845 ? 367 ALA B CB  1 
ATOM   5779 N N   . ARG B 1 368 ? 13.62000  7.08000   45.44400  1.000 32.81099 ? 368 ARG B N   1 
ATOM   5780 C CA  . ARG B 1 368 ? 14.99700  7.30800   45.01500  1.000 28.43143 ? 368 ARG B CA  1 
ATOM   5781 C C   . ARG B 1 368 ? 15.15600  7.01600   43.53100  1.000 29.82072 ? 368 ARG B C   1 
ATOM   5782 O O   . ARG B 1 368 ? 15.80600  7.77800   42.80400  1.000 29.40741 ? 368 ARG B O   1 
ATOM   5783 C CB  . ARG B 1 368 ? 15.96600  6.44900   45.83100  1.000 24.08426 ? 368 ARG B CB  1 
ATOM   5784 C CG  . ARG B 1 368 ? 15.91100  6.67900   47.33000  1.000 25.02280 ? 368 ARG B CG  1 
ATOM   5785 C CD  . ARG B 1 368 ? 17.10700  6.04100   48.03900  1.000 27.52281 ? 368 ARG B CD  1 
ATOM   5786 N NE  . ARG B 1 368 ? 17.29700  4.63700   47.68500  1.000 30.23650 ? 368 ARG B NE  1 
ATOM   5787 C CZ  . ARG B 1 368 ? 16.96000  3.61100   48.45800  1.000 32.73859 ? 368 ARG B CZ  1 
ATOM   5788 N NH1 . ARG B 1 368 ? 16.39400  3.79300   49.64100  1.000 27.14190 ? 368 ARG B NH1 1 
ATOM   5789 N NH2 . ARG B 1 368 ? 17.20300  2.37200   48.03600  1.000 31.38236 ? 368 ARG B NH2 1 
ATOM   5790 N N   . ALA B 1 369 ? 14.56200  5.91700   43.06300  1.000 32.30938 ? 369 ALA B N   1 
ATOM   5791 C CA  . ALA B 1 369 ? 14.61300  5.59500   41.64200  1.000 30.67348 ? 369 ALA B CA  1 
ATOM   5792 C C   . ALA B 1 369 ? 14.00700  6.71800   40.81100  1.000 29.46512 ? 369 ALA B C   1 
ATOM   5793 O O   . ALA B 1 369 ? 14.55000  7.08900   39.76300  1.000 28.48291 ? 369 ALA B O   1 
ATOM   5794 C CB  . ALA B 1 369 ? 13.89000  4.27400   41.37900  1.000 29.35397 ? 369 ALA B CB  1 
ATOM   5795 N N   . ALA B 1 370 ? 12.89200  7.28700   41.27500  1.000 26.97459 ? 370 ALA B N   1 
ATOM   5796 C CA  . ALA B 1 370 ? 12.29600  8.42000   40.57600  1.000 28.88691 ? 370 ALA B CA  1 
ATOM   5797 C C   . ALA B 1 370 ? 13.25700  9.60200   40.52600  1.000 29.02809 ? 370 ALA B C   1 
ATOM   5798 O O   . ALA B 1 370 ? 13.35200  10.28900  39.50400  1.000 30.86424 ? 370 ALA B O   1 
ATOM   5799 C CB  . ALA B 1 370 ? 10.98200  8.82600   41.24600  1.000 26.04873 ? 370 ALA B CB  1 
ATOM   5800 N N   . ALA B 1 371 ? 13.98100  9.85300   41.61800  1.000 26.61950 ? 371 ALA B N   1 
ATOM   5801 C CA  . ALA B 1 371 ? 14.92400  10.96300  41.65400  1.000 30.07335 ? 371 ALA B CA  1 
ATOM   5802 C C   . ALA B 1 371 ? 16.24300  10.65400  40.95500  1.000 30.98692 ? 371 ALA B C   1 
ATOM   5803 O O   . ALA B 1 371 ? 17.02400  11.58300  40.71800  1.000 26.90349 ? 371 ALA B O   1 
ATOM   5804 C CB  . ALA B 1 371 ? 15.20000  11.37600  43.10000  1.000 26.83425 ? 371 ALA B CB  1 
ATOM   5805 N N   . GLY B 1 372 ? 16.50500  9.39400   40.60900  1.000 25.79486 ? 372 GLY B N   1 
ATOM   5806 C CA  . GLY B 1 372 ? 17.75800  9.02300   39.98000  1.000 24.01833 ? 372 GLY B CA  1 
ATOM   5807 C C   . GLY B 1 372 ? 18.88500  8.67900   40.92800  1.000 25.81156 ? 372 GLY B C   1 
ATOM   5808 O O   . GLY B 1 372 ? 20.04300  8.62600   40.49700  1.000 25.77438 ? 372 GLY B O   1 
ATOM   5809 N N   . VAL B 1 373 ? 18.58700  8.44300   42.20100  1.000 22.77014 ? 373 VAL B N   1 
ATOM   5810 C CA  . VAL B 1 373 ? 19.59600  8.10000   43.20100  1.000 23.85044 ? 373 VAL B CA  1 
ATOM   5811 C C   . VAL B 1 373 ? 19.59300  6.58000   43.30900  1.000 26.48250 ? 373 VAL B C   1 
ATOM   5812 O O   . VAL B 1 373 ? 18.82400  5.98800   44.07000  1.000 23.89485 ? 373 VAL B O   1 
ATOM   5813 C CB  . VAL B 1 373 ? 19.31600  8.77300   44.54200  1.000 23.28563 ? 373 VAL B CB  1 
ATOM   5814 C CG1 . VAL B 1 373 ? 20.39800  8.42000   45.55700  1.000 20.04780 ? 373 VAL B CG1 1 
ATOM   5815 C CG2 . VAL B 1 373 ? 19.20300  10.28100  44.36000  1.000 27.42222 ? 373 VAL B CG2 1 
ATOM   5816 N N   . GLY B 1 374 ? 20.47800  5.93700   42.54100  1.000 26.78443 ? 374 GLY B N   1 
ATOM   5817 C CA  . GLY B 1 374 ? 20.50200  4.49100   42.47400  1.000 24.39631 ? 374 GLY B CA  1 
ATOM   5818 C C   . GLY B 1 374 ? 21.27200  3.85000   43.61100  1.000 27.49043 ? 374 GLY B C   1 
ATOM   5819 O O   . GLY B 1 374 ? 21.91700  4.51600   44.42200  1.000 25.65669 ? 374 GLY B O   1 
ATOM   5820 N N   . ASP B 1 375 ? 21.19400  2.51900   43.66300  1.000 19.33195 ? 375 ASP B N   1 
ATOM   5821 C CA  . ASP B 1 375 ? 21.88900  1.76600   44.69700  1.000 20.42148 ? 375 ASP B CA  1 
ATOM   5822 C C   . ASP B 1 375 ? 23.36700  1.58900   44.40700  1.000 19.26232 ? 375 ASP B C   1 
ATOM   5823 O O   . ASP B 1 375 ? 24.10500  1.17100   45.30300  1.000 22.09349 ? 375 ASP B O   1 
ATOM   5824 C CB  . ASP B 1 375 ? 21.24700  0.39200   44.88800  1.000 26.91567 ? 375 ASP B CB  1 
ATOM   5825 C CG  . ASP B 1 375 ? 20.00800  0.44500   45.75500  1.000 32.20805 ? 375 ASP B CG  1 
ATOM   5826 O OD1 . ASP B 1 375 ? 19.57800  1.56100   46.11800  1.000 26.77816 ? 375 ASP B OD1 1 
ATOM   5827 O OD2 . ASP B 1 375 ? 19.46500  -0.63400  46.07500  1.000 40.86851 ? 375 ASP B OD2 1 
ATOM   5828 N N   . GLY B 1 376 ? 23.81400  1.87500   43.18800  1.000 20.31995 ? 376 GLY B N   1 
ATOM   5829 C CA  . GLY B 1 376 ? 25.22100  1.86800   42.85100  1.000 21.33891 ? 376 GLY B CA  1 
ATOM   5830 C C   . GLY B 1 376 ? 25.90800  3.21500   42.92900  1.000 21.15847 ? 376 GLY B C   1 
ATOM   5831 O O   . GLY B 1 376 ? 27.07200  3.32000   42.52400  1.000 19.35532 ? 376 GLY B O   1 
ATOM   5832 N N   . LEU B 1 377 ? 25.23700  4.24500   43.44400  1.000 18.45079 ? 377 LEU B N   1 
ATOM   5833 C CA  . LEU B 1 377 ? 25.77200  5.60300   43.45400  1.000 23.00249 ? 377 LEU B CA  1 
ATOM   5834 C C   . LEU B 1 377 ? 26.60400  5.84800   44.70800  1.000 19.96852 ? 377 LEU B C   1 
ATOM   5835 O O   . LEU B 1 377 ? 26.18700  5.51000   45.82200  1.000 19.60705 ? 377 LEU B O   1 
ATOM   5836 C CB  . LEU B 1 377 ? 24.63800  6.63200   43.36800  1.000 24.84665 ? 377 LEU B CB  1 
ATOM   5837 C CG  . LEU B 1 377 ? 24.98400  8.12400   43.23300  1.000 23.59408 ? 377 LEU B CG  1 
ATOM   5838 C CD1 . LEU B 1 377 ? 23.88700  8.85100   42.49500  1.000 25.08547 ? 377 LEU B CD1 1 
ATOM   5839 C CD2 . LEU B 1 377 ? 25.20900  8.78900   44.58500  1.000 22.53227 ? 377 LEU B CD2 1 
ATOM   5840 N N   . LEU B 1 378 ? 27.77300  6.44900   44.51500  1.000 20.78478 ? 378 LEU B N   1 
ATOM   5841 C CA  . LEU B 1 378 ? 28.63400  6.92200   45.59000  1.000 22.73271 ? 378 LEU B CA  1 
ATOM   5842 C C   . LEU B 1 378 ? 28.86900  8.41300   45.40300  1.000 20.41936 ? 378 LEU B C   1 
ATOM   5843 O O   . LEU B 1 378 ? 29.02700  8.88500   44.27100  1.000 17.82031 ? 378 LEU B O   1 
ATOM   5844 C CB  . LEU B 1 378 ? 29.97500  6.17600   45.60400  1.000 18.87357 ? 378 LEU B CB  1 
ATOM   5845 C CG  . LEU B 1 378 ? 29.87500  4.72800   46.07800  1.000 22.39123 ? 378 LEU B CG  1 
ATOM   5846 C CD1 . LEU B 1 378 ? 31.16900  3.97900   45.82400  1.000 18.24213 ? 378 LEU B CD1 1 
ATOM   5847 C CD2 . LEU B 1 378 ? 29.49900  4.71000   47.55100  1.000 18.16583 ? 378 LEU B CD2 1 
ATOM   5848 N N   . ARG B 1 379 ? 28.87900  9.15400   46.50800  1.000 21.31965 ? 379 ARG B N   1 
ATOM   5849 C CA  . ARG B 1 379 ? 29.10500  10.59200  46.48200  1.000 15.94544 ? 379 ARG B CA  1 
ATOM   5850 C C   . ARG B 1 379 ? 30.44700  10.91100  47.12000  1.000 20.64333 ? 379 ARG B C   1 
ATOM   5851 O O   . ARG B 1 379 ? 30.73700  10.44900  48.22800  1.000 16.42220 ? 379 ARG B O   1 
ATOM   5852 C CB  . ARG B 1 379 ? 28.00400  11.35400  47.21400  1.000 16.85193 ? 379 ARG B CB  1 
ATOM   5853 C CG  . ARG B 1 379 ? 28.23500  12.84900  47.12800  1.000 18.72653 ? 379 ARG B CG  1 
ATOM   5854 C CD  . ARG B 1 379 ? 27.46300  13.61000  48.16200  1.000 25.04143 ? 379 ARG B CD  1 
ATOM   5855 N NE  . ARG B 1 379 ? 27.95400  13.38100  49.51600  1.000 19.11635 ? 379 ARG B NE  1 
ATOM   5856 C CZ  . ARG B 1 379 ? 27.43100  13.94800  50.59100  1.000 18.61491 ? 379 ARG B CZ  1 
ATOM   5857 N NH1 . ARG B 1 379 ? 26.40600  14.78000  50.49900  1.000 20.26280 ? 379 ARG B NH1 1 
ATOM   5858 N NH2 . ARG B 1 379 ? 27.95100  13.67900  51.78800  1.000 19.10321 ? 379 ARG B NH2 1 
ATOM   5859 N N   . ILE B 1 380 ? 31.25800  11.70600  46.42900  1.000 16.99925 ? 380 ILE B N   1 
ATOM   5860 C CA  . ILE B 1 380 ? 32.56200  12.11300  46.92800  1.000 15.42847 ? 380 ILE B CA  1 
ATOM   5861 C C   . ILE B 1 380 ? 32.56400  13.62200  47.09800  1.000 19.82371 ? 380 ILE B C   1 
ATOM   5862 O O   . ILE B 1 380 ? 32.26300  14.36000  46.15000  1.000 21.02427 ? 380 ILE B O   1 
ATOM   5863 C CB  . ILE B 1 380 ? 33.70100  11.68000  45.99700  1.000 19.00130 ? 380 ILE B CB  1 
ATOM   5864 C CG1 . ILE B 1 380 ? 33.85900  10.15800  46.01500  1.000 18.18731 ? 380 ILE B CG1 1 
ATOM   5865 C CG2 . ILE B 1 380 ? 35.00300  12.36400  46.40800  1.000 14.45463 ? 380 ILE B CG2 1 
ATOM   5866 C CD1 . ILE B 1 380 ? 34.93500  9.65800   45.07700  1.000 18.65545 ? 380 ILE B CD1 1 
ATOM   5867 N N   . SER B 1 381 ? 32.89200  14.08000  48.30400  1.000 17.97299 ? 381 SER B N   1 
ATOM   5868 C CA  . SER B 1 381 ? 33.26200  15.47100  48.53300  1.000 15.03139 ? 381 SER B CA  1 
ATOM   5869 C C   . SER B 1 381 ? 34.77600  15.53600  48.40700  1.000 15.44220 ? 381 SER B C   1 
ATOM   5870 O O   . SER B 1 381 ? 35.49600  15.00600  49.26000  1.000 17.33412 ? 381 SER B O   1 
ATOM   5871 C CB  . SER B 1 381 ? 32.78400  15.94900  49.90200  1.000 18.23470 ? 381 SER B CB  1 
ATOM   5872 O OG  . SER B 1 381 ? 33.26600  17.24600  50.19200  1.000 15.91321 ? 381 SER B OG  1 
ATOM   5873 N N   . VAL B 1 382 ? 35.25700  16.15100  47.33100  1.000 17.15506 ? 382 VAL B N   1 
ATOM   5874 C CA  . VAL B 1 382 ? 36.67000  16.07400  46.97100  1.000 16.65738 ? 382 VAL B CA  1 
ATOM   5875 C C   . VAL B 1 382 ? 37.44900  17.08200  47.80300  1.000 15.30910 ? 382 VAL B C   1 
ATOM   5876 O O   . VAL B 1 382 ? 37.23200  18.29300  47.69300  1.000 18.70657 ? 382 VAL B O   1 
ATOM   5877 C CB  . VAL B 1 382 ? 36.87500  16.32100  45.46800  1.000 24.97591 ? 382 VAL B CB  1 
ATOM   5878 C CG1 . VAL B 1 382 ? 38.34500  16.16900  45.10400  1.000 14.94120 ? 382 VAL B CG1 1 
ATOM   5879 C CG2 . VAL B 1 382 ? 36.01800  15.36200  44.63700  1.000 17.63074 ? 382 VAL B CG2 1 
ATOM   5880 N N   . GLY B 1 383 ? 38.36700  16.58600  48.62100  1.000 15.52690 ? 383 GLY B N   1 
ATOM   5881 C CA  . GLY B 1 383 ? 39.12200  17.41300  49.53600  1.000 15.32450 ? 383 GLY B CA  1 
ATOM   5882 C C   . GLY B 1 383 ? 40.36900  18.00500  48.91400  1.000 19.95206 ? 383 GLY B C   1 
ATOM   5883 O O   . GLY B 1 383 ? 40.49000  18.14300  47.69400  1.000 17.72856 ? 383 GLY B O   1 
ATOM   5884 N N   . LEU B 1 384 ? 41.31400  18.35900  49.78300  1.000 18.82180 ? 384 LEU B N   1 
ATOM   5885 C CA  . LEU B 1 384 ? 42.51000  19.09000  49.39800  1.000 15.25973 ? 384 LEU B CA  1 
ATOM   5886 C C   . LEU B 1 384 ? 43.75300  18.21500  49.38500  1.000 18.19240 ? 384 LEU B C   1 
ATOM   5887 O O   . LEU B 1 384 ? 44.85600  18.73500  49.19900  1.000 18.41166 ? 384 LEU B O   1 
ATOM   5888 C CB  . LEU B 1 384 ? 42.71500  20.28000  50.33600  1.000 17.31303 ? 384 LEU B CB  1 
ATOM   5889 C CG  . LEU B 1 384 ? 41.55600  21.28100  50.36000  1.000 19.39441 ? 384 LEU B CG  1 
ATOM   5890 C CD1 . LEU B 1 384 ? 41.80700  22.37400  51.38400  1.000 16.24231 ? 384 LEU B CD1 1 
ATOM   5891 C CD2 . LEU B 1 384 ? 41.32400  21.88500  48.96700  1.000 20.13491 ? 384 LEU B CD2 1 
ATOM   5892 N N   . GLU B 1 385 ? 43.60600  16.90600  49.58000  1.000 19.01844 ? 385 GLU B N   1 
ATOM   5893 C CA  . GLU B 1 385 ? 44.74500  16.00900  49.46300  1.000 19.70308 ? 385 GLU B CA  1 
ATOM   5894 C C   . GLU B 1 385 ? 45.24200  15.97500  48.01600  1.000 18.12717 ? 385 GLU B C   1 
ATOM   5895 O O   . GLU B 1 385 ? 44.57100  16.43100  47.08400  1.000 16.30474 ? 385 GLU B O   1 
ATOM   5896 C CB  . GLU B 1 385 ? 44.37700  14.59800  49.92200  1.000 18.60834 ? 385 GLU B CB  1 
ATOM   5897 C CG  . GLU B 1 385 ? 43.75200  14.51800  51.30800  1.000 20.14715 ? 385 GLU B CG  1 
ATOM   5898 C CD  . GLU B 1 385 ? 42.23200  14.48400  51.25600  1.000 20.60624 ? 385 GLU B CD  1 
ATOM   5899 O OE1 . GLU B 1 385 ? 41.65400  15.00400  50.28000  1.000 17.54269 ? 385 GLU B OE1 1 
ATOM   5900 O OE2 . GLU B 1 385 ? 41.61400  13.92100  52.18300  1.000 19.39242 ? 385 GLU B OE2 1 
ATOM   5901 N N   . HIS B 1 386 ? 46.44700  15.44500  47.83400  1.000 19.85387 ? 386 HIS B N   1 
ATOM   5902 C CA  . HIS B 1 386 ? 46.98400  15.28400  46.48800  1.000 21.93491 ? 386 HIS B CA  1 
ATOM   5903 C C   . HIS B 1 386 ? 46.11600  14.31500  45.69100  1.000 22.88110 ? 386 HIS B C   1 
ATOM   5904 O O   . HIS B 1 386 ? 45.80100  13.21500  46.15900  1.000 22.32866 ? 386 HIS B O   1 
ATOM   5905 C CB  . HIS B 1 386 ? 48.42600  14.78300  46.54500  1.000 23.06871 ? 386 HIS B CB  1 
ATOM   5906 C CG  . HIS B 1 386 ? 49.20000  15.04700  45.29200  1.000 30.08984 ? 386 HIS B CG  1 
ATOM   5907 N ND1 . HIS B 1 386 ? 49.00100  14.33300  44.13000  1.000 28.08347 ? 386 HIS B ND1 1 
ATOM   5908 C CD2 . HIS B 1 386 ? 50.16100  15.96000  45.01400  1.000 27.52466 ? 386 HIS B CD2 1 
ATOM   5909 C CE1 . HIS B 1 386 ? 49.81000  14.79200  43.19100  1.000 30.42918 ? 386 HIS B CE1 1 
ATOM   5910 N NE2 . HIS B 1 386 ? 50.52200  15.78100  43.70100  1.000 30.04098 ? 386 HIS B NE2 1 
ATOM   5911 N N   . ALA B 1 387 ? 45.73800  14.73200  44.47600  1.000 21.69476 ? 387 ALA B N   1 
ATOM   5912 C CA  . ALA B 1 387 ? 44.84400  13.92700  43.64500  1.000 25.52726 ? 387 ALA B CA  1 
ATOM   5913 C C   . ALA B 1 387 ? 45.41900  12.54700  43.35900  1.000 25.92361 ? 387 ALA B C   1 
ATOM   5914 O O   . ALA B 1 387 ? 44.66700  11.56700  43.29500  1.000 24.24907 ? 387 ALA B O   1 
ATOM   5915 C CB  . ALA B 1 387 ? 44.54200  14.65200  42.33400  1.000 20.64349 ? 387 ALA B CB  1 
ATOM   5916 N N   . ASP B 1 388 ? 46.74000  12.44500  43.20300  1.000 23.92312 ? 388 ASP B N   1 
ATOM   5917 C CA  . ASP B 1 388 ? 47.35900  11.14100  42.99600  1.000 26.89817 ? 388 ASP B CA  1 
ATOM   5918 C C   . ASP B 1 388 ? 47.04800  10.20200  44.15500  1.000 31.15481 ? 388 ASP B C   1 
ATOM   5919 O O   . ASP B 1 388 ? 46.67000  9.04300   43.94700  1.000 30.41873 ? 388 ASP B O   1 
ATOM   5920 C CB  . ASP B 1 388 ? 48.87200  11.29100  42.81800  1.000 30.22590 ? 388 ASP B CB  1 
ATOM   5921 C CG  . ASP B 1 388 ? 49.25200  11.91600  41.48000  1.000 33.02019 ? 388 ASP B CG  1 
ATOM   5922 O OD1 . ASP B 1 388 ? 48.36000  12.09700  40.62600  1.000 30.93728 ? 388 ASP B OD1 1 
ATOM   5923 O OD2 . ASP B 1 388 ? 50.44800  12.22600  41.28500  1.000 34.76406 ? 388 ASP B OD2 1 
ATOM   5924 N N   . ASP B 1 389 ? 47.19400  10.68700  45.39100  1.000 29.70098 ? 389 ASP B N   1 
ATOM   5925 C CA  . ASP B 1 389 ? 46.89000  9.84500   46.54400  1.000 27.16185 ? 389 ASP B CA  1 
ATOM   5926 C C   . ASP B 1 389 ? 45.41300  9.48300   46.57900  1.000 25.25018 ? 389 ASP B C   1 
ATOM   5927 O O   . ASP B 1 389 ? 45.05500  8.33700   46.87200  1.000 26.05778 ? 389 ASP B O   1 
ATOM   5928 C CB  . ASP B 1 389 ? 47.31100  10.54200  47.83700  1.000 24.67723 ? 389 ASP B CB  1 
ATOM   5929 C CG  . ASP B 1 389 ? 48.81000  10.70000  47.94100  1.000 27.58930 ? 389 ASP B CG  1 
ATOM   5930 O OD1 . ASP B 1 389 ? 49.52200  9.78900   47.47400  1.000 31.72320 ? 389 ASP B OD1 1 
ATOM   5931 O OD2 . ASP B 1 389 ? 49.27900  11.73000  48.47600  1.000 26.55236 ? 389 ASP B OD2 1 
ATOM   5932 N N   . LEU B 1 390 ? 44.54000  10.44600  46.27800  1.000 24.85879 ? 390 LEU B N   1 
ATOM   5933 C CA  . LEU B 1 390 ? 43.12100  10.13400  46.17700  1.000 25.36036 ? 390 LEU B CA  1 
ATOM   5934 C C   . LEU B 1 390 ? 42.86300  9.12200   45.06700  1.000 25.87254 ? 390 LEU B C   1 
ATOM   5935 O O   . LEU B 1 390 ? 42.10500  8.16300   45.25900  1.000 25.25591 ? 390 LEU B O   1 
ATOM   5936 C CB  . LEU B 1 390 ? 42.31800  11.41100  45.94100  1.000 20.97915 ? 390 LEU B CB  1 
ATOM   5937 C CG  . LEU B 1 390 ? 42.45000  12.51000  46.99600  1.000 21.10723 ? 390 LEU B CG  1 
ATOM   5938 C CD1 . LEU B 1 390 ? 41.58200  13.69200  46.61600  1.000 19.69258 ? 390 LEU B CD1 1 
ATOM   5939 C CD2 . LEU B 1 390 ? 42.06500  11.99600  48.37900  1.000 17.92889 ? 390 LEU B CD2 1 
ATOM   5940 N N   . ARG B 1 391 ? 43.50400  9.30900   43.90500  1.000 25.15652 ? 391 ARG B N   1 
ATOM   5941 C CA  A ARG B 1 391 ? 43.32200  8.37600   42.79800  0.493 28.20236 ? 391 ARG B CA  1 
ATOM   5942 C CA  B ARG B 1 391 ? 43.32200  8.37300   42.79800  0.507 28.21928 ? 391 ARG B CA  1 
ATOM   5943 C C   . ARG B 1 391 ? 43.78000  6.97400   43.18100  1.000 29.70808 ? 391 ARG B C   1 
ATOM   5944 O O   . ARG B 1 391 ? 43.08100  5.98800   42.91700  1.000 26.01861 ? 391 ARG B O   1 
ATOM   5945 C CB  A ARG B 1 391 ? 44.08100  8.87900   41.56900  0.493 28.66276 ? 391 ARG B CB  1 
ATOM   5946 C CB  B ARG B 1 391 ? 44.08300  8.84900   41.55800  0.507 28.65782 ? 391 ARG B CB  1 
ATOM   5947 C CG  A ARG B 1 391 ? 43.82800  8.10300   40.28300  0.493 29.72529 ? 391 ARG B CG  1 
ATOM   5948 C CG  B ARG B 1 391 ? 43.60200  8.20500   40.25500  0.507 29.75946 ? 391 ARG B CG  1 
ATOM   5949 C CD  A ARG B 1 391 ? 44.14600  8.95800   39.05100  0.493 28.73642 ? 391 ARG B CD  1 
ATOM   5950 C CD  B ARG B 1 391 ? 44.74000  7.69700   39.36000  0.507 28.01718 ? 391 ARG B CD  1 
ATOM   5951 N NE  A ARG B 1 391 ? 43.25700  10.11300  38.95000  0.493 33.89204 ? 391 ARG B NE  1 
ATOM   5952 N NE  B ARG B 1 391 ? 45.81700  8.66600   39.20200  0.507 27.21815 ? 391 ARG B NE  1 
ATOM   5953 C CZ  A ARG B 1 391 ? 43.57300  11.34700  39.32000  0.493 24.48548 ? 391 ARG B CZ  1 
ATOM   5954 C CZ  B ARG B 1 391 ? 47.04600  8.49700   39.67200  0.507 28.25192 ? 391 ARG B CZ  1 
ATOM   5955 N NH1 A ARG B 1 391 ? 44.77500  11.64500  39.78300  0.493 26.07913 ? 391 ARG B NH1 1 
ATOM   5956 N NH1 B ARG B 1 391 ? 47.40000  7.38400   40.29200  0.507 31.23706 ? 391 ARG B NH1 1 
ATOM   5957 N NH2 A ARG B 1 391 ? 42.65900  12.30600  39.22300  0.493 17.77640 ? 391 ARG B NH2 1 
ATOM   5958 N NH2 B ARG B 1 391 ? 47.94000  9.46800   39.51600  0.507 28.53249 ? 391 ARG B NH2 1 
ATOM   5959 N N   . GLU B 1 392 ? 44.94600  6.87000   43.82300  1.000 27.27924 ? 392 GLU B N   1 
ATOM   5960 C CA  . GLU B 1 392 ? 45.46800  5.56200   44.19300  1.000 28.54335 ? 392 GLU B CA  1 
ATOM   5961 C C   . GLU B 1 392 ? 44.59900  4.88500   45.24000  1.000 29.23620 ? 392 GLU B C   1 
ATOM   5962 O O   . GLU B 1 392 ? 44.50400  3.65300   45.25700  1.000 32.50343 ? 392 GLU B O   1 
ATOM   5963 C CB  . GLU B 1 392 ? 46.90400  5.69100   44.69400  1.000 30.42969 ? 392 GLU B CB  1 
ATOM   5964 C CG  . GLU B 1 392 ? 47.89300  6.10500   43.61700  1.000 34.97287 ? 392 GLU B CG  1 
ATOM   5965 C CD  . GLU B 1 392 ? 49.31600  6.19400   44.13400  1.000 41.84575 ? 392 GLU B CD  1 
ATOM   5966 O OE1 . GLU B 1 392 ? 49.63700  5.51400   45.13500  1.000 42.39765 ? 392 GLU B OE1 1 
ATOM   5967 O OE2 . GLU B 1 392 ? 50.11200  6.94800   43.53600  1.000 50.48237 ? 392 GLU B OE2 1 
ATOM   5968 N N   . ASP B 1 393 ? 43.97100  5.66000   46.12700  1.000 26.42810 ? 393 ASP B N   1 
ATOM   5969 C CA  . ASP B 1 393 ? 43.06800  5.04900   47.09300  1.000 26.72348 ? 393 ASP B CA  1 
ATOM   5970 C C   . ASP B 1 393 ? 41.82500  4.50900   46.40500  1.000 24.74138 ? 393 ASP B C   1 
ATOM   5971 O O   . ASP B 1 393 ? 41.35400  3.41300   46.73100  1.000 25.76006 ? 393 ASP B O   1 
ATOM   5972 C CB  . ASP B 1 393 ? 42.69500  6.04900   48.18900  1.000 23.31213 ? 393 ASP B CB  1 
ATOM   5973 C CG  . ASP B 1 393 ? 42.03000  5.38000   49.38400  1.000 25.35596 ? 393 ASP B CG  1 
ATOM   5974 O OD1 . ASP B 1 393 ? 42.55000  4.34300   49.85700  1.000 26.82463 ? 393 ASP B OD1 1 
ATOM   5975 O OD2 . ASP B 1 393 ? 40.99400  5.89400   49.85500  1.000 25.20742 ? 393 ASP B OD2 1 
ATOM   5976 N N   . MET B 1 394 ? 41.28400  5.25800   45.44400  1.000 22.89687 ? 394 MET B N   1 
ATOM   5977 C CA  . MET B 1 394 ? 40.10300  4.78600   44.73200  1.000 27.38651 ? 394 MET B CA  1 
ATOM   5978 C C   . MET B 1 394 ? 40.42200  3.58500   43.84600  1.000 30.49665 ? 394 MET B C   1 
ATOM   5979 O O   . MET B 1 394 ? 39.54200  2.75100   43.60100  1.000 27.71025 ? 394 MET B O   1 
ATOM   5980 C CB  . MET B 1 394 ? 39.49500  5.92600   43.91900  1.000 26.13863 ? 394 MET B CB  1 
ATOM   5981 C CG  . MET B 1 394 ? 38.65500  6.87400   44.76100  1.000 24.23774 ? 394 MET B CG  1 
ATOM   5982 S SD  . MET B 1 394 ? 38.04800  8.29100   43.83000  1.000 26.68486 ? 394 MET B SD  1 
ATOM   5983 C CE  . MET B 1 394 ? 39.59600  9.07500   43.40200  1.000 25.74729 ? 394 MET B CE  1 
ATOM   5984 N N   . GLU B 1 395 ? 41.66600  3.47200   43.37000  1.000 26.21712 ? 395 GLU B N   1 
ATOM   5985 C CA  . GLU B 1 395 ? 42.07600  2.26700   42.65700  1.000 32.44193 ? 395 GLU B CA  1 
ATOM   5986 C C   . GLU B 1 395 ? 42.02500  1.04000   43.56000  1.000 33.88995 ? 395 GLU B C   1 
ATOM   5987 O O   . GLU B 1 395 ? 41.82800  -0.07900  43.07100  1.000 36.66191 ? 395 GLU B O   1 
ATOM   5988 C CB  . GLU B 1 395 ? 43.48000  2.44800   42.07000  1.000 29.21310 ? 395 GLU B CB  1 
ATOM   5989 C CG  . GLU B 1 395 ? 43.52300  3.37100   40.85400  1.000 29.71917 ? 395 GLU B CG  1 
ATOM   5990 C CD  . GLU B 1 395 ? 44.93800  3.75800   40.43900  1.000 37.89776 ? 395 GLU B CD  1 
ATOM   5991 O OE1 . GLU B 1 395 ? 45.89400  3.45100   41.18600  1.000 42.06359 ? 395 GLU B OE1 1 
ATOM   5992 O OE2 . GLU B 1 395 ? 45.09400  4.38000   39.36300  1.000 39.85031 ? 395 GLU B OE2 1 
ATOM   5993 N N   . ARG B 1 396 ? 42.19900  1.22200   44.87400  1.000 28.80841 ? 396 ARG B N   1 
ATOM   5994 C CA  . ARG B 1 396 ? 41.99900  0.10900   45.79800  1.000 29.90064 ? 396 ARG B CA  1 
ATOM   5995 C C   . ARG B 1 396 ? 40.53800  -0.31400  45.83600  1.000 27.21371 ? 396 ARG B C   1 
ATOM   5996 O O   . ARG B 1 396 ? 40.23200  -1.49800  46.01300  1.000 31.64385 ? 396 ARG B O   1 
ATOM   5997 C CB  . ARG B 1 396 ? 42.46800  0.48000   47.20500  1.000 30.95805 ? 396 ARG B CB  1 
ATOM   5998 C CG  . ARG B 1 396 ? 43.93700  0.82400   47.33600  1.000 31.17409 ? 396 ARG B CG  1 
ATOM   5999 C CD  . ARG B 1 396 ? 44.30200  1.07700   48.79900  1.000 31.00910 ? 396 ARG B CD  1 
ATOM   6000 N NE  . ARG B 1 396 ? 45.70800  1.43400   48.94100  1.000 41.64606 ? 396 ARG B NE  1 
ATOM   6001 C CZ  . ARG B 1 396 ? 46.16800  2.67700   49.00400  1.000 39.11097 ? 396 ARG B CZ  1 
ATOM   6002 N NH1 . ARG B 1 396 ? 45.35300  3.71900   49.00000  1.000 33.89648 ? 396 ARG B NH1 1 
ATOM   6003 N NH2 . ARG B 1 396 ? 47.48200  2.87900   49.07200  1.000 37.56763 ? 396 ARG B NH2 1 
ATOM   6004 N N   . GLY B 1 397 ? 39.62000  0.64400   45.71900  1.000 29.07500 ? 397 GLY B N   1 
ATOM   6005 C CA  . GLY B 1 397 ? 38.20900  0.29800   45.69300  1.000 31.00400 ? 397 GLY B CA  1 
ATOM   6006 C C   . GLY B 1 397 ? 37.81900  -0.43500  44.42500  1.000 28.48840 ? 397 GLY B C   1 
ATOM   6007 O O   . GLY B 1 397 ? 36.99000  -1.34800  44.45300  1.000 28.39245 ? 397 GLY B O   1 
ATOM   6008 N N   . PHE B 1 398 ? 38.39300  -0.02800  43.29400  1.000 23.97042 ? 398 PHE B N   1 
ATOM   6009 C CA  . PHE B 1 398 ? 38.10400  -0.69400  42.03100  1.000 31.43020 ? 398 PHE B CA  1 
ATOM   6010 C C   . PHE B 1 398 ? 38.73300  -2.07900  41.98500  1.000 33.69970 ? 398 PHE B C   1 
ATOM   6011 O O   . PHE B 1 398 ? 38.13400  -3.02100  41.45500  1.000 32.59463 ? 398 PHE B O   1 
ATOM   6012 C CB  . PHE B 1 398 ? 38.60000  0.16200   40.86900  1.000 27.81306 ? 398 PHE B CB  1 
ATOM   6013 C CG  . PHE B 1 398 ? 37.72900  1.35000   40.57400  1.000 28.96556 ? 398 PHE B CG  1 
ATOM   6014 C CD1 . PHE B 1 398 ? 36.35400  1.21200   40.47200  1.000 24.65324 ? 398 PHE B CD1 1 
ATOM   6015 C CD2 . PHE B 1 398 ? 38.28900  2.60800   40.39800  1.000 26.58126 ? 398 PHE B CD2 1 
ATOM   6016 C CE1 . PHE B 1 398 ? 35.55300  2.30600   40.18800  1.000 25.80918 ? 398 PHE B CE1 1 
ATOM   6017 C CE2 . PHE B 1 398 ? 37.49300  3.70800   40.11700  1.000 22.12901 ? 398 PHE B CE2 1 
ATOM   6018 C CZ  . PHE B 1 398 ? 36.12400  3.55900   40.01100  1.000 25.01140 ? 398 PHE B CZ  1 
ATOM   6019 N N   . ALA B 1 399 ? 39.93900  -2.22100  42.54100  1.000 32.53807 ? 399 ALA B N   1 
ATOM   6020 C CA  . ALA B 1 399 ? 40.57000  -3.53200  42.60400  1.000 34.08799 ? 399 ALA B CA  1 
ATOM   6021 C C   . ALA B 1 399 ? 39.74600  -4.50800  43.43200  1.000 36.39622 ? 399 ALA B C   1 
ATOM   6022 O O   . ALA B 1 399 ? 39.74800  -5.71100  43.15100  1.000 45.37427 ? 399 ALA B O   1 
ATOM   6023 C CB  . ALA B 1 399 ? 41.98400  -3.40700  43.17300  1.000 32.95499 ? 399 ALA B CB  1 
ATOM   6024 N N   . ALA B 1 400 ? 39.02500  -4.01600  44.44200  1.000 31.45614 ? 400 ALA B N   1 
ATOM   6025 C CA  . ALA B 1 400 ? 38.18100  -4.88700  45.25200  1.000 38.02878 ? 400 ALA B CA  1 
ATOM   6026 C C   . ALA B 1 400 ? 36.94700  -5.37900  44.50500  1.000 39.18191 ? 400 ALA B C   1 
ATOM   6027 O O   . ALA B 1 400 ? 36.27000  -6.29100  44.99200  1.000 41.07314 ? 400 ALA B O   1 
ATOM   6028 C CB  . ALA B 1 400 ? 37.75200  -4.17300  46.53500  1.000 36.49753 ? 400 ALA B CB  1 
ATOM   6029 N N   . LEU B 1 401 ? 36.63100  -4.79400  43.35200  1.000 40.70229 ? 401 LEU B N   1 
ATOM   6030 C CA  . LEU B 1 401 ? 35.54600  -5.29800  42.52300  1.000 42.61515 ? 401 LEU B CA  1 
ATOM   6031 C C   . LEU B 1 401 ? 35.92200  -6.57000  41.77200  1.000 48.19888 ? 401 LEU B C   1 
ATOM   6032 O O   . LEU B 1 401 ? 35.04000  -7.21100  41.19200  1.000 53.28098 ? 401 LEU B O   1 
ATOM   6033 C CB  . LEU B 1 401 ? 35.10500  -4.21800  41.53300  1.000 39.21311 ? 401 LEU B CB  1 
ATOM   6034 C CG  . LEU B 1 401 ? 33.97900  -3.27700  41.97100  1.000 39.12290 ? 401 LEU B CG  1 
ATOM   6035 C CD1 . LEU B 1 401 ? 33.86200  -3.20000  43.48300  1.000 34.09629 ? 401 LEU B CD1 1 
ATOM   6036 C CD2 . LEU B 1 401 ? 34.17700  -1.88600  41.37300  1.000 34.82436 ? 401 LEU B CD2 1 
ATOM   6037 N N   . VAL B 1 402 ? 37.20400  -6.94400  41.76900  1.000 47.80764 ? 402 VAL B N   1 
ATOM   6038 C CA  . VAL B 1 402 ? 37.63100  -8.17100  41.10000  1.000 55.54066 ? 402 VAL B CA  1 
ATOM   6039 C C   . VAL B 1 402 ? 37.06700  -9.39700  41.81300  1.000 55.65210 ? 402 VAL B C   1 
ATOM   6040 O O   . VAL B 1 402 ? 36.54800  -10.32200 41.17600  1.000 62.86960 ? 402 VAL B O   1 
ATOM   6041 C CB  . VAL B 1 402 ? 39.16600  -8.21900  41.00700  1.000 51.08268 ? 402 VAL B CB  1 
ATOM   6042 C CG1 . VAL B 1 402 ? 39.62800  -9.54900  40.43300  1.000 52.60677 ? 402 VAL B CG1 1 
ATOM   6043 C CG2 . VAL B 1 402 ? 39.67500  -7.06800  40.15500  1.000 45.61914 ? 402 VAL B CG2 1 
ATOM   6044 N N   . ALA B 1 403 ? 37.15100  -9.42300  43.14000  1.000 54.93032 ? 403 ALA B N   1 
ATOM   6045 C CA  . ALA B 1 403 ? 36.58900  -10.52700 43.91900  1.000 63.37031 ? 403 ALA B CA  1 
ATOM   6046 C C   . ALA B 1 403 ? 35.92500  -10.02000 45.19800  1.000 56.47489 ? 403 ALA B C   1 
ATOM   6047 O O   . ALA B 1 403 ? 34.78700  -9.54800  45.17500  1.000 55.64132 ? 403 ALA B O   1 
ATOM   6048 C CB  . ALA B 1 403 ? 37.66800  -11.55400 44.25200  1.000 61.06342 ? 403 ALA B CB  1 
HETATM 6049 N N1  . PLP C 2 .   ? 14.44400  32.45800  80.83700  1.000 27.39533 ? 501 PLP A N1  1 
HETATM 6050 C C2  . PLP C 2 .   ? 14.96300  33.18500  81.89100  1.000 26.43461 ? 501 PLP A C2  1 
HETATM 6051 C C2A . PLP C 2 .   ? 14.28900  33.11700  83.23100  1.000 25.86286 ? 501 PLP A C2A 1 
HETATM 6052 C C3  . PLP C 2 .   ? 16.09800  33.97400  81.70700  1.000 24.33201 ? 501 PLP A C3  1 
HETATM 6053 O O3  . PLP C 2 .   ? 16.63500  34.70000  82.74000  1.000 27.96029 ? 501 PLP A O3  1 
HETATM 6054 C C4  . PLP C 2 .   ? 16.70300  34.01900  80.45900  1.000 26.78125 ? 501 PLP A C4  1 
HETATM 6055 C C4A . PLP C 2 .   ? 17.93900  34.84200  80.26900  1.000 26.81479 ? 501 PLP A C4A 1 
HETATM 6056 C C5  . PLP C 2 .   ? 16.16900  33.28600  79.40500  1.000 26.56515 ? 501 PLP A C5  1 
HETATM 6057 C C6  . PLP C 2 .   ? 15.03800  32.50500  79.59300  1.000 22.35852 ? 501 PLP A C6  1 
HETATM 6058 C C5A . PLP C 2 .   ? 16.81100  33.33900  78.04600  1.000 26.07808 ? 501 PLP A C5A 1 
HETATM 6059 O O4P . PLP C 2 .   ? 18.02400  32.63700  78.06300  1.000 29.38179 ? 501 PLP A O4P 1 
HETATM 6060 P P   . PLP C 2 .   ? 19.11400  32.97900  76.93000  1.000 25.36305 ? 501 PLP A P   1 
HETATM 6061 O O1P . PLP C 2 .   ? 20.25900  32.00900  77.11900  1.000 23.29302 ? 501 PLP A O1P 1 
HETATM 6062 O O2P . PLP C 2 .   ? 19.58900  34.39900  77.11100  1.000 23.58149 ? 501 PLP A O2P 1 
HETATM 6063 O O3P . PLP C 2 .   ? 18.47500  32.78800  75.57200  1.000 21.19436 ? 501 PLP A O3P 1 
HETATM 6064 N N1  . PLP D 2 .   ? 21.99300  22.74700  53.31200  1.000 16.91212 ? 501 PLP B N1  1 
HETATM 6065 C C2  . PLP D 2 .   ? 22.99500  22.03000  52.69200  1.000 16.54868 ? 501 PLP B C2  1 
HETATM 6066 C C2A . PLP D 2 .   ? 23.11300  22.05000  51.19600  1.000 16.28447 ? 501 PLP B C2A 1 
HETATM 6067 C C3  . PLP D 2 .   ? 23.88700  21.28700  53.45300  1.000 16.63226 ? 501 PLP B C3  1 
HETATM 6068 O O3  . PLP D 2 .   ? 24.88500  20.57000  52.84800  1.000 18.15674 ? 501 PLP B O3  1 
HETATM 6069 C C4  . PLP D 2 .   ? 23.78100  21.27300  54.83700  1.000 17.66855 ? 501 PLP B C4  1 
HETATM 6070 C C4A . PLP D 2 .   ? 24.79300  20.49400  55.61800  1.000 19.25439 ? 501 PLP B C4A 1 
HETATM 6071 C C5  . PLP D 2 .   ? 22.76100  21.99300  55.46000  1.000 19.38767 ? 501 PLP B C5  1 
HETATM 6072 C C6  . PLP D 2 .   ? 21.87800  22.73400  54.68300  1.000 16.53542 ? 501 PLP B C6  1 
HETATM 6073 C C5A . PLP D 2 .   ? 22.59800  22.01100  56.96400  1.000 16.00532 ? 501 PLP B C5A 1 
HETATM 6074 O O4P . PLP D 2 .   ? 23.81700  22.41700  57.53500  1.000 22.26079 ? 501 PLP B O4P 1 
HETATM 6075 P P   . PLP D 2 .   ? 24.14100  22.16300  59.08500  1.000 15.70944 ? 501 PLP B P   1 
HETATM 6076 O O1P . PLP D 2 .   ? 22.86500  22.31700  59.87900  1.000 16.19413 ? 501 PLP B O1P 1 
HETATM 6077 O O2P . PLP D 2 .   ? 25.17300  23.18500  59.51000  1.000 20.01854 ? 501 PLP B O2P 1 
HETATM 6078 O O3P . PLP D 2 .   ? 24.71900  20.77600  59.25500  1.000 18.64719 ? 501 PLP B O3P 1 
HETATM 6079 O O   . HOH E 3 .   ? 30.20300  53.26300  103.30500 1.000 34.61525 ? 601 HOH A O   1 
HETATM 6080 O O   . HOH E 3 .   ? 27.19700  -2.45900  62.07800  1.000 34.78978 ? 602 HOH A O   1 
HETATM 6081 O O   . HOH E 3 .   ? 10.71800  8.01800   79.70300  1.000 22.98624 ? 603 HOH A O   1 
HETATM 6082 O O   . HOH E 3 .   ? 18.29900  60.59900  88.58100  1.000 31.28417 ? 604 HOH A O   1 
HETATM 6083 O O   . HOH E 3 .   ? -3.75700  20.03900  93.25600  1.000 38.78585 ? 605 HOH A O   1 
HETATM 6084 O O   . HOH E 3 .   ? 24.42900  59.39900  91.06500  1.000 28.05080 ? 606 HOH A O   1 
HETATM 6085 O O   . HOH E 3 .   ? 34.06700  51.94400  101.79500 1.000 40.84125 ? 607 HOH A O   1 
HETATM 6086 O O   . HOH E 3 .   ? -2.23400  38.98900  81.64800  1.000 38.67266 ? 608 HOH A O   1 
HETATM 6087 O O   . HOH E 3 .   ? 26.64800  22.15300  98.01600  1.000 32.47010 ? 609 HOH A O   1 
HETATM 6088 O O   . HOH E 3 .   ? 9.08800   51.66500  92.55500  1.000 32.10957 ? 610 HOH A O   1 
HETATM 6089 O O   . HOH E 3 .   ? 13.07900  11.43700  86.45100  1.000 27.71565 ? 611 HOH A O   1 
HETATM 6090 O O   . HOH E 3 .   ? 26.42200  33.86500  83.87800  1.000 18.20655 ? 612 HOH A O   1 
HETATM 6091 O O   . HOH E 3 .   ? 8.59200   40.65400  84.53500  1.000 28.75492 ? 613 HOH A O   1 
HETATM 6092 O O   . HOH E 3 .   ? 7.25100   15.46600  87.39400  1.000 33.61279 ? 614 HOH A O   1 
HETATM 6093 O O   . HOH E 3 .   ? 4.68000   35.43400  103.67500 1.000 29.62148 ? 615 HOH A O   1 
HETATM 6094 O O   . HOH E 3 .   ? -4.55300  22.43700  91.07700  1.000 37.18315 ? 616 HOH A O   1 
HETATM 6095 O O   . HOH E 3 .   ? 20.16100  58.77600  101.62400 1.000 38.94084 ? 617 HOH A O   1 
HETATM 6096 O O   . HOH E 3 .   ? 19.58300  12.36100  89.34600  1.000 28.34868 ? 618 HOH A O   1 
HETATM 6097 O O   . HOH E 3 .   ? 38.45300  19.55700  80.04800  1.000 13.92539 ? 619 HOH A O   1 
HETATM 6098 O O   . HOH E 3 .   ? 33.05900  26.76500  88.15300  1.000 26.29837 ? 620 HOH A O   1 
HETATM 6099 O O   . HOH E 3 .   ? 6.89000   33.42000  86.05300  1.000 24.55561 ? 621 HOH A O   1 
HETATM 6100 O O   . HOH E 3 .   ? 22.87700  36.15200  91.30400  1.000 18.23668 ? 622 HOH A O   1 
HETATM 6101 O O   . HOH E 3 .   ? 37.45300  -0.11800  59.17800  1.000 39.32145 ? 623 HOH A O   1 
HETATM 6102 O O   . HOH E 3 .   ? 21.88600  15.95300  59.09000  1.000 27.79912 ? 624 HOH A O   1 
HETATM 6103 O O   . HOH E 3 .   ? 0.72800   32.72700  71.06600  1.000 29.35146 ? 625 HOH A O   1 
HETATM 6104 O O   . HOH E 3 .   ? 12.57400  21.76000  94.47500  1.000 31.15186 ? 626 HOH A O   1 
HETATM 6105 O O   . HOH E 3 .   ? 20.92600  2.17100   56.58600  1.000 28.16727 ? 627 HOH A O   1 
HETATM 6106 O O   . HOH E 3 .   ? 29.91200  28.24300  98.94900  1.000 20.44776 ? 628 HOH A O   1 
HETATM 6107 O O   . HOH E 3 .   ? 12.13500  61.81400  92.58000  1.000 27.64343 ? 629 HOH A O   1 
HETATM 6108 O O   . HOH E 3 .   ? 14.29300  27.87500  100.40300 1.000 29.86242 ? 630 HOH A O   1 
HETATM 6109 O O   . HOH E 3 .   ? 30.24000  37.89100  100.91300 1.000 19.72636 ? 631 HOH A O   1 
HETATM 6110 O O   . HOH E 3 .   ? 9.67300   28.77000  93.34700  1.000 23.88109 ? 632 HOH A O   1 
HETATM 6111 O O   . HOH E 3 .   ? 24.79500  54.36700  105.03000 1.000 37.06324 ? 633 HOH A O   1 
HETATM 6112 O O   . HOH E 3 .   ? 5.87400   13.99200  81.65100  1.000 30.01178 ? 634 HOH A O   1 
HETATM 6113 O O   . HOH E 3 .   ? 15.92400  38.97900  83.55600  1.000 23.79202 ? 635 HOH A O   1 
HETATM 6114 O O   . HOH E 3 .   ? 18.82100  33.51700  92.26600  1.000 27.43921 ? 636 HOH A O   1 
HETATM 6115 O O   . HOH E 3 .   ? 13.42600  18.89600  88.11500  1.000 24.38970 ? 637 HOH A O   1 
HETATM 6116 O O   . HOH E 3 .   ? -7.90100  31.93600  78.00100  1.000 40.69723 ? 638 HOH A O   1 
HETATM 6117 O O   . HOH E 3 .   ? -7.45900  34.25900  84.04100  1.000 33.07349 ? 639 HOH A O   1 
HETATM 6118 O O   . HOH E 3 .   ? 13.34500  40.60600  73.67400  1.000 38.17485 ? 640 HOH A O   1 
HETATM 6119 O O   . HOH E 3 .   ? 9.99900   17.95100  66.41000  1.000 22.86323 ? 641 HOH A O   1 
HETATM 6120 O O   . HOH E 3 .   ? 29.30200  22.99500  94.55600  1.000 33.29850 ? 642 HOH A O   1 
HETATM 6121 O O   . HOH E 3 .   ? 14.35400  42.99900  84.41300  1.000 35.38326 ? 643 HOH A O   1 
HETATM 6122 O O   . HOH E 3 .   ? 32.47300  47.24900  88.29500  1.000 28.90928 ? 644 HOH A O   1 
HETATM 6123 O O   . HOH E 3 .   ? 23.26800  29.93900  101.64300 1.000 27.09430 ? 645 HOH A O   1 
HETATM 6124 O O   . HOH E 3 .   ? 6.87200   51.54500  85.55300  1.000 36.58094 ? 646 HOH A O   1 
HETATM 6125 O O   . HOH E 3 .   ? 29.45500  50.46900  88.24900  1.000 36.31383 ? 647 HOH A O   1 
HETATM 6126 O O   . HOH E 3 .   ? 24.85500  29.78700  71.21100  1.000 23.51122 ? 648 HOH A O   1 
HETATM 6127 O O   . HOH E 3 .   ? 27.73900  36.15700  102.77600 1.000 31.37532 ? 649 HOH A O   1 
HETATM 6128 O O   . HOH E 3 .   ? 33.54800  34.62300  96.41900  1.000 20.51466 ? 650 HOH A O   1 
HETATM 6129 O O   . HOH E 3 .   ? 7.82200   48.19000  92.10200  1.000 34.83264 ? 651 HOH A O   1 
HETATM 6130 O O   . HOH E 3 .   ? 9.43400   35.55400  85.72600  1.000 24.55673 ? 652 HOH A O   1 
HETATM 6131 O O   . HOH E 3 .   ? 32.452    36.724    86.001    1.000 19.40353 ? 653 HOH A O   1 
HETATM 6132 O O   . HOH E 3 .   ? 31.38700  38.15800  83.37000  1.000 16.56034 ? 654 HOH A O   1 
HETATM 6133 O O   . HOH E 3 .   ? 5.94000   35.59400  105.48000 1.000 30.61493 ? 655 HOH A O   1 
HETATM 6134 O O   . HOH E 3 .   ? 31.01900  -4.77400  51.48300  1.000 29.64851 ? 656 HOH A O   1 
HETATM 6135 O O   . HOH E 3 .   ? 23.65300  17.50600  98.92000  1.000 35.99763 ? 657 HOH A O   1 
HETATM 6136 O O   . HOH E 3 .   ? -3.58600  53.73500  78.23800  1.000 32.35240 ? 658 HOH A O   1 
HETATM 6137 O O   . HOH E 3 .   ? 27.69200  53.42000  88.11400  1.000 31.73184 ? 659 HOH A O   1 
HETATM 6138 O O   . HOH E 3 .   ? 18.94600  7.28300   91.91700  1.000 45.70205 ? 660 HOH A O   1 
HETATM 6139 O O   . HOH E 3 .   ? 1.34300   36.82500  90.77100  1.000 37.67632 ? 661 HOH A O   1 
HETATM 6140 O O   . HOH E 3 .   ? 11.99400  48.44400  103.32800 1.000 32.94079 ? 662 HOH A O   1 
HETATM 6141 O O   . HOH E 3 .   ? 12.24800  36.42100  83.41100  1.000 26.21450 ? 663 HOH A O   1 
HETATM 6142 O O   . HOH E 3 .   ? 10.45700  42.30800  80.28800  1.000 31.23218 ? 664 HOH A O   1 
HETATM 6143 O O   . HOH E 3 .   ? 24.51900  7.58800   78.49000  1.000 36.54042 ? 665 HOH A O   1 
HETATM 6144 O O   . HOH E 3 .   ? 15.01900  36.21300  84.22400  1.000 23.38579 ? 666 HOH A O   1 
HETATM 6145 O O   . HOH E 3 .   ? 43.10200  3.15600   77.54300  1.000 28.22129 ? 667 HOH A O   1 
HETATM 6146 O O   . HOH E 3 .   ? 19.58200  27.91700  83.99900  1.000 25.79885 ? 668 HOH A O   1 
HETATM 6147 O O   . HOH E 3 .   ? 11.11900  31.44800  101.48500 1.000 26.46848 ? 669 HOH A O   1 
HETATM 6148 O O   . HOH E 3 .   ? 19.45200  11.39200  84.82900  1.000 29.09447 ? 670 HOH A O   1 
HETATM 6149 O O   . HOH E 3 .   ? 40.25400  16.42000  78.00600  1.000 15.87543 ? 671 HOH A O   1 
HETATM 6150 O O   . HOH E 3 .   ? 22.71700  21.00600  70.80300  1.000 23.71810 ? 672 HOH A O   1 
HETATM 6151 O O   . HOH E 3 .   ? 38.45451  6.14700   72.67325  0.50  32.48606 ? 673 HOH A O   1 
HETATM 6152 O O   . HOH E 3 .   ? 34.37900  48.27600  99.67000  1.000 30.63497 ? 674 HOH A O   1 
HETATM 6153 O O   . HOH E 3 .   ? 26.75900  33.76400  80.14400  1.000 18.90508 ? 675 HOH A O   1 
HETATM 6154 O O   . HOH E 3 .   ? 4.40700   18.03800  95.81400  1.000 38.50137 ? 676 HOH A O   1 
HETATM 6155 O O   . HOH E 3 .   ? 12.19700  49.82900  87.38400  1.000 28.65860 ? 677 HOH A O   1 
HETATM 6156 O O   . HOH E 3 .   ? 32.69400  48.81800  97.53000  1.000 25.39037 ? 678 HOH A O   1 
HETATM 6157 O O   . HOH E 3 .   ? 27.80200  58.80500  96.10800  1.000 28.78127 ? 679 HOH A O   1 
HETATM 6158 O O   . HOH E 3 .   ? 31.61200  28.78400  87.11000  1.000 24.04355 ? 680 HOH A O   1 
HETATM 6159 O O   . HOH E 3 .   ? 23.57800  35.37700  104.79700 1.000 28.27918 ? 681 HOH A O   1 
HETATM 6160 O O   . HOH E 3 .   ? 1.78900   37.77900  93.51500  1.000 31.18059 ? 682 HOH A O   1 
HETATM 6161 O O   . HOH E 3 .   ? 11.07500  32.24400  79.88400  1.000 23.64814 ? 683 HOH A O   1 
HETATM 6162 O O   . HOH E 3 .   ? 27.23100  38.13500  82.84000  1.000 17.11564 ? 684 HOH A O   1 
HETATM 6163 O O   . HOH E 3 .   ? 31.56100  36.32800  99.04000  1.000 24.60790 ? 685 HOH A O   1 
HETATM 6164 O O   . HOH E 3 .   ? 28.18400  32.02900  89.61600  1.000 16.32778 ? 686 HOH A O   1 
HETATM 6165 O O   . HOH E 3 .   ? 36.07400  13.13700  77.46500  1.000 24.20244 ? 687 HOH A O   1 
HETATM 6166 O O   . HOH E 3 .   ? 16.77200  9.27400   76.90000  1.000 27.42400 ? 688 HOH A O   1 
HETATM 6167 O O   . HOH E 3 .   ? 18.23400  8.47100   82.41700  1.000 31.41824 ? 689 HOH A O   1 
HETATM 6168 O O   . HOH E 3 .   ? 12.51000  33.67000  86.69300  1.000 21.84599 ? 690 HOH A O   1 
HETATM 6169 O O   . HOH E 3 .   ? 7.11900   55.32400  98.36900  1.000 35.27828 ? 691 HOH A O   1 
HETATM 6170 O O   . HOH E 3 .   ? 30.40600  57.28700  93.66200  1.000 36.34096 ? 692 HOH A O   1 
HETATM 6171 O O   . HOH E 3 .   ? 0.54600   29.86400  91.26700  1.000 32.85275 ? 693 HOH A O   1 
HETATM 6172 O O   . HOH E 3 .   ? -0.77100  14.93700  91.73100  1.000 39.57649 ? 694 HOH A O   1 
HETATM 6173 O O   . HOH E 3 .   ? 21.55300  13.25300  75.97800  1.000 21.49158 ? 695 HOH A O   1 
HETATM 6174 O O   . HOH E 3 .   ? 0.20100   15.82500  89.03500  1.000 34.58318 ? 696 HOH A O   1 
HETATM 6175 O O   . HOH E 3 .   ? 25.17100  18.65500  69.57100  1.000 31.04864 ? 697 HOH A O   1 
HETATM 6176 O O   . HOH E 3 .   ? 9.97000   40.50100  100.21000 1.000 28.81619 ? 698 HOH A O   1 
HETATM 6177 O O   . HOH E 3 .   ? 13.92900  39.57800  77.76300  1.000 25.94626 ? 699 HOH A O   1 
HETATM 6178 O O   . HOH E 3 .   ? 21.73500  11.68400  83.33800  1.000 21.23848 ? 700 HOH A O   1 
HETATM 6179 O O   . HOH E 3 .   ? 19.28700  49.73900  83.96300  1.000 28.81899 ? 701 HOH A O   1 
HETATM 6180 O O   . HOH E 3 .   ? 32.61300  9.89300   86.19500  1.000 22.34659 ? 702 HOH A O   1 
HETATM 6181 O O   . HOH E 3 .   ? 23.73200  14.53100  72.69200  1.000 32.41472 ? 703 HOH A O   1 
HETATM 6182 O O   . HOH E 3 .   ? 22.69800  10.78900  76.30000  1.000 26.82553 ? 704 HOH A O   1 
HETATM 6183 O O   . HOH E 3 .   ? 8.78000   14.45100  81.60300  1.000 26.19967 ? 705 HOH A O   1 
HETATM 6184 O O   . HOH E 3 .   ? 33.47300  26.67800  83.11500  1.000 24.75722 ? 706 HOH A O   1 
HETATM 6185 O O   . HOH E 3 .   ? 30.58700  53.93300  100.61700 1.000 37.32884 ? 707 HOH A O   1 
HETATM 6186 O O   . HOH E 3 .   ? 28.98100  10.72600  59.35000  1.000 20.33559 ? 708 HOH A O   1 
HETATM 6187 O O   . HOH E 3 .   ? 28.84400  48.96900  85.92900  1.000 30.71096 ? 709 HOH A O   1 
HETATM 6188 O O   . HOH E 3 .   ? 27.17200  21.66900  92.05300  1.000 23.74213 ? 710 HOH A O   1 
HETATM 6189 O O   . HOH E 3 .   ? 22.11400  42.23000  106.64200 1.000 28.69255 ? 711 HOH A O   1 
HETATM 6190 O O   . HOH E 3 .   ? 0.00300   25.48500  98.15200  1.000 31.85347 ? 712 HOH A O   1 
HETATM 6191 O O   . HOH E 3 .   ? 11.83200  14.00300  69.51900  1.000 25.93254 ? 713 HOH A O   1 
HETATM 6192 O O   . HOH E 3 .   ? 25.14200  38.29600  88.87700  1.000 18.88295 ? 714 HOH A O   1 
HETATM 6193 O O   . HOH E 3 .   ? 7.83900   33.92400  108.36400 1.000 37.40016 ? 715 HOH A O   1 
HETATM 6194 O O   . HOH E 3 .   ? 33.60300  5.76500   77.38100  1.000 32.11405 ? 716 HOH A O   1 
HETATM 6195 O O   . HOH E 3 .   ? 42.434    7.837     70.643    1.000 33.29036 ? 717 HOH A O   1 
HETATM 6196 O O   . HOH E 3 .   ? 29.66200  10.11800  73.92000  1.000 23.44304 ? 718 HOH A O   1 
HETATM 6197 O O   . HOH E 3 .   ? 13.40600  30.88300  86.34900  1.000 25.96836 ? 719 HOH A O   1 
HETATM 6198 O O   . HOH E 3 .   ? 38.66600  5.05600   79.08900  1.000 26.40398 ? 720 HOH A O   1 
HETATM 6199 O O   . HOH E 3 .   ? 8.04600   47.58300  103.12800 1.000 37.40885 ? 721 HOH A O   1 
HETATM 6200 O O   . HOH E 3 .   ? 9.29600   53.40100  78.31000  1.000 41.77043 ? 722 HOH A O   1 
HETATM 6201 O O   . HOH E 3 .   ? 20.23000  49.20600  106.74100 1.000 40.01821 ? 723 HOH A O   1 
HETATM 6202 O O   . HOH E 3 .   ? 35.55100  28.90900  85.95700  1.000 19.84385 ? 724 HOH A O   1 
HETATM 6203 O O   . HOH E 3 .   ? 13.89600  28.82100  89.12100  1.000 23.62300 ? 725 HOH A O   1 
HETATM 6204 O O   . HOH E 3 .   ? 28.02100  10.92600  71.67800  1.000 26.23034 ? 726 HOH A O   1 
HETATM 6205 O O   . HOH E 3 .   ? -1.61800  32.11100  63.10100  1.000 38.07420 ? 727 HOH A O   1 
HETATM 6206 O O   . HOH E 3 .   ? 7.73800   39.69700  88.77000  1.000 26.25201 ? 728 HOH A O   1 
HETATM 6207 O O   . HOH E 3 .   ? 16.17400  10.65800  70.61300  1.000 33.01718 ? 729 HOH A O   1 
HETATM 6208 O O   . HOH E 3 .   ? -3.35200  37.41500  77.89600  1.000 28.77819 ? 730 HOH A O   1 
HETATM 6209 O O   . HOH E 3 .   ? 12.43200  51.31300  105.24800 1.000 40.35808 ? 731 HOH A O   1 
HETATM 6210 O O   . HOH E 3 .   ? 15.02700  6.28700   80.00400  1.000 30.33102 ? 732 HOH A O   1 
HETATM 6211 O O   . HOH E 3 .   ? 15.69200  43.91800  107.78600 1.000 32.72588 ? 733 HOH A O   1 
HETATM 6212 O O   . HOH E 3 .   ? 34.09700  7.05400   81.66400  1.000 26.29780 ? 734 HOH A O   1 
HETATM 6213 O O   . HOH E 3 .   ? 26.14600  8.19700   70.37100  1.000 36.27874 ? 735 HOH A O   1 
HETATM 6214 O O   . HOH E 3 .   ? 20.02600  13.12600  78.27200  1.000 30.00985 ? 736 HOH A O   1 
HETATM 6215 O O   . HOH E 3 .   ? 21.84200  18.38300  71.49300  1.000 31.80822 ? 737 HOH A O   1 
HETATM 6216 O O   . HOH E 3 .   ? 15.17500  1.84600   60.62700  1.000 35.95526 ? 738 HOH A O   1 
HETATM 6217 O O   . HOH E 3 .   ? 20.33200  29.89600  85.70100  1.000 27.88514 ? 739 HOH A O   1 
HETATM 6218 O O   . HOH E 3 .   ? 10.95400  38.74200  83.32900  1.000 23.09037 ? 740 HOH A O   1 
HETATM 6219 O O   . HOH E 3 .   ? 26.14600  27.36500  70.51400  1.000 22.59900 ? 741 HOH A O   1 
HETATM 6220 O O   . HOH E 3 .   ? 10.99700  40.85700  106.15300 1.000 31.41308 ? 742 HOH A O   1 
HETATM 6221 O O   . HOH E 3 .   ? 30.52100  55.70900  89.16700  1.000 34.08925 ? 743 HOH A O   1 
HETATM 6222 O O   . HOH E 3 .   ? 29.10000  20.10800  93.13900  1.000 17.11461 ? 744 HOH A O   1 
HETATM 6223 O O   . HOH E 3 .   ? 12.74100  39.03100  107.04000 1.000 29.86775 ? 745 HOH A O   1 
HETATM 6224 O O   . HOH E 3 .   ? 19.42600  33.19400  101.28000 1.000 30.61390 ? 746 HOH A O   1 
HETATM 6225 O O   . HOH E 3 .   ? 28.27700  38.55200  80.29500  1.000 19.07660 ? 747 HOH A O   1 
HETATM 6226 O O   . HOH E 3 .   ? 9.73300   58.35200  88.22600  1.000 27.17717 ? 748 HOH A O   1 
HETATM 6227 O O   . HOH E 3 .   ? 11.92200  40.39100  81.16000  1.000 25.55251 ? 749 HOH A O   1 
HETATM 6228 O O   . HOH E 3 .   ? 21.30800  60.05700  87.65000  1.000 35.16386 ? 750 HOH A O   1 
HETATM 6229 O O   . HOH E 3 .   ? 5.42300   16.89900  68.29500  1.000 31.38601 ? 751 HOH A O   1 
HETATM 6230 O O   . HOH E 3 .   ? 20.42400  43.12900  87.25800  1.000 31.50988 ? 752 HOH A O   1 
HETATM 6231 O O   . HOH E 3 .   ? 25.36200  36.11300  82.99400  1.000 22.23502 ? 753 HOH A O   1 
HETATM 6232 O O   . HOH E 3 .   ? 20.32800  11.33100  80.32200  1.000 26.22612 ? 754 HOH A O   1 
HETATM 6233 O O   . HOH E 3 .   ? 22.57900  51.11200  106.75800 1.000 40.51288 ? 755 HOH A O   1 
HETATM 6234 O O   . HOH E 3 .   ? 10.99600  53.06600  104.31200 1.000 39.62028 ? 756 HOH A O   1 
HETATM 6235 O O   . HOH E 3 .   ? -1.75100  21.72200  63.47300  1.000 39.26252 ? 757 HOH A O   1 
HETATM 6236 O O   . HOH E 3 .   ? 0.07900   41.13100  86.32100  1.000 34.75582 ? 758 HOH A O   1 
HETATM 6237 O O   . HOH E 3 .   ? 33.36800  15.00100  76.07900  1.000 27.97863 ? 759 HOH A O   1 
HETATM 6238 O O   . HOH E 3 .   ? 15.42100  21.11000  96.18800  1.000 36.97146 ? 760 HOH A O   1 
HETATM 6239 O O   . HOH E 3 .   ? 12.19100  12.53300  83.66000  1.000 24.59396 ? 761 HOH A O   1 
HETATM 6240 O O   . HOH E 3 .   ? 3.83000   23.29800  94.90400  1.000 30.42440 ? 762 HOH A O   1 
HETATM 6241 O O   . HOH E 3 .   ? 27.81600  32.15500  73.26300  1.000 16.60103 ? 763 HOH A O   1 
HETATM 6242 O O   . HOH E 3 .   ? 46.561    6.222     77.826    1.000 33.60799 ? 764 HOH A O   1 
HETATM 6243 O O   . HOH E 3 .   ? 36.25000  13.45400  82.19600  1.000 32.58977 ? 765 HOH A O   1 
HETATM 6244 O O   . HOH E 3 .   ? 11.28600  60.21300  88.91300  1.000 28.17558 ? 766 HOH A O   1 
HETATM 6245 O O   . HOH E 3 .   ? -8.213    18.752    76.378    1.000 43.03599 ? 767 HOH A O   1 
HETATM 6246 O O   . HOH E 3 .   ? 0.01600   19.13500  70.95500  1.000 39.64582 ? 768 HOH A O   1 
HETATM 6247 O O   . HOH E 3 .   ? 13.43200  32.90700  104.76800 1.000 32.40483 ? 769 HOH A O   1 
HETATM 6248 O O   . HOH E 3 .   ? 29.37400  9.31000   84.82000  1.000 28.48556 ? 770 HOH A O   1 
HETATM 6249 O O   . HOH E 3 .   ? 30.58200  20.71500  66.39700  1.000 22.63586 ? 771 HOH A O   1 
HETATM 6250 O O   . HOH E 3 .   ? 7.97500   42.83300  101.01500 1.000 36.21995 ? 772 HOH A O   1 
HETATM 6251 O O   . HOH E 3 .   ? 15.31900  24.14700  102.62200 1.000 33.54361 ? 773 HOH A O   1 
HETATM 6252 O O   . HOH E 3 .   ? 21.30400  48.08300  82.61200  1.000 29.53879 ? 774 HOH A O   1 
HETATM 6253 O O   . HOH E 3 .   ? 7.95500   40.79200  98.41000  1.000 30.16401 ? 775 HOH A O   1 
HETATM 6254 O O   . HOH E 3 .   ? 34.94400  10.19400  86.83000  1.000 26.11218 ? 776 HOH A O   1 
HETATM 6255 O O   . HOH E 3 .   ? 4.15400   37.37100  59.10400  1.000 37.38556 ? 777 HOH A O   1 
HETATM 6256 O O   . HOH E 3 .   ? 6.73100   14.65400  91.45200  1.000 41.10650 ? 778 HOH A O   1 
HETATM 6257 O O   . HOH E 3 .   ? 36.95100  6.57000   83.02100  1.000 35.83819 ? 779 HOH A O   1 
HETATM 6258 O O   . HOH E 3 .   ? 25.28600  55.82300  102.79100 1.000 34.54150 ? 780 HOH A O   1 
HETATM 6259 O O   . HOH E 3 .   ? 22.11000  5.31200   65.64100  1.000 41.22199 ? 781 HOH A O   1 
HETATM 6260 O O   . HOH E 3 .   ? 30.12800  11.70600  76.05300  1.000 24.95904 ? 782 HOH A O   1 
HETATM 6261 O O   . HOH E 3 .   ? -2.99300  34.75000  71.31300  1.000 33.50891 ? 783 HOH A O   1 
HETATM 6262 O O   . HOH E 3 .   ? 33.17300  12.61300  78.62700  1.000 32.71544 ? 784 HOH A O   1 
HETATM 6263 O O   . HOH E 3 .   ? 24.24300  16.63600  70.64800  1.000 31.09262 ? 785 HOH A O   1 
HETATM 6264 O O   . HOH E 3 .   ? 48.00100  7.28800   73.73000  1.000 33.53797 ? 786 HOH A O   1 
HETATM 6265 O O   . HOH E 3 .   ? 26.49400  -0.27500  95.83700  1.000 42.00292 ? 787 HOH A O   1 
HETATM 6266 O O   . HOH E 3 .   ? -8.72400  34.90700  77.16300  1.000 46.46545 ? 788 HOH A O   1 
HETATM 6267 O O   . HOH E 3 .   ? 7.84400   41.62400  76.27800  1.000 32.75866 ? 789 HOH A O   1 
HETATM 6268 O O   . HOH E 3 .   ? 2.99200   31.23500  100.45600 1.000 31.60121 ? 790 HOH A O   1 
HETATM 6269 O O   . HOH E 3 .   ? 0.08600   40.49000  88.75300  1.000 44.47426 ? 791 HOH A O   1 
HETATM 6270 O O   . HOH E 3 .   ? 4.13700   50.57200  88.26800  1.000 36.10549 ? 792 HOH A O   1 
HETATM 6271 O O   . HOH E 3 .   ? 6.76000   50.30600  97.21700  1.000 33.80001 ? 793 HOH A O   1 
HETATM 6272 O O   . HOH E 3 .   ? 1.74600   31.52100  98.21000  1.000 33.48168 ? 794 HOH A O   1 
HETATM 6273 O O   . HOH E 3 .   ? 12.83200  29.93900  99.82600  1.000 25.84564 ? 795 HOH A O   1 
HETATM 6274 O O   . HOH E 3 .   ? 27.71700  10.37700  88.67100  1.000 23.79310 ? 796 HOH A O   1 
HETATM 6275 O O   . HOH E 3 .   ? 4.94900   41.49300  84.07400  1.000 39.55013 ? 797 HOH A O   1 
HETATM 6276 O O   . HOH E 3 .   ? 29.27100  56.51300  100.15300 1.000 31.65009 ? 798 HOH A O   1 
HETATM 6277 O O   . HOH E 3 .   ? 5.785     32.166    105.738   1.000 29.80129 ? 799 HOH A O   1 
HETATM 6278 O O   . HOH E 3 .   ? 4.01200   49.24500  90.42800  1.000 35.29578 ? 800 HOH A O   1 
HETATM 6279 O O   . HOH E 3 .   ? 25.76100  12.25100  71.87100  1.000 30.33454 ? 801 HOH A O   1 
HETATM 6280 O O   . HOH E 3 .   ? 29.689    47.171    109.350   1.000 34.61896 ? 802 HOH A O   1 
HETATM 6281 O O   . HOH E 3 .   ? 21.28400  31.71300  102.60900 1.000 31.81301 ? 803 HOH A O   1 
HETATM 6282 O O   . HOH E 3 .   ? 3.579     43.386    94.090    1.000 31.65066 ? 804 HOH A O   1 
HETATM 6283 O O   . HOH E 3 .   ? -0.693    15.292    78.396    1.000 37.27325 ? 805 HOH A O   1 
HETATM 6284 O O   . HOH E 3 .   ? 10.95100  62.31100  90.52100  1.000 26.75378 ? 806 HOH A O   1 
HETATM 6285 O O   . HOH E 3 .   ? 6.43200   41.03500  87.12600  1.000 30.54092 ? 807 HOH A O   1 
HETATM 6286 O O   . HOH E 3 .   ? 14.68900  40.52100  81.74600  1.000 25.36527 ? 808 HOH A O   1 
HETATM 6287 O O   . HOH E 3 .   ? 4.74200   49.37700  95.87800  1.000 36.06928 ? 809 HOH A O   1 
HETATM 6288 O O   . HOH E 3 .   ? 35.40300  12.78800  80.00300  1.000 27.14826 ? 810 HOH A O   1 
HETATM 6289 O O   . HOH E 3 .   ? 37.379    6.915     87.717    1.000 34.82397 ? 811 HOH A O   1 
HETATM 6290 O O   . HOH E 3 .   ? 24.18500  21.29600  94.86500  1.000 34.75302 ? 812 HOH A O   1 
HETATM 6291 O O   . HOH E 3 .   ? 14.77900  35.16600  86.38500  1.000 25.31137 ? 813 HOH A O   1 
HETATM 6292 O O   . HOH E 3 .   ? 23.87600  20.70800  92.72100  1.000 25.62284 ? 814 HOH A O   1 
HETATM 6293 O O   . HOH E 3 .   ? 29.41100  8.57600   88.68500  1.000 34.29563 ? 815 HOH A O   1 
HETATM 6294 O O   . HOH E 3 .   ? 5.29000   43.56000  83.13400  1.000 21.17323 ? 816 HOH A O   1 
HETATM 6295 O O   . HOH E 3 .   ? -2.55000  24.68800  98.69900  1.000 32.91143 ? 817 HOH A O   1 
HETATM 6296 O O   . HOH E 3 .   ? 22.33800  32.97200  104.74300 1.000 27.04169 ? 818 HOH A O   1 
HETATM 6297 O O   . HOH E 3 .   ? 4.93800   48.91500  99.55700  1.000 44.24229 ? 819 HOH A O   1 
HETATM 6298 O O   . HOH E 3 .   ? 12.00800  19.35100  96.91200  1.000 40.08767 ? 820 HOH A O   1 
HETATM 6299 O O   . HOH E 3 .   ? 11.89600  15.84300  98.19700  1.000 45.37276 ? 821 HOH A O   1 
HETATM 6300 O O   . HOH E 3 .   ? 18.01700  41.73300  76.70200  1.000 34.43651 ? 822 HOH A O   1 
HETATM 6301 O O   . HOH E 3 .   ? 1.85100   40.80900  75.70400  1.000 31.81862 ? 823 HOH A O   1 
HETATM 6302 O O   . HOH E 3 .   ? 3.32700   42.32100  74.91700  1.000 41.34473 ? 824 HOH A O   1 
HETATM 6303 O O   . HOH F 3 .   ? 14.63600  40.33300  44.83700  1.000 33.27632 ? 601 HOH B O   1 
HETATM 6304 O O   . HOH F 3 .   ? 37.57800  1.64300   53.81000  1.000 28.67086 ? 602 HOH B O   1 
HETATM 6305 O O   . HOH F 3 .   ? 4.98100   22.13800  54.92600  1.000 26.51810 ? 603 HOH B O   1 
HETATM 6306 O O   . HOH F 3 .   ? 27.67700  55.99900  85.80700  1.000 35.22087 ? 604 HOH B O   1 
HETATM 6307 O O   . HOH F 3 .   ? 22.47700  40.90600  61.32900  1.000 22.41826 ? 605 HOH B O   1 
HETATM 6308 O O   . HOH F 3 .   ? 8.88100   0.46600   48.89400  1.000 33.02324 ? 606 HOH B O   1 
HETATM 6309 O O   . HOH F 3 .   ? 17.16200  39.19200  75.77400  1.000 26.27414 ? 607 HOH B O   1 
HETATM 6310 O O   . HOH F 3 .   ? 21.69400  17.75300  35.49600  1.000 30.29394 ? 608 HOH B O   1 
HETATM 6311 O O   . HOH F 3 .   ? 12.73800  34.47100  33.42900  1.000 29.11363 ? 609 HOH B O   1 
HETATM 6312 O O   . HOH F 3 .   ? 35.99800  39.67300  67.17600  1.000 22.51540 ? 610 HOH B O   1 
HETATM 6313 O O   . HOH F 3 .   ? 22.30300  6.79000   40.44800  1.000 19.49161 ? 611 HOH B O   1 
HETATM 6314 O O   . HOH F 3 .   ? 41.56200  15.96500  33.71300  1.000 34.21304 ? 612 HOH B O   1 
HETATM 6315 O O   . HOH F 3 .   ? 42.313    35.784    66.321    1.000 18.64220 ? 613 HOH B O   1 
HETATM 6316 O O   . HOH F 3 .   ? 26.45900  57.56100  80.00200  1.000 31.22692 ? 614 HOH B O   1 
HETATM 6317 O O   . HOH F 3 .   ? 34.65600  19.17500  48.56800  1.000 18.71604 ? 615 HOH B O   1 
HETATM 6318 O O   . HOH F 3 .   ? 38.98700  42.30000  67.37300  1.000 23.28474 ? 616 HOH B O   1 
HETATM 6319 O O   . HOH F 3 .   ? 18.17300  3.48400   45.41600  1.000 28.23129 ? 617 HOH B O   1 
HETATM 6320 O O   . HOH F 3 .   ? 29.12300  10.14300  32.73300  1.000 28.29371 ? 618 HOH B O   1 
HETATM 6321 O O   . HOH F 3 .   ? 39.70900  58.50200  48.01400  1.000 52.45134 ? 619 HOH B O   1 
HETATM 6322 O O   . HOH F 3 .   ? 44.78000  28.70700  43.52800  1.000 37.10763 ? 620 HOH B O   1 
HETATM 6323 O O   . HOH F 3 .   ? 16.19600  5.97600   38.23100  1.000 32.17299 ? 621 HOH B O   1 
HETATM 6324 O O   . HOH F 3 .   ? 41.44400  28.55900  56.65200  1.000 26.23469 ? 622 HOH B O   1 
HETATM 6325 O O   . HOH F 3 .   ? 12.92900  14.24100  41.35200  1.000 29.90084 ? 623 HOH B O   1 
HETATM 6326 O O   . HOH F 3 .   ? 19.03500  39.74500  44.02300  1.000 21.95593 ? 624 HOH B O   1 
HETATM 6327 O O   . HOH F 3 .   ? 37.92400  17.38500  59.85300  1.000 17.88989 ? 625 HOH B O   1 
HETATM 6328 O O   . HOH F 3 .   ? 11.47100  47.43700  48.68500  1.000 35.47506 ? 626 HOH B O   1 
HETATM 6329 O O   . HOH F 3 .   ? 34.01100  21.47200  56.86000  1.000 16.27697 ? 627 HOH B O   1 
HETATM 6330 O O   . HOH F 3 .   ? 20.61000  9.25200   38.09400  1.000 22.83075 ? 628 HOH B O   1 
HETATM 6331 O O   . HOH F 3 .   ? 46.00200  17.69700  43.94000  1.000 28.92657 ? 629 HOH B O   1 
HETATM 6332 O O   . HOH F 3 .   ? 31.33200  31.49600  35.13600  1.000 20.46710 ? 630 HOH B O   1 
HETATM 6333 O O   . HOH F 3 .   ? 41.55900  -3.49400  46.95400  1.000 28.99274 ? 631 HOH B O   1 
HETATM 6334 O O   . HOH F 3 .   ? 17.96200  23.22700  33.62400  1.000 33.65240 ? 632 HOH B O   1 
HETATM 6335 O O   . HOH F 3 .   ? 24.75000  16.23500  51.84700  1.000 19.55094 ? 633 HOH B O   1 
HETATM 6336 O O   . HOH F 3 .   ? 35.49500  16.31300  26.78500  1.000 38.50224 ? 634 HOH B O   1 
HETATM 6337 O O   . HOH F 3 .   ? 19.53400  1.36400   42.03500  1.000 31.47175 ? 635 HOH B O   1 
HETATM 6338 O O   . HOH F 3 .   ? 20.73800  31.24300  31.28000  1.000 40.02885 ? 636 HOH B O   1 
HETATM 6339 O O   . HOH F 3 .   ? 4.74600   20.50400  39.35900  1.000 27.77097 ? 637 HOH B O   1 
HETATM 6340 O O   . HOH F 3 .   ? 14.51600  52.90200  77.15400  1.000 34.92596 ? 638 HOH B O   1 
HETATM 6341 O O   . HOH F 3 .   ? 23.04200  48.03500  48.46500  1.000 36.00760 ? 639 HOH B O   1 
HETATM 6342 O O   . HOH F 3 .   ? 25.73100  26.52200  45.85900  1.000 17.43276 ? 640 HOH B O   1 
HETATM 6343 O O   . HOH F 3 .   ? 23.95700  4.99600   35.94700  1.000 29.40039 ? 641 HOH B O   1 
HETATM 6344 O O   . HOH F 3 .   ? 13.65900  41.28500  61.51200  1.000 21.45586 ? 642 HOH B O   1 
HETATM 6345 O O   . HOH F 3 .   ? 31.63200  45.21200  66.97300  1.000 25.93468 ? 643 HOH B O   1 
HETATM 6346 O O   . HOH F 3 .   ? 41.25100  7.87300   56.27900  1.000 29.51283 ? 644 HOH B O   1 
HETATM 6347 O O   . HOH F 3 .   ? 23.94300  12.65300  50.28900  1.000 24.98547 ? 645 HOH B O   1 
HETATM 6348 O O   . HOH F 3 .   ? 24.23400  26.52100  40.03100  1.000 12.04704 ? 646 HOH B O   1 
HETATM 6349 O O   . HOH F 3 .   ? 24.77000  36.40500  46.28000  1.000 16.47122 ? 647 HOH B O   1 
HETATM 6350 O O   . HOH F 3 .   ? 41.46800  33.21200  44.92800  1.000 35.59436 ? 648 HOH B O   1 
HETATM 6351 O O   . HOH F 3 .   ? 12.73500  38.79500  38.91100  1.000 24.87769 ? 649 HOH B O   1 
HETATM 6352 O O   . HOH F 3 .   ? 17.62400  14.55400  59.02200  1.000 29.74777 ? 650 HOH B O   1 
HETATM 6353 O O   . HOH F 3 .   ? 20.42200  16.35900  49.15100  1.000 23.59386 ? 651 HOH B O   1 
HETATM 6354 O O   . HOH F 3 .   ? 18.81300  29.19400  31.32900  1.000 31.19468 ? 652 HOH B O   1 
HETATM 6355 O O   . HOH F 3 .   ? 19.81600  31.63100  35.85900  1.000 24.10867 ? 653 HOH B O   1 
HETATM 6356 O O   . HOH F 3 .   ? 23.29800  21.53700  47.30900  1.000 14.61206 ? 654 HOH B O   1 
HETATM 6357 O O   . HOH F 3 .   ? 40.25400  18.55000  58.18600  1.000 15.06657 ? 655 HOH B O   1 
HETATM 6358 O O   . HOH F 3 .   ? 20.33800  15.58000  43.03200  1.000 20.53811 ? 656 HOH B O   1 
HETATM 6359 O O   . HOH F 3 .   ? -0.99400  24.16400  41.62800  1.000 33.50413 ? 657 HOH B O   1 
HETATM 6360 O O   . HOH F 3 .   ? 27.06500  19.41100  28.08400  1.000 27.04349 ? 658 HOH B O   1 
HETATM 6361 O O   . HOH F 3 .   ? 29.73000  25.25700  51.95100  1.000 24.44423 ? 659 HOH B O   1 
HETATM 6362 O O   . HOH F 3 .   ? 20.29600  19.46500  46.60300  1.000 17.23312 ? 660 HOH B O   1 
HETATM 6363 O O   . HOH F 3 .   ? 29.05000  51.44800  84.67700  1.000 34.57261 ? 661 HOH B O   1 
HETATM 6364 O O   . HOH F 3 .   ? 19.15700  39.60500  38.04200  1.000 26.33483 ? 662 HOH B O   1 
HETATM 6365 O O   . HOH F 3 .   ? 38.45451  48.87700  72.67325  0.50  34.30589 ? 663 HOH B O   1 
HETATM 6366 O O   . HOH F 3 .   ? 16.00000  2.59800   44.34000  1.000 29.30881 ? 664 HOH B O   1 
HETATM 6367 O O   . HOH F 3 .   ? 31.48500  21.73700  45.85500  1.000 19.72777 ? 665 HOH B O   1 
HETATM 6368 O O   . HOH F 3 .   ? 23.34900  44.53700  78.87700  1.000 34.30511 ? 666 HOH B O   1 
HETATM 6369 O O   . HOH F 3 .   ? 17.70200  47.19300  52.23500  1.000 24.07284 ? 667 HOH B O   1 
HETATM 6370 O O   . HOH F 3 .   ? 25.36200  41.97900  58.04200  1.000 25.11955 ? 668 HOH B O   1 
HETATM 6371 O O   . HOH F 3 .   ? 21.79900  46.01600  57.75800  1.000 28.30077 ? 669 HOH B O   1 
HETATM 6372 O O   . HOH F 3 .   ? 27.33600  33.69800  40.47300  1.000 21.10415 ? 670 HOH B O   1 
HETATM 6373 O O   . HOH F 3 .   ? 16.06100  24.62700  34.35700  1.000 25.35827 ? 671 HOH B O   1 
HETATM 6374 O O   . HOH F 3 .   ? 42.27100  50.13000  67.41100  1.000 26.66491 ? 672 HOH B O   1 
HETATM 6375 O O   . HOH F 3 .   ? 15.60500  26.86200  32.72600  1.000 27.33150 ? 673 HOH B O   1 
HETATM 6376 O O   . HOH F 3 .   ? 32.93200  4.25400   31.82400  1.000 31.86350 ? 674 HOH B O   1 
HETATM 6377 O O   . HOH F 3 .   ? 0.97900   22.98200  44.71800  1.000 36.05634 ? 675 HOH B O   1 
HETATM 6378 O O   . HOH F 3 .   ? 35.24800  16.96300  52.03100  1.000 15.50331 ? 676 HOH B O   1 
HETATM 6379 O O   . HOH F 3 .   ? 42.02300  20.10800  37.44700  1.000 22.06354 ? 677 HOH B O   1 
HETATM 6380 O O   . HOH F 3 .   ? 28.77000  44.15900  68.14400  1.000 27.37374 ? 678 HOH B O   1 
HETATM 6381 O O   . HOH F 3 .   ? 26.12500  25.51400  66.94400  1.000 23.29531 ? 679 HOH B O   1 
HETATM 6382 O O   . HOH F 3 .   ? 38.34000  23.46800  52.71400  1.000 13.78149 ? 680 HOH B O   1 
HETATM 6383 O O   . HOH F 3 .   ? 38.96600  5.01400   54.99400  1.000 33.11739 ? 681 HOH B O   1 
HETATM 6384 O O   . HOH F 3 .   ? 17.23700  40.68000  49.56500  1.000 19.60748 ? 682 HOH B O   1 
HETATM 6385 O O   . HOH F 3 .   ? 41.54300  44.22100  77.39200  1.000 32.93458 ? 683 HOH B O   1 
HETATM 6386 O O   . HOH F 3 .   ? 11.79800  45.36800  57.18100  1.000 34.80502 ? 684 HOH B O   1 
HETATM 6387 O O   . HOH F 3 .   ? 31.39900  0.83000   31.60100  1.000 36.51913 ? 685 HOH B O   1 
HETATM 6388 O O   . HOH F 3 .   ? 26.57600  43.90900  56.43500  1.000 21.56984 ? 686 HOH B O   1 
HETATM 6389 O O   . HOH F 3 .   ? 21.80200  -2.90000  44.77600  1.000 31.98496 ? 687 HOH B O   1 
HETATM 6390 O O   . HOH F 3 .   ? 25.67000  46.95100  54.14100  1.000 29.81939 ? 688 HOH B O   1 
HETATM 6391 O O   . HOH F 3 .   ? 7.82600   38.22300  59.14100  1.000 29.96408 ? 689 HOH B O   1 
HETATM 6392 O O   . HOH F 3 .   ? 31.11700  43.06200  48.23500  1.000 30.44633 ? 690 HOH B O   1 
HETATM 6393 O O   . HOH F 3 .   ? 10.85800  32.60900  34.47400  1.000 32.04755 ? 691 HOH B O   1 
HETATM 6394 O O   . HOH F 3 .   ? 18.58100  23.07200  52.38600  1.000 19.79705 ? 692 HOH B O   1 
HETATM 6395 O O   . HOH F 3 .   ? 15.21800  41.05400  47.81500  1.000 21.22235 ? 693 HOH B O   1 
HETATM 6396 O O   . HOH F 3 .   ? 23.60800  5.46200   46.76500  1.000 18.36088 ? 694 HOH B O   1 
HETATM 6397 O O   . HOH F 3 .   ? 29.33400  43.57600  55.13300  1.000 20.09150 ? 695 HOH B O   1 
HETATM 6398 O O   . HOH F 3 .   ? 39.23600  37.86600  42.34900  1.000 40.02018 ? 696 HOH B O   1 
HETATM 6399 O O   . HOH F 3 .   ? 32.39100  21.49600  60.34300  1.000 13.68631 ? 697 HOH B O   1 
HETATM 6400 O O   . HOH F 3 .   ? 20.18700  14.96100  51.74900  1.000 21.20067 ? 698 HOH B O   1 
HETATM 6401 O O   . HOH F 3 .   ? 29.18500  47.90900  60.63800  1.000 38.69248 ? 699 HOH B O   1 
HETATM 6402 O O   . HOH F 3 .   ? 41.34200  35.45900  50.51300  1.000 18.95602 ? 700 HOH B O   1 
HETATM 6403 O O   . HOH F 3 .   ? 37.02800  6.61800   56.80400  1.000 30.33351 ? 701 HOH B O   1 
HETATM 6404 O O   . HOH F 3 .   ? 40.47100  45.42100  57.78300  1.000 27.44192 ? 702 HOH B O   1 
HETATM 6405 O O   . HOH F 3 .   ? 36.14200  -4.28400  50.12700  1.000 24.90723 ? 703 HOH B O   1 
HETATM 6406 O O   . HOH F 3 .   ? 46.36500  20.97000  49.77400  1.000 19.98513 ? 704 HOH B O   1 
HETATM 6407 O O   . HOH F 3 .   ? 32.78100  43.41100  65.44100  1.000 29.90617 ? 705 HOH B O   1 
HETATM 6408 O O   . HOH F 3 .   ? 42.58200  -1.93600  51.09800  1.000 33.37491 ? 706 HOH B O   1 
HETATM 6409 O O   . HOH F 3 .   ? 26.95000  28.03200  68.07200  1.000 21.72708 ? 707 HOH B O   1 
HETATM 6410 O O   . HOH F 3 .   ? 41.78500  41.65100  63.29700  1.000 32.94668 ? 708 HOH B O   1 
HETATM 6411 O O   . HOH F 3 .   ? 23.34300  15.52600  36.84400  1.000 22.13008 ? 709 HOH B O   1 
HETATM 6412 O O   . HOH F 3 .   ? 42.87600  38.92600  69.17600  1.000 18.96339 ? 710 HOH B O   1 
HETATM 6413 O O   . HOH F 3 .   ? 7.30700   15.59800  45.38600  1.000 43.49553 ? 711 HOH B O   1 
HETATM 6414 O O   . HOH F 3 .   ? 15.45600  25.21300  37.25600  1.000 19.82738 ? 712 HOH B O   1 
HETATM 6415 O O   . HOH F 3 .   ? 15.24600  37.87900  33.35300  1.000 31.62915 ? 713 HOH B O   1 
HETATM 6416 O O   . HOH F 3 .   ? 10.18800  5.02000   40.74000  1.000 31.44079 ? 714 HOH B O   1 
HETATM 6417 O O   . HOH F 3 .   ? 41.95800  13.21700  35.06500  1.000 28.38072 ? 715 HOH B O   1 
HETATM 6418 O O   . HOH F 3 .   ? 29.56500  23.30000  66.51900  1.000 14.16706 ? 716 HOH B O   1 
HETATM 6419 O O   . HOH F 3 .   ? 36.67400  40.99400  65.07900  1.000 29.67026 ? 717 HOH B O   1 
HETATM 6420 O O   . HOH F 3 .   ? 39.38300  -1.96100  35.32400  1.000 32.82532 ? 718 HOH B O   1 
HETATM 6421 O O   . HOH F 3 .   ? 44.69100  52.32000  71.02400  1.000 37.03091 ? 719 HOH B O   1 
HETATM 6422 O O   . HOH F 3 .   ? 28.06300  14.72700  34.62700  1.000 27.24387 ? 720 HOH B O   1 
HETATM 6423 O O   . HOH F 3 .   ? 18.50000  52.45700  82.85800  1.000 27.13043 ? 721 HOH B O   1 
HETATM 6424 O O   . HOH F 3 .   ? 17.30000  14.18800  41.71000  1.000 26.23736 ? 722 HOH B O   1 
HETATM 6425 O O   . HOH F 3 .   ? 41.21900  25.32800  64.21100  1.000 22.35145 ? 723 HOH B O   1 
HETATM 6426 O O   . HOH F 3 .   ? 16.26400  15.41900  48.72900  1.000 21.18038 ? 724 HOH B O   1 
HETATM 6427 O O   . HOH F 3 .   ? 28.34400  43.88900  52.54800  1.000 26.02979 ? 725 HOH B O   1 
HETATM 6428 O O   . HOH F 3 .   ? 42.48300  -0.79100  40.43600  1.000 32.53530 ? 726 HOH B O   1 
HETATM 6429 O O   . HOH F 3 .   ? 44.70000  27.19100  45.68500  1.000 22.79067 ? 727 HOH B O   1 
HETATM 6430 O O   . HOH F 3 .   ? 42.659    26.713    59.848    1.000 23.16019 ? 728 HOH B O   1 
HETATM 6431 O O   . HOH F 3 .   ? 11.02400  10.89400  44.16300  1.000 37.88687 ? 729 HOH B O   1 
HETATM 6432 O O   . HOH F 3 .   ? 52.08300  18.12400  43.66200  1.000 34.61394 ? 730 HOH B O   1 
HETATM 6433 O O   . HOH F 3 .   ? 15.50700  2.19900   51.78700  1.000 41.21931 ? 731 HOH B O   1 
HETATM 6434 O O   . HOH F 3 .   ? 25.56900  42.18100  61.08500  1.000 25.56256 ? 732 HOH B O   1 
HETATM 6435 O O   . HOH F 3 .   ? 36.68700  49.55300  66.18700  1.000 29.80652 ? 733 HOH B O   1 
HETATM 6436 O O   . HOH F 3 .   ? 46.56900  6.69000   48.58700  1.000 24.38266 ? 734 HOH B O   1 
HETATM 6437 O O   . HOH F 3 .   ? 37.11400  11.01500  30.79500  1.000 27.30675 ? 735 HOH B O   1 
HETATM 6438 O O   . HOH F 3 .   ? 24.28200  18.76700  50.76300  1.000 19.39780 ? 736 HOH B O   1 
HETATM 6439 O O   . HOH F 3 .   ? 21.96600  48.89600  54.20200  1.000 29.19690 ? 737 HOH B O   1 
HETATM 6440 O O   . HOH F 3 .   ? 26.96400  2.74500   53.65500  1.000 19.60729 ? 738 HOH B O   1 
HETATM 6441 O O   . HOH F 3 .   ? 20.15900  15.74600  55.57300  1.000 22.24607 ? 739 HOH B O   1 
HETATM 6442 O O   . HOH F 3 .   ? 18.10400  21.38400  45.00500  1.000 19.32254 ? 740 HOH B O   1 
HETATM 6443 O O   . HOH F 3 .   ? 30.00700  23.87900  34.08900  1.000 19.65418 ? 741 HOH B O   1 
HETATM 6444 O O   . HOH F 3 .   ? 5.26700   17.61100  46.93200  1.000 29.44893 ? 742 HOH B O   1 
HETATM 6445 O O   . HOH F 3 .   ? 31.48200  6.35800   32.86500  1.000 30.82476 ? 743 HOH B O   1 
HETATM 6446 O O   . HOH F 3 .   ? 32.21700  14.42600  29.97500  1.000 31.30240 ? 744 HOH B O   1 
HETATM 6447 O O   . HOH F 3 .   ? 7.82300   40.80500  43.38200  1.000 36.78785 ? 745 HOH B O   1 
HETATM 6448 O O   . HOH F 3 .   ? 42.92800  45.12200  58.95600  1.000 27.06047 ? 746 HOH B O   1 
HETATM 6449 O O   . HOH F 3 .   ? 34.00700  45.63200  56.41900  1.000 23.08227 ? 747 HOH B O   1 
HETATM 6450 O O   . HOH F 3 .   ? 41.19800  50.16400  46.94800  1.000 39.59913 ? 748 HOH B O   1 
HETATM 6451 O O   . HOH F 3 .   ? 23.36300  37.46800  36.48200  1.000 30.72743 ? 749 HOH B O   1 
HETATM 6452 O O   . HOH F 3 .   ? 22.97000  43.68300  47.44700  1.000 28.71575 ? 750 HOH B O   1 
HETATM 6453 O O   . HOH F 3 .   ? 23.38100  3.43500   40.82800  1.000 25.43528 ? 751 HOH B O   1 
HETATM 6454 O O   . HOH F 3 .   ? 21.82700  18.69900  50.06500  1.000 18.09502 ? 752 HOH B O   1 
HETATM 6455 O O   . HOH F 3 .   ? 27.66600  29.23300  29.88400  1.000 31.15779 ? 753 HOH B O   1 
HETATM 6456 O O   . HOH F 3 .   ? 29.51400  33.05500  36.58000  1.000 35.49722 ? 754 HOH B O   1 
HETATM 6457 O O   . HOH F 3 .   ? 31.72900  39.63600  43.87400  1.000 35.66529 ? 755 HOH B O   1 
HETATM 6458 O O   . HOH F 3 .   ? 33.92800  17.10500  58.18900  1.000 15.83742 ? 756 HOH B O   1 
HETATM 6459 O O   . HOH F 3 .   ? 28.21200  5.15700   53.19000  1.000 18.54968 ? 757 HOH B O   1 
HETATM 6460 O O   . HOH F 3 .   ? 18.50400  14.74600  47.31000  1.000 20.37111 ? 758 HOH B O   1 
HETATM 6461 O O   . HOH F 3 .   ? 23.86000  24.14000  47.95900  1.000 19.49333 ? 759 HOH B O   1 
HETATM 6462 O O   . HOH F 3 .   ? 12.17300  15.10900  48.84200  1.000 35.22544 ? 760 HOH B O   1 
HETATM 6463 O O   . HOH F 3 .   ? 32.25700  27.16500  36.16300  1.000 25.76184 ? 761 HOH B O   1 
HETATM 6464 O O   . HOH F 3 .   ? 11.51200  16.91400  35.50700  1.000 31.48838 ? 762 HOH B O   1 
HETATM 6465 O O   . HOH F 3 .   ? 32.80400  19.03200  56.87900  1.000 15.37438 ? 763 HOH B O   1 
HETATM 6466 O O   . HOH F 3 .   ? 31.50200  34.29800  43.05100  1.000 24.33013 ? 764 HOH B O   1 
HETATM 6467 O O   . HOH F 3 .   ? 33.70700  16.68200  60.86000  1.000 14.25832 ? 765 HOH B O   1 
HETATM 6468 O O   . HOH F 3 .   ? 14.12700  13.70300  53.88000  1.000 24.55572 ? 766 HOH B O   1 
HETATM 6469 O O   . HOH F 3 .   ? 39.72900  26.86800  56.73300  1.000 22.97829 ? 767 HOH B O   1 
HETATM 6470 O O   . HOH F 3 .   ? 17.36000  32.11600  32.58500  1.000 34.99231 ? 768 HOH B O   1 
HETATM 6471 O O   . HOH F 3 .   ? 28.38700  27.19400  52.82200  1.000 23.95122 ? 769 HOH B O   1 
HETATM 6472 O O   . HOH F 3 .   ? 35.27700  50.07300  63.73300  1.000 40.45146 ? 770 HOH B O   1 
HETATM 6473 O O   . HOH F 3 .   ? 40.36200  25.47300  39.97400  1.000 29.21308 ? 771 HOH B O   1 
HETATM 6474 O O   . HOH F 3 .   ? 33.10300  37.28800  46.44200  1.000 26.18111 ? 772 HOH B O   1 
HETATM 6475 O O   . HOH F 3 .   ? 16.88400  9.51400   54.74200  1.000 26.85677 ? 773 HOH B O   1 
HETATM 6476 O O   . HOH F 3 .   ? 22.76700  24.12100  30.33300  1.000 24.40325 ? 774 HOH B O   1 
HETATM 6477 O O   . HOH F 3 .   ? 39.84600  51.18500  67.88100  1.000 37.48298 ? 775 HOH B O   1 
HETATM 6478 O O   . HOH F 3 .   ? 9.74400   7.90400   50.39400  1.000 29.89500 ? 776 HOH B O   1 
HETATM 6479 O O   . HOH F 3 .   ? 17.98500  12.96500  51.76500  1.000 20.40534 ? 777 HOH B O   1 
HETATM 6480 O O   . HOH F 3 .   ? 28.91200  7.67100   31.11700  1.000 34.90155 ? 778 HOH B O   1 
HETATM 6481 O O   . HOH F 3 .   ? 18.93400  13.17300  55.14400  1.000 19.77270 ? 779 HOH B O   1 
HETATM 6482 O O   . HOH F 3 .   ? 10.18300  36.96800  63.33400  1.000 30.35860 ? 780 HOH B O   1 
HETATM 6483 O O   . HOH F 3 .   ? 29.65700  7.11400   54.75500  1.000 22.34499 ? 781 HOH B O   1 
HETATM 6484 O O   . HOH F 3 .   ? 11.18100  40.40600  45.94100  1.000 29.69589 ? 782 HOH B O   1 
HETATM 6485 O O   . HOH F 3 .   ? 2.58300   18.93200  47.60500  1.000 32.83794 ? 783 HOH B O   1 
HETATM 6486 O O   . HOH F 3 .   ? 46.47400  1.44900   44.52100  1.000 36.58647 ? 784 HOH B O   1 
HETATM 6487 O O   . HOH F 3 .   ? 21.47900  42.71500  49.43000  1.000 22.16359 ? 785 HOH B O   1 
HETATM 6488 O O   . HOH F 3 .   ? 34.53300  16.35600  29.84500  1.000 35.87750 ? 786 HOH B O   1 
HETATM 6489 O O   . HOH F 3 .   ? 26.32800  39.88100  44.52200  1.000 30.69071 ? 787 HOH B O   1 
HETATM 6490 O O   . HOH F 3 .   ? 22.19200  39.67200  64.89300  1.000 40.43392 ? 788 HOH B O   1 
HETATM 6491 O O   . HOH F 3 .   ? 15.62000  17.61900  41.88900  1.000 22.44902 ? 789 HOH B O   1 
HETATM 6492 O O   . HOH F 3 .   ? 39.52600  56.57200  46.90300  1.000 47.15683 ? 790 HOH B O   1 
HETATM 6493 O O   . HOH F 3 .   ? 0.001     22.752    56.793    1.000 30.06463 ? 791 HOH B O   1 
HETATM 6494 O O   . HOH F 3 .   ? 29.55300  53.87200  75.13700  1.000 41.11647 ? 792 HOH B O   1 
HETATM 6495 O O   . HOH F 3 .   ? 0.83500   38.03800  42.02000  1.000 38.21259 ? 793 HOH B O   1 
HETATM 6496 O O   . HOH F 3 .   ? -0.32000  19.39200  59.32400  1.000 31.87927 ? 794 HOH B O   1 
HETATM 6497 O O   . HOH F 3 .   ? 32.44700  23.33400  32.61400  1.000 27.85135 ? 795 HOH B O   1 
HETATM 6498 O O   . HOH F 3 .   ? 24.49200  22.59100  28.82700  1.000 30.73345 ? 796 HOH B O   1 
HETATM 6499 O O   . HOH F 3 .   ? 8.52800   39.29400  45.39000  1.000 31.78653 ? 797 HOH B O   1 
HETATM 6500 O O   . HOH F 3 .   ? 33.94000  17.33600  23.76100  1.000 43.83840 ? 798 HOH B O   1 
HETATM 6501 O O   . HOH F 3 .   ? 18.94200  11.10100  34.13700  1.000 41.51347 ? 799 HOH B O   1 
HETATM 6502 O O   . HOH F 3 .   ? 20.96600  -0.59300  52.75900  1.000 39.76540 ? 800 HOH B O   1 
HETATM 6503 O O   . HOH F 3 .   ? 28.51600  34.37000  74.16600  1.000 23.39075 ? 801 HOH B O   1 
HETATM 6504 O O   . HOH F 3 .   ? 11.03300  -1.50000  47.94400  1.000 34.57676 ? 802 HOH B O   1 
HETATM 6505 O O   . HOH F 3 .   ? 30.40000  25.56600  36.29800  1.000 23.36002 ? 803 HOH B O   1 
HETATM 6506 O O   . HOH F 3 .   ? 40.57900  3.35400   31.98700  1.000 38.81633 ? 804 HOH B O   1 
HETATM 6507 O O   . HOH F 3 .   ? 3.02200   20.23700  53.68600  1.000 32.28593 ? 805 HOH B O   1 
HETATM 6508 O O   . HOH F 3 .   ? -1.09000  22.94200  60.89400  1.000 31.66104 ? 806 HOH B O   1 
HETATM 6509 O O   . HOH F 3 .   ? 33.28200  40.14700  47.03400  1.000 31.98755 ? 807 HOH B O   1 
HETATM 6510 O O   . HOH F 3 .   ? 34.93400  21.83800  31.13600  1.000 36.25577 ? 808 HOH B O   1 
HETATM 6511 O O   . HOH F 3 .   ? 48.40100  0.75700   46.73200  1.000 34.02749 ? 809 HOH B O   1 
HETATM 6512 O O   . HOH F 3 .   ? 10.83100  41.63600  62.68500  1.000 33.23238 ? 810 HOH B O   1 
HETATM 6513 O O   . HOH F 3 .   ? 26.21900  32.22500  71.47000  1.000 24.44835 ? 811 HOH B O   1 
HETATM 6514 O O   . HOH F 3 .   ? 30.25500  34.86200  40.98400  1.000 30.90508 ? 812 HOH B O   1 
HETATM 6515 O O   . HOH F 3 .   ? 44.81200  -1.27000  44.07000  1.000 32.39477 ? 813 HOH B O   1 
HETATM 6516 O O   . HOH F 3 .   ? 15.73600  39.73300  39.30500  1.000 32.93087 ? 814 HOH B O   1 
HETATM 6517 O O   . HOH F 3 .   ? 26.49900  15.90300  53.92900  1.000 29.77114 ? 815 HOH B O   1 
HETATM 6518 O O   . HOH F 3 .   ? 20.32800  5.18700   39.21000  1.000 26.73961 ? 816 HOH B O   1 
HETATM 6519 O O   . HOH F 3 .   ? 36.87800  33.94600  45.80400  1.000 34.53459 ? 817 HOH B O   1 
HETATM 6520 O O   . HOH F 3 .   ? 16.79500  13.40900  56.61700  1.000 27.17710 ? 818 HOH B O   1 
HETATM 6521 O O   . HOH F 3 .   ? 34.18700  35.66400  44.56900  1.000 31.94583 ? 819 HOH B O   1 
HETATM 6522 O O   . HOH F 3 .   ? -0.90200  30.58500  41.44400  1.000 34.35284 ? 820 HOH B O   1 
HETATM 6523 O O   . HOH F 3 .   ? 14.23200  51.92300  67.59100  1.000 42.37816 ? 821 HOH B O   1 
HETATM 6524 O O   . HOH F 3 .   ? 25.34000  14.67900  35.36700  1.000 25.32298 ? 822 HOH B O   1 
HETATM 6525 O O   . HOH F 3 .   ? 10.52200  46.40400  59.37000  1.000 36.56999 ? 823 HOH B O   1 
HETATM 6526 O O   . HOH F 3 .   ? 22.84800  14.56900  52.42500  1.000 17.79043 ? 824 HOH B O   1 
HETATM 6527 O O   . HOH F 3 .   ? 21.10800  13.99000  36.68500  1.000 33.25085 ? 825 HOH B O   1 
HETATM 6528 O O   . HOH F 3 .   ? 34.15800  -5.50800  51.21300  1.000 28.87877 ? 826 HOH B O   1 
HETATM 6529 O O   . HOH F 3 .   ? 36.68400  35.07700  48.21000  1.000 23.43308 ? 827 HOH B O   1 
HETATM 6530 O O   . HOH F 3 .   ? 39.38800  23.68500  38.19200  1.000 25.99636 ? 828 HOH B O   1 
HETATM 6531 O O   . HOH F 3 .   ? 19.69600  11.56800  36.82800  1.000 28.20681 ? 829 HOH B O   1 
HETATM 6532 O O   . HOH F 3 .   ? 44.791    7.874     56.473    1.000 39.60513 ? 830 HOH B O   1 
HETATM 6533 O O   . HOH F 3 .   ? 14.93500  43.17600  62.89400  1.000 26.63385 ? 831 HOH B O   1 
HETATM 6534 O O   . HOH F 3 .   ? 18.00200  5.54200   39.88700  1.000 31.28877 ? 832 HOH B O   1 
HETATM 6535 O O   . HOH F 3 .   ? 16.10600  12.96600  49.90300  1.000 22.78371 ? 833 HOH B O   1 
HETATM 6536 O O   . HOH F 3 .   ? 19.46000  41.73800  47.98500  1.000 26.09653 ? 834 HOH B O   1 
HETATM 6537 O O   . HOH F 3 .   ? 18.58000  14.02800  44.11800  1.000 26.54887 ? 835 HOH B O   1 
HETATM 6538 O O   . HOH F 3 .   ? 0.00200   30.22500  39.20900  1.000 40.55817 ? 836 HOH B O   1 
HETATM 6539 O O   . HOH F 3 .   ? 15.78500  42.83800  65.56000  1.000 29.95956 ? 837 HOH B O   1 
HETATM 6540 O O   . HOH F 3 .   ? 15.91900  40.73000  42.70600  1.000 35.35958 ? 838 HOH B O   1 
HETATM 6541 O O   . HOH F 3 .   ? 7.32900   39.71400  47.82500  1.000 33.28366 ? 839 HOH B O   1 
HETATM 6542 O O   . HOH F 3 .   ? 14.99200  15.21800  42.88300  1.000 22.53739 ? 840 HOH B O   1 
HETATM 6543 O O   . HOH F 3 .   ? 12.71900  -2.45500  46.50700  1.000 40.84313 ? 841 HOH B O   1 
HETATM 6544 O O   . HOH F 3 .   ? 17.12900  3.36600   41.80400  1.000 38.58786 ? 842 HOH B O   1 
HETATM 6545 O O   . HOH F 3 .   ? 36.893    17.659    24.466    1.000 36.36501 ? 843 HOH B O   1 
HETATM 6546 O O   . HOH F 3 .   ? 15.90400  13.47100  45.58800  1.000 27.47545 ? 844 HOH B O   1 
HETATM 6547 O O   . HOH F 3 .   ? 13.04700  53.84500  67.50000  1.000 45.14039 ? 845 HOH B O   1 
HETATM 6548 O O   . HOH F 3 .   ? 22.60300  42.12300  44.87900  1.000 32.36093 ? 846 HOH B O   1 
HETATM 6549 O O   . HOH F 3 .   ? 19.59400  41.65100  45.43300  1.000 26.17474 ? 847 HOH B O   1 
HETATM 6550 O O   . HOH F 3 .   ? 25.64900  37.34100  37.00800  1.000 32.41456 ? 848 HOH B O   1 
HETATM 6551 O O   . HOH F 3 .   ? 10.50300  2.42000   40.83200  1.000 40.00756 ? 849 HOH B O   1 
HETATM 6552 O O   . HOH F 3 .   ? 31.15100  4.46500   29.89000  1.000 36.72889 ? 850 HOH B O   1 
HETATM 6553 O O   . HOH F 3 .   ? 26.61200  8.86700   31.12000  1.000 40.53004 ? 851 HOH B O   1 
HETATM 6554 O O   . HOH F 3 .   ? 25.44000  20.15500  48.63200  1.000 19.33331 ? 852 HOH B O   1 
HETATM 6555 O O   . HOH F 3 .   ? 24.09200  48.35600  52.75000  1.000 37.54856 ? 853 HOH B O   1 
HETATM 6556 O O   . HOH F 3 .   ? 15.41000  11.42800  46.88100  1.000 12.74593 ? 854 HOH B O   1 
HETATM 6557 O O   . HOH F 3 .   ? 36.92400  36.68700  41.54700  1.000 36.56117 ? 855 HOH B O   1 
HETATM 6558 O O   . HOH F 3 .   ? 41.33000  22.53100  36.93700  1.000 27.56194 ? 856 HOH B O   1 
HETATM 6559 O O   . HOH F 3 .   ? 27.73300  35.78100  38.30700  1.000 30.84632 ? 857 HOH B O   1 
HETATM 6560 O O   . HOH F 3 .   ? 23.70000  2.32400   36.34900  1.000 32.33274 ? 858 HOH B O   1 
HETATM 6561 O O   . HOH F 3 .   ? 18.17300  44.43200  47.38200  1.000 26.49999 ? 859 HOH B O   1 
HETATM 6562 O O   . HOH F 3 .   ? 27.99800  47.52900  55.66800  1.000 35.94458 ? 860 HOH B O   1 
HETATM 6563 O O   . HOH F 3 .   ? 40.85300  27.77700  39.37100  1.000 33.51347 ? 861 HOH B O   1 
HETATM 6564 O O   . HOH F 3 .   ? 25.00800  49.36300  50.92900  1.000 44.41337 ? 862 HOH B O   1 
HETATM 6565 O O   . HOH F 3 .   ? 14.05700  13.52300  51.23600  1.000 30.17180 ? 863 HOH B O   1 
HETATM 6566 O O   . HOH F 3 .   ? 11.50500  43.38000  46.53700  1.000 35.99087 ? 864 HOH B O   1 
HETATM 6567 O O   . HOH F 3 .   ? 23.27800  13.21800  58.87600  1.000 26.90003 ? 865 HOH B O   1 
# 
