CNRS Nantes University US2B US2B
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***  1pv6 full  ***

elNémo ID: 2411130006181849819

Job options:

ID        	=	 2411130006181849819
JOBID     	=	 1pv6 full
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 1pv6 full

data_1PV6
# 
_entry.id   1PV6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.392 
_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   1PV6         pdb_00001pv6 10.2210/pdb1pv6/pdb 
RCSB  RCSB019597   ?            ?                   
WWPDB D_1000019597 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2003-08-12 
2 'Structure model' 1 1 2008-04-29 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2021-11-10 
5 'Structure model' 1 4 2024-05-29 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Database references'       
4 5 'Structure model' 'Data collection'           
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' database_2         
2 4 'Structure model' struct_ref_seq_dif 
3 5 'Structure model' chem_comp_atom     
4 5 'Structure model' chem_comp_bond     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_database_2.pdbx_DOI'                
2 4 'Structure model' '_database_2.pdbx_database_accession' 
3 4 'Structure model' '_struct_ref_seq_dif.details'         
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1PV6 
_pdbx_database_status.recvd_initial_deposition_date   2003-06-26 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          1PV7 
_pdbx_database_related.details        'The same protein complexed with TDG' 
_pdbx_database_related.content_type   unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Abramson, J.' 1 
'Smirnova, I.' 2 
'Kasho, V.'    3 
'Verner, G.'   4 
'Kaback, H.R.' 5 
'Iwata, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Structure and mechanism of the lactose permease of Escherichia coli' 
_citation.journal_abbrev            SCIENCE 
_citation.journal_volume            301 
_citation.page_first                610 
_citation.page_last                 615 
_citation.year                      2003 
_citation.journal_id_ASTM           SCIEAS 
_citation.country                   US 
_citation.journal_id_ISSN           0036-8075 
_citation.journal_id_CSD            0038 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12893935 
_citation.pdbx_database_id_DOI      10.1126/science.1088196 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Abramson, J.' 1 ? 
primary 'Smirnova, I.' 2 ? 
primary 'Kasho, V.'    3 ? 
primary 'Verner, G.'   4 ? 
primary 'Kaback, H.R.' 5 ? 
primary 'Iwata, S.'    6 ? 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'Lactose permease' 
_entity.formula_weight             46484.797 
_entity.pdbx_number_of_molecules   2 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              C154G 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_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       
;MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWII
TGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALGASIVGI
MFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFD
QQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKT
LHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQLAMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTL
SGPGPLSLLRRQVNEVA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWII
TGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALGASIVGI
MFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFD
QQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKT
LHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQLAMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTL
SGPGPLSLLRRQVNEVA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
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   TYR n 
1 3   TYR n 
1 4   LEU n 
1 5   LYS n 
1 6   ASN n 
1 7   THR n 
1 8   ASN n 
1 9   PHE n 
1 10  TRP n 
1 11  MET n 
1 12  PHE n 
1 13  GLY n 
1 14  LEU n 
1 15  PHE n 
1 16  PHE n 
1 17  PHE n 
1 18  PHE n 
1 19  TYR n 
1 20  PHE n 
1 21  PHE n 
1 22  ILE n 
1 23  MET n 
1 24  GLY n 
1 25  ALA n 
1 26  TYR n 
1 27  PHE n 
1 28  PRO n 
1 29  PHE n 
1 30  PHE n 
1 31  PRO n 
1 32  ILE n 
1 33  TRP n 
1 34  LEU n 
1 35  HIS n 
1 36  ASP n 
1 37  ILE n 
1 38  ASN n 
1 39  HIS n 
1 40  ILE n 
1 41  SER n 
1 42  LYS n 
1 43  SER n 
1 44  ASP n 
1 45  THR n 
1 46  GLY n 
1 47  ILE n 
1 48  ILE n 
1 49  PHE n 
1 50  ALA n 
1 51  ALA n 
1 52  ILE n 
1 53  SER n 
1 54  LEU n 
1 55  PHE n 
1 56  SER n 
1 57  LEU n 
1 58  LEU n 
1 59  PHE n 
1 60  GLN n 
1 61  PRO n 
1 62  LEU n 
1 63  PHE n 
1 64  GLY n 
1 65  LEU n 
1 66  LEU n 
1 67  SER n 
1 68  ASP n 
1 69  LYS n 
1 70  LEU n 
1 71  GLY n 
1 72  LEU n 
1 73  ARG n 
1 74  LYS n 
1 75  TYR n 
1 76  LEU n 
1 77  LEU n 
1 78  TRP n 
1 79  ILE n 
1 80  ILE n 
1 81  THR n 
1 82  GLY n 
1 83  MET n 
1 84  LEU n 
1 85  VAL n 
1 86  MET n 
1 87  PHE n 
1 88  ALA n 
1 89  PRO n 
1 90  PHE n 
1 91  PHE n 
1 92  ILE n 
1 93  PHE n 
1 94  ILE n 
1 95  PHE n 
1 96  GLY n 
1 97  PRO n 
1 98  LEU n 
1 99  LEU n 
1 100 GLN n 
1 101 TYR n 
1 102 ASN n 
1 103 ILE n 
1 104 LEU n 
1 105 VAL n 
1 106 GLY n 
1 107 SER n 
1 108 ILE n 
1 109 VAL n 
1 110 GLY n 
1 111 GLY n 
1 112 ILE n 
1 113 TYR n 
1 114 LEU n 
1 115 GLY n 
1 116 PHE n 
1 117 CYS n 
1 118 PHE n 
1 119 ASN n 
1 120 ALA n 
1 121 GLY n 
1 122 ALA n 
1 123 PRO n 
1 124 ALA n 
1 125 VAL n 
1 126 GLU n 
1 127 ALA n 
1 128 PHE n 
1 129 ILE n 
1 130 GLU n 
1 131 LYS n 
1 132 VAL n 
1 133 SER n 
1 134 ARG n 
1 135 ARG n 
1 136 SER n 
1 137 ASN n 
1 138 PHE n 
1 139 GLU n 
1 140 PHE n 
1 141 GLY n 
1 142 ARG n 
1 143 ALA n 
1 144 ARG n 
1 145 MET n 
1 146 PHE n 
1 147 GLY n 
1 148 CYS n 
1 149 VAL n 
1 150 GLY n 
1 151 TRP n 
1 152 ALA n 
1 153 LEU n 
1 154 GLY n 
1 155 ALA n 
1 156 SER n 
1 157 ILE n 
1 158 VAL n 
1 159 GLY n 
1 160 ILE n 
1 161 MET n 
1 162 PHE n 
1 163 THR n 
1 164 ILE n 
1 165 ASN n 
1 166 ASN n 
1 167 GLN n 
1 168 PHE n 
1 169 VAL n 
1 170 PHE n 
1 171 TRP n 
1 172 LEU n 
1 173 GLY n 
1 174 SER n 
1 175 GLY n 
1 176 CYS n 
1 177 ALA n 
1 178 LEU n 
1 179 ILE n 
1 180 LEU n 
1 181 ALA n 
1 182 VAL n 
1 183 LEU n 
1 184 LEU n 
1 185 PHE n 
1 186 PHE n 
1 187 ALA n 
1 188 LYS n 
1 189 THR n 
1 190 ASP n 
1 191 ALA n 
1 192 PRO n 
1 193 SER n 
1 194 SER n 
1 195 ALA n 
1 196 THR n 
1 197 VAL n 
1 198 ALA n 
1 199 ASN n 
1 200 ALA n 
1 201 VAL n 
1 202 GLY n 
1 203 ALA n 
1 204 ASN n 
1 205 HIS n 
1 206 SER n 
1 207 ALA n 
1 208 PHE n 
1 209 SER n 
1 210 LEU n 
1 211 LYS n 
1 212 LEU n 
1 213 ALA n 
1 214 LEU n 
1 215 GLU n 
1 216 LEU n 
1 217 PHE n 
1 218 ARG n 
1 219 GLN n 
1 220 PRO n 
1 221 LYS n 
1 222 LEU n 
1 223 TRP n 
1 224 PHE n 
1 225 LEU n 
1 226 SER n 
1 227 LEU n 
1 228 TYR n 
1 229 VAL n 
1 230 ILE n 
1 231 GLY n 
1 232 VAL n 
1 233 SER n 
1 234 CYS n 
1 235 THR n 
1 236 TYR n 
1 237 ASP n 
1 238 VAL n 
1 239 PHE n 
1 240 ASP n 
1 241 GLN n 
1 242 GLN n 
1 243 PHE n 
1 244 ALA n 
1 245 ASN n 
1 246 PHE n 
1 247 PHE n 
1 248 THR n 
1 249 SER n 
1 250 PHE n 
1 251 PHE n 
1 252 ALA n 
1 253 THR n 
1 254 GLY n 
1 255 GLU n 
1 256 GLN n 
1 257 GLY n 
1 258 THR n 
1 259 ARG n 
1 260 VAL n 
1 261 PHE n 
1 262 GLY n 
1 263 TYR n 
1 264 VAL n 
1 265 THR n 
1 266 THR n 
1 267 MET n 
1 268 GLY n 
1 269 GLU n 
1 270 LEU n 
1 271 LEU n 
1 272 ASN n 
1 273 ALA n 
1 274 SER n 
1 275 ILE n 
1 276 MET n 
1 277 PHE n 
1 278 PHE n 
1 279 ALA n 
1 280 PRO n 
1 281 LEU n 
1 282 ILE n 
1 283 ILE n 
1 284 ASN n 
1 285 ARG n 
1 286 ILE n 
1 287 GLY n 
1 288 GLY n 
1 289 LYS n 
1 290 ASN n 
1 291 ALA n 
1 292 LEU n 
1 293 LEU n 
1 294 LEU n 
1 295 ALA n 
1 296 GLY n 
1 297 THR n 
1 298 ILE n 
1 299 MET n 
1 300 SER n 
1 301 VAL n 
1 302 ARG n 
1 303 ILE n 
1 304 ILE n 
1 305 GLY n 
1 306 SER n 
1 307 SER n 
1 308 PHE n 
1 309 ALA n 
1 310 THR n 
1 311 SER n 
1 312 ALA n 
1 313 LEU n 
1 314 GLU n 
1 315 VAL n 
1 316 VAL n 
1 317 ILE n 
1 318 LEU n 
1 319 LYS n 
1 320 THR n 
1 321 LEU n 
1 322 HIS n 
1 323 MET n 
1 324 PHE n 
1 325 GLU n 
1 326 VAL n 
1 327 PRO n 
1 328 PHE n 
1 329 LEU n 
1 330 LEU n 
1 331 VAL n 
1 332 GLY n 
1 333 CYS n 
1 334 PHE n 
1 335 LYS n 
1 336 TYR n 
1 337 ILE n 
1 338 THR n 
1 339 SER n 
1 340 GLN n 
1 341 PHE n 
1 342 GLU n 
1 343 VAL n 
1 344 ARG n 
1 345 PHE n 
1 346 SER n 
1 347 ALA n 
1 348 THR n 
1 349 ILE n 
1 350 TYR n 
1 351 LEU n 
1 352 VAL n 
1 353 CYS n 
1 354 PHE n 
1 355 CYS n 
1 356 PHE n 
1 357 PHE n 
1 358 LYS n 
1 359 GLN n 
1 360 LEU n 
1 361 ALA n 
1 362 MET n 
1 363 ILE n 
1 364 PHE n 
1 365 MET n 
1 366 SER n 
1 367 VAL n 
1 368 LEU n 
1 369 ALA n 
1 370 GLY n 
1 371 ASN n 
1 372 MET n 
1 373 TYR n 
1 374 GLU n 
1 375 SER n 
1 376 ILE n 
1 377 GLY n 
1 378 PHE n 
1 379 GLN n 
1 380 GLY n 
1 381 ALA n 
1 382 TYR n 
1 383 LEU n 
1 384 VAL n 
1 385 LEU n 
1 386 GLY n 
1 387 LEU n 
1 388 VAL n 
1 389 ALA n 
1 390 LEU n 
1 391 GLY n 
1 392 PHE n 
1 393 THR n 
1 394 LEU n 
1 395 ILE n 
1 396 SER n 
1 397 VAL n 
1 398 PHE n 
1 399 THR n 
1 400 LEU n 
1 401 SER n 
1 402 GLY n 
1 403 PRO n 
1 404 GLY n 
1 405 PRO n 
1 406 LEU n 
1 407 SER n 
1 408 LEU n 
1 409 LEU n 
1 410 ARG n 
1 411 ARG n 
1 412 GLN n 
1 413 VAL n 
1 414 ASN n 
1 415 GLU n 
1 416 VAL n 
1 417 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     Escherichia 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_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 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   TYR 2   2   2   TYR TYR A . n 
A 1 3   TYR 3   3   3   TYR TYR A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   THR 7   7   7   THR THR A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  MET 11  11  11  MET MET A . n 
A 1 12  PHE 12  12  12  PHE PHE A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  PHE 15  15  15  PHE PHE A . n 
A 1 16  PHE 16  16  16  PHE PHE A . n 
A 1 17  PHE 17  17  17  PHE PHE A . n 
A 1 18  PHE 18  18  18  PHE PHE A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  MET 23  23  23  MET MET A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  TYR 26  26  26  TYR TYR A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  PHE 29  29  29  PHE PHE A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  PRO 31  31  31  PRO PRO A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  TRP 33  33  33  TRP TRP A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  HIS 35  35  35  HIS HIS A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  HIS 39  39  39  HIS HIS A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  PHE 55  55  55  PHE PHE A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  PHE 63  63  63  PHE PHE A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  MET 83  83  83  MET MET A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  MET 86  86  86  MET MET A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 GLN 100 100 100 GLN GLN A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 LYS 131 131 131 LYS LYS A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ARG 134 134 134 ARG ARG A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 ARG 142 142 142 ARG ARG A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 MET 145 145 145 MET MET A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 CYS 148 148 148 CYS CYS A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 TRP 151 151 151 TRP TRP A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 MET 161 161 161 MET MET A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 ASN 166 166 166 ASN ASN A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 TRP 171 171 171 TRP TRP A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 SER 174 174 174 SER SER A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 CYS 176 176 176 CYS CYS A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ILE 179 179 179 ILE ILE 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 VAL 182 182 182 VAL VAL A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 PHE 186 186 186 PHE PHE A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 ASN 199 199 199 ASN ASN A . n 
A 1 200 ALA 200 200 200 ALA ALA A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 ASN 204 204 204 ASN ASN A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 LYS 211 211 211 LYS LYS A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 ARG 218 218 218 ARG ARG A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 TRP 223 223 223 TRP TRP A . n 
A 1 224 PHE 224 224 224 PHE PHE A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 TYR 228 228 228 TYR TYR A . n 
A 1 229 VAL 229 229 229 VAL VAL A . n 
A 1 230 ILE 230 230 230 ILE ILE A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 CYS 234 234 234 CYS CYS A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 PHE 239 239 239 PHE PHE A . n 
A 1 240 ASP 240 240 240 ASP ASP A . n 
A 1 241 GLN 241 241 241 GLN GLN A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 PHE 250 250 250 PHE PHE A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 GLY 254 254 254 GLY GLY A . n 
A 1 255 GLU 255 255 255 GLU GLU A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 GLY 257 257 257 GLY GLY A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 VAL 260 260 260 VAL VAL A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 GLY 262 262 262 GLY GLY A . n 
A 1 263 TYR 263 263 263 TYR TYR A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 MET 267 267 267 MET MET A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 PHE 277 277 277 PHE PHE A . n 
A 1 278 PHE 278 278 278 PHE PHE A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 PRO 280 280 280 PRO PRO A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 ILE 283 283 283 ILE ILE A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 ARG 285 285 285 ARG ARG A . n 
A 1 286 ILE 286 286 286 ILE ILE A . n 
A 1 287 GLY 287 287 287 GLY GLY A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 ASN 290 290 290 ASN ASN A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 LEU 294 294 294 LEU LEU A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 THR 297 297 297 THR THR A . n 
A 1 298 ILE 298 298 298 ILE ILE A . n 
A 1 299 MET 299 299 299 MET MET A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 VAL 301 301 301 VAL VAL A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 ILE 303 303 303 ILE ILE A . n 
A 1 304 ILE 304 304 304 ILE ILE A . n 
A 1 305 GLY 305 305 305 GLY GLY A . n 
A 1 306 SER 306 306 306 SER SER A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 PHE 308 308 308 PHE PHE A . n 
A 1 309 ALA 309 309 309 ALA ALA A . n 
A 1 310 THR 310 310 310 THR THR A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 VAL 315 315 315 VAL VAL A . n 
A 1 316 VAL 316 316 316 VAL VAL 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 LYS 319 319 319 LYS LYS A . n 
A 1 320 THR 320 320 320 THR THR A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 HIS 322 322 322 HIS HIS A . n 
A 1 323 MET 323 323 323 MET MET A . n 
A 1 324 PHE 324 324 324 PHE PHE A . n 
A 1 325 GLU 325 325 325 GLU GLU A . n 
A 1 326 VAL 326 326 326 VAL VAL A . n 
A 1 327 PRO 327 327 327 PRO PRO A . n 
A 1 328 PHE 328 328 328 PHE PHE A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 VAL 331 331 331 VAL VAL A . n 
A 1 332 GLY 332 332 332 GLY GLY A . n 
A 1 333 CYS 333 333 333 CYS CYS A . n 
A 1 334 PHE 334 334 334 PHE PHE A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 TYR 336 336 336 TYR TYR A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 THR 338 338 338 THR THR A . n 
A 1 339 SER 339 339 339 SER SER A . n 
A 1 340 GLN 340 340 340 GLN GLN A . n 
A 1 341 PHE 341 341 341 PHE PHE A . n 
A 1 342 GLU 342 342 342 GLU GLU A . n 
A 1 343 VAL 343 343 343 VAL VAL A . n 
A 1 344 ARG 344 344 344 ARG ARG A . n 
A 1 345 PHE 345 345 345 PHE PHE A . n 
A 1 346 SER 346 346 346 SER SER A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 THR 348 348 348 THR THR A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 TYR 350 350 350 TYR TYR A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 VAL 352 352 352 VAL VAL A . n 
A 1 353 CYS 353 353 353 CYS CYS A . n 
A 1 354 PHE 354 354 354 PHE PHE A . n 
A 1 355 CYS 355 355 355 CYS CYS A . n 
A 1 356 PHE 356 356 356 PHE PHE A . n 
A 1 357 PHE 357 357 357 PHE PHE A . n 
A 1 358 LYS 358 358 358 LYS LYS A . n 
A 1 359 GLN 359 359 359 GLN GLN A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 MET 362 362 362 MET MET A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 PHE 364 364 364 PHE PHE A . n 
A 1 365 MET 365 365 365 MET MET A . n 
A 1 366 SER 366 366 366 SER SER A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 MET 372 372 372 MET MET A . n 
A 1 373 TYR 373 373 373 TYR TYR A . n 
A 1 374 GLU 374 374 374 GLU GLU A . n 
A 1 375 SER 375 375 375 SER SER A . n 
A 1 376 ILE 376 376 376 ILE ILE A . n 
A 1 377 GLY 377 377 377 GLY GLY A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 GLN 379 379 379 GLN GLN A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 ALA 381 381 381 ALA ALA A . n 
A 1 382 TYR 382 382 382 TYR TYR A . n 
A 1 383 LEU 383 383 383 LEU LEU A . n 
A 1 384 VAL 384 384 384 VAL VAL A . n 
A 1 385 LEU 385 385 385 LEU LEU A . n 
A 1 386 GLY 386 386 386 GLY GLY A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 VAL 388 388 388 VAL VAL A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 LEU 390 390 390 LEU LEU A . n 
A 1 391 GLY 391 391 391 GLY GLY A . n 
A 1 392 PHE 392 392 392 PHE PHE A . n 
A 1 393 THR 393 393 393 THR THR A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 ILE 395 395 395 ILE ILE A . n 
A 1 396 SER 396 396 396 SER SER A . n 
A 1 397 VAL 397 397 397 VAL VAL A . n 
A 1 398 PHE 398 398 398 PHE PHE A . n 
A 1 399 THR 399 399 399 THR THR A . n 
A 1 400 LEU 400 400 400 LEU LEU A . n 
A 1 401 SER 401 401 401 SER SER A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 PRO 403 403 403 PRO PRO A . n 
A 1 404 GLY 404 404 404 GLY GLY A . n 
A 1 405 PRO 405 405 405 PRO PRO A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 SER 407 407 407 SER SER A . n 
A 1 408 LEU 408 408 408 LEU LEU A . n 
A 1 409 LEU 409 409 409 LEU LEU A . n 
A 1 410 ARG 410 410 410 ARG ARG A . n 
A 1 411 ARG 411 411 411 ARG ARG A . n 
A 1 412 GLN 412 412 412 GLN GLN A . n 
A 1 413 VAL 413 413 413 VAL VAL A . n 
A 1 414 ASN 414 414 414 ASN ASN A . n 
A 1 415 GLU 415 415 415 GLU GLU A . n 
A 1 416 VAL 416 416 416 VAL VAL A . n 
A 1 417 ALA 417 417 417 ALA ALA A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   TYR 2   2   2   TYR TYR B . n 
B 1 3   TYR 3   3   3   TYR TYR B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ASN 6   6   6   ASN ASN B . n 
B 1 7   THR 7   7   7   THR THR B . n 
B 1 8   ASN 8   8   8   ASN ASN B . n 
B 1 9   PHE 9   9   9   PHE PHE B . n 
B 1 10  TRP 10  10  10  TRP TRP B . n 
B 1 11  MET 11  11  11  MET MET B . n 
B 1 12  PHE 12  12  12  PHE PHE B . n 
B 1 13  GLY 13  13  13  GLY GLY B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  PHE 15  15  15  PHE PHE B . n 
B 1 16  PHE 16  16  16  PHE PHE B . n 
B 1 17  PHE 17  17  17  PHE PHE B . n 
B 1 18  PHE 18  18  18  PHE PHE B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  MET 23  23  23  MET MET B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  TYR 26  26  26  TYR TYR B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  PHE 29  29  29  PHE PHE B . n 
B 1 30  PHE 30  30  30  PHE PHE B . n 
B 1 31  PRO 31  31  31  PRO PRO B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  TRP 33  33  33  TRP TRP B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  HIS 35  35  35  HIS HIS B . n 
B 1 36  ASP 36  36  36  ASP ASP B . n 
B 1 37  ILE 37  37  37  ILE ILE B . n 
B 1 38  ASN 38  38  38  ASN ASN B . n 
B 1 39  HIS 39  39  39  HIS HIS B . n 
B 1 40  ILE 40  40  40  ILE ILE B . n 
B 1 41  SER 41  41  41  SER SER B . n 
B 1 42  LYS 42  42  42  LYS LYS B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  ASP 44  44  44  ASP ASP B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  ILE 48  48  48  ILE ILE B . n 
B 1 49  PHE 49  49  49  PHE PHE B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  ILE 52  52  52  ILE ILE B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  PHE 55  55  55  PHE PHE B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  GLN 60  60  60  GLN GLN B . n 
B 1 61  PRO 61  61  61  PRO PRO B . n 
B 1 62  LEU 62  62  62  LEU LEU B . n 
B 1 63  PHE 63  63  63  PHE PHE B . n 
B 1 64  GLY 64  64  64  GLY GLY B . n 
B 1 65  LEU 65  65  65  LEU LEU B . n 
B 1 66  LEU 66  66  66  LEU LEU B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  LYS 74  74  74  LYS LYS B . n 
B 1 75  TYR 75  75  75  TYR TYR B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  TRP 78  78  78  TRP TRP B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  THR 81  81  81  THR THR B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  MET 83  83  83  MET MET B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  MET 86  86  86  MET MET B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  ALA 88  88  88  ALA ALA B . n 
B 1 89  PRO 89  89  89  PRO PRO B . n 
B 1 90  PHE 90  90  90  PHE PHE B . n 
B 1 91  PHE 91  91  91  PHE PHE B . n 
B 1 92  ILE 92  92  92  ILE ILE B . n 
B 1 93  PHE 93  93  93  PHE PHE B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  GLY 96  96  96  GLY GLY B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 GLN 100 100 100 GLN GLN B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 ILE 103 103 103 ILE ILE B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 VAL 105 105 105 VAL VAL B . n 
B 1 106 GLY 106 106 106 GLY GLY B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 ILE 108 108 108 ILE ILE B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 GLY 110 110 110 GLY GLY B . n 
B 1 111 GLY 111 111 111 GLY GLY B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 LEU 114 114 114 LEU LEU B . n 
B 1 115 GLY 115 115 115 GLY GLY B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 PHE 118 118 118 PHE PHE B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 GLY 121 121 121 GLY GLY B . n 
B 1 122 ALA 122 122 122 ALA ALA B . n 
B 1 123 PRO 123 123 123 PRO PRO B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 ALA 127 127 127 ALA ALA B . n 
B 1 128 PHE 128 128 128 PHE PHE B . n 
B 1 129 ILE 129 129 129 ILE ILE B . n 
B 1 130 GLU 130 130 130 GLU GLU B . n 
B 1 131 LYS 131 131 131 LYS LYS B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 ARG 134 134 134 ARG ARG B . n 
B 1 135 ARG 135 135 135 ARG ARG B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 ASN 137 137 137 ASN ASN B . n 
B 1 138 PHE 138 138 138 PHE PHE B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 ARG 142 142 142 ARG ARG B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 MET 145 145 145 MET MET B . n 
B 1 146 PHE 146 146 146 PHE PHE B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 CYS 148 148 148 CYS CYS B . n 
B 1 149 VAL 149 149 149 VAL VAL B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 TRP 151 151 151 TRP TRP B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 ALA 155 155 155 ALA ALA B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 ILE 157 157 157 ILE ILE B . n 
B 1 158 VAL 158 158 158 VAL VAL B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 ILE 160 160 160 ILE ILE B . n 
B 1 161 MET 161 161 161 MET MET B . n 
B 1 162 PHE 162 162 162 PHE PHE B . n 
B 1 163 THR 163 163 163 THR THR B . n 
B 1 164 ILE 164 164 164 ILE ILE B . n 
B 1 165 ASN 165 165 165 ASN ASN B . n 
B 1 166 ASN 166 166 166 ASN ASN B . n 
B 1 167 GLN 167 167 167 GLN GLN B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 VAL 169 169 169 VAL VAL B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 TRP 171 171 171 TRP TRP B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 SER 174 174 174 SER SER B . n 
B 1 175 GLY 175 175 175 GLY GLY B . n 
B 1 176 CYS 176 176 176 CYS CYS B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 LEU 178 178 178 LEU LEU B . n 
B 1 179 ILE 179 179 179 ILE ILE 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 VAL 182 182 182 VAL VAL B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 PHE 186 186 186 PHE PHE B . n 
B 1 187 ALA 187 187 187 ALA ALA B . n 
B 1 188 LYS 188 188 188 LYS LYS B . n 
B 1 189 THR 189 189 189 THR THR B . n 
B 1 190 ASP 190 190 190 ASP ASP B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 PRO 192 192 192 PRO PRO B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 SER 194 194 194 SER SER B . n 
B 1 195 ALA 195 195 195 ALA ALA B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 VAL 197 197 197 VAL VAL B . n 
B 1 198 ALA 198 198 198 ALA ALA B . n 
B 1 199 ASN 199 199 199 ASN ASN B . n 
B 1 200 ALA 200 200 200 ALA ALA B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 GLY 202 202 202 GLY GLY B . n 
B 1 203 ALA 203 203 203 ALA ALA B . n 
B 1 204 ASN 204 204 204 ASN ASN B . n 
B 1 205 HIS 205 205 205 HIS HIS B . n 
B 1 206 SER 206 206 206 SER SER B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 PHE 208 208 208 PHE PHE B . n 
B 1 209 SER 209 209 209 SER SER B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 LYS 211 211 211 LYS LYS B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 ALA 213 213 213 ALA ALA B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 GLU 215 215 215 GLU GLU B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 PHE 217 217 217 PHE PHE B . n 
B 1 218 ARG 218 218 218 ARG ARG B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 PRO 220 220 220 PRO PRO B . n 
B 1 221 LYS 221 221 221 LYS LYS B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 TRP 223 223 223 TRP TRP B . n 
B 1 224 PHE 224 224 224 PHE PHE B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 SER 226 226 226 SER SER B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 TYR 228 228 228 TYR TYR B . n 
B 1 229 VAL 229 229 229 VAL VAL B . n 
B 1 230 ILE 230 230 230 ILE ILE B . n 
B 1 231 GLY 231 231 231 GLY GLY B . n 
B 1 232 VAL 232 232 232 VAL VAL B . n 
B 1 233 SER 233 233 233 SER SER B . n 
B 1 234 CYS 234 234 234 CYS CYS B . n 
B 1 235 THR 235 235 235 THR THR B . n 
B 1 236 TYR 236 236 236 TYR TYR B . n 
B 1 237 ASP 237 237 237 ASP ASP B . n 
B 1 238 VAL 238 238 238 VAL VAL B . n 
B 1 239 PHE 239 239 239 PHE PHE B . n 
B 1 240 ASP 240 240 240 ASP ASP B . n 
B 1 241 GLN 241 241 241 GLN GLN B . n 
B 1 242 GLN 242 242 242 GLN GLN B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 ALA 244 244 244 ALA ALA B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 PHE 247 247 247 PHE PHE B . n 
B 1 248 THR 248 248 248 THR THR B . n 
B 1 249 SER 249 249 249 SER SER B . n 
B 1 250 PHE 250 250 250 PHE PHE B . n 
B 1 251 PHE 251 251 251 PHE PHE B . n 
B 1 252 ALA 252 252 252 ALA ALA B . n 
B 1 253 THR 253 253 253 THR THR B . n 
B 1 254 GLY 254 254 254 GLY GLY B . n 
B 1 255 GLU 255 255 255 GLU GLU B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 GLY 257 257 257 GLY GLY B . n 
B 1 258 THR 258 258 258 THR THR B . n 
B 1 259 ARG 259 259 259 ARG ARG B . n 
B 1 260 VAL 260 260 260 VAL VAL B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 GLY 262 262 262 GLY GLY B . n 
B 1 263 TYR 263 263 263 TYR TYR B . n 
B 1 264 VAL 264 264 264 VAL VAL B . n 
B 1 265 THR 265 265 265 THR THR B . n 
B 1 266 THR 266 266 266 THR THR B . n 
B 1 267 MET 267 267 267 MET MET B . n 
B 1 268 GLY 268 268 268 GLY GLY B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 LEU 270 270 270 LEU LEU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 ASN 272 272 272 ASN ASN B . n 
B 1 273 ALA 273 273 273 ALA ALA B . n 
B 1 274 SER 274 274 274 SER SER B . n 
B 1 275 ILE 275 275 275 ILE ILE B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 PHE 277 277 277 PHE PHE B . n 
B 1 278 PHE 278 278 278 PHE PHE B . n 
B 1 279 ALA 279 279 279 ALA ALA B . n 
B 1 280 PRO 280 280 280 PRO PRO B . n 
B 1 281 LEU 281 281 281 LEU LEU B . n 
B 1 282 ILE 282 282 282 ILE ILE B . n 
B 1 283 ILE 283 283 283 ILE ILE B . n 
B 1 284 ASN 284 284 284 ASN ASN B . n 
B 1 285 ARG 285 285 285 ARG ARG B . n 
B 1 286 ILE 286 286 286 ILE ILE B . n 
B 1 287 GLY 287 287 287 GLY GLY B . n 
B 1 288 GLY 288 288 288 GLY GLY B . n 
B 1 289 LYS 289 289 289 LYS LYS B . n 
B 1 290 ASN 290 290 290 ASN ASN B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 LEU 292 292 292 LEU LEU B . n 
B 1 293 LEU 293 293 293 LEU LEU B . n 
B 1 294 LEU 294 294 294 LEU LEU B . n 
B 1 295 ALA 295 295 295 ALA ALA B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 THR 297 297 297 THR THR B . n 
B 1 298 ILE 298 298 298 ILE ILE B . n 
B 1 299 MET 299 299 299 MET MET B . n 
B 1 300 SER 300 300 300 SER SER B . n 
B 1 301 VAL 301 301 301 VAL VAL B . n 
B 1 302 ARG 302 302 302 ARG ARG B . n 
B 1 303 ILE 303 303 303 ILE ILE B . n 
B 1 304 ILE 304 304 304 ILE ILE B . n 
B 1 305 GLY 305 305 305 GLY GLY B . n 
B 1 306 SER 306 306 306 SER SER B . n 
B 1 307 SER 307 307 307 SER SER B . n 
B 1 308 PHE 308 308 308 PHE PHE B . n 
B 1 309 ALA 309 309 309 ALA ALA B . n 
B 1 310 THR 310 310 310 THR THR B . n 
B 1 311 SER 311 311 311 SER SER B . n 
B 1 312 ALA 312 312 312 ALA ALA B . n 
B 1 313 LEU 313 313 313 LEU LEU B . n 
B 1 314 GLU 314 314 314 GLU GLU B . n 
B 1 315 VAL 315 315 315 VAL VAL B . n 
B 1 316 VAL 316 316 316 VAL VAL 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 LYS 319 319 319 LYS LYS B . n 
B 1 320 THR 320 320 320 THR THR B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 HIS 322 322 322 HIS HIS B . n 
B 1 323 MET 323 323 323 MET MET B . n 
B 1 324 PHE 324 324 324 PHE PHE B . n 
B 1 325 GLU 325 325 325 GLU GLU B . n 
B 1 326 VAL 326 326 326 VAL VAL B . n 
B 1 327 PRO 327 327 327 PRO PRO B . n 
B 1 328 PHE 328 328 328 PHE PHE B . n 
B 1 329 LEU 329 329 329 LEU LEU B . n 
B 1 330 LEU 330 330 330 LEU LEU B . n 
B 1 331 VAL 331 331 331 VAL VAL B . n 
B 1 332 GLY 332 332 332 GLY GLY B . n 
B 1 333 CYS 333 333 333 CYS CYS B . n 
B 1 334 PHE 334 334 334 PHE PHE B . n 
B 1 335 LYS 335 335 335 LYS LYS B . n 
B 1 336 TYR 336 336 336 TYR TYR B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 THR 338 338 338 THR THR B . n 
B 1 339 SER 339 339 339 SER SER B . n 
B 1 340 GLN 340 340 340 GLN GLN B . n 
B 1 341 PHE 341 341 341 PHE PHE B . n 
B 1 342 GLU 342 342 342 GLU GLU B . n 
B 1 343 VAL 343 343 343 VAL VAL B . n 
B 1 344 ARG 344 344 344 ARG ARG B . n 
B 1 345 PHE 345 345 345 PHE PHE B . n 
B 1 346 SER 346 346 346 SER SER B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 THR 348 348 348 THR THR B . n 
B 1 349 ILE 349 349 349 ILE ILE B . n 
B 1 350 TYR 350 350 350 TYR TYR B . n 
B 1 351 LEU 351 351 351 LEU LEU B . n 
B 1 352 VAL 352 352 352 VAL VAL B . n 
B 1 353 CYS 353 353 353 CYS CYS B . n 
B 1 354 PHE 354 354 354 PHE PHE B . n 
B 1 355 CYS 355 355 355 CYS CYS B . n 
B 1 356 PHE 356 356 356 PHE PHE B . n 
B 1 357 PHE 357 357 357 PHE PHE B . n 
B 1 358 LYS 358 358 358 LYS LYS B . n 
B 1 359 GLN 359 359 359 GLN GLN B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 ALA 361 361 361 ALA ALA B . n 
B 1 362 MET 362 362 362 MET MET B . n 
B 1 363 ILE 363 363 363 ILE ILE B . n 
B 1 364 PHE 364 364 364 PHE PHE B . n 
B 1 365 MET 365 365 365 MET MET B . n 
B 1 366 SER 366 366 366 SER SER B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 LEU 368 368 368 LEU LEU B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 GLY 370 370 370 GLY GLY B . n 
B 1 371 ASN 371 371 371 ASN ASN B . n 
B 1 372 MET 372 372 372 MET MET B . n 
B 1 373 TYR 373 373 373 TYR TYR B . n 
B 1 374 GLU 374 374 374 GLU GLU B . n 
B 1 375 SER 375 375 375 SER SER B . n 
B 1 376 ILE 376 376 376 ILE ILE B . n 
B 1 377 GLY 377 377 377 GLY GLY B . n 
B 1 378 PHE 378 378 378 PHE PHE B . n 
B 1 379 GLN 379 379 379 GLN GLN B . n 
B 1 380 GLY 380 380 380 GLY GLY B . n 
B 1 381 ALA 381 381 381 ALA ALA B . n 
B 1 382 TYR 382 382 382 TYR TYR B . n 
B 1 383 LEU 383 383 383 LEU LEU B . n 
B 1 384 VAL 384 384 384 VAL VAL B . n 
B 1 385 LEU 385 385 385 LEU LEU B . n 
B 1 386 GLY 386 386 386 GLY GLY B . n 
B 1 387 LEU 387 387 387 LEU LEU B . n 
B 1 388 VAL 388 388 388 VAL VAL B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 LEU 390 390 390 LEU LEU B . n 
B 1 391 GLY 391 391 391 GLY GLY B . n 
B 1 392 PHE 392 392 392 PHE PHE B . n 
B 1 393 THR 393 393 393 THR THR B . n 
B 1 394 LEU 394 394 394 LEU LEU B . n 
B 1 395 ILE 395 395 395 ILE ILE B . n 
B 1 396 SER 396 396 396 SER SER B . n 
B 1 397 VAL 397 397 397 VAL VAL B . n 
B 1 398 PHE 398 398 398 PHE PHE B . n 
B 1 399 THR 399 399 399 THR THR B . n 
B 1 400 LEU 400 400 400 LEU LEU B . n 
B 1 401 SER 401 401 401 SER SER B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 PRO 403 403 403 PRO PRO B . n 
B 1 404 GLY 404 404 404 GLY GLY B . n 
B 1 405 PRO 405 405 405 PRO PRO B . n 
B 1 406 LEU 406 406 406 LEU LEU B . n 
B 1 407 SER 407 407 407 SER SER B . n 
B 1 408 LEU 408 408 408 LEU LEU B . n 
B 1 409 LEU 409 409 409 LEU LEU B . n 
B 1 410 ARG 410 410 410 ARG ARG B . n 
B 1 411 ARG 411 411 411 ARG ARG B . n 
B 1 412 GLN 412 412 412 GLN GLN B . n 
B 1 413 VAL 413 413 413 VAL VAL B . n 
B 1 414 ASN 414 414 414 ASN ASN B . n 
B 1 415 GLU 415 415 415 GLU GLU B . n 
B 1 416 VAL 416 416 416 VAL VAL B . n 
B 1 417 ALA 417 417 417 ALA ALA B . n 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
DENZO     'data reduction' . ? 1 
SCALEPACK 'data scaling'   . ? 2 
SHARP     phasing          . ? 3 
CNS       refinement       . ? 4 
# 
_cell.entry_id           1PV6 
_cell.length_a           101.351 
_cell.length_b           125.845 
_cell.length_c           188.118 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              8 
# 
_symmetry.entry_id                         1PV6 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.Int_Tables_number                19 
_symmetry.cell_setting                     ? 
# 
_exptl.entry_id          1PV6 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      6.45 
_exptl_crystal.density_percent_sol   ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pdbx_details    'PEG 400, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2003-03-28 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si 111' 
_diffrn_radiation.pdbx_diffrn_protocol             MAD 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.009 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SLS BEAMLINE X06SA' 
_diffrn_source.pdbx_synchrotron_site       SLS 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.009 
# 
_reflns.entry_id                     1PV6 
_reflns.observed_criterion_sigma_F   0.0 
_reflns.observed_criterion_sigma_I   -1.0 
_reflns.d_resolution_high            3.5 
_reflns.d_resolution_low             40.0 
_reflns.number_all                   31004 
_reflns.number_obs                   25733 
_reflns.percent_possible_obs         83.0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             3.5 
_reflns_shell.d_res_low              3.6 
_reflns_shell.percent_possible_all   71.8 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1PV6 
_refine.ls_d_res_high                            3.5 
_refine.ls_d_res_low                             40 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     31004 
_refine.ls_number_reflns_obs                     25733 
_refine.ls_number_reflns_R_free                  1310 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.294 
_refine.ls_R_factor_R_work                       0.294 
_refine.ls_R_factor_R_free                       0.337 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_method_to_determine_struct          MAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.B_iso_mean                               ? 
_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.details                                  ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6580 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               6580 
_refine_hist.d_res_high                       3.5 
_refine_hist.d_res_low                        40 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d           0.012 ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        1.8   ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d 19.6  ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d 1.0   ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_database_PDB_matrix.entry_id          1PV6 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_struct.entry_id                  1PV6 
_struct.title                     'Crystal structure of lactose permease' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1PV6 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
_struct_keywords.text            'Transport, Sugar transport, Symport, membrane protein, TRANSPORT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LACY_ECOLI 
_struct_ref.pdbx_db_accession          P02920 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWII
TGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGI
MFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFD
QQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKT
LHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQLAMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTL
SGPGPLSLLRRQVNEVA
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
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 1PV6 A 1 ? 417 ? P02920 1 ? 417 ? 1 417 
2 1 1PV6 B 1 ? 417 ? P02920 1 ? 417 ? 1 417 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 1PV6 GLY A 154 ? UNP P02920 CYS 154 'engineered mutation' 154 1 
2 1PV6 GLY B 154 ? UNP P02920 CYS 154 'engineered mutation' 154 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A 
2 1 B 
# 
_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  1  MET A 1   ? ASN A 6   ? MET A 1   ASN A 6   1 ? 6  
HELX_P HELX_P2  2  ASN A 6   ? HIS A 39  ? ASN A 6   HIS A 39  1 ? 34 
HELX_P HELX_P3  3  SER A 41  ? PHE A 59  ? SER A 41  PHE A 59  1 ? 19 
HELX_P HELX_P4  4  PHE A 59  ? GLY A 71  ? PHE A 59  GLY A 71  1 ? 13 
HELX_P HELX_P5  5  LYS A 74  ? MET A 86  ? LYS A 74  MET A 86  1 ? 13 
HELX_P HELX_P6  6  MET A 86  ? ILE A 94  ? MET A 86  ILE A 94  1 ? 9  
HELX_P HELX_P7  7  ILE A 94  ? TYR A 101 ? ILE A 94  TYR A 101 1 ? 8  
HELX_P HELX_P8  8  ILE A 103 ? ILE A 112 ? ILE A 103 ILE A 112 1 ? 10 
HELX_P HELX_P9  9  ALA A 120 ? ASN A 137 ? ALA A 120 ASN A 137 1 ? 18 
HELX_P HELX_P10 10 GLU A 139 ? ASN A 165 ? GLU A 139 ASN A 165 1 ? 27 
HELX_P HELX_P11 11 ASN A 165 ? PHE A 186 ? ASN A 165 PHE A 186 1 ? 22 
HELX_P HELX_P12 12 SER A 209 ? GLN A 219 ? SER A 209 GLN A 219 1 ? 11 
HELX_P HELX_P13 13 GLN A 219 ? THR A 248 ? GLN A 219 THR A 248 1 ? 30 
HELX_P HELX_P14 14 THR A 253 ? PHE A 277 ? THR A 253 PHE A 277 1 ? 25 
HELX_P HELX_P15 15 PHE A 278 ? GLY A 287 ? PHE A 278 GLY A 287 1 ? 10 
HELX_P HELX_P16 16 GLY A 287 ? PHE A 308 ? GLY A 287 PHE A 308 1 ? 22 
HELX_P HELX_P17 17 SER A 311 ? PHE A 341 ? SER A 311 PHE A 341 1 ? 31 
HELX_P HELX_P18 18 GLU A 342 ? ARG A 344 ? GLU A 342 ARG A 344 5 ? 3  
HELX_P HELX_P19 19 PHE A 345 ? CYS A 355 ? PHE A 345 CYS A 355 1 ? 11 
HELX_P HELX_P20 20 PHE A 357 ? GLY A 377 ? PHE A 357 GLY A 377 1 ? 21 
HELX_P HELX_P21 21 GLY A 377 ? LEU A 400 ? GLY A 377 LEU A 400 1 ? 24 
HELX_P HELX_P22 22 SER A 407 ? ALA A 417 ? SER A 407 ALA A 417 1 ? 11 
HELX_P HELX_P23 23 MET B 1   ? ASN B 6   ? MET B 1   ASN B 6   1 ? 6  
HELX_P HELX_P24 24 ASN B 6   ? HIS B 39  ? ASN B 6   HIS B 39  1 ? 34 
HELX_P HELX_P25 25 SER B 41  ? PHE B 59  ? SER B 41  PHE B 59  1 ? 19 
HELX_P HELX_P26 26 PHE B 59  ? GLY B 71  ? PHE B 59  GLY B 71  1 ? 13 
HELX_P HELX_P27 27 LYS B 74  ? MET B 86  ? LYS B 74  MET B 86  1 ? 13 
HELX_P HELX_P28 28 MET B 86  ? ILE B 94  ? MET B 86  ILE B 94  1 ? 9  
HELX_P HELX_P29 29 ILE B 94  ? TYR B 101 ? ILE B 94  TYR B 101 1 ? 8  
HELX_P HELX_P30 30 ILE B 103 ? ILE B 112 ? ILE B 103 ILE B 112 1 ? 10 
HELX_P HELX_P31 31 ALA B 120 ? ASN B 137 ? ALA B 120 ASN B 137 1 ? 18 
HELX_P HELX_P32 32 GLU B 139 ? ASN B 165 ? GLU B 139 ASN B 165 1 ? 27 
HELX_P HELX_P33 33 ASN B 165 ? PHE B 186 ? ASN B 165 PHE B 186 1 ? 22 
HELX_P HELX_P34 34 SER B 209 ? GLN B 219 ? SER B 209 GLN B 219 1 ? 11 
HELX_P HELX_P35 35 GLN B 219 ? THR B 248 ? GLN B 219 THR B 248 1 ? 30 
HELX_P HELX_P36 36 THR B 253 ? PHE B 277 ? THR B 253 PHE B 277 1 ? 25 
HELX_P HELX_P37 37 PHE B 278 ? GLY B 287 ? PHE B 278 GLY B 287 1 ? 10 
HELX_P HELX_P38 38 GLY B 287 ? PHE B 308 ? GLY B 287 PHE B 308 1 ? 22 
HELX_P HELX_P39 39 SER B 311 ? PHE B 341 ? SER B 311 PHE B 341 1 ? 31 
HELX_P HELX_P40 40 GLU B 342 ? ARG B 344 ? GLU B 342 ARG B 344 5 ? 3  
HELX_P HELX_P41 41 PHE B 345 ? CYS B 355 ? PHE B 345 CYS B 355 1 ? 11 
HELX_P HELX_P42 42 PHE B 357 ? GLY B 377 ? PHE B 357 GLY B 377 1 ? 21 
HELX_P HELX_P43 43 GLY B 377 ? LEU B 400 ? GLY B 377 LEU B 400 1 ? 24 
HELX_P HELX_P44 44 SER B 407 ? ALA B 417 ? SER B 407 ALA B 417 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A MET 1 ? ? N A LEU 4 ? ? 2.13 
2 1 O B MET 1 ? ? N B TYR 3 ? ? 2.15 
3 1 O B MET 1 ? ? N B LEU 4 ? ? 2.17 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            B 
_pdbx_validate_rmsd_bond.auth_comp_id_1            CYS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             176 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            SG 
_pdbx_validate_rmsd_bond.auth_asym_id_2            B 
_pdbx_validate_rmsd_bond.auth_comp_id_2            CYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             176 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.716 
_pdbx_validate_rmsd_bond.bond_target_value         1.812 
_pdbx_validate_rmsd_bond.bond_deviation            -0.096 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.016 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1   1 TYR A 2   ? ? -12.24  -45.18  
2   1 THR A 7   ? ? -54.50  -71.64  
3   1 PHE A 9   ? ? -52.17  -70.96  
4   1 MET A 11  ? ? -47.71  -75.78  
5   1 TYR A 26  ? ? -28.30  -89.32  
6   1 PHE A 27  ? ? -31.17  -72.68  
7   1 PHE A 30  ? ? -35.38  -79.01  
8   1 HIS A 35  ? ? -60.20  -81.82  
9   1 HIS A 39  ? ? 30.67   43.01   
10  1 LEU A 72  ? ? -104.78 46.00   
11  1 TYR A 75  ? ? -23.52  -62.33  
12  1 ILE A 79  ? ? -47.53  -14.52  
13  1 ILE A 80  ? ? -90.28  -60.87  
14  1 LEU A 99  ? ? -80.80  -71.12  
15  1 ASN A 102 ? ? 81.47   62.23   
16  1 ILE A 103 ? ? -152.84 59.63   
17  1 ILE A 108 ? ? -59.68  -82.84  
18  1 ILE A 112 ? ? -94.58  45.77   
19  1 CYS A 117 ? ? -46.70  3.07    
20  1 ALA A 122 ? ? -53.10  -72.36  
21  1 ALA A 124 ? ? -68.50  -77.28  
22  1 ALA A 127 ? ? -78.43  -82.24  
23  1 PHE A 128 ? ? -27.66  -63.03  
24  1 ASN A 137 ? ? 123.70  -31.01  
25  1 ILE A 160 ? ? -48.48  -79.56  
26  1 ASN A 165 ? ? 179.02  83.62   
27  1 LYS A 188 ? ? -118.93 -157.06 
28  1 SER A 193 ? ? -162.37 58.29   
29  1 SER A 194 ? ? 101.19  -7.48   
30  1 ALA A 195 ? ? -93.81  39.34   
31  1 THR A 196 ? ? 56.43   140.00  
32  1 ASN A 204 ? ? 57.19   -167.51 
33  1 ALA A 213 ? ? -51.14  -70.42  
34  1 TYR A 228 ? ? -44.01  -80.68  
35  1 THR A 235 ? ? -40.43  -71.85  
36  1 PHE A 239 ? ? -40.78  -73.47  
37  1 PHE A 250 ? ? -63.53  9.79    
38  1 VAL A 264 ? ? -32.68  -83.34  
39  1 ALA A 279 ? ? -35.39  -71.03  
40  1 ILE A 286 ? ? -94.56  -63.10  
41  1 LYS A 289 ? ? -29.54  -45.77  
42  1 LYS A 319 ? ? -65.05  -74.78  
43  1 THR A 320 ? ? -12.53  -59.03  
44  1 LEU A 321 ? ? -43.85  -17.59  
45  1 VAL A 326 ? ? -42.35  -84.53  
46  1 VAL A 343 ? ? -33.99  -32.96  
47  1 SER A 346 ? ? -33.26  -84.20  
48  1 PHE A 378 ? ? -34.96  -72.96  
49  1 PRO A 405 ? ? -46.54  173.71  
50  1 LEU A 406 ? ? -50.53  14.29   
51  1 SER A 407 ? ? 179.44  69.52   
52  1 TYR B 2   ? ? -8.49   -47.54  
53  1 MET B 11  ? ? -51.86  -70.53  
54  1 TYR B 26  ? ? -30.62  -89.08  
55  1 PHE B 27  ? ? -30.19  -72.77  
56  1 PHE B 29  ? ? -28.80  -55.36  
57  1 PHE B 30  ? ? -35.24  -78.61  
58  1 HIS B 35  ? ? -61.93  -83.25  
59  1 HIS B 39  ? ? 34.77   44.96   
60  1 LEU B 72  ? ? -106.81 47.50   
61  1 TYR B 75  ? ? -20.95  -64.95  
62  1 ILE B 79  ? ? -48.21  -16.49  
63  1 MET B 86  ? ? -79.40  27.25   
64  1 PHE B 95  ? ? -53.41  -71.93  
65  1 LEU B 99  ? ? -78.82  -72.08  
66  1 ASN B 102 ? ? 80.81   62.92   
67  1 ILE B 103 ? ? -154.84 59.55   
68  1 ILE B 108 ? ? -59.15  -85.89  
69  1 ILE B 112 ? ? -92.32  43.64   
70  1 CYS B 117 ? ? -46.30  1.97    
71  1 ALA B 122 ? ? -53.42  -71.23  
72  1 ALA B 124 ? ? -65.19  -82.02  
73  1 ALA B 127 ? ? -75.55  -81.56  
74  1 PHE B 128 ? ? -28.14  -62.10  
75  1 ASN B 137 ? ? 123.36  -31.37  
76  1 ILE B 160 ? ? -50.11  -81.39  
77  1 ASN B 165 ? ? 179.74  87.69   
78  1 LYS B 188 ? ? -115.29 -157.35 
79  1 SER B 193 ? ? -162.02 60.66   
80  1 SER B 194 ? ? 98.04   -5.67   
81  1 ALA B 195 ? ? -96.08  38.54   
82  1 THR B 196 ? ? 58.19   138.63  
83  1 ASN B 204 ? ? 52.60   -166.80 
84  1 ALA B 213 ? ? -52.67  -71.08  
85  1 TYR B 228 ? ? -45.43  -78.52  
86  1 THR B 235 ? ? -40.80  -71.28  
87  1 PHE B 239 ? ? -40.25  -72.88  
88  1 PHE B 250 ? ? -60.72  6.94    
89  1 VAL B 264 ? ? -33.05  -81.90  
90  1 ALA B 279 ? ? -35.29  -71.12  
91  1 ILE B 286 ? ? -90.07  -68.22  
92  1 LYS B 289 ? ? -29.48  -44.69  
93  1 LYS B 319 ? ? -63.61  -73.37  
94  1 THR B 320 ? ? -11.14  -61.90  
95  1 LEU B 321 ? ? -41.47  -17.87  
96  1 VAL B 326 ? ? -41.75  -86.44  
97  1 VAL B 343 ? ? -34.43  -30.82  
98  1 SER B 346 ? ? -34.74  -82.24  
99  1 PHE B 378 ? ? -37.82  -74.01  
100 1 PRO B 405 ? ? -42.94  174.29  
101 1 LEU B 406 ? ? -51.00  14.30   
102 1 SER B 407 ? ? 178.28  69.43   
# 
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 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
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 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_atom_sites.entry_id                    1PV6 
_atom_sites.fract_transf_matrix[1][1]   0.009867 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007946 
_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]   0.005316 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . MET A 1 1   ? 48.103 90.327  145.275 1.00 83.10  ? 1   MET A N   1 
ATOM 2    C CA  . MET A 1 1   ? 48.436 90.003  143.850 1.00 84.32  ? 1   MET A CA  1 
ATOM 3    C C   . MET A 1 1   ? 48.040 88.555  143.560 1.00 85.11  ? 1   MET A C   1 
ATOM 4    O O   . MET A 1 1   ? 47.987 87.754  144.474 1.00 84.74  ? 1   MET A O   1 
ATOM 5    C CB  . MET A 1 1   ? 49.920 90.272  143.604 1.00 83.86  ? 1   MET A CB  1 
ATOM 6    C CG  . MET A 1 1   ? 50.338 91.659  144.116 1.00 84.17  ? 1   MET A CG  1 
ATOM 7    S SD  . MET A 1 1   ? 52.042 92.097  143.769 1.00 85.04  ? 1   MET A SD  1 
ATOM 8    C CE  . MET A 1 1   ? 51.964 92.350  141.924 1.00 84.84  ? 1   MET A CE  1 
ATOM 9    N N   . TYR A 1 2   ? 47.745 88.238  142.296 1.00 86.77  ? 2   TYR A N   1 
ATOM 10   C CA  . TYR A 1 2   ? 47.266 86.901  141.895 1.00 88.64  ? 2   TYR A CA  1 
ATOM 11   C C   . TYR A 1 2   ? 47.417 85.840  142.981 1.00 89.50  ? 2   TYR A C   1 
ATOM 12   O O   . TYR A 1 2   ? 46.490 85.071  143.240 1.00 90.25  ? 2   TYR A O   1 
ATOM 13   C CB  . TYR A 1 2   ? 47.936 86.430  140.594 1.00 88.19  ? 2   TYR A CB  1 
ATOM 14   C CG  . TYR A 1 2   ? 49.229 85.680  140.760 1.00 87.50  ? 2   TYR A CG  1 
ATOM 15   C CD1 . TYR A 1 2   ? 49.236 84.317  141.078 1.00 86.99  ? 2   TYR A CD1 1 
ATOM 16   C CD2 . TYR A 1 2   ? 50.445 86.316  140.511 1.00 87.31  ? 2   TYR A CD2 1 
ATOM 17   C CE1 . TYR A 1 2   ? 50.425 83.606  141.129 1.00 86.77  ? 2   TYR A CE1 1 
ATOM 18   C CE2 . TYR A 1 2   ? 51.634 85.623  140.554 1.00 87.18  ? 2   TYR A CE2 1 
ATOM 19   C CZ  . TYR A 1 2   ? 51.622 84.265  140.857 1.00 87.28  ? 2   TYR A CZ  1 
ATOM 20   O OH  . TYR A 1 2   ? 52.809 83.569  140.831 1.00 87.40  ? 2   TYR A OH  1 
ATOM 21   N N   . TYR A 1 3   ? 48.580 85.818  143.620 1.00 90.25  ? 3   TYR A N   1 
ATOM 22   C CA  . TYR A 1 3   ? 48.855 84.875  144.684 1.00 90.83  ? 3   TYR A CA  1 
ATOM 23   C C   . TYR A 1 3   ? 48.042 85.163  145.950 1.00 89.46  ? 3   TYR A C   1 
ATOM 24   O O   . TYR A 1 3   ? 47.906 84.302  146.831 1.00 90.17  ? 3   TYR A O   1 
ATOM 25   C CB  . TYR A 1 3   ? 50.355 84.886  144.992 1.00 92.47  ? 3   TYR A CB  1 
ATOM 26   C CG  . TYR A 1 3   ? 51.062 86.197  144.698 1.00 94.79  ? 3   TYR A CG  1 
ATOM 27   C CD1 . TYR A 1 3   ? 51.007 87.266  145.600 1.00 95.97  ? 3   TYR A CD1 1 
ATOM 28   C CD2 . TYR A 1 3   ? 51.816 86.358  143.528 1.00 95.51  ? 3   TYR A CD2 1 
ATOM 29   C CE1 . TYR A 1 3   ? 51.694 88.458  145.352 1.00 96.46  ? 3   TYR A CE1 1 
ATOM 30   C CE2 . TYR A 1 3   ? 52.508 87.550  143.263 1.00 95.81  ? 3   TYR A CE2 1 
ATOM 31   C CZ  . TYR A 1 3   ? 52.440 88.592  144.186 1.00 96.26  ? 3   TYR A CZ  1 
ATOM 32   O OH  . TYR A 1 3   ? 53.125 89.765  143.980 1.00 96.08  ? 3   TYR A OH  1 
ATOM 33   N N   . LEU A 1 4   ? 47.488 86.372  146.014 1.00 88.14  ? 4   LEU A N   1 
ATOM 34   C CA  . LEU A 1 4   ? 46.683 86.826  147.149 1.00 85.99  ? 4   LEU A CA  1 
ATOM 35   C C   . LEU A 1 4   ? 45.238 87.054  146.714 1.00 83.47  ? 4   LEU A C   1 
ATOM 36   O O   . LEU A 1 4   ? 44.325 87.111  147.548 1.00 82.88  ? 4   LEU A O   1 
ATOM 37   C CB  . LEU A 1 4   ? 47.268 88.130  147.735 1.00 87.93  ? 4   LEU A CB  1 
ATOM 38   C CG  . LEU A 1 4   ? 48.694 88.163  148.354 1.00 88.86  ? 4   LEU A CG  1 
ATOM 39   C CD1 . LEU A 1 4   ? 48.971 89.573  148.907 1.00 88.62  ? 4   LEU A CD1 1 
ATOM 40   C CD2 . LEU A 1 4   ? 48.857 87.117  149.445 1.00 88.66  ? 4   LEU A CD2 1 
ATOM 41   N N   . LYS A 1 5   ? 45.032 87.187  145.411 1.00 79.65  ? 5   LYS A N   1 
ATOM 42   C CA  . LYS A 1 5   ? 43.690 87.399  144.918 1.00 76.53  ? 5   LYS A CA  1 
ATOM 43   C C   . LYS A 1 5   ? 42.907 86.101  144.819 1.00 75.32  ? 5   LYS A C   1 
ATOM 44   O O   . LYS A 1 5   ? 41.763 86.046  145.230 1.00 75.82  ? 5   LYS A O   1 
ATOM 45   C CB  . LYS A 1 5   ? 43.727 88.045  143.549 1.00 75.19  ? 5   LYS A CB  1 
ATOM 46   C CG  . LYS A 1 5   ? 44.562 89.285  143.461 1.00 74.73  ? 5   LYS A CG  1 
ATOM 47   C CD  . LYS A 1 5   ? 44.614 89.763  142.009 1.00 74.77  ? 5   LYS A CD  1 
ATOM 48   C CE  . LYS A 1 5   ? 45.396 91.072  141.876 1.00 75.13  ? 5   LYS A CE  1 
ATOM 49   N NZ  . LYS A 1 5   ? 45.599 91.552  140.465 1.00 75.08  ? 5   LYS A NZ  1 
ATOM 50   N N   . ASN A 1 6   ? 43.512 85.050  144.279 1.00 73.71  ? 6   ASN A N   1 
ATOM 51   C CA  . ASN A 1 6   ? 42.798 83.776  144.108 1.00 71.66  ? 6   ASN A CA  1 
ATOM 52   C C   . ASN A 1 6   ? 42.254 83.107  145.360 1.00 70.35  ? 6   ASN A C   1 
ATOM 53   O O   . ASN A 1 6   ? 42.761 83.280  146.467 1.00 69.28  ? 6   ASN A O   1 
ATOM 54   C CB  . ASN A 1 6   ? 43.679 82.768  143.392 1.00 72.22  ? 6   ASN A CB  1 
ATOM 55   C CG  . ASN A 1 6   ? 44.763 82.243  144.282 1.00 72.51  ? 6   ASN A CG  1 
ATOM 56   O OD1 . ASN A 1 6   ? 44.485 81.612  145.306 1.00 72.27  ? 6   ASN A OD1 1 
ATOM 57   N ND2 . ASN A 1 6   ? 46.015 82.521  143.917 1.00 72.65  ? 6   ASN A ND2 1 
ATOM 58   N N   . THR A 1 7   ? 41.238 82.290  145.128 1.00 68.65  ? 7   THR A N   1 
ATOM 59   C CA  . THR A 1 7   ? 40.525 81.541  146.155 1.00 67.53  ? 7   THR A CA  1 
ATOM 60   C C   . THR A 1 7   ? 41.363 80.649  147.077 1.00 65.90  ? 7   THR A C   1 
ATOM 61   O O   . THR A 1 7   ? 41.540 80.945  148.261 1.00 65.79  ? 7   THR A O   1 
ATOM 62   C CB  . THR A 1 7   ? 39.436 80.637  145.488 1.00 68.67  ? 7   THR A CB  1 
ATOM 63   O OG1 . THR A 1 7   ? 38.527 81.451  144.727 1.00 69.39  ? 7   THR A OG1 1 
ATOM 64   C CG2 . THR A 1 7   ? 38.660 79.827  146.550 1.00 69.08  ? 7   THR A CG2 1 
ATOM 65   N N   . ASN A 1 8   ? 41.865 79.549  146.524 1.00 64.23  ? 8   ASN A N   1 
ATOM 66   C CA  . ASN A 1 8   ? 42.615 78.563  147.296 1.00 61.64  ? 8   ASN A CA  1 
ATOM 67   C C   . ASN A 1 8   ? 43.790 79.060  148.073 1.00 59.33  ? 8   ASN A C   1 
ATOM 68   O O   . ASN A 1 8   ? 44.011 78.631  149.207 1.00 58.48  ? 8   ASN A O   1 
ATOM 69   C CB  . ASN A 1 8   ? 43.017 77.442  146.375 1.00 62.85  ? 8   ASN A CB  1 
ATOM 70   C CG  . ASN A 1 8   ? 41.851 76.961  145.576 1.00 64.15  ? 8   ASN A CG  1 
ATOM 71   O OD1 . ASN A 1 8   ? 40.792 76.645  146.132 1.00 64.27  ? 8   ASN A OD1 1 
ATOM 72   N ND2 . ASN A 1 8   ? 42.013 76.926  144.263 1.00 64.90  ? 8   ASN A ND2 1 
ATOM 73   N N   . PHE A 1 9   ? 44.562 79.956  147.483 1.00 56.40  ? 9   PHE A N   1 
ATOM 74   C CA  . PHE A 1 9   ? 45.659 80.461  148.266 1.00 54.01  ? 9   PHE A CA  1 
ATOM 75   C C   . PHE A 1 9   ? 45.082 80.932  149.571 1.00 52.78  ? 9   PHE A C   1 
ATOM 76   O O   . PHE A 1 9   ? 45.332 80.349  150.615 1.00 52.11  ? 9   PHE A O   1 
ATOM 77   C CB  . PHE A 1 9   ? 46.298 81.663  147.673 1.00 53.43  ? 9   PHE A CB  1 
ATOM 78   C CG  . PHE A 1 9   ? 47.255 82.308  148.595 1.00 52.58  ? 9   PHE A CG  1 
ATOM 79   C CD1 . PHE A 1 9   ? 48.547 81.831  148.700 1.00 53.23  ? 9   PHE A CD1 1 
ATOM 80   C CD2 . PHE A 1 9   ? 46.877 83.388  149.365 1.00 52.30  ? 9   PHE A CD2 1 
ATOM 81   C CE1 . PHE A 1 9   ? 49.465 82.441  149.539 1.00 53.48  ? 9   PHE A CE1 1 
ATOM 82   C CE2 . PHE A 1 9   ? 47.792 84.001  150.207 1.00 53.34  ? 9   PHE A CE2 1 
ATOM 83   C CZ  . PHE A 1 9   ? 49.080 83.525  150.298 1.00 53.71  ? 9   PHE A CZ  1 
ATOM 84   N N   . TRP A 1 10  ? 44.348 82.036  149.499 1.00 51.20  ? 10  TRP A N   1 
ATOM 85   C CA  . TRP A 1 10  ? 43.727 82.593  150.676 1.00 50.26  ? 10  TRP A CA  1 
ATOM 86   C C   . TRP A 1 10  ? 43.269 81.428  151.522 1.00 50.18  ? 10  TRP A C   1 
ATOM 87   O O   . TRP A 1 10  ? 43.760 81.231  152.622 1.00 50.65  ? 10  TRP A O   1 
ATOM 88   C CB  . TRP A 1 10  ? 42.523 83.477  150.308 1.00 49.20  ? 10  TRP A CB  1 
ATOM 89   C CG  . TRP A 1 10  ? 42.629 84.916  150.839 1.00 47.36  ? 10  TRP A CG  1 
ATOM 90   C CD1 . TRP A 1 10  ? 41.638 85.664  151.412 1.00 46.30  ? 10  TRP A CD1 1 
ATOM 91   C CD2 . TRP A 1 10  ? 43.811 85.720  150.864 1.00 45.47  ? 10  TRP A CD2 1 
ATOM 92   N NE1 . TRP A 1 10  ? 42.146 86.887  151.808 1.00 45.56  ? 10  TRP A NE1 1 
ATOM 93   C CE2 . TRP A 1 10  ? 43.477 86.943  151.494 1.00 45.54  ? 10  TRP A CE2 1 
ATOM 94   C CE3 . TRP A 1 10  ? 45.115 85.534  150.454 1.00 43.85  ? 10  TRP A CE3 1 
ATOM 95   C CZ2 . TRP A 1 10  ? 44.420 87.956  151.679 1.00 44.41  ? 10  TRP A CZ2 1 
ATOM 96   C CZ3 . TRP A 1 10  ? 46.022 86.517  150.640 1.00 43.58  ? 10  TRP A CZ3 1 
ATOM 97   C CH2 . TRP A 1 10  ? 45.684 87.715  151.257 1.00 43.37  ? 10  TRP A CH2 1 
ATOM 98   N N   . MET A 1 11  ? 42.369 80.621  150.979 1.00 50.55  ? 11  MET A N   1 
ATOM 99   C CA  . MET A 1 11  ? 41.823 79.486  151.709 1.00 51.03  ? 11  MET A CA  1 
ATOM 100  C C   . MET A 1 11  ? 42.830 78.601  152.408 1.00 50.62  ? 11  MET A C   1 
ATOM 101  O O   . MET A 1 11  ? 42.972 78.647  153.635 1.00 50.76  ? 11  MET A O   1 
ATOM 102  C CB  . MET A 1 11  ? 40.956 78.646  150.782 1.00 52.59  ? 11  MET A CB  1 
ATOM 103  C CG  . MET A 1 11  ? 39.883 79.464  150.130 1.00 52.95  ? 11  MET A CG  1 
ATOM 104  S SD  . MET A 1 11  ? 38.883 80.255  151.363 1.00 54.79  ? 11  MET A SD  1 
ATOM 105  C CE  . MET A 1 11  ? 39.790 81.844  151.658 1.00 54.41  ? 11  MET A CE  1 
ATOM 106  N N   . PHE A 1 12  ? 43.528 77.775  151.651 1.00 49.62  ? 12  PHE A N   1 
ATOM 107  C CA  . PHE A 1 12  ? 44.481 76.911  152.306 1.00 47.82  ? 12  PHE A CA  1 
ATOM 108  C C   . PHE A 1 12  ? 45.516 77.658  153.118 1.00 46.18  ? 12  PHE A C   1 
ATOM 109  O O   . PHE A 1 12  ? 45.874 77.209  154.202 1.00 45.47  ? 12  PHE A O   1 
ATOM 110  C CB  . PHE A 1 12  ? 45.143 75.989  151.293 1.00 48.56  ? 12  PHE A CB  1 
ATOM 111  C CG  . PHE A 1 12  ? 44.308 74.793  150.944 1.00 49.14  ? 12  PHE A CG  1 
ATOM 112  C CD1 . PHE A 1 12  ? 43.031 74.660  151.464 1.00 49.47  ? 12  PHE A CD1 1 
ATOM 113  C CD2 . PHE A 1 12  ? 44.784 73.815  150.086 1.00 49.18  ? 12  PHE A CD2 1 
ATOM 114  C CE1 . PHE A 1 12  ? 42.244 73.570  151.145 1.00 49.20  ? 12  PHE A CE1 1 
ATOM 115  C CE2 . PHE A 1 12  ? 44.005 72.721  149.761 1.00 49.06  ? 12  PHE A CE2 1 
ATOM 116  C CZ  . PHE A 1 12  ? 42.728 72.602  150.288 1.00 49.08  ? 12  PHE A CZ  1 
ATOM 117  N N   . GLY A 1 13  ? 45.978 78.804  152.624 1.00 44.37  ? 13  GLY A N   1 
ATOM 118  C CA  . GLY A 1 13  ? 46.984 79.563  153.359 1.00 42.65  ? 13  GLY A CA  1 
ATOM 119  C C   . GLY A 1 13  ? 46.541 79.732  154.791 1.00 40.22  ? 13  GLY A C   1 
ATOM 120  O O   . GLY A 1 13  ? 47.322 79.992  155.705 1.00 38.56  ? 13  GLY A O   1 
ATOM 121  N N   . LEU A 1 14  ? 45.245 79.588  154.971 1.00 38.70  ? 14  LEU A N   1 
ATOM 122  C CA  . LEU A 1 14  ? 44.690 79.697  156.278 1.00 37.21  ? 14  LEU A CA  1 
ATOM 123  C C   . LEU A 1 14  ? 44.753 78.313  156.858 1.00 36.98  ? 14  LEU A C   1 
ATOM 124  O O   . LEU A 1 14  ? 45.159 78.142  158.002 1.00 37.10  ? 14  LEU A O   1 
ATOM 125  C CB  . LEU A 1 14  ? 43.245 80.184  156.217 1.00 37.15  ? 14  LEU A CB  1 
ATOM 126  C CG  . LEU A 1 14  ? 43.033 81.649  155.823 1.00 36.95  ? 14  LEU A CG  1 
ATOM 127  C CD1 . LEU A 1 14  ? 41.595 82.035  156.165 1.00 36.60  ? 14  LEU A CD1 1 
ATOM 128  C CD2 . LEU A 1 14  ? 44.027 82.554  156.544 1.00 36.46  ? 14  LEU A CD2 1 
ATOM 129  N N   . PHE A 1 15  ? 44.379 77.315  156.067 1.00 35.96  ? 15  PHE A N   1 
ATOM 130  C CA  . PHE A 1 15  ? 44.395 75.955  156.570 1.00 35.91  ? 15  PHE A CA  1 
ATOM 131  C C   . PHE A 1 15  ? 45.722 75.724  157.244 1.00 37.07  ? 15  PHE A C   1 
ATOM 132  O O   . PHE A 1 15  ? 45.786 75.206  158.361 1.00 38.18  ? 15  PHE A O   1 
ATOM 133  C CB  . PHE A 1 15  ? 44.194 74.941  155.459 1.00 33.80  ? 15  PHE A CB  1 
ATOM 134  C CG  . PHE A 1 15  ? 43.627 73.650  155.954 1.00 32.25  ? 15  PHE A CG  1 
ATOM 135  C CD1 . PHE A 1 15  ? 42.407 73.634  156.621 1.00 31.63  ? 15  PHE A CD1 1 
ATOM 136  C CD2 . PHE A 1 15  ? 44.319 72.465  155.814 1.00 31.31  ? 15  PHE A CD2 1 
ATOM 137  C CE1 . PHE A 1 15  ? 41.895 72.461  157.143 1.00 31.38  ? 15  PHE A CE1 1 
ATOM 138  C CE2 . PHE A 1 15  ? 43.816 71.285  156.332 1.00 30.89  ? 15  PHE A CE2 1 
ATOM 139  C CZ  . PHE A 1 15  ? 42.604 71.282  156.997 1.00 31.21  ? 15  PHE A CZ  1 
ATOM 140  N N   . PHE A 1 16  ? 46.786 76.123  156.559 1.00 38.47  ? 16  PHE A N   1 
ATOM 141  C CA  . PHE A 1 16  ? 48.131 76.014  157.110 1.00 40.03  ? 16  PHE A CA  1 
ATOM 142  C C   . PHE A 1 16  ? 48.072 76.657  158.501 1.00 40.30  ? 16  PHE A C   1 
ATOM 143  O O   . PHE A 1 16  ? 48.223 75.990  159.525 1.00 40.59  ? 16  PHE A O   1 
ATOM 144  C CB  . PHE A 1 16  ? 49.122 76.798  156.231 1.00 41.63  ? 16  PHE A CB  1 
ATOM 145  C CG  . PHE A 1 16  ? 49.920 75.939  155.273 1.00 43.35  ? 16  PHE A CG  1 
ATOM 146  C CD1 . PHE A 1 16  ? 49.308 75.316  154.202 1.00 43.08  ? 16  PHE A CD1 1 
ATOM 147  C CD2 . PHE A 1 16  ? 51.282 75.721  155.478 1.00 43.69  ? 16  PHE A CD2 1 
ATOM 148  C CE1 . PHE A 1 16  ? 50.032 74.489  153.362 1.00 42.86  ? 16  PHE A CE1 1 
ATOM 149  C CE2 . PHE A 1 16  ? 52.007 74.895  154.642 1.00 43.35  ? 16  PHE A CE2 1 
ATOM 150  C CZ  . PHE A 1 16  ? 51.377 74.279  153.583 1.00 43.40  ? 16  PHE A CZ  1 
ATOM 151  N N   . PHE A 1 17  ? 47.830 77.965  158.494 1.00 39.68  ? 17  PHE A N   1 
ATOM 152  C CA  . PHE A 1 17  ? 47.737 78.813  159.673 1.00 39.20  ? 17  PHE A CA  1 
ATOM 153  C C   . PHE A 1 17  ? 47.047 78.164  160.876 1.00 37.81  ? 17  PHE A C   1 
ATOM 154  O O   . PHE A 1 17  ? 47.557 78.211  161.986 1.00 38.05  ? 17  PHE A O   1 
ATOM 155  C CB  . PHE A 1 17  ? 47.030 80.102  159.249 1.00 40.47  ? 17  PHE A CB  1 
ATOM 156  C CG  . PHE A 1 17  ? 46.893 81.124  160.329 1.00 41.30  ? 17  PHE A CG  1 
ATOM 157  C CD1 . PHE A 1 17  ? 47.924 81.998  160.645 1.00 41.16  ? 17  PHE A CD1 1 
ATOM 158  C CD2 . PHE A 1 17  ? 45.720 81.239  161.014 1.00 40.29  ? 17  PHE A CD2 1 
ATOM 159  C CE1 . PHE A 1 17  ? 47.753 82.977  161.617 1.00 40.94  ? 17  PHE A CE1 1 
ATOM 160  C CE2 . PHE A 1 17  ? 45.563 82.213  161.975 1.00 40.08  ? 17  PHE A CE2 1 
ATOM 161  C CZ  . PHE A 1 17  ? 46.570 83.072  162.280 1.00 40.94  ? 17  PHE A CZ  1 
ATOM 162  N N   . PHE A 1 18  ? 45.911 77.528  160.673 1.00 36.69  ? 18  PHE A N   1 
ATOM 163  C CA  . PHE A 1 18  ? 45.262 76.932  161.804 1.00 36.43  ? 18  PHE A CA  1 
ATOM 164  C C   . PHE A 1 18  ? 45.684 75.498  162.148 1.00 37.99  ? 18  PHE A C   1 
ATOM 165  O O   . PHE A 1 18  ? 45.160 74.889  163.073 1.00 38.16  ? 18  PHE A O   1 
ATOM 166  C CB  . PHE A 1 18  ? 43.773 77.079  161.616 1.00 34.73  ? 18  PHE A CB  1 
ATOM 167  C CG  . PHE A 1 18  ? 43.315 78.502  161.674 1.00 33.36  ? 18  PHE A CG  1 
ATOM 168  C CD1 . PHE A 1 18  ? 42.970 79.047  162.882 1.00 33.60  ? 18  PHE A CD1 1 
ATOM 169  C CD2 . PHE A 1 18  ? 43.221 79.295  160.536 1.00 33.11  ? 18  PHE A CD2 1 
ATOM 170  C CE1 . PHE A 1 18  ? 42.534 80.356  162.985 1.00 33.89  ? 18  PHE A CE1 1 
ATOM 171  C CE2 . PHE A 1 18  ? 42.778 80.621  160.622 1.00 32.46  ? 18  PHE A CE2 1 
ATOM 172  C CZ  . PHE A 1 18  ? 42.435 81.149  161.852 1.00 33.03  ? 18  PHE A CZ  1 
ATOM 173  N N   . TYR A 1 19  ? 46.665 74.962  161.442 1.00 39.09  ? 19  TYR A N   1 
ATOM 174  C CA  . TYR A 1 19  ? 47.125 73.632  161.771 1.00 41.15  ? 19  TYR A CA  1 
ATOM 175  C C   . TYR A 1 19  ? 48.095 73.909  162.889 1.00 43.42  ? 19  TYR A C   1 
ATOM 176  O O   . TYR A 1 19  ? 47.937 73.453  164.015 1.00 44.54  ? 19  TYR A O   1 
ATOM 177  C CB  . TYR A 1 19  ? 47.844 73.027  160.591 1.00 40.96  ? 19  TYR A CB  1 
ATOM 178  C CG  . TYR A 1 19  ? 47.989 71.539  160.710 1.00 42.29  ? 19  TYR A CG  1 
ATOM 179  C CD1 . TYR A 1 19  ? 46.880 70.730  160.960 1.00 42.33  ? 19  TYR A CD1 1 
ATOM 180  C CD2 . TYR A 1 19  ? 49.221 70.925  160.521 1.00 42.24  ? 19  TYR A CD2 1 
ATOM 181  C CE1 . TYR A 1 19  ? 47.002 69.337  161.009 1.00 42.08  ? 19  TYR A CE1 1 
ATOM 182  C CE2 . TYR A 1 19  ? 49.349 69.538  160.569 1.00 41.95  ? 19  TYR A CE2 1 
ATOM 183  C CZ  . TYR A 1 19  ? 48.240 68.751  160.808 1.00 41.54  ? 19  TYR A CZ  1 
ATOM 184  O OH  . TYR A 1 19  ? 48.366 67.387  160.820 1.00 40.60  ? 19  TYR A OH  1 
ATOM 185  N N   . PHE A 1 20  ? 49.099 74.697  162.568 1.00 46.30  ? 20  PHE A N   1 
ATOM 186  C CA  . PHE A 1 20  ? 50.083 75.093  163.550 1.00 49.45  ? 20  PHE A CA  1 
ATOM 187  C C   . PHE A 1 20  ? 49.452 75.520  164.883 1.00 49.64  ? 20  PHE A C   1 
ATOM 188  O O   . PHE A 1 20  ? 50.103 75.481  165.920 1.00 48.53  ? 20  PHE A O   1 
ATOM 189  C CB  . PHE A 1 20  ? 50.880 76.258  163.007 1.00 53.54  ? 20  PHE A CB  1 
ATOM 190  C CG  . PHE A 1 20  ? 51.664 75.936  161.773 1.00 57.28  ? 20  PHE A CG  1 
ATOM 191  C CD1 . PHE A 1 20  ? 51.043 75.472  160.627 1.00 58.36  ? 20  PHE A CD1 1 
ATOM 192  C CD2 . PHE A 1 20  ? 53.042 76.125  161.751 1.00 58.53  ? 20  PHE A CD2 1 
ATOM 193  C CE1 . PHE A 1 20  ? 51.812 75.208  159.471 1.00 59.31  ? 20  PHE A CE1 1 
ATOM 194  C CE2 . PHE A 1 20  ? 53.804 75.867  160.618 1.00 58.91  ? 20  PHE A CE2 1 
ATOM 195  C CZ  . PHE A 1 20  ? 53.194 75.411  159.478 1.00 59.35  ? 20  PHE A CZ  1 
ATOM 196  N N   . PHE A 1 21  ? 48.188 75.924  164.869 1.00 49.94  ? 21  PHE A N   1 
ATOM 197  C CA  . PHE A 1 21  ? 47.561 76.360  166.110 1.00 51.04  ? 21  PHE A CA  1 
ATOM 198  C C   . PHE A 1 21  ? 47.366 75.222  167.020 1.00 50.26  ? 21  PHE A C   1 
ATOM 199  O O   . PHE A 1 21  ? 47.881 75.195  168.132 1.00 49.75  ? 21  PHE A O   1 
ATOM 200  C CB  . PHE A 1 21  ? 46.174 76.952  165.909 1.00 53.87  ? 21  PHE A CB  1 
ATOM 201  C CG  . PHE A 1 21  ? 46.126 78.442  166.035 1.00 57.13  ? 21  PHE A CG  1 
ATOM 202  C CD1 . PHE A 1 21  ? 46.370 79.225  164.926 1.00 59.96  ? 21  PHE A CD1 1 
ATOM 203  C CD2 . PHE A 1 21  ? 45.869 79.071  167.263 1.00 55.34  ? 21  PHE A CD2 1 
ATOM 204  C CE1 . PHE A 1 21  ? 46.361 80.604  165.038 1.00 61.25  ? 21  PHE A CE1 1 
ATOM 205  C CE2 . PHE A 1 21  ? 45.862 80.465  167.372 1.00 56.03  ? 21  PHE A CE2 1 
ATOM 206  C CZ  . PHE A 1 21  ? 46.106 81.223  166.274 1.00 59.29  ? 21  PHE A CZ  1 
ATOM 207  N N   . ILE A 1 22  ? 46.548 74.297  166.560 1.00 50.67  ? 22  ILE A N   1 
ATOM 208  C CA  . ILE A 1 22  ? 46.288 73.154  167.374 1.00 52.32  ? 22  ILE A CA  1 
ATOM 209  C C   . ILE A 1 22  ? 47.600 72.453  167.600 1.00 52.95  ? 22  ILE A C   1 
ATOM 210  O O   . ILE A 1 22  ? 47.873 72.020  168.718 1.00 53.37  ? 22  ILE A O   1 
ATOM 211  C CB  . ILE A 1 22  ? 45.371 72.155  166.718 1.00 53.23  ? 22  ILE A CB  1 
ATOM 212  C CG1 . ILE A 1 22  ? 44.448 72.843  165.731 1.00 54.25  ? 22  ILE A CG1 1 
ATOM 213  C CG2 . ILE A 1 22  ? 44.571 71.436  167.805 1.00 54.00  ? 22  ILE A CG2 1 
ATOM 214  C CD1 . ILE A 1 22  ? 43.729 71.840  164.840 1.00 56.04  ? 22  ILE A CD1 1 
ATOM 215  N N   . MET A 1 23  ? 48.410 72.330  166.550 1.00 53.71  ? 23  MET A N   1 
ATOM 216  C CA  . MET A 1 23  ? 49.685 71.640  166.695 1.00 54.61  ? 23  MET A CA  1 
ATOM 217  C C   . MET A 1 23  ? 50.465 72.379  167.745 1.00 54.21  ? 23  MET A C   1 
ATOM 218  O O   . MET A 1 23  ? 51.046 71.767  168.657 1.00 55.44  ? 23  MET A O   1 
ATOM 219  C CB  . MET A 1 23  ? 50.478 71.625  165.394 1.00 56.60  ? 23  MET A CB  1 
ATOM 220  C CG  . MET A 1 23  ? 51.847 70.930  165.517 1.00 58.72  ? 23  MET A CG  1 
ATOM 221  S SD  . MET A 1 23  ? 52.608 70.415  163.926 1.00 61.86  ? 23  MET A SD  1 
ATOM 222  C CE  . MET A 1 23  ? 53.240 72.005  163.354 1.00 60.81  ? 23  MET A CE  1 
ATOM 223  N N   . GLY A 1 24  ? 50.458 73.703  167.624 1.00 52.67  ? 24  GLY A N   1 
ATOM 224  C CA  . GLY A 1 24  ? 51.151 74.519  168.600 1.00 50.81  ? 24  GLY A CA  1 
ATOM 225  C C   . GLY A 1 24  ? 50.850 74.001  169.997 1.00 48.51  ? 24  GLY A C   1 
ATOM 226  O O   . GLY A 1 24  ? 51.648 73.252  170.576 1.00 48.99  ? 24  GLY A O   1 
ATOM 227  N N   . ALA A 1 25  ? 49.699 74.377  170.541 1.00 46.21  ? 25  ALA A N   1 
ATOM 228  C CA  . ALA A 1 25  ? 49.344 73.918  171.870 1.00 43.77  ? 25  ALA A CA  1 
ATOM 229  C C   . ALA A 1 25  ? 49.825 72.505  172.038 1.00 42.64  ? 25  ALA A C   1 
ATOM 230  O O   . ALA A 1 25  ? 50.716 72.244  172.826 1.00 41.97  ? 25  ALA A O   1 
ATOM 231  C CB  . ALA A 1 25  ? 47.853 73.952  172.062 1.00 44.91  ? 25  ALA A CB  1 
ATOM 232  N N   . TYR A 1 26  ? 49.251 71.602  171.256 1.00 40.98  ? 26  TYR A N   1 
ATOM 233  C CA  . TYR A 1 26  ? 49.623 70.208  171.340 1.00 39.93  ? 26  TYR A CA  1 
ATOM 234  C C   . TYR A 1 26  ? 51.047 69.984  171.802 1.00 40.85  ? 26  TYR A C   1 
ATOM 235  O O   . TYR A 1 26  ? 51.276 69.871  172.989 1.00 41.34  ? 26  TYR A O   1 
ATOM 236  C CB  . TYR A 1 26  ? 49.426 69.493  170.008 1.00 37.59  ? 26  TYR A CB  1 
ATOM 237  C CG  . TYR A 1 26  ? 49.871 68.038  170.035 1.00 36.00  ? 26  TYR A CG  1 
ATOM 238  C CD1 . TYR A 1 26  ? 51.188 67.683  169.728 1.00 34.96  ? 26  TYR A CD1 1 
ATOM 239  C CD2 . TYR A 1 26  ? 48.990 67.021  170.400 1.00 33.95  ? 26  TYR A CD2 1 
ATOM 240  C CE1 . TYR A 1 26  ? 51.620 66.350  169.787 1.00 32.74  ? 26  TYR A CE1 1 
ATOM 241  C CE2 . TYR A 1 26  ? 49.413 65.679  170.456 1.00 32.91  ? 26  TYR A CE2 1 
ATOM 242  C CZ  . TYR A 1 26  ? 50.729 65.355  170.148 1.00 32.13  ? 26  TYR A CZ  1 
ATOM 243  O OH  . TYR A 1 26  ? 51.155 64.047  170.182 1.00 30.37  ? 26  TYR A OH  1 
ATOM 244  N N   . PHE A 1 27  ? 52.002 69.936  170.881 1.00 42.90  ? 27  PHE A N   1 
ATOM 245  C CA  . PHE A 1 27  ? 53.377 69.639  171.243 1.00 46.70  ? 27  PHE A CA  1 
ATOM 246  C C   . PHE A 1 27  ? 53.818 70.107  172.645 1.00 48.43  ? 27  PHE A C   1 
ATOM 247  O O   . PHE A 1 27  ? 54.029 69.270  173.530 1.00 48.84  ? 27  PHE A O   1 
ATOM 248  C CB  . PHE A 1 27  ? 54.323 70.151  170.180 1.00 48.31  ? 27  PHE A CB  1 
ATOM 249  C CG  . PHE A 1 27  ? 55.680 69.566  170.290 1.00 52.26  ? 27  PHE A CG  1 
ATOM 250  C CD1 . PHE A 1 27  ? 56.604 70.091  171.204 1.00 54.13  ? 27  PHE A CD1 1 
ATOM 251  C CD2 . PHE A 1 27  ? 56.030 68.450  169.532 1.00 52.53  ? 27  PHE A CD2 1 
ATOM 252  C CE1 . PHE A 1 27  ? 57.872 69.502  171.365 1.00 56.03  ? 27  PHE A CE1 1 
ATOM 253  C CE2 . PHE A 1 27  ? 57.290 67.850  169.677 1.00 54.40  ? 27  PHE A CE2 1 
ATOM 254  C CZ  . PHE A 1 27  ? 58.218 68.374  170.596 1.00 55.86  ? 27  PHE A CZ  1 
ATOM 255  N N   . PRO A 1 28  ? 54.012 71.429  172.865 1.00 49.29  ? 28  PRO A N   1 
ATOM 256  C CA  . PRO A 1 28  ? 54.415 71.907  174.204 1.00 50.60  ? 28  PRO A CA  1 
ATOM 257  C C   . PRO A 1 28  ? 53.389 71.532  175.285 1.00 50.17  ? 28  PRO A C   1 
ATOM 258  O O   . PRO A 1 28  ? 53.688 70.785  176.204 1.00 49.62  ? 28  PRO A O   1 
ATOM 259  C CB  . PRO A 1 28  ? 54.521 73.422  174.020 1.00 50.28  ? 28  PRO A CB  1 
ATOM 260  C CG  . PRO A 1 28  ? 53.904 73.697  172.660 1.00 50.24  ? 28  PRO A CG  1 
ATOM 261  C CD  . PRO A 1 28  ? 54.216 72.491  171.866 1.00 49.54  ? 28  PRO A CD  1 
ATOM 262  N N   . PHE A 1 29  ? 52.184 72.072  175.157 1.00 50.39  ? 29  PHE A N   1 
ATOM 263  C CA  . PHE A 1 29  ? 51.090 71.787  176.082 1.00 51.22  ? 29  PHE A CA  1 
ATOM 264  C C   . PHE A 1 29  ? 51.270 70.351  176.631 1.00 47.71  ? 29  PHE A C   1 
ATOM 265  O O   . PHE A 1 29  ? 51.360 70.137  177.836 1.00 46.64  ? 29  PHE A O   1 
ATOM 266  C CB  . PHE A 1 29  ? 49.748 71.959  175.302 1.00 57.88  ? 29  PHE A CB  1 
ATOM 267  C CG  . PHE A 1 29  ? 48.460 71.822  176.143 1.00 64.61  ? 29  PHE A CG  1 
ATOM 268  C CD1 . PHE A 1 29  ? 48.012 70.566  176.560 1.00 66.83  ? 29  PHE A CD1 1 
ATOM 269  C CD2 . PHE A 1 29  ? 47.639 72.948  176.429 1.00 67.59  ? 29  PHE A CD2 1 
ATOM 270  C CE1 . PHE A 1 29  ? 46.792 70.425  177.243 1.00 67.77  ? 29  PHE A CE1 1 
ATOM 271  C CE2 . PHE A 1 29  ? 46.393 72.804  177.126 1.00 68.48  ? 29  PHE A CE2 1 
ATOM 272  C CZ  . PHE A 1 29  ? 45.976 71.535  177.525 1.00 68.38  ? 29  PHE A CZ  1 
ATOM 273  N N   . PHE A 1 30  ? 51.372 69.395  175.715 1.00 43.52  ? 30  PHE A N   1 
ATOM 274  C CA  . PHE A 1 30  ? 51.520 67.988  176.026 1.00 38.87  ? 30  PHE A CA  1 
ATOM 275  C C   . PHE A 1 30  ? 52.353 67.717  177.261 1.00 36.71  ? 30  PHE A C   1 
ATOM 276  O O   . PHE A 1 30  ? 51.816 67.438  178.346 1.00 36.39  ? 30  PHE A O   1 
ATOM 277  C CB  . PHE A 1 30  ? 52.111 67.282  174.814 1.00 37.55  ? 30  PHE A CB  1 
ATOM 278  C CG  . PHE A 1 30  ? 51.818 65.837  174.762 1.00 36.06  ? 30  PHE A CG  1 
ATOM 279  C CD1 . PHE A 1 30  ? 51.336 65.190  175.872 1.00 34.77  ? 30  PHE A CD1 1 
ATOM 280  C CD2 . PHE A 1 30  ? 51.999 65.118  173.589 1.00 36.84  ? 30  PHE A CD2 1 
ATOM 281  C CE1 . PHE A 1 30  ? 51.028 63.855  175.839 1.00 34.03  ? 30  PHE A CE1 1 
ATOM 282  C CE2 . PHE A 1 30  ? 51.688 63.772  173.552 1.00 36.45  ? 30  PHE A CE2 1 
ATOM 283  C CZ  . PHE A 1 30  ? 51.201 63.143  174.681 1.00 34.56  ? 30  PHE A CZ  1 
ATOM 284  N N   . PRO A 1 31  ? 53.674 67.786  177.129 1.00 35.52  ? 31  PRO A N   1 
ATOM 285  C CA  . PRO A 1 31  ? 54.430 67.514  178.342 1.00 34.42  ? 31  PRO A CA  1 
ATOM 286  C C   . PRO A 1 31  ? 53.864 68.215  179.577 1.00 35.44  ? 31  PRO A C   1 
ATOM 287  O O   . PRO A 1 31  ? 53.581 67.583  180.595 1.00 34.15  ? 31  PRO A O   1 
ATOM 288  C CB  . PRO A 1 31  ? 55.818 68.011  177.986 1.00 35.19  ? 31  PRO A CB  1 
ATOM 289  C CG  . PRO A 1 31  ? 55.899 67.760  176.526 1.00 34.96  ? 31  PRO A CG  1 
ATOM 290  C CD  . PRO A 1 31  ? 54.562 68.213  176.039 1.00 34.54  ? 31  PRO A CD  1 
ATOM 291  N N   . ILE A 1 32  ? 53.698 69.528  179.490 1.00 36.95  ? 32  ILE A N   1 
ATOM 292  C CA  . ILE A 1 32  ? 53.180 70.276  180.627 1.00 37.93  ? 32  ILE A CA  1 
ATOM 293  C C   . ILE A 1 32  ? 51.880 69.678  181.075 1.00 38.78  ? 32  ILE A C   1 
ATOM 294  O O   . ILE A 1 32  ? 51.690 69.399  182.252 1.00 39.04  ? 32  ILE A O   1 
ATOM 295  C CB  . ILE A 1 32  ? 52.892 71.733  180.289 1.00 38.31  ? 32  ILE A CB  1 
ATOM 296  C CG1 . ILE A 1 32  ? 54.185 72.435  179.916 1.00 39.39  ? 32  ILE A CG1 1 
ATOM 297  C CG2 . ILE A 1 32  ? 52.235 72.417  181.476 1.00 37.49  ? 32  ILE A CG2 1 
ATOM 298  C CD1 . ILE A 1 32  ? 53.970 73.683  179.106 1.00 42.32  ? 32  ILE A CD1 1 
ATOM 299  N N   . TRP A 1 33  ? 50.985 69.485  180.119 1.00 39.66  ? 33  TRP A N   1 
ATOM 300  C CA  . TRP A 1 33  ? 49.669 68.950  180.400 1.00 40.90  ? 33  TRP A CA  1 
ATOM 301  C C   . TRP A 1 33  ? 49.749 67.693  181.226 1.00 43.20  ? 33  TRP A C   1 
ATOM 302  O O   . TRP A 1 33  ? 48.857 67.392  182.012 1.00 43.68  ? 33  TRP A O   1 
ATOM 303  C CB  . TRP A 1 33  ? 48.949 68.651  179.106 1.00 38.68  ? 33  TRP A CB  1 
ATOM 304  C CG  . TRP A 1 33  ? 47.560 68.179  179.280 1.00 37.89  ? 33  TRP A CG  1 
ATOM 305  C CD1 . TRP A 1 33  ? 46.502 68.911  179.663 1.00 37.63  ? 33  TRP A CD1 1 
ATOM 306  C CD2 . TRP A 1 33  ? 47.074 66.869  179.032 1.00 38.35  ? 33  TRP A CD2 1 
ATOM 307  N NE1 . TRP A 1 33  ? 45.361 68.153  179.660 1.00 38.19  ? 33  TRP A NE1 1 
ATOM 308  C CE2 . TRP A 1 33  ? 45.683 66.894  179.264 1.00 38.31  ? 33  TRP A CE2 1 
ATOM 309  C CE3 . TRP A 1 33  ? 47.668 65.691  178.608 1.00 39.36  ? 33  TRP A CE3 1 
ATOM 310  C CZ2 . TRP A 1 33  ? 44.883 65.761  179.118 1.00 39.31  ? 33  TRP A CZ2 1 
ATOM 311  C CZ3 . TRP A 1 33  ? 46.879 64.567  178.460 1.00 40.35  ? 33  TRP A CZ3 1 
ATOM 312  C CH2 . TRP A 1 33  ? 45.492 64.613  178.703 1.00 39.94  ? 33  TRP A CH2 1 
ATOM 313  N N   . LEU A 1 34  ? 50.834 66.962  181.059 1.00 46.05  ? 34  LEU A N   1 
ATOM 314  C CA  . LEU A 1 34  ? 51.017 65.736  181.800 1.00 49.35  ? 34  LEU A CA  1 
ATOM 315  C C   . LEU A 1 34  ? 51.332 66.004  183.262 1.00 51.38  ? 34  LEU A C   1 
ATOM 316  O O   . LEU A 1 34  ? 50.688 65.474  184.174 1.00 51.54  ? 34  LEU A O   1 
ATOM 317  C CB  . LEU A 1 34  ? 52.151 64.962  181.169 1.00 48.79  ? 34  LEU A CB  1 
ATOM 318  C CG  . LEU A 1 34  ? 51.830 64.447  179.778 1.00 48.91  ? 34  LEU A CG  1 
ATOM 319  C CD1 . LEU A 1 34  ? 53.010 63.695  179.207 1.00 48.28  ? 34  LEU A CD1 1 
ATOM 320  C CD2 . LEU A 1 34  ? 50.621 63.541  179.866 1.00 48.81  ? 34  LEU A CD2 1 
ATOM 321  N N   . HIS A 1 35  ? 52.335 66.840  183.471 1.00 54.37  ? 35  HIS A N   1 
ATOM 322  C CA  . HIS A 1 35  ? 52.771 67.173  184.810 1.00 56.86  ? 35  HIS A CA  1 
ATOM 323  C C   . HIS A 1 35  ? 51.679 67.829  185.663 1.00 56.30  ? 35  HIS A C   1 
ATOM 324  O O   . HIS A 1 35  ? 51.004 67.152  186.442 1.00 56.20  ? 35  HIS A O   1 
ATOM 325  C CB  . HIS A 1 35  ? 54.006 68.074  184.711 1.00 60.14  ? 35  HIS A CB  1 
ATOM 326  C CG  . HIS A 1 35  ? 54.834 68.105  185.950 1.00 62.86  ? 35  HIS A CG  1 
ATOM 327  N ND1 . HIS A 1 35  ? 54.826 69.180  186.810 1.00 65.12  ? 35  HIS A ND1 1 
ATOM 328  C CD2 . HIS A 1 35  ? 55.696 67.207  186.475 1.00 63.92  ? 35  HIS A CD2 1 
ATOM 329  C CE1 . HIS A 1 35  ? 55.649 68.942  187.812 1.00 66.90  ? 35  HIS A CE1 1 
ATOM 330  N NE2 . HIS A 1 35  ? 56.194 67.746  187.634 1.00 65.84  ? 35  HIS A NE2 1 
ATOM 331  N N   . ASP A 1 36  ? 51.486 69.134  185.493 1.00 55.57  ? 36  ASP A N   1 
ATOM 332  C CA  . ASP A 1 36  ? 50.504 69.854  186.296 1.00 54.62  ? 36  ASP A CA  1 
ATOM 333  C C   . ASP A 1 36  ? 49.100 69.317  186.227 1.00 52.91  ? 36  ASP A C   1 
ATOM 334  O O   . ASP A 1 36  ? 48.353 69.323  187.213 1.00 53.27  ? 36  ASP A O   1 
ATOM 335  C CB  . ASP A 1 36  ? 50.472 71.325  185.909 1.00 55.98  ? 36  ASP A CB  1 
ATOM 336  C CG  . ASP A 1 36  ? 51.820 71.991  186.063 1.00 57.08  ? 36  ASP A CG  1 
ATOM 337  O OD1 . ASP A 1 36  ? 52.627 71.553  186.903 1.00 57.18  ? 36  ASP A OD1 1 
ATOM 338  O OD2 . ASP A 1 36  ? 52.066 72.975  185.347 1.00 58.71  ? 36  ASP A OD2 1 
ATOM 339  N N   . ILE A 1 37  ? 48.737 68.847  185.056 1.00 50.04  ? 37  ILE A N   1 
ATOM 340  C CA  . ILE A 1 37  ? 47.403 68.364  184.889 1.00 48.34  ? 37  ILE A CA  1 
ATOM 341  C C   . ILE A 1 37  ? 47.258 66.867  185.065 1.00 46.43  ? 37  ILE A C   1 
ATOM 342  O O   . ILE A 1 37  ? 46.258 66.398  185.584 1.00 45.88  ? 37  ILE A O   1 
ATOM 343  C CB  . ILE A 1 37  ? 46.903 68.805  183.523 1.00 49.11  ? 37  ILE A CB  1 
ATOM 344  C CG1 . ILE A 1 37  ? 47.097 70.317  183.402 1.00 49.85  ? 37  ILE A CG1 1 
ATOM 345  C CG2 . ILE A 1 37  ? 45.441 68.411  183.339 1.00 49.36  ? 37  ILE A CG2 1 
ATOM 346  C CD1 . ILE A 1 37  ? 47.237 70.781  181.984 1.00 52.18  ? 37  ILE A CD1 1 
ATOM 347  N N   . ASN A 1 38  ? 48.260 66.103  184.681 1.00 44.98  ? 38  ASN A N   1 
ATOM 348  C CA  . ASN A 1 38  ? 48.080 64.686  184.796 1.00 44.16  ? 38  ASN A CA  1 
ATOM 349  C C   . ASN A 1 38  ? 49.081 63.966  185.627 1.00 44.14  ? 38  ASN A C   1 
ATOM 350  O O   . ASN A 1 38  ? 49.305 62.775  185.450 1.00 43.97  ? 38  ASN A O   1 
ATOM 351  C CB  . ASN A 1 38  ? 48.009 64.080  183.412 1.00 44.29  ? 38  ASN A CB  1 
ATOM 352  C CG  . ASN A 1 38  ? 46.864 64.646  182.611 1.00 44.79  ? 38  ASN A CG  1 
ATOM 353  O OD1 . ASN A 1 38  ? 45.713 64.634  183.065 1.00 44.00  ? 38  ASN A OD1 1 
ATOM 354  N ND2 . ASN A 1 38  ? 47.165 65.149  181.412 1.00 44.95  ? 38  ASN A ND2 1 
ATOM 355  N N   . HIS A 1 39  ? 49.701 64.697  186.536 1.00 44.76  ? 39  HIS A N   1 
ATOM 356  C CA  . HIS A 1 39  ? 50.688 64.117  187.443 1.00 46.24  ? 39  HIS A CA  1 
ATOM 357  C C   . HIS A 1 39  ? 51.469 62.942  186.865 1.00 46.30  ? 39  HIS A C   1 
ATOM 358  O O   . HIS A 1 39  ? 51.709 61.943  187.547 1.00 45.38  ? 39  HIS A O   1 
ATOM 359  C CB  . HIS A 1 39  ? 49.968 63.661  188.694 1.00 48.35  ? 39  HIS A CB  1 
ATOM 360  C CG  . HIS A 1 39  ? 49.129 64.719  189.312 1.00 50.11  ? 39  HIS A CG  1 
ATOM 361  N ND1 . HIS A 1 39  ? 49.669 65.867  189.866 1.00 50.75  ? 39  HIS A ND1 1 
ATOM 362  C CD2 . HIS A 1 39  ? 47.784 64.851  189.429 1.00 50.67  ? 39  HIS A CD2 1 
ATOM 363  C CE1 . HIS A 1 39  ? 48.707 66.646  190.280 1.00 51.43  ? 39  HIS A CE1 1 
ATOM 364  N NE2 . HIS A 1 39  ? 47.540 66.060  190.032 1.00 51.22  ? 39  HIS A NE2 1 
ATOM 365  N N   . ILE A 1 40  ? 51.882 63.086  185.618 1.00 46.57  ? 40  ILE A N   1 
ATOM 366  C CA  . ILE A 1 40  ? 52.610 62.037  184.945 1.00 46.90  ? 40  ILE A CA  1 
ATOM 367  C C   . ILE A 1 40  ? 54.020 61.789  185.437 1.00 46.71  ? 40  ILE A C   1 
ATOM 368  O O   . ILE A 1 40  ? 54.763 62.716  185.743 1.00 46.80  ? 40  ILE A O   1 
ATOM 369  C CB  . ILE A 1 40  ? 52.696 62.329  183.474 1.00 47.58  ? 40  ILE A CB  1 
ATOM 370  C CG1 . ILE A 1 40  ? 53.154 61.096  182.733 1.00 48.50  ? 40  ILE A CG1 1 
ATOM 371  C CG2 . ILE A 1 40  ? 53.713 63.428  183.233 1.00 47.86  ? 40  ILE A CG2 1 
ATOM 372  C CD1 . ILE A 1 40  ? 52.973 61.242  181.221 1.00 49.02  ? 40  ILE A CD1 1 
ATOM 373  N N   . SER A 1 41  ? 54.382 60.523  185.528 1.00 47.10  ? 41  SER A N   1 
ATOM 374  C CA  . SER A 1 41  ? 55.720 60.202  185.947 1.00 48.42  ? 41  SER A CA  1 
ATOM 375  C C   . SER A 1 41  ? 56.501 59.975  184.675 1.00 49.31  ? 41  SER A C   1 
ATOM 376  O O   . SER A 1 41  ? 56.043 60.294  183.589 1.00 48.48  ? 41  SER A O   1 
ATOM 377  C CB  . SER A 1 41  ? 55.733 58.947  186.814 1.00 49.25  ? 41  SER A CB  1 
ATOM 378  O OG  . SER A 1 41  ? 54.922 57.944  186.239 1.00 50.62  ? 41  SER A OG  1 
ATOM 379  N N   . LYS A 1 42  ? 57.681 59.402  184.817 1.00 50.85  ? 42  LYS A N   1 
ATOM 380  C CA  . LYS A 1 42  ? 58.547 59.133  183.683 1.00 52.52  ? 42  LYS A CA  1 
ATOM 381  C C   . LYS A 1 42  ? 58.107 57.919  182.897 1.00 52.18  ? 42  LYS A C   1 
ATOM 382  O O   . LYS A 1 42  ? 57.891 58.002  181.690 1.00 51.79  ? 42  LYS A O   1 
ATOM 383  C CB  . LYS A 1 42  ? 59.980 58.930  184.172 1.00 55.31  ? 42  LYS A CB  1 
ATOM 384  C CG  . LYS A 1 42  ? 60.512 60.070  185.049 1.00 56.69  ? 42  LYS A CG  1 
ATOM 385  C CD  . LYS A 1 42  ? 60.583 61.381  184.291 1.00 57.41  ? 42  LYS A CD  1 
ATOM 386  C CE  . LYS A 1 42  ? 61.217 62.443  185.144 1.00 57.00  ? 42  LYS A CE  1 
ATOM 387  N NZ  . LYS A 1 42  ? 61.977 63.326  184.263 1.00 59.09  ? 42  LYS A NZ  1 
ATOM 388  N N   . SER A 1 43  ? 58.007 56.785  183.579 1.00 52.52  ? 43  SER A N   1 
ATOM 389  C CA  . SER A 1 43  ? 57.562 55.568  182.922 1.00 53.47  ? 43  SER A CA  1 
ATOM 390  C C   . SER A 1 43  ? 56.400 55.961  182.020 1.00 52.85  ? 43  SER A C   1 
ATOM 391  O O   . SER A 1 43  ? 56.393 55.657  180.823 1.00 53.65  ? 43  SER A O   1 
ATOM 392  C CB  . SER A 1 43  ? 57.100 54.542  183.961 1.00 54.09  ? 43  SER A CB  1 
ATOM 393  O OG  . SER A 1 43  ? 58.216 53.877  184.520 1.00 56.17  ? 43  SER A OG  1 
ATOM 394  N N   . ASP A 1 44  ? 55.436 56.667  182.604 1.00 51.47  ? 44  ASP A N   1 
ATOM 395  C CA  . ASP A 1 44  ? 54.263 57.121  181.875 1.00 49.71  ? 44  ASP A CA  1 
ATOM 396  C C   . ASP A 1 44  ? 54.641 57.990  180.660 1.00 47.10  ? 44  ASP A C   1 
ATOM 397  O O   . ASP A 1 44  ? 54.403 57.597  179.512 1.00 47.08  ? 44  ASP A O   1 
ATOM 398  C CB  . ASP A 1 44  ? 53.316 57.869  182.829 1.00 51.88  ? 44  ASP A CB  1 
ATOM 399  C CG  . ASP A 1 44  ? 52.984 57.065  184.106 1.00 52.64  ? 44  ASP A CG  1 
ATOM 400  O OD1 . ASP A 1 44  ? 52.953 55.802  184.082 1.00 51.57  ? 44  ASP A OD1 1 
ATOM 401  O OD2 . ASP A 1 44  ? 52.728 57.732  185.135 1.00 53.44  ? 44  ASP A OD2 1 
ATOM 402  N N   . THR A 1 45  ? 55.251 59.146  180.902 1.00 44.12  ? 45  THR A N   1 
ATOM 403  C CA  . THR A 1 45  ? 55.662 60.027  179.816 1.00 41.10  ? 45  THR A CA  1 
ATOM 404  C C   . THR A 1 45  ? 56.364 59.172  178.777 1.00 39.25  ? 45  THR A C   1 
ATOM 405  O O   . THR A 1 45  ? 55.871 58.961  177.662 1.00 38.43  ? 45  THR A O   1 
ATOM 406  C CB  . THR A 1 45  ? 56.657 61.077  180.316 1.00 40.54  ? 45  THR A CB  1 
ATOM 407  O OG1 . THR A 1 45  ? 57.791 60.419  180.885 1.00 40.66  ? 45  THR A OG1 1 
ATOM 408  C CG2 . THR A 1 45  ? 56.040 61.969  181.379 1.00 41.02  ? 45  THR A CG2 1 
ATOM 409  N N   . GLY A 1 46  ? 57.522 58.678  179.200 1.00 37.05  ? 46  GLY A N   1 
ATOM 410  C CA  . GLY A 1 46  ? 58.365 57.830  178.390 1.00 34.09  ? 46  GLY A CA  1 
ATOM 411  C C   . GLY A 1 46  ? 57.626 56.926  177.435 1.00 31.51  ? 46  GLY A C   1 
ATOM 412  O O   . GLY A 1 46  ? 57.997 56.825  176.276 1.00 31.65  ? 46  GLY A O   1 
ATOM 413  N N   . ILE A 1 47  ? 56.583 56.266  177.904 1.00 28.86  ? 47  ILE A N   1 
ATOM 414  C CA  . ILE A 1 47  ? 55.849 55.398  177.032 1.00 26.57  ? 47  ILE A CA  1 
ATOM 415  C C   . ILE A 1 47  ? 54.930 56.236  176.214 1.00 25.43  ? 47  ILE A C   1 
ATOM 416  O O   . ILE A 1 47  ? 54.874 56.093  175.011 1.00 25.19  ? 47  ILE A O   1 
ATOM 417  C CB  . ILE A 1 47  ? 55.051 54.400  177.804 1.00 26.11  ? 47  ILE A CB  1 
ATOM 418  C CG1 . ILE A 1 47  ? 56.011 53.478  178.540 1.00 26.93  ? 47  ILE A CG1 1 
ATOM 419  C CG2 . ILE A 1 47  ? 54.181 53.618  176.867 1.00 27.62  ? 47  ILE A CG2 1 
ATOM 420  C CD1 . ILE A 1 47  ? 55.331 52.355  179.256 1.00 28.14  ? 47  ILE A CD1 1 
ATOM 421  N N   . ILE A 1 48  ? 54.203 57.127  176.852 1.00 25.42  ? 48  ILE A N   1 
ATOM 422  C CA  . ILE A 1 48  ? 53.329 57.956  176.071 1.00 26.94  ? 48  ILE A CA  1 
ATOM 423  C C   . ILE A 1 48  ? 54.112 58.435  174.865 1.00 27.90  ? 48  ILE A C   1 
ATOM 424  O O   . ILE A 1 48  ? 53.781 58.093  173.728 1.00 27.27  ? 48  ILE A O   1 
ATOM 425  C CB  . ILE A 1 48  ? 52.848 59.146  176.871 1.00 28.13  ? 48  ILE A CB  1 
ATOM 426  C CG1 . ILE A 1 48  ? 51.977 58.656  178.024 1.00 29.43  ? 48  ILE A CG1 1 
ATOM 427  C CG2 . ILE A 1 48  ? 52.068 60.090  175.979 1.00 28.09  ? 48  ILE A CG2 1 
ATOM 428  C CD1 . ILE A 1 48  ? 51.254 59.772  178.769 1.00 31.36  ? 48  ILE A CD1 1 
ATOM 429  N N   . PHE A 1 49  ? 55.176 59.194  175.102 1.00 29.30  ? 49  PHE A N   1 
ATOM 430  C CA  . PHE A 1 49  ? 55.959 59.691  173.980 1.00 30.73  ? 49  PHE A CA  1 
ATOM 431  C C   . PHE A 1 49  ? 56.434 58.606  173.039 1.00 32.09  ? 49  PHE A C   1 
ATOM 432  O O   . PHE A 1 49  ? 56.118 58.621  171.849 1.00 32.86  ? 49  PHE A O   1 
ATOM 433  C CB  . PHE A 1 49  ? 57.140 60.503  174.460 1.00 29.53  ? 49  PHE A CB  1 
ATOM 434  C CG  . PHE A 1 49  ? 56.842 61.937  174.550 1.00 29.83  ? 49  PHE A CG  1 
ATOM 435  C CD1 . PHE A 1 49  ? 56.942 62.733  173.435 1.00 30.45  ? 49  PHE A CD1 1 
ATOM 436  C CD2 . PHE A 1 49  ? 56.426 62.495  175.734 1.00 30.91  ? 49  PHE A CD2 1 
ATOM 437  C CE1 . PHE A 1 49  ? 56.635 64.075  173.498 1.00 32.19  ? 49  PHE A CE1 1 
ATOM 438  C CE2 . PHE A 1 49  ? 56.117 63.841  175.808 1.00 32.03  ? 49  PHE A CE2 1 
ATOM 439  C CZ  . PHE A 1 49  ? 56.222 64.633  174.689 1.00 32.00  ? 49  PHE A CZ  1 
ATOM 440  N N   . ALA A 1 50  ? 57.185 57.654  173.571 1.00 33.10  ? 50  ALA A N   1 
ATOM 441  C CA  . ALA A 1 50  ? 57.684 56.560  172.751 1.00 33.52  ? 50  ALA A CA  1 
ATOM 442  C C   . ALA A 1 50  ? 56.555 55.913  171.973 1.00 33.34  ? 50  ALA A C   1 
ATOM 443  O O   . ALA A 1 50  ? 56.628 55.766  170.765 1.00 34.30  ? 50  ALA A O   1 
ATOM 444  C CB  . ALA A 1 50  ? 58.348 55.533  173.615 1.00 34.93  ? 50  ALA A CB  1 
ATOM 445  N N   . ALA A 1 51  ? 55.513 55.512  172.673 1.00 32.40  ? 51  ALA A N   1 
ATOM 446  C CA  . ALA A 1 51  ? 54.405 54.878  172.016 1.00 32.10  ? 51  ALA A CA  1 
ATOM 447  C C   . ALA A 1 51  ? 54.048 55.681  170.790 1.00 32.22  ? 51  ALA A C   1 
ATOM 448  O O   . ALA A 1 51  ? 53.996 55.150  169.684 1.00 31.24  ? 51  ALA A O   1 
ATOM 449  C CB  . ALA A 1 51  ? 53.260 54.809  172.952 1.00 33.11  ? 51  ALA A CB  1 
ATOM 450  N N   . ILE A 1 52  ? 53.821 56.970  170.991 1.00 33.24  ? 52  ILE A N   1 
ATOM 451  C CA  . ILE A 1 52  ? 53.481 57.848  169.895 1.00 35.84  ? 52  ILE A CA  1 
ATOM 452  C C   . ILE A 1 52  ? 54.320 57.475  168.692 1.00 37.48  ? 52  ILE A C   1 
ATOM 453  O O   . ILE A 1 52  ? 53.802 57.267  167.601 1.00 38.18  ? 52  ILE A O   1 
ATOM 454  C CB  . ILE A 1 52  ? 53.759 59.306  170.252 1.00 37.20  ? 52  ILE A CB  1 
ATOM 455  C CG1 . ILE A 1 52  ? 52.710 59.810  171.243 1.00 38.75  ? 52  ILE A CG1 1 
ATOM 456  C CG2 . ILE A 1 52  ? 53.760 60.141  169.001 1.00 37.78  ? 52  ILE A CG2 1 
ATOM 457  C CD1 . ILE A 1 52  ? 52.743 61.315  171.469 1.00 40.34  ? 52  ILE A CD1 1 
ATOM 458  N N   . SER A 1 53  ? 55.625 57.381  168.896 1.00 39.53  ? 53  SER A N   1 
ATOM 459  C CA  . SER A 1 53  ? 56.522 57.025  167.808 1.00 41.20  ? 53  SER A CA  1 
ATOM 460  C C   . SER A 1 53  ? 55.986 55.817  167.035 1.00 41.39  ? 53  SER A C   1 
ATOM 461  O O   . SER A 1 53  ? 55.903 55.864  165.801 1.00 41.49  ? 53  SER A O   1 
ATOM 462  C CB  . SER A 1 53  ? 57.935 56.747  168.352 1.00 42.72  ? 53  SER A CB  1 
ATOM 463  O OG  . SER A 1 53  ? 58.535 55.608  167.750 1.00 45.55  ? 53  SER A OG  1 
ATOM 464  N N   . LEU A 1 54  ? 55.590 54.756  167.747 1.00 41.39  ? 54  LEU A N   1 
ATOM 465  C CA  . LEU A 1 54  ? 55.093 53.559  167.073 1.00 41.22  ? 54  LEU A CA  1 
ATOM 466  C C   . LEU A 1 54  ? 54.138 53.954  165.977 1.00 41.19  ? 54  LEU A C   1 
ATOM 467  O O   . LEU A 1 54  ? 54.303 53.562  164.825 1.00 41.71  ? 54  LEU A O   1 
ATOM 468  C CB  . LEU A 1 54  ? 54.368 52.606  168.018 1.00 40.99  ? 54  LEU A CB  1 
ATOM 469  C CG  . LEU A 1 54  ? 53.856 51.407  167.206 1.00 40.23  ? 54  LEU A CG  1 
ATOM 470  C CD1 . LEU A 1 54  ? 54.999 50.430  167.024 1.00 40.00  ? 54  LEU A CD1 1 
ATOM 471  C CD2 . LEU A 1 54  ? 52.681 50.742  167.884 1.00 39.58  ? 54  LEU A CD2 1 
ATOM 472  N N   . PHE A 1 55  ? 53.137 54.741  166.325 1.00 40.55  ? 55  PHE A N   1 
ATOM 473  C CA  . PHE A 1 55  ? 52.203 55.149  165.312 1.00 39.75  ? 55  PHE A CA  1 
ATOM 474  C C   . PHE A 1 55  ? 52.766 56.145  164.311 1.00 39.66  ? 55  PHE A C   1 
ATOM 475  O O   . PHE A 1 55  ? 52.203 56.323  163.232 1.00 38.88  ? 55  PHE A O   1 
ATOM 476  C CB  . PHE A 1 55  ? 50.935 55.641  165.982 1.00 38.78  ? 55  PHE A CB  1 
ATOM 477  C CG  . PHE A 1 55  ? 50.175 54.556  166.652 1.00 37.37  ? 55  PHE A CG  1 
ATOM 478  C CD1 . PHE A 1 55  ? 49.501 53.630  165.895 1.00 36.97  ? 55  PHE A CD1 1 
ATOM 479  C CD2 . PHE A 1 55  ? 50.241 54.372  168.013 1.00 36.90  ? 55  PHE A CD2 1 
ATOM 480  C CE1 . PHE A 1 55  ? 48.866 52.573  166.484 1.00 35.85  ? 55  PHE A CE1 1 
ATOM 481  C CE2 . PHE A 1 55  ? 49.594 53.303  168.607 1.00 36.81  ? 55  PHE A CE2 1 
ATOM 482  C CZ  . PHE A 1 55  ? 48.931 52.389  167.838 1.00 35.81  ? 55  PHE A CZ  1 
ATOM 483  N N   . SER A 1 56  ? 53.896 56.764  164.649 1.00 39.77  ? 56  SER A N   1 
ATOM 484  C CA  . SER A 1 56  ? 54.548 57.719  163.749 1.00 39.81  ? 56  SER A CA  1 
ATOM 485  C C   . SER A 1 56  ? 55.429 56.880  162.875 1.00 39.80  ? 56  SER A C   1 
ATOM 486  O O   . SER A 1 56  ? 56.234 57.384  162.101 1.00 39.75  ? 56  SER A O   1 
ATOM 487  C CB  . SER A 1 56  ? 55.424 58.714  164.513 1.00 39.96  ? 56  SER A CB  1 
ATOM 488  O OG  . SER A 1 56  ? 56.262 59.451  163.629 1.00 39.56  ? 56  SER A OG  1 
ATOM 489  N N   . LEU A 1 57  ? 55.281 55.578  163.020 1.00 39.72  ? 57  LEU A N   1 
ATOM 490  C CA  . LEU A 1 57  ? 56.070 54.679  162.228 1.00 40.44  ? 57  LEU A CA  1 
ATOM 491  C C   . LEU A 1 57  ? 55.160 53.807  161.417 1.00 40.99  ? 57  LEU A C   1 
ATOM 492  O O   . LEU A 1 57  ? 55.386 53.606  160.231 1.00 39.87  ? 57  LEU A O   1 
ATOM 493  C CB  . LEU A 1 57  ? 56.956 53.837  163.139 1.00 40.39  ? 57  LEU A CB  1 
ATOM 494  C CG  . LEU A 1 57  ? 57.448 52.487  162.602 1.00 40.47  ? 57  LEU A CG  1 
ATOM 495  C CD1 . LEU A 1 57  ? 58.189 52.649  161.284 1.00 39.97  ? 57  LEU A CD1 1 
ATOM 496  C CD2 . LEU A 1 57  ? 58.298 51.837  163.689 1.00 40.14  ? 57  LEU A CD2 1 
ATOM 497  N N   . LEU A 1 58  ? 54.108 53.316  162.051 1.00 43.25  ? 58  LEU A N   1 
ATOM 498  C CA  . LEU A 1 58  ? 53.203 52.429  161.353 1.00 46.38  ? 58  LEU A CA  1 
ATOM 499  C C   . LEU A 1 58  ? 52.072 53.138  160.667 1.00 48.25  ? 58  LEU A C   1 
ATOM 500  O O   . LEU A 1 58  ? 51.569 52.665  159.653 1.00 50.01  ? 58  LEU A O   1 
ATOM 501  C CB  . LEU A 1 58  ? 52.622 51.381  162.308 1.00 46.47  ? 58  LEU A CB  1 
ATOM 502  C CG  . LEU A 1 58  ? 53.625 50.466  163.036 1.00 47.73  ? 58  LEU A CG  1 
ATOM 503  C CD1 . LEU A 1 58  ? 52.934 49.718  164.188 1.00 49.14  ? 58  LEU A CD1 1 
ATOM 504  C CD2 . LEU A 1 58  ? 54.224 49.485  162.041 1.00 46.92  ? 58  LEU A CD2 1 
ATOM 505  N N   . PHE A 1 59  ? 51.673 54.284  161.187 1.00 50.20  ? 59  PHE A N   1 
ATOM 506  C CA  . PHE A 1 59  ? 50.543 54.972  160.583 1.00 52.38  ? 59  PHE A CA  1 
ATOM 507  C C   . PHE A 1 59  ? 50.814 55.785  159.332 1.00 53.58  ? 59  PHE A C   1 
ATOM 508  O O   . PHE A 1 59  ? 50.173 55.607  158.281 1.00 53.34  ? 59  PHE A O   1 
ATOM 509  C CB  . PHE A 1 59  ? 49.898 55.873  161.618 1.00 52.36  ? 59  PHE A CB  1 
ATOM 510  C CG  . PHE A 1 59  ? 48.456 55.599  161.828 1.00 53.50  ? 59  PHE A CG  1 
ATOM 511  C CD1 . PHE A 1 59  ? 48.050 54.384  162.342 1.00 54.01  ? 59  PHE A CD1 1 
ATOM 512  C CD2 . PHE A 1 59  ? 47.498 56.552  161.499 1.00 53.93  ? 59  PHE A CD2 1 
ATOM 513  C CE1 . PHE A 1 59  ? 46.705 54.113  162.539 1.00 55.49  ? 59  PHE A CE1 1 
ATOM 514  C CE2 . PHE A 1 59  ? 46.150 56.299  161.689 1.00 54.60  ? 59  PHE A CE2 1 
ATOM 515  C CZ  . PHE A 1 59  ? 45.748 55.072  162.210 1.00 55.46  ? 59  PHE A CZ  1 
ATOM 516  N N   . GLN A 1 60  ? 51.779 56.677  159.475 1.00 55.50  ? 60  GLN A N   1 
ATOM 517  C CA  . GLN A 1 60  ? 52.179 57.619  158.438 1.00 56.66  ? 60  GLN A CA  1 
ATOM 518  C C   . GLN A 1 60  ? 52.690 57.125  157.089 1.00 56.43  ? 60  GLN A C   1 
ATOM 519  O O   . GLN A 1 60  ? 52.591 57.864  156.105 1.00 56.83  ? 60  GLN A O   1 
ATOM 520  C CB  . GLN A 1 60  ? 53.190 58.604  159.049 1.00 59.35  ? 60  GLN A CB  1 
ATOM 521  C CG  . GLN A 1 60  ? 53.884 59.549  158.072 1.00 60.73  ? 60  GLN A CG  1 
ATOM 522  C CD  . GLN A 1 60  ? 55.080 60.261  158.723 1.00 62.07  ? 60  GLN A CD  1 
ATOM 523  O OE1 . GLN A 1 60  ? 55.820 60.994  158.060 1.00 63.08  ? 60  GLN A OE1 1 
ATOM 524  N NE2 . GLN A 1 60  ? 55.275 60.036  160.031 1.00 62.60  ? 60  GLN A NE2 1 
ATOM 525  N N   . PRO A 1 61  ? 53.298 55.923  157.027 1.00 55.94  ? 61  PRO A N   1 
ATOM 526  C CA  . PRO A 1 61  ? 53.749 55.516  155.694 1.00 54.40  ? 61  PRO A CA  1 
ATOM 527  C C   . PRO A 1 61  ? 52.562 55.035  154.866 1.00 54.62  ? 61  PRO A C   1 
ATOM 528  O O   . PRO A 1 61  ? 52.523 55.210  153.651 1.00 54.20  ? 61  PRO A O   1 
ATOM 529  C CB  . PRO A 1 61  ? 54.715 54.369  155.973 1.00 55.02  ? 61  PRO A CB  1 
ATOM 530  C CG  . PRO A 1 61  ? 55.201 54.622  157.333 1.00 54.79  ? 61  PRO A CG  1 
ATOM 531  C CD  . PRO A 1 61  ? 53.969 55.120  158.064 1.00 55.16  ? 61  PRO A CD  1 
ATOM 532  N N   . LEU A 1 62  ? 51.603 54.407  155.534 1.00 54.43  ? 62  LEU A N   1 
ATOM 533  C CA  . LEU A 1 62  ? 50.422 53.895  154.860 1.00 54.63  ? 62  LEU A CA  1 
ATOM 534  C C   . LEU A 1 62  ? 49.517 55.075  154.502 1.00 55.57  ? 62  LEU A C   1 
ATOM 535  O O   . LEU A 1 62  ? 48.785 55.063  153.501 1.00 55.31  ? 62  LEU A O   1 
ATOM 536  C CB  . LEU A 1 62  ? 49.734 52.859  155.774 1.00 53.92  ? 62  LEU A CB  1 
ATOM 537  C CG  . LEU A 1 62  ? 48.292 52.964  156.277 1.00 53.92  ? 62  LEU A CG  1 
ATOM 538  C CD1 . LEU A 1 62  ? 47.332 52.963  155.093 1.00 53.92  ? 62  LEU A CD1 1 
ATOM 539  C CD2 . LEU A 1 62  ? 47.995 51.777  157.210 1.00 53.00  ? 62  LEU A CD2 1 
ATOM 540  N N   . PHE A 1 63  ? 49.618 56.115  155.308 1.00 57.11  ? 63  PHE A N   1 
ATOM 541  C CA  . PHE A 1 63  ? 48.844 57.307  155.107 1.00 58.74  ? 63  PHE A CA  1 
ATOM 542  C C   . PHE A 1 63  ? 49.412 58.107  153.931 1.00 58.04  ? 63  PHE A C   1 
ATOM 543  O O   . PHE A 1 63  ? 48.663 58.744  153.208 1.00 58.02  ? 63  PHE A O   1 
ATOM 544  C CB  . PHE A 1 63  ? 48.849 58.101  156.417 1.00 61.88  ? 63  PHE A CB  1 
ATOM 545  C CG  . PHE A 1 63  ? 48.319 59.459  156.272 1.00 65.68  ? 63  PHE A CG  1 
ATOM 546  C CD1 . PHE A 1 63  ? 49.118 60.424  155.737 1.00 66.77  ? 63  PHE A CD1 1 
ATOM 547  C CD2 . PHE A 1 63  ? 47.014 59.778  156.565 1.00 66.62  ? 63  PHE A CD2 1 
ATOM 548  C CE1 . PHE A 1 63  ? 48.627 61.686  155.482 1.00 68.89  ? 63  PHE A CE1 1 
ATOM 549  C CE2 . PHE A 1 63  ? 46.526 61.079  156.299 1.00 68.26  ? 63  PHE A CE2 1 
ATOM 550  C CZ  . PHE A 1 63  ? 47.324 62.010  155.767 1.00 69.32  ? 63  PHE A CZ  1 
ATOM 551  N N   . GLY A 1 64  ? 50.726 58.035  153.730 1.00 57.39  ? 64  GLY A N   1 
ATOM 552  C CA  . GLY A 1 64  ? 51.359 58.733  152.621 1.00 56.77  ? 64  GLY A CA  1 
ATOM 553  C C   . GLY A 1 64  ? 51.178 57.992  151.305 1.00 56.85  ? 64  GLY A C   1 
ATOM 554  O O   . GLY A 1 64  ? 51.238 58.579  150.225 1.00 55.98  ? 64  GLY A O   1 
ATOM 555  N N   . LEU A 1 65  ? 50.955 56.686  151.392 1.00 57.31  ? 65  LEU A N   1 
ATOM 556  C CA  . LEU A 1 65  ? 50.743 55.897  150.189 1.00 57.40  ? 65  LEU A CA  1 
ATOM 557  C C   . LEU A 1 65  ? 49.286 56.068  149.772 1.00 56.69  ? 65  LEU A C   1 
ATOM 558  O O   . LEU A 1 65  ? 48.976 56.035  148.579 1.00 56.62  ? 65  LEU A O   1 
ATOM 559  C CB  . LEU A 1 65  ? 51.075 54.414  150.428 1.00 57.50  ? 65  LEU A CB  1 
ATOM 560  C CG  . LEU A 1 65  ? 52.494 54.070  150.945 1.00 57.54  ? 65  LEU A CG  1 
ATOM 561  C CD1 . LEU A 1 65  ? 52.617 52.549  151.040 1.00 57.52  ? 65  LEU A CD1 1 
ATOM 562  C CD2 . LEU A 1 65  ? 53.589 54.633  150.034 1.00 56.20  ? 65  LEU A CD2 1 
ATOM 563  N N   . LEU A 1 66  ? 48.395 56.265  150.745 1.00 56.21  ? 66  LEU A N   1 
ATOM 564  C CA  . LEU A 1 66  ? 46.990 56.470  150.422 1.00 56.41  ? 66  LEU A CA  1 
ATOM 565  C C   . LEU A 1 66  ? 46.882 57.790  149.666 1.00 57.01  ? 66  LEU A C   1 
ATOM 566  O O   . LEU A 1 66  ? 46.033 57.946  148.793 1.00 57.26  ? 66  LEU A O   1 
ATOM 567  C CB  . LEU A 1 66  ? 46.129 56.512  151.692 1.00 55.33  ? 66  LEU A CB  1 
ATOM 568  C CG  . LEU A 1 66  ? 45.996 55.220  152.505 1.00 54.78  ? 66  LEU A CG  1 
ATOM 569  C CD1 . LEU A 1 66  ? 45.076 55.466  153.703 1.00 55.10  ? 66  LEU A CD1 1 
ATOM 570  C CD2 . LEU A 1 66  ? 45.445 54.087  151.633 1.00 54.34  ? 66  LEU A CD2 1 
ATOM 571  N N   . SER A 1 67  ? 47.765 58.733  149.976 1.00 57.97  ? 67  SER A N   1 
ATOM 572  C CA  . SER A 1 67  ? 47.737 60.030  149.303 1.00 59.37  ? 67  SER A CA  1 
ATOM 573  C C   . SER A 1 67  ? 47.821 59.937  147.785 1.00 59.56  ? 67  SER A C   1 
ATOM 574  O O   . SER A 1 67  ? 47.225 60.739  147.057 1.00 59.75  ? 67  SER A O   1 
ATOM 575  C CB  . SER A 1 67  ? 48.887 60.901  149.770 1.00 60.66  ? 67  SER A CB  1 
ATOM 576  O OG  . SER A 1 67  ? 49.145 61.889  148.776 1.00 61.64  ? 67  SER A OG  1 
ATOM 577  N N   . ASP A 1 68  ? 48.598 58.973  147.318 1.00 60.10  ? 68  ASP A N   1 
ATOM 578  C CA  . ASP A 1 68  ? 48.766 58.772  145.900 1.00 60.60  ? 68  ASP A CA  1 
ATOM 579  C C   . ASP A 1 68  ? 47.479 58.170  145.356 1.00 60.15  ? 68  ASP A C   1 
ATOM 580  O O   . ASP A 1 68  ? 46.834 58.778  144.502 1.00 60.02  ? 68  ASP A O   1 
ATOM 581  C CB  . ASP A 1 68  ? 49.963 57.856  145.662 1.00 63.13  ? 68  ASP A CB  1 
ATOM 582  C CG  . ASP A 1 68  ? 51.095 58.126  146.647 1.00 65.15  ? 68  ASP A CG  1 
ATOM 583  O OD1 . ASP A 1 68  ? 51.381 59.327  146.908 1.00 66.03  ? 68  ASP A OD1 1 
ATOM 584  O OD2 . ASP A 1 68  ? 51.694 57.141  147.157 1.00 66.31  ? 68  ASP A OD2 1 
ATOM 585  N N   . LYS A 1 69  ? 47.081 56.999  145.855 1.00 59.37  ? 69  LYS A N   1 
ATOM 586  C CA  . LYS A 1 69  ? 45.843 56.382  145.373 1.00 58.37  ? 69  LYS A CA  1 
ATOM 587  C C   . LYS A 1 69  ? 44.765 57.464  145.341 1.00 57.87  ? 69  LYS A C   1 
ATOM 588  O O   . LYS A 1 69  ? 43.970 57.545  144.398 1.00 57.60  ? 69  LYS A O   1 
ATOM 589  C CB  . LYS A 1 69  ? 45.404 55.238  146.293 1.00 58.21  ? 69  LYS A CB  1 
ATOM 590  C CG  . LYS A 1 69  ? 44.207 54.456  145.759 1.00 59.16  ? 69  LYS A CG  1 
ATOM 591  C CD  . LYS A 1 69  ? 43.739 53.387  146.746 1.00 60.60  ? 69  LYS A CD  1 
ATOM 592  C CE  . LYS A 1 69  ? 42.450 52.694  146.265 1.00 61.62  ? 69  LYS A CE  1 
ATOM 593  N NZ  . LYS A 1 69  ? 41.915 51.648  147.217 1.00 61.50  ? 69  LYS A NZ  1 
ATOM 594  N N   . LEU A 1 70  ? 44.775 58.312  146.371 1.00 56.91  ? 70  LEU A N   1 
ATOM 595  C CA  . LEU A 1 70  ? 43.809 59.411  146.512 1.00 55.77  ? 70  LEU A CA  1 
ATOM 596  C C   . LEU A 1 70  ? 44.021 60.512  145.504 1.00 55.89  ? 70  LEU A C   1 
ATOM 597  O O   . LEU A 1 70  ? 43.089 61.212  145.140 1.00 55.37  ? 70  LEU A O   1 
ATOM 598  C CB  . LEU A 1 70  ? 43.908 60.067  147.893 1.00 54.68  ? 70  LEU A CB  1 
ATOM 599  C CG  . LEU A 1 70  ? 43.651 59.309  149.188 1.00 53.10  ? 70  LEU A CG  1 
ATOM 600  C CD1 . LEU A 1 70  ? 43.782 60.286  150.311 1.00 53.22  ? 70  LEU A CD1 1 
ATOM 601  C CD2 . LEU A 1 70  ? 42.286 58.667  149.194 1.00 53.05  ? 70  LEU A CD2 1 
ATOM 602  N N   . GLY A 1 71  ? 45.253 60.690  145.069 1.00 56.13  ? 71  GLY A N   1 
ATOM 603  C CA  . GLY A 1 71  ? 45.484 61.764  144.143 1.00 57.46  ? 71  GLY A CA  1 
ATOM 604  C C   . GLY A 1 71  ? 45.151 63.028  144.908 1.00 58.91  ? 71  GLY A C   1 
ATOM 605  O O   . GLY A 1 71  ? 45.540 63.187  146.066 1.00 58.55  ? 71  GLY A O   1 
ATOM 606  N N   . LEU A 1 72  ? 44.410 63.926  144.282 1.00 60.35  ? 72  LEU A N   1 
ATOM 607  C CA  . LEU A 1 72  ? 44.078 65.172  144.946 1.00 61.68  ? 72  LEU A CA  1 
ATOM 608  C C   . LEU A 1 72  ? 42.609 65.186  145.434 1.00 63.11  ? 72  LEU A C   1 
ATOM 609  O O   . LEU A 1 72  ? 41.878 66.163  145.260 1.00 62.44  ? 72  LEU A O   1 
ATOM 610  C CB  . LEU A 1 72  ? 44.417 66.323  143.977 1.00 61.21  ? 72  LEU A CB  1 
ATOM 611  C CG  . LEU A 1 72  ? 43.922 67.760  144.148 1.00 60.14  ? 72  LEU A CG  1 
ATOM 612  C CD1 . LEU A 1 72  ? 44.502 68.328  145.412 1.00 59.93  ? 72  LEU A CD1 1 
ATOM 613  C CD2 . LEU A 1 72  ? 44.308 68.611  142.940 1.00 59.57  ? 72  LEU A CD2 1 
ATOM 614  N N   . ARG A 1 73  ? 42.189 64.089  146.068 1.00 65.31  ? 73  ARG A N   1 
ATOM 615  C CA  . ARG A 1 73  ? 40.827 63.976  146.598 1.00 67.71  ? 73  ARG A CA  1 
ATOM 616  C C   . ARG A 1 73  ? 40.858 64.381  148.084 1.00 68.06  ? 73  ARG A C   1 
ATOM 617  O O   . ARG A 1 73  ? 41.745 63.973  148.849 1.00 68.19  ? 73  ARG A O   1 
ATOM 618  C CB  . ARG A 1 73  ? 40.302 62.533  146.399 1.00 69.57  ? 73  ARG A CB  1 
ATOM 619  C CG  . ARG A 1 73  ? 40.224 62.104  144.895 1.00 72.39  ? 73  ARG A CG  1 
ATOM 620  C CD  . ARG A 1 73  ? 40.100 60.573  144.644 1.00 75.08  ? 73  ARG A CD  1 
ATOM 621  N NE  . ARG A 1 73  ? 40.415 60.199  143.256 1.00 77.06  ? 73  ARG A NE  1 
ATOM 622  C CZ  . ARG A 1 73  ? 40.428 58.949  142.784 1.00 77.75  ? 73  ARG A CZ  1 
ATOM 623  N NH1 . ARG A 1 73  ? 40.138 57.924  143.578 1.00 77.79  ? 73  ARG A NH1 1 
ATOM 624  N NH2 . ARG A 1 73  ? 40.753 58.717  141.513 1.00 77.92  ? 73  ARG A NH2 1 
ATOM 625  N N   . LYS A 1 74  ? 39.890 65.199  148.479 1.00 68.07  ? 74  LYS A N   1 
ATOM 626  C CA  . LYS A 1 74  ? 39.808 65.719  149.843 1.00 67.99  ? 74  LYS A CA  1 
ATOM 627  C C   . LYS A 1 74  ? 39.529 64.674  150.938 1.00 67.59  ? 74  LYS A C   1 
ATOM 628  O O   . LYS A 1 74  ? 39.988 64.826  152.085 1.00 67.86  ? 74  LYS A O   1 
ATOM 629  C CB  . LYS A 1 74  ? 38.739 66.832  149.890 1.00 68.37  ? 74  LYS A CB  1 
ATOM 630  C CG  . LYS A 1 74  ? 38.989 68.006  148.934 1.00 70.02  ? 74  LYS A CG  1 
ATOM 631  C CD  . LYS A 1 74  ? 39.041 67.552  147.469 1.00 71.24  ? 74  LYS A CD  1 
ATOM 632  C CE  . LYS A 1 74  ? 39.437 68.686  146.518 1.00 72.05  ? 74  LYS A CE  1 
ATOM 633  N NZ  . LYS A 1 74  ? 39.660 68.215  145.107 1.00 71.52  ? 74  LYS A NZ  1 
ATOM 634  N N   . TYR A 1 75  ? 38.796 63.620  150.570 1.00 66.29  ? 75  TYR A N   1 
ATOM 635  C CA  . TYR A 1 75  ? 38.391 62.548  151.488 1.00 64.29  ? 75  TYR A CA  1 
ATOM 636  C C   . TYR A 1 75  ? 39.249 62.335  152.750 1.00 61.24  ? 75  TYR A C   1 
ATOM 637  O O   . TYR A 1 75  ? 38.769 62.495  153.874 1.00 60.20  ? 75  TYR A O   1 
ATOM 638  C CB  . TYR A 1 75  ? 38.264 61.227  150.708 1.00 67.09  ? 75  TYR A CB  1 
ATOM 639  C CG  . TYR A 1 75  ? 37.586 60.135  151.500 1.00 70.02  ? 75  TYR A CG  1 
ATOM 640  C CD1 . TYR A 1 75  ? 36.195 60.086  151.600 1.00 71.37  ? 75  TYR A CD1 1 
ATOM 641  C CD2 . TYR A 1 75  ? 38.336 59.203  152.226 1.00 71.11  ? 75  TYR A CD2 1 
ATOM 642  C CE1 . TYR A 1 75  ? 35.563 59.142  152.409 1.00 72.24  ? 75  TYR A CE1 1 
ATOM 643  C CE2 . TYR A 1 75  ? 37.719 58.256  153.039 1.00 72.11  ? 75  TYR A CE2 1 
ATOM 644  C CZ  . TYR A 1 75  ? 36.327 58.233  153.132 1.00 72.56  ? 75  TYR A CZ  1 
ATOM 645  O OH  . TYR A 1 75  ? 35.694 57.337  153.975 1.00 72.80  ? 75  TYR A OH  1 
ATOM 646  N N   . LEU A 1 76  ? 40.516 61.987  152.559 1.00 57.89  ? 76  LEU A N   1 
ATOM 647  C CA  . LEU A 1 76  ? 41.400 61.745  153.686 1.00 55.14  ? 76  LEU A CA  1 
ATOM 648  C C   . LEU A 1 76  ? 41.633 62.947  154.574 1.00 53.18  ? 76  LEU A C   1 
ATOM 649  O O   . LEU A 1 76  ? 41.512 62.859  155.795 1.00 52.11  ? 76  LEU A O   1 
ATOM 650  C CB  . LEU A 1 76  ? 42.744 61.238  153.210 1.00 55.71  ? 76  LEU A CB  1 
ATOM 651  C CG  . LEU A 1 76  ? 43.707 60.901  154.328 1.00 55.72  ? 76  LEU A CG  1 
ATOM 652  C CD1 . LEU A 1 76  ? 43.101 59.919  155.322 1.00 56.09  ? 76  LEU A CD1 1 
ATOM 653  C CD2 . LEU A 1 76  ? 44.920 60.278  153.667 1.00 56.97  ? 76  LEU A CD2 1 
ATOM 654  N N   . LEU A 1 77  ? 41.979 64.068  153.956 1.00 51.75  ? 77  LEU A N   1 
ATOM 655  C CA  . LEU A 1 77  ? 42.231 65.288  154.699 1.00 50.40  ? 77  LEU A CA  1 
ATOM 656  C C   . LEU A 1 77  ? 41.079 65.554  155.647 1.00 50.67  ? 77  LEU A C   1 
ATOM 657  O O   . LEU A 1 77  ? 41.294 66.040  156.756 1.00 50.84  ? 77  LEU A O   1 
ATOM 658  C CB  . LEU A 1 77  ? 42.412 66.480  153.762 1.00 49.44  ? 77  LEU A CB  1 
ATOM 659  C CG  . LEU A 1 77  ? 42.991 67.720  154.449 1.00 48.42  ? 77  LEU A CG  1 
ATOM 660  C CD1 . LEU A 1 77  ? 44.311 67.367  155.113 1.00 47.24  ? 77  LEU A CD1 1 
ATOM 661  C CD2 . LEU A 1 77  ? 43.202 68.822  153.429 1.00 48.96  ? 77  LEU A CD2 1 
ATOM 662  N N   . TRP A 1 78  ? 39.854 65.248  155.220 1.00 50.85  ? 78  TRP A N   1 
ATOM 663  C CA  . TRP A 1 78  ? 38.708 65.445  156.110 1.00 50.90  ? 78  TRP A CA  1 
ATOM 664  C C   . TRP A 1 78  ? 38.902 64.554  157.354 1.00 50.28  ? 78  TRP A C   1 
ATOM 665  O O   . TRP A 1 78  ? 38.792 65.025  158.497 1.00 49.84  ? 78  TRP A O   1 
ATOM 666  C CB  . TRP A 1 78  ? 37.375 65.039  155.457 1.00 52.31  ? 78  TRP A CB  1 
ATOM 667  C CG  . TRP A 1 78  ? 36.794 65.989  154.467 1.00 53.66  ? 78  TRP A CG  1 
ATOM 668  C CD1 . TRP A 1 78  ? 37.364 66.380  153.298 1.00 53.71  ? 78  TRP A CD1 1 
ATOM 669  C CD2 . TRP A 1 78  ? 35.484 66.596  154.503 1.00 54.43  ? 78  TRP A CD2 1 
ATOM 670  N NE1 . TRP A 1 78  ? 36.500 67.186  152.590 1.00 55.10  ? 78  TRP A NE1 1 
ATOM 671  C CE2 . TRP A 1 78  ? 35.340 67.336  153.304 1.00 54.93  ? 78  TRP A CE2 1 
ATOM 672  C CE3 . TRP A 1 78  ? 34.419 66.582  155.420 1.00 54.04  ? 78  TRP A CE3 1 
ATOM 673  C CZ2 . TRP A 1 78  ? 34.177 68.057  153.001 1.00 55.00  ? 78  TRP A CZ2 1 
ATOM 674  C CZ3 . TRP A 1 78  ? 33.264 67.296  155.117 1.00 54.20  ? 78  TRP A CZ3 1 
ATOM 675  C CH2 . TRP A 1 78  ? 33.154 68.023  153.916 1.00 54.77  ? 78  TRP A CH2 1 
ATOM 676  N N   . ILE A 1 79  ? 39.183 63.268  157.114 1.00 48.91  ? 79  ILE A N   1 
ATOM 677  C CA  . ILE A 1 79  ? 39.371 62.280  158.175 1.00 47.76  ? 79  ILE A CA  1 
ATOM 678  C C   . ILE A 1 79  ? 40.297 62.872  159.191 1.00 47.25  ? 79  ILE A C   1 
ATOM 679  O O   . ILE A 1 79  ? 40.420 62.372  160.303 1.00 47.94  ? 79  ILE A O   1 
ATOM 680  C CB  . ILE A 1 79  ? 39.985 60.959  157.639 1.00 47.87  ? 79  ILE A CB  1 
ATOM 681  C CG1 . ILE A 1 79  ? 39.124 60.434  156.485 1.00 48.38  ? 79  ILE A CG1 1 
ATOM 682  C CG2 . ILE A 1 79  ? 40.043 59.899  158.761 1.00 46.62  ? 79  ILE A CG2 1 
ATOM 683  C CD1 . ILE A 1 79  ? 39.754 59.305  155.664 1.00 49.15  ? 79  ILE A CD1 1 
ATOM 684  N N   . ILE A 1 80  ? 40.955 63.950  158.797 1.00 46.78  ? 80  ILE A N   1 
ATOM 685  C CA  . ILE A 1 80  ? 41.859 64.632  159.687 1.00 47.19  ? 80  ILE A CA  1 
ATOM 686  C C   . ILE A 1 80  ? 41.081 65.684  160.433 1.00 47.14  ? 80  ILE A C   1 
ATOM 687  O O   . ILE A 1 80  ? 41.002 65.644  161.650 1.00 46.42  ? 80  ILE A O   1 
ATOM 688  C CB  . ILE A 1 80  ? 42.970 65.305  158.924 1.00 47.31  ? 80  ILE A CB  1 
ATOM 689  C CG1 . ILE A 1 80  ? 43.770 64.253  158.156 1.00 47.96  ? 80  ILE A CG1 1 
ATOM 690  C CG2 . ILE A 1 80  ? 43.845 66.070  159.891 1.00 47.36  ? 80  ILE A CG2 1 
ATOM 691  C CD1 . ILE A 1 80  ? 44.800 64.842  157.215 1.00 48.47  ? 80  ILE A CD1 1 
ATOM 692  N N   . THR A 1 81  ? 40.507 66.633  159.713 1.00 48.20  ? 81  THR A N   1 
ATOM 693  C CA  . THR A 1 81  ? 39.745 67.657  160.388 1.00 50.70  ? 81  THR A CA  1 
ATOM 694  C C   . THR A 1 81  ? 38.778 66.989  161.348 1.00 52.66  ? 81  THR A C   1 
ATOM 695  O O   . THR A 1 81  ? 38.537 67.470  162.463 1.00 53.37  ? 81  THR A O   1 
ATOM 696  C CB  . THR A 1 81  ? 38.968 68.522  159.393 1.00 50.41  ? 81  THR A CB  1 
ATOM 697  O OG1 . THR A 1 81  ? 39.870 69.443  158.774 1.00 50.47  ? 81  THR A OG1 1 
ATOM 698  C CG2 . THR A 1 81  ? 37.861 69.296  160.093 1.00 50.94  ? 81  THR A CG2 1 
ATOM 699  N N   . GLY A 1 82  ? 38.247 65.851  160.920 1.00 54.79  ? 82  GLY A N   1 
ATOM 700  C CA  . GLY A 1 82  ? 37.298 65.124  161.748 1.00 57.66  ? 82  GLY A CA  1 
ATOM 701  C C   . GLY A 1 82  ? 37.809 64.753  163.124 1.00 58.69  ? 82  GLY A C   1 
ATOM 702  O O   . GLY A 1 82  ? 37.233 65.129  164.140 1.00 58.42  ? 82  GLY A O   1 
ATOM 703  N N   . MET A 1 83  ? 38.900 64.005  163.158 1.00 60.28  ? 83  MET A N   1 
ATOM 704  C CA  . MET A 1 83  ? 39.456 63.591  164.426 1.00 62.06  ? 83  MET A CA  1 
ATOM 705  C C   . MET A 1 83  ? 40.090 64.768  165.130 1.00 62.84  ? 83  MET A C   1 
ATOM 706  O O   . MET A 1 83  ? 40.150 64.797  166.359 1.00 63.95  ? 83  MET A O   1 
ATOM 707  C CB  . MET A 1 83  ? 40.492 62.491  164.234 1.00 62.99  ? 83  MET A CB  1 
ATOM 708  C CG  . MET A 1 83  ? 39.907 61.155  163.829 1.00 65.11  ? 83  MET A CG  1 
ATOM 709  S SD  . MET A 1 83  ? 41.194 59.932  163.664 1.00 68.22  ? 83  MET A SD  1 
ATOM 710  C CE  . MET A 1 83  ? 41.668 59.815  165.406 1.00 67.33  ? 83  MET A CE  1 
ATOM 711  N N   . LEU A 1 84  ? 40.572 65.742  164.370 1.00 63.06  ? 84  LEU A N   1 
ATOM 712  C CA  . LEU A 1 84  ? 41.181 66.892  165.012 1.00 63.61  ? 84  LEU A CA  1 
ATOM 713  C C   . LEU A 1 84  ? 40.135 67.603  165.849 1.00 63.38  ? 84  LEU A C   1 
ATOM 714  O O   . LEU A 1 84  ? 40.347 67.864  167.039 1.00 63.39  ? 84  LEU A O   1 
ATOM 715  C CB  . LEU A 1 84  ? 41.782 67.834  163.972 1.00 63.91  ? 84  LEU A CB  1 
ATOM 716  C CG  . LEU A 1 84  ? 43.096 67.270  163.412 1.00 64.89  ? 84  LEU A CG  1 
ATOM 717  C CD1 . LEU A 1 84  ? 43.660 68.231  162.386 1.00 66.14  ? 84  LEU A CD1 1 
ATOM 718  C CD2 . LEU A 1 84  ? 44.094 67.061  164.545 1.00 64.31  ? 84  LEU A CD2 1 
ATOM 719  N N   . VAL A 1 85  ? 38.986 67.862  165.238 1.00 63.03  ? 85  VAL A N   1 
ATOM 720  C CA  . VAL A 1 85  ? 37.903 68.549  165.917 1.00 62.64  ? 85  VAL A CA  1 
ATOM 721  C C   . VAL A 1 85  ? 37.538 68.081  167.331 1.00 61.48  ? 85  VAL A C   1 
ATOM 722  O O   . VAL A 1 85  ? 37.351 68.912  168.199 1.00 61.30  ? 85  VAL A O   1 
ATOM 723  C CB  . VAL A 1 85  ? 36.647 68.542  165.060 1.00 63.36  ? 85  VAL A CB  1 
ATOM 724  C CG1 . VAL A 1 85  ? 35.500 69.187  165.818 1.00 63.54  ? 85  VAL A CG1 1 
ATOM 725  C CG2 . VAL A 1 85  ? 36.941 69.258  163.779 1.00 63.25  ? 85  VAL A CG2 1 
ATOM 726  N N   . MET A 1 86  ? 37.436 66.784  167.598 1.00 60.32  ? 86  MET A N   1 
ATOM 727  C CA  . MET A 1 86  ? 37.076 66.418  168.962 1.00 59.15  ? 86  MET A CA  1 
ATOM 728  C C   . MET A 1 86  ? 38.266 66.406  169.926 1.00 57.70  ? 86  MET A C   1 
ATOM 729  O O   . MET A 1 86  ? 38.273 65.683  170.938 1.00 56.95  ? 86  MET A O   1 
ATOM 730  C CB  . MET A 1 86  ? 36.323 65.083  169.006 1.00 61.11  ? 86  MET A CB  1 
ATOM 731  C CG  . MET A 1 86  ? 37.141 63.860  168.674 1.00 63.09  ? 86  MET A CG  1 
ATOM 732  S SD  . MET A 1 86  ? 36.126 62.341  168.683 1.00 64.99  ? 86  MET A SD  1 
ATOM 733  C CE  . MET A 1 86  ? 35.702 62.226  166.879 1.00 65.07  ? 86  MET A CE  1 
ATOM 734  N N   . PHE A 1 87  ? 39.253 67.241  169.591 1.00 55.25  ? 87  PHE A N   1 
ATOM 735  C CA  . PHE A 1 87  ? 40.484 67.425  170.355 1.00 52.83  ? 87  PHE A CA  1 
ATOM 736  C C   . PHE A 1 87  ? 40.178 67.520  171.852 1.00 52.58  ? 87  PHE A C   1 
ATOM 737  O O   . PHE A 1 87  ? 40.640 66.697  172.643 1.00 52.38  ? 87  PHE A O   1 
ATOM 738  C CB  . PHE A 1 87  ? 41.199 68.710  169.890 1.00 50.51  ? 87  PHE A CB  1 
ATOM 739  C CG  . PHE A 1 87  ? 42.647 68.806  170.334 1.00 48.22  ? 87  PHE A CG  1 
ATOM 740  C CD1 . PHE A 1 87  ? 43.484 67.697  170.259 1.00 47.31  ? 87  PHE A CD1 1 
ATOM 741  C CD2 . PHE A 1 87  ? 43.180 70.001  170.803 1.00 46.96  ? 87  PHE A CD2 1 
ATOM 742  C CE1 . PHE A 1 87  ? 44.826 67.779  170.645 1.00 46.25  ? 87  PHE A CE1 1 
ATOM 743  C CE2 . PHE A 1 87  ? 44.522 70.087  171.189 1.00 46.22  ? 87  PHE A CE2 1 
ATOM 744  C CZ  . PHE A 1 87  ? 45.340 68.973  171.108 1.00 45.82  ? 87  PHE A CZ  1 
ATOM 745  N N   . ALA A 1 88  ? 39.388 68.527  172.223 1.00 51.93  ? 88  ALA A N   1 
ATOM 746  C CA  . ALA A 1 88  ? 39.009 68.772  173.615 1.00 51.14  ? 88  ALA A CA  1 
ATOM 747  C C   . ALA A 1 88  ? 38.292 67.602  174.280 1.00 50.72  ? 88  ALA A C   1 
ATOM 748  O O   . ALA A 1 88  ? 38.741 67.084  175.304 1.00 50.70  ? 88  ALA A O   1 
ATOM 749  C CB  . ALA A 1 88  ? 38.136 70.020  173.706 1.00 51.17  ? 88  ALA A CB  1 
ATOM 750  N N   . PRO A 1 89  ? 37.155 67.177  173.716 1.00 50.79  ? 89  PRO A N   1 
ATOM 751  C CA  . PRO A 1 89  ? 36.423 66.060  174.314 1.00 50.95  ? 89  PRO A CA  1 
ATOM 752  C C   . PRO A 1 89  ? 37.348 64.873  174.430 1.00 51.75  ? 89  PRO A C   1 
ATOM 753  O O   . PRO A 1 89  ? 37.446 64.209  175.467 1.00 52.17  ? 89  PRO A O   1 
ATOM 754  C CB  . PRO A 1 89  ? 35.313 65.802  173.310 1.00 50.12  ? 89  PRO A CB  1 
ATOM 755  C CG  . PRO A 1 89  ? 35.109 67.127  172.672 1.00 49.66  ? 89  PRO A CG  1 
ATOM 756  C CD  . PRO A 1 89  ? 36.489 67.648  172.493 1.00 49.96  ? 89  PRO A CD  1 
ATOM 757  N N   . PHE A 1 90  ? 38.026 64.615  173.329 1.00 53.12  ? 90  PHE A N   1 
ATOM 758  C CA  . PHE A 1 90  ? 38.960 63.521  173.254 1.00 54.54  ? 90  PHE A CA  1 
ATOM 759  C C   . PHE A 1 90  ? 39.988 63.575  174.382 1.00 54.12  ? 90  PHE A C   1 
ATOM 760  O O   . PHE A 1 90  ? 40.083 62.660  175.197 1.00 54.62  ? 90  PHE A O   1 
ATOM 761  C CB  . PHE A 1 90  ? 39.663 63.601  171.920 1.00 56.56  ? 90  PHE A CB  1 
ATOM 762  C CG  . PHE A 1 90  ? 40.823 62.677  171.793 1.00 59.40  ? 90  PHE A CG  1 
ATOM 763  C CD1 . PHE A 1 90  ? 40.631 61.318  171.645 1.00 60.13  ? 90  PHE A CD1 1 
ATOM 764  C CD2 . PHE A 1 90  ? 42.100 63.155  171.818 1.00 60.71  ? 90  PHE A CD2 1 
ATOM 765  C CE1 . PHE A 1 90  ? 41.687 60.438  171.513 1.00 60.38  ? 90  PHE A CE1 1 
ATOM 766  C CE2 . PHE A 1 90  ? 43.149 62.286  171.686 1.00 61.46  ? 90  PHE A CE2 1 
ATOM 767  C CZ  . PHE A 1 90  ? 42.926 60.911  171.536 1.00 61.05  ? 90  PHE A CZ  1 
ATOM 768  N N   . PHE A 1 91  ? 40.756 64.661  174.408 1.00 53.69  ? 91  PHE A N   1 
ATOM 769  C CA  . PHE A 1 91  ? 41.803 64.871  175.409 1.00 53.17  ? 91  PHE A CA  1 
ATOM 770  C C   . PHE A 1 91  ? 41.315 64.935  176.856 1.00 52.71  ? 91  PHE A C   1 
ATOM 771  O O   . PHE A 1 91  ? 41.684 64.100  177.689 1.00 52.30  ? 91  PHE A O   1 
ATOM 772  C CB  . PHE A 1 91  ? 42.575 66.155  175.106 1.00 53.07  ? 91  PHE A CB  1 
ATOM 773  C CG  . PHE A 1 91  ? 43.975 65.925  174.618 1.00 52.13  ? 91  PHE A CG  1 
ATOM 774  C CD1 . PHE A 1 91  ? 44.217 65.577  173.301 1.00 52.02  ? 91  PHE A CD1 1 
ATOM 775  C CD2 . PHE A 1 91  ? 45.053 66.037  175.486 1.00 52.32  ? 91  PHE A CD2 1 
ATOM 776  C CE1 . PHE A 1 91  ? 45.512 65.340  172.858 1.00 51.83  ? 91  PHE A CE1 1 
ATOM 777  C CE2 . PHE A 1 91  ? 46.353 65.801  175.047 1.00 51.63  ? 91  PHE A CE2 1 
ATOM 778  C CZ  . PHE A 1 91  ? 46.579 65.452  173.732 1.00 51.52  ? 91  PHE A CZ  1 
ATOM 779  N N   . ILE A 1 92  ? 40.512 65.949  177.157 1.00 51.95  ? 92  ILE A N   1 
ATOM 780  C CA  . ILE A 1 92  ? 39.969 66.115  178.494 1.00 51.40  ? 92  ILE A CA  1 
ATOM 781  C C   . ILE A 1 92  ? 39.371 64.823  179.014 1.00 51.63  ? 92  ILE A C   1 
ATOM 782  O O   . ILE A 1 92  ? 39.730 64.352  180.091 1.00 51.62  ? 92  ILE A O   1 
ATOM 783  C CB  . ILE A 1 92  ? 38.839 67.147  178.530 1.00 50.51  ? 92  ILE A CB  1 
ATOM 784  C CG1 . ILE A 1 92  ? 39.385 68.549  178.310 1.00 50.70  ? 92  ILE A CG1 1 
ATOM 785  C CG2 . ILE A 1 92  ? 38.127 67.066  179.858 1.00 49.78  ? 92  ILE A CG2 1 
ATOM 786  C CD1 . ILE A 1 92  ? 38.312 69.631  178.407 1.00 51.42  ? 92  ILE A CD1 1 
ATOM 787  N N   . PHE A 1 93  ? 38.470 64.247  178.227 1.00 51.76  ? 93  PHE A N   1 
ATOM 788  C CA  . PHE A 1 93  ? 37.763 63.039  178.618 1.00 52.05  ? 93  PHE A CA  1 
ATOM 789  C C   . PHE A 1 93  ? 38.375 61.668  178.443 1.00 51.78  ? 93  PHE A C   1 
ATOM 790  O O   . PHE A 1 93  ? 38.123 60.802  179.266 1.00 52.31  ? 93  PHE A O   1 
ATOM 791  C CB  . PHE A 1 93  ? 36.393 63.053  177.973 1.00 52.87  ? 93  PHE A CB  1 
ATOM 792  C CG  . PHE A 1 93  ? 35.608 64.259  178.329 1.00 54.83  ? 93  PHE A CG  1 
ATOM 793  C CD1 . PHE A 1 93  ? 35.986 65.505  177.848 1.00 55.32  ? 93  PHE A CD1 1 
ATOM 794  C CD2 . PHE A 1 93  ? 34.548 64.178  179.217 1.00 56.01  ? 93  PHE A CD2 1 
ATOM 795  C CE1 . PHE A 1 93  ? 35.331 66.656  178.246 1.00 55.91  ? 93  PHE A CE1 1 
ATOM 796  C CE2 . PHE A 1 93  ? 33.882 65.329  179.626 1.00 57.05  ? 93  PHE A CE2 1 
ATOM 797  C CZ  . PHE A 1 93  ? 34.279 66.573  179.136 1.00 56.60  ? 93  PHE A CZ  1 
ATOM 798  N N   . ILE A 1 94  ? 39.165 61.457  177.395 1.00 51.23  ? 94  ILE A N   1 
ATOM 799  C CA  . ILE A 1 94  ? 39.777 60.144  177.171 1.00 50.19  ? 94  ILE A CA  1 
ATOM 800  C C   . ILE A 1 94  ? 41.065 59.939  177.954 1.00 50.40  ? 94  ILE A C   1 
ATOM 801  O O   . ILE A 1 94  ? 41.151 59.069  178.839 1.00 49.71  ? 94  ILE A O   1 
ATOM 802  C CB  . ILE A 1 94  ? 40.095 59.925  175.706 1.00 49.61  ? 94  ILE A CB  1 
ATOM 803  C CG1 . ILE A 1 94  ? 38.845 60.209  174.892 1.00 48.21  ? 94  ILE A CG1 1 
ATOM 804  C CG2 . ILE A 1 94  ? 40.574 58.535  175.496 1.00 49.94  ? 94  ILE A CG2 1 
ATOM 805  C CD1 . ILE A 1 94  ? 38.959 59.810  173.574 1.00 47.83  ? 94  ILE A CD1 1 
ATOM 806  N N   . PHE A 1 95  ? 42.078 60.732  177.624 1.00 51.46  ? 95  PHE A N   1 
ATOM 807  C CA  . PHE A 1 95  ? 43.353 60.614  178.323 1.00 53.50  ? 95  PHE A CA  1 
ATOM 808  C C   . PHE A 1 95  ? 43.227 60.723  179.792 1.00 54.07  ? 95  PHE A C   1 
ATOM 809  O O   . PHE A 1 95  ? 43.496 59.762  180.504 1.00 53.23  ? 95  PHE A O   1 
ATOM 810  C CB  . PHE A 1 95  ? 44.354 61.685  177.946 1.00 55.48  ? 95  PHE A CB  1 
ATOM 811  C CG  . PHE A 1 95  ? 44.898 61.527  176.604 1.00 58.36  ? 95  PHE A CG  1 
ATOM 812  C CD1 . PHE A 1 95  ? 44.044 61.549  175.537 1.00 59.01  ? 95  PHE A CD1 1 
ATOM 813  C CD2 . PHE A 1 95  ? 46.279 61.379  176.381 1.00 58.98  ? 95  PHE A CD2 1 
ATOM 814  C CE1 . PHE A 1 95  ? 44.535 61.437  174.285 1.00 59.46  ? 95  PHE A CE1 1 
ATOM 815  C CE2 . PHE A 1 95  ? 46.778 61.265  175.090 1.00 58.85  ? 95  PHE A CE2 1 
ATOM 816  C CZ  . PHE A 1 95  ? 45.900 61.295  174.042 1.00 59.58  ? 95  PHE A CZ  1 
ATOM 817  N N   . GLY A 1 96  ? 42.889 61.924  180.252 1.00 55.04  ? 96  GLY A N   1 
ATOM 818  C CA  . GLY A 1 96  ? 42.751 62.140  181.682 1.00 56.34  ? 96  GLY A CA  1 
ATOM 819  C C   . GLY A 1 96  ? 42.386 60.859  182.411 1.00 58.07  ? 96  GLY A C   1 
ATOM 820  O O   . GLY A 1 96  ? 43.169 60.359  183.206 1.00 58.73  ? 96  GLY A O   1 
ATOM 821  N N   . PRO A 1 97  ? 41.202 60.296  182.155 1.00 59.53  ? 97  PRO A N   1 
ATOM 822  C CA  . PRO A 1 97  ? 40.671 59.065  182.752 1.00 60.14  ? 97  PRO A CA  1 
ATOM 823  C C   . PRO A 1 97  ? 41.509 57.809  182.571 1.00 60.81  ? 97  PRO A C   1 
ATOM 824  O O   . PRO A 1 97  ? 41.970 57.214  183.548 1.00 60.71  ? 97  PRO A O   1 
ATOM 825  C CB  . PRO A 1 97  ? 39.312 58.911  182.087 1.00 60.49  ? 97  PRO A CB  1 
ATOM 826  C CG  . PRO A 1 97  ? 38.878 60.317  181.913 1.00 60.44  ? 97  PRO A CG  1 
ATOM 827  C CD  . PRO A 1 97  ? 40.151 61.012  181.423 1.00 59.40  ? 97  PRO A CD  1 
ATOM 828  N N   . LEU A 1 98  ? 41.693 57.381  181.331 1.00 61.84  ? 98  LEU A N   1 
ATOM 829  C CA  . LEU A 1 98  ? 42.476 56.183  181.135 1.00 63.84  ? 98  LEU A CA  1 
ATOM 830  C C   . LEU A 1 98  ? 43.729 56.289  182.000 1.00 66.52  ? 98  LEU A C   1 
ATOM 831  O O   . LEU A 1 98  ? 44.151 55.319  182.633 1.00 66.74  ? 98  LEU A O   1 
ATOM 832  C CB  . LEU A 1 98  ? 42.800 56.003  179.652 1.00 61.80  ? 98  LEU A CB  1 
ATOM 833  C CG  . LEU A 1 98  ? 41.590 55.622  178.803 1.00 60.59  ? 98  LEU A CG  1 
ATOM 834  C CD1 . LEU A 1 98  ? 41.969 55.408  177.359 1.00 59.64  ? 98  LEU A CD1 1 
ATOM 835  C CD2 . LEU A 1 98  ? 41.018 54.344  179.355 1.00 60.43  ? 98  LEU A CD2 1 
ATOM 836  N N   . LEU A 1 99  ? 44.280 57.492  182.073 1.00 70.48  ? 99  LEU A N   1 
ATOM 837  C CA  . LEU A 1 99  ? 45.465 57.745  182.874 1.00 75.15  ? 99  LEU A CA  1 
ATOM 838  C C   . LEU A 1 99  ? 45.152 57.935  184.364 1.00 78.73  ? 99  LEU A C   1 
ATOM 839  O O   . LEU A 1 99  ? 45.450 57.069  185.186 1.00 78.53  ? 99  LEU A O   1 
ATOM 840  C CB  . LEU A 1 99  ? 46.173 58.983  182.331 1.00 74.59  ? 99  LEU A CB  1 
ATOM 841  C CG  . LEU A 1 99  ? 46.639 58.780  180.895 1.00 75.23  ? 99  LEU A CG  1 
ATOM 842  C CD1 . LEU A 1 99  ? 47.150 60.068  180.251 1.00 75.17  ? 99  LEU A CD1 1 
ATOM 843  C CD2 . LEU A 1 99  ? 47.720 57.731  180.965 1.00 75.89  ? 99  LEU A CD2 1 
ATOM 844  N N   . GLN A 1 100 ? 44.532 59.067  184.693 1.00 83.39  ? 100 GLN A N   1 
ATOM 845  C CA  . GLN A 1 100 ? 44.185 59.423  186.071 1.00 88.11  ? 100 GLN A CA  1 
ATOM 846  C C   . GLN A 1 100 ? 43.474 58.357  186.888 1.00 90.02  ? 100 GLN A C   1 
ATOM 847  O O   . GLN A 1 100 ? 43.727 58.252  188.093 1.00 90.68  ? 100 GLN A O   1 
ATOM 848  C CB  . GLN A 1 100 ? 43.328 60.699  186.121 1.00 90.19  ? 100 GLN A CB  1 
ATOM 849  C CG  . GLN A 1 100 ? 44.054 61.994  185.772 1.00 93.04  ? 100 GLN A CG  1 
ATOM 850  C CD  . GLN A 1 100 ? 45.536 61.930  186.043 1.00 94.79  ? 100 GLN A CD  1 
ATOM 851  O OE1 . GLN A 1 100 ? 45.977 61.459  187.108 1.00 95.39  ? 100 GLN A OE1 1 
ATOM 852  N NE2 . GLN A 1 100 ? 46.324 62.409  185.082 1.00 96.24  ? 100 GLN A NE2 1 
ATOM 853  N N   . TYR A 1 101 ? 42.582 57.591  186.249 1.00 91.79  ? 101 TYR A N   1 
ATOM 854  C CA  . TYR A 1 101 ? 41.835 56.521  186.926 1.00 92.42  ? 101 TYR A CA  1 
ATOM 855  C C   . TYR A 1 101 ? 42.857 55.403  187.229 1.00 90.50  ? 101 TYR A C   1 
ATOM 856  O O   . TYR A 1 101 ? 42.545 54.372  187.866 1.00 91.02  ? 101 TYR A O   1 
ATOM 857  C CB  . TYR A 1 101 ? 40.693 56.019  186.026 1.00 95.99  ? 101 TYR A CB  1 
ATOM 858  C CG  . TYR A 1 101 ? 39.570 55.323  186.775 1.00 99.48  ? 101 TYR A CG  1 
ATOM 859  C CD1 . TYR A 1 101 ? 38.655 56.047  187.555 1.00 100.68 ? 101 TYR A CD1 1 
ATOM 860  C CD2 . TYR A 1 101 ? 39.445 53.932  186.734 1.00 100.85 ? 101 TYR A CD2 1 
ATOM 861  C CE1 . TYR A 1 101 ? 37.639 55.385  188.281 1.00 102.31 ? 101 TYR A CE1 1 
ATOM 862  C CE2 . TYR A 1 101 ? 38.440 53.263  187.453 1.00 101.76 ? 101 TYR A CE2 1 
ATOM 863  C CZ  . TYR A 1 101 ? 37.541 53.989  188.225 1.00 102.23 ? 101 TYR A CZ  1 
ATOM 864  O OH  . TYR A 1 101 ? 36.568 53.316  188.943 1.00 101.79 ? 101 TYR A OH  1 
ATOM 865  N N   . ASN A 1 102 ? 44.084 55.661  186.762 1.00 86.84  ? 102 ASN A N   1 
ATOM 866  C CA  . ASN A 1 102 ? 45.224 54.805  186.993 1.00 82.57  ? 102 ASN A CA  1 
ATOM 867  C C   . ASN A 1 102 ? 45.311 53.607  186.054 1.00 78.71  ? 102 ASN A C   1 
ATOM 868  O O   . ASN A 1 102 ? 45.246 52.480  186.524 1.00 78.78  ? 102 ASN A O   1 
ATOM 869  C CB  . ASN A 1 102 ? 45.198 54.318  188.468 1.00 83.93  ? 102 ASN A CB  1 
ATOM 870  C CG  . ASN A 1 102 ? 45.199 55.477  189.505 1.00 84.44  ? 102 ASN A CG  1 
ATOM 871  O OD1 . ASN A 1 102 ? 44.686 55.327  190.631 1.00 84.15  ? 102 ASN A OD1 1 
ATOM 872  N ND2 . ASN A 1 102 ? 45.798 56.618  189.133 1.00 84.45  ? 102 ASN A ND2 1 
ATOM 873  N N   . ILE A 1 103 ? 45.447 53.831  184.745 1.00 74.35  ? 103 ILE A N   1 
ATOM 874  C CA  . ILE A 1 103 ? 45.589 52.725  183.761 1.00 69.75  ? 103 ILE A CA  1 
ATOM 875  C C   . ILE A 1 103 ? 46.371 53.180  182.512 1.00 65.54  ? 103 ILE A C   1 
ATOM 876  O O   . ILE A 1 103 ? 45.877 53.114  181.376 1.00 64.17  ? 103 ILE A O   1 
ATOM 877  C CB  . ILE A 1 103 ? 44.230 52.186  183.243 1.00 69.46  ? 103 ILE A CB  1 
ATOM 878  C CG1 . ILE A 1 103 ? 43.258 51.951  184.394 1.00 69.21  ? 103 ILE A CG1 1 
ATOM 879  C CG2 . ILE A 1 103 ? 44.463 50.873  182.465 1.00 69.33  ? 103 ILE A CG2 1 
ATOM 880  C CD1 . ILE A 1 103 ? 41.983 51.302  183.915 1.00 69.09  ? 103 ILE A CD1 1 
ATOM 881  N N   . LEU A 1 104 ? 47.602 53.614  182.744 1.00 60.96  ? 104 LEU A N   1 
ATOM 882  C CA  . LEU A 1 104 ? 48.483 54.141  181.714 1.00 56.81  ? 104 LEU A CA  1 
ATOM 883  C C   . LEU A 1 104 ? 48.613 53.437  180.359 1.00 54.23  ? 104 LEU A C   1 
ATOM 884  O O   . LEU A 1 104 ? 48.241 54.001  179.338 1.00 53.81  ? 104 LEU A O   1 
ATOM 885  C CB  . LEU A 1 104 ? 49.877 54.336  182.306 1.00 55.13  ? 104 LEU A CB  1 
ATOM 886  C CG  . LEU A 1 104 ? 50.805 55.060  181.351 1.00 53.70  ? 104 LEU A CG  1 
ATOM 887  C CD1 . LEU A 1 104 ? 50.673 56.554  181.531 1.00 53.16  ? 104 LEU A CD1 1 
ATOM 888  C CD2 . LEU A 1 104 ? 52.200 54.611  181.599 1.00 53.06  ? 104 LEU A CD2 1 
ATOM 889  N N   . VAL A 1 105 ? 49.146 52.223  180.333 1.00 52.44  ? 105 VAL A N   1 
ATOM 890  C CA  . VAL A 1 105 ? 49.341 51.540  179.056 1.00 50.96  ? 105 VAL A CA  1 
ATOM 891  C C   . VAL A 1 105 ? 48.222 51.673  178.037 1.00 50.68  ? 105 VAL A C   1 
ATOM 892  O O   . VAL A 1 105 ? 48.497 51.765  176.840 1.00 50.39  ? 105 VAL A O   1 
ATOM 893  C CB  . VAL A 1 105 ? 49.607 50.034  179.209 1.00 50.00  ? 105 VAL A CB  1 
ATOM 894  C CG1 . VAL A 1 105 ? 50.189 49.498  177.910 1.00 48.28  ? 105 VAL A CG1 1 
ATOM 895  C CG2 . VAL A 1 105 ? 50.552 49.776  180.352 1.00 49.96  ? 105 VAL A CG2 1 
ATOM 896  N N   . GLY A 1 106 ? 46.970 51.660  178.488 1.00 50.63  ? 106 GLY A N   1 
ATOM 897  C CA  . GLY A 1 106 ? 45.855 51.791  177.555 1.00 50.51  ? 106 GLY A CA  1 
ATOM 898  C C   . GLY A 1 106 ? 45.712 53.194  176.966 1.00 50.68  ? 106 GLY A C   1 
ATOM 899  O O   . GLY A 1 106 ? 45.695 53.371  175.733 1.00 50.51  ? 106 GLY A O   1 
ATOM 900  N N   . SER A 1 107 ? 45.609 54.190  177.849 1.00 50.08  ? 107 SER A N   1 
ATOM 901  C CA  . SER A 1 107 ? 45.464 55.597  177.449 1.00 48.36  ? 107 SER A CA  1 
ATOM 902  C C   . SER A 1 107 ? 46.450 55.940  176.336 1.00 46.38  ? 107 SER A C   1 
ATOM 903  O O   . SER A 1 107 ? 46.099 56.559  175.337 1.00 45.45  ? 107 SER A O   1 
ATOM 904  C CB  . SER A 1 107 ? 45.712 56.510  178.660 1.00 49.12  ? 107 SER A CB  1 
ATOM 905  O OG  . SER A 1 107 ? 44.896 57.679  178.654 1.00 49.65  ? 107 SER A OG  1 
ATOM 906  N N   . ILE A 1 108 ? 47.691 55.530  176.524 1.00 44.13  ? 108 ILE A N   1 
ATOM 907  C CA  . ILE A 1 108 ? 48.710 55.779  175.541 1.00 42.07  ? 108 ILE A CA  1 
ATOM 908  C C   . ILE A 1 108 ? 48.275 55.116  174.244 1.00 40.58  ? 108 ILE A C   1 
ATOM 909  O O   . ILE A 1 108 ? 47.688 55.753  173.373 1.00 39.45  ? 108 ILE A O   1 
ATOM 910  C CB  . ILE A 1 108 ? 50.043 55.187  176.010 1.00 42.54  ? 108 ILE A CB  1 
ATOM 911  C CG1 . ILE A 1 108 ? 50.250 55.539  177.483 1.00 43.23  ? 108 ILE A CG1 1 
ATOM 912  C CG2 . ILE A 1 108 ? 51.179 55.745  175.200 1.00 42.36  ? 108 ILE A CG2 1 
ATOM 913  C CD1 . ILE A 1 108 ? 51.629 55.214  178.016 1.00 44.97  ? 108 ILE A CD1 1 
ATOM 914  N N   . VAL A 1 109 ? 48.537 53.823  174.135 1.00 39.12  ? 109 VAL A N   1 
ATOM 915  C CA  . VAL A 1 109 ? 48.194 53.100  172.934 1.00 38.17  ? 109 VAL A CA  1 
ATOM 916  C C   . VAL A 1 109 ? 46.890 53.616  172.371 1.00 38.80  ? 109 VAL A C   1 
ATOM 917  O O   . VAL A 1 109 ? 46.846 54.133  171.254 1.00 38.93  ? 109 VAL A O   1 
ATOM 918  C CB  . VAL A 1 109 ? 48.075 51.604  173.216 1.00 37.33  ? 109 VAL A CB  1 
ATOM 919  C CG1 . VAL A 1 109 ? 47.921 50.848  171.925 1.00 36.78  ? 109 VAL A CG1 1 
ATOM 920  C CG2 . VAL A 1 109 ? 49.306 51.130  173.971 1.00 37.19  ? 109 VAL A CG2 1 
ATOM 921  N N   . GLY A 1 110 ? 45.828 53.502  173.156 1.00 39.07  ? 110 GLY A N   1 
ATOM 922  C CA  . GLY A 1 110 ? 44.536 53.969  172.691 1.00 40.05  ? 110 GLY A CA  1 
ATOM 923  C C   . GLY A 1 110 ? 44.528 55.462  172.450 1.00 39.97  ? 110 GLY A C   1 
ATOM 924  O O   . GLY A 1 110 ? 43.755 55.975  171.654 1.00 39.49  ? 110 GLY A O   1 
ATOM 925  N N   . GLY A 1 111 ? 45.418 56.158  173.128 1.00 40.70  ? 111 GLY A N   1 
ATOM 926  C CA  . GLY A 1 111 ? 45.460 57.591  172.996 1.00 42.92  ? 111 GLY A CA  1 
ATOM 927  C C   . GLY A 1 111 ? 46.277 58.138  171.859 1.00 44.09  ? 111 GLY A C   1 
ATOM 928  O O   . GLY A 1 111 ? 46.164 59.315  171.516 1.00 45.34  ? 111 GLY A O   1 
ATOM 929  N N   . ILE A 1 112 ? 47.081 57.305  171.230 1.00 44.85  ? 112 ILE A N   1 
ATOM 930  C CA  . ILE A 1 112 ? 47.893 57.843  170.170 1.00 47.07  ? 112 ILE A CA  1 
ATOM 931  C C   . ILE A 1 112 ? 47.338 57.725  168.758 1.00 48.75  ? 112 ILE A C   1 
ATOM 932  O O   . ILE A 1 112 ? 48.039 57.344  167.815 1.00 48.27  ? 112 ILE A O   1 
ATOM 933  C CB  . ILE A 1 112 ? 49.260 57.242  170.221 1.00 46.78  ? 112 ILE A CB  1 
ATOM 934  C CG1 . ILE A 1 112 ? 49.721 57.208  171.676 1.00 46.88  ? 112 ILE A CG1 1 
ATOM 935  C CG2 . ILE A 1 112 ? 50.196 58.077  169.391 1.00 46.67  ? 112 ILE A CG2 1 
ATOM 936  C CD1 . ILE A 1 112 ? 50.975 56.488  171.864 1.00 47.75  ? 112 ILE A CD1 1 
ATOM 937  N N   . TYR A 1 113 ? 46.063 58.059  168.616 1.00 51.91  ? 113 TYR A N   1 
ATOM 938  C CA  . TYR A 1 113 ? 45.408 58.037  167.319 1.00 54.39  ? 113 TYR A CA  1 
ATOM 939  C C   . TYR A 1 113 ? 44.937 59.453  166.997 1.00 54.23  ? 113 TYR A C   1 
ATOM 940  O O   . TYR A 1 113 ? 45.388 60.047  166.013 1.00 53.38  ? 113 TYR A O   1 
ATOM 941  C CB  . TYR A 1 113 ? 44.265 57.017  167.318 1.00 57.15  ? 113 TYR A CB  1 
ATOM 942  C CG  . TYR A 1 113 ? 44.775 55.622  167.053 1.00 59.82  ? 113 TYR A CG  1 
ATOM 943  C CD1 . TYR A 1 113 ? 45.782 55.057  167.844 1.00 60.22  ? 113 TYR A CD1 1 
ATOM 944  C CD2 . TYR A 1 113 ? 44.279 54.884  165.986 1.00 62.12  ? 113 TYR A CD2 1 
ATOM 945  C CE1 . TYR A 1 113 ? 46.273 53.795  167.579 1.00 61.50  ? 113 TYR A CE1 1 
ATOM 946  C CE2 . TYR A 1 113 ? 44.768 53.614  165.700 1.00 64.08  ? 113 TYR A CE2 1 
ATOM 947  C CZ  . TYR A 1 113 ? 45.768 53.068  166.501 1.00 63.59  ? 113 TYR A CZ  1 
ATOM 948  O OH  . TYR A 1 113 ? 46.232 51.794  166.216 1.00 63.75  ? 113 TYR A OH  1 
ATOM 949  N N   . LEU A 1 114 ? 44.053 60.017  167.819 1.00 53.95  ? 114 LEU A N   1 
ATOM 950  C CA  . LEU A 1 114 ? 43.650 61.390  167.561 1.00 54.53  ? 114 LEU A CA  1 
ATOM 951  C C   . LEU A 1 114 ? 45.009 62.073  167.729 1.00 55.24  ? 114 LEU A C   1 
ATOM 952  O O   . LEU A 1 114 ? 45.242 63.184  167.236 1.00 56.57  ? 114 LEU A O   1 
ATOM 953  C CB  . LEU A 1 114 ? 42.640 61.897  168.610 1.00 53.87  ? 114 LEU A CB  1 
ATOM 954  C CG  . LEU A 1 114 ? 42.087 63.319  168.354 1.00 54.05  ? 114 LEU A CG  1 
ATOM 955  C CD1 . LEU A 1 114 ? 40.665 63.458  168.840 1.00 54.09  ? 114 LEU A CD1 1 
ATOM 956  C CD2 . LEU A 1 114 ? 42.980 64.360  169.003 1.00 53.40  ? 114 LEU A CD2 1 
ATOM 957  N N   . GLY A 1 115 ? 45.920 61.352  168.392 1.00 55.51  ? 115 GLY A N   1 
ATOM 958  C CA  . GLY A 1 115 ? 47.266 61.846  168.644 1.00 55.76  ? 115 GLY A CA  1 
ATOM 959  C C   . GLY A 1 115 ? 48.181 61.673  167.452 1.00 56.25  ? 115 GLY A C   1 
ATOM 960  O O   . GLY A 1 115 ? 49.334 62.107  167.478 1.00 57.02  ? 115 GLY A O   1 
ATOM 961  N N   . PHE A 1 116 ? 47.659 61.045  166.403 1.00 55.78  ? 116 PHE A N   1 
ATOM 962  C CA  . PHE A 1 116 ? 48.427 60.815  165.188 1.00 55.17  ? 116 PHE A CA  1 
ATOM 963  C C   . PHE A 1 116 ? 48.242 61.996  164.271 1.00 55.57  ? 116 PHE A C   1 
ATOM 964  O O   . PHE A 1 116 ? 49.153 62.377  163.535 1.00 55.72  ? 116 PHE A O   1 
ATOM 965  C CB  . PHE A 1 116 ? 47.900 59.594  164.479 1.00 54.35  ? 116 PHE A CB  1 
ATOM 966  C CG  . PHE A 1 116 ? 47.038 59.903  163.281 1.00 53.98  ? 116 PHE A CG  1 
ATOM 967  C CD1 . PHE A 1 116 ? 47.616 60.250  162.066 1.00 54.99  ? 116 PHE A CD1 1 
ATOM 968  C CD2 . PHE A 1 116 ? 45.659 59.771  163.341 1.00 53.87  ? 116 PHE A CD2 1 
ATOM 969  C CE1 . PHE A 1 116 ? 46.836 60.451  160.925 1.00 55.44  ? 116 PHE A CE1 1 
ATOM 970  C CE2 . PHE A 1 116 ? 44.869 59.969  162.205 1.00 54.15  ? 116 PHE A CE2 1 
ATOM 971  C CZ  . PHE A 1 116 ? 45.457 60.306  160.999 1.00 54.91  ? 116 PHE A CZ  1 
ATOM 972  N N   . CYS A 1 117 ? 47.021 62.525  164.289 1.00 55.09  ? 117 CYS A N   1 
ATOM 973  C CA  . CYS A 1 117 ? 46.609 63.657  163.469 1.00 54.49  ? 117 CYS A CA  1 
ATOM 974  C C   . CYS A 1 117 ? 47.567 64.819  163.458 1.00 54.01  ? 117 CYS A C   1 
ATOM 975  O O   . CYS A 1 117 ? 47.273 65.835  162.850 1.00 53.37  ? 117 CYS A O   1 
ATOM 976  C CB  . CYS A 1 117 ? 45.246 64.139  163.936 1.00 53.57  ? 117 CYS A CB  1 
ATOM 977  S SG  . CYS A 1 117 ? 43.980 62.792  163.770 1.00 52.92  ? 117 CYS A SG  1 
ATOM 978  N N   . PHE A 1 118 ? 48.703 64.683  164.130 1.00 54.11  ? 118 PHE A N   1 
ATOM 979  C CA  . PHE A 1 118 ? 49.671 65.761  164.170 1.00 53.87  ? 118 PHE A CA  1 
ATOM 980  C C   . PHE A 1 118 ? 51.088 65.379  163.779 1.00 53.09  ? 118 PHE A C   1 
ATOM 981  O O   . PHE A 1 118 ? 51.990 66.218  163.801 1.00 53.89  ? 118 PHE A O   1 
ATOM 982  C CB  . PHE A 1 118 ? 49.636 66.433  165.547 1.00 54.13  ? 118 PHE A CB  1 
ATOM 983  C CG  . PHE A 1 118 ? 48.599 67.502  165.649 1.00 53.84  ? 118 PHE A CG  1 
ATOM 984  C CD1 . PHE A 1 118 ? 48.310 68.278  164.539 1.00 54.23  ? 118 PHE A CD1 1 
ATOM 985  C CD2 . PHE A 1 118 ? 47.875 67.693  166.801 1.00 54.05  ? 118 PHE A CD2 1 
ATOM 986  C CE1 . PHE A 1 118 ? 47.322 69.227  164.566 1.00 54.43  ? 118 PHE A CE1 1 
ATOM 987  C CE2 . PHE A 1 118 ? 46.879 68.646  166.834 1.00 55.03  ? 118 PHE A CE2 1 
ATOM 988  C CZ  . PHE A 1 118 ? 46.603 69.410  165.700 1.00 54.67  ? 118 PHE A CZ  1 
ATOM 989  N N   . ASN A 1 119 ? 51.294 64.118  163.420 1.00 51.71  ? 119 ASN A N   1 
ATOM 990  C CA  . ASN A 1 119 ? 52.612 63.715  162.971 1.00 50.01  ? 119 ASN A CA  1 
ATOM 991  C C   . ASN A 1 119 ? 52.535 63.374  161.477 1.00 48.17  ? 119 ASN A C   1 
ATOM 992  O O   . ASN A 1 119 ? 53.353 63.833  160.674 1.00 47.76  ? 119 ASN A O   1 
ATOM 993  C CB  . ASN A 1 119 ? 53.141 62.531  163.769 1.00 50.05  ? 119 ASN A CB  1 
ATOM 994  C CG  . ASN A 1 119 ? 54.634 62.379  163.610 1.00 51.26  ? 119 ASN A CG  1 
ATOM 995  O OD1 . ASN A 1 119 ? 55.208 62.839  162.619 1.00 52.66  ? 119 ASN A OD1 1 
ATOM 996  N ND2 . ASN A 1 119 ? 55.274 61.737  164.572 1.00 50.88  ? 119 ASN A ND2 1 
ATOM 997  N N   . ALA A 1 120 ? 51.549 62.576  161.098 1.00 46.32  ? 120 ALA A N   1 
ATOM 998  C CA  . ALA A 1 120 ? 51.383 62.238  159.697 1.00 44.13  ? 120 ALA A CA  1 
ATOM 999  C C   . ALA A 1 120 ? 50.779 63.463  159.036 1.00 43.26  ? 120 ALA A C   1 
ATOM 1000 O O   . ALA A 1 120 ? 51.337 64.031  158.099 1.00 42.01  ? 120 ALA A O   1 
ATOM 1001 C CB  . ALA A 1 120 ? 50.441 61.065  159.558 1.00 43.72  ? 120 ALA A CB  1 
ATOM 1002 N N   . GLY A 1 121 ? 49.628 63.860  159.566 1.00 42.50  ? 121 GLY A N   1 
ATOM 1003 C CA  . GLY A 1 121 ? 48.905 65.003  159.056 1.00 41.18  ? 121 GLY A CA  1 
ATOM 1004 C C   . GLY A 1 121 ? 49.833 66.106  158.629 1.00 39.84  ? 121 GLY A C   1 
ATOM 1005 O O   . GLY A 1 121 ? 49.650 66.729  157.595 1.00 38.93  ? 121 GLY A O   1 
ATOM 1006 N N   . ALA A 1 122 ? 50.851 66.351  159.431 1.00 39.37  ? 122 ALA A N   1 
ATOM 1007 C CA  . ALA A 1 122 ? 51.781 67.400  159.079 1.00 38.38  ? 122 ALA A CA  1 
ATOM 1008 C C   . ALA A 1 122 ? 52.256 67.128  157.672 1.00 37.57  ? 122 ALA A C   1 
ATOM 1009 O O   . ALA A 1 122 ? 51.869 67.832  156.753 1.00 37.76  ? 122 ALA A O   1 
ATOM 1010 C CB  . ALA A 1 122 ? 52.937 67.443  160.048 1.00 38.94  ? 122 ALA A CB  1 
ATOM 1011 N N   . PRO A 1 123 ? 53.098 66.106  157.473 1.00 36.87  ? 123 PRO A N   1 
ATOM 1012 C CA  . PRO A 1 123 ? 53.502 65.908  156.085 1.00 36.48  ? 123 PRO A CA  1 
ATOM 1013 C C   . PRO A 1 123 ? 52.295 65.753  155.209 1.00 36.71  ? 123 PRO A C   1 
ATOM 1014 O O   . PRO A 1 123 ? 52.378 65.913  153.995 1.00 37.86  ? 123 PRO A O   1 
ATOM 1015 C CB  . PRO A 1 123 ? 54.381 64.662  156.143 1.00 35.80  ? 123 PRO A CB  1 
ATOM 1016 C CG  . PRO A 1 123 ? 54.137 64.085  157.538 1.00 36.38  ? 123 PRO A CG  1 
ATOM 1017 C CD  . PRO A 1 123 ? 53.934 65.296  158.367 1.00 36.34  ? 123 PRO A CD  1 
ATOM 1018 N N   . ALA A 1 124 ? 51.168 65.451  155.839 1.00 36.43  ? 124 ALA A N   1 
ATOM 1019 C CA  . ALA A 1 124 ? 49.911 65.331  155.120 1.00 36.79  ? 124 ALA A CA  1 
ATOM 1020 C C   . ALA A 1 124 ? 49.466 66.722  154.604 1.00 37.64  ? 124 ALA A C   1 
ATOM 1021 O O   . ALA A 1 124 ? 49.654 66.983  153.429 1.00 36.79  ? 124 ALA A O   1 
ATOM 1022 C CB  . ALA A 1 124 ? 48.900 64.721  156.029 1.00 36.48  ? 124 ALA A CB  1 
ATOM 1023 N N   . VAL A 1 125 ? 48.914 67.604  155.450 1.00 38.85  ? 125 VAL A N   1 
ATOM 1024 C CA  . VAL A 1 125 ? 48.508 68.978  155.038 1.00 40.12  ? 125 VAL A CA  1 
ATOM 1025 C C   . VAL A 1 125 ? 49.659 69.588  154.254 1.00 41.16  ? 125 VAL A C   1 
ATOM 1026 O O   . VAL A 1 125 ? 49.474 70.088  153.148 1.00 41.59  ? 125 VAL A O   1 
ATOM 1027 C CB  . VAL A 1 125 ? 48.238 69.877  156.294 1.00 39.99  ? 125 VAL A CB  1 
ATOM 1028 C CG1 . VAL A 1 125 ? 47.920 71.335  155.950 1.00 39.89  ? 125 VAL A CG1 1 
ATOM 1029 C CG2 . VAL A 1 125 ? 47.118 69.260  157.083 1.00 40.09  ? 125 VAL A CG2 1 
ATOM 1030 N N   . GLU A 1 126 ? 50.858 69.510  154.830 1.00 42.84  ? 126 GLU A N   1 
ATOM 1031 C CA  . GLU A 1 126 ? 52.071 70.001  154.168 1.00 44.51  ? 126 GLU A CA  1 
ATOM 1032 C C   . GLU A 1 126 ? 52.053 69.461  152.736 1.00 45.59  ? 126 GLU A C   1 
ATOM 1033 O O   . GLU A 1 126 ? 52.446 70.163  151.800 1.00 46.77  ? 126 GLU A O   1 
ATOM 1034 C CB  . GLU A 1 126 ? 53.344 69.474  154.851 1.00 45.28  ? 126 GLU A CB  1 
ATOM 1035 C CG  . GLU A 1 126 ? 53.698 70.130  156.178 1.00 47.23  ? 126 GLU A CG  1 
ATOM 1036 C CD  . GLU A 1 126 ? 55.131 69.840  156.605 1.00 47.93  ? 126 GLU A CD  1 
ATOM 1037 O OE1 . GLU A 1 126 ? 55.485 68.657  156.801 1.00 47.71  ? 126 GLU A OE1 1 
ATOM 1038 O OE2 . GLU A 1 126 ? 55.909 70.813  156.731 1.00 49.88  ? 126 GLU A OE2 1 
ATOM 1039 N N   . ALA A 1 127 ? 51.574 68.229  152.565 1.00 45.79  ? 127 ALA A N   1 
ATOM 1040 C CA  . ALA A 1 127 ? 51.537 67.619  151.245 1.00 45.11  ? 127 ALA A CA  1 
ATOM 1041 C C   . ALA A 1 127 ? 50.385 68.123  150.410 1.00 44.21  ? 127 ALA A C   1 
ATOM 1042 O O   . ALA A 1 127 ? 50.537 69.011  149.567 1.00 43.58  ? 127 ALA A O   1 
ATOM 1043 C CB  . ALA A 1 127 ? 51.410 66.111  151.367 1.00 45.23  ? 127 ALA A CB  1 
ATOM 1044 N N   . PHE A 1 128 ? 49.223 67.536  150.642 1.00 42.79  ? 128 PHE A N   1 
ATOM 1045 C CA  . PHE A 1 128 ? 48.093 67.924  149.856 1.00 42.60  ? 128 PHE A CA  1 
ATOM 1046 C C   . PHE A 1 128 ? 48.141 69.329  149.332 1.00 42.77  ? 128 PHE A C   1 
ATOM 1047 O O   . PHE A 1 128 ? 48.122 69.571  148.136 1.00 42.16  ? 128 PHE A O   1 
ATOM 1048 C CB  . PHE A 1 128 ? 46.853 67.775  150.655 1.00 43.06  ? 128 PHE A CB  1 
ATOM 1049 C CG  . PHE A 1 128 ? 45.629 68.062  149.888 1.00 43.29  ? 128 PHE A CG  1 
ATOM 1050 C CD1 . PHE A 1 128 ? 45.297 69.359  149.518 1.00 42.53  ? 128 PHE A CD1 1 
ATOM 1051 C CD2 . PHE A 1 128 ? 44.751 67.037  149.604 1.00 43.76  ? 128 PHE A CD2 1 
ATOM 1052 C CE1 . PHE A 1 128 ? 44.107 69.615  148.889 1.00 42.52  ? 128 PHE A CE1 1 
ATOM 1053 C CE2 . PHE A 1 128 ? 43.559 67.291  148.975 1.00 43.41  ? 128 PHE A CE2 1 
ATOM 1054 C CZ  . PHE A 1 128 ? 43.234 68.580  148.620 1.00 43.02  ? 128 PHE A CZ  1 
ATOM 1055 N N   . ILE A 1 129 ? 48.146 70.267  150.252 1.00 43.77  ? 129 ILE A N   1 
ATOM 1056 C CA  . ILE A 1 129 ? 48.172 71.665  149.889 1.00 45.02  ? 129 ILE A CA  1 
ATOM 1057 C C   . ILE A 1 129 ? 49.224 71.923  148.832 1.00 46.03  ? 129 ILE A C   1 
ATOM 1058 O O   . ILE A 1 129 ? 49.006 72.661  147.881 1.00 45.29  ? 129 ILE A O   1 
ATOM 1059 C CB  . ILE A 1 129 ? 48.453 72.503  151.116 1.00 45.51  ? 129 ILE A CB  1 
ATOM 1060 C CG1 . ILE A 1 129 ? 47.429 72.147  152.192 1.00 47.13  ? 129 ILE A CG1 1 
ATOM 1061 C CG2 . ILE A 1 129 ? 48.383 73.951  150.774 1.00 45.89  ? 129 ILE A CG2 1 
ATOM 1062 C CD1 . ILE A 1 129 ? 47.081 73.272  153.130 1.00 48.86  ? 129 ILE A CD1 1 
ATOM 1063 N N   . GLU A 1 130 ? 50.375 71.299  149.002 1.00 47.79  ? 130 GLU A N   1 
ATOM 1064 C CA  . GLU A 1 130 ? 51.445 71.453  148.036 1.00 50.03  ? 130 GLU A CA  1 
ATOM 1065 C C   . GLU A 1 130 ? 50.913 71.119  146.652 1.00 50.10  ? 130 GLU A C   1 
ATOM 1066 O O   . GLU A 1 130 ? 51.093 71.902  145.722 1.00 50.64  ? 130 GLU A O   1 
ATOM 1067 C CB  . GLU A 1 130 ? 52.627 70.542  148.384 1.00 51.66  ? 130 GLU A CB  1 
ATOM 1068 C CG  . GLU A 1 130 ? 53.702 70.412  147.293 1.00 54.09  ? 130 GLU A CG  1 
ATOM 1069 C CD  . GLU A 1 130 ? 55.041 69.903  147.848 1.00 55.91  ? 130 GLU A CD  1 
ATOM 1070 O OE1 . GLU A 1 130 ? 55.086 69.475  149.033 1.00 56.96  ? 130 GLU A OE1 1 
ATOM 1071 O OE2 . GLU A 1 130 ? 56.053 69.932  147.098 1.00 56.73  ? 130 GLU A OE2 1 
ATOM 1072 N N   . LYS A 1 131 ? 50.251 69.973  146.505 1.00 50.38  ? 131 LYS A N   1 
ATOM 1073 C CA  . LYS A 1 131 ? 49.716 69.620  145.198 1.00 50.28  ? 131 LYS A CA  1 
ATOM 1074 C C   . LYS A 1 131 ? 48.777 70.727  144.734 1.00 50.35  ? 131 LYS A C   1 
ATOM 1075 O O   . LYS A 1 131 ? 48.748 71.056  143.555 1.00 50.05  ? 131 LYS A O   1 
ATOM 1076 C CB  . LYS A 1 131 ? 49.000 68.255  145.220 1.00 50.81  ? 131 LYS A CB  1 
ATOM 1077 C CG  . LYS A 1 131 ? 49.949 67.071  144.985 1.00 51.87  ? 131 LYS A CG  1 
ATOM 1078 C CD  . LYS A 1 131 ? 49.269 65.711  145.061 1.00 52.92  ? 131 LYS A CD  1 
ATOM 1079 C CE  . LYS A 1 131 ? 50.348 64.636  145.192 1.00 54.28  ? 131 LYS A CE  1 
ATOM 1080 N NZ  . LYS A 1 131 ? 49.813 63.267  145.479 1.00 55.60  ? 131 LYS A NZ  1 
ATOM 1081 N N   . VAL A 1 132 ? 48.040 71.345  145.647 1.00 49.82  ? 132 VAL A N   1 
ATOM 1082 C CA  . VAL A 1 132 ? 47.149 72.405  145.213 1.00 49.39  ? 132 VAL A CA  1 
ATOM 1083 C C   . VAL A 1 132 ? 47.935 73.645  144.808 1.00 49.95  ? 132 VAL A C   1 
ATOM 1084 O O   . VAL A 1 132 ? 47.419 74.496  144.094 1.00 50.12  ? 132 VAL A O   1 
ATOM 1085 C CB  . VAL A 1 132 ? 46.131 72.751  146.297 1.00 49.39  ? 132 VAL A CB  1 
ATOM 1086 C CG1 . VAL A 1 132 ? 44.918 73.449  145.678 1.00 49.13  ? 132 VAL A CG1 1 
ATOM 1087 C CG2 . VAL A 1 132 ? 45.720 71.481  146.994 1.00 48.80  ? 132 VAL A CG2 1 
ATOM 1088 N N   . SER A 1 133 ? 49.190 73.755  145.219 1.00 50.53  ? 133 SER A N   1 
ATOM 1089 C CA  . SER A 1 133 ? 49.931 74.933  144.808 1.00 51.42  ? 133 SER A CA  1 
ATOM 1090 C C   . SER A 1 133 ? 50.289 74.821  143.329 1.00 52.99  ? 133 SER A C   1 
ATOM 1091 O O   . SER A 1 133 ? 50.392 75.837  142.641 1.00 53.25  ? 133 SER A O   1 
ATOM 1092 C CB  . SER A 1 133 ? 51.196 75.119  145.637 1.00 51.18  ? 133 SER A CB  1 
ATOM 1093 O OG  . SER A 1 133 ? 51.962 76.169  145.082 1.00 50.40  ? 133 SER A OG  1 
ATOM 1094 N N   . ARG A 1 134 ? 50.459 73.588  142.848 1.00 54.95  ? 134 ARG A N   1 
ATOM 1095 C CA  . ARG A 1 134 ? 50.794 73.336  141.445 1.00 56.92  ? 134 ARG A CA  1 
ATOM 1096 C C   . ARG A 1 134 ? 49.553 73.540  140.572 1.00 58.24  ? 134 ARG A C   1 
ATOM 1097 O O   . ARG A 1 134 ? 49.653 73.706  139.347 1.00 58.98  ? 134 ARG A O   1 
ATOM 1098 C CB  . ARG A 1 134 ? 51.330 71.903  141.256 1.00 57.17  ? 134 ARG A CB  1 
ATOM 1099 C CG  . ARG A 1 134 ? 52.839 71.712  141.516 1.00 57.40  ? 134 ARG A CG  1 
ATOM 1100 C CD  . ARG A 1 134 ? 53.238 70.226  141.538 1.00 58.48  ? 134 ARG A CD  1 
ATOM 1101 N NE  . ARG A 1 134 ? 54.681 70.002  141.617 1.00 58.90  ? 134 ARG A NE  1 
ATOM 1102 C CZ  . ARG A 1 134 ? 55.240 68.814  141.845 1.00 58.91  ? 134 ARG A CZ  1 
ATOM 1103 N NH1 . ARG A 1 134 ? 54.471 67.746  142.018 1.00 58.84  ? 134 ARG A NH1 1 
ATOM 1104 N NH2 . ARG A 1 134 ? 56.567 68.687  141.897 1.00 58.44  ? 134 ARG A NH2 1 
ATOM 1105 N N   . ARG A 1 135 ? 48.383 73.542  141.206 1.00 59.01  ? 135 ARG A N   1 
ATOM 1106 C CA  . ARG A 1 135 ? 47.145 73.715  140.460 1.00 59.75  ? 135 ARG A CA  1 
ATOM 1107 C C   . ARG A 1 135 ? 46.841 75.177  140.186 1.00 59.29  ? 135 ARG A C   1 
ATOM 1108 O O   . ARG A 1 135 ? 46.453 75.532  139.084 1.00 59.57  ? 135 ARG A O   1 
ATOM 1109 C CB  . ARG A 1 135 ? 45.958 73.088  141.205 1.00 60.90  ? 135 ARG A CB  1 
ATOM 1110 C CG  . ARG A 1 135 ? 44.804 72.620  140.284 1.00 62.86  ? 135 ARG A CG  1 
ATOM 1111 C CD  . ARG A 1 135 ? 44.199 73.771  139.436 1.00 66.30  ? 135 ARG A CD  1 
ATOM 1112 N NE  . ARG A 1 135 ? 43.065 73.384  138.586 1.00 69.17  ? 135 ARG A NE  1 
ATOM 1113 C CZ  . ARG A 1 135 ? 42.434 74.194  137.721 1.00 69.97  ? 135 ARG A CZ  1 
ATOM 1114 N NH1 . ARG A 1 135 ? 42.810 75.460  137.560 1.00 69.97  ? 135 ARG A NH1 1 
ATOM 1115 N NH2 . ARG A 1 135 ? 41.400 73.744  137.014 1.00 70.14  ? 135 ARG A NH2 1 
ATOM 1116 N N   . SER A 1 136 ? 47.037 76.030  141.176 1.00 58.62  ? 136 SER A N   1 
ATOM 1117 C CA  . SER A 1 136 ? 46.715 77.425  140.990 1.00 58.31  ? 136 SER A CA  1 
ATOM 1118 C C   . SER A 1 136 ? 47.836 78.348  140.626 1.00 58.98  ? 136 SER A C   1 
ATOM 1119 O O   . SER A 1 136 ? 47.580 79.382  140.049 1.00 59.46  ? 136 SER A O   1 
ATOM 1120 C CB  . SER A 1 136 ? 46.037 77.980  142.227 1.00 58.72  ? 136 SER A CB  1 
ATOM 1121 O OG  . SER A 1 136 ? 46.535 79.284  142.507 1.00 58.82  ? 136 SER A OG  1 
ATOM 1122 N N   . ASN A 1 137 ? 49.060 78.006  140.997 1.00 59.82  ? 137 ASN A N   1 
ATOM 1123 C CA  . ASN A 1 137 ? 50.240 78.825  140.693 1.00 60.92  ? 137 ASN A CA  1 
ATOM 1124 C C   . ASN A 1 137 ? 51.055 79.237  141.910 1.00 61.13  ? 137 ASN A C   1 
ATOM 1125 O O   . ASN A 1 137 ? 52.267 79.397  141.764 1.00 61.97  ? 137 ASN A O   1 
ATOM 1126 C CB  . ASN A 1 137 ? 49.898 80.105  139.883 1.00 61.07  ? 137 ASN A CB  1 
ATOM 1127 C CG  . ASN A 1 137 ? 51.151 80.912  139.451 1.00 60.83  ? 137 ASN A CG  1 
ATOM 1128 O OD1 . ASN A 1 137 ? 52.286 80.463  139.610 1.00 61.28  ? 137 ASN A OD1 1 
ATOM 1129 N ND2 . ASN A 1 137 ? 50.929 82.101  138.893 1.00 60.14  ? 137 ASN A ND2 1 
ATOM 1130 N N   . PHE A 1 138 ? 50.468 79.432  143.098 1.00 60.51  ? 138 PHE A N   1 
ATOM 1131 C CA  . PHE A 1 138 ? 51.409 79.808  144.129 1.00 60.31  ? 138 PHE A CA  1 
ATOM 1132 C C   . PHE A 1 138 ? 51.934 78.805  145.071 1.00 59.94  ? 138 PHE A C   1 
ATOM 1133 O O   . PHE A 1 138 ? 51.228 78.229  145.898 1.00 59.03  ? 138 PHE A O   1 
ATOM 1134 C CB  . PHE A 1 138 ? 51.051 81.067  144.907 1.00 61.07  ? 138 PHE A CB  1 
ATOM 1135 C CG  . PHE A 1 138 ? 52.264 81.977  145.133 1.00 61.71  ? 138 PHE A CG  1 
ATOM 1136 C CD1 . PHE A 1 138 ? 53.338 81.936  144.238 1.00 61.38  ? 138 PHE A CD1 1 
ATOM 1137 C CD2 . PHE A 1 138 ? 52.327 82.892  146.193 1.00 62.48  ? 138 PHE A CD2 1 
ATOM 1138 C CE1 . PHE A 1 138 ? 54.444 82.800  144.368 1.00 60.23  ? 138 PHE A CE1 1 
ATOM 1139 C CE2 . PHE A 1 138 ? 53.436 83.764  146.323 1.00 60.95  ? 138 PHE A CE2 1 
ATOM 1140 C CZ  . PHE A 1 138 ? 54.493 83.709  145.418 1.00 60.20  ? 138 PHE A CZ  1 
ATOM 1141 N N   . GLU A 1 139 ? 53.240 78.641  144.893 1.00 60.89  ? 139 GLU A N   1 
ATOM 1142 C CA  . GLU A 1 139 ? 54.080 77.732  145.629 1.00 62.03  ? 139 GLU A CA  1 
ATOM 1143 C C   . GLU A 1 139 ? 53.778 77.670  147.111 1.00 63.32  ? 139 GLU A C   1 
ATOM 1144 O O   . GLU A 1 139 ? 53.480 78.672  147.776 1.00 62.57  ? 139 GLU A O   1 
ATOM 1145 C CB  . GLU A 1 139 ? 55.552 78.083  145.365 1.00 61.56  ? 139 GLU A CB  1 
ATOM 1146 C CG  . GLU A 1 139 ? 55.894 79.570  145.436 1.00 60.77  ? 139 GLU A CG  1 
ATOM 1147 C CD  . GLU A 1 139 ? 57.362 79.851  145.141 1.00 60.98  ? 139 GLU A CD  1 
ATOM 1148 O OE1 . GLU A 1 139 ? 57.886 79.309  144.137 1.00 60.92  ? 139 GLU A OE1 1 
ATOM 1149 O OE2 . GLU A 1 139 ? 57.989 80.620  145.910 1.00 60.29  ? 139 GLU A OE2 1 
ATOM 1150 N N   . PHE A 1 140 ? 53.839 76.457  147.628 1.00 64.75  ? 140 PHE A N   1 
ATOM 1151 C CA  . PHE A 1 140 ? 53.584 76.250  149.030 1.00 67.24  ? 140 PHE A CA  1 
ATOM 1152 C C   . PHE A 1 140 ? 54.639 77.076  149.742 1.00 69.00  ? 140 PHE A C   1 
ATOM 1153 O O   . PHE A 1 140 ? 54.501 77.402  150.923 1.00 70.01  ? 140 PHE A O   1 
ATOM 1154 C CB  . PHE A 1 140 ? 53.733 74.769  149.348 1.00 67.54  ? 140 PHE A CB  1 
ATOM 1155 C CG  . PHE A 1 140 ? 55.123 74.255  149.216 1.00 68.43  ? 140 PHE A CG  1 
ATOM 1156 C CD1 . PHE A 1 140 ? 55.620 73.872  147.972 1.00 69.69  ? 140 PHE A CD1 1 
ATOM 1157 C CD2 . PHE A 1 140 ? 55.936 74.141  150.337 1.00 68.69  ? 140 PHE A CD2 1 
ATOM 1158 C CE1 . PHE A 1 140 ? 56.922 73.379  147.845 1.00 71.23  ? 140 PHE A CE1 1 
ATOM 1159 C CE2 . PHE A 1 140 ? 57.232 73.653  150.234 1.00 69.89  ? 140 PHE A CE2 1 
ATOM 1160 C CZ  . PHE A 1 140 ? 57.731 73.270  148.986 1.00 71.10  ? 140 PHE A CZ  1 
ATOM 1161 N N   . GLY A 1 141 ? 55.685 77.426  148.992 1.00 70.78  ? 141 GLY A N   1 
ATOM 1162 C CA  . GLY A 1 141 ? 56.785 78.207  149.531 1.00 72.70  ? 141 GLY A CA  1 
ATOM 1163 C C   . GLY A 1 141 ? 56.316 79.355  150.398 1.00 73.68  ? 141 GLY A C   1 
ATOM 1164 O O   . GLY A 1 141 ? 56.830 79.573  151.497 1.00 73.94  ? 141 GLY A O   1 
ATOM 1165 N N   . ARG A 1 142 ? 55.326 80.091  149.914 1.00 74.09  ? 142 ARG A N   1 
ATOM 1166 C CA  . ARG A 1 142 ? 54.835 81.210  150.684 1.00 74.79  ? 142 ARG A CA  1 
ATOM 1167 C C   . ARG A 1 142 ? 53.664 80.756  151.522 1.00 74.49  ? 142 ARG A C   1 
ATOM 1168 O O   . ARG A 1 142 ? 53.277 81.428  152.465 1.00 74.15  ? 142 ARG A O   1 
ATOM 1169 C CB  . ARG A 1 142 ? 54.460 82.352  149.746 1.00 76.80  ? 142 ARG A CB  1 
ATOM 1170 C CG  . ARG A 1 142 ? 55.587 82.639  148.732 1.00 78.69  ? 142 ARG A CG  1 
ATOM 1171 C CD  . ARG A 1 142 ? 56.028 84.102  148.698 1.00 79.82  ? 142 ARG A CD  1 
ATOM 1172 N NE  . ARG A 1 142 ? 57.333 84.260  148.059 1.00 80.75  ? 142 ARG A NE  1 
ATOM 1173 C CZ  . ARG A 1 142 ? 57.799 85.409  147.575 1.00 81.57  ? 142 ARG A CZ  1 
ATOM 1174 N NH1 . ARG A 1 142 ? 57.062 86.516  147.651 1.00 82.26  ? 142 ARG A NH1 1 
ATOM 1175 N NH2 . ARG A 1 142 ? 59.005 85.454  147.010 1.00 81.98  ? 142 ARG A NH2 1 
ATOM 1176 N N   . ALA A 1 143 ? 53.113 79.599  151.182 1.00 74.79  ? 143 ALA A N   1 
ATOM 1177 C CA  . ALA A 1 143 ? 52.006 79.040  151.938 1.00 75.46  ? 143 ALA A CA  1 
ATOM 1178 C C   . ALA A 1 143 ? 52.502 78.657  153.319 1.00 75.57  ? 143 ALA A C   1 
ATOM 1179 O O   . ALA A 1 143 ? 51.868 78.961  154.319 1.00 75.29  ? 143 ALA A O   1 
ATOM 1180 C CB  . ALA A 1 143 ? 51.479 77.822  151.252 1.00 75.41  ? 143 ALA A CB  1 
ATOM 1181 N N   . ARG A 1 144 ? 53.640 77.976  153.363 1.00 76.33  ? 144 ARG A N   1 
ATOM 1182 C CA  . ARG A 1 144 ? 54.230 77.561  154.629 1.00 78.00  ? 144 ARG A CA  1 
ATOM 1183 C C   . ARG A 1 144 ? 54.568 78.807  155.435 1.00 77.61  ? 144 ARG A C   1 
ATOM 1184 O O   . ARG A 1 144 ? 54.239 78.905  156.623 1.00 77.85  ? 144 ARG A O   1 
ATOM 1185 C CB  . ARG A 1 144 ? 55.501 76.718  154.372 1.00 79.82  ? 144 ARG A CB  1 
ATOM 1186 C CG  . ARG A 1 144 ? 56.520 76.577  155.546 1.00 82.34  ? 144 ARG A CG  1 
ATOM 1187 C CD  . ARG A 1 144 ? 56.165 75.529  156.641 1.00 82.85  ? 144 ARG A CD  1 
ATOM 1188 N NE  . ARG A 1 144 ? 57.091 75.610  157.778 1.00 83.90  ? 144 ARG A NE  1 
ATOM 1189 C CZ  . ARG A 1 144 ? 56.926 74.971  158.932 1.00 84.35  ? 144 ARG A CZ  1 
ATOM 1190 N NH1 . ARG A 1 144 ? 55.866 74.198  159.089 1.00 85.23  ? 144 ARG A NH1 1 
ATOM 1191 N NH2 . ARG A 1 144 ? 57.798 75.118  159.934 1.00 84.72  ? 144 ARG A NH2 1 
ATOM 1192 N N   . MET A 1 145 ? 55.210 79.766  154.772 1.00 77.19  ? 145 MET A N   1 
ATOM 1193 C CA  . MET A 1 145 ? 55.601 80.999  155.432 1.00 75.60  ? 145 MET A CA  1 
ATOM 1194 C C   . MET A 1 145 ? 54.362 81.662  156.000 1.00 73.46  ? 145 MET A C   1 
ATOM 1195 O O   . MET A 1 145 ? 54.425 82.339  157.027 1.00 73.51  ? 145 MET A O   1 
ATOM 1196 C CB  . MET A 1 145 ? 56.333 81.921  154.452 1.00 76.41  ? 145 MET A CB  1 
ATOM 1197 C CG  . MET A 1 145 ? 57.591 81.278  153.854 1.00 77.95  ? 145 MET A CG  1 
ATOM 1198 S SD  . MET A 1 145 ? 58.633 82.454  152.935 1.00 79.67  ? 145 MET A SD  1 
ATOM 1199 C CE  . MET A 1 145 ? 60.264 82.189  153.796 1.00 77.77  ? 145 MET A CE  1 
ATOM 1200 N N   . PHE A 1 146 ? 53.223 81.450  155.355 1.00 70.28  ? 146 PHE A N   1 
ATOM 1201 C CA  . PHE A 1 146 ? 52.010 82.037  155.879 1.00 67.01  ? 146 PHE A CA  1 
ATOM 1202 C C   . PHE A 1 146 ? 51.492 81.143  156.973 1.00 63.71  ? 146 PHE A C   1 
ATOM 1203 O O   . PHE A 1 146 ? 51.026 81.597  158.012 1.00 63.04  ? 146 PHE A O   1 
ATOM 1204 C CB  . PHE A 1 146 ? 50.948 82.150  154.806 1.00 68.66  ? 146 PHE A CB  1 
ATOM 1205 C CG  . PHE A 1 146 ? 49.804 82.996  155.224 1.00 69.51  ? 146 PHE A CG  1 
ATOM 1206 C CD1 . PHE A 1 146 ? 49.958 84.385  155.334 1.00 70.10  ? 146 PHE A CD1 1 
ATOM 1207 C CD2 . PHE A 1 146 ? 48.609 82.414  155.607 1.00 69.34  ? 146 PHE A CD2 1 
ATOM 1208 C CE1 . PHE A 1 146 ? 48.945 85.179  155.823 1.00 70.38  ? 146 PHE A CE1 1 
ATOM 1209 C CE2 . PHE A 1 146 ? 47.584 83.193  156.098 1.00 70.38  ? 146 PHE A CE2 1 
ATOM 1210 C CZ  . PHE A 1 146 ? 47.753 84.589  156.211 1.00 70.89  ? 146 PHE A CZ  1 
ATOM 1211 N N   . GLY A 1 147 ? 51.567 79.855  156.704 1.00 60.78  ? 147 GLY A N   1 
ATOM 1212 C CA  . GLY A 1 147 ? 51.112 78.900  157.665 1.00 57.49  ? 147 GLY A CA  1 
ATOM 1213 C C   . GLY A 1 147 ? 51.892 78.957  158.937 1.00 55.15  ? 147 GLY A C   1 
ATOM 1214 O O   . GLY A 1 147 ? 51.311 78.775  159.968 1.00 54.87  ? 147 GLY A O   1 
ATOM 1215 N N   . CYS A 1 148 ? 53.185 79.230  158.901 1.00 53.44  ? 148 CYS A N   1 
ATOM 1216 C CA  . CYS A 1 148 ? 53.941 79.233  160.152 1.00 51.72  ? 148 CYS A CA  1 
ATOM 1217 C C   . CYS A 1 148 ? 53.548 80.279  161.208 1.00 50.41  ? 148 CYS A C   1 
ATOM 1218 O O   . CYS A 1 148 ? 53.901 80.159  162.385 1.00 49.77  ? 148 CYS A O   1 
ATOM 1219 C CB  . CYS A 1 148 ? 55.435 79.356  159.877 1.00 51.92  ? 148 CYS A CB  1 
ATOM 1220 S SG  . CYS A 1 148 ? 56.360 79.348  161.424 1.00 53.97  ? 148 CYS A SG  1 
ATOM 1221 N N   . VAL A 1 149 ? 52.823 81.307  160.797 1.00 48.65  ? 149 VAL A N   1 
ATOM 1222 C CA  . VAL A 1 149 ? 52.401 82.347  161.727 1.00 47.03  ? 149 VAL A CA  1 
ATOM 1223 C C   . VAL A 1 149 ? 51.649 81.717  162.874 1.00 46.26  ? 149 VAL A C   1 
ATOM 1224 O O   . VAL A 1 149 ? 52.003 81.868  164.039 1.00 45.88  ? 149 VAL A O   1 
ATOM 1225 C CB  . VAL A 1 149 ? 51.483 83.325  161.025 1.00 47.00  ? 149 VAL A CB  1 
ATOM 1226 C CG1 . VAL A 1 149 ? 50.853 84.273  162.013 1.00 47.31  ? 149 VAL A CG1 1 
ATOM 1227 C CG2 . VAL A 1 149 ? 52.272 84.063  160.001 1.00 47.61  ? 149 VAL A CG2 1 
ATOM 1228 N N   . GLY A 1 150 ? 50.597 81.001  162.504 1.00 45.81  ? 150 GLY A N   1 
ATOM 1229 C CA  . GLY A 1 150 ? 49.750 80.309  163.457 1.00 46.26  ? 150 GLY A CA  1 
ATOM 1230 C C   . GLY A 1 150 ? 50.521 79.632  164.560 1.00 46.77  ? 150 GLY A C   1 
ATOM 1231 O O   . GLY A 1 150 ? 50.170 79.743  165.731 1.00 46.95  ? 150 GLY A O   1 
ATOM 1232 N N   . TRP A 1 151 ? 51.567 78.917  164.171 1.00 47.30  ? 151 TRP A N   1 
ATOM 1233 C CA  . TRP A 1 151 ? 52.448 78.219  165.099 1.00 48.45  ? 151 TRP A CA  1 
ATOM 1234 C C   . TRP A 1 151 ? 52.933 79.280  166.056 1.00 48.61  ? 151 TRP A C   1 
ATOM 1235 O O   . TRP A 1 151 ? 52.757 79.191  167.264 1.00 49.29  ? 151 TRP A O   1 
ATOM 1236 C CB  . TRP A 1 151 ? 53.625 77.638  164.302 1.00 49.89  ? 151 TRP A CB  1 
ATOM 1237 C CG  . TRP A 1 151 ? 54.791 77.052  165.082 1.00 52.50  ? 151 TRP A CG  1 
ATOM 1238 C CD1 . TRP A 1 151 ? 56.035 77.580  165.201 1.00 52.72  ? 151 TRP A CD1 1 
ATOM 1239 C CD2 . TRP A 1 151 ? 54.803 75.819  165.814 1.00 53.84  ? 151 TRP A CD2 1 
ATOM 1240 N NE1 . TRP A 1 151 ? 56.830 76.757  165.960 1.00 53.95  ? 151 TRP A NE1 1 
ATOM 1241 C CE2 . TRP A 1 151 ? 56.106 75.679  166.349 1.00 54.61  ? 151 TRP A CE2 1 
ATOM 1242 C CE3 . TRP A 1 151 ? 53.849 74.833  166.061 1.00 54.02  ? 151 TRP A CE3 1 
ATOM 1243 C CZ2 . TRP A 1 151 ? 56.465 74.566  167.134 1.00 55.34  ? 151 TRP A CZ2 1 
ATOM 1244 C CZ3 . TRP A 1 151 ? 54.211 73.734  166.835 1.00 54.95  ? 151 TRP A CZ3 1 
ATOM 1245 C CH2 . TRP A 1 151 ? 55.511 73.612  167.362 1.00 55.62  ? 151 TRP A CH2 1 
ATOM 1246 N N   . ALA A 1 152 ? 53.517 80.325  165.501 1.00 48.41  ? 152 ALA A N   1 
ATOM 1247 C CA  . ALA A 1 152 ? 54.044 81.372  166.353 1.00 47.67  ? 152 ALA A CA  1 
ATOM 1248 C C   . ALA A 1 152 ? 53.000 81.941  167.316 1.00 46.85  ? 152 ALA A C   1 
ATOM 1249 O O   . ALA A 1 152 ? 53.176 81.936  168.523 1.00 45.40  ? 152 ALA A O   1 
ATOM 1250 C CB  . ALA A 1 152 ? 54.647 82.467  165.484 1.00 48.99  ? 152 ALA A CB  1 
ATOM 1251 N N   . LEU A 1 153 ? 51.897 82.403  166.761 1.00 46.73  ? 153 LEU A N   1 
ATOM 1252 C CA  . LEU A 1 153 ? 50.838 82.995  167.546 1.00 46.42  ? 153 LEU A CA  1 
ATOM 1253 C C   . LEU A 1 153 ? 50.302 82.099  168.673 1.00 45.90  ? 153 LEU A C   1 
ATOM 1254 O O   . LEU A 1 153 ? 50.355 82.467  169.842 1.00 46.56  ? 153 LEU A O   1 
ATOM 1255 C CB  . LEU A 1 153 ? 49.716 83.416  166.594 1.00 46.71  ? 153 LEU A CB  1 
ATOM 1256 C CG  . LEU A 1 153 ? 48.719 84.455  167.103 1.00 46.44  ? 153 LEU A CG  1 
ATOM 1257 C CD1 . LEU A 1 153 ? 49.479 85.706  167.477 1.00 46.64  ? 153 LEU A CD1 1 
ATOM 1258 C CD2 . LEU A 1 153 ? 47.682 84.768  166.044 1.00 45.92  ? 153 LEU A CD2 1 
ATOM 1259 N N   . GLY A 1 154 ? 49.801 80.925  168.316 1.00 45.37  ? 154 GLY A N   1 
ATOM 1260 C CA  . GLY A 1 154 ? 49.254 80.015  169.304 1.00 46.21  ? 154 GLY A CA  1 
ATOM 1261 C C   . GLY A 1 154 ? 50.136 79.826  170.523 1.00 46.20  ? 154 GLY A C   1 
ATOM 1262 O O   . GLY A 1 154 ? 49.757 80.148  171.661 1.00 46.34  ? 154 GLY A O   1 
ATOM 1263 N N   . ALA A 1 155 ? 51.319 79.281  170.280 1.00 45.66  ? 155 ALA A N   1 
ATOM 1264 C CA  . ALA A 1 155 ? 52.271 79.059  171.341 1.00 45.65  ? 155 ALA A CA  1 
ATOM 1265 C C   . ALA A 1 155 ? 52.083 80.181  172.357 1.00 46.37  ? 155 ALA A C   1 
ATOM 1266 O O   . ALA A 1 155 ? 51.583 79.962  173.457 1.00 46.14  ? 155 ALA A O   1 
ATOM 1267 C CB  . ALA A 1 155 ? 53.672 79.086  170.780 1.00 44.85  ? 155 ALA A CB  1 
ATOM 1268 N N   . SER A 1 156 ? 52.438 81.398  171.970 1.00 47.80  ? 156 SER A N   1 
ATOM 1269 C CA  . SER A 1 156 ? 52.322 82.513  172.892 1.00 49.10  ? 156 SER A CA  1 
ATOM 1270 C C   . SER A 1 156 ? 50.988 82.501  173.626 1.00 49.81  ? 156 SER A C   1 
ATOM 1271 O O   . SER A 1 156 ? 50.931 82.612  174.848 1.00 49.70  ? 156 SER A O   1 
ATOM 1272 C CB  . SER A 1 156 ? 52.531 83.842  172.160 1.00 49.46  ? 156 SER A CB  1 
ATOM 1273 O OG  . SER A 1 156 ? 53.870 83.948  171.693 1.00 50.37  ? 156 SER A OG  1 
ATOM 1274 N N   . ILE A 1 157 ? 49.904 82.338  172.901 1.00 50.10  ? 157 ILE A N   1 
ATOM 1275 C CA  . ILE A 1 157 ? 48.642 82.336  173.579 1.00 50.85  ? 157 ILE A CA  1 
ATOM 1276 C C   . ILE A 1 157 ? 48.503 81.154  174.508 1.00 51.03  ? 157 ILE A C   1 
ATOM 1277 O O   . ILE A 1 157 ? 47.904 81.263  175.566 1.00 51.63  ? 157 ILE A O   1 
ATOM 1278 C CB  . ILE A 1 157 ? 47.524 82.368  172.585 1.00 51.11  ? 157 ILE A CB  1 
ATOM 1279 C CG1 . ILE A 1 157 ? 47.573 83.722  171.871 1.00 52.28  ? 157 ILE A CG1 1 
ATOM 1280 C CG2 . ILE A 1 157 ? 46.203 82.101  173.275 1.00 51.29  ? 157 ILE A CG2 1 
ATOM 1281 C CD1 . ILE A 1 157 ? 46.354 84.049  171.040 1.00 53.06  ? 157 ILE A CD1 1 
ATOM 1282 N N   . VAL A 1 158 ? 49.079 80.027  174.126 1.00 51.53  ? 158 VAL A N   1 
ATOM 1283 C CA  . VAL A 1 158 ? 49.007 78.834  174.957 1.00 52.49  ? 158 VAL A CA  1 
ATOM 1284 C C   . VAL A 1 158 ? 49.484 79.114  176.362 1.00 52.31  ? 158 VAL A C   1 
ATOM 1285 O O   . VAL A 1 158 ? 48.704 79.102  177.305 1.00 52.09  ? 158 VAL A O   1 
ATOM 1286 C CB  . VAL A 1 158 ? 49.850 77.670  174.369 1.00 53.50  ? 158 VAL A CB  1 
ATOM 1287 C CG1 . VAL A 1 158 ? 50.088 76.561  175.435 1.00 53.59  ? 158 VAL A CG1 1 
ATOM 1288 C CG2 . VAL A 1 158 ? 49.113 77.087  173.175 1.00 54.95  ? 158 VAL A CG2 1 
ATOM 1289 N N   . GLY A 1 159 ? 50.780 79.347  176.496 1.00 52.60  ? 159 GLY A N   1 
ATOM 1290 C CA  . GLY A 1 159 ? 51.339 79.622  177.805 1.00 53.02  ? 159 GLY A CA  1 
ATOM 1291 C C   . GLY A 1 159 ? 50.409 80.440  178.677 1.00 52.73  ? 159 GLY A C   1 
ATOM 1292 O O   . GLY A 1 159 ? 49.923 79.969  179.708 1.00 53.17  ? 159 GLY A O   1 
ATOM 1293 N N   . ILE A 1 160 ? 50.165 81.675  178.262 1.00 52.17  ? 160 ILE A N   1 
ATOM 1294 C CA  . ILE A 1 160 ? 49.287 82.557  178.998 1.00 51.53  ? 160 ILE A CA  1 
ATOM 1295 C C   . ILE A 1 160 ? 48.022 81.769  179.296 1.00 51.63  ? 160 ILE A C   1 
ATOM 1296 O O   . ILE A 1 160 ? 47.852 81.212  180.390 1.00 51.24  ? 160 ILE A O   1 
ATOM 1297 C CB  . ILE A 1 160 ? 48.990 83.822  178.140 1.00 51.47  ? 160 ILE A CB  1 
ATOM 1298 C CG1 . ILE A 1 160 ? 50.309 84.580  177.931 1.00 51.31  ? 160 ILE A CG1 1 
ATOM 1299 C CG2 . ILE A 1 160 ? 47.921 84.713  178.798 1.00 52.56  ? 160 ILE A CG2 1 
ATOM 1300 C CD1 . ILE A 1 160 ? 50.204 85.867  177.135 1.00 51.53  ? 160 ILE A CD1 1 
ATOM 1301 N N   . MET A 1 161 ? 47.167 81.682  178.289 1.00 51.85  ? 161 MET A N   1 
ATOM 1302 C CA  . MET A 1 161 ? 45.907 80.978  178.410 1.00 52.43  ? 161 MET A CA  1 
ATOM 1303 C C   . MET A 1 161 ? 46.006 79.592  179.042 1.00 52.35  ? 161 MET A C   1 
ATOM 1304 O O   . MET A 1 161 ? 45.102 79.154  179.749 1.00 52.34  ? 161 MET A O   1 
ATOM 1305 C CB  . MET A 1 161 ? 45.251 80.871  177.031 1.00 52.63  ? 161 MET A CB  1 
ATOM 1306 C CG  . MET A 1 161 ? 45.014 82.212  176.337 1.00 53.70  ? 161 MET A CG  1 
ATOM 1307 S SD  . MET A 1 161 ? 43.525 83.146  176.862 1.00 55.08  ? 161 MET A SD  1 
ATOM 1308 C CE  . MET A 1 161 ? 44.204 84.246  178.206 1.00 54.81  ? 161 MET A CE  1 
ATOM 1309 N N   . PHE A 1 162 ? 47.089 78.879  178.812 1.00 52.44  ? 162 PHE A N   1 
ATOM 1310 C CA  . PHE A 1 162 ? 47.121 77.566  179.397 1.00 53.20  ? 162 PHE A CA  1 
ATOM 1311 C C   . PHE A 1 162 ? 46.958 77.565  180.886 1.00 54.21  ? 162 PHE A C   1 
ATOM 1312 O O   . PHE A 1 162 ? 45.981 77.048  181.405 1.00 54.21  ? 162 PHE A O   1 
ATOM 1313 C CB  . PHE A 1 162 ? 48.402 76.827  179.107 1.00 53.39  ? 162 PHE A CB  1 
ATOM 1314 C CG  . PHE A 1 162 ? 48.537 75.563  179.909 1.00 53.71  ? 162 PHE A CG  1 
ATOM 1315 C CD1 . PHE A 1 162 ? 47.749 74.461  179.627 1.00 53.51  ? 162 PHE A CD1 1 
ATOM 1316 C CD2 . PHE A 1 162 ? 49.440 75.479  180.955 1.00 54.81  ? 162 PHE A CD2 1 
ATOM 1317 C CE1 . PHE A 1 162 ? 47.864 73.298  180.360 1.00 53.50  ? 162 PHE A CE1 1 
ATOM 1318 C CE2 . PHE A 1 162 ? 49.562 74.314  181.700 1.00 54.71  ? 162 PHE A CE2 1 
ATOM 1319 C CZ  . PHE A 1 162 ? 48.773 73.225  181.400 1.00 54.24  ? 162 PHE A CZ  1 
ATOM 1320 N N   . THR A 1 163 ? 47.945 78.133  181.565 1.00 55.66  ? 163 THR A N   1 
ATOM 1321 C CA  . THR A 1 163 ? 47.970 78.150  183.015 1.00 57.01  ? 163 THR A CA  1 
ATOM 1322 C C   . THR A 1 163 ? 46.744 78.760  183.632 1.00 57.69  ? 163 THR A C   1 
ATOM 1323 O O   . THR A 1 163 ? 46.393 78.459  184.769 1.00 57.92  ? 163 THR A O   1 
ATOM 1324 C CB  . THR A 1 163 ? 49.173 78.923  183.570 1.00 57.37  ? 163 THR A CB  1 
ATOM 1325 O OG1 . THR A 1 163 ? 50.278 78.820  182.666 1.00 58.08  ? 163 THR A OG1 1 
ATOM 1326 C CG2 . THR A 1 163 ? 49.564 78.346  184.955 1.00 57.90  ? 163 THR A CG2 1 
ATOM 1327 N N   . ILE A 1 164 ? 46.077 79.617  182.884 1.00 57.96  ? 164 ILE A N   1 
ATOM 1328 C CA  . ILE A 1 164 ? 44.902 80.261  183.427 1.00 58.84  ? 164 ILE A CA  1 
ATOM 1329 C C   . ILE A 1 164 ? 43.699 79.342  183.502 1.00 59.50  ? 164 ILE A C   1 
ATOM 1330 O O   . ILE A 1 164 ? 42.827 79.502  184.355 1.00 60.21  ? 164 ILE A O   1 
ATOM 1331 C CB  . ILE A 1 164 ? 44.553 81.487  182.618 1.00 59.08  ? 164 ILE A CB  1 
ATOM 1332 C CG1 . ILE A 1 164 ? 45.696 82.493  182.718 1.00 59.32  ? 164 ILE A CG1 1 
ATOM 1333 C CG2 . ILE A 1 164 ? 43.261 82.073  183.123 1.00 59.90  ? 164 ILE A CG2 1 
ATOM 1334 C CD1 . ILE A 1 164 ? 45.434 83.781  181.987 1.00 59.27  ? 164 ILE A CD1 1 
ATOM 1335 N N   . ASN A 1 165 ? 43.664 78.387  182.586 1.00 59.69  ? 165 ASN A N   1 
ATOM 1336 C CA  . ASN A 1 165 ? 42.598 77.400  182.506 1.00 59.64  ? 165 ASN A CA  1 
ATOM 1337 C C   . ASN A 1 165 ? 42.865 76.468  181.318 1.00 59.80  ? 165 ASN A C   1 
ATOM 1338 O O   . ASN A 1 165 ? 42.333 76.670  180.227 1.00 59.70  ? 165 ASN A O   1 
ATOM 1339 C CB  . ASN A 1 165 ? 41.238 78.078  182.334 1.00 59.20  ? 165 ASN A CB  1 
ATOM 1340 C CG  . ASN A 1 165 ? 40.121 77.072  182.177 1.00 59.24  ? 165 ASN A CG  1 
ATOM 1341 O OD1 . ASN A 1 165 ? 40.356 75.864  182.157 1.00 59.09  ? 165 ASN A OD1 1 
ATOM 1342 N ND2 . ASN A 1 165 ? 38.903 77.558  182.067 1.00 59.84  ? 165 ASN A ND2 1 
ATOM 1343 N N   . ASN A 1 166 ? 43.697 75.452  181.542 1.00 59.79  ? 166 ASN A N   1 
ATOM 1344 C CA  . ASN A 1 166 ? 44.040 74.495  180.496 1.00 59.59  ? 166 ASN A CA  1 
ATOM 1345 C C   . ASN A 1 166 ? 42.775 73.986  179.753 1.00 59.81  ? 166 ASN A C   1 
ATOM 1346 O O   . ASN A 1 166 ? 42.735 73.979  178.523 1.00 60.18  ? 166 ASN A O   1 
ATOM 1347 C CB  . ASN A 1 166 ? 44.812 73.326  181.101 1.00 58.77  ? 166 ASN A CB  1 
ATOM 1348 C CG  . ASN A 1 166 ? 43.915 72.379  181.806 1.00 58.12  ? 166 ASN A CG  1 
ATOM 1349 O OD1 . ASN A 1 166 ? 42.800 72.735  182.165 1.00 57.90  ? 166 ASN A OD1 1 
ATOM 1350 N ND2 . ASN A 1 166 ? 44.375 71.165  182.015 1.00 58.19  ? 166 ASN A ND2 1 
ATOM 1351 N N   . GLN A 1 167 ? 41.744 73.579  180.491 1.00 59.93  ? 167 GLN A N   1 
ATOM 1352 C CA  . GLN A 1 167 ? 40.501 73.097  179.889 1.00 59.68  ? 167 GLN A CA  1 
ATOM 1353 C C   . GLN A 1 167 ? 40.068 74.062  178.765 1.00 58.96  ? 167 GLN A C   1 
ATOM 1354 O O   . GLN A 1 167 ? 39.460 73.664  177.751 1.00 58.72  ? 167 GLN A O   1 
ATOM 1355 C CB  . GLN A 1 167 ? 39.406 73.002  180.972 1.00 61.19  ? 167 GLN A CB  1 
ATOM 1356 C CG  . GLN A 1 167 ? 38.018 72.515  180.492 1.00 63.64  ? 167 GLN A CG  1 
ATOM 1357 C CD  . GLN A 1 167 ? 37.021 72.292  181.638 1.00 64.57  ? 167 GLN A CD  1 
ATOM 1358 O OE1 . GLN A 1 167 ? 37.121 72.914  182.708 1.00 65.42  ? 167 GLN A OE1 1 
ATOM 1359 N NE2 . GLN A 1 167 ? 36.041 71.410  181.407 1.00 65.05  ? 167 GLN A NE2 1 
ATOM 1360 N N   . PHE A 1 168 ? 40.401 75.336  178.949 1.00 57.39  ? 168 PHE A N   1 
ATOM 1361 C CA  . PHE A 1 168 ? 40.055 76.376  177.988 1.00 56.23  ? 168 PHE A CA  1 
ATOM 1362 C C   . PHE A 1 168 ? 40.771 76.231  176.642 1.00 55.70  ? 168 PHE A C   1 
ATOM 1363 O O   . PHE A 1 168 ? 40.128 75.994  175.625 1.00 56.34  ? 168 PHE A O   1 
ATOM 1364 C CB  . PHE A 1 168 ? 40.349 77.752  178.610 1.00 55.63  ? 168 PHE A CB  1 
ATOM 1365 C CG  . PHE A 1 168 ? 40.541 78.872  177.599 1.00 55.32  ? 168 PHE A CG  1 
ATOM 1366 C CD1 . PHE A 1 168 ? 39.447 79.505  176.992 1.00 55.21  ? 168 PHE A CD1 1 
ATOM 1367 C CD2 . PHE A 1 168 ? 41.827 79.326  177.294 1.00 54.75  ? 168 PHE A CD2 1 
ATOM 1368 C CE1 . PHE A 1 168 ? 39.644 80.577  176.106 1.00 54.87  ? 168 PHE A CE1 1 
ATOM 1369 C CE2 . PHE A 1 168 ? 42.030 80.394  176.410 1.00 54.00  ? 168 PHE A CE2 1 
ATOM 1370 C CZ  . PHE A 1 168 ? 40.945 81.020  175.820 1.00 54.35  ? 168 PHE A CZ  1 
ATOM 1371 N N   . VAL A 1 169 ? 42.095 76.381  176.649 1.00 54.58  ? 169 VAL A N   1 
ATOM 1372 C CA  . VAL A 1 169 ? 42.918 76.289  175.442 1.00 53.55  ? 169 VAL A CA  1 
ATOM 1373 C C   . VAL A 1 169 ? 42.431 75.243  174.460 1.00 52.87  ? 169 VAL A C   1 
ATOM 1374 O O   . VAL A 1 169 ? 42.269 75.495  173.269 1.00 52.12  ? 169 VAL A O   1 
ATOM 1375 C CB  . VAL A 1 169 ? 44.378 75.938  175.776 1.00 52.88  ? 169 VAL A CB  1 
ATOM 1376 C CG1 . VAL A 1 169 ? 45.194 75.900  174.499 1.00 52.52  ? 169 VAL A CG1 1 
ATOM 1377 C CG2 . VAL A 1 169 ? 44.948 76.945  176.758 1.00 52.68  ? 169 VAL A CG2 1 
ATOM 1378 N N   . PHE A 1 170 ? 42.232 74.046  174.971 1.00 53.20  ? 170 PHE A N   1 
ATOM 1379 C CA  . PHE A 1 170 ? 41.754 72.979  174.136 1.00 54.79  ? 170 PHE A CA  1 
ATOM 1380 C C   . PHE A 1 170 ? 40.558 73.482  173.406 1.00 56.06  ? 170 PHE A C   1 
ATOM 1381 O O   . PHE A 1 170 ? 40.493 73.441  172.180 1.00 55.68  ? 170 PHE A O   1 
ATOM 1382 C CB  . PHE A 1 170 ? 41.372 71.794  174.992 1.00 54.78  ? 170 PHE A CB  1 
ATOM 1383 C CG  . PHE A 1 170 ? 42.516 70.879  175.283 1.00 55.13  ? 170 PHE A CG  1 
ATOM 1384 C CD1 . PHE A 1 170 ? 43.692 70.965  174.548 1.00 55.11  ? 170 PHE A CD1 1 
ATOM 1385 C CD2 . PHE A 1 170 ? 42.397 69.879  176.246 1.00 55.73  ? 170 PHE A CD2 1 
ATOM 1386 C CE1 . PHE A 1 170 ? 44.718 70.064  174.761 1.00 54.31  ? 170 PHE A CE1 1 
ATOM 1387 C CE2 . PHE A 1 170 ? 43.424 68.966  176.471 1.00 54.66  ? 170 PHE A CE2 1 
ATOM 1388 C CZ  . PHE A 1 170 ? 44.577 69.056  175.731 1.00 54.14  ? 170 PHE A CZ  1 
ATOM 1389 N N   . TRP A 1 171 ? 39.603 73.962  174.185 1.00 58.35  ? 171 TRP A N   1 
ATOM 1390 C CA  . TRP A 1 171 ? 38.386 74.514  173.626 1.00 60.64  ? 171 TRP A CA  1 
ATOM 1391 C C   . TRP A 1 171 ? 38.700 75.387  172.400 1.00 61.29  ? 171 TRP A C   1 
ATOM 1392 O O   . TRP A 1 171 ? 38.225 75.083  171.308 1.00 61.48  ? 171 TRP A O   1 
ATOM 1393 C CB  . TRP A 1 171 ? 37.655 75.345  174.687 1.00 61.76  ? 171 TRP A CB  1 
ATOM 1394 C CG  . TRP A 1 171 ? 36.530 74.660  175.386 1.00 62.14  ? 171 TRP A CG  1 
ATOM 1395 C CD1 . TRP A 1 171 ? 36.012 74.986  176.604 1.00 62.67  ? 171 TRP A CD1 1 
ATOM 1396 C CD2 . TRP A 1 171 ? 35.744 73.575  174.893 1.00 62.02  ? 171 TRP A CD2 1 
ATOM 1397 N NE1 . TRP A 1 171 ? 34.951 74.170  176.902 1.00 62.91  ? 171 TRP A NE1 1 
ATOM 1398 C CE2 . TRP A 1 171 ? 34.764 73.294  175.867 1.00 62.48  ? 171 TRP A CE2 1 
ATOM 1399 C CE3 . TRP A 1 171 ? 35.770 72.814  173.723 1.00 61.50  ? 171 TRP A CE3 1 
ATOM 1400 C CZ2 . TRP A 1 171 ? 33.818 72.279  175.706 1.00 62.35  ? 171 TRP A CZ2 1 
ATOM 1401 C CZ3 . TRP A 1 171 ? 34.832 71.807  173.565 1.00 61.87  ? 171 TRP A CZ3 1 
ATOM 1402 C CH2 . TRP A 1 171 ? 33.868 71.548  174.551 1.00 61.89  ? 171 TRP A CH2 1 
ATOM 1403 N N   . LEU A 1 172 ? 39.498 76.450  172.558 1.00 61.97  ? 172 LEU A N   1 
ATOM 1404 C CA  . LEU A 1 172 ? 39.789 77.323  171.412 1.00 61.90  ? 172 LEU A CA  1 
ATOM 1405 C C   . LEU A 1 172 ? 40.645 76.651  170.361 1.00 61.41  ? 172 LEU A C   1 
ATOM 1406 O O   . LEU A 1 172 ? 40.427 76.813  169.156 1.00 61.14  ? 172 LEU A O   1 
ATOM 1407 C CB  . LEU A 1 172 ? 40.459 78.641  171.845 1.00 63.23  ? 172 LEU A CB  1 
ATOM 1408 C CG  . LEU A 1 172 ? 39.552 79.784  172.367 1.00 64.64  ? 172 LEU A CG  1 
ATOM 1409 C CD1 . LEU A 1 172 ? 40.405 81.026  172.579 1.00 64.83  ? 172 LEU A CD1 1 
ATOM 1410 C CD2 . LEU A 1 172 ? 38.406 80.088  171.379 1.00 64.34  ? 172 LEU A CD2 1 
ATOM 1411 N N   . GLY A 1 173 ? 41.632 75.892  170.807 1.00 60.45  ? 173 GLY A N   1 
ATOM 1412 C CA  . GLY A 1 173 ? 42.459 75.213  169.836 1.00 59.83  ? 173 GLY A CA  1 
ATOM 1413 C C   . GLY A 1 173 ? 41.549 74.426  168.919 1.00 58.59  ? 173 GLY A C   1 
ATOM 1414 O O   . GLY A 1 173 ? 41.454 74.703  167.727 1.00 57.21  ? 173 GLY A O   1 
ATOM 1415 N N   . SER A 1 174 ? 40.859 73.458  169.512 1.00 58.61  ? 174 SER A N   1 
ATOM 1416 C CA  . SER A 1 174 ? 39.940 72.568  168.811 1.00 58.59  ? 174 SER A CA  1 
ATOM 1417 C C   . SER A 1 174 ? 38.851 73.328  168.085 1.00 58.47  ? 174 SER A C   1 
ATOM 1418 O O   . SER A 1 174 ? 38.475 72.999  166.957 1.00 58.13  ? 174 SER A O   1 
ATOM 1419 C CB  . SER A 1 174 ? 39.295 71.610  169.820 1.00 57.96  ? 174 SER A CB  1 
ATOM 1420 O OG  . SER A 1 174 ? 38.270 70.828  169.230 1.00 57.44  ? 174 SER A OG  1 
ATOM 1421 N N   . GLY A 1 175 ? 38.346 74.354  168.751 1.00 59.26  ? 175 GLY A N   1 
ATOM 1422 C CA  . GLY A 1 175 ? 37.281 75.135  168.167 1.00 60.12  ? 175 GLY A CA  1 
ATOM 1423 C C   . GLY A 1 175 ? 37.652 75.843  166.887 1.00 60.52  ? 175 GLY A C   1 
ATOM 1424 O O   . GLY A 1 175 ? 37.220 75.452  165.795 1.00 60.65  ? 175 GLY A O   1 
ATOM 1425 N N   . CYS A 1 176 ? 38.448 76.896  167.008 1.00 61.08  ? 176 CYS A N   1 
ATOM 1426 C CA  . CYS A 1 176 ? 38.822 77.632  165.816 1.00 61.26  ? 176 CYS A CA  1 
ATOM 1427 C C   . CYS A 1 176 ? 39.261 76.596  164.793 1.00 61.14  ? 176 CYS A C   1 
ATOM 1428 O O   . CYS A 1 176 ? 38.999 76.733  163.597 1.00 61.66  ? 176 CYS A O   1 
ATOM 1429 C CB  . CYS A 1 176 ? 39.941 78.633  166.123 1.00 61.59  ? 176 CYS A CB  1 
ATOM 1430 S SG  . CYS A 1 176 ? 41.357 77.896  166.877 1.00 61.78  ? 176 CYS A SG  1 
ATOM 1431 N N   . ALA A 1 177 ? 39.882 75.534  165.294 1.00 60.95  ? 177 ALA A N   1 
ATOM 1432 C CA  . ALA A 1 177 ? 40.365 74.445  164.467 1.00 60.56  ? 177 ALA A CA  1 
ATOM 1433 C C   . ALA A 1 177 ? 39.254 73.829  163.623 1.00 60.40  ? 177 ALA A C   1 
ATOM 1434 O O   . ALA A 1 177 ? 39.347 73.770  162.403 1.00 60.12  ? 177 ALA A O   1 
ATOM 1435 C CB  . ALA A 1 177 ? 40.984 73.394  165.348 1.00 60.20  ? 177 ALA A CB  1 
ATOM 1436 N N   . LEU A 1 178 ? 38.205 73.369  164.285 1.00 59.83  ? 178 LEU A N   1 
ATOM 1437 C CA  . LEU A 1 178 ? 37.096 72.763  163.589 1.00 59.23  ? 178 LEU A CA  1 
ATOM 1438 C C   . LEU A 1 178 ? 36.384 73.777  162.737 1.00 58.26  ? 178 LEU A C   1 
ATOM 1439 O O   . LEU A 1 178 ? 36.345 73.657  161.519 1.00 57.44  ? 178 LEU A O   1 
ATOM 1440 C CB  . LEU A 1 178 ? 36.088 72.192  164.572 1.00 60.62  ? 178 LEU A CB  1 
ATOM 1441 C CG  . LEU A 1 178 ? 34.662 72.102  163.988 1.00 61.97  ? 178 LEU A CG  1 
ATOM 1442 C CD1 . LEU A 1 178 ? 34.579 70.984  162.968 1.00 62.80  ? 178 LEU A CD1 1 
ATOM 1443 C CD2 . LEU A 1 178 ? 33.647 71.859  165.088 1.00 62.30  ? 178 LEU A CD2 1 
ATOM 1444 N N   . ILE A 1 179 ? 35.793 74.763  163.394 1.00 57.88  ? 179 ILE A N   1 
ATOM 1445 C CA  . ILE A 1 179 ? 35.060 75.788  162.682 1.00 58.56  ? 179 ILE A CA  1 
ATOM 1446 C C   . ILE A 1 179 ? 35.793 76.181  161.379 1.00 58.21  ? 179 ILE A C   1 
ATOM 1447 O O   . ILE A 1 179 ? 35.308 75.881  160.273 1.00 59.23  ? 179 ILE A O   1 
ATOM 1448 C CB  . ILE A 1 179 ? 34.824 77.040  163.599 1.00 59.26  ? 179 ILE A CB  1 
ATOM 1449 C CG1 . ILE A 1 179 ? 34.062 76.603  164.856 1.00 59.10  ? 179 ILE A CG1 1 
ATOM 1450 C CG2 . ILE A 1 179 ? 34.024 78.140  162.851 1.00 59.74  ? 179 ILE A CG2 1 
ATOM 1451 C CD1 . ILE A 1 179 ? 33.794 77.737  165.854 1.00 58.43  ? 179 ILE A CD1 1 
ATOM 1452 N N   . LEU A 1 180 ? 36.962 76.812  161.495 1.00 57.18  ? 180 LEU A N   1 
ATOM 1453 C CA  . LEU A 1 180 ? 37.702 77.231  160.313 1.00 55.64  ? 180 LEU A CA  1 
ATOM 1454 C C   . LEU A 1 180 ? 38.164 76.058  159.425 1.00 55.10  ? 180 LEU A C   1 
ATOM 1455 O O   . LEU A 1 180 ? 38.330 76.220  158.224 1.00 55.26  ? 180 LEU A O   1 
ATOM 1456 C CB  . LEU A 1 180 ? 38.866 78.133  160.739 1.00 54.67  ? 180 LEU A CB  1 
ATOM 1457 C CG  . LEU A 1 180 ? 38.444 79.374  161.545 1.00 54.17  ? 180 LEU A CG  1 
ATOM 1458 C CD1 . LEU A 1 180 ? 39.640 80.262  161.719 1.00 53.85  ? 180 LEU A CD1 1 
ATOM 1459 C CD2 . LEU A 1 180 ? 37.346 80.153  160.844 1.00 54.15  ? 180 LEU A CD2 1 
ATOM 1460 N N   . ALA A 1 181 ? 38.349 74.877  160.006 1.00 54.30  ? 181 ALA A N   1 
ATOM 1461 C CA  . ALA A 1 181 ? 38.745 73.719  159.220 1.00 53.59  ? 181 ALA A CA  1 
ATOM 1462 C C   . ALA A 1 181 ? 37.629 73.449  158.230 1.00 53.94  ? 181 ALA A C   1 
ATOM 1463 O O   . ALA A 1 181 ? 37.830 73.591  157.030 1.00 53.09  ? 181 ALA A O   1 
ATOM 1464 C CB  . ALA A 1 181 ? 38.933 72.526  160.103 1.00 53.57  ? 181 ALA A CB  1 
ATOM 1465 N N   . VAL A 1 182 ? 36.451 73.074  158.732 1.00 54.75  ? 182 VAL A N   1 
ATOM 1466 C CA  . VAL A 1 182 ? 35.302 72.797  157.858 1.00 56.41  ? 182 VAL A CA  1 
ATOM 1467 C C   . VAL A 1 182 ? 35.011 74.028  156.981 1.00 57.45  ? 182 VAL A C   1 
ATOM 1468 O O   . VAL A 1 182 ? 34.782 73.912  155.765 1.00 57.46  ? 182 VAL A O   1 
ATOM 1469 C CB  . VAL A 1 182 ? 34.005 72.391  158.682 1.00 56.39  ? 182 VAL A CB  1 
ATOM 1470 C CG1 . VAL A 1 182 ? 32.765 72.362  157.777 1.00 55.93  ? 182 VAL A CG1 1 
ATOM 1471 C CG2 . VAL A 1 182 ? 34.191 70.990  159.295 1.00 56.17  ? 182 VAL A CG2 1 
ATOM 1472 N N   . LEU A 1 183 ? 35.058 75.204  157.600 1.00 58.89  ? 183 LEU A N   1 
ATOM 1473 C CA  . LEU A 1 183 ? 34.808 76.436  156.880 1.00 60.47  ? 183 LEU A CA  1 
ATOM 1474 C C   . LEU A 1 183 ? 35.644 76.374  155.599 1.00 61.71  ? 183 LEU A C   1 
ATOM 1475 O O   . LEU A 1 183 ? 35.151 76.697  154.526 1.00 62.51  ? 183 LEU A O   1 
ATOM 1476 C CB  . LEU A 1 183 ? 35.196 77.665  157.734 1.00 61.17  ? 183 LEU A CB  1 
ATOM 1477 C CG  . LEU A 1 183 ? 34.346 78.957  157.560 1.00 61.81  ? 183 LEU A CG  1 
ATOM 1478 C CD1 . LEU A 1 183 ? 33.081 78.849  158.433 1.00 61.44  ? 183 LEU A CD1 1 
ATOM 1479 C CD2 . LEU A 1 183 ? 35.142 80.230  157.937 1.00 61.61  ? 183 LEU A CD2 1 
ATOM 1480 N N   . LEU A 1 184 ? 36.875 75.880  155.697 1.00 63.17  ? 184 LEU A N   1 
ATOM 1481 C CA  . LEU A 1 184 ? 37.768 75.818  154.543 1.00 65.24  ? 184 LEU A CA  1 
ATOM 1482 C C   . LEU A 1 184 ? 37.561 74.725  153.493 1.00 66.97  ? 184 LEU A C   1 
ATOM 1483 O O   . LEU A 1 184 ? 38.084 74.830  152.380 1.00 67.18  ? 184 LEU A O   1 
ATOM 1484 C CB  . LEU A 1 184 ? 39.215 75.808  155.037 1.00 65.41  ? 184 LEU A CB  1 
ATOM 1485 C CG  . LEU A 1 184 ? 39.518 76.975  156.000 1.00 66.40  ? 184 LEU A CG  1 
ATOM 1486 C CD1 . LEU A 1 184 ? 41.010 77.013  156.350 1.00 66.79  ? 184 LEU A CD1 1 
ATOM 1487 C CD2 . LEU A 1 184 ? 39.078 78.304  155.385 1.00 65.80  ? 184 LEU A CD2 1 
ATOM 1488 N N   . PHE A 1 185 ? 36.801 73.688  153.826 1.00 68.89  ? 185 PHE A N   1 
ATOM 1489 C CA  . PHE A 1 185 ? 36.534 72.618  152.869 1.00 71.31  ? 185 PHE A CA  1 
ATOM 1490 C C   . PHE A 1 185 ? 35.490 73.009  151.835 1.00 72.69  ? 185 PHE A C   1 
ATOM 1491 O O   . PHE A 1 185 ? 35.644 72.714  150.635 1.00 72.96  ? 185 PHE A O   1 
ATOM 1492 C CB  . PHE A 1 185 ? 36.040 71.363  153.576 1.00 72.76  ? 185 PHE A CB  1 
ATOM 1493 C CG  . PHE A 1 185 ? 37.139 70.499  154.090 1.00 75.14  ? 185 PHE A CG  1 
ATOM 1494 C CD1 . PHE A 1 185 ? 37.903 69.745  153.209 1.00 76.57  ? 185 PHE A CD1 1 
ATOM 1495 C CD2 . PHE A 1 185 ? 37.458 70.473  155.443 1.00 77.36  ? 185 PHE A CD2 1 
ATOM 1496 C CE1 . PHE A 1 185 ? 38.981 68.973  153.659 1.00 77.61  ? 185 PHE A CE1 1 
ATOM 1497 C CE2 . PHE A 1 185 ? 38.535 69.704  155.912 1.00 78.96  ? 185 PHE A CE2 1 
ATOM 1498 C CZ  . PHE A 1 185 ? 39.300 68.951  155.009 1.00 78.39  ? 185 PHE A CZ  1 
ATOM 1499 N N   . PHE A 1 186 ? 34.430 73.680  152.286 1.00 74.06  ? 186 PHE A N   1 
ATOM 1500 C CA  . PHE A 1 186 ? 33.366 74.052  151.363 1.00 75.72  ? 186 PHE A CA  1 
ATOM 1501 C C   . PHE A 1 186 ? 33.751 74.914  150.183 1.00 76.38  ? 186 PHE A C   1 
ATOM 1502 O O   . PHE A 1 186 ? 33.014 74.988  149.192 1.00 77.26  ? 186 PHE A O   1 
ATOM 1503 C CB  . PHE A 1 186 ? 32.167 74.626  152.113 1.00 76.26  ? 186 PHE A CB  1 
ATOM 1504 C CG  . PHE A 1 186 ? 31.381 73.574  152.819 1.00 77.71  ? 186 PHE A CG  1 
ATOM 1505 C CD1 . PHE A 1 186 ? 30.483 72.759  152.121 1.00 77.84  ? 186 PHE A CD1 1 
ATOM 1506 C CD2 . PHE A 1 186 ? 31.571 73.353  154.169 1.00 79.22  ? 186 PHE A CD2 1 
ATOM 1507 C CE1 . PHE A 1 186 ? 29.786 71.740  152.771 1.00 78.67  ? 186 PHE A CE1 1 
ATOM 1508 C CE2 . PHE A 1 186 ? 30.877 72.339  154.829 1.00 80.55  ? 186 PHE A CE2 1 
ATOM 1509 C CZ  . PHE A 1 186 ? 29.983 71.529  154.133 1.00 79.85  ? 186 PHE A CZ  1 
ATOM 1510 N N   . ALA A 1 187 ? 34.930 75.518  150.266 1.00 76.42  ? 187 ALA A N   1 
ATOM 1511 C CA  . ALA A 1 187 ? 35.454 76.325  149.168 1.00 76.25  ? 187 ALA A CA  1 
ATOM 1512 C C   . ALA A 1 187 ? 36.754 75.656  148.644 1.00 76.07  ? 187 ALA A C   1 
ATOM 1513 O O   . ALA A 1 187 ? 37.861 75.978  149.080 1.00 76.82  ? 187 ALA A O   1 
ATOM 1514 C CB  . ALA A 1 187 ? 35.719 77.743  149.653 1.00 75.62  ? 187 ALA A CB  1 
ATOM 1515 N N   . LYS A 1 188 ? 36.612 74.743  147.685 1.00 76.23  ? 188 LYS A N   1 
ATOM 1516 C CA  . LYS A 1 188 ? 37.763 74.008  147.163 1.00 76.53  ? 188 LYS A CA  1 
ATOM 1517 C C   . LYS A 1 188 ? 38.143 74.126  145.669 1.00 77.09  ? 188 LYS A C   1 
ATOM 1518 O O   . LYS A 1 188 ? 37.802 75.108  144.999 1.00 76.66  ? 188 LYS A O   1 
ATOM 1519 C CB  . LYS A 1 188 ? 37.586 72.530  147.540 1.00 76.10  ? 188 LYS A CB  1 
ATOM 1520 C CG  . LYS A 1 188 ? 36.197 71.952  147.214 1.00 75.94  ? 188 LYS A CG  1 
ATOM 1521 C CD  . LYS A 1 188 ? 35.991 70.579  147.870 1.00 75.06  ? 188 LYS A CD  1 
ATOM 1522 C CE  . LYS A 1 188 ? 34.691 69.895  147.413 1.00 74.72  ? 188 LYS A CE  1 
ATOM 1523 N NZ  . LYS A 1 188 ? 34.456 68.589  148.127 1.00 73.80  ? 188 LYS A NZ  1 
ATOM 1524 N N   . THR A 1 189 ? 38.861 73.107  145.172 1.00 78.15  ? 189 THR A N   1 
ATOM 1525 C CA  . THR A 1 189 ? 39.340 73.018  143.772 1.00 79.23  ? 189 THR A CA  1 
ATOM 1526 C C   . THR A 1 189 ? 39.236 71.553  143.247 1.00 80.56  ? 189 THR A C   1 
ATOM 1527 O O   . THR A 1 189 ? 40.035 70.701  143.640 1.00 80.11  ? 189 THR A O   1 
ATOM 1528 C CB  . THR A 1 189 ? 40.827 73.468  143.676 1.00 78.23  ? 189 THR A CB  1 
ATOM 1529 O OG1 . THR A 1 189 ? 41.019 74.663  144.438 1.00 77.92  ? 189 THR A OG1 1 
ATOM 1530 C CG2 . THR A 1 189 ? 41.213 73.751  142.237 1.00 77.47  ? 189 THR A CG2 1 
ATOM 1531 N N   . ASP A 1 190 ? 38.295 71.293  142.328 1.00 82.74  ? 190 ASP A N   1 
ATOM 1532 C CA  . ASP A 1 190 ? 38.022 69.939  141.799 1.00 85.65  ? 190 ASP A CA  1 
ATOM 1533 C C   . ASP A 1 190 ? 38.452 69.397  140.421 1.00 87.78  ? 190 ASP A C   1 
ATOM 1534 O O   . ASP A 1 190 ? 38.817 68.214  140.313 1.00 87.27  ? 190 ASP A O   1 
ATOM 1535 C CB  . ASP A 1 190 ? 36.519 69.637  141.937 1.00 85.06  ? 190 ASP A CB  1 
ATOM 1536 C CG  . ASP A 1 190 ? 36.139 69.264  143.346 1.00 84.70  ? 190 ASP A CG  1 
ATOM 1537 O OD1 . ASP A 1 190 ? 37.083 69.110  144.148 1.00 85.00  ? 190 ASP A OD1 1 
ATOM 1538 O OD2 . ASP A 1 190 ? 34.927 69.110  143.663 1.00 83.67  ? 190 ASP A OD2 1 
ATOM 1539 N N   . ALA A 1 191 ? 38.365 70.217  139.372 1.00 90.13  ? 191 ALA A N   1 
ATOM 1540 C CA  . ALA A 1 191 ? 38.733 69.799  138.007 1.00 91.95  ? 191 ALA A CA  1 
ATOM 1541 C C   . ALA A 1 191 ? 39.761 70.739  137.368 1.00 93.23  ? 191 ALA A C   1 
ATOM 1542 O O   . ALA A 1 191 ? 39.952 71.862  137.825 1.00 93.20  ? 191 ALA A O   1 
ATOM 1543 C CB  . ALA A 1 191 ? 37.474 69.729  137.129 1.00 91.04  ? 191 ALA A CB  1 
ATOM 1544 N N   . PRO A 1 192 ? 40.461 70.276  136.315 1.00 94.49  ? 192 PRO A N   1 
ATOM 1545 C CA  . PRO A 1 192 ? 41.451 71.170  135.684 1.00 95.99  ? 192 PRO A CA  1 
ATOM 1546 C C   . PRO A 1 192 ? 40.837 72.255  134.806 1.00 96.87  ? 192 PRO A C   1 
ATOM 1547 O O   . PRO A 1 192 ? 39.606 72.376  134.691 1.00 96.81  ? 192 PRO A O   1 
ATOM 1548 C CB  . PRO A 1 192 ? 42.302 70.229  134.821 1.00 95.53  ? 192 PRO A CB  1 
ATOM 1549 C CG  . PRO A 1 192 ? 42.130 68.892  135.463 1.00 95.66  ? 192 PRO A CG  1 
ATOM 1550 C CD  . PRO A 1 192 ? 40.677 68.874  135.893 1.00 95.37  ? 192 PRO A CD  1 
ATOM 1551 N N   . SER A 1 193 ? 41.749 73.017  134.195 1.00 98.30  ? 193 SER A N   1 
ATOM 1552 C CA  . SER A 1 193 ? 41.473 74.123  133.266 1.00 99.97  ? 193 SER A CA  1 
ATOM 1553 C C   . SER A 1 193 ? 42.780 74.389  132.497 1.00 100.57 ? 193 SER A C   1 
ATOM 1554 O O   . SER A 1 193 ? 43.330 75.510  132.534 1.00 100.50 ? 193 SER A O   1 
ATOM 1555 C CB  . SER A 1 193 ? 41.050 75.401  134.018 1.00 99.71  ? 193 SER A CB  1 
ATOM 1556 O OG  . SER A 1 193 ? 42.041 75.823  134.944 1.00 100.49 ? 193 SER A OG  1 
ATOM 1557 N N   . SER A 1 194 ? 43.255 73.334  131.818 1.00 101.21 ? 194 SER A N   1 
ATOM 1558 C CA  . SER A 1 194 ? 44.500 73.311  131.018 1.00 101.64 ? 194 SER A CA  1 
ATOM 1559 C C   . SER A 1 194 ? 45.647 72.623  131.802 1.00 102.15 ? 194 SER A C   1 
ATOM 1560 O O   . SER A 1 194 ? 46.730 72.371  131.248 1.00 101.79 ? 194 SER A O   1 
ATOM 1561 C CB  . SER A 1 194 ? 44.927 74.741  130.581 1.00 101.01 ? 194 SER A CB  1 
ATOM 1562 O OG  . SER A 1 194 ? 46.007 74.734  129.653 1.00 100.24 ? 194 SER A OG  1 
ATOM 1563 N N   . ALA A 1 195 ? 45.394 72.315  133.081 1.00 102.95 ? 195 ALA A N   1 
ATOM 1564 C CA  . ALA A 1 195 ? 46.390 71.668  133.948 1.00 103.42 ? 195 ALA A CA  1 
ATOM 1565 C C   . ALA A 1 195 ? 46.255 70.139  133.970 1.00 103.45 ? 195 ALA A C   1 
ATOM 1566 O O   . ALA A 1 195 ? 46.413 69.496  135.027 1.00 103.70 ? 195 ALA A O   1 
ATOM 1567 C CB  . ALA A 1 195 ? 46.303 72.231  135.378 1.00 103.63 ? 195 ALA A CB  1 
ATOM 1568 N N   . THR A 1 196 ? 45.966 69.583  132.788 1.00 103.14 ? 196 THR A N   1 
ATOM 1569 C CA  . THR A 1 196 ? 45.801 68.143  132.570 1.00 101.83 ? 196 THR A CA  1 
ATOM 1570 C C   . THR A 1 196 ? 44.734 67.448  133.449 1.00 101.58 ? 196 THR A C   1 
ATOM 1571 O O   . THR A 1 196 ? 44.617 67.738  134.648 1.00 101.42 ? 196 THR A O   1 
ATOM 1572 C CB  . THR A 1 196 ? 47.145 67.399  132.741 1.00 101.03 ? 196 THR A CB  1 
ATOM 1573 O OG1 . THR A 1 196 ? 47.028 66.099  132.154 1.00 101.15 ? 196 THR A OG1 1 
ATOM 1574 C CG2 . THR A 1 196 ? 47.513 67.248  134.230 1.00 100.94 ? 196 THR A CG2 1 
ATOM 1575 N N   . VAL A 1 197 ? 43.987 66.519  132.824 1.00 100.82 ? 197 VAL A N   1 
ATOM 1576 C CA  . VAL A 1 197 ? 42.884 65.710  133.423 1.00 100.33 ? 197 VAL A CA  1 
ATOM 1577 C C   . VAL A 1 197 ? 43.298 64.640  134.472 1.00 99.10  ? 197 VAL A C   1 
ATOM 1578 O O   . VAL A 1 197 ? 42.662 64.542  135.536 1.00 98.55  ? 197 VAL A O   1 
ATOM 1579 C CB  . VAL A 1 197 ? 42.035 64.922  132.305 1.00 100.49 ? 197 VAL A CB  1 
ATOM 1580 C CG1 . VAL A 1 197 ? 40.915 64.107  132.985 1.00 100.19 ? 197 VAL A CG1 1 
ATOM 1581 C CG2 . VAL A 1 197 ? 41.440 65.887  131.228 1.00 99.77  ? 197 VAL A CG2 1 
ATOM 1582 N N   . ALA A 1 198 ? 44.321 63.828  134.145 1.00 98.04  ? 198 ALA A N   1 
ATOM 1583 C CA  . ALA A 1 198 ? 44.823 62.764  135.032 1.00 96.36  ? 198 ALA A CA  1 
ATOM 1584 C C   . ALA A 1 198 ? 45.677 63.281  136.214 1.00 95.63  ? 198 ALA A C   1 
ATOM 1585 O O   . ALA A 1 198 ? 46.534 64.180  136.057 1.00 94.96  ? 198 ALA A O   1 
ATOM 1586 C CB  . ALA A 1 198 ? 45.628 61.699  134.210 1.00 94.85  ? 198 ALA A CB  1 
ATOM 1587 N N   . ASN A 1 199 ? 45.418 62.701  137.393 1.00 93.89  ? 199 ASN A N   1 
ATOM 1588 C CA  . ASN A 1 199 ? 46.111 63.029  138.648 1.00 91.83  ? 199 ASN A CA  1 
ATOM 1589 C C   . ASN A 1 199 ? 47.587 62.655  138.565 1.00 92.02  ? 199 ASN A C   1 
ATOM 1590 O O   . ASN A 1 199 ? 48.430 63.190  139.309 1.00 90.68  ? 199 ASN A O   1 
ATOM 1591 C CB  . ASN A 1 199 ? 45.464 62.265  139.810 1.00 91.09  ? 199 ASN A CB  1 
ATOM 1592 C CG  . ASN A 1 199 ? 45.635 60.742  139.693 1.00 90.00  ? 199 ASN A CG  1 
ATOM 1593 O OD1 . ASN A 1 199 ? 45.811 60.195  138.597 1.00 88.90  ? 199 ASN A OD1 1 
ATOM 1594 N ND2 . ASN A 1 199 ? 45.552 60.055  140.828 1.00 89.57  ? 199 ASN A ND2 1 
ATOM 1595 N N   . ALA A 1 200 ? 47.889 61.718  137.669 1.00 91.85  ? 200 ALA A N   1 
ATOM 1596 C CA  . ALA A 1 200 ? 49.254 61.261  137.462 1.00 91.55  ? 200 ALA A CA  1 
ATOM 1597 C C   . ALA A 1 200 ? 50.073 62.182  136.542 1.00 91.70  ? 200 ALA A C   1 
ATOM 1598 O O   . ALA A 1 200 ? 51.258 61.921  136.309 1.00 92.21  ? 200 ALA A O   1 
ATOM 1599 C CB  . ALA A 1 200 ? 49.233 59.843  136.865 1.00 89.29  ? 200 ALA A CB  1 
ATOM 1600 N N   . VAL A 1 201 ? 49.480 63.278  136.067 1.00 90.90  ? 201 VAL A N   1 
ATOM 1601 C CA  . VAL A 1 201 ? 50.163 64.162  135.115 1.00 89.34  ? 201 VAL A CA  1 
ATOM 1602 C C   . VAL A 1 201 ? 51.000 65.367  135.544 1.00 89.01  ? 201 VAL A C   1 
ATOM 1603 O O   . VAL A 1 201 ? 52.084 65.625  134.990 1.00 88.86  ? 201 VAL A O   1 
ATOM 1604 C CB  . VAL A 1 201 ? 49.150 64.670  134.097 1.00 89.36  ? 201 VAL A CB  1 
ATOM 1605 C CG1 . VAL A 1 201 ? 49.863 65.366  132.940 1.00 89.93  ? 201 VAL A CG1 1 
ATOM 1606 C CG2 . VAL A 1 201 ? 48.291 63.505  133.607 1.00 88.98  ? 201 VAL A CG2 1 
ATOM 1607 N N   . GLY A 1 202 ? 50.489 66.109  136.518 1.00 88.01  ? 202 GLY A N   1 
ATOM 1608 C CA  . GLY A 1 202 ? 51.186 67.286  137.004 1.00 86.76  ? 202 GLY A CA  1 
ATOM 1609 C C   . GLY A 1 202 ? 52.225 67.064  138.093 1.00 86.32  ? 202 GLY A C   1 
ATOM 1610 O O   . GLY A 1 202 ? 53.379 67.467  137.909 1.00 85.77  ? 202 GLY A O   1 
ATOM 1611 N N   . ALA A 1 203 ? 51.823 66.428  139.205 1.00 85.95  ? 203 ALA A N   1 
ATOM 1612 C CA  . ALA A 1 203 ? 52.706 66.164  140.369 1.00 84.81  ? 203 ALA A CA  1 
ATOM 1613 C C   . ALA A 1 203 ? 53.634 64.941  140.299 1.00 83.50  ? 203 ALA A C   1 
ATOM 1614 O O   . ALA A 1 203 ? 54.635 64.870  141.032 1.00 82.76  ? 203 ALA A O   1 
ATOM 1615 C CB  . ALA A 1 203 ? 51.865 66.092  141.664 1.00 84.34  ? 203 ALA A CB  1 
ATOM 1616 N N   . ASN A 1 204 ? 53.285 63.974  139.451 1.00 81.68  ? 204 ASN A N   1 
ATOM 1617 C CA  . ASN A 1 204 ? 54.112 62.778  139.276 1.00 79.50  ? 204 ASN A CA  1 
ATOM 1618 C C   . ASN A 1 204 ? 54.333 62.032  140.598 1.00 77.68  ? 204 ASN A C   1 
ATOM 1619 O O   . ASN A 1 204 ? 53.670 62.323  141.599 1.00 77.81  ? 204 ASN A O   1 
ATOM 1620 C CB  . ASN A 1 204 ? 55.466 63.191  138.688 1.00 79.87  ? 204 ASN A CB  1 
ATOM 1621 C CG  . ASN A 1 204 ? 55.342 63.894  137.332 1.00 80.46  ? 204 ASN A CG  1 
ATOM 1622 O OD1 . ASN A 1 204 ? 56.311 64.491  136.849 1.00 80.17  ? 204 ASN A OD1 1 
ATOM 1623 N ND2 . ASN A 1 204 ? 54.162 63.820  136.712 1.00 80.77  ? 204 ASN A ND2 1 
ATOM 1624 N N   . HIS A 1 205 ? 55.265 61.082  140.627 1.00 75.10  ? 205 HIS A N   1 
ATOM 1625 C CA  . HIS A 1 205 ? 55.487 60.370  141.883 1.00 72.32  ? 205 HIS A CA  1 
ATOM 1626 C C   . HIS A 1 205 ? 56.908 59.772  142.017 1.00 69.50  ? 205 HIS A C   1 
ATOM 1627 O O   . HIS A 1 205 ? 57.718 59.905  141.107 1.00 69.34  ? 205 HIS A O   1 
ATOM 1628 C CB  . HIS A 1 205 ? 54.384 59.301  142.020 1.00 72.98  ? 205 HIS A CB  1 
ATOM 1629 C CG  . HIS A 1 205 ? 54.108 58.885  143.434 1.00 74.58  ? 205 HIS A CG  1 
ATOM 1630 N ND1 . HIS A 1 205 ? 54.040 57.555  143.810 1.00 74.91  ? 205 HIS A ND1 1 
ATOM 1631 C CD2 . HIS A 1 205 ? 53.906 59.603  144.562 1.00 74.47  ? 205 HIS A CD2 1 
ATOM 1632 C CE1 . HIS A 1 205 ? 53.817 57.477  145.107 1.00 75.26  ? 205 HIS A CE1 1 
ATOM 1633 N NE2 . HIS A 1 205 ? 53.731 58.707  145.590 1.00 75.44  ? 205 HIS A NE2 1 
ATOM 1634 N N   . SER A 1 206 ? 57.210 59.171  143.172 1.00 66.16  ? 206 SER A N   1 
ATOM 1635 C CA  . SER A 1 206 ? 58.505 58.531  143.469 1.00 62.91  ? 206 SER A CA  1 
ATOM 1636 C C   . SER A 1 206 ? 58.188 57.118  143.995 1.00 61.24  ? 206 SER A C   1 
ATOM 1637 O O   . SER A 1 206 ? 57.143 56.918  144.609 1.00 61.52  ? 206 SER A O   1 
ATOM 1638 C CB  . SER A 1 206 ? 59.257 59.334  144.537 1.00 61.98  ? 206 SER A CB  1 
ATOM 1639 O OG  . SER A 1 206 ? 59.568 60.631  144.064 1.00 61.21  ? 206 SER A OG  1 
ATOM 1640 N N   . ALA A 1 207 ? 59.057 56.133  143.772 1.00 58.96  ? 207 ALA A N   1 
ATOM 1641 C CA  . ALA A 1 207 ? 58.740 54.770  144.236 1.00 56.15  ? 207 ALA A CA  1 
ATOM 1642 C C   . ALA A 1 207 ? 59.898 54.013  144.875 1.00 53.94  ? 207 ALA A C   1 
ATOM 1643 O O   . ALA A 1 207 ? 61.032 54.463  144.830 1.00 51.94  ? 207 ALA A O   1 
ATOM 1644 C CB  . ALA A 1 207 ? 58.157 53.946  143.075 1.00 56.42  ? 207 ALA A CB  1 
ATOM 1645 N N   . PHE A 1 208 ? 59.591 52.859  145.465 1.00 52.72  ? 208 PHE A N   1 
ATOM 1646 C CA  . PHE A 1 208 ? 60.597 52.047  146.141 1.00 52.26  ? 208 PHE A CA  1 
ATOM 1647 C C   . PHE A 1 208 ? 60.325 50.540  146.178 1.00 51.00  ? 208 PHE A C   1 
ATOM 1648 O O   . PHE A 1 208 ? 59.197 50.090  145.939 1.00 50.41  ? 208 PHE A O   1 
ATOM 1649 C CB  . PHE A 1 208 ? 60.802 52.558  147.574 1.00 54.16  ? 208 PHE A CB  1 
ATOM 1650 C CG  . PHE A 1 208 ? 59.537 52.623  148.391 1.00 55.97  ? 208 PHE A CG  1 
ATOM 1651 C CD1 . PHE A 1 208 ? 58.553 53.574  148.098 1.00 57.02  ? 208 PHE A CD1 1 
ATOM 1652 C CD2 . PHE A 1 208 ? 59.326 51.745  149.455 1.00 57.21  ? 208 PHE A CD2 1 
ATOM 1653 C CE1 . PHE A 1 208 ? 57.378 53.667  148.870 1.00 58.00  ? 208 PHE A CE1 1 
ATOM 1654 C CE2 . PHE A 1 208 ? 58.151 51.824  150.244 1.00 58.03  ? 208 PHE A CE2 1 
ATOM 1655 C CZ  . PHE A 1 208 ? 57.173 52.786  149.944 1.00 58.29  ? 208 PHE A CZ  1 
ATOM 1656 N N   . SER A 1 209 ? 61.367 49.771  146.514 1.00 49.71  ? 209 SER A N   1 
ATOM 1657 C CA  . SER A 1 209 ? 61.256 48.319  146.532 1.00 48.33  ? 209 SER A CA  1 
ATOM 1658 C C   . SER A 1 209 ? 62.464 47.570  147.061 1.00 46.78  ? 209 SER A C   1 
ATOM 1659 O O   . SER A 1 209 ? 63.551 48.130  147.200 1.00 46.39  ? 209 SER A O   1 
ATOM 1660 C CB  . SER A 1 209 ? 61.047 47.839  145.119 1.00 49.55  ? 209 SER A CB  1 
ATOM 1661 O OG  . SER A 1 209 ? 62.154 48.276  144.344 1.00 49.94  ? 209 SER A OG  1 
ATOM 1662 N N   . LEU A 1 210 ? 62.241 46.272  147.274 1.00 45.06  ? 210 LEU A N   1 
ATOM 1663 C CA  . LEU A 1 210 ? 63.235 45.333  147.769 1.00 44.02  ? 210 LEU A CA  1 
ATOM 1664 C C   . LEU A 1 210 ? 64.619 45.489  147.161 1.00 43.26  ? 210 LEU A C   1 
ATOM 1665 O O   . LEU A 1 210 ? 65.609 45.578  147.888 1.00 43.01  ? 210 LEU A O   1 
ATOM 1666 C CB  . LEU A 1 210 ? 62.779 43.891  147.537 1.00 44.14  ? 210 LEU A CB  1 
ATOM 1667 C CG  . LEU A 1 210 ? 63.817 42.829  147.940 1.00 44.35  ? 210 LEU A CG  1 
ATOM 1668 C CD1 . LEU A 1 210 ? 63.892 42.802  149.451 1.00 44.32  ? 210 LEU A CD1 1 
ATOM 1669 C CD2 . LEU A 1 210 ? 63.462 41.436  147.405 1.00 44.51  ? 210 LEU A CD2 1 
ATOM 1670 N N   . LYS A 1 211 ? 64.716 45.512  145.836 1.00 42.42  ? 211 LYS A N   1 
ATOM 1671 C CA  . LYS A 1 211 ? 66.045 45.638  145.247 1.00 41.45  ? 211 LYS A CA  1 
ATOM 1672 C C   . LYS A 1 211 ? 66.668 46.978  145.626 1.00 40.20  ? 211 LYS A C   1 
ATOM 1673 O O   . LYS A 1 211 ? 67.824 47.031  146.066 1.00 40.08  ? 211 LYS A O   1 
ATOM 1674 C CB  . LYS A 1 211 ? 66.024 45.450  143.710 1.00 41.64  ? 211 LYS A CB  1 
ATOM 1675 C CG  . LYS A 1 211 ? 65.848 43.988  143.214 1.00 40.72  ? 211 LYS A CG  1 
ATOM 1676 C CD  . LYS A 1 211 ? 67.033 43.085  143.539 1.00 39.57  ? 211 LYS A CD  1 
ATOM 1677 C CE  . LYS A 1 211 ? 66.636 41.631  143.414 1.00 39.01  ? 211 LYS A CE  1 
ATOM 1678 N NZ  . LYS A 1 211 ? 67.692 40.744  143.953 1.00 38.53  ? 211 LYS A NZ  1 
ATOM 1679 N N   . LEU A 1 212 ? 65.913 48.060  145.479 1.00 38.74  ? 212 LEU A N   1 
ATOM 1680 C CA  . LEU A 1 212 ? 66.457 49.353  145.854 1.00 38.17  ? 212 LEU A CA  1 
ATOM 1681 C C   . LEU A 1 212 ? 67.023 49.175  147.232 1.00 36.82  ? 212 LEU A C   1 
ATOM 1682 O O   . LEU A 1 212 ? 68.189 49.463  147.516 1.00 35.00  ? 212 LEU A O   1 
ATOM 1683 C CB  . LEU A 1 212 ? 65.359 50.402  145.906 1.00 38.51  ? 212 LEU A CB  1 
ATOM 1684 C CG  . LEU A 1 212 ? 64.992 51.043  144.569 1.00 39.38  ? 212 LEU A CG  1 
ATOM 1685 C CD1 . LEU A 1 212 ? 64.008 52.163  144.854 1.00 38.56  ? 212 LEU A CD1 1 
ATOM 1686 C CD2 . LEU A 1 212 ? 66.249 51.584  143.851 1.00 39.67  ? 212 LEU A CD2 1 
ATOM 1687 N N   . ALA A 1 213 ? 66.150 48.664  148.078 1.00 36.83  ? 213 ALA A N   1 
ATOM 1688 C CA  . ALA A 1 213 ? 66.474 48.410  149.449 1.00 37.02  ? 213 ALA A CA  1 
ATOM 1689 C C   . ALA A 1 213 ? 67.752 47.609  149.508 1.00 37.51  ? 213 ALA A C   1 
ATOM 1690 O O   . ALA A 1 213 ? 68.799 48.119  149.890 1.00 37.03  ? 213 ALA A O   1 
ATOM 1691 C CB  . ALA A 1 213 ? 65.344 47.650  150.093 1.00 36.32  ? 213 ALA A CB  1 
ATOM 1692 N N   . LEU A 1 214 ? 67.661 46.354  149.095 1.00 38.79  ? 214 LEU A N   1 
ATOM 1693 C CA  . LEU A 1 214 ? 68.802 45.463  149.123 1.00 40.26  ? 214 LEU A CA  1 
ATOM 1694 C C   . LEU A 1 214 ? 70.033 46.115  148.558 1.00 41.32  ? 214 LEU A C   1 
ATOM 1695 O O   . LEU A 1 214 ? 71.151 45.880  149.018 1.00 41.05  ? 214 LEU A O   1 
ATOM 1696 C CB  . LEU A 1 214 ? 68.485 44.179  148.360 1.00 40.56  ? 214 LEU A CB  1 
ATOM 1697 C CG  . LEU A 1 214 ? 67.436 43.316  149.068 1.00 41.01  ? 214 LEU A CG  1 
ATOM 1698 C CD1 . LEU A 1 214 ? 67.268 41.993  148.331 1.00 41.15  ? 214 LEU A CD1 1 
ATOM 1699 C CD2 . LEU A 1 214 ? 67.880 43.072  150.510 1.00 41.42  ? 214 LEU A CD2 1 
ATOM 1700 N N   . GLU A 1 215 ? 69.842 46.959  147.567 1.00 42.44  ? 215 GLU A N   1 
ATOM 1701 C CA  . GLU A 1 215 ? 70.998 47.590  147.016 1.00 44.02  ? 215 GLU A CA  1 
ATOM 1702 C C   . GLU A 1 215 ? 71.507 48.565  148.062 1.00 44.60  ? 215 GLU A C   1 
ATOM 1703 O O   . GLU A 1 215 ? 72.707 48.617  148.315 1.00 45.10  ? 215 GLU A O   1 
ATOM 1704 C CB  . GLU A 1 215 ? 70.627 48.267  145.713 1.00 45.39  ? 215 GLU A CB  1 
ATOM 1705 C CG  . GLU A 1 215 ? 71.804 48.846  145.006 1.00 47.56  ? 215 GLU A CG  1 
ATOM 1706 C CD  . GLU A 1 215 ? 72.261 50.116  145.670 1.00 49.11  ? 215 GLU A CD  1 
ATOM 1707 O OE1 . GLU A 1 215 ? 71.587 50.557  146.632 1.00 50.30  ? 215 GLU A OE1 1 
ATOM 1708 O OE2 . GLU A 1 215 ? 73.280 50.679  145.222 1.00 49.58  ? 215 GLU A OE2 1 
ATOM 1709 N N   . LEU A 1 216 ? 70.588 49.310  148.680 1.00 44.91  ? 216 LEU A N   1 
ATOM 1710 C CA  . LEU A 1 216 ? 70.930 50.282  149.722 1.00 45.54  ? 216 LEU A CA  1 
ATOM 1711 C C   . LEU A 1 216 ? 71.682 49.596  150.836 1.00 46.57  ? 216 LEU A C   1 
ATOM 1712 O O   . LEU A 1 216 ? 72.723 50.079  151.264 1.00 46.50  ? 216 LEU A O   1 
ATOM 1713 C CB  . LEU A 1 216 ? 69.677 50.938  150.301 1.00 44.71  ? 216 LEU A CB  1 
ATOM 1714 C CG  . LEU A 1 216 ? 69.236 52.215  149.583 1.00 44.56  ? 216 LEU A CG  1 
ATOM 1715 C CD1 . LEU A 1 216 ? 68.046 52.821  150.272 1.00 44.28  ? 216 LEU A CD1 1 
ATOM 1716 C CD2 . LEU A 1 216 ? 70.365 53.202  149.610 1.00 43.84  ? 216 LEU A CD2 1 
ATOM 1717 N N   . PHE A 1 217 ? 71.168 48.463  151.303 1.00 48.19  ? 217 PHE A N   1 
ATOM 1718 C CA  . PHE A 1 217 ? 71.870 47.753  152.358 1.00 50.25  ? 217 PHE A CA  1 
ATOM 1719 C C   . PHE A 1 217 ? 73.238 47.277  151.896 1.00 51.05  ? 217 PHE A C   1 
ATOM 1720 O O   . PHE A 1 217 ? 74.114 47.010  152.711 1.00 50.69  ? 217 PHE A O   1 
ATOM 1721 C CB  . PHE A 1 217 ? 71.056 46.579  152.874 1.00 51.33  ? 217 PHE A CB  1 
ATOM 1722 C CG  . PHE A 1 217 ? 69.820 46.986  153.605 1.00 52.65  ? 217 PHE A CG  1 
ATOM 1723 C CD1 . PHE A 1 217 ? 68.697 47.401  152.909 1.00 53.24  ? 217 PHE A CD1 1 
ATOM 1724 C CD2 . PHE A 1 217 ? 69.770 46.937  154.997 1.00 53.04  ? 217 PHE A CD2 1 
ATOM 1725 C CE1 . PHE A 1 217 ? 67.532 47.756  153.588 1.00 53.26  ? 217 PHE A CE1 1 
ATOM 1726 C CE2 . PHE A 1 217 ? 68.616 47.289  155.686 1.00 52.79  ? 217 PHE A CE2 1 
ATOM 1727 C CZ  . PHE A 1 217 ? 67.492 47.699  154.979 1.00 52.76  ? 217 PHE A CZ  1 
ATOM 1728 N N   . ARG A 1 218 ? 73.423 47.167  150.588 1.00 52.85  ? 218 ARG A N   1 
ATOM 1729 C CA  . ARG A 1 218 ? 74.716 46.764  150.046 1.00 54.65  ? 218 ARG A CA  1 
ATOM 1730 C C   . ARG A 1 218 ? 75.652 47.933  150.349 1.00 54.02  ? 218 ARG A C   1 
ATOM 1731 O O   . ARG A 1 218 ? 76.818 47.765  150.704 1.00 53.63  ? 218 ARG A O   1 
ATOM 1732 C CB  . ARG A 1 218 ? 74.588 46.554  148.524 1.00 58.02  ? 218 ARG A CB  1 
ATOM 1733 C CG  . ARG A 1 218 ? 75.892 46.358  147.749 1.00 62.09  ? 218 ARG A CG  1 
ATOM 1734 C CD  . ARG A 1 218 ? 75.680 46.656  146.273 1.00 65.68  ? 218 ARG A CD  1 
ATOM 1735 N NE  . ARG A 1 218 ? 76.909 46.478  145.511 1.00 69.97  ? 218 ARG A NE  1 
ATOM 1736 C CZ  . ARG A 1 218 ? 77.007 46.708  144.205 1.00 72.26  ? 218 ARG A CZ  1 
ATOM 1737 N NH1 . ARG A 1 218 ? 75.940 47.129  143.535 1.00 73.68  ? 218 ARG A NH1 1 
ATOM 1738 N NH2 . ARG A 1 218 ? 78.161 46.506  143.561 1.00 73.57  ? 218 ARG A NH2 1 
ATOM 1739 N N   . GLN A 1 219 ? 75.102 49.131  150.236 1.00 53.10  ? 219 GLN A N   1 
ATOM 1740 C CA  . GLN A 1 219 ? 75.880 50.333  150.445 1.00 52.10  ? 219 GLN A CA  1 
ATOM 1741 C C   . GLN A 1 219 ? 76.359 50.489  151.864 1.00 51.74  ? 219 GLN A C   1 
ATOM 1742 O O   . GLN A 1 219 ? 75.662 50.126  152.805 1.00 53.14  ? 219 GLN A O   1 
ATOM 1743 C CB  . GLN A 1 219 ? 75.053 51.556  150.086 1.00 53.02  ? 219 GLN A CB  1 
ATOM 1744 C CG  . GLN A 1 219 ? 74.402 51.535  148.715 1.00 54.43  ? 219 GLN A CG  1 
ATOM 1745 C CD  . GLN A 1 219 ? 73.688 52.839  148.432 1.00 55.27  ? 219 GLN A CD  1 
ATOM 1746 O OE1 . GLN A 1 219 ? 73.002 53.361  149.314 1.00 56.93  ? 219 GLN A OE1 1 
ATOM 1747 N NE2 . GLN A 1 219 ? 73.843 53.381  147.209 1.00 55.77  ? 219 GLN A NE2 1 
ATOM 1748 N N   . PRO A 1 220 ? 77.576 51.009  152.042 1.00 51.14  ? 220 PRO A N   1 
ATOM 1749 C CA  . PRO A 1 220 ? 78.092 51.202  153.397 1.00 48.95  ? 220 PRO A CA  1 
ATOM 1750 C C   . PRO A 1 220 ? 77.665 52.576  153.922 1.00 48.53  ? 220 PRO A C   1 
ATOM 1751 O O   . PRO A 1 220 ? 77.476 52.758  155.121 1.00 48.45  ? 220 PRO A O   1 
ATOM 1752 C CB  . PRO A 1 220 ? 79.603 51.108  153.213 1.00 49.51  ? 220 PRO A CB  1 
ATOM 1753 C CG  . PRO A 1 220 ? 79.793 51.670  151.859 1.00 49.52  ? 220 PRO A CG  1 
ATOM 1754 C CD  . PRO A 1 220 ? 78.666 51.055  151.058 1.00 49.99  ? 220 PRO A CD  1 
ATOM 1755 N N   . LYS A 1 221 ? 77.498 53.531  153.013 1.00 47.47  ? 221 LYS A N   1 
ATOM 1756 C CA  . LYS A 1 221 ? 77.126 54.872  153.413 1.00 46.78  ? 221 LYS A CA  1 
ATOM 1757 C C   . LYS A 1 221 ? 75.865 54.923  154.216 1.00 46.22  ? 221 LYS A C   1 
ATOM 1758 O O   . LYS A 1 221 ? 75.729 55.764  155.095 1.00 46.53  ? 221 LYS A O   1 
ATOM 1759 C CB  . LYS A 1 221 ? 76.997 55.819  152.211 1.00 47.37  ? 221 LYS A CB  1 
ATOM 1760 C CG  . LYS A 1 221 ? 76.291 55.235  150.992 1.00 47.69  ? 221 LYS A CG  1 
ATOM 1761 C CD  . LYS A 1 221 ? 76.240 56.226  149.797 1.00 46.94  ? 221 LYS A CD  1 
ATOM 1762 C CE  . LYS A 1 221 ? 75.466 55.612  148.626 1.00 46.25  ? 221 LYS A CE  1 
ATOM 1763 N NZ  . LYS A 1 221 ? 74.862 56.584  147.683 1.00 46.08  ? 221 LYS A NZ  1 
ATOM 1764 N N   . LEU A 1 222 ? 74.925 54.042  153.935 1.00 46.69  ? 222 LEU A N   1 
ATOM 1765 C CA  . LEU A 1 222 ? 73.718 54.087  154.728 1.00 48.16  ? 222 LEU A CA  1 
ATOM 1766 C C   . LEU A 1 222 ? 74.095 53.840  156.185 1.00 49.01  ? 222 LEU A C   1 
ATOM 1767 O O   . LEU A 1 222 ? 73.798 54.655  157.064 1.00 48.74  ? 222 LEU A O   1 
ATOM 1768 C CB  . LEU A 1 222 ? 72.704 53.023  154.293 1.00 48.93  ? 222 LEU A CB  1 
ATOM 1769 C CG  . LEU A 1 222 ? 71.450 52.963  155.194 1.00 49.68  ? 222 LEU A CG  1 
ATOM 1770 C CD1 . LEU A 1 222 ? 70.654 54.266  155.022 1.00 49.76  ? 222 LEU A CD1 1 
ATOM 1771 C CD2 . LEU A 1 222 ? 70.589 51.744  154.853 1.00 49.24  ? 222 LEU A CD2 1 
ATOM 1772 N N   . TRP A 1 223 ? 74.767 52.718  156.421 1.00 49.45  ? 223 TRP A N   1 
ATOM 1773 C CA  . TRP A 1 223 ? 75.162 52.336  157.759 1.00 50.17  ? 223 TRP A CA  1 
ATOM 1774 C C   . TRP A 1 223 ? 75.689 53.521  158.524 1.00 47.93  ? 223 TRP A C   1 
ATOM 1775 O O   . TRP A 1 223 ? 75.254 53.818  159.635 1.00 48.46  ? 223 TRP A O   1 
ATOM 1776 C CB  . TRP A 1 223 ? 76.235 51.263  157.689 1.00 54.52  ? 223 TRP A CB  1 
ATOM 1777 C CG  . TRP A 1 223 ? 75.764 49.957  157.097 1.00 59.23  ? 223 TRP A CG  1 
ATOM 1778 C CD1 . TRP A 1 223 ? 76.543 49.022  156.471 1.00 60.64  ? 223 TRP A CD1 1 
ATOM 1779 C CD2 . TRP A 1 223 ? 74.431 49.401  157.147 1.00 61.32  ? 223 TRP A CD2 1 
ATOM 1780 N NE1 . TRP A 1 223 ? 75.787 47.922  156.132 1.00 62.98  ? 223 TRP A NE1 1 
ATOM 1781 C CE2 . TRP A 1 223 ? 74.494 48.125  156.530 1.00 62.59  ? 223 TRP A CE2 1 
ATOM 1782 C CE3 . TRP A 1 223 ? 73.200 49.863  157.651 1.00 61.20  ? 223 TRP A CE3 1 
ATOM 1783 C CZ2 . TRP A 1 223 ? 73.365 47.292  156.409 1.00 63.35  ? 223 TRP A CZ2 1 
ATOM 1784 C CZ3 . TRP A 1 223 ? 72.083 49.034  157.527 1.00 62.43  ? 223 TRP A CZ3 1 
ATOM 1785 C CH2 . TRP A 1 223 ? 72.178 47.763  156.907 1.00 63.49  ? 223 TRP A CH2 1 
ATOM 1786 N N   . PHE A 1 224 ? 76.618 54.214  157.902 1.00 45.52  ? 224 PHE A N   1 
ATOM 1787 C CA  . PHE A 1 224 ? 77.218 55.340  158.533 1.00 43.14  ? 224 PHE A CA  1 
ATOM 1788 C C   . PHE A 1 224 ? 76.325 56.552  158.557 1.00 41.23  ? 224 PHE A C   1 
ATOM 1789 O O   . PHE A 1 224 ? 76.447 57.390  159.446 1.00 41.76  ? 224 PHE A O   1 
ATOM 1790 C CB  . PHE A 1 224 ? 78.560 55.568  157.879 1.00 43.39  ? 224 PHE A CB  1 
ATOM 1791 C CG  . PHE A 1 224 ? 79.496 54.422  158.098 1.00 44.66  ? 224 PHE A CG  1 
ATOM 1792 C CD1 . PHE A 1 224 ? 79.048 53.210  158.605 1.00 44.67  ? 224 PHE A CD1 1 
ATOM 1793 C CD2 . PHE A 1 224 ? 80.822 54.548  157.829 1.00 45.71  ? 224 PHE A CD2 1 
ATOM 1794 C CE1 . PHE A 1 224 ? 79.947 52.158  158.830 1.00 46.25  ? 224 PHE A CE1 1 
ATOM 1795 C CE2 . PHE A 1 224 ? 81.716 53.501  158.055 1.00 47.10  ? 224 PHE A CE2 1 
ATOM 1796 C CZ  . PHE A 1 224 ? 81.282 52.318  158.551 1.00 47.12  ? 224 PHE A CZ  1 
ATOM 1797 N N   . LEU A 1 225 ? 75.382 56.643  157.635 1.00 38.42  ? 225 LEU A N   1 
ATOM 1798 C CA  . LEU A 1 225 ? 74.503 57.784  157.716 1.00 35.76  ? 225 LEU A CA  1 
ATOM 1799 C C   . LEU A 1 225 ? 73.520 57.491  158.807 1.00 33.35  ? 225 LEU A C   1 
ATOM 1800 O O   . LEU A 1 225 ? 73.305 58.313  159.688 1.00 32.95  ? 225 LEU A O   1 
ATOM 1801 C CB  . LEU A 1 225 ? 73.719 58.027  156.443 1.00 36.59  ? 225 LEU A CB  1 
ATOM 1802 C CG  . LEU A 1 225 ? 72.823 59.216  156.820 1.00 36.66  ? 225 LEU A CG  1 
ATOM 1803 C CD1 . LEU A 1 225 ? 73.618 60.513  156.760 1.00 36.41  ? 225 LEU A CD1 1 
ATOM 1804 C CD2 . LEU A 1 225 ? 71.649 59.274  155.911 1.00 37.30  ? 225 LEU A CD2 1 
ATOM 1805 N N   . SER A 1 226 ? 72.917 56.311  158.741 1.00 30.92  ? 226 SER A N   1 
ATOM 1806 C CA  . SER A 1 226 ? 71.945 55.936  159.751 1.00 28.80  ? 226 SER A CA  1 
ATOM 1807 C C   . SER A 1 226 ? 72.500 56.128  161.180 1.00 27.30  ? 226 SER A C   1 
ATOM 1808 O O   . SER A 1 226 ? 71.803 56.665  162.040 1.00 28.39  ? 226 SER A O   1 
ATOM 1809 C CB  . SER A 1 226 ? 71.451 54.498  159.528 1.00 27.71  ? 226 SER A CB  1 
ATOM 1810 O OG  . SER A 1 226 ? 70.531 54.429  158.449 1.00 25.23  ? 226 SER A OG  1 
ATOM 1811 N N   . LEU A 1 227 ? 73.737 55.717  161.453 1.00 24.71  ? 227 LEU A N   1 
ATOM 1812 C CA  . LEU A 1 227 ? 74.241 55.937  162.800 1.00 22.18  ? 227 LEU A CA  1 
ATOM 1813 C C   . LEU A 1 227 ? 73.914 57.369  163.128 1.00 20.23  ? 227 LEU A C   1 
ATOM 1814 O O   . LEU A 1 227 ? 73.164 57.651  164.053 1.00 19.53  ? 227 LEU A O   1 
ATOM 1815 C CB  . LEU A 1 227 ? 75.753 55.755  162.917 1.00 22.25  ? 227 LEU A CB  1 
ATOM 1816 C CG  . LEU A 1 227 ? 76.242 54.332  163.198 1.00 22.31  ? 227 LEU A CG  1 
ATOM 1817 C CD1 . LEU A 1 227 ? 77.729 54.339  163.440 1.00 21.51  ? 227 LEU A CD1 1 
ATOM 1818 C CD2 . LEU A 1 227 ? 75.523 53.790  164.405 1.00 22.26  ? 227 LEU A CD2 1 
ATOM 1819 N N   . TYR A 1 228 ? 74.449 58.283  162.334 1.00 18.15  ? 228 TYR A N   1 
ATOM 1820 C CA  . TYR A 1 228 ? 74.232 59.692  162.577 1.00 16.33  ? 228 TYR A CA  1 
ATOM 1821 C C   . TYR A 1 228 ? 72.796 59.911  162.900 1.00 16.09  ? 228 TYR A C   1 
ATOM 1822 O O   . TYR A 1 228 ? 72.411 60.051  164.059 1.00 14.90  ? 228 TYR A O   1 
ATOM 1823 C CB  . TYR A 1 228 ? 74.561 60.535  161.361 1.00 15.09  ? 228 TYR A CB  1 
ATOM 1824 C CG  . TYR A 1 228 ? 74.476 62.015  161.643 1.00 13.11  ? 228 TYR A CG  1 
ATOM 1825 C CD1 . TYR A 1 228 ? 73.279 62.696  161.473 1.00 11.72  ? 228 TYR A CD1 1 
ATOM 1826 C CD2 . TYR A 1 228 ? 75.581 62.730  162.093 1.00 11.85  ? 228 TYR A CD2 1 
ATOM 1827 C CE1 . TYR A 1 228 ? 73.165 64.025  161.764 1.00 10.89  ? 228 TYR A CE1 1 
ATOM 1828 C CE2 . TYR A 1 228 ? 75.476 64.082  162.384 1.00 10.70  ? 228 TYR A CE2 1 
ATOM 1829 C CZ  . TYR A 1 228 ? 74.264 64.721  162.203 1.00 10.67  ? 228 TYR A CZ  1 
ATOM 1830 O OH  . TYR A 1 228 ? 74.120 66.057  162.460 1.00 10.03  ? 228 TYR A OH  1 
ATOM 1831 N N   . VAL A 1 229 ? 71.973 59.969  161.881 1.00 17.66  ? 229 VAL A N   1 
ATOM 1832 C CA  . VAL A 1 229 ? 70.571 60.204  162.117 1.00 20.64  ? 229 VAL A CA  1 
ATOM 1833 C C   . VAL A 1 229 ? 70.071 59.427  163.331 1.00 21.54  ? 229 VAL A C   1 
ATOM 1834 O O   . VAL A 1 229 ? 69.742 60.024  164.328 1.00 21.00  ? 229 VAL A O   1 
ATOM 1835 C CB  . VAL A 1 229 ? 69.693 59.741  160.879 1.00 22.03  ? 229 VAL A CB  1 
ATOM 1836 C CG1 . VAL A 1 229 ? 68.226 59.927  161.270 1.00 22.31  ? 229 VAL A CG1 1 
ATOM 1837 C CG2 . VAL A 1 229 ? 70.053 60.580  159.613 1.00 24.11  ? 229 VAL A CG2 1 
ATOM 1838 N N   . ILE A 1 230 ? 69.998 58.099  163.225 1.00 23.63  ? 230 ILE A N   1 
ATOM 1839 C CA  . ILE A 1 230 ? 69.467 57.276  164.322 1.00 26.35  ? 230 ILE A CA  1 
ATOM 1840 C C   . ILE A 1 230 ? 70.027 57.578  165.680 1.00 27.15  ? 230 ILE A C   1 
ATOM 1841 O O   . ILE A 1 230 ? 69.300 57.681  166.656 1.00 27.31  ? 230 ILE A O   1 
ATOM 1842 C CB  . ILE A 1 230 ? 69.693 55.768  164.091 1.00 27.01  ? 230 ILE A CB  1 
ATOM 1843 C CG1 . ILE A 1 230 ? 68.921 55.349  162.855 1.00 29.15  ? 230 ILE A CG1 1 
ATOM 1844 C CG2 . ILE A 1 230 ? 69.220 54.942  165.302 1.00 26.73  ? 230 ILE A CG2 1 
ATOM 1845 C CD1 . ILE A 1 230 ? 68.983 53.896  162.485 1.00 31.82  ? 230 ILE A CD1 1 
ATOM 1846 N N   . GLY A 1 231 ? 71.339 57.679  165.738 1.00 27.59  ? 231 GLY A N   1 
ATOM 1847 C CA  . GLY A 1 231 ? 71.978 57.959  167.001 1.00 27.87  ? 231 GLY A CA  1 
ATOM 1848 C C   . GLY A 1 231 ? 71.641 59.341  167.520 1.00 27.43  ? 231 GLY A C   1 
ATOM 1849 O O   . GLY A 1 231 ? 71.008 59.481  168.566 1.00 27.20  ? 231 GLY A O   1 
ATOM 1850 N N   . VAL A 1 232 ? 72.031 60.356  166.754 1.00 27.13  ? 232 VAL A N   1 
ATOM 1851 C CA  . VAL A 1 232 ? 71.821 61.735  167.128 1.00 25.22  ? 232 VAL A CA  1 
ATOM 1852 C C   . VAL A 1 232 ? 70.373 62.196  167.182 1.00 24.53  ? 232 VAL A C   1 
ATOM 1853 O O   . VAL A 1 232 ? 69.961 62.767  168.184 1.00 25.28  ? 232 VAL A O   1 
ATOM 1854 C CB  . VAL A 1 232 ? 72.649 62.663  166.235 1.00 25.31  ? 232 VAL A CB  1 
ATOM 1855 C CG1 . VAL A 1 232 ? 72.424 64.091  166.628 1.00 25.70  ? 232 VAL A CG1 1 
ATOM 1856 C CG2 . VAL A 1 232 ? 74.136 62.322  166.389 1.00 24.53  ? 232 VAL A CG2 1 
ATOM 1857 N N   . SER A 1 233 ? 69.588 61.952  166.140 1.00 22.27  ? 233 SER A N   1 
ATOM 1858 C CA  . SER A 1 233 ? 68.187 62.341  166.196 1.00 21.26  ? 233 SER A CA  1 
ATOM 1859 C C   . SER A 1 233 ? 67.526 61.719  167.432 1.00 21.94  ? 233 SER A C   1 
ATOM 1860 O O   . SER A 1 233 ? 67.097 62.435  168.341 1.00 23.64  ? 233 SER A O   1 
ATOM 1861 C CB  . SER A 1 233 ? 67.445 61.879  164.955 1.00 19.85  ? 233 SER A CB  1 
ATOM 1862 O OG  . SER A 1 233 ? 67.847 62.655  163.865 1.00 20.51  ? 233 SER A OG  1 
ATOM 1863 N N   . CYS A 1 234 ? 67.454 60.388  167.473 1.00 21.38  ? 234 CYS A N   1 
ATOM 1864 C CA  . CYS A 1 234 ? 66.833 59.668  168.595 1.00 19.33  ? 234 CYS A CA  1 
ATOM 1865 C C   . CYS A 1 234 ? 67.200 60.389  169.881 1.00 17.68  ? 234 CYS A C   1 
ATOM 1866 O O   . CYS A 1 234 ? 66.361 61.003  170.548 1.00 17.26  ? 234 CYS A O   1 
ATOM 1867 C CB  . CYS A 1 234 ? 67.365 58.245  168.614 1.00 19.27  ? 234 CYS A CB  1 
ATOM 1868 S SG  . CYS A 1 234 ? 66.557 57.018  169.641 1.00 16.87  ? 234 CYS A SG  1 
ATOM 1869 N N   . THR A 1 235 ? 68.477 60.309  170.199 1.00 15.37  ? 235 THR A N   1 
ATOM 1870 C CA  . THR A 1 235 ? 69.027 60.946  171.349 1.00 14.57  ? 235 THR A CA  1 
ATOM 1871 C C   . THR A 1 235 ? 68.406 62.325  171.501 1.00 14.05  ? 235 THR A C   1 
ATOM 1872 O O   . THR A 1 235 ? 67.556 62.534  172.369 1.00 13.02  ? 235 THR A O   1 
ATOM 1873 C CB  . THR A 1 235 ? 70.528 61.022  171.153 1.00 14.35  ? 235 THR A CB  1 
ATOM 1874 O OG1 . THR A 1 235 ? 71.022 59.693  170.981 1.00 13.81  ? 235 THR A OG1 1 
ATOM 1875 C CG2 . THR A 1 235 ? 71.206 61.651  172.326 1.00 14.93  ? 235 THR A CG2 1 
ATOM 1876 N N   . TYR A 1 236 ? 68.786 63.244  170.615 1.00 14.21  ? 236 TYR A N   1 
ATOM 1877 C CA  . TYR A 1 236 ? 68.304 64.631  170.671 1.00 14.93  ? 236 TYR A CA  1 
ATOM 1878 C C   . TYR A 1 236 ? 66.812 64.771  170.763 1.00 15.56  ? 236 TYR A C   1 
ATOM 1879 O O   . TYR A 1 236 ? 66.304 65.532  171.576 1.00 16.26  ? 236 TYR A O   1 
ATOM 1880 C CB  . TYR A 1 236 ? 68.784 65.450  169.474 1.00 14.21  ? 236 TYR A CB  1 
ATOM 1881 C CG  . TYR A 1 236 ? 68.350 66.896  169.525 1.00 13.35  ? 236 TYR A CG  1 
ATOM 1882 C CD1 . TYR A 1 236 ? 69.000 67.819  170.338 1.00 11.76  ? 236 TYR A CD1 1 
ATOM 1883 C CD2 . TYR A 1 236 ? 67.303 67.339  168.739 1.00 13.13  ? 236 TYR A CD2 1 
ATOM 1884 C CE1 . TYR A 1 236 ? 68.614 69.143  170.350 1.00 12.40  ? 236 TYR A CE1 1 
ATOM 1885 C CE2 . TYR A 1 236 ? 66.913 68.657  168.748 1.00 13.40  ? 236 TYR A CE2 1 
ATOM 1886 C CZ  . TYR A 1 236 ? 67.569 69.551  169.548 1.00 13.00  ? 236 TYR A CZ  1 
ATOM 1887 O OH  . TYR A 1 236 ? 67.185 70.859  169.511 1.00 13.30  ? 236 TYR A OH  1 
ATOM 1888 N N   . ASP A 1 237 ? 66.093 64.064  169.920 1.00 15.25  ? 237 ASP A N   1 
ATOM 1889 C CA  . ASP A 1 237 ? 64.665 64.166  170.004 1.00 16.13  ? 237 ASP A CA  1 
ATOM 1890 C C   . ASP A 1 237 ? 64.209 63.755  171.405 1.00 16.03  ? 237 ASP A C   1 
ATOM 1891 O O   . ASP A 1 237 ? 63.620 64.566  172.129 1.00 16.97  ? 237 ASP A O   1 
ATOM 1892 C CB  . ASP A 1 237 ? 64.031 63.311  168.911 1.00 17.92  ? 237 ASP A CB  1 
ATOM 1893 C CG  . ASP A 1 237 ? 64.125 63.969  167.554 1.00 20.14  ? 237 ASP A CG  1 
ATOM 1894 O OD1 . ASP A 1 237 ? 65.140 64.658  167.321 1.00 22.10  ? 237 ASP A OD1 1 
ATOM 1895 O OD2 . ASP A 1 237 ? 63.211 63.804  166.717 1.00 19.50  ? 237 ASP A OD2 1 
ATOM 1896 N N   . VAL A 1 238 ? 64.507 62.529  171.818 1.00 15.06  ? 238 VAL A N   1 
ATOM 1897 C CA  . VAL A 1 238 ? 64.085 62.112  173.142 1.00 14.24  ? 238 VAL A CA  1 
ATOM 1898 C C   . VAL A 1 238 ? 64.197 63.292  174.060 1.00 13.39  ? 238 VAL A C   1 
ATOM 1899 O O   . VAL A 1 238 ? 63.224 63.776  174.612 1.00 12.57  ? 238 VAL A O   1 
ATOM 1900 C CB  . VAL A 1 238 ? 64.964 61.032  173.699 1.00 14.57  ? 238 VAL A CB  1 
ATOM 1901 C CG1 . VAL A 1 238 ? 64.637 60.838  175.136 1.00 14.95  ? 238 VAL A CG1 1 
ATOM 1902 C CG2 . VAL A 1 238 ? 64.708 59.756  172.975 1.00 15.91  ? 238 VAL A CG2 1 
ATOM 1903 N N   . PHE A 1 239 ? 65.421 63.749  174.191 1.00 13.46  ? 239 PHE A N   1 
ATOM 1904 C CA  . PHE A 1 239 ? 65.735 64.884  175.009 1.00 15.19  ? 239 PHE A CA  1 
ATOM 1905 C C   . PHE A 1 239 ? 64.673 65.986  174.854 1.00 17.05  ? 239 PHE A C   1 
ATOM 1906 O O   . PHE A 1 239 ? 63.860 66.181  175.746 1.00 18.06  ? 239 PHE A O   1 
ATOM 1907 C CB  . PHE A 1 239 ? 67.129 65.331  174.600 1.00 14.11  ? 239 PHE A CB  1 
ATOM 1908 C CG  . PHE A 1 239 ? 67.591 66.577  175.241 1.00 13.12  ? 239 PHE A CG  1 
ATOM 1909 C CD1 . PHE A 1 239 ? 66.821 67.704  175.230 1.00 12.30  ? 239 PHE A CD1 1 
ATOM 1910 C CD2 . PHE A 1 239 ? 68.851 66.658  175.763 1.00 12.58  ? 239 PHE A CD2 1 
ATOM 1911 C CE1 . PHE A 1 239 ? 67.300 68.885  175.719 1.00 12.80  ? 239 PHE A CE1 1 
ATOM 1912 C CE2 . PHE A 1 239 ? 69.332 67.856  176.258 1.00 12.42  ? 239 PHE A CE2 1 
ATOM 1913 C CZ  . PHE A 1 239 ? 68.562 68.961  176.233 1.00 12.86  ? 239 PHE A CZ  1 
ATOM 1914 N N   . ASP A 1 240 ? 64.667 66.688  173.725 1.00 18.50  ? 240 ASP A N   1 
ATOM 1915 C CA  . ASP A 1 240 ? 63.712 67.768  173.488 1.00 20.01  ? 240 ASP A CA  1 
ATOM 1916 C C   . ASP A 1 240 ? 62.284 67.405  173.817 1.00 20.46  ? 240 ASP A C   1 
ATOM 1917 O O   . ASP A 1 240 ? 61.475 68.270  174.114 1.00 20.85  ? 240 ASP A O   1 
ATOM 1918 C CB  . ASP A 1 240 ? 63.761 68.230  172.025 1.00 20.65  ? 240 ASP A CB  1 
ATOM 1919 C CG  . ASP A 1 240 ? 62.766 69.347  171.721 1.00 21.44  ? 240 ASP A CG  1 
ATOM 1920 O OD1 . ASP A 1 240 ? 62.677 70.302  172.513 1.00 22.02  ? 240 ASP A OD1 1 
ATOM 1921 O OD2 . ASP A 1 240 ? 62.078 69.285  170.679 1.00 21.48  ? 240 ASP A OD2 1 
ATOM 1922 N N   . GLN A 1 241 ? 61.954 66.129  173.794 1.00 21.82  ? 241 GLN A N   1 
ATOM 1923 C CA  . GLN A 1 241 ? 60.566 65.778  174.042 1.00 23.57  ? 241 GLN A CA  1 
ATOM 1924 C C   . GLN A 1 241 ? 60.110 65.898  175.479 1.00 23.97  ? 241 GLN A C   1 
ATOM 1925 O O   . GLN A 1 241 ? 58.914 65.864  175.757 1.00 23.62  ? 241 GLN A O   1 
ATOM 1926 C CB  . GLN A 1 241 ? 60.288 64.363  173.549 1.00 25.25  ? 241 GLN A CB  1 
ATOM 1927 C CG  . GLN A 1 241 ? 60.190 63.325  174.647 1.00 26.93  ? 241 GLN A CG  1 
ATOM 1928 C CD  . GLN A 1 241 ? 60.335 61.925  174.114 1.00 28.15  ? 241 GLN A CD  1 
ATOM 1929 O OE1 . GLN A 1 241 ? 59.473 61.424  173.391 1.00 28.03  ? 241 GLN A OE1 1 
ATOM 1930 N NE2 . GLN A 1 241 ? 61.447 61.285  174.457 1.00 28.10  ? 241 GLN A NE2 1 
ATOM 1931 N N   . GLN A 1 242 ? 61.052 66.032  176.399 1.00 24.84  ? 242 GLN A N   1 
ATOM 1932 C CA  . GLN A 1 242 ? 60.692 66.121  177.814 1.00 25.78  ? 242 GLN A CA  1 
ATOM 1933 C C   . GLN A 1 242 ? 61.517 67.198  178.448 1.00 24.22  ? 242 GLN A C   1 
ATOM 1934 O O   . GLN A 1 242 ? 61.372 67.520  179.615 1.00 22.31  ? 242 GLN A O   1 
ATOM 1935 C CB  . GLN A 1 242 ? 60.986 64.785  178.489 1.00 28.37  ? 242 GLN A CB  1 
ATOM 1936 C CG  . GLN A 1 242 ? 60.464 64.596  179.887 1.00 30.79  ? 242 GLN A CG  1 
ATOM 1937 C CD  . GLN A 1 242 ? 60.273 63.120  180.192 1.00 32.53  ? 242 GLN A CD  1 
ATOM 1938 O OE1 . GLN A 1 242 ? 60.044 62.735  181.330 1.00 33.67  ? 242 GLN A OE1 1 
ATOM 1939 N NE2 . GLN A 1 242 ? 60.356 62.285  179.160 1.00 32.30  ? 242 GLN A NE2 1 
ATOM 1940 N N   . PHE A 1 243 ? 62.408 67.738  177.647 1.00 23.83  ? 243 PHE A N   1 
ATOM 1941 C CA  . PHE A 1 243 ? 63.276 68.772  178.106 1.00 23.94  ? 243 PHE A CA  1 
ATOM 1942 C C   . PHE A 1 243 ? 62.447 69.815  178.768 1.00 21.88  ? 243 PHE A C   1 
ATOM 1943 O O   . PHE A 1 243 ? 62.745 70.232  179.869 1.00 23.04  ? 243 PHE A O   1 
ATOM 1944 C CB  . PHE A 1 243 ? 64.007 69.377  176.937 1.00 27.30  ? 243 PHE A CB  1 
ATOM 1945 C CG  . PHE A 1 243 ? 64.670 70.680  177.244 1.00 31.76  ? 243 PHE A CG  1 
ATOM 1946 C CD1 . PHE A 1 243 ? 65.903 70.728  177.899 1.00 33.83  ? 243 PHE A CD1 1 
ATOM 1947 C CD2 . PHE A 1 243 ? 64.072 71.865  176.855 1.00 32.49  ? 243 PHE A CD2 1 
ATOM 1948 C CE1 . PHE A 1 243 ? 66.536 71.945  178.159 1.00 35.00  ? 243 PHE A CE1 1 
ATOM 1949 C CE2 . PHE A 1 243 ? 64.690 73.081  177.109 1.00 34.94  ? 243 PHE A CE2 1 
ATOM 1950 C CZ  . PHE A 1 243 ? 65.928 73.121  177.763 1.00 35.85  ? 243 PHE A CZ  1 
ATOM 1951 N N   . ALA A 1 244 ? 61.395 70.245  178.103 1.00 18.97  ? 244 ALA A N   1 
ATOM 1952 C CA  . ALA A 1 244 ? 60.538 71.267  178.680 1.00 16.39  ? 244 ALA A CA  1 
ATOM 1953 C C   . ALA A 1 244 ? 60.258 71.132  180.203 1.00 14.24  ? 244 ALA A C   1 
ATOM 1954 O O   . ALA A 1 244 ? 60.651 71.987  181.014 1.00 12.61  ? 244 ALA A O   1 
ATOM 1955 C CB  . ALA A 1 244 ? 59.244 71.305  177.910 1.00 17.15  ? 244 ALA A CB  1 
ATOM 1956 N N   . ASN A 1 245 ? 59.570 70.065  180.595 1.00 11.79  ? 245 ASN A N   1 
ATOM 1957 C CA  . ASN A 1 245 ? 59.232 69.869  182.002 1.00 9.06   ? 245 ASN A CA  1 
ATOM 1958 C C   . ASN A 1 245 ? 60.394 70.328  182.860 1.00 7.33   ? 245 ASN A C   1 
ATOM 1959 O O   . ASN A 1 245 ? 60.232 71.023  183.842 1.00 5.58   ? 245 ASN A O   1 
ATOM 1960 C CB  . ASN A 1 245 ? 58.907 68.400  182.272 1.00 10.75  ? 245 ASN A CB  1 
ATOM 1961 C CG  . ASN A 1 245 ? 57.433 68.085  182.079 1.00 11.60  ? 245 ASN A CG  1 
ATOM 1962 O OD1 . ASN A 1 245 ? 56.617 68.980  181.885 1.00 12.90  ? 245 ASN A OD1 1 
ATOM 1963 N ND2 . ASN A 1 245 ? 57.086 66.809  182.145 1.00 11.50  ? 245 ASN A ND2 1 
ATOM 1964 N N   . PHE A 1 246 ? 61.581 69.940  182.456 1.00 6.16   ? 246 PHE A N   1 
ATOM 1965 C CA  . PHE A 1 246 ? 62.778 70.308  183.157 1.00 5.89   ? 246 PHE A CA  1 
ATOM 1966 C C   . PHE A 1 246 ? 62.905 71.807  183.211 1.00 5.87   ? 246 PHE A C   1 
ATOM 1967 O O   . PHE A 1 246 ? 63.135 72.390  184.256 1.00 4.86   ? 246 PHE A O   1 
ATOM 1968 C CB  . PHE A 1 246 ? 63.934 69.704  182.405 1.00 5.41   ? 246 PHE A CB  1 
ATOM 1969 C CG  . PHE A 1 246 ? 65.236 70.293  182.723 1.00 5.76   ? 246 PHE A CG  1 
ATOM 1970 C CD1 . PHE A 1 246 ? 65.478 71.640  182.548 1.00 5.61   ? 246 PHE A CD1 1 
ATOM 1971 C CD2 . PHE A 1 246 ? 66.267 69.472  183.094 1.00 7.24   ? 246 PHE A CD2 1 
ATOM 1972 C CE1 . PHE A 1 246 ? 66.717 72.162  182.760 1.00 6.86   ? 246 PHE A CE1 1 
ATOM 1973 C CE2 . PHE A 1 246 ? 67.516 69.984  183.310 1.00 8.94   ? 246 PHE A CE2 1 
ATOM 1974 C CZ  . PHE A 1 246 ? 67.750 71.326  183.131 1.00 8.56   ? 246 PHE A CZ  1 
ATOM 1975 N N   . PHE A 1 247 ? 62.800 72.418  182.047 1.00 6.91   ? 247 PHE A N   1 
ATOM 1976 C CA  . PHE A 1 247 ? 62.903 73.861  181.866 1.00 9.11   ? 247 PHE A CA  1 
ATOM 1977 C C   . PHE A 1 247 ? 61.948 74.480  182.860 1.00 9.60   ? 247 PHE A C   1 
ATOM 1978 O O   . PHE A 1 247 ? 62.216 75.518  183.449 1.00 7.42   ? 247 PHE A O   1 
ATOM 1979 C CB  . PHE A 1 247 ? 62.496 74.190  180.412 1.00 10.48  ? 247 PHE A CB  1 
ATOM 1980 C CG  . PHE A 1 247 ? 62.497 75.672  180.059 1.00 11.74  ? 247 PHE A CG  1 
ATOM 1981 C CD1 . PHE A 1 247 ? 61.376 76.432  180.206 1.00 12.06  ? 247 PHE A CD1 1 
ATOM 1982 C CD2 . PHE A 1 247 ? 63.608 76.286  179.534 1.00 11.89  ? 247 PHE A CD2 1 
ATOM 1983 C CE1 . PHE A 1 247 ? 61.369 77.773  179.813 1.00 12.41  ? 247 PHE A CE1 1 
ATOM 1984 C CE2 . PHE A 1 247 ? 63.601 77.630  179.144 1.00 12.26  ? 247 PHE A CE2 1 
ATOM 1985 C CZ  . PHE A 1 247 ? 62.490 78.363  179.286 1.00 12.18  ? 247 PHE A CZ  1 
ATOM 1986 N N   . THR A 1 248 ? 60.852 73.780  183.091 1.00 11.96  ? 248 THR A N   1 
ATOM 1987 C CA  . THR A 1 248 ? 59.845 74.290  183.992 1.00 14.77  ? 248 THR A CA  1 
ATOM 1988 C C   . THR A 1 248 ? 60.197 74.290  185.481 1.00 16.97  ? 248 THR A C   1 
ATOM 1989 O O   . THR A 1 248 ? 59.524 74.935  186.293 1.00 17.16  ? 248 THR A O   1 
ATOM 1990 C CB  . THR A 1 248 ? 58.557 73.556  183.745 1.00 14.44  ? 248 THR A CB  1 
ATOM 1991 O OG1 . THR A 1 248 ? 58.262 73.645  182.349 1.00 11.69  ? 248 THR A OG1 1 
ATOM 1992 C CG2 . THR A 1 248 ? 57.422 74.173  184.543 1.00 14.27  ? 248 THR A CG2 1 
ATOM 1993 N N   . SER A 1 249 ? 61.244 73.565  185.849 1.00 19.12  ? 249 SER A N   1 
ATOM 1994 C CA  . SER A 1 249 ? 61.649 73.553  187.236 1.00 20.72  ? 249 SER A CA  1 
ATOM 1995 C C   . SER A 1 249 ? 62.277 74.907  187.544 1.00 21.55  ? 249 SER A C   1 
ATOM 1996 O O   . SER A 1 249 ? 62.018 75.483  188.582 1.00 21.51  ? 249 SER A O   1 
ATOM 1997 C CB  . SER A 1 249 ? 62.655 72.428  187.494 1.00 21.24  ? 249 SER A CB  1 
ATOM 1998 O OG  . SER A 1 249 ? 62.001 71.247  187.934 1.00 22.24  ? 249 SER A OG  1 
ATOM 1999 N N   . PHE A 1 250 ? 63.060 75.431  186.610 1.00 22.79  ? 250 PHE A N   1 
ATOM 2000 C CA  . PHE A 1 250 ? 63.763 76.693  186.794 1.00 25.01  ? 250 PHE A CA  1 
ATOM 2001 C C   . PHE A 1 250 ? 63.011 77.987  186.980 1.00 28.01  ? 250 PHE A C   1 
ATOM 2002 O O   . PHE A 1 250 ? 63.626 79.043  186.953 1.00 27.48  ? 250 PHE A O   1 
ATOM 2003 C CB  . PHE A 1 250 ? 64.739 76.900  185.651 1.00 23.56  ? 250 PHE A CB  1 
ATOM 2004 C CG  . PHE A 1 250 ? 65.872 75.936  185.654 1.00 23.39  ? 250 PHE A CG  1 
ATOM 2005 C CD1 . PHE A 1 250 ? 65.629 74.582  185.695 1.00 22.74  ? 250 PHE A CD1 1 
ATOM 2006 C CD2 . PHE A 1 250 ? 67.191 76.380  185.605 1.00 23.20  ? 250 PHE A CD2 1 
ATOM 2007 C CE1 . PHE A 1 250 ? 66.674 73.680  185.684 1.00 22.92  ? 250 PHE A CE1 1 
ATOM 2008 C CE2 . PHE A 1 250 ? 68.251 75.475  185.592 1.00 22.48  ? 250 PHE A CE2 1 
ATOM 2009 C CZ  . PHE A 1 250 ? 67.988 74.124  185.633 1.00 22.40  ? 250 PHE A CZ  1 
ATOM 2010 N N   . PHE A 1 251 ? 61.705 77.961  187.171 1.00 32.13  ? 251 PHE A N   1 
ATOM 2011 C CA  . PHE A 1 251 ? 61.058 79.251  187.328 1.00 37.63  ? 251 PHE A CA  1 
ATOM 2012 C C   . PHE A 1 251 ? 60.451 79.698  188.590 1.00 40.08  ? 251 PHE A C   1 
ATOM 2013 O O   . PHE A 1 251 ? 60.263 78.934  189.501 1.00 42.29  ? 251 PHE A O   1 
ATOM 2014 C CB  . PHE A 1 251 ? 60.054 79.477  186.253 1.00 39.27  ? 251 PHE A CB  1 
ATOM 2015 C CG  . PHE A 1 251 ? 60.681 79.761  184.994 1.00 42.06  ? 251 PHE A CG  1 
ATOM 2016 C CD1 . PHE A 1 251 ? 61.152 78.725  184.223 1.00 43.85  ? 251 PHE A CD1 1 
ATOM 2017 C CD2 . PHE A 1 251 ? 60.865 81.061  184.590 1.00 42.64  ? 251 PHE A CD2 1 
ATOM 2018 C CE1 . PHE A 1 251 ? 61.815 78.973  183.064 1.00 45.87  ? 251 PHE A CE1 1 
ATOM 2019 C CE2 . PHE A 1 251 ? 61.529 81.330  183.434 1.00 44.62  ? 251 PHE A CE2 1 
ATOM 2020 C CZ  . PHE A 1 251 ? 62.004 80.283  182.655 1.00 45.73  ? 251 PHE A CZ  1 
ATOM 2021 N N   . ALA A 1 252 ? 60.116 80.975  188.624 1.00 43.52  ? 252 ALA A N   1 
ATOM 2022 C CA  . ALA A 1 252 ? 59.563 81.554  189.825 1.00 47.05  ? 252 ALA A CA  1 
ATOM 2023 C C   . ALA A 1 252 ? 58.372 80.766  190.285 1.00 49.44  ? 252 ALA A C   1 
ATOM 2024 O O   . ALA A 1 252 ? 58.166 80.569  191.490 1.00 50.60  ? 252 ALA A O   1 
ATOM 2025 C CB  . ALA A 1 252 ? 59.186 82.978  189.572 1.00 47.11  ? 252 ALA A CB  1 
ATOM 2026 N N   . THR A 1 253 ? 57.602 80.300  189.306 1.00 51.91  ? 253 THR A N   1 
ATOM 2027 C CA  . THR A 1 253 ? 56.404 79.517  189.567 1.00 54.55  ? 253 THR A CA  1 
ATOM 2028 C C   . THR A 1 253 ? 55.975 78.743  188.344 1.00 54.98  ? 253 THR A C   1 
ATOM 2029 O O   . THR A 1 253 ? 56.308 79.094  187.210 1.00 54.26  ? 253 THR A O   1 
ATOM 2030 C CB  . THR A 1 253 ? 55.253 80.416  189.975 1.00 55.67  ? 253 THR A CB  1 
ATOM 2031 O OG1 . THR A 1 253 ? 55.632 81.178  191.130 1.00 56.83  ? 253 THR A OG1 1 
ATOM 2032 C CG2 . THR A 1 253 ? 54.024 79.576  190.321 1.00 55.76  ? 253 THR A CG2 1 
ATOM 2033 N N   . GLY A 1 254 ? 55.218 77.684  188.618 1.00 56.39  ? 254 GLY A N   1 
ATOM 2034 C CA  . GLY A 1 254 ? 54.693 76.816  187.581 1.00 58.58  ? 254 GLY A CA  1 
ATOM 2035 C C   . GLY A 1 254 ? 54.065 77.684  186.505 1.00 59.03  ? 254 GLY A C   1 
ATOM 2036 O O   . GLY A 1 254 ? 54.328 77.507  185.315 1.00 58.11  ? 254 GLY A O   1 
ATOM 2037 N N   . GLU A 1 255 ? 53.235 78.626  186.957 1.00 60.23  ? 255 GLU A N   1 
ATOM 2038 C CA  . GLU A 1 255 ? 52.547 79.552  186.087 1.00 61.60  ? 255 GLU A CA  1 
ATOM 2039 C C   . GLU A 1 255 ? 53.555 80.287  185.165 1.00 60.48  ? 255 GLU A C   1 
ATOM 2040 O O   . GLU A 1 255 ? 53.498 80.126  183.946 1.00 60.40  ? 255 GLU A O   1 
ATOM 2041 C CB  . GLU A 1 255 ? 51.687 80.554  186.920 1.00 63.72  ? 255 GLU A CB  1 
ATOM 2042 C CG  . GLU A 1 255 ? 50.434 81.190  186.190 1.00 67.06  ? 255 GLU A CG  1 
ATOM 2043 C CD  . GLU A 1 255 ? 49.325 81.736  187.125 1.00 67.74  ? 255 GLU A CD  1 
ATOM 2044 O OE1 . GLU A 1 255 ? 49.438 81.543  188.355 1.00 68.24  ? 255 GLU A OE1 1 
ATOM 2045 O OE2 . GLU A 1 255 ? 48.331 82.345  186.628 1.00 67.55  ? 255 GLU A OE2 1 
ATOM 2046 N N   . GLN A 1 256 ? 54.500 81.051  185.719 1.00 59.34  ? 256 GLN A N   1 
ATOM 2047 C CA  . GLN A 1 256 ? 55.458 81.807  184.888 1.00 57.59  ? 256 GLN A CA  1 
ATOM 2048 C C   . GLN A 1 256 ? 56.352 80.940  184.024 1.00 55.54  ? 256 GLN A C   1 
ATOM 2049 O O   . GLN A 1 256 ? 56.679 81.296  182.886 1.00 55.84  ? 256 GLN A O   1 
ATOM 2050 C CB  . GLN A 1 256 ? 56.362 82.725  185.737 1.00 58.93  ? 256 GLN A CB  1 
ATOM 2051 C CG  . GLN A 1 256 ? 57.231 83.719  184.904 1.00 60.56  ? 256 GLN A CG  1 
ATOM 2052 C CD  . GLN A 1 256 ? 56.404 84.831  184.201 1.00 61.74  ? 256 GLN A CD  1 
ATOM 2053 O OE1 . GLN A 1 256 ? 55.177 84.726  184.089 1.00 62.41  ? 256 GLN A OE1 1 
ATOM 2054 N NE2 . GLN A 1 256 ? 57.084 85.891  183.724 1.00 61.37  ? 256 GLN A NE2 1 
ATOM 2055 N N   . GLY A 1 257 ? 56.776 79.810  184.564 1.00 52.99  ? 257 GLY A N   1 
ATOM 2056 C CA  . GLY A 1 257 ? 57.620 78.939  183.773 1.00 50.87  ? 257 GLY A CA  1 
ATOM 2057 C C   . GLY A 1 257 ? 56.988 78.738  182.414 1.00 48.43  ? 257 GLY A C   1 
ATOM 2058 O O   . GLY A 1 257 ? 57.478 79.226  181.393 1.00 48.22  ? 257 GLY A O   1 
ATOM 2059 N N   . THR A 1 258 ? 55.871 78.028  182.423 1.00 46.39  ? 258 THR A N   1 
ATOM 2060 C CA  . THR A 1 258 ? 55.120 77.735  181.216 1.00 44.47  ? 258 THR A CA  1 
ATOM 2061 C C   . THR A 1 258 ? 55.128 78.903  180.232 1.00 44.11  ? 258 THR A C   1 
ATOM 2062 O O   . THR A 1 258 ? 55.444 78.726  179.065 1.00 43.69  ? 258 THR A O   1 
ATOM 2063 C CB  . THR A 1 258 ? 53.673 77.392  181.578 1.00 44.26  ? 258 THR A CB  1 
ATOM 2064 O OG1 . THR A 1 258 ? 53.669 76.409  182.624 1.00 42.80  ? 258 THR A OG1 1 
ATOM 2065 C CG2 . THR A 1 258 ? 52.940 76.852  180.362 1.00 43.86  ? 258 THR A CG2 1 
ATOM 2066 N N   . ARG A 1 259 ? 54.779 80.094  180.710 1.00 44.18  ? 259 ARG A N   1 
ATOM 2067 C CA  . ARG A 1 259 ? 54.756 81.283  179.865 1.00 44.12  ? 259 ARG A CA  1 
ATOM 2068 C C   . ARG A 1 259 ? 56.021 81.330  179.045 1.00 42.96  ? 259 ARG A C   1 
ATOM 2069 O O   . ARG A 1 259 ? 55.981 81.265  177.831 1.00 42.46  ? 259 ARG A O   1 
ATOM 2070 C CB  . ARG A 1 259 ? 54.711 82.561  180.704 1.00 46.67  ? 259 ARG A CB  1 
ATOM 2071 C CG  . ARG A 1 259 ? 53.353 82.999  181.284 1.00 49.28  ? 259 ARG A CG  1 
ATOM 2072 C CD  . ARG A 1 259 ? 53.533 84.339  182.034 1.00 50.76  ? 259 ARG A CD  1 
ATOM 2073 N NE  . ARG A 1 259 ? 52.312 84.872  182.627 1.00 52.10  ? 259 ARG A NE  1 
ATOM 2074 C CZ  . ARG A 1 259 ? 52.242 86.067  183.207 1.00 53.30  ? 259 ARG A CZ  1 
ATOM 2075 N NH1 . ARG A 1 259 ? 53.330 86.835  183.265 1.00 52.85  ? 259 ARG A NH1 1 
ATOM 2076 N NH2 . ARG A 1 259 ? 51.087 86.502  183.715 1.00 54.09  ? 259 ARG A NH2 1 
ATOM 2077 N N   . VAL A 1 260 ? 57.143 81.462  179.731 1.00 42.04  ? 260 VAL A N   1 
ATOM 2078 C CA  . VAL A 1 260 ? 58.425 81.545  179.075 1.00 41.82  ? 260 VAL A CA  1 
ATOM 2079 C C   . VAL A 1 260 ? 58.497 80.593  177.915 1.00 41.85  ? 260 VAL A C   1 
ATOM 2080 O O   . VAL A 1 260 ? 58.806 80.977  176.780 1.00 42.51  ? 260 VAL A O   1 
ATOM 2081 C CB  . VAL A 1 260 ? 59.541 81.200  180.044 1.00 40.88  ? 260 VAL A CB  1 
ATOM 2082 C CG1 . VAL A 1 260 ? 60.907 81.260  179.358 1.00 40.34  ? 260 VAL A CG1 1 
ATOM 2083 C CG2 . VAL A 1 260 ? 59.460 82.142  181.202 1.00 40.74  ? 260 VAL A CG2 1 
ATOM 2084 N N   . PHE A 1 261 ? 58.198 79.337  178.185 1.00 41.88  ? 261 PHE A N   1 
ATOM 2085 C CA  . PHE A 1 261 ? 58.280 78.384  177.114 1.00 41.96  ? 261 PHE A CA  1 
ATOM 2086 C C   . PHE A 1 261 ? 57.571 78.994  175.888 1.00 41.27  ? 261 PHE A C   1 
ATOM 2087 O O   . PHE A 1 261 ? 58.172 79.135  174.822 1.00 40.71  ? 261 PHE A O   1 
ATOM 2088 C CB  . PHE A 1 261 ? 57.675 77.038  177.555 1.00 42.32  ? 261 PHE A CB  1 
ATOM 2089 C CG  . PHE A 1 261 ? 58.320 75.856  176.897 1.00 42.55  ? 261 PHE A CG  1 
ATOM 2090 C CD1 . PHE A 1 261 ? 59.714 75.735  176.838 1.00 43.42  ? 261 PHE A CD1 1 
ATOM 2091 C CD2 . PHE A 1 261 ? 57.547 74.919  176.266 1.00 42.49  ? 261 PHE A CD2 1 
ATOM 2092 C CE1 . PHE A 1 261 ? 60.311 74.695  176.139 1.00 43.91  ? 261 PHE A CE1 1 
ATOM 2093 C CE2 . PHE A 1 261 ? 58.128 73.883  175.570 1.00 44.49  ? 261 PHE A CE2 1 
ATOM 2094 C CZ  . PHE A 1 261 ? 59.512 73.768  175.502 1.00 44.72  ? 261 PHE A CZ  1 
ATOM 2095 N N   . GLY A 1 262 ? 56.334 79.437  176.095 1.00 40.98  ? 262 GLY A N   1 
ATOM 2096 C CA  . GLY A 1 262 ? 55.545 80.038  175.037 1.00 40.43  ? 262 GLY A CA  1 
ATOM 2097 C C   . GLY A 1 262 ? 56.266 81.118  174.263 1.00 39.73  ? 262 GLY A C   1 
ATOM 2098 O O   . GLY A 1 262 ? 56.277 81.137  173.029 1.00 39.77  ? 262 GLY A O   1 
ATOM 2099 N N   . TYR A 1 263 ? 56.860 82.042  174.992 1.00 39.31  ? 263 TYR A N   1 
ATOM 2100 C CA  . TYR A 1 263 ? 57.597 83.090  174.351 1.00 39.37  ? 263 TYR A CA  1 
ATOM 2101 C C   . TYR A 1 263 ? 58.636 82.400  173.500 1.00 38.14  ? 263 TYR A C   1 
ATOM 2102 O O   . TYR A 1 263 ? 58.574 82.452  172.276 1.00 38.54  ? 263 TYR A O   1 
ATOM 2103 C CB  . TYR A 1 263 ? 58.238 83.964  175.405 1.00 40.69  ? 263 TYR A CB  1 
ATOM 2104 C CG  . TYR A 1 263 ? 57.209 84.695  176.216 1.00 42.93  ? 263 TYR A CG  1 
ATOM 2105 C CD1 . TYR A 1 263 ? 56.154 84.015  176.804 1.00 43.42  ? 263 TYR A CD1 1 
ATOM 2106 C CD2 . TYR A 1 263 ? 57.268 86.066  176.372 1.00 43.37  ? 263 TYR A CD2 1 
ATOM 2107 C CE1 . TYR A 1 263 ? 55.179 84.683  177.527 1.00 44.56  ? 263 TYR A CE1 1 
ATOM 2108 C CE2 . TYR A 1 263 ? 56.295 86.745  177.096 1.00 44.31  ? 263 TYR A CE2 1 
ATOM 2109 C CZ  . TYR A 1 263 ? 55.254 86.042  177.667 1.00 44.65  ? 263 TYR A CZ  1 
ATOM 2110 O OH  . TYR A 1 263 ? 54.279 86.686  178.382 1.00 45.28  ? 263 TYR A OH  1 
ATOM 2111 N N   . VAL A 1 264 ? 59.566 81.720  174.155 1.00 37.00  ? 264 VAL A N   1 
ATOM 2112 C CA  . VAL A 1 264 ? 60.633 81.012  173.463 1.00 36.98  ? 264 VAL A CA  1 
ATOM 2113 C C   . VAL A 1 264 ? 60.202 80.462  172.122 1.00 36.31  ? 264 VAL A C   1 
ATOM 2114 O O   . VAL A 1 264 ? 60.426 81.071  171.076 1.00 35.98  ? 264 VAL A O   1 
ATOM 2115 C CB  . VAL A 1 264 ? 61.148 79.830  174.289 1.00 37.36  ? 264 VAL A CB  1 
ATOM 2116 C CG1 . VAL A 1 264 ? 62.277 79.094  173.534 1.00 37.35  ? 264 VAL A CG1 1 
ATOM 2117 C CG2 . VAL A 1 264 ? 61.615 80.330  175.631 1.00 38.29  ? 264 VAL A CG2 1 
ATOM 2118 N N   . THR A 1 265 ? 59.580 79.295  172.160 1.00 36.62  ? 265 THR A N   1 
ATOM 2119 C CA  . THR A 1 265 ? 59.138 78.657  170.942 1.00 37.25  ? 265 THR A CA  1 
ATOM 2120 C C   . THR A 1 265 ? 58.779 79.734  169.952 1.00 36.77  ? 265 THR A C   1 
ATOM 2121 O O   . THR A 1 265 ? 59.435 79.872  168.930 1.00 36.65  ? 265 THR A O   1 
ATOM 2122 C CB  . THR A 1 265 ? 57.936 77.743  171.200 1.00 38.14  ? 265 THR A CB  1 
ATOM 2123 O OG1 . THR A 1 265 ? 58.327 76.712  172.120 1.00 38.88  ? 265 THR A OG1 1 
ATOM 2124 C CG2 . THR A 1 265 ? 57.478 77.092  169.908 1.00 38.44  ? 265 THR A CG2 1 
ATOM 2125 N N   . THR A 1 266 ? 57.779 80.537  170.284 1.00 36.94  ? 266 THR A N   1 
ATOM 2126 C CA  . THR A 1 266 ? 57.366 81.599  169.389 1.00 38.23  ? 266 THR A CA  1 
ATOM 2127 C C   . THR A 1 266 ? 58.496 82.509  168.903 1.00 39.21  ? 266 THR A C   1 
ATOM 2128 O O   . THR A 1 266 ? 58.572 82.803  167.722 1.00 39.72  ? 266 THR A O   1 
ATOM 2129 C CB  . THR A 1 266 ? 56.279 82.473  170.025 1.00 37.71  ? 266 THR A CB  1 
ATOM 2130 O OG1 . THR A 1 266 ? 55.011 81.806  169.968 1.00 38.31  ? 266 THR A OG1 1 
ATOM 2131 C CG2 . THR A 1 266 ? 56.165 83.758  169.287 1.00 37.28  ? 266 THR A CG2 1 
ATOM 2132 N N   . MET A 1 267 ? 59.373 82.957  169.791 1.00 40.61  ? 267 MET A N   1 
ATOM 2133 C CA  . MET A 1 267 ? 60.446 83.870  169.381 1.00 42.58  ? 267 MET A CA  1 
ATOM 2134 C C   . MET A 1 267 ? 61.452 83.115  168.561 1.00 43.42  ? 267 MET A C   1 
ATOM 2135 O O   . MET A 1 267 ? 62.293 83.690  167.854 1.00 43.74  ? 267 MET A O   1 
ATOM 2136 C CB  . MET A 1 267 ? 61.158 84.450  170.590 1.00 44.05  ? 267 MET A CB  1 
ATOM 2137 C CG  . MET A 1 267 ? 62.008 85.690  170.324 1.00 44.80  ? 267 MET A CG  1 
ATOM 2138 S SD  . MET A 1 267 ? 61.027 87.180  170.018 1.00 47.12  ? 267 MET A SD  1 
ATOM 2139 C CE  . MET A 1 267 ? 60.500 87.674  171.662 1.00 44.83  ? 267 MET A CE  1 
ATOM 2140 N N   . GLY A 1 268 ? 61.327 81.800  168.661 1.00 44.42  ? 268 GLY A N   1 
ATOM 2141 C CA  . GLY A 1 268 ? 62.199 80.884  167.960 1.00 46.28  ? 268 GLY A CA  1 
ATOM 2142 C C   . GLY A 1 268 ? 62.099 80.955  166.459 1.00 47.41  ? 268 GLY A C   1 
ATOM 2143 O O   . GLY A 1 268 ? 63.068 81.315  165.797 1.00 47.68  ? 268 GLY A O   1 
ATOM 2144 N N   . GLU A 1 269 ? 60.937 80.627  165.911 1.00 48.47  ? 269 GLU A N   1 
ATOM 2145 C CA  . GLU A 1 269 ? 60.788 80.623  164.462 1.00 49.45  ? 269 GLU A CA  1 
ATOM 2146 C C   . GLU A 1 269 ? 61.326 81.875  163.793 1.00 48.47  ? 269 GLU A C   1 
ATOM 2147 O O   . GLU A 1 269 ? 61.808 81.827  162.664 1.00 48.35  ? 269 GLU A O   1 
ATOM 2148 C CB  . GLU A 1 269 ? 59.322 80.359  164.090 1.00 51.61  ? 269 GLU A CB  1 
ATOM 2149 C CG  . GLU A 1 269 ? 58.814 79.007  164.611 1.00 55.62  ? 269 GLU A CG  1 
ATOM 2150 C CD  . GLU A 1 269 ? 59.687 77.804  164.189 1.00 58.81  ? 269 GLU A CD  1 
ATOM 2151 O OE1 . GLU A 1 269 ? 59.675 77.454  162.982 1.00 61.18  ? 269 GLU A OE1 1 
ATOM 2152 O OE2 . GLU A 1 269 ? 60.379 77.210  165.068 1.00 60.16  ? 269 GLU A OE2 1 
ATOM 2153 N N   . LEU A 1 270 ? 61.270 82.997  164.494 1.00 47.57  ? 270 LEU A N   1 
ATOM 2154 C CA  . LEU A 1 270 ? 61.786 84.221  163.917 1.00 46.95  ? 270 LEU A CA  1 
ATOM 2155 C C   . LEU A 1 270 ? 63.281 84.035  163.707 1.00 46.52  ? 270 LEU A C   1 
ATOM 2156 O O   . LEU A 1 270 ? 63.886 84.693  162.862 1.00 46.40  ? 270 LEU A O   1 
ATOM 2157 C CB  . LEU A 1 270 ? 61.481 85.404  164.827 1.00 46.81  ? 270 LEU A CB  1 
ATOM 2158 C CG  . LEU A 1 270 ? 59.997 85.786  164.862 1.00 46.84  ? 270 LEU A CG  1 
ATOM 2159 C CD1 . LEU A 1 270 ? 59.850 87.038  165.685 1.00 47.44  ? 270 LEU A CD1 1 
ATOM 2160 C CD2 . LEU A 1 270 ? 59.462 86.028  163.459 1.00 45.96  ? 270 LEU A CD2 1 
ATOM 2161 N N   . LEU A 1 271 ? 63.878 83.124  164.461 1.00 46.50  ? 271 LEU A N   1 
ATOM 2162 C CA  . LEU A 1 271 ? 65.294 82.864  164.294 1.00 47.02  ? 271 LEU A CA  1 
ATOM 2163 C C   . LEU A 1 271 ? 65.431 81.888  163.119 1.00 47.79  ? 271 LEU A C   1 
ATOM 2164 O O   . LEU A 1 271 ? 66.266 82.055  162.239 1.00 47.77  ? 271 LEU A O   1 
ATOM 2165 C CB  . LEU A 1 271 ? 65.879 82.268  165.587 1.00 46.20  ? 271 LEU A CB  1 
ATOM 2166 C CG  . LEU A 1 271 ? 67.340 81.761  165.556 1.00 45.50  ? 271 LEU A CG  1 
ATOM 2167 C CD1 . LEU A 1 271 ? 68.208 82.951  165.386 1.00 46.02  ? 271 LEU A CD1 1 
ATOM 2168 C CD2 . LEU A 1 271 ? 67.737 81.053  166.838 1.00 45.19  ? 271 LEU A CD2 1 
ATOM 2169 N N   . ASN A 1 272 ? 64.553 80.901  163.088 1.00 49.27  ? 272 ASN A N   1 
ATOM 2170 C CA  . ASN A 1 272 ? 64.546 79.880  162.047 1.00 51.34  ? 272 ASN A CA  1 
ATOM 2171 C C   . ASN A 1 272 ? 64.732 80.518  160.647 1.00 52.42  ? 272 ASN A C   1 
ATOM 2172 O O   . ASN A 1 272 ? 65.593 80.116  159.851 1.00 51.00  ? 272 ASN A O   1 
ATOM 2173 C CB  . ASN A 1 272 ? 63.206 79.165  162.167 1.00 51.51  ? 272 ASN A CB  1 
ATOM 2174 C CG  . ASN A 1 272 ? 63.182 77.802  161.493 1.00 52.45  ? 272 ASN A CG  1 
ATOM 2175 O OD1 . ASN A 1 272 ? 64.022 76.930  161.762 1.00 52.51  ? 272 ASN A OD1 1 
ATOM 2176 N ND2 . ASN A 1 272 ? 62.188 77.599  160.630 1.00 52.73  ? 272 ASN A ND2 1 
ATOM 2177 N N   . ALA A 1 273 ? 63.916 81.536  160.394 1.00 54.59  ? 273 ALA A N   1 
ATOM 2178 C CA  . ALA A 1 273 ? 63.907 82.251  159.133 1.00 55.90  ? 273 ALA A CA  1 
ATOM 2179 C C   . ALA A 1 273 ? 65.267 82.824  158.846 1.00 56.55  ? 273 ALA A C   1 
ATOM 2180 O O   . ALA A 1 273 ? 65.904 82.479  157.852 1.00 55.13  ? 273 ALA A O   1 
ATOM 2181 C CB  . ALA A 1 273 ? 62.878 83.367  159.167 1.00 56.42  ? 273 ALA A CB  1 
ATOM 2182 N N   . SER A 1 274 ? 65.701 83.721  159.719 1.00 58.19  ? 274 SER A N   1 
ATOM 2183 C CA  . SER A 1 274 ? 66.993 84.335  159.550 1.00 60.20  ? 274 SER A CA  1 
ATOM 2184 C C   . SER A 1 274 ? 67.997 83.250  159.151 1.00 61.62  ? 274 SER A C   1 
ATOM 2185 O O   . SER A 1 274 ? 68.767 83.401  158.195 1.00 61.88  ? 274 SER A O   1 
ATOM 2186 C CB  . SER A 1 274 ? 67.420 85.041  160.847 1.00 59.50  ? 274 SER A CB  1 
ATOM 2187 O OG  . SER A 1 274 ? 67.192 84.212  161.969 1.00 60.59  ? 274 SER A OG  1 
ATOM 2188 N N   . ILE A 1 275 ? 67.962 82.126  159.841 1.00 62.75  ? 275 ILE A N   1 
ATOM 2189 C CA  . ILE A 1 275 ? 68.910 81.096  159.517 1.00 64.70  ? 275 ILE A CA  1 
ATOM 2190 C C   . ILE A 1 275 ? 68.754 80.525  158.113 1.00 65.55  ? 275 ILE A C   1 
ATOM 2191 O O   . ILE A 1 275 ? 69.637 80.691  157.259 1.00 65.78  ? 275 ILE A O   1 
ATOM 2192 C CB  . ILE A 1 275 ? 68.834 79.992  160.535 1.00 65.37  ? 275 ILE A CB  1 
ATOM 2193 C CG1 . ILE A 1 275 ? 68.942 80.616  161.934 1.00 66.56  ? 275 ILE A CG1 1 
ATOM 2194 C CG2 . ILE A 1 275 ? 69.968 79.011  160.297 1.00 66.69  ? 275 ILE A CG2 1 
ATOM 2195 C CD1 . ILE A 1 275 ? 68.725 79.654  163.097 1.00 68.22  ? 275 ILE A CD1 1 
ATOM 2196 N N   . MET A 1 276 ? 67.625 79.882  157.855 1.00 67.08  ? 276 MET A N   1 
ATOM 2197 C CA  . MET A 1 276 ? 67.400 79.262  156.558 1.00 68.29  ? 276 MET A CA  1 
ATOM 2198 C C   . MET A 1 276 ? 67.618 80.160  155.336 1.00 67.89  ? 276 MET A C   1 
ATOM 2199 O O   . MET A 1 276 ? 68.085 79.688  154.288 1.00 67.42  ? 276 MET A O   1 
ATOM 2200 C CB  . MET A 1 276 ? 65.998 78.669  156.545 1.00 70.90  ? 276 MET A CB  1 
ATOM 2201 C CG  . MET A 1 276 ? 65.677 77.870  155.309 1.00 74.37  ? 276 MET A CG  1 
ATOM 2202 S SD  . MET A 1 276 ? 64.078 77.007  155.506 1.00 78.86  ? 276 MET A SD  1 
ATOM 2203 C CE  . MET A 1 276 ? 62.842 78.280  154.799 1.00 77.25  ? 276 MET A CE  1 
ATOM 2204 N N   . PHE A 1 277 ? 67.289 81.445  155.485 1.00 66.96  ? 277 PHE A N   1 
ATOM 2205 C CA  . PHE A 1 277 ? 67.441 82.440  154.420 1.00 65.78  ? 277 PHE A CA  1 
ATOM 2206 C C   . PHE A 1 277 ? 68.911 82.380  153.947 1.00 63.67  ? 277 PHE A C   1 
ATOM 2207 O O   . PHE A 1 277 ? 69.238 82.808  152.844 1.00 63.58  ? 277 PHE A O   1 
ATOM 2208 C CB  . PHE A 1 277 ? 67.104 83.843  154.988 1.00 67.03  ? 277 PHE A CB  1 
ATOM 2209 C CG  . PHE A 1 277 ? 66.813 84.893  153.942 1.00 68.16  ? 277 PHE A CG  1 
ATOM 2210 C CD1 . PHE A 1 277 ? 65.570 84.947  153.308 1.00 68.69  ? 277 PHE A CD1 1 
ATOM 2211 C CD2 . PHE A 1 277 ? 67.791 85.821  153.584 1.00 68.48  ? 277 PHE A CD2 1 
ATOM 2212 C CE1 . PHE A 1 277 ? 65.310 85.914  152.329 1.00 69.15  ? 277 PHE A CE1 1 
ATOM 2213 C CE2 . PHE A 1 277 ? 67.546 86.788  152.611 1.00 69.06  ? 277 PHE A CE2 1 
ATOM 2214 C CZ  . PHE A 1 277 ? 66.305 86.839  151.979 1.00 69.16  ? 277 PHE A CZ  1 
ATOM 2215 N N   . PHE A 1 278 ? 69.777 81.799  154.777 1.00 61.46  ? 278 PHE A N   1 
ATOM 2216 C CA  . PHE A 1 278 ? 71.201 81.718  154.478 1.00 59.03  ? 278 PHE A CA  1 
ATOM 2217 C C   . PHE A 1 278 ? 71.661 80.265  154.354 1.00 57.21  ? 278 PHE A C   1 
ATOM 2218 O O   . PHE A 1 278 ? 72.716 79.960  153.785 1.00 56.81  ? 278 PHE A O   1 
ATOM 2219 C CB  . PHE A 1 278 ? 72.003 82.412  155.587 1.00 58.76  ? 278 PHE A CB  1 
ATOM 2220 C CG  . PHE A 1 278 ? 71.644 83.876  155.810 1.00 58.35  ? 278 PHE A CG  1 
ATOM 2221 C CD1 . PHE A 1 278 ? 70.382 84.404  155.490 1.00 58.40  ? 278 PHE A CD1 1 
ATOM 2222 C CD2 . PHE A 1 278 ? 72.585 84.724  156.375 1.00 57.78  ? 278 PHE A CD2 1 
ATOM 2223 C CE1 . PHE A 1 278 ? 70.083 85.760  155.739 1.00 58.05  ? 278 PHE A CE1 1 
ATOM 2224 C CE2 . PHE A 1 278 ? 72.300 86.068  156.624 1.00 57.60  ? 278 PHE A CE2 1 
ATOM 2225 C CZ  . PHE A 1 278 ? 71.051 86.587  156.308 1.00 57.83  ? 278 PHE A CZ  1 
ATOM 2226 N N   . ALA A 1 279 ? 70.847 79.385  154.916 1.00 54.92  ? 279 ALA A N   1 
ATOM 2227 C CA  . ALA A 1 279 ? 71.091 77.967  154.906 1.00 52.76  ? 279 ALA A CA  1 
ATOM 2228 C C   . ALA A 1 279 ? 71.758 77.476  153.601 1.00 51.21  ? 279 ALA A C   1 
ATOM 2229 O O   . ALA A 1 279 ? 72.948 77.123  153.615 1.00 50.17  ? 279 ALA A O   1 
ATOM 2230 C CB  . ALA A 1 279 ? 69.773 77.247  155.160 1.00 53.93  ? 279 ALA A CB  1 
ATOM 2231 N N   . PRO A 1 280 ? 71.013 77.464  152.465 1.00 49.72  ? 280 PRO A N   1 
ATOM 2232 C CA  . PRO A 1 280 ? 71.551 77.011  151.185 1.00 49.01  ? 280 PRO A CA  1 
ATOM 2233 C C   . PRO A 1 280 ? 72.951 77.447  150.992 1.00 48.62  ? 280 PRO A C   1 
ATOM 2234 O O   . PRO A 1 280 ? 73.862 76.634  150.912 1.00 47.79  ? 280 PRO A O   1 
ATOM 2235 C CB  . PRO A 1 280 ? 70.597 77.664  150.194 1.00 49.17  ? 280 PRO A CB  1 
ATOM 2236 C CG  . PRO A 1 280 ? 69.345 77.402  150.849 1.00 49.58  ? 280 PRO A CG  1 
ATOM 2237 C CD  . PRO A 1 280 ? 69.698 78.080  152.196 1.00 49.66  ? 280 PRO A CD  1 
ATOM 2238 N N   . LEU A 1 281 ? 73.108 78.759  150.930 1.00 48.39  ? 281 LEU A N   1 
ATOM 2239 C CA  . LEU A 1 281 ? 74.421 79.346  150.712 1.00 48.59  ? 281 LEU A CA  1 
ATOM 2240 C C   . LEU A 1 281 ? 75.407 78.696  151.659 1.00 48.13  ? 281 LEU A C   1 
ATOM 2241 O O   . LEU A 1 281 ? 76.402 78.093  151.241 1.00 47.83  ? 281 LEU A O   1 
ATOM 2242 C CB  . LEU A 1 281 ? 74.385 80.860  150.968 1.00 49.58  ? 281 LEU A CB  1 
ATOM 2243 C CG  . LEU A 1 281 ? 73.460 81.821  150.171 1.00 50.35  ? 281 LEU A CG  1 
ATOM 2244 C CD1 . LEU A 1 281 ? 73.764 83.274  150.600 1.00 49.77  ? 281 LEU A CD1 1 
ATOM 2245 C CD2 . LEU A 1 281 ? 73.662 81.668  148.653 1.00 50.25  ? 281 LEU A CD2 1 
ATOM 2246 N N   . ILE A 1 282 ? 75.106 78.833  152.942 1.00 48.12  ? 282 ILE A N   1 
ATOM 2247 C CA  . ILE A 1 282 ? 75.917 78.281  154.001 1.00 48.00  ? 282 ILE A CA  1 
ATOM 2248 C C   . ILE A 1 282 ? 76.342 76.867  153.627 1.00 49.22  ? 282 ILE A C   1 
ATOM 2249 O O   . ILE A 1 282 ? 77.536 76.557  153.486 1.00 48.71  ? 282 ILE A O   1 
ATOM 2250 C CB  . ILE A 1 282 ? 75.087 78.273  155.283 1.00 46.74  ? 282 ILE A CB  1 
ATOM 2251 C CG1 . ILE A 1 282 ? 74.781 79.714  155.686 1.00 45.74  ? 282 ILE A CG1 1 
ATOM 2252 C CG2 . ILE A 1 282 ? 75.800 77.521  156.365 1.00 46.17  ? 282 ILE A CG2 1 
ATOM 2253 C CD1 . ILE A 1 282 ? 73.813 79.826  156.813 1.00 46.08  ? 282 ILE A CD1 1 
ATOM 2254 N N   . ILE A 1 283 ? 75.337 76.026  153.442 1.00 50.69  ? 283 ILE A N   1 
ATOM 2255 C CA  . ILE A 1 283 ? 75.541 74.637  153.091 1.00 52.99  ? 283 ILE A CA  1 
ATOM 2256 C C   . ILE A 1 283 ? 76.459 74.437  151.901 1.00 54.88  ? 283 ILE A C   1 
ATOM 2257 O O   . ILE A 1 283 ? 77.548 73.898  152.029 1.00 54.55  ? 283 ILE A O   1 
ATOM 2258 C CB  . ILE A 1 283 ? 74.206 73.981  152.778 1.00 52.97  ? 283 ILE A CB  1 
ATOM 2259 C CG1 . ILE A 1 283 ? 73.253 74.229  153.935 1.00 52.73  ? 283 ILE A CG1 1 
ATOM 2260 C CG2 . ILE A 1 283 ? 74.408 72.493  152.550 1.00 53.26  ? 283 ILE A CG2 1 
ATOM 2261 C CD1 . ILE A 1 283 ? 73.830 73.846  155.262 1.00 53.39  ? 283 ILE A CD1 1 
ATOM 2262 N N   . ASN A 1 284 ? 76.011 74.871  150.736 1.00 57.81  ? 284 ASN A N   1 
ATOM 2263 C CA  . ASN A 1 284 ? 76.828 74.682  149.560 1.00 60.61  ? 284 ASN A CA  1 
ATOM 2264 C C   . ASN A 1 284 ? 78.208 75.260  149.766 1.00 61.96  ? 284 ASN A C   1 
ATOM 2265 O O   . ASN A 1 284 ? 79.200 74.708  149.275 1.00 62.05  ? 284 ASN A O   1 
ATOM 2266 C CB  . ASN A 1 284 ? 76.171 75.312  148.344 1.00 61.70  ? 284 ASN A CB  1 
ATOM 2267 C CG  . ASN A 1 284 ? 74.853 74.659  148.013 1.00 62.49  ? 284 ASN A CG  1 
ATOM 2268 O OD1 . ASN A 1 284 ? 74.706 73.432  148.118 1.00 62.37  ? 284 ASN A OD1 1 
ATOM 2269 N ND2 . ASN A 1 284 ? 73.881 75.469  147.608 1.00 63.17  ? 284 ASN A ND2 1 
ATOM 2270 N N   . ARG A 1 285 ? 78.278 76.370  150.489 1.00 63.08  ? 285 ARG A N   1 
ATOM 2271 C CA  . ARG A 1 285 ? 79.567 76.969  150.723 1.00 64.44  ? 285 ARG A CA  1 
ATOM 2272 C C   . ARG A 1 285 ? 80.361 76.000  151.569 1.00 63.57  ? 285 ARG A C   1 
ATOM 2273 O O   . ARG A 1 285 ? 81.580 75.854  151.400 1.00 64.40  ? 285 ARG A O   1 
ATOM 2274 C CB  . ARG A 1 285 ? 79.434 78.300  151.453 1.00 67.02  ? 285 ARG A CB  1 
ATOM 2275 C CG  . ARG A 1 285 ? 79.108 79.503  150.554 1.00 71.42  ? 285 ARG A CG  1 
ATOM 2276 C CD  . ARG A 1 285 ? 78.951 80.781  151.424 1.00 76.15  ? 285 ARG A CD  1 
ATOM 2277 N NE  . ARG A 1 285 ? 78.633 82.003  150.671 1.00 79.88  ? 285 ARG A NE  1 
ATOM 2278 C CZ  . ARG A 1 285 ? 78.258 83.164  151.223 1.00 81.42  ? 285 ARG A CZ  1 
ATOM 2279 N NH1 . ARG A 1 285 ? 78.148 83.280  152.543 1.00 82.27  ? 285 ARG A NH1 1 
ATOM 2280 N NH2 . ARG A 1 285 ? 77.980 84.219  150.455 1.00 82.12  ? 285 ARG A NH2 1 
ATOM 2281 N N   . ILE A 1 286 ? 79.657 75.302  152.454 1.00 62.33  ? 286 ILE A N   1 
ATOM 2282 C CA  . ILE A 1 286 ? 80.301 74.354  153.356 1.00 60.72  ? 286 ILE A CA  1 
ATOM 2283 C C   . ILE A 1 286 ? 80.324 72.916  152.892 1.00 60.15  ? 286 ILE A C   1 
ATOM 2284 O O   . ILE A 1 286 ? 81.389 72.325  152.711 1.00 60.55  ? 286 ILE A O   1 
ATOM 2285 C CB  . ILE A 1 286 ? 79.630 74.357  154.700 1.00 60.23  ? 286 ILE A CB  1 
ATOM 2286 C CG1 . ILE A 1 286 ? 79.586 75.774  155.247 1.00 60.29  ? 286 ILE A CG1 1 
ATOM 2287 C CG2 . ILE A 1 286 ? 80.377 73.417  155.621 1.00 60.22  ? 286 ILE A CG2 1 
ATOM 2288 C CD1 . ILE A 1 286 ? 78.716 75.922  156.459 1.00 60.51  ? 286 ILE A CD1 1 
ATOM 2289 N N   . GLY A 1 287 ? 79.132 72.355  152.755 1.00 58.54  ? 287 GLY A N   1 
ATOM 2290 C CA  . GLY A 1 287 ? 79.011 70.974  152.349 1.00 57.20  ? 287 GLY A CA  1 
ATOM 2291 C C   . GLY A 1 287 ? 78.128 70.208  153.320 1.00 55.17  ? 287 GLY A C   1 
ATOM 2292 O O   . GLY A 1 287 ? 78.051 70.545  154.506 1.00 54.93  ? 287 GLY A O   1 
ATOM 2293 N N   . GLY A 1 288 ? 77.468 69.172  152.813 1.00 53.18  ? 288 GLY A N   1 
ATOM 2294 C CA  . GLY A 1 288 ? 76.589 68.390  153.648 1.00 50.00  ? 288 GLY A CA  1 
ATOM 2295 C C   . GLY A 1 288 ? 77.272 67.784  154.853 1.00 47.69  ? 288 GLY A C   1 
ATOM 2296 O O   . GLY A 1 288 ? 77.013 68.188  155.996 1.00 46.95  ? 288 GLY A O   1 
ATOM 2297 N N   . LYS A 1 289 ? 78.145 66.811  154.595 1.00 45.92  ? 289 LYS A N   1 
ATOM 2298 C CA  . LYS A 1 289 ? 78.859 66.113  155.660 1.00 44.18  ? 289 LYS A CA  1 
ATOM 2299 C C   . LYS A 1 289 ? 79.046 67.038  156.838 1.00 42.95  ? 289 LYS A C   1 
ATOM 2300 O O   . LYS A 1 289 ? 78.769 66.684  157.974 1.00 42.36  ? 289 LYS A O   1 
ATOM 2301 C CB  . LYS A 1 289 ? 80.219 65.587  155.167 1.00 44.18  ? 289 LYS A CB  1 
ATOM 2302 C CG  . LYS A 1 289 ? 81.076 64.984  156.275 1.00 43.60  ? 289 LYS A CG  1 
ATOM 2303 C CD  . LYS A 1 289 ? 82.214 64.114  155.768 1.00 44.29  ? 289 LYS A CD  1 
ATOM 2304 C CE  . LYS A 1 289 ? 82.952 63.451  156.930 1.00 44.58  ? 289 LYS A CE  1 
ATOM 2305 N NZ  . LYS A 1 289 ? 84.124 62.643  156.465 1.00 45.06  ? 289 LYS A NZ  1 
ATOM 2306 N N   . ASN A 1 290 ? 79.464 68.250  156.542 1.00 42.06  ? 290 ASN A N   1 
ATOM 2307 C CA  . ASN A 1 290 ? 79.692 69.240  157.558 1.00 41.28  ? 290 ASN A CA  1 
ATOM 2308 C C   . ASN A 1 290 ? 78.413 69.720  158.200 1.00 39.88  ? 290 ASN A C   1 
ATOM 2309 O O   . ASN A 1 290 ? 78.238 69.612  159.409 1.00 39.95  ? 290 ASN A O   1 
ATOM 2310 C CB  . ASN A 1 290 ? 80.436 70.380  156.910 1.00 41.90  ? 290 ASN A CB  1 
ATOM 2311 C CG  . ASN A 1 290 ? 81.710 69.914  156.284 1.00 43.72  ? 290 ASN A CG  1 
ATOM 2312 O OD1 . ASN A 1 290 ? 82.753 69.889  156.939 1.00 44.21  ? 290 ASN A OD1 1 
ATOM 2313 N ND2 . ASN A 1 290 ? 81.634 69.475  155.028 1.00 43.90  ? 290 ASN A ND2 1 
ATOM 2314 N N   . ALA A 1 291 ? 77.512 70.236  157.382 1.00 38.41  ? 291 ALA A N   1 
ATOM 2315 C CA  . ALA A 1 291 ? 76.246 70.719  157.885 1.00 36.78  ? 291 ALA A CA  1 
ATOM 2316 C C   . ALA A 1 291 ? 75.792 69.888  159.077 1.00 35.78  ? 291 ALA A C   1 
ATOM 2317 O O   . ALA A 1 291 ? 75.626 70.404  160.186 1.00 34.17  ? 291 ALA A O   1 
ATOM 2318 C CB  . ALA A 1 291 ? 75.214 70.647  156.794 1.00 37.53  ? 291 ALA A CB  1 
ATOM 2319 N N   . LEU A 1 292 ? 75.623 68.589  158.839 1.00 34.94  ? 292 LEU A N   1 
ATOM 2320 C CA  . LEU A 1 292 ? 75.161 67.659  159.869 1.00 33.47  ? 292 LEU A CA  1 
ATOM 2321 C C   . LEU A 1 292 ? 75.977 67.728  161.138 1.00 32.67  ? 292 LEU A C   1 
ATOM 2322 O O   . LEU A 1 292 ? 75.447 67.914  162.238 1.00 32.66  ? 292 LEU A O   1 
ATOM 2323 C CB  . LEU A 1 292 ? 75.173 66.226  159.339 1.00 33.43  ? 292 LEU A CB  1 
ATOM 2324 C CG  . LEU A 1 292 ? 74.331 65.988  158.085 1.00 33.64  ? 292 LEU A CG  1 
ATOM 2325 C CD1 . LEU A 1 292 ? 74.161 64.504  157.888 1.00 33.63  ? 292 LEU A CD1 1 
ATOM 2326 C CD2 . LEU A 1 292 ? 72.984 66.649  158.196 1.00 34.24  ? 292 LEU A CD2 1 
ATOM 2327 N N   . LEU A 1 293 ? 77.276 67.566  160.979 1.00 31.59  ? 293 LEU A N   1 
ATOM 2328 C CA  . LEU A 1 293 ? 78.176 67.624  162.102 1.00 31.36  ? 293 LEU A CA  1 
ATOM 2329 C C   . LEU A 1 293 ? 77.957 68.905  162.914 1.00 31.21  ? 293 LEU A C   1 
ATOM 2330 O O   . LEU A 1 293 ? 77.552 68.842  164.073 1.00 31.14  ? 293 LEU A O   1 
ATOM 2331 C CB  . LEU A 1 293 ? 79.597 67.533  161.581 1.00 31.67  ? 293 LEU A CB  1 
ATOM 2332 C CG  . LEU A 1 293 ? 79.733 66.316  160.676 1.00 32.52  ? 293 LEU A CG  1 
ATOM 2333 C CD1 . LEU A 1 293 ? 81.047 66.364  159.934 1.00 33.74  ? 293 LEU A CD1 1 
ATOM 2334 C CD2 . LEU A 1 293 ? 79.624 65.066  161.501 1.00 32.31  ? 293 LEU A CD2 1 
ATOM 2335 N N   . LEU A 1 294 ? 78.200 70.068  162.321 1.00 31.05  ? 294 LEU A N   1 
ATOM 2336 C CA  . LEU A 1 294 ? 78.007 71.303  163.069 1.00 30.39  ? 294 LEU A CA  1 
ATOM 2337 C C   . LEU A 1 294 ? 76.651 71.258  163.778 1.00 29.62  ? 294 LEU A C   1 
ATOM 2338 O O   . LEU A 1 294 ? 76.549 71.588  164.950 1.00 29.02  ? 294 LEU A O   1 
ATOM 2339 C CB  . LEU A 1 294 ? 78.084 72.523  162.145 1.00 31.22  ? 294 LEU A CB  1 
ATOM 2340 C CG  . LEU A 1 294 ? 78.108 73.853  162.917 1.00 31.19  ? 294 LEU A CG  1 
ATOM 2341 C CD1 . LEU A 1 294 ? 79.495 74.041  163.533 1.00 32.15  ? 294 LEU A CD1 1 
ATOM 2342 C CD2 . LEU A 1 294 ? 77.779 75.018  162.016 1.00 31.00  ? 294 LEU A CD2 1 
ATOM 2343 N N   . ALA A 1 295 ? 75.617 70.827  163.070 1.00 29.64  ? 295 ALA A N   1 
ATOM 2344 C CA  . ALA A 1 295 ? 74.281 70.725  163.647 1.00 30.32  ? 295 ALA A CA  1 
ATOM 2345 C C   . ALA A 1 295 ? 74.295 69.811  164.872 1.00 30.52  ? 295 ALA A C   1 
ATOM 2346 O O   . ALA A 1 295 ? 73.851 70.194  165.960 1.00 30.57  ? 295 ALA A O   1 
ATOM 2347 C CB  . ALA A 1 295 ? 73.310 70.188  162.593 1.00 31.47  ? 295 ALA A CB  1 
ATOM 2348 N N   . GLY A 1 296 ? 74.809 68.597  164.676 1.00 31.06  ? 296 GLY A N   1 
ATOM 2349 C CA  . GLY A 1 296 ? 74.912 67.611  165.752 1.00 30.99  ? 296 GLY A CA  1 
ATOM 2350 C C   . GLY A 1 296 ? 75.728 68.096  166.943 1.00 30.69  ? 296 GLY A C   1 
ATOM 2351 O O   . GLY A 1 296 ? 75.338 67.907  168.096 1.00 30.26  ? 296 GLY A O   1 
ATOM 2352 N N   . THR A 1 297 ? 76.871 68.714  166.669 1.00 30.27  ? 297 THR A N   1 
ATOM 2353 C CA  . THR A 1 297 ? 77.700 69.251  167.735 1.00 29.38  ? 297 THR A CA  1 
ATOM 2354 C C   . THR A 1 297 ? 76.792 70.153  168.563 1.00 28.08  ? 297 THR A C   1 
ATOM 2355 O O   . THR A 1 297 ? 76.689 69.983  169.768 1.00 27.58  ? 297 THR A O   1 
ATOM 2356 C CB  . THR A 1 297 ? 78.887 70.067  167.164 1.00 29.63  ? 297 THR A CB  1 
ATOM 2357 O OG1 . THR A 1 297 ? 79.787 69.187  166.483 1.00 30.02  ? 297 THR A OG1 1 
ATOM 2358 C CG2 . THR A 1 297 ? 79.653 70.750  168.262 1.00 29.48  ? 297 THR A CG2 1 
ATOM 2359 N N   . ILE A 1 298 ? 76.105 71.083  167.905 1.00 26.78  ? 298 ILE A N   1 
ATOM 2360 C CA  . ILE A 1 298 ? 75.213 72.003  168.601 1.00 26.19  ? 298 ILE A CA  1 
ATOM 2361 C C   . ILE A 1 298 ? 74.369 71.288  169.640 1.00 25.94  ? 298 ILE A C   1 
ATOM 2362 O O   . ILE A 1 298 ? 74.373 71.649  170.821 1.00 25.77  ? 298 ILE A O   1 
ATOM 2363 C CB  . ILE A 1 298 ? 74.259 72.709  167.641 1.00 25.47  ? 298 ILE A CB  1 
ATOM 2364 C CG1 . ILE A 1 298 ? 75.043 73.602  166.686 1.00 26.80  ? 298 ILE A CG1 1 
ATOM 2365 C CG2 . ILE A 1 298 ? 73.285 73.556  168.429 1.00 24.90  ? 298 ILE A CG2 1 
ATOM 2366 C CD1 . ILE A 1 298 ? 74.169 74.367  165.697 1.00 28.00  ? 298 ILE A CD1 1 
ATOM 2367 N N   . MET A 1 299 ? 73.633 70.281  169.187 1.00 25.96  ? 299 MET A N   1 
ATOM 2368 C CA  . MET A 1 299 ? 72.776 69.514  170.072 1.00 25.81  ? 299 MET A CA  1 
ATOM 2369 C C   . MET A 1 299 ? 73.573 68.980  171.242 1.00 25.58  ? 299 MET A C   1 
ATOM 2370 O O   . MET A 1 299 ? 73.210 69.195  172.399 1.00 25.49  ? 299 MET A O   1 
ATOM 2371 C CB  . MET A 1 299 ? 72.147 68.367  169.314 1.00 25.45  ? 299 MET A CB  1 
ATOM 2372 C CG  . MET A 1 299 ? 71.260 68.843  168.234 1.00 25.78  ? 299 MET A CG  1 
ATOM 2373 S SD  . MET A 1 299 ? 70.537 67.477  167.424 1.00 28.61  ? 299 MET A SD  1 
ATOM 2374 C CE  . MET A 1 299 ? 71.580 67.379  165.981 1.00 26.42  ? 299 MET A CE  1 
ATOM 2375 N N   . SER A 1 300 ? 74.658 68.276  170.938 1.00 25.01  ? 300 SER A N   1 
ATOM 2376 C CA  . SER A 1 300 ? 75.491 67.739  171.991 1.00 24.21  ? 300 SER A CA  1 
ATOM 2377 C C   . SER A 1 300 ? 75.654 68.851  173.024 1.00 24.40  ? 300 SER A C   1 
ATOM 2378 O O   . SER A 1 300 ? 75.243 68.711  174.174 1.00 23.60  ? 300 SER A O   1 
ATOM 2379 C CB  . SER A 1 300 ? 76.859 67.307  171.444 1.00 23.92  ? 300 SER A CB  1 
ATOM 2380 O OG  . SER A 1 300 ? 76.789 66.074  170.749 1.00 23.31  ? 300 SER A OG  1 
ATOM 2381 N N   . VAL A 1 301 ? 76.210 69.979  172.606 1.00 24.86  ? 301 VAL A N   1 
ATOM 2382 C CA  . VAL A 1 301 ? 76.401 71.067  173.534 1.00 25.05  ? 301 VAL A CA  1 
ATOM 2383 C C   . VAL A 1 301 ? 75.105 71.479  174.178 1.00 25.72  ? 301 VAL A C   1 
ATOM 2384 O O   . VAL A 1 301 ? 75.109 71.928  175.305 1.00 26.58  ? 301 VAL A O   1 
ATOM 2385 C CB  . VAL A 1 301 ? 77.052 72.278  172.869 1.00 24.47  ? 301 VAL A CB  1 
ATOM 2386 C CG1 . VAL A 1 301 ? 76.944 73.506  173.755 1.00 23.22  ? 301 VAL A CG1 1 
ATOM 2387 C CG2 . VAL A 1 301 ? 78.514 71.976  172.625 1.00 23.77  ? 301 VAL A CG2 1 
ATOM 2388 N N   . ARG A 1 302 ? 73.982 71.317  173.502 1.00 26.66  ? 302 ARG A N   1 
ATOM 2389 C CA  . ARG A 1 302 ? 72.730 71.702  174.146 1.00 27.93  ? 302 ARG A CA  1 
ATOM 2390 C C   . ARG A 1 302 ? 72.372 70.790  175.308 1.00 27.47  ? 302 ARG A C   1 
ATOM 2391 O O   . ARG A 1 302 ? 71.653 71.176  176.227 1.00 27.13  ? 302 ARG A O   1 
ATOM 2392 C CB  . ARG A 1 302 ? 71.564 71.680  173.173 1.00 30.53  ? 302 ARG A CB  1 
ATOM 2393 C CG  . ARG A 1 302 ? 70.268 72.128  173.838 1.00 33.22  ? 302 ARG A CG  1 
ATOM 2394 C CD  . ARG A 1 302 ? 69.090 71.841  172.963 1.00 35.07  ? 302 ARG A CD  1 
ATOM 2395 N NE  . ARG A 1 302 ? 67.833 72.261  173.560 1.00 37.41  ? 302 ARG A NE  1 
ATOM 2396 C CZ  . ARG A 1 302 ? 66.645 71.942  173.054 1.00 38.57  ? 302 ARG A CZ  1 
ATOM 2397 N NH1 . ARG A 1 302 ? 66.573 71.204  171.955 1.00 39.82  ? 302 ARG A NH1 1 
ATOM 2398 N NH2 . ARG A 1 302 ? 65.526 72.355  173.634 1.00 39.23  ? 302 ARG A NH2 1 
ATOM 2399 N N   . ILE A 1 303 ? 72.866 69.565  175.256 1.00 27.20  ? 303 ILE A N   1 
ATOM 2400 C CA  . ILE A 1 303 ? 72.571 68.563  176.279 1.00 27.77  ? 303 ILE A CA  1 
ATOM 2401 C C   . ILE A 1 303 ? 73.527 68.690  177.406 1.00 27.79  ? 303 ILE A C   1 
ATOM 2402 O O   . ILE A 1 303 ? 73.187 68.926  178.563 1.00 26.87  ? 303 ILE A O   1 
ATOM 2403 C CB  . ILE A 1 303 ? 72.728 67.171  175.690 1.00 27.84  ? 303 ILE A CB  1 
ATOM 2404 C CG1 . ILE A 1 303 ? 71.863 67.063  174.435 1.00 28.52  ? 303 ILE A CG1 1 
ATOM 2405 C CG2 . ILE A 1 303 ? 72.348 66.147  176.705 1.00 27.76  ? 303 ILE A CG2 1 
ATOM 2406 C CD1 . ILE A 1 303 ? 71.805 65.685  173.847 1.00 30.14  ? 303 ILE A CD1 1 
ATOM 2407 N N   . ILE A 1 304 ? 74.769 68.481  177.042 1.00 28.64  ? 304 ILE A N   1 
ATOM 2408 C CA  . ILE A 1 304 ? 75.832 68.569  178.008 1.00 29.78  ? 304 ILE A CA  1 
ATOM 2409 C C   . ILE A 1 304 ? 75.626 69.900  178.714 1.00 30.53  ? 304 ILE A C   1 
ATOM 2410 O O   . ILE A 1 304 ? 75.944 70.050  179.889 1.00 30.23  ? 304 ILE A O   1 
ATOM 2411 C CB  . ILE A 1 304 ? 77.136 68.504  177.287 1.00 29.61  ? 304 ILE A CB  1 
ATOM 2412 C CG1 . ILE A 1 304 ? 77.331 67.160  176.675 1.00 28.20  ? 304 ILE A CG1 1 
ATOM 2413 C CG2 . ILE A 1 304 ? 78.254 68.915  178.248 1.00 30.25  ? 304 ILE A CG2 1 
ATOM 2414 C CD1 . ILE A 1 304 ? 78.720 66.877  176.196 1.00 28.04  ? 304 ILE A CD1 1 
ATOM 2415 N N   . GLY A 1 305 ? 75.054 70.838  177.971 1.00 31.23  ? 305 GLY A N   1 
ATOM 2416 C CA  . GLY A 1 305 ? 74.807 72.142  178.519 1.00 32.63  ? 305 GLY A CA  1 
ATOM 2417 C C   . GLY A 1 305 ? 73.662 72.139  179.493 1.00 34.14  ? 305 GLY A C   1 
ATOM 2418 O O   . GLY A 1 305 ? 73.276 73.202  179.968 1.00 34.86  ? 305 GLY A O   1 
ATOM 2419 N N   . SER A 1 306 ? 73.111 70.970  179.798 1.00 34.45  ? 306 SER A N   1 
ATOM 2420 C CA  . SER A 1 306 ? 72.012 70.928  180.745 1.00 36.00  ? 306 SER A CA  1 
ATOM 2421 C C   . SER A 1 306 ? 72.378 70.336  182.111 1.00 36.73  ? 306 SER A C   1 
ATOM 2422 O O   . SER A 1 306 ? 71.793 70.715  183.130 1.00 37.05  ? 306 SER A O   1 
ATOM 2423 C CB  . SER A 1 306 ? 70.819 70.219  180.116 1.00 36.36  ? 306 SER A CB  1 
ATOM 2424 O OG  . SER A 1 306 ? 70.328 70.991  179.031 1.00 37.30  ? 306 SER A OG  1 
ATOM 2425 N N   . SER A 1 307 ? 73.364 69.441  182.150 1.00 37.47  ? 307 SER A N   1 
ATOM 2426 C CA  . SER A 1 307 ? 73.793 68.854  183.426 1.00 37.77  ? 307 SER A CA  1 
ATOM 2427 C C   . SER A 1 307 ? 74.609 69.854  184.247 1.00 37.58  ? 307 SER A C   1 
ATOM 2428 O O   . SER A 1 307 ? 74.854 69.655  185.426 1.00 37.95  ? 307 SER A O   1 
ATOM 2429 C CB  . SER A 1 307 ? 74.661 67.620  183.199 1.00 38.31  ? 307 SER A CB  1 
ATOM 2430 O OG  . SER A 1 307 ? 76.030 67.992  183.159 1.00 37.71  ? 307 SER A OG  1 
ATOM 2431 N N   . PHE A 1 308 ? 75.040 70.928  183.620 1.00 37.28  ? 308 PHE A N   1 
ATOM 2432 C CA  . PHE A 1 308 ? 75.827 71.911  184.322 1.00 37.44  ? 308 PHE A CA  1 
ATOM 2433 C C   . PHE A 1 308 ? 75.072 73.218  184.408 1.00 36.59  ? 308 PHE A C   1 
ATOM 2434 O O   . PHE A 1 308 ? 75.662 74.279  184.625 1.00 36.89  ? 308 PHE A O   1 
ATOM 2435 C CB  . PHE A 1 308 ? 77.151 72.098  183.587 1.00 38.73  ? 308 PHE A CB  1 
ATOM 2436 C CG  . PHE A 1 308 ? 78.131 70.978  183.816 1.00 40.40  ? 308 PHE A CG  1 
ATOM 2437 C CD1 . PHE A 1 308 ? 78.099 70.246  184.989 1.00 40.29  ? 308 PHE A CD1 1 
ATOM 2438 C CD2 . PHE A 1 308 ? 79.132 70.700  182.893 1.00 40.74  ? 308 PHE A CD2 1 
ATOM 2439 C CE1 . PHE A 1 308 ? 79.050 69.275  185.229 1.00 40.28  ? 308 PHE A CE1 1 
ATOM 2440 C CE2 . PHE A 1 308 ? 80.090 69.715  183.141 1.00 41.55  ? 308 PHE A CE2 1 
ATOM 2441 C CZ  . PHE A 1 308 ? 80.049 69.006  184.305 1.00 40.98  ? 308 PHE A CZ  1 
ATOM 2442 N N   . ALA A 1 309 ? 73.757 73.131  184.277 1.00 35.67  ? 309 ALA A N   1 
ATOM 2443 C CA  . ALA A 1 309 ? 72.927 74.318  184.298 1.00 35.35  ? 309 ALA A CA  1 
ATOM 2444 C C   . ALA A 1 309 ? 72.186 74.546  185.578 1.00 35.65  ? 309 ALA A C   1 
ATOM 2445 O O   . ALA A 1 309 ? 71.640 73.611  186.114 1.00 35.88  ? 309 ALA A O   1 
ATOM 2446 C CB  . ALA A 1 309 ? 71.947 74.246  183.187 1.00 35.47  ? 309 ALA A CB  1 
ATOM 2447 N N   . THR A 1 310 ? 72.119 75.800  186.018 1.00 36.49  ? 310 THR A N   1 
ATOM 2448 C CA  . THR A 1 310 ? 71.446 76.153  187.259 1.00 38.59  ? 310 THR A CA  1 
ATOM 2449 C C   . THR A 1 310 ? 70.297 77.160  187.186 1.00 39.10  ? 310 THR A C   1 
ATOM 2450 O O   . THR A 1 310 ? 69.274 76.979  187.831 1.00 39.01  ? 310 THR A O   1 
ATOM 2451 C CB  . THR A 1 310 ? 72.458 76.692  188.288 1.00 39.96  ? 310 THR A CB  1 
ATOM 2452 O OG1 . THR A 1 310 ? 73.282 77.687  187.670 1.00 40.52  ? 310 THR A OG1 1 
ATOM 2453 C CG2 . THR A 1 310 ? 73.341 75.585  188.796 1.00 40.54  ? 310 THR A CG2 1 
ATOM 2454 N N   . SER A 1 311 ? 70.448 78.220  186.407 1.00 39.70  ? 311 SER A N   1 
ATOM 2455 C CA  . SER A 1 311 ? 69.400 79.234  186.341 1.00 40.19  ? 311 SER A CA  1 
ATOM 2456 C C   . SER A 1 311 ? 68.498 79.165  185.133 1.00 40.27  ? 311 SER A C   1 
ATOM 2457 O O   . SER A 1 311 ? 68.853 78.594  184.104 1.00 40.06  ? 311 SER A O   1 
ATOM 2458 C CB  . SER A 1 311 ? 70.019 80.620  186.388 1.00 41.25  ? 311 SER A CB  1 
ATOM 2459 O OG  . SER A 1 311 ? 70.884 80.784  185.277 1.00 41.82  ? 311 SER A OG  1 
ATOM 2460 N N   . ALA A 1 312 ? 67.327 79.774  185.266 1.00 41.02  ? 312 ALA A N   1 
ATOM 2461 C CA  . ALA A 1 312 ? 66.357 79.803  184.179 1.00 41.80  ? 312 ALA A CA  1 
ATOM 2462 C C   . ALA A 1 312 ? 66.964 80.466  182.963 1.00 41.90  ? 312 ALA A C   1 
ATOM 2463 O O   . ALA A 1 312 ? 67.011 79.895  181.881 1.00 41.59  ? 312 ALA A O   1 
ATOM 2464 C CB  . ALA A 1 312 ? 65.113 80.576  184.606 1.00 43.11  ? 312 ALA A CB  1 
ATOM 2465 N N   . LEU A 1 313 ? 67.430 81.685  183.154 1.00 41.87  ? 313 LEU A N   1 
ATOM 2466 C CA  . LEU A 1 313 ? 68.028 82.412  182.062 1.00 42.36  ? 313 LEU A CA  1 
ATOM 2467 C C   . LEU A 1 313 ? 69.031 81.494  181.384 1.00 41.44  ? 313 LEU A C   1 
ATOM 2468 O O   . LEU A 1 313 ? 69.171 81.489  180.155 1.00 41.05  ? 313 LEU A O   1 
ATOM 2469 C CB  . LEU A 1 313 ? 68.693 83.685  182.601 1.00 44.88  ? 313 LEU A CB  1 
ATOM 2470 C CG  . LEU A 1 313 ? 67.731 84.684  183.293 1.00 47.13  ? 313 LEU A CG  1 
ATOM 2471 C CD1 . LEU A 1 313 ? 68.522 85.779  184.054 1.00 47.90  ? 313 LEU A CD1 1 
ATOM 2472 C CD2 . LEU A 1 313 ? 66.801 85.316  182.230 1.00 47.47  ? 313 LEU A CD2 1 
ATOM 2473 N N   . GLU A 1 314 ? 69.704 80.686  182.189 1.00 40.45  ? 314 GLU A N   1 
ATOM 2474 C CA  . GLU A 1 314 ? 70.679 79.775  181.641 1.00 39.58  ? 314 GLU A CA  1 
ATOM 2475 C C   . GLU A 1 314 ? 69.974 78.839  180.662 1.00 36.59  ? 314 GLU A C   1 
ATOM 2476 O O   . GLU A 1 314 ? 70.444 78.625  179.552 1.00 35.90  ? 314 GLU A O   1 
ATOM 2477 C CB  . GLU A 1 314 ? 71.356 78.996  182.769 1.00 41.83  ? 314 GLU A CB  1 
ATOM 2478 C CG  . GLU A 1 314 ? 72.535 78.168  182.309 1.00 45.51  ? 314 GLU A CG  1 
ATOM 2479 C CD  . GLU A 1 314 ? 73.591 77.976  183.386 1.00 47.58  ? 314 GLU A CD  1 
ATOM 2480 O OE1 . GLU A 1 314 ? 73.262 78.086  184.601 1.00 48.74  ? 314 GLU A OE1 1 
ATOM 2481 O OE2 . GLU A 1 314 ? 74.757 77.694  183.005 1.00 48.52  ? 314 GLU A OE2 1 
ATOM 2482 N N   . VAL A 1 315 ? 68.819 78.323  181.061 1.00 33.92  ? 315 VAL A N   1 
ATOM 2483 C CA  . VAL A 1 315 ? 68.057 77.431  180.209 1.00 32.12  ? 315 VAL A CA  1 
ATOM 2484 C C   . VAL A 1 315 ? 67.632 78.141  178.948 1.00 30.93  ? 315 VAL A C   1 
ATOM 2485 O O   . VAL A 1 315 ? 67.781 77.608  177.849 1.00 30.82  ? 315 VAL A O   1 
ATOM 2486 C CB  . VAL A 1 315 ? 66.792 76.938  180.881 1.00 32.12  ? 315 VAL A CB  1 
ATOM 2487 C CG1 . VAL A 1 315 ? 66.509 75.552  180.398 1.00 32.21  ? 315 VAL A CG1 1 
ATOM 2488 C CG2 . VAL A 1 315 ? 66.953 76.954  182.363 1.00 33.86  ? 315 VAL A CG2 1 
ATOM 2489 N N   . VAL A 1 316 ? 67.075 79.335  179.112 1.00 29.34  ? 316 VAL A N   1 
ATOM 2490 C CA  . VAL A 1 316 ? 66.645 80.098  177.970 1.00 27.26  ? 316 VAL A CA  1 
ATOM 2491 C C   . VAL A 1 316 ? 67.753 79.936  176.952 1.00 26.92  ? 316 VAL A C   1 
ATOM 2492 O O   . VAL A 1 316 ? 67.524 79.400  175.873 1.00 26.64  ? 316 VAL A O   1 
ATOM 2493 C CB  . VAL A 1 316 ? 66.470 81.586  178.313 1.00 26.90  ? 316 VAL A CB  1 
ATOM 2494 C CG1 . VAL A 1 316 ? 66.379 82.398  177.057 1.00 26.52  ? 316 VAL A CG1 1 
ATOM 2495 C CG2 . VAL A 1 316 ? 65.211 81.789  179.134 1.00 26.11  ? 316 VAL A CG2 1 
ATOM 2496 N N   . ILE A 1 317 ? 68.970 80.327  177.313 1.00 27.16  ? 317 ILE A N   1 
ATOM 2497 C CA  . ILE A 1 317 ? 70.072 80.212  176.362 1.00 29.13  ? 317 ILE A CA  1 
ATOM 2498 C C   . ILE A 1 317 ? 70.236 78.798  175.780 1.00 30.16  ? 317 ILE A C   1 
ATOM 2499 O O   . ILE A 1 317 ? 70.660 78.647  174.629 1.00 31.41  ? 317 ILE A O   1 
ATOM 2500 C CB  . ILE A 1 317 ? 71.432 80.693  176.967 1.00 28.90  ? 317 ILE A CB  1 
ATOM 2501 C CG1 . ILE A 1 317 ? 71.344 82.174  177.318 1.00 29.51  ? 317 ILE A CG1 1 
ATOM 2502 C CG2 . ILE A 1 317 ? 72.575 80.551  175.936 1.00 29.05  ? 317 ILE A CG2 1 
ATOM 2503 C CD1 . ILE A 1 317 ? 72.634 82.735  177.897 1.00 30.32  ? 317 ILE A CD1 1 
ATOM 2504 N N   . LEU A 1 318 ? 69.879 77.771  176.551 1.00 30.40  ? 318 LEU A N   1 
ATOM 2505 C CA  . LEU A 1 318 ? 69.995 76.387  176.094 1.00 30.02  ? 318 LEU A CA  1 
ATOM 2506 C C   . LEU A 1 318 ? 68.908 75.985  175.118 1.00 28.98  ? 318 LEU A C   1 
ATOM 2507 O O   . LEU A 1 318 ? 69.157 75.174  174.229 1.00 29.21  ? 318 LEU A O   1 
ATOM 2508 C CB  . LEU A 1 318 ? 69.997 75.444  177.290 1.00 29.67  ? 318 LEU A CB  1 
ATOM 2509 C CG  . LEU A 1 318 ? 71.158 75.625  178.262 1.00 29.48  ? 318 LEU A CG  1 
ATOM 2510 C CD1 . LEU A 1 318 ? 71.018 74.595  179.339 1.00 30.14  ? 318 LEU A CD1 1 
ATOM 2511 C CD2 . LEU A 1 318 ? 72.494 75.472  177.554 1.00 28.26  ? 318 LEU A CD2 1 
ATOM 2512 N N   . LYS A 1 319 ? 67.699 76.519  175.291 1.00 29.24  ? 319 LYS A N   1 
ATOM 2513 C CA  . LYS A 1 319 ? 66.598 76.197  174.379 1.00 30.34  ? 319 LYS A CA  1 
ATOM 2514 C C   . LYS A 1 319 ? 67.015 76.757  173.060 1.00 31.81  ? 319 LYS A C   1 
ATOM 2515 O O   . LYS A 1 319 ? 67.391 76.039  172.143 1.00 32.00  ? 319 LYS A O   1 
ATOM 2516 C CB  . LYS A 1 319 ? 65.289 76.871  174.793 1.00 30.06  ? 319 LYS A CB  1 
ATOM 2517 C CG  . LYS A 1 319 ? 64.120 76.535  173.881 1.00 30.65  ? 319 LYS A CG  1 
ATOM 2518 C CD  . LYS A 1 319 ? 63.718 75.098  174.040 1.00 31.18  ? 319 LYS A CD  1 
ATOM 2519 C CE  . LYS A 1 319 ? 62.390 74.815  173.393 1.00 30.93  ? 319 LYS A CE  1 
ATOM 2520 N NZ  . LYS A 1 319 ? 62.170 73.347  173.440 1.00 32.40  ? 319 LYS A NZ  1 
ATOM 2521 N N   . THR A 1 320 ? 66.927 78.067  172.961 1.00 32.62  ? 320 THR A N   1 
ATOM 2522 C CA  . THR A 1 320 ? 67.354 78.752  171.753 1.00 33.90  ? 320 THR A CA  1 
ATOM 2523 C C   . THR A 1 320 ? 68.154 77.860  170.817 1.00 34.77  ? 320 THR A C   1 
ATOM 2524 O O   . THR A 1 320 ? 67.754 77.657  169.678 1.00 34.65  ? 320 THR A O   1 
ATOM 2525 C CB  . THR A 1 320 ? 68.256 79.895  172.109 1.00 34.37  ? 320 THR A CB  1 
ATOM 2526 O OG1 . THR A 1 320 ? 67.520 80.880  172.847 1.00 34.13  ? 320 THR A OG1 1 
ATOM 2527 C CG2 . THR A 1 320 ? 68.819 80.511  170.846 1.00 34.69  ? 320 THR A CG2 1 
ATOM 2528 N N   . LEU A 1 321 ? 69.275 77.322  171.299 1.00 36.62  ? 321 LEU A N   1 
ATOM 2529 C CA  . LEU A 1 321 ? 70.107 76.471  170.454 1.00 39.15  ? 321 LEU A CA  1 
ATOM 2530 C C   . LEU A 1 321 ? 69.323 75.478  169.639 1.00 40.91  ? 321 LEU A C   1 
ATOM 2531 O O   . LEU A 1 321 ? 69.869 74.913  168.698 1.00 41.64  ? 321 LEU A O   1 
ATOM 2532 C CB  . LEU A 1 321 ? 71.107 75.719  171.287 1.00 39.17  ? 321 LEU A CB  1 
ATOM 2533 C CG  . LEU A 1 321 ? 72.017 76.638  172.018 1.00 39.79  ? 321 LEU A CG  1 
ATOM 2534 C CD1 . LEU A 1 321 ? 73.131 75.844  172.693 1.00 39.64  ? 321 LEU A CD1 1 
ATOM 2535 C CD2 . LEU A 1 321 ? 72.597 77.686  171.051 1.00 39.65  ? 321 LEU A CD2 1 
ATOM 2536 N N   . HIS A 1 322 ? 68.067 75.246  170.043 1.00 42.23  ? 322 HIS A N   1 
ATOM 2537 C CA  . HIS A 1 322 ? 67.171 74.318  169.339 1.00 43.64  ? 322 HIS A CA  1 
ATOM 2538 C C   . HIS A 1 322 ? 67.103 74.824  167.924 1.00 43.94  ? 322 HIS A C   1 
ATOM 2539 O O   . HIS A 1 322 ? 67.426 74.094  166.995 1.00 44.51  ? 322 HIS A O   1 
ATOM 2540 C CB  . HIS A 1 322 ? 65.723 74.293  169.911 1.00 44.50  ? 322 HIS A CB  1 
ATOM 2541 C CG  . HIS A 1 322 ? 64.773 73.362  169.185 1.00 45.39  ? 322 HIS A CG  1 
ATOM 2542 N ND1 . HIS A 1 322 ? 64.955 71.996  169.148 1.00 45.95  ? 322 HIS A ND1 1 
ATOM 2543 C CD2 . HIS A 1 322 ? 63.635 73.601  168.498 1.00 45.41  ? 322 HIS A CD2 1 
ATOM 2544 C CE1 . HIS A 1 322 ? 63.980 71.434  168.467 1.00 45.84  ? 322 HIS A CE1 1 
ATOM 2545 N NE2 . HIS A 1 322 ? 63.153 72.395  168.052 1.00 45.36  ? 322 HIS A NE2 1 
ATOM 2546 N N   . MET A 1 323 ? 66.693 76.078  167.765 1.00 44.19  ? 323 MET A N   1 
ATOM 2547 C CA  . MET A 1 323 ? 66.551 76.668  166.444 1.00 44.49  ? 323 MET A CA  1 
ATOM 2548 C C   . MET A 1 323 ? 67.822 76.642  165.633 1.00 43.43  ? 323 MET A C   1 
ATOM 2549 O O   . MET A 1 323 ? 67.774 76.460  164.421 1.00 43.11  ? 323 MET A O   1 
ATOM 2550 C CB  . MET A 1 323 ? 66.036 78.106  166.547 1.00 46.73  ? 323 MET A CB  1 
ATOM 2551 C CG  . MET A 1 323 ? 64.589 78.211  167.022 1.00 48.25  ? 323 MET A CG  1 
ATOM 2552 S SD  . MET A 1 323 ? 64.138 76.919  168.210 1.00 50.37  ? 323 MET A SD  1 
ATOM 2553 C CE  . MET A 1 323 ? 62.572 77.574  168.893 1.00 49.12  ? 323 MET A CE  1 
ATOM 2554 N N   . PHE A 1 324 ? 68.954 76.819  166.300 1.00 41.99  ? 324 PHE A N   1 
ATOM 2555 C CA  . PHE A 1 324 ? 70.221 76.812  165.616 1.00 41.50  ? 324 PHE A CA  1 
ATOM 2556 C C   . PHE A 1 324 ? 70.456 75.524  164.909 1.00 41.59  ? 324 PHE A C   1 
ATOM 2557 O O   . PHE A 1 324 ? 71.212 75.492  163.966 1.00 41.98  ? 324 PHE A O   1 
ATOM 2558 C CB  . PHE A 1 324 ? 71.384 77.010  166.571 1.00 42.14  ? 324 PHE A CB  1 
ATOM 2559 C CG  . PHE A 1 324 ? 71.983 78.369  166.494 1.00 43.11  ? 324 PHE A CG  1 
ATOM 2560 C CD1 . PHE A 1 324 ? 71.156 79.462  166.281 1.00 42.62  ? 324 PHE A CD1 1 
ATOM 2561 C CD2 . PHE A 1 324 ? 73.359 78.573  166.636 1.00 42.97  ? 324 PHE A CD2 1 
ATOM 2562 C CE1 . PHE A 1 324 ? 71.668 80.744  166.204 1.00 42.99  ? 324 PHE A CE1 1 
ATOM 2563 C CE2 . PHE A 1 324 ? 73.896 79.866  166.562 1.00 43.33  ? 324 PHE A CE2 1 
ATOM 2564 C CZ  . PHE A 1 324 ? 73.040 80.956  166.344 1.00 43.64  ? 324 PHE A CZ  1 
ATOM 2565 N N   . GLU A 1 325 ? 69.824 74.449  165.342 1.00 41.30  ? 325 GLU A N   1 
ATOM 2566 C CA  . GLU A 1 325 ? 70.101 73.194  164.684 1.00 41.61  ? 325 GLU A CA  1 
ATOM 2567 C C   . GLU A 1 325 ? 69.085 72.885  163.615 1.00 41.33  ? 325 GLU A C   1 
ATOM 2568 O O   . GLU A 1 325 ? 69.396 72.254  162.598 1.00 41.16  ? 325 GLU A O   1 
ATOM 2569 C CB  . GLU A 1 325 ? 70.184 72.082  165.736 1.00 42.87  ? 325 GLU A CB  1 
ATOM 2570 C CG  . GLU A 1 325 ? 69.984 70.657  165.248 1.00 45.15  ? 325 GLU A CG  1 
ATOM 2571 C CD  . GLU A 1 325 ? 68.639 70.110  165.694 1.00 46.76  ? 325 GLU A CD  1 
ATOM 2572 O OE1 . GLU A 1 325 ? 67.654 70.876  165.618 1.00 47.28  ? 325 GLU A OE1 1 
ATOM 2573 O OE2 . GLU A 1 325 ? 68.556 68.930  166.118 1.00 48.63  ? 325 GLU A OE2 1 
ATOM 2574 N N   . VAL A 1 326 ? 67.877 73.370  163.838 1.00 41.06  ? 326 VAL A N   1 
ATOM 2575 C CA  . VAL A 1 326 ? 66.796 73.110  162.936 1.00 40.66  ? 326 VAL A CA  1 
ATOM 2576 C C   . VAL A 1 326 ? 67.297 73.243  161.543 1.00 42.35  ? 326 VAL A C   1 
ATOM 2577 O O   . VAL A 1 326 ? 67.718 72.258  160.925 1.00 42.37  ? 326 VAL A O   1 
ATOM 2578 C CB  . VAL A 1 326 ? 65.645 74.080  163.149 1.00 40.71  ? 326 VAL A CB  1 
ATOM 2579 C CG1 . VAL A 1 326 ? 64.405 73.597  162.422 1.00 39.15  ? 326 VAL A CG1 1 
ATOM 2580 C CG2 . VAL A 1 326 ? 65.381 74.209  164.608 1.00 42.33  ? 326 VAL A CG2 1 
ATOM 2581 N N   . PRO A 1 327 ? 67.315 74.474  161.039 1.00 43.50  ? 327 PRO A N   1 
ATOM 2582 C CA  . PRO A 1 327 ? 67.783 74.669  159.672 1.00 43.17  ? 327 PRO A CA  1 
ATOM 2583 C C   . PRO A 1 327 ? 68.872 73.680  159.294 1.00 43.27  ? 327 PRO A C   1 
ATOM 2584 O O   . PRO A 1 327 ? 68.658 72.781  158.478 1.00 43.49  ? 327 PRO A O   1 
ATOM 2585 C CB  . PRO A 1 327 ? 68.276 76.105  159.695 1.00 44.65  ? 327 PRO A CB  1 
ATOM 2586 C CG  . PRO A 1 327 ? 68.622 76.307  161.171 1.00 44.24  ? 327 PRO A CG  1 
ATOM 2587 C CD  . PRO A 1 327 ? 67.486 75.707  161.826 1.00 43.40  ? 327 PRO A CD  1 
ATOM 2588 N N   . PHE A 1 328 ? 70.030 73.837  159.922 1.00 42.53  ? 328 PHE A N   1 
ATOM 2589 C CA  . PHE A 1 328 ? 71.160 72.988  159.612 1.00 41.89  ? 328 PHE A CA  1 
ATOM 2590 C C   . PHE A 1 328 ? 70.827 71.525  159.415 1.00 40.93  ? 328 PHE A C   1 
ATOM 2591 O O   . PHE A 1 328 ? 71.268 70.925  158.434 1.00 40.88  ? 328 PHE A O   1 
ATOM 2592 C CB  . PHE A 1 328 ? 72.258 73.139  160.655 1.00 43.17  ? 328 PHE A CB  1 
ATOM 2593 C CG  . PHE A 1 328 ? 72.885 74.510  160.668 1.00 44.90  ? 328 PHE A CG  1 
ATOM 2594 C CD1 . PHE A 1 328 ? 72.162 75.611  161.079 1.00 44.96  ? 328 PHE A CD1 1 
ATOM 2595 C CD2 . PHE A 1 328 ? 74.187 74.709  160.234 1.00 44.87  ? 328 PHE A CD2 1 
ATOM 2596 C CE1 . PHE A 1 328 ? 72.721 76.890  161.056 1.00 45.06  ? 328 PHE A CE1 1 
ATOM 2597 C CE2 . PHE A 1 328 ? 74.750 75.990  160.207 1.00 44.18  ? 328 PHE A CE2 1 
ATOM 2598 C CZ  . PHE A 1 328 ? 74.013 77.077  160.619 1.00 44.36  ? 328 PHE A CZ  1 
ATOM 2599 N N   . LEU A 1 329 ? 70.032 70.928  160.293 1.00 39.88  ? 329 LEU A N   1 
ATOM 2600 C CA  . LEU A 1 329 ? 69.766 69.528  160.060 1.00 38.69  ? 329 LEU A CA  1 
ATOM 2601 C C   . LEU A 1 329 ? 68.900 69.300  158.863 1.00 38.44  ? 329 LEU A C   1 
ATOM 2602 O O   . LEU A 1 329 ? 69.293 68.613  157.932 1.00 38.27  ? 329 LEU A O   1 
ATOM 2603 C CB  . LEU A 1 329 ? 69.135 68.829  161.255 1.00 37.94  ? 329 LEU A CB  1 
ATOM 2604 C CG  . LEU A 1 329 ? 69.310 67.330  160.997 1.00 37.50  ? 329 LEU A CG  1 
ATOM 2605 C CD1 . LEU A 1 329 ? 70.779 67.055  160.924 1.00 37.49  ? 329 LEU A CD1 1 
ATOM 2606 C CD2 . LEU A 1 329 ? 68.681 66.484  162.070 1.00 37.42  ? 329 LEU A CD2 1 
ATOM 2607 N N   . LEU A 1 330 ? 67.713 69.872  158.870 1.00 39.64  ? 330 LEU A N   1 
ATOM 2608 C CA  . LEU A 1 330 ? 66.824 69.671  157.745 1.00 41.22  ? 330 LEU A CA  1 
ATOM 2609 C C   . LEU A 1 330 ? 67.627 69.821  156.462 1.00 40.97  ? 330 LEU A C   1 
ATOM 2610 O O   . LEU A 1 330 ? 67.781 68.882  155.679 1.00 40.08  ? 330 LEU A O   1 
ATOM 2611 C CB  . LEU A 1 330 ? 65.702 70.707  157.784 1.00 42.42  ? 330 LEU A CB  1 
ATOM 2612 C CG  . LEU A 1 330 ? 64.543 70.524  156.793 1.00 43.66  ? 330 LEU A CG  1 
ATOM 2613 C CD1 . LEU A 1 330 ? 63.758 69.248  157.141 1.00 43.70  ? 330 LEU A CD1 1 
ATOM 2614 C CD2 . LEU A 1 330 ? 63.626 71.750  156.849 1.00 43.30  ? 330 LEU A CD2 1 
ATOM 2615 N N   . VAL A 1 331 ? 68.158 71.018  156.284 1.00 40.64  ? 331 VAL A N   1 
ATOM 2616 C CA  . VAL A 1 331 ? 68.935 71.361  155.116 1.00 40.79  ? 331 VAL A CA  1 
ATOM 2617 C C   . VAL A 1 331 ? 70.038 70.350  154.847 1.00 40.79  ? 331 VAL A C   1 
ATOM 2618 O O   . VAL A 1 331 ? 70.070 69.696  153.805 1.00 40.90  ? 331 VAL A O   1 
ATOM 2619 C CB  . VAL A 1 331 ? 69.552 72.740  155.314 1.00 39.53  ? 331 VAL A CB  1 
ATOM 2620 C CG1 . VAL A 1 331 ? 70.297 73.139  154.089 1.00 38.58  ? 331 VAL A CG1 1 
ATOM 2621 C CG2 . VAL A 1 331 ? 68.457 73.751  155.642 1.00 39.13  ? 331 VAL A CG2 1 
ATOM 2622 N N   . GLY A 1 332 ? 70.947 70.241  155.803 1.00 41.71  ? 332 GLY A N   1 
ATOM 2623 C CA  . GLY A 1 332 ? 72.046 69.314  155.667 1.00 43.39  ? 332 GLY A CA  1 
ATOM 2624 C C   . GLY A 1 332 ? 71.554 67.940  155.296 1.00 44.58  ? 332 GLY A C   1 
ATOM 2625 O O   . GLY A 1 332 ? 71.787 67.464  154.184 1.00 44.77  ? 332 GLY A O   1 
ATOM 2626 N N   . CYS A 1 333 ? 70.870 67.295  156.225 1.00 45.61  ? 333 CYS A N   1 
ATOM 2627 C CA  . CYS A 1 333 ? 70.359 65.964  155.977 1.00 47.41  ? 333 CYS A CA  1 
ATOM 2628 C C   . CYS A 1 333 ? 69.951 65.819  154.509 1.00 48.42  ? 333 CYS A C   1 
ATOM 2629 O O   . CYS A 1 333 ? 70.466 64.981  153.774 1.00 48.75  ? 333 CYS A O   1 
ATOM 2630 C CB  . CYS A 1 333 ? 69.172 65.758  156.893 1.00 47.54  ? 333 CYS A CB  1 
ATOM 2631 S SG  . CYS A 1 333 ? 69.375 64.611  158.347 1.00 48.14  ? 333 CYS A SG  1 
ATOM 2632 N N   . PHE A 1 334 ? 69.040 66.681  154.096 1.00 50.26  ? 334 PHE A N   1 
ATOM 2633 C CA  . PHE A 1 334 ? 68.502 66.701  152.743 1.00 52.01  ? 334 PHE A CA  1 
ATOM 2634 C C   . PHE A 1 334 ? 69.555 66.826  151.639 1.00 51.33  ? 334 PHE A C   1 
ATOM 2635 O O   . PHE A 1 334 ? 69.576 66.051  150.679 1.00 51.37  ? 334 PHE A O   1 
ATOM 2636 C CB  . PHE A 1 334 ? 67.500 67.856  152.677 1.00 54.70  ? 334 PHE A CB  1 
ATOM 2637 C CG  . PHE A 1 334 ? 66.975 68.163  151.303 1.00 56.81  ? 334 PHE A CG  1 
ATOM 2638 C CD1 . PHE A 1 334 ? 66.219 67.236  150.598 1.00 56.65  ? 334 PHE A CD1 1 
ATOM 2639 C CD2 . PHE A 1 334 ? 67.196 69.421  150.742 1.00 57.91  ? 334 PHE A CD2 1 
ATOM 2640 C CE1 . PHE A 1 334 ? 65.691 67.562  149.362 1.00 57.11  ? 334 PHE A CE1 1 
ATOM 2641 C CE2 . PHE A 1 334 ? 66.673 69.756  149.508 1.00 58.00  ? 334 PHE A CE2 1 
ATOM 2642 C CZ  . PHE A 1 334 ? 65.918 68.827  148.814 1.00 57.88  ? 334 PHE A CZ  1 
ATOM 2643 N N   . LYS A 1 335 ? 70.430 67.807  151.786 1.00 50.73  ? 335 LYS A N   1 
ATOM 2644 C CA  . LYS A 1 335 ? 71.459 68.039  150.797 1.00 50.41  ? 335 LYS A CA  1 
ATOM 2645 C C   . LYS A 1 335 ? 72.528 66.963  150.874 1.00 48.83  ? 335 LYS A C   1 
ATOM 2646 O O   . LYS A 1 335 ? 73.147 66.640  149.872 1.00 49.75  ? 335 LYS A O   1 
ATOM 2647 C CB  . LYS A 1 335 ? 72.094 69.415  151.005 1.00 51.74  ? 335 LYS A CB  1 
ATOM 2648 C CG  . LYS A 1 335 ? 71.149 70.610  150.843 1.00 52.94  ? 335 LYS A CG  1 
ATOM 2649 C CD  . LYS A 1 335 ? 70.919 71.012  149.401 1.00 54.19  ? 335 LYS A CD  1 
ATOM 2650 C CE  . LYS A 1 335 ? 70.143 72.325  149.367 1.00 54.61  ? 335 LYS A CE  1 
ATOM 2651 N NZ  . LYS A 1 335 ? 69.957 72.860  147.980 1.00 56.11  ? 335 LYS A NZ  1 
ATOM 2652 N N   . TYR A 1 336 ? 72.752 66.398  152.049 1.00 46.41  ? 336 TYR A N   1 
ATOM 2653 C CA  . TYR A 1 336 ? 73.772 65.382  152.133 1.00 44.30  ? 336 TYR A CA  1 
ATOM 2654 C C   . TYR A 1 336 ? 73.328 64.144  151.427 1.00 43.29  ? 336 TYR A C   1 
ATOM 2655 O O   . TYR A 1 336 ? 74.148 63.369  150.931 1.00 43.33  ? 336 TYR A O   1 
ATOM 2656 C CB  . TYR A 1 336 ? 74.077 65.001  153.547 1.00 43.38  ? 336 TYR A CB  1 
ATOM 2657 C CG  . TYR A 1 336 ? 75.010 63.843  153.583 1.00 42.99  ? 336 TYR A CG  1 
ATOM 2658 C CD1 . TYR A 1 336 ? 76.228 63.904  152.921 1.00 43.27  ? 336 TYR A CD1 1 
ATOM 2659 C CD2 . TYR A 1 336 ? 74.693 62.701  154.286 1.00 42.83  ? 336 TYR A CD2 1 
ATOM 2660 C CE1 . TYR A 1 336 ? 77.106 62.869  152.962 1.00 43.79  ? 336 TYR A CE1 1 
ATOM 2661 C CE2 . TYR A 1 336 ? 75.570 61.654  154.339 1.00 43.72  ? 336 TYR A CE2 1 
ATOM 2662 C CZ  . TYR A 1 336 ? 76.775 61.747  153.675 1.00 44.29  ? 336 TYR A CZ  1 
ATOM 2663 O OH  . TYR A 1 336 ? 77.674 60.725  153.738 1.00 45.83  ? 336 TYR A OH  1 
ATOM 2664 N N   . ILE A 1 337 ? 72.026 63.930  151.411 1.00 43.00  ? 337 ILE A N   1 
ATOM 2665 C CA  . ILE A 1 337 ? 71.508 62.775  150.714 1.00 43.66  ? 337 ILE A CA  1 
ATOM 2666 C C   . ILE A 1 337 ? 71.764 63.022  149.226 1.00 44.44  ? 337 ILE A C   1 
ATOM 2667 O O   . ILE A 1 337 ? 72.530 62.299  148.578 1.00 44.37  ? 337 ILE A O   1 
ATOM 2668 C CB  . ILE A 1 337 ? 70.002 62.609  150.949 1.00 43.08  ? 337 ILE A CB  1 
ATOM 2669 C CG1 . ILE A 1 337 ? 69.742 62.388  152.430 1.00 43.07  ? 337 ILE A CG1 1 
ATOM 2670 C CG2 . ILE A 1 337 ? 69.478 61.428  150.164 1.00 43.01  ? 337 ILE A CG2 1 
ATOM 2671 C CD1 . ILE A 1 337 ? 68.283 62.189  152.758 1.00 43.73  ? 337 ILE A CD1 1 
ATOM 2672 N N   . THR A 1 338 ? 71.142 64.066  148.696 1.00 44.70  ? 338 THR A N   1 
ATOM 2673 C CA  . THR A 1 338 ? 71.314 64.377  147.303 1.00 45.38  ? 338 THR A CA  1 
ATOM 2674 C C   . THR A 1 338 ? 72.775 64.248  146.895 1.00 45.17  ? 338 THR A C   1 
ATOM 2675 O O   . THR A 1 338 ? 73.085 63.572  145.936 1.00 45.98  ? 338 THR A O   1 
ATOM 2676 C CB  . THR A 1 338 ? 70.830 65.797  146.996 1.00 46.62  ? 338 THR A CB  1 
ATOM 2677 O OG1 . THR A 1 338 ? 70.487 65.890  145.612 1.00 48.26  ? 338 THR A OG1 1 
ATOM 2678 C CG2 . THR A 1 338 ? 71.918 66.808  147.281 1.00 46.85  ? 338 THR A CG2 1 
ATOM 2679 N N   . SER A 1 339 ? 73.674 64.866  147.645 1.00 45.44  ? 339 SER A N   1 
ATOM 2680 C CA  . SER A 1 339 ? 75.087 64.833  147.300 1.00 46.31  ? 339 SER A CA  1 
ATOM 2681 C C   . SER A 1 339 ? 75.793 63.484  147.285 1.00 46.06  ? 339 SER A C   1 
ATOM 2682 O O   . SER A 1 339 ? 76.607 63.239  146.403 1.00 47.20  ? 339 SER A O   1 
ATOM 2683 C CB  . SER A 1 339 ? 75.875 65.805  148.183 1.00 46.93  ? 339 SER A CB  1 
ATOM 2684 O OG  . SER A 1 339 ? 75.591 67.147  147.819 1.00 48.68  ? 339 SER A OG  1 
ATOM 2685 N N   . GLN A 1 340 ? 75.534 62.601  148.234 1.00 44.67  ? 340 GLN A N   1 
ATOM 2686 C CA  . GLN A 1 340 ? 76.244 61.334  148.160 1.00 44.41  ? 340 GLN A CA  1 
ATOM 2687 C C   . GLN A 1 340 ? 75.302 60.183  147.853 1.00 41.99  ? 340 GLN A C   1 
ATOM 2688 O O   . GLN A 1 340 ? 75.580 59.022  148.169 1.00 43.01  ? 340 GLN A O   1 
ATOM 2689 C CB  . GLN A 1 340 ? 77.023 61.076  149.455 1.00 47.31  ? 340 GLN A CB  1 
ATOM 2690 C CG  . GLN A 1 340 ? 78.091 59.943  149.397 1.00 51.54  ? 340 GLN A CG  1 
ATOM 2691 C CD  . GLN A 1 340 ? 79.347 60.277  148.575 1.00 53.15  ? 340 GLN A CD  1 
ATOM 2692 O OE1 . GLN A 1 340 ? 79.334 60.267  147.338 1.00 54.63  ? 340 GLN A OE1 1 
ATOM 2693 N NE2 . GLN A 1 340 ? 80.443 60.568  149.276 1.00 53.88  ? 340 GLN A NE2 1 
ATOM 2694 N N   . PHE A 1 341 ? 74.184 60.501  147.219 1.00 40.01  ? 341 PHE A N   1 
ATOM 2695 C CA  . PHE A 1 341 ? 73.226 59.466  146.892 1.00 37.74  ? 341 PHE A CA  1 
ATOM 2696 C C   . PHE A 1 341 ? 72.470 59.537  145.592 1.00 36.65  ? 341 PHE A C   1 
ATOM 2697 O O   . PHE A 1 341 ? 71.994 60.590  145.164 1.00 35.84  ? 341 PHE A O   1 
ATOM 2698 C CB  . PHE A 1 341 ? 72.223 59.343  148.007 1.00 37.26  ? 341 PHE A CB  1 
ATOM 2699 C CG  . PHE A 1 341 ? 72.778 58.752  149.218 1.00 36.14  ? 341 PHE A CG  1 
ATOM 2700 C CD1 . PHE A 1 341 ? 73.556 59.500  150.076 1.00 35.96  ? 341 PHE A CD1 1 
ATOM 2701 C CD2 . PHE A 1 341 ? 72.509 57.439  149.518 1.00 35.71  ? 341 PHE A CD2 1 
ATOM 2702 C CE1 . PHE A 1 341 ? 74.059 58.940  151.229 1.00 36.04  ? 341 PHE A CE1 1 
ATOM 2703 C CE2 . PHE A 1 341 ? 73.002 56.870  150.663 1.00 35.25  ? 341 PHE A CE2 1 
ATOM 2704 C CZ  . PHE A 1 341 ? 73.780 57.618  151.528 1.00 35.66  ? 341 PHE A CZ  1 
ATOM 2705 N N   . GLU A 1 342 ? 72.344 58.364  144.998 1.00 34.21  ? 342 GLU A N   1 
ATOM 2706 C CA  . GLU A 1 342 ? 71.654 58.198  143.748 1.00 32.82  ? 342 GLU A CA  1 
ATOM 2707 C C   . GLU A 1 342 ? 70.207 58.641  143.917 1.00 31.08  ? 342 GLU A C   1 
ATOM 2708 O O   . GLU A 1 342 ? 69.403 57.975  144.560 1.00 31.71  ? 342 GLU A O   1 
ATOM 2709 C CB  . GLU A 1 342 ? 71.764 56.729  143.351 1.00 34.36  ? 342 GLU A CB  1 
ATOM 2710 C CG  . GLU A 1 342 ? 73.184 56.177  143.603 1.00 35.31  ? 342 GLU A CG  1 
ATOM 2711 C CD  . GLU A 1 342 ? 73.304 54.669  143.390 1.00 35.36  ? 342 GLU A CD  1 
ATOM 2712 O OE1 . GLU A 1 342 ? 72.634 54.122  142.508 1.00 35.61  ? 342 GLU A OE1 1 
ATOM 2713 O OE2 . GLU A 1 342 ? 74.093 54.018  144.091 1.00 35.22  ? 342 GLU A OE2 1 
ATOM 2714 N N   . VAL A 1 343 ? 69.897 59.793  143.339 1.00 29.48  ? 343 VAL A N   1 
ATOM 2715 C CA  . VAL A 1 343 ? 68.565 60.379  143.411 1.00 27.70  ? 343 VAL A CA  1 
ATOM 2716 C C   . VAL A 1 343 ? 67.435 59.365  143.429 1.00 27.55  ? 343 VAL A C   1 
ATOM 2717 O O   . VAL A 1 343 ? 66.403 59.577  144.045 1.00 26.59  ? 343 VAL A O   1 
ATOM 2718 C CB  . VAL A 1 343 ? 68.302 61.346  142.244 1.00 26.63  ? 343 VAL A CB  1 
ATOM 2719 C CG1 . VAL A 1 343 ? 66.964 61.990  142.430 1.00 25.39  ? 343 VAL A CG1 1 
ATOM 2720 C CG2 . VAL A 1 343 ? 69.391 62.406  142.170 1.00 25.33  ? 343 VAL A CG2 1 
ATOM 2721 N N   . ARG A 1 344 ? 67.623 58.254  142.750 1.00 27.03  ? 344 ARG A N   1 
ATOM 2722 C CA  . ARG A 1 344 ? 66.584 57.253  142.731 1.00 27.49  ? 344 ARG A CA  1 
ATOM 2723 C C   . ARG A 1 344 ? 66.368 56.715  144.122 1.00 27.56  ? 344 ARG A C   1 
ATOM 2724 O O   . ARG A 1 344 ? 65.350 56.126  144.414 1.00 27.63  ? 344 ARG A O   1 
ATOM 2725 C CB  . ARG A 1 344 ? 66.963 56.097  141.805 1.00 28.36  ? 344 ARG A CB  1 
ATOM 2726 C CG  . ARG A 1 344 ? 68.213 55.344  142.220 1.00 29.31  ? 344 ARG A CG  1 
ATOM 2727 C CD  . ARG A 1 344 ? 68.613 54.284  141.186 1.00 30.44  ? 344 ARG A CD  1 
ATOM 2728 N NE  . ARG A 1 344 ? 69.464 53.235  141.752 1.00 32.15  ? 344 ARG A NE  1 
ATOM 2729 C CZ  . ARG A 1 344 ? 70.122 52.324  141.043 1.00 32.44  ? 344 ARG A CZ  1 
ATOM 2730 N NH1 . ARG A 1 344 ? 70.035 52.329  139.727 1.00 34.99  ? 344 ARG A NH1 1 
ATOM 2731 N NH2 . ARG A 1 344 ? 70.862 51.404  141.648 1.00 32.20  ? 344 ARG A NH2 1 
ATOM 2732 N N   . PHE A 1 345 ? 67.308 56.928  145.013 1.00 28.52  ? 345 PHE A N   1 
ATOM 2733 C CA  . PHE A 1 345 ? 67.120 56.367  146.328 1.00 29.93  ? 345 PHE A CA  1 
ATOM 2734 C C   . PHE A 1 345 ? 66.398 57.224  147.342 1.00 31.52  ? 345 PHE A C   1 
ATOM 2735 O O   . PHE A 1 345 ? 65.975 56.719  148.382 1.00 30.50  ? 345 PHE A O   1 
ATOM 2736 C CB  . PHE A 1 345 ? 68.461 55.921  146.888 1.00 29.05  ? 345 PHE A CB  1 
ATOM 2737 C CG  . PHE A 1 345 ? 68.953 54.640  146.293 1.00 29.70  ? 345 PHE A CG  1 
ATOM 2738 C CD1 . PHE A 1 345 ? 68.223 53.466  146.414 1.00 30.06  ? 345 PHE A CD1 1 
ATOM 2739 C CD2 . PHE A 1 345 ? 70.144 54.584  145.636 1.00 29.35  ? 345 PHE A CD2 1 
ATOM 2740 C CE1 . PHE A 1 345 ? 68.688 52.274  145.885 1.00 29.69  ? 345 PHE A CE1 1 
ATOM 2741 C CE2 . PHE A 1 345 ? 70.589 53.381  145.113 1.00 29.81  ? 345 PHE A CE2 1 
ATOM 2742 C CZ  . PHE A 1 345 ? 69.873 52.243  145.237 1.00 30.11  ? 345 PHE A CZ  1 
ATOM 2743 N N   . SER A 1 346 ? 66.238 58.508  147.038 1.00 33.42  ? 346 SER A N   1 
ATOM 2744 C CA  . SER A 1 346 ? 65.568 59.430  147.954 1.00 35.09  ? 346 SER A CA  1 
ATOM 2745 C C   . SER A 1 346 ? 64.464 58.730  148.741 1.00 35.14  ? 346 SER A C   1 
ATOM 2746 O O   . SER A 1 346 ? 64.688 58.278  149.855 1.00 35.06  ? 346 SER A O   1 
ATOM 2747 C CB  . SER A 1 346 ? 64.971 60.618  147.184 1.00 36.65  ? 346 SER A CB  1 
ATOM 2748 O OG  . SER A 1 346 ? 63.834 60.226  146.424 1.00 38.97  ? 346 SER A OG  1 
ATOM 2749 N N   . ALA A 1 347 ? 63.283 58.633  148.139 1.00 35.90  ? 347 ALA A N   1 
ATOM 2750 C CA  . ALA A 1 347 ? 62.137 58.020  148.782 1.00 36.51  ? 347 ALA A CA  1 
ATOM 2751 C C   . ALA A 1 347 ? 62.545 56.866  149.650 1.00 37.19  ? 347 ALA A C   1 
ATOM 2752 O O   . ALA A 1 347 ? 62.218 56.831  150.827 1.00 37.35  ? 347 ALA A O   1 
ATOM 2753 C CB  . ALA A 1 347 ? 61.125 57.549  147.752 1.00 35.99  ? 347 ALA A CB  1 
ATOM 2754 N N   . THR A 1 348 ? 63.272 55.922  149.084 1.00 37.72  ? 348 THR A N   1 
ATOM 2755 C CA  . THR A 1 348 ? 63.659 54.782  149.871 1.00 39.12  ? 348 THR A CA  1 
ATOM 2756 C C   . THR A 1 348 ? 64.414 55.177  151.118 1.00 38.25  ? 348 THR A C   1 
ATOM 2757 O O   . THR A 1 348 ? 64.088 54.727  152.217 1.00 37.81  ? 348 THR A O   1 
ATOM 2758 C CB  . THR A 1 348 ? 64.511 53.847  149.073 1.00 41.59  ? 348 THR A CB  1 
ATOM 2759 O OG1 . THR A 1 348 ? 63.928 53.673  147.772 1.00 44.44  ? 348 THR A OG1 1 
ATOM 2760 C CG2 . THR A 1 348 ? 64.592 52.505  149.790 1.00 43.21  ? 348 THR A CG2 1 
ATOM 2761 N N   . ILE A 1 349 ? 65.424 56.022  150.947 1.00 38.63  ? 349 ILE A N   1 
ATOM 2762 C CA  . ILE A 1 349 ? 66.225 56.482  152.077 1.00 38.87  ? 349 ILE A CA  1 
ATOM 2763 C C   . ILE A 1 349 ? 65.330 56.884  153.255 1.00 37.65  ? 349 ILE A C   1 
ATOM 2764 O O   . ILE A 1 349 ? 65.407 56.296  154.337 1.00 37.29  ? 349 ILE A O   1 
ATOM 2765 C CB  . ILE A 1 349 ? 67.145 57.665  151.652 1.00 40.49  ? 349 ILE A CB  1 
ATOM 2766 C CG1 . ILE A 1 349 ? 68.296 57.105  150.810 1.00 41.43  ? 349 ILE A CG1 1 
ATOM 2767 C CG2 . ILE A 1 349 ? 67.663 58.419  152.872 1.00 40.24  ? 349 ILE A CG2 1 
ATOM 2768 C CD1 . ILE A 1 349 ? 69.230 58.151  150.221 1.00 42.94  ? 349 ILE A CD1 1 
ATOM 2769 N N   . TYR A 1 350 ? 64.465 57.867  153.033 1.00 35.73  ? 350 TYR A N   1 
ATOM 2770 C CA  . TYR A 1 350 ? 63.570 58.315  154.078 1.00 33.90  ? 350 TYR A CA  1 
ATOM 2771 C C   . TYR A 1 350 ? 62.859 57.119  154.665 1.00 33.54  ? 350 TYR A C   1 
ATOM 2772 O O   . TYR A 1 350 ? 63.033 56.794  155.828 1.00 33.56  ? 350 TYR A O   1 
ATOM 2773 C CB  . TYR A 1 350 ? 62.571 59.331  153.525 1.00 32.73  ? 350 TYR A CB  1 
ATOM 2774 C CG  . TYR A 1 350 ? 63.221 60.667  153.209 1.00 33.13  ? 350 TYR A CG  1 
ATOM 2775 C CD1 . TYR A 1 350 ? 64.614 60.821  153.254 1.00 33.69  ? 350 TYR A CD1 1 
ATOM 2776 C CD2 . TYR A 1 350 ? 62.457 61.776  152.853 1.00 33.15  ? 350 TYR A CD2 1 
ATOM 2777 C CE1 . TYR A 1 350 ? 65.226 62.039  152.951 1.00 33.11  ? 350 TYR A CE1 1 
ATOM 2778 C CE2 . TYR A 1 350 ? 63.070 63.005  152.547 1.00 33.60  ? 350 TYR A CE2 1 
ATOM 2779 C CZ  . TYR A 1 350 ? 64.454 63.122  152.597 1.00 32.78  ? 350 TYR A CZ  1 
ATOM 2780 O OH  . TYR A 1 350 ? 65.064 64.308  152.273 1.00 31.51  ? 350 TYR A OH  1 
ATOM 2781 N N   . LEU A 1 351 ? 62.080 56.442  153.848 1.00 33.63  ? 351 LEU A N   1 
ATOM 2782 C CA  . LEU A 1 351 ? 61.356 55.276  154.309 1.00 34.53  ? 351 LEU A CA  1 
ATOM 2783 C C   . LEU A 1 351 ? 62.159 54.404  155.232 1.00 34.01  ? 351 LEU A C   1 
ATOM 2784 O O   . LEU A 1 351 ? 61.759 54.154  156.351 1.00 34.43  ? 351 LEU A O   1 
ATOM 2785 C CB  . LEU A 1 351 ? 60.924 54.429  153.131 1.00 36.41  ? 351 LEU A CB  1 
ATOM 2786 C CG  . LEU A 1 351 ? 60.200 55.317  152.130 1.00 38.71  ? 351 LEU A CG  1 
ATOM 2787 C CD1 . LEU A 1 351 ? 60.122 54.651  150.782 1.00 39.47  ? 351 LEU A CD1 1 
ATOM 2788 C CD2 . LEU A 1 351 ? 58.845 55.650  152.694 1.00 39.22  ? 351 LEU A CD2 1 
ATOM 2789 N N   . VAL A 1 352 ? 63.310 53.944  154.774 1.00 34.18  ? 352 VAL A N   1 
ATOM 2790 C CA  . VAL A 1 352 ? 64.108 53.051  155.597 1.00 34.83  ? 352 VAL A CA  1 
ATOM 2791 C C   . VAL A 1 352 ? 64.934 53.694  156.689 1.00 33.93  ? 352 VAL A C   1 
ATOM 2792 O O   . VAL A 1 352 ? 64.876 53.281  157.850 1.00 32.97  ? 352 VAL A O   1 
ATOM 2793 C CB  . VAL A 1 352 ? 65.035 52.204  154.738 1.00 35.29  ? 352 VAL A CB  1 
ATOM 2794 C CG1 . VAL A 1 352 ? 65.914 51.344  155.624 1.00 35.51  ? 352 VAL A CG1 1 
ATOM 2795 C CG2 . VAL A 1 352 ? 64.215 51.338  153.815 1.00 35.83  ? 352 VAL A CG2 1 
ATOM 2796 N N   . CYS A 1 353 ? 65.720 54.687  156.308 1.00 34.32  ? 353 CYS A N   1 
ATOM 2797 C CA  . CYS A 1 353 ? 66.574 55.377  157.253 1.00 35.68  ? 353 CYS A CA  1 
ATOM 2798 C C   . CYS A 1 353 ? 65.824 56.295  158.220 1.00 36.40  ? 353 CYS A C   1 
ATOM 2799 O O   . CYS A 1 353 ? 66.213 56.383  159.370 1.00 37.31  ? 353 CYS A O   1 
ATOM 2800 C CB  . CYS A 1 353 ? 67.645 56.192  156.507 1.00 35.34  ? 353 CYS A CB  1 
ATOM 2801 S SG  . CYS A 1 353 ? 68.973 56.900  157.529 1.00 34.87  ? 353 CYS A SG  1 
ATOM 2802 N N   . PHE A 1 354 ? 64.746 56.954  157.787 1.00 37.38  ? 354 PHE A N   1 
ATOM 2803 C CA  . PHE A 1 354 ? 64.025 57.890  158.673 1.00 37.78  ? 354 PHE A CA  1 
ATOM 2804 C C   . PHE A 1 354 ? 62.721 57.457  159.332 1.00 37.85  ? 354 PHE A C   1 
ATOM 2805 O O   . PHE A 1 354 ? 62.347 58.001  160.365 1.00 38.14  ? 354 PHE A O   1 
ATOM 2806 C CB  . PHE A 1 354 ? 63.784 59.237  157.959 1.00 37.90  ? 354 PHE A CB  1 
ATOM 2807 C CG  . PHE A 1 354 ? 64.992 60.148  157.959 1.00 37.62  ? 354 PHE A CG  1 
ATOM 2808 C CD1 . PHE A 1 354 ? 66.198 59.708  157.414 1.00 35.86  ? 354 PHE A CD1 1 
ATOM 2809 C CD2 . PHE A 1 354 ? 64.953 61.403  158.577 1.00 38.03  ? 354 PHE A CD2 1 
ATOM 2810 C CE1 . PHE A 1 354 ? 67.346 60.480  157.491 1.00 34.81  ? 354 PHE A CE1 1 
ATOM 2811 C CE2 . PHE A 1 354 ? 66.113 62.196  158.661 1.00 37.57  ? 354 PHE A CE2 1 
ATOM 2812 C CZ  . PHE A 1 354 ? 67.309 61.722  158.116 1.00 36.26  ? 354 PHE A CZ  1 
ATOM 2813 N N   . CYS A 1 355 ? 62.025 56.499  158.742 1.00 37.43  ? 355 CYS A N   1 
ATOM 2814 C CA  . CYS A 1 355 ? 60.786 56.038  159.320 1.00 37.18  ? 355 CYS A CA  1 
ATOM 2815 C C   . CYS A 1 355 ? 60.955 54.671  159.973 1.00 37.36  ? 355 CYS A C   1 
ATOM 2816 O O   . CYS A 1 355 ? 60.658 54.524  161.133 1.00 37.56  ? 355 CYS A O   1 
ATOM 2817 C CB  . CYS A 1 355 ? 59.712 55.988  158.246 1.00 37.37  ? 355 CYS A CB  1 
ATOM 2818 S SG  . CYS A 1 355 ? 58.309 57.039  158.509 1.00 37.21  ? 355 CYS A SG  1 
ATOM 2819 N N   . PHE A 1 356 ? 61.461 53.674  159.267 1.00 37.66  ? 356 PHE A N   1 
ATOM 2820 C CA  . PHE A 1 356 ? 61.577 52.396  159.916 1.00 38.93  ? 356 PHE A CA  1 
ATOM 2821 C C   . PHE A 1 356 ? 62.759 52.355  160.843 1.00 40.34  ? 356 PHE A C   1 
ATOM 2822 O O   . PHE A 1 356 ? 62.811 51.507  161.722 1.00 41.76  ? 356 PHE A O   1 
ATOM 2823 C CB  . PHE A 1 356 ? 61.698 51.269  158.913 1.00 37.60  ? 356 PHE A CB  1 
ATOM 2824 C CG  . PHE A 1 356 ? 62.134 49.986  159.531 1.00 37.13  ? 356 PHE A CG  1 
ATOM 2825 C CD1 . PHE A 1 356 ? 61.250 49.176  160.208 1.00 36.72  ? 356 PHE A CD1 1 
ATOM 2826 C CD2 . PHE A 1 356 ? 63.462 49.646  159.546 1.00 36.33  ? 356 PHE A CD2 1 
ATOM 2827 C CE1 . PHE A 1 356 ? 61.712 48.046  160.898 1.00 36.60  ? 356 PHE A CE1 1 
ATOM 2828 C CE2 . PHE A 1 356 ? 63.913 48.524  160.235 1.00 35.39  ? 356 PHE A CE2 1 
ATOM 2829 C CZ  . PHE A 1 356 ? 63.051 47.733  160.906 1.00 35.68  ? 356 PHE A CZ  1 
ATOM 2830 N N   . PHE A 1 357 ? 63.703 53.268  160.686 1.00 41.63  ? 357 PHE A N   1 
ATOM 2831 C CA  . PHE A 1 357 ? 64.837 53.200  161.570 1.00 42.59  ? 357 PHE A CA  1 
ATOM 2832 C C   . PHE A 1 357 ? 65.043 54.233  162.663 1.00 41.45  ? 357 PHE A C   1 
ATOM 2833 O O   . PHE A 1 357 ? 65.729 53.986  163.664 1.00 41.26  ? 357 PHE A O   1 
ATOM 2834 C CB  . PHE A 1 357 ? 66.084 53.054  160.735 1.00 44.81  ? 357 PHE A CB  1 
ATOM 2835 C CG  . PHE A 1 357 ? 66.491 51.659  160.580 1.00 47.18  ? 357 PHE A CG  1 
ATOM 2836 C CD1 . PHE A 1 357 ? 66.925 50.949  161.692 1.00 47.91  ? 357 PHE A CD1 1 
ATOM 2837 C CD2 . PHE A 1 357 ? 66.428 51.034  159.352 1.00 48.36  ? 357 PHE A CD2 1 
ATOM 2838 C CE1 . PHE A 1 357 ? 67.290 49.628  161.596 1.00 48.99  ? 357 PHE A CE1 1 
ATOM 2839 C CE2 . PHE A 1 357 ? 66.792 49.702  159.237 1.00 50.35  ? 357 PHE A CE2 1 
ATOM 2840 C CZ  . PHE A 1 357 ? 67.229 48.991  160.365 1.00 50.28  ? 357 PHE A CZ  1 
ATOM 2841 N N   . LYS A 1 358 ? 64.453 55.395  162.483 1.00 39.85  ? 358 LYS A N   1 
ATOM 2842 C CA  . LYS A 1 358 ? 64.580 56.421  163.488 1.00 38.93  ? 358 LYS A CA  1 
ATOM 2843 C C   . LYS A 1 358 ? 63.506 56.181  164.530 1.00 38.32  ? 358 LYS A C   1 
ATOM 2844 O O   . LYS A 1 358 ? 63.811 55.927  165.680 1.00 38.39  ? 358 LYS A O   1 
ATOM 2845 C CB  . LYS A 1 358 ? 64.408 57.793  162.857 1.00 39.94  ? 358 LYS A CB  1 
ATOM 2846 C CG  . LYS A 1 358 ? 64.137 58.918  163.843 1.00 42.32  ? 358 LYS A CG  1 
ATOM 2847 C CD  . LYS A 1 358 ? 63.682 60.171  163.086 1.00 45.41  ? 358 LYS A CD  1 
ATOM 2848 C CE  . LYS A 1 358 ? 63.265 61.348  163.984 1.00 47.86  ? 358 LYS A CE  1 
ATOM 2849 N NZ  . LYS A 1 358 ? 62.674 62.470  163.177 1.00 49.23  ? 358 LYS A NZ  1 
ATOM 2850 N N   . GLN A 1 359 ? 62.247 56.250  164.121 1.00 37.75  ? 359 GLN A N   1 
ATOM 2851 C CA  . GLN A 1 359 ? 61.133 56.041  165.030 1.00 37.31  ? 359 GLN A CA  1 
ATOM 2852 C C   . GLN A 1 359 ? 61.346 54.816  165.922 1.00 36.43  ? 359 GLN A C   1 
ATOM 2853 O O   . GLN A 1 359 ? 61.128 54.872  167.132 1.00 36.42  ? 359 GLN A O   1 
ATOM 2854 C CB  . GLN A 1 359 ? 59.836 55.893  164.227 1.00 38.21  ? 359 GLN A CB  1 
ATOM 2855 C CG  . GLN A 1 359 ? 59.535 57.069  163.268 1.00 39.38  ? 359 GLN A CG  1 
ATOM 2856 C CD  . GLN A 1 359 ? 59.421 58.400  163.993 1.00 39.64  ? 359 GLN A CD  1 
ATOM 2857 O OE1 . GLN A 1 359 ? 59.561 58.448  165.207 1.00 40.38  ? 359 GLN A OE1 1 
ATOM 2858 N NE2 . GLN A 1 359 ? 59.165 59.483  163.255 1.00 39.71  ? 359 GLN A NE2 1 
ATOM 2859 N N   . LEU A 1 360 ? 61.787 53.710  165.338 1.00 35.45  ? 360 LEU A N   1 
ATOM 2860 C CA  . LEU A 1 360 ? 62.013 52.509  166.130 1.00 35.30  ? 360 LEU A CA  1 
ATOM 2861 C C   . LEU A 1 360 ? 62.910 52.808  167.326 1.00 34.80  ? 360 LEU A C   1 
ATOM 2862 O O   . LEU A 1 360 ? 62.547 52.520  168.464 1.00 35.50  ? 360 LEU A O   1 
ATOM 2863 C CB  . LEU A 1 360 ? 62.646 51.399  165.283 1.00 36.19  ? 360 LEU A CB  1 
ATOM 2864 C CG  . LEU A 1 360 ? 63.046 50.174  166.119 1.00 36.99  ? 360 LEU A CG  1 
ATOM 2865 C CD1 . LEU A 1 360 ? 61.815 49.632  166.838 1.00 36.90  ? 360 LEU A CD1 1 
ATOM 2866 C CD2 . LEU A 1 360 ? 63.681 49.109  165.238 1.00 36.74  ? 360 LEU A CD2 1 
ATOM 2867 N N   . ALA A 1 361 ? 64.078 53.386  167.060 1.00 33.77  ? 361 ALA A N   1 
ATOM 2868 C CA  . ALA A 1 361 ? 65.027 53.737  168.113 1.00 32.39  ? 361 ALA A CA  1 
ATOM 2869 C C   . ALA A 1 361 ? 64.342 54.510  169.213 1.00 31.32  ? 361 ALA A C   1 
ATOM 2870 O O   . ALA A 1 361 ? 64.554 54.257  170.392 1.00 32.13  ? 361 ALA A O   1 
ATOM 2871 C CB  . ALA A 1 361 ? 66.152 54.574  167.550 1.00 32.91  ? 361 ALA A CB  1 
ATOM 2872 N N   . MET A 1 362 ? 63.517 55.464  168.834 1.00 29.90  ? 362 MET A N   1 
ATOM 2873 C CA  . MET A 1 362 ? 62.847 56.241  169.843 1.00 28.76  ? 362 MET A CA  1 
ATOM 2874 C C   . MET A 1 362 ? 61.995 55.393  170.776 1.00 27.62  ? 362 MET A C   1 
ATOM 2875 O O   . MET A 1 362 ? 62.170 55.445  171.985 1.00 27.07  ? 362 MET A O   1 
ATOM 2876 C CB  . MET A 1 362 ? 62.050 57.346  169.174 1.00 29.72  ? 362 MET A CB  1 
ATOM 2877 C CG  . MET A 1 362 ? 62.957 58.219  168.320 1.00 30.54  ? 362 MET A CG  1 
ATOM 2878 S SD  . MET A 1 362 ? 62.242 59.791  167.888 1.00 32.54  ? 362 MET A SD  1 
ATOM 2879 C CE  . MET A 1 362 ? 61.855 60.420  169.494 1.00 33.21  ? 362 MET A CE  1 
ATOM 2880 N N   . ILE A 1 363 ? 61.098 54.584  170.243 1.00 26.57  ? 363 ILE A N   1 
ATOM 2881 C CA  . ILE A 1 363 ? 60.293 53.771  171.131 1.00 26.21  ? 363 ILE A CA  1 
ATOM 2882 C C   . ILE A 1 363 ? 61.170 53.171  172.212 1.00 26.83  ? 363 ILE A C   1 
ATOM 2883 O O   . ILE A 1 363 ? 60.750 53.038  173.337 1.00 27.00  ? 363 ILE A O   1 
ATOM 2884 C CB  . ILE A 1 363 ? 59.594 52.635  170.389 1.00 26.01  ? 363 ILE A CB  1 
ATOM 2885 C CG1 . ILE A 1 363 ? 58.705 53.214  169.292 1.00 25.03  ? 363 ILE A CG1 1 
ATOM 2886 C CG2 . ILE A 1 363 ? 58.759 51.824  171.356 1.00 25.73  ? 363 ILE A CG2 1 
ATOM 2887 C CD1 . ILE A 1 363 ? 57.992 52.187  168.461 1.00 23.64  ? 363 ILE A CD1 1 
ATOM 2888 N N   . PHE A 1 364 ? 62.400 52.815  171.898 1.00 27.85  ? 364 PHE A N   1 
ATOM 2889 C CA  . PHE A 1 364 ? 63.217 52.241  172.942 1.00 29.05  ? 364 PHE A CA  1 
ATOM 2890 C C   . PHE A 1 364 ? 63.922 53.249  173.804 1.00 29.06  ? 364 PHE A C   1 
ATOM 2891 O O   . PHE A 1 364 ? 63.749 53.269  175.024 1.00 28.93  ? 364 PHE A O   1 
ATOM 2892 C CB  . PHE A 1 364 ? 64.243 51.292  172.364 1.00 31.00  ? 364 PHE A CB  1 
ATOM 2893 C CG  . PHE A 1 364 ? 63.721 49.925  172.147 1.00 33.69  ? 364 PHE A CG  1 
ATOM 2894 C CD1 . PHE A 1 364 ? 62.358 49.677  172.179 1.00 34.64  ? 364 PHE A CD1 1 
ATOM 2895 C CD2 . PHE A 1 364 ? 64.594 48.872  171.923 1.00 35.12  ? 364 PHE A CD2 1 
ATOM 2896 C CE1 . PHE A 1 364 ? 61.867 48.391  171.993 1.00 36.16  ? 364 PHE A CE1 1 
ATOM 2897 C CE2 . PHE A 1 364 ? 64.118 47.574  171.734 1.00 36.13  ? 364 PHE A CE2 1 
ATOM 2898 C CZ  . PHE A 1 364 ? 62.751 47.330  171.769 1.00 36.53  ? 364 PHE A CZ  1 
ATOM 2899 N N   . MET A 1 365 ? 64.731 54.085  173.176 1.00 28.27  ? 365 MET A N   1 
ATOM 2900 C CA  . MET A 1 365 ? 65.466 55.066  173.932 1.00 28.13  ? 365 MET A CA  1 
ATOM 2901 C C   . MET A 1 365 ? 64.526 55.912  174.768 1.00 28.54  ? 365 MET A C   1 
ATOM 2902 O O   . MET A 1 365 ? 64.872 56.276  175.888 1.00 29.76  ? 365 MET A O   1 
ATOM 2903 C CB  . MET A 1 365 ? 66.317 55.927  173.002 1.00 26.93  ? 365 MET A CB  1 
ATOM 2904 C CG  . MET A 1 365 ? 67.419 55.143  172.344 1.00 26.92  ? 365 MET A CG  1 
ATOM 2905 S SD  . MET A 1 365 ? 68.533 56.136  171.455 1.00 26.91  ? 365 MET A SD  1 
ATOM 2906 C CE  . MET A 1 365 ? 69.589 56.659  172.682 1.00 27.64  ? 365 MET A CE  1 
ATOM 2907 N N   . SER A 1 366 ? 63.328 56.195  174.254 1.00 28.37  ? 366 SER A N   1 
ATOM 2908 C CA  . SER A 1 366 ? 62.359 57.014  175.004 1.00 28.34  ? 366 SER A CA  1 
ATOM 2909 C C   . SER A 1 366 ? 62.129 56.422  176.387 1.00 28.81  ? 366 SER A C   1 
ATOM 2910 O O   . SER A 1 366 ? 62.302 57.078  177.416 1.00 29.10  ? 366 SER A O   1 
ATOM 2911 C CB  . SER A 1 366 ? 60.997 57.078  174.303 1.00 27.26  ? 366 SER A CB  1 
ATOM 2912 O OG  . SER A 1 366 ? 61.080 57.540  172.969 1.00 29.24  ? 366 SER A OG  1 
ATOM 2913 N N   . VAL A 1 367 ? 61.724 55.166  176.391 1.00 29.34  ? 367 VAL A N   1 
ATOM 2914 C CA  . VAL A 1 367 ? 61.457 54.458  177.615 1.00 29.91  ? 367 VAL A CA  1 
ATOM 2915 C C   . VAL A 1 367 ? 62.705 54.454  178.480 1.00 30.01  ? 367 VAL A C   1 
ATOM 2916 O O   . VAL A 1 367 ? 62.662 54.881  179.627 1.00 29.60  ? 367 VAL A O   1 
ATOM 2917 C CB  . VAL A 1 367 ? 60.972 53.030  177.282 1.00 30.71  ? 367 VAL A CB  1 
ATOM 2918 C CG1 . VAL A 1 367 ? 60.815 52.211  178.523 1.00 31.97  ? 367 VAL A CG1 1 
ATOM 2919 C CG2 . VAL A 1 367 ? 59.629 53.115  176.562 1.00 30.61  ? 367 VAL A CG2 1 
ATOM 2920 N N   . LEU A 1 368 ? 63.827 54.012  177.924 1.00 31.41  ? 368 LEU A N   1 
ATOM 2921 C CA  . LEU A 1 368 ? 65.067 53.991  178.688 1.00 33.92  ? 368 LEU A CA  1 
ATOM 2922 C C   . LEU A 1 368 ? 65.199 55.355  179.334 1.00 35.13  ? 368 LEU A C   1 
ATOM 2923 O O   . LEU A 1 368 ? 65.379 55.486  180.545 1.00 35.20  ? 368 LEU A O   1 
ATOM 2924 C CB  . LEU A 1 368 ? 66.284 53.753  177.784 1.00 34.29  ? 368 LEU A CB  1 
ATOM 2925 C CG  . LEU A 1 368 ? 67.612 53.648  178.551 1.00 35.27  ? 368 LEU A CG  1 
ATOM 2926 C CD1 . LEU A 1 368 ? 67.683 52.289  179.247 1.00 35.30  ? 368 LEU A CD1 1 
ATOM 2927 C CD2 . LEU A 1 368 ? 68.799 53.810  177.626 1.00 34.58  ? 368 LEU A CD2 1 
ATOM 2928 N N   . ALA A 1 369 ? 65.089 56.376  178.504 1.00 36.75  ? 369 ALA A N   1 
ATOM 2929 C CA  . ALA A 1 369 ? 65.194 57.751  178.954 1.00 38.11  ? 369 ALA A CA  1 
ATOM 2930 C C   . ALA A 1 369 ? 64.283 57.981  180.129 1.00 39.11  ? 369 ALA A C   1 
ATOM 2931 O O   . ALA A 1 369 ? 64.738 58.310  181.220 1.00 39.70  ? 369 ALA A O   1 
ATOM 2932 C CB  . ALA A 1 369 ? 64.807 58.674  177.832 1.00 39.89  ? 369 ALA A CB  1 
ATOM 2933 N N   . GLY A 1 370 ? 62.986 57.823  179.878 1.00 40.16  ? 370 GLY A N   1 
ATOM 2934 C CA  . GLY A 1 370 ? 62.004 58.010  180.919 1.00 41.96  ? 370 GLY A CA  1 
ATOM 2935 C C   . GLY A 1 370 ? 62.574 57.482  182.211 1.00 43.13  ? 370 GLY A C   1 
ATOM 2936 O O   . GLY A 1 370 ? 62.983 58.236  183.082 1.00 42.56  ? 370 GLY A O   1 
ATOM 2937 N N   . ASN A 1 371 ? 62.617 56.168  182.327 1.00 44.56  ? 371 ASN A N   1 
ATOM 2938 C CA  . ASN A 1 371 ? 63.154 55.533  183.517 1.00 46.13  ? 371 ASN A CA  1 
ATOM 2939 C C   . ASN A 1 371 ? 64.357 56.277  184.055 1.00 46.41  ? 371 ASN A C   1 
ATOM 2940 O O   . ASN A 1 371 ? 64.331 56.760  185.180 1.00 45.88  ? 371 ASN A O   1 
ATOM 2941 C CB  . ASN A 1 371 ? 63.545 54.105  183.180 1.00 47.91  ? 371 ASN A CB  1 
ATOM 2942 C CG  . ASN A 1 371 ? 62.389 53.316  182.617 1.00 48.90  ? 371 ASN A CG  1 
ATOM 2943 O OD1 . ASN A 1 371 ? 62.519 52.647  181.593 1.00 50.77  ? 371 ASN A OD1 1 
ATOM 2944 N ND2 . ASN A 1 371 ? 61.243 53.394  183.281 1.00 48.78  ? 371 ASN A ND2 1 
ATOM 2945 N N   . MET A 1 372 ? 65.406 56.360  183.242 1.00 47.11  ? 372 MET A N   1 
ATOM 2946 C CA  . MET A 1 372 ? 66.632 57.047  183.629 1.00 47.24  ? 372 MET A CA  1 
ATOM 2947 C C   . MET A 1 372 ? 66.301 58.311  184.402 1.00 46.68  ? 372 MET A C   1 
ATOM 2948 O O   . MET A 1 372 ? 66.873 58.565  185.464 1.00 46.49  ? 372 MET A O   1 
ATOM 2949 C CB  . MET A 1 372 ? 67.434 57.417  182.388 1.00 48.20  ? 372 MET A CB  1 
ATOM 2950 C CG  . MET A 1 372 ? 67.985 56.247  181.617 1.00 48.44  ? 372 MET A CG  1 
ATOM 2951 S SD  . MET A 1 372 ? 69.076 56.840  180.339 1.00 49.84  ? 372 MET A SD  1 
ATOM 2952 C CE  . MET A 1 372 ? 70.553 57.214  181.316 1.00 49.78  ? 372 MET A CE  1 
ATOM 2953 N N   . TYR A 1 373 ? 65.386 59.106  183.847 1.00 46.66  ? 373 TYR A N   1 
ATOM 2954 C CA  . TYR A 1 373 ? 64.948 60.361  184.473 1.00 46.57  ? 373 TYR A CA  1 
ATOM 2955 C C   . TYR A 1 373 ? 64.456 60.054  185.893 1.00 47.62  ? 373 TYR A C   1 
ATOM 2956 O O   . TYR A 1 373 ? 65.021 60.533  186.886 1.00 47.75  ? 373 TYR A O   1 
ATOM 2957 C CB  . TYR A 1 373 ? 63.784 60.978  183.677 1.00 43.87  ? 373 TYR A CB  1 
ATOM 2958 C CG  . TYR A 1 373 ? 64.083 61.597  182.317 1.00 40.88  ? 373 TYR A CG  1 
ATOM 2959 C CD1 . TYR A 1 373 ? 64.889 62.707  182.198 1.00 39.86  ? 373 TYR A CD1 1 
ATOM 2960 C CD2 . TYR A 1 373 ? 63.451 61.148  181.169 1.00 39.20  ? 373 TYR A CD2 1 
ATOM 2961 C CE1 . TYR A 1 373 ? 65.046 63.361  180.971 1.00 38.14  ? 373 TYR A CE1 1 
ATOM 2962 C CE2 . TYR A 1 373 ? 63.608 61.805  179.953 1.00 37.55  ? 373 TYR A CE2 1 
ATOM 2963 C CZ  . TYR A 1 373 ? 64.401 62.910  179.866 1.00 37.25  ? 373 TYR A CZ  1 
ATOM 2964 O OH  . TYR A 1 373 ? 64.512 63.598  178.689 1.00 36.02  ? 373 TYR A OH  1 
ATOM 2965 N N   . GLU A 1 374 ? 63.392 59.252  185.952 1.00 48.52  ? 374 GLU A N   1 
ATOM 2966 C CA  . GLU A 1 374 ? 62.769 58.851  187.205 1.00 48.97  ? 374 GLU A CA  1 
ATOM 2967 C C   . GLU A 1 374 ? 63.806 58.386  188.197 1.00 47.92  ? 374 GLU A C   1 
ATOM 2968 O O   . GLU A 1 374 ? 63.890 58.900  189.299 1.00 48.51  ? 374 GLU A O   1 
ATOM 2969 C CB  . GLU A 1 374 ? 61.830 57.687  186.976 1.00 50.39  ? 374 GLU A CB  1 
ATOM 2970 C CG  . GLU A 1 374 ? 60.816 57.465  188.075 1.00 53.04  ? 374 GLU A CG  1 
ATOM 2971 C CD  . GLU A 1 374 ? 59.916 56.302  187.758 1.00 54.86  ? 374 GLU A CD  1 
ATOM 2972 O OE1 . GLU A 1 374 ? 59.489 56.225  186.576 1.00 55.96  ? 374 GLU A OE1 1 
ATOM 2973 O OE2 . GLU A 1 374 ? 59.625 55.477  188.663 1.00 55.95  ? 374 GLU A OE2 1 
ATOM 2974 N N   . SER A 1 375 ? 64.599 57.415  187.760 1.00 47.35  ? 375 SER A N   1 
ATOM 2975 C CA  . SER A 1 375 ? 65.625 56.793  188.582 1.00 46.80  ? 375 SER A CA  1 
ATOM 2976 C C   . SER A 1 375 ? 66.950 57.504  188.762 1.00 45.35  ? 375 SER A C   1 
ATOM 2977 O O   . SER A 1 375 ? 67.768 57.114  189.602 1.00 44.27  ? 375 SER A O   1 
ATOM 2978 C CB  . SER A 1 375 ? 65.918 55.382  188.068 1.00 48.25  ? 375 SER A CB  1 
ATOM 2979 O OG  . SER A 1 375 ? 66.307 55.386  186.684 1.00 48.50  ? 375 SER A OG  1 
ATOM 2980 N N   . ILE A 1 376 ? 67.196 58.539  187.986 1.00 43.15  ? 376 ILE A N   1 
ATOM 2981 C CA  . ILE A 1 376 ? 68.467 59.211  188.116 1.00 41.35  ? 376 ILE A CA  1 
ATOM 2982 C C   . ILE A 1 376 ? 68.345 60.703  188.195 1.00 39.59  ? 376 ILE A C   1 
ATOM 2983 O O   . ILE A 1 376 ? 69.207 61.358  188.774 1.00 40.55  ? 376 ILE A O   1 
ATOM 2984 C CB  . ILE A 1 376 ? 69.371 58.839  186.957 1.00 41.54  ? 376 ILE A CB  1 
ATOM 2985 C CG1 . ILE A 1 376 ? 69.701 57.357  187.073 1.00 42.84  ? 376 ILE A CG1 1 
ATOM 2986 C CG2 . ILE A 1 376 ? 70.609 59.725  186.957 1.00 41.63  ? 376 ILE A CG2 1 
ATOM 2987 C CD1 . ILE A 1 376 ? 70.621 56.838  185.979 1.00 44.26  ? 376 ILE A CD1 1 
ATOM 2988 N N   . GLY A 1 377 ? 67.281 61.238  187.610 1.00 37.19  ? 377 GLY A N   1 
ATOM 2989 C CA  . GLY A 1 377 ? 67.089 62.671  187.633 1.00 34.69  ? 377 GLY A CA  1 
ATOM 2990 C C   . GLY A 1 377 ? 67.494 63.297  186.319 1.00 31.38  ? 377 GLY A C   1 
ATOM 2991 O O   . GLY A 1 377 ? 68.485 62.907  185.720 1.00 30.62  ? 377 GLY A O   1 
ATOM 2992 N N   . PHE A 1 378 ? 66.725 64.281  185.885 1.00 29.01  ? 378 PHE A N   1 
ATOM 2993 C CA  . PHE A 1 378 ? 66.981 64.955  184.637 1.00 26.96  ? 378 PHE A CA  1 
ATOM 2994 C C   . PHE A 1 378 ? 68.430 65.124  184.272 1.00 27.08  ? 378 PHE A C   1 
ATOM 2995 O O   . PHE A 1 378 ? 68.931 64.461  183.372 1.00 26.97  ? 378 PHE A O   1 
ATOM 2996 C CB  . PHE A 1 378 ? 66.343 66.324  184.640 1.00 24.61  ? 378 PHE A CB  1 
ATOM 2997 C CG  . PHE A 1 378 ? 64.865 66.295  184.501 1.00 22.52  ? 378 PHE A CG  1 
ATOM 2998 C CD1 . PHE A 1 378 ? 64.070 65.757  185.484 1.00 22.30  ? 378 PHE A CD1 1 
ATOM 2999 C CD2 . PHE A 1 378 ? 64.265 66.831  183.398 1.00 20.31  ? 378 PHE A CD2 1 
ATOM 3000 C CE1 . PHE A 1 378 ? 62.700 65.755  185.355 1.00 21.59  ? 378 PHE A CE1 1 
ATOM 3001 C CE2 . PHE A 1 378 ? 62.901 66.829  183.268 1.00 19.97  ? 378 PHE A CE2 1 
ATOM 3002 C CZ  . PHE A 1 378 ? 62.123 66.292  184.253 1.00 21.12  ? 378 PHE A CZ  1 
ATOM 3003 N N   . GLN A 1 379 ? 69.108 66.025  184.966 1.00 28.42  ? 379 GLN A N   1 
ATOM 3004 C CA  . GLN A 1 379 ? 70.502 66.287  184.652 1.00 29.55  ? 379 GLN A CA  1 
ATOM 3005 C C   . GLN A 1 379 ? 71.328 65.016  184.712 1.00 29.72  ? 379 GLN A C   1 
ATOM 3006 O O   . GLN A 1 379 ? 72.246 64.827  183.918 1.00 29.62  ? 379 GLN A O   1 
ATOM 3007 C CB  . GLN A 1 379 ? 71.080 67.354  185.590 1.00 30.80  ? 379 GLN A CB  1 
ATOM 3008 C CG  . GLN A 1 379 ? 70.221 68.606  185.695 1.00 32.82  ? 379 GLN A CG  1 
ATOM 3009 C CD  . GLN A 1 379 ? 71.003 69.909  185.610 1.00 33.97  ? 379 GLN A CD  1 
ATOM 3010 O OE1 . GLN A 1 379 ? 70.423 70.987  185.652 1.00 35.55  ? 379 GLN A OE1 1 
ATOM 3011 N NE2 . GLN A 1 379 ? 72.312 69.815  185.479 1.00 34.31  ? 379 GLN A NE2 1 
ATOM 3012 N N   . GLY A 1 380 ? 70.984 64.135  185.643 1.00 29.41  ? 380 GLY A N   1 
ATOM 3013 C CA  . GLY A 1 380 ? 71.716 62.891  185.768 1.00 29.38  ? 380 GLY A CA  1 
ATOM 3014 C C   . GLY A 1 380 ? 71.757 62.162  184.445 1.00 28.69  ? 380 GLY A C   1 
ATOM 3015 O O   . GLY A 1 380 ? 72.809 62.044  183.815 1.00 28.38  ? 380 GLY A O   1 
ATOM 3016 N N   . ALA A 1 381 ? 70.592 61.683  184.020 1.00 28.51  ? 381 ALA A N   1 
ATOM 3017 C CA  . ALA A 1 381 ? 70.465 60.957  182.758 1.00 27.54  ? 381 ALA A CA  1 
ATOM 3018 C C   . ALA A 1 381 ? 71.244 61.672  181.690 1.00 26.31  ? 381 ALA A C   1 
ATOM 3019 O O   . ALA A 1 381 ? 72.092 61.098  181.013 1.00 24.71  ? 381 ALA A O   1 
ATOM 3020 C CB  . ALA A 1 381 ? 69.001 60.873  182.349 1.00 28.74  ? 381 ALA A CB  1 
ATOM 3021 N N   . TYR A 1 382 ? 70.938 62.951  181.564 1.00 25.87  ? 382 TYR A N   1 
ATOM 3022 C CA  . TYR A 1 382 ? 71.557 63.800  180.571 1.00 25.52  ? 382 TYR A CA  1 
ATOM 3023 C C   . TYR A 1 382 ? 72.986 63.418  180.280 1.00 23.65  ? 382 TYR A C   1 
ATOM 3024 O O   . TYR A 1 382 ? 73.354 63.222  179.134 1.00 22.95  ? 382 TYR A O   1 
ATOM 3025 C CB  . TYR A 1 382 ? 71.403 65.261  180.998 1.00 27.33  ? 382 TYR A CB  1 
ATOM 3026 C CG  . TYR A 1 382 ? 69.954 65.708  180.875 1.00 29.67  ? 382 TYR A CG  1 
ATOM 3027 C CD1 . TYR A 1 382 ? 68.929 64.780  180.675 1.00 29.99  ? 382 TYR A CD1 1 
ATOM 3028 C CD2 . TYR A 1 382 ? 69.610 67.050  180.901 1.00 31.34  ? 382 TYR A CD2 1 
ATOM 3029 C CE1 . TYR A 1 382 ? 67.606 65.187  180.500 1.00 31.45  ? 382 TYR A CE1 1 
ATOM 3030 C CE2 . TYR A 1 382 ? 68.286 67.465  180.721 1.00 32.04  ? 382 TYR A CE2 1 
ATOM 3031 C CZ  . TYR A 1 382 ? 67.293 66.535  180.522 1.00 31.88  ? 382 TYR A CZ  1 
ATOM 3032 O OH  . TYR A 1 382 ? 65.997 66.983  180.346 1.00 32.62  ? 382 TYR A OH  1 
ATOM 3033 N N   . LEU A 1 383 ? 73.801 63.268  181.300 1.00 22.11  ? 383 LEU A N   1 
ATOM 3034 C CA  . LEU A 1 383 ? 75.146 62.871  180.993 1.00 21.66  ? 383 LEU A CA  1 
ATOM 3035 C C   . LEU A 1 383 ? 75.105 61.725  179.999 1.00 20.95  ? 383 LEU A C   1 
ATOM 3036 O O   . LEU A 1 383 ? 75.668 61.808  178.914 1.00 20.15  ? 383 LEU A O   1 
ATOM 3037 C CB  . LEU A 1 383 ? 75.850 62.422  182.246 1.00 22.98  ? 383 LEU A CB  1 
ATOM 3038 C CG  . LEU A 1 383 ? 76.249 63.548  183.170 1.00 24.20  ? 383 LEU A CG  1 
ATOM 3039 C CD1 . LEU A 1 383 ? 76.887 62.980  184.425 1.00 26.12  ? 383 LEU A CD1 1 
ATOM 3040 C CD2 . LEU A 1 383 ? 77.207 64.449  182.424 1.00 24.51  ? 383 LEU A CD2 1 
ATOM 3041 N N   . VAL A 1 384 ? 74.420 60.655  180.359 1.00 21.04  ? 384 VAL A N   1 
ATOM 3042 C CA  . VAL A 1 384 ? 74.371 59.511  179.483 1.00 21.63  ? 384 VAL A CA  1 
ATOM 3043 C C   . VAL A 1 384 ? 74.045 59.918  178.072 1.00 20.75  ? 384 VAL A C   1 
ATOM 3044 O O   . VAL A 1 384 ? 74.800 59.644  177.152 1.00 21.27  ? 384 VAL A O   1 
ATOM 3045 C CB  . VAL A 1 384 ? 73.344 58.483  179.974 1.00 22.29  ? 384 VAL A CB  1 
ATOM 3046 C CG1 . VAL A 1 384 ? 73.280 57.287  179.024 1.00 23.92  ? 384 VAL A CG1 1 
ATOM 3047 C CG2 . VAL A 1 384 ? 73.749 58.015  181.349 1.00 22.13  ? 384 VAL A CG2 1 
ATOM 3048 N N   . LEU A 1 385 ? 72.943 60.617  177.890 1.00 19.53  ? 385 LEU A N   1 
ATOM 3049 C CA  . LEU A 1 385 ? 72.570 60.991  176.542 1.00 18.82  ? 385 LEU A CA  1 
ATOM 3050 C C   . LEU A 1 385 ? 73.535 61.938  175.856 1.00 18.45  ? 385 LEU A C   1 
ATOM 3051 O O   . LEU A 1 385 ? 74.190 61.591  174.872 1.00 17.26  ? 385 LEU A O   1 
ATOM 3052 C CB  . LEU A 1 385 ? 71.190 61.593  176.568 1.00 17.60  ? 385 LEU A CB  1 
ATOM 3053 C CG  . LEU A 1 385 ? 70.148 60.640  177.126 1.00 15.82  ? 385 LEU A CG  1 
ATOM 3054 C CD1 . LEU A 1 385 ? 68.834 61.332  177.045 1.00 15.99  ? 385 LEU A CD1 1 
ATOM 3055 C CD2 . LEU A 1 385 ? 70.114 59.348  176.340 1.00 15.42  ? 385 LEU A CD2 1 
ATOM 3056 N N   . GLY A 1 386 ? 73.601 63.150  176.374 1.00 18.90  ? 386 GLY A N   1 
ATOM 3057 C CA  . GLY A 1 386 ? 74.485 64.127  175.795 1.00 19.02  ? 386 GLY A CA  1 
ATOM 3058 C C   . GLY A 1 386 ? 75.828 63.514  175.497 1.00 20.10  ? 386 GLY A C   1 
ATOM 3059 O O   . GLY A 1 386 ? 76.390 63.783  174.447 1.00 21.12  ? 386 GLY A O   1 
ATOM 3060 N N   . LEU A 1 387 ? 76.346 62.681  176.398 1.00 20.78  ? 387 LEU A N   1 
ATOM 3061 C CA  . LEU A 1 387 ? 77.660 62.080  176.179 1.00 21.71  ? 387 LEU A CA  1 
ATOM 3062 C C   . LEU A 1 387 ? 77.553 61.214  174.965 1.00 22.01  ? 387 LEU A C   1 
ATOM 3063 O O   . LEU A 1 387 ? 78.197 61.463  173.945 1.00 20.81  ? 387 LEU A O   1 
ATOM 3064 C CB  . LEU A 1 387 ? 78.121 61.215  177.358 1.00 22.99  ? 387 LEU A CB  1 
ATOM 3065 C CG  . LEU A 1 387 ? 79.596 60.758  177.288 1.00 25.12  ? 387 LEU A CG  1 
ATOM 3066 C CD1 . LEU A 1 387 ? 80.512 61.975  177.419 1.00 25.15  ? 387 LEU A CD1 1 
ATOM 3067 C CD2 . LEU A 1 387 ? 79.912 59.739  178.399 1.00 25.95  ? 387 LEU A CD2 1 
ATOM 3068 N N   . VAL A 1 388 ? 76.729 60.188  175.077 1.00 22.77  ? 388 VAL A N   1 
ATOM 3069 C CA  . VAL A 1 388 ? 76.533 59.302  173.960 1.00 24.87  ? 388 VAL A CA  1 
ATOM 3070 C C   . VAL A 1 388 ? 76.337 60.159  172.714 1.00 25.64  ? 388 VAL A C   1 
ATOM 3071 O O   . VAL A 1 388 ? 76.847 59.826  171.643 1.00 26.84  ? 388 VAL A O   1 
ATOM 3072 C CB  . VAL A 1 388 ? 75.297 58.416  174.161 1.00 25.63  ? 388 VAL A CB  1 
ATOM 3073 C CG1 . VAL A 1 388 ? 74.857 57.844  172.833 1.00 26.54  ? 388 VAL A CG1 1 
ATOM 3074 C CG2 . VAL A 1 388 ? 75.630 57.285  175.107 1.00 25.90  ? 388 VAL A CG2 1 
ATOM 3075 N N   . ALA A 1 389 ? 75.617 61.270  172.851 1.00 25.59  ? 389 ALA A N   1 
ATOM 3076 C CA  . ALA A 1 389 ? 75.384 62.129  171.702 1.00 25.87  ? 389 ALA A CA  1 
ATOM 3077 C C   . ALA A 1 389 ? 76.689 62.639  171.113 1.00 27.08  ? 389 ALA A C   1 
ATOM 3078 O O   . ALA A 1 389 ? 76.991 62.361  169.952 1.00 27.21  ? 389 ALA A O   1 
ATOM 3079 C CB  . ALA A 1 389 ? 74.501 63.288  172.088 1.00 25.91  ? 389 ALA A CB  1 
ATOM 3080 N N   . LEU A 1 390 ? 77.467 63.371  171.912 1.00 27.96  ? 390 LEU A N   1 
ATOM 3081 C CA  . LEU A 1 390 ? 78.724 63.914  171.417 1.00 29.36  ? 390 LEU A CA  1 
ATOM 3082 C C   . LEU A 1 390 ? 79.594 62.841  170.838 1.00 31.19  ? 390 LEU A C   1 
ATOM 3083 O O   . LEU A 1 390 ? 80.194 63.047  169.787 1.00 30.87  ? 390 LEU A O   1 
ATOM 3084 C CB  . LEU A 1 390 ? 79.532 64.638  172.491 1.00 28.92  ? 390 LEU A CB  1 
ATOM 3085 C CG  . LEU A 1 390 ? 80.861 65.163  171.899 1.00 29.22  ? 390 LEU A CG  1 
ATOM 3086 C CD1 . LEU A 1 390 ? 81.242 66.461  172.567 1.00 29.42  ? 390 LEU A CD1 1 
ATOM 3087 C CD2 . LEU A 1 390 ? 81.983 64.133  172.045 1.00 28.84  ? 390 LEU A CD2 1 
ATOM 3088 N N   . GLY A 1 391 ? 79.686 61.703  171.520 1.00 32.40  ? 391 GLY A N   1 
ATOM 3089 C CA  . GLY A 1 391 ? 80.520 60.623  171.010 1.00 33.63  ? 391 GLY A CA  1 
ATOM 3090 C C   . GLY A 1 391 ? 80.118 60.190  169.612 1.00 33.50  ? 391 GLY A C   1 
ATOM 3091 O O   . GLY A 1 391 ? 80.952 59.965  168.717 1.00 33.17  ? 391 GLY A O   1 
ATOM 3092 N N   . PHE A 1 392 ? 78.814 60.069  169.420 1.00 33.92  ? 392 PHE A N   1 
ATOM 3093 C CA  . PHE A 1 392 ? 78.319 59.674  168.128 1.00 34.17  ? 392 PHE A CA  1 
ATOM 3094 C C   . PHE A 1 392 ? 78.569 60.814  167.150 1.00 34.23  ? 392 PHE A C   1 
ATOM 3095 O O   . PHE A 1 392 ? 78.915 60.572  166.004 1.00 34.14  ? 392 PHE A O   1 
ATOM 3096 C CB  . PHE A 1 392 ? 76.837 59.252  168.224 1.00 34.55  ? 392 PHE A CB  1 
ATOM 3097 C CG  . PHE A 1 392 ? 76.644 57.745  168.405 1.00 35.14  ? 392 PHE A CG  1 
ATOM 3098 C CD1 . PHE A 1 392 ? 77.748 56.907  168.563 1.00 36.09  ? 392 PHE A CD1 1 
ATOM 3099 C CD2 . PHE A 1 392 ? 75.382 57.165  168.375 1.00 35.10  ? 392 PHE A CD2 1 
ATOM 3100 C CE1 . PHE A 1 392 ? 77.601 55.524  168.683 1.00 36.20  ? 392 PHE A CE1 1 
ATOM 3101 C CE2 . PHE A 1 392 ? 75.227 55.774  168.495 1.00 35.83  ? 392 PHE A CE2 1 
ATOM 3102 C CZ  . PHE A 1 392 ? 76.341 54.956  168.648 1.00 36.00  ? 392 PHE A CZ  1 
ATOM 3103 N N   . THR A 1 393 ? 78.449 62.057  167.594 1.00 34.39  ? 393 THR A N   1 
ATOM 3104 C CA  . THR A 1 393 ? 78.721 63.165  166.685 1.00 35.29  ? 393 THR A CA  1 
ATOM 3105 C C   . THR A 1 393 ? 80.177 63.068  166.235 1.00 34.82  ? 393 THR A C   1 
ATOM 3106 O O   . THR A 1 393 ? 80.486 63.176  165.052 1.00 34.88  ? 393 THR A O   1 
ATOM 3107 C CB  . THR A 1 393 ? 78.501 64.543  167.362 1.00 35.74  ? 393 THR A CB  1 
ATOM 3108 O OG1 . THR A 1 393 ? 77.102 64.752  167.586 1.00 36.31  ? 393 THR A OG1 1 
ATOM 3109 C CG2 . THR A 1 393 ? 79.017 65.665  166.476 1.00 35.68  ? 393 THR A CG2 1 
ATOM 3110 N N   . LEU A 1 394 ? 81.072 62.850  167.188 1.00 34.64  ? 394 LEU A N   1 
ATOM 3111 C CA  . LEU A 1 394 ? 82.483 62.740  166.868 1.00 35.01  ? 394 LEU A CA  1 
ATOM 3112 C C   . LEU A 1 394 ? 82.735 61.663  165.830 1.00 35.03  ? 394 LEU A C   1 
ATOM 3113 O O   . LEU A 1 394 ? 83.316 61.937  164.777 1.00 34.12  ? 394 LEU A O   1 
ATOM 3114 C CB  . LEU A 1 394 ? 83.280 62.400  168.115 1.00 36.07  ? 394 LEU A CB  1 
ATOM 3115 C CG  . LEU A 1 394 ? 84.787 62.382  167.908 1.00 37.22  ? 394 LEU A CG  1 
ATOM 3116 C CD1 . LEU A 1 394 ? 85.249 63.827  167.858 1.00 38.47  ? 394 LEU A CD1 1 
ATOM 3117 C CD2 . LEU A 1 394 ? 85.494 61.620  169.035 1.00 37.39  ? 394 LEU A CD2 1 
ATOM 3118 N N   . ILE A 1 395 ? 82.299 60.441  166.140 1.00 35.87  ? 395 ILE A N   1 
ATOM 3119 C CA  . ILE A 1 395 ? 82.501 59.304  165.248 1.00 37.17  ? 395 ILE A CA  1 
ATOM 3120 C C   . ILE A 1 395 ? 82.085 59.611  163.803 1.00 38.36  ? 395 ILE A C   1 
ATOM 3121 O O   . ILE A 1 395 ? 82.799 59.270  162.858 1.00 38.81  ? 395 ILE A O   1 
ATOM 3122 C CB  . ILE A 1 395 ? 81.777 58.033  165.789 1.00 36.22  ? 395 ILE A CB  1 
ATOM 3123 C CG1 . ILE A 1 395 ? 82.340 57.689  167.167 1.00 36.65  ? 395 ILE A CG1 1 
ATOM 3124 C CG2 . ILE A 1 395 ? 82.037 56.839  164.888 1.00 36.64  ? 395 ILE A CG2 1 
ATOM 3125 C CD1 . ILE A 1 395 ? 81.984 56.298  167.667 1.00 36.65  ? 395 ILE A CD1 1 
ATOM 3126 N N   . SER A 1 396 ? 80.951 60.280  163.627 1.00 39.56  ? 396 SER A N   1 
ATOM 3127 C CA  . SER A 1 396 ? 80.490 60.624  162.290 1.00 41.01  ? 396 SER A CA  1 
ATOM 3128 C C   . SER A 1 396 ? 81.518 61.491  161.610 1.00 42.92  ? 396 SER A C   1 
ATOM 3129 O O   . SER A 1 396 ? 81.816 61.308  160.443 1.00 42.24  ? 396 SER A O   1 
ATOM 3130 C CB  . SER A 1 396 ? 79.168 61.372  162.351 1.00 40.57  ? 396 SER A CB  1 
ATOM 3131 O OG  . SER A 1 396 ? 78.096 60.463  162.233 1.00 40.62  ? 396 SER A OG  1 
ATOM 3132 N N   . VAL A 1 397 ? 82.062 62.440  162.353 1.00 46.11  ? 397 VAL A N   1 
ATOM 3133 C CA  . VAL A 1 397 ? 83.069 63.330  161.808 1.00 49.25  ? 397 VAL A CA  1 
ATOM 3134 C C   . VAL A 1 397 ? 84.188 62.540  161.159 1.00 51.73  ? 397 VAL A C   1 
ATOM 3135 O O   . VAL A 1 397 ? 84.512 62.743  159.989 1.00 52.06  ? 397 VAL A O   1 
ATOM 3136 C CB  . VAL A 1 397 ? 83.678 64.220  162.906 1.00 48.54  ? 397 VAL A CB  1 
ATOM 3137 C CG1 . VAL A 1 397 ? 84.937 64.910  162.390 1.00 46.71  ? 397 VAL A CG1 1 
ATOM 3138 C CG2 . VAL A 1 397 ? 82.646 65.249  163.351 1.00 48.49  ? 397 VAL A CG2 1 
ATOM 3139 N N   . PHE A 1 398 ? 84.781 61.645  161.939 1.00 54.68  ? 398 PHE A N   1 
ATOM 3140 C CA  . PHE A 1 398 ? 85.877 60.808  161.476 1.00 57.59  ? 398 PHE A CA  1 
ATOM 3141 C C   . PHE A 1 398 ? 85.364 59.724  160.518 1.00 58.07  ? 398 PHE A C   1 
ATOM 3142 O O   . PHE A 1 398 ? 86.157 59.064  159.860 1.00 58.28  ? 398 PHE A O   1 
ATOM 3143 C CB  . PHE A 1 398 ? 86.571 60.128  162.681 1.00 59.99  ? 398 PHE A CB  1 
ATOM 3144 C CG  . PHE A 1 398 ? 87.998 60.605  162.964 1.00 62.83  ? 398 PHE A CG  1 
ATOM 3145 C CD1 . PHE A 1 398 ? 88.256 61.903  163.428 1.00 63.76  ? 398 PHE A CD1 1 
ATOM 3146 C CD2 . PHE A 1 398 ? 89.094 59.760  162.721 1.00 64.03  ? 398 PHE A CD2 1 
ATOM 3147 C CE1 . PHE A 1 398 ? 89.586 62.334  163.683 1.00 64.67  ? 398 PHE A CE1 1 
ATOM 3148 C CE2 . PHE A 1 398 ? 90.429 60.178  162.971 1.00 64.64  ? 398 PHE A CE2 1 
ATOM 3149 C CZ  . PHE A 1 398 ? 90.669 61.474  163.433 1.00 65.00  ? 398 PHE A CZ  1 
ATOM 3150 N N   . THR A 1 399 ? 84.048 59.563  160.405 1.00 59.26  ? 399 THR A N   1 
ATOM 3151 C CA  . THR A 1 399 ? 83.514 58.488  159.580 1.00 60.78  ? 399 THR A CA  1 
ATOM 3152 C C   . THR A 1 399 ? 82.522 58.760  158.463 1.00 61.61  ? 399 THR A C   1 
ATOM 3153 O O   . THR A 1 399 ? 82.443 57.980  157.518 1.00 61.67  ? 399 THR A O   1 
ATOM 3154 C CB  . THR A 1 399 ? 82.911 57.421  160.485 1.00 60.83  ? 399 THR A CB  1 
ATOM 3155 O OG1 . THR A 1 399 ? 83.956 56.852  161.285 1.00 62.05  ? 399 THR A OG1 1 
ATOM 3156 C CG2 . THR A 1 399 ? 82.228 56.356  159.676 1.00 60.38  ? 399 THR A CG2 1 
ATOM 3157 N N   . LEU A 1 400 ? 81.761 59.842  158.567 1.00 62.48  ? 400 LEU A N   1 
ATOM 3158 C CA  . LEU A 1 400 ? 80.774 60.199  157.545 1.00 63.68  ? 400 LEU A CA  1 
ATOM 3159 C C   . LEU A 1 400 ? 81.382 60.232  156.130 1.00 64.52  ? 400 LEU A C   1 
ATOM 3160 O O   . LEU A 1 400 ? 82.601 60.210  155.973 1.00 65.09  ? 400 LEU A O   1 
ATOM 3161 C CB  . LEU A 1 400 ? 80.134 61.558  157.879 1.00 64.25  ? 400 LEU A CB  1 
ATOM 3162 C CG  . LEU A 1 400 ? 79.120 62.095  156.851 1.00 64.78  ? 400 LEU A CG  1 
ATOM 3163 C CD1 . LEU A 1 400 ? 77.943 61.127  156.731 1.00 64.81  ? 400 LEU A CD1 1 
ATOM 3164 C CD2 . LEU A 1 400 ? 78.604 63.464  157.287 1.00 65.50  ? 400 LEU A CD2 1 
ATOM 3165 N N   . SER A 1 401 ? 80.538 60.294  155.103 1.00 65.05  ? 401 SER A N   1 
ATOM 3166 C CA  . SER A 1 401 ? 81.014 60.276  153.727 1.00 65.72  ? 401 SER A CA  1 
ATOM 3167 C C   . SER A 1 401 ? 81.586 61.585  153.239 1.00 66.79  ? 401 SER A C   1 
ATOM 3168 O O   . SER A 1 401 ? 81.004 62.654  153.430 1.00 65.48  ? 401 SER A O   1 
ATOM 3169 C CB  . SER A 1 401 ? 79.887 59.844  152.793 1.00 65.81  ? 401 SER A CB  1 
ATOM 3170 O OG  . SER A 1 401 ? 80.337 58.989  151.764 1.00 66.29  ? 401 SER A OG  1 
ATOM 3171 N N   . GLY A 1 402 ? 82.728 61.449  152.569 1.00 69.03  ? 402 GLY A N   1 
ATOM 3172 C CA  . GLY A 1 402 ? 83.469 62.559  152.008 1.00 71.29  ? 402 GLY A CA  1 
ATOM 3173 C C   . GLY A 1 402 ? 82.674 63.813  151.783 1.00 73.60  ? 402 GLY A C   1 
ATOM 3174 O O   . GLY A 1 402 ? 81.538 63.785  151.288 1.00 73.05  ? 402 GLY A O   1 
ATOM 3175 N N   . PRO A 1 403 ? 83.263 64.946  152.173 1.00 75.65  ? 403 PRO A N   1 
ATOM 3176 C CA  . PRO A 1 403 ? 82.624 66.257  152.020 1.00 77.42  ? 403 PRO A CA  1 
ATOM 3177 C C   . PRO A 1 403 ? 82.621 66.621  150.525 1.00 78.74  ? 403 PRO A C   1 
ATOM 3178 O O   . PRO A 1 403 ? 81.830 67.459  150.055 1.00 78.30  ? 403 PRO A O   1 
ATOM 3179 C CB  . PRO A 1 403 ? 83.514 67.186  152.858 1.00 76.66  ? 403 PRO A CB  1 
ATOM 3180 C CG  . PRO A 1 403 ? 84.244 66.247  153.825 1.00 75.86  ? 403 PRO A CG  1 
ATOM 3181 C CD  . PRO A 1 403 ? 84.485 65.019  152.997 1.00 75.33  ? 403 PRO A CD  1 
ATOM 3182 N N   . GLY A 1 404 ? 83.523 65.960  149.798 1.00 80.01  ? 404 GLY A N   1 
ATOM 3183 C CA  . GLY A 1 404 ? 83.661 66.152  148.363 1.00 82.92  ? 404 GLY A CA  1 
ATOM 3184 C C   . GLY A 1 404 ? 84.048 64.796  147.805 1.00 84.36  ? 404 GLY A C   1 
ATOM 3185 O O   . GLY A 1 404 ? 85.234 64.558  147.496 1.00 84.29  ? 404 GLY A O   1 
ATOM 3186 N N   . PRO A 1 405 ? 83.052 63.893  147.648 1.00 85.35  ? 405 PRO A N   1 
ATOM 3187 C CA  . PRO A 1 405 ? 83.191 62.525  147.145 1.00 86.17  ? 405 PRO A CA  1 
ATOM 3188 C C   . PRO A 1 405 ? 84.031 62.493  145.917 1.00 86.93  ? 405 PRO A C   1 
ATOM 3189 O O   . PRO A 1 405 ? 84.411 63.551  145.381 1.00 88.06  ? 405 PRO A O   1 
ATOM 3190 C CB  . PRO A 1 405 ? 81.750 62.090  146.871 1.00 85.49  ? 405 PRO A CB  1 
ATOM 3191 C CG  . PRO A 1 405 ? 81.088 63.365  146.489 1.00 85.79  ? 405 PRO A CG  1 
ATOM 3192 C CD  . PRO A 1 405 ? 81.650 64.336  147.520 1.00 85.93  ? 405 PRO A CD  1 
ATOM 3193 N N   . LEU A 1 406 ? 84.307 61.270  145.483 1.00 86.95  ? 406 LEU A N   1 
ATOM 3194 C CA  . LEU A 1 406 ? 85.124 61.030  144.307 1.00 87.27  ? 406 LEU A CA  1 
ATOM 3195 C C   . LEU A 1 406 ? 84.755 61.796  142.997 1.00 87.55  ? 406 LEU A C   1 
ATOM 3196 O O   . LEU A 1 406 ? 85.256 61.426  141.934 1.00 87.83  ? 406 LEU A O   1 
ATOM 3197 C CB  . LEU A 1 406 ? 85.209 59.514  144.055 1.00 86.01  ? 406 LEU A CB  1 
ATOM 3198 C CG  . LEU A 1 406 ? 85.975 58.673  145.090 1.00 85.59  ? 406 LEU A CG  1 
ATOM 3199 C CD1 . LEU A 1 406 ? 85.331 57.308  145.168 1.00 85.08  ? 406 LEU A CD1 1 
ATOM 3200 C CD2 . LEU A 1 406 ? 87.448 58.556  144.718 1.00 85.35  ? 406 LEU A CD2 1 
ATOM 3201 N N   . SER A 1 407 ? 83.908 62.842  143.074 1.00 87.27  ? 407 SER A N   1 
ATOM 3202 C CA  . SER A 1 407 ? 83.528 63.698  141.920 1.00 86.01  ? 407 SER A CA  1 
ATOM 3203 C C   . SER A 1 407 ? 82.541 64.783  142.351 1.00 84.49  ? 407 SER A C   1 
ATOM 3204 O O   . SER A 1 407 ? 81.369 64.732  141.957 1.00 84.08  ? 407 SER A O   1 
ATOM 3205 C CB  . SER A 1 407 ? 82.897 62.867  140.776 1.00 85.18  ? 407 SER A CB  1 
ATOM 3206 O OG  . SER A 1 407 ? 82.190 63.697  139.862 1.00 84.02  ? 407 SER A OG  1 
ATOM 3207 N N   . LEU A 1 408 ? 83.004 65.759  143.141 1.00 84.05  ? 408 LEU A N   1 
ATOM 3208 C CA  . LEU A 1 408 ? 82.106 66.815  143.629 1.00 84.18  ? 408 LEU A CA  1 
ATOM 3209 C C   . LEU A 1 408 ? 81.649 67.890  142.637 1.00 83.79  ? 408 LEU A C   1 
ATOM 3210 O O   . LEU A 1 408 ? 80.469 68.237  142.622 1.00 83.98  ? 408 LEU A O   1 
ATOM 3211 C CB  . LEU A 1 408 ? 82.678 67.543  144.872 1.00 83.71  ? 408 LEU A CB  1 
ATOM 3212 C CG  . LEU A 1 408 ? 81.712 68.559  145.550 1.00 84.40  ? 408 LEU A CG  1 
ATOM 3213 C CD1 . LEU A 1 408 ? 80.663 67.816  146.404 1.00 83.74  ? 408 LEU A CD1 1 
ATOM 3214 C CD2 . LEU A 1 408 ? 82.503 69.554  146.421 1.00 84.19  ? 408 LEU A CD2 1 
ATOM 3215 N N   . LEU A 1 409 ? 82.557 68.444  141.835 1.00 83.25  ? 409 LEU A N   1 
ATOM 3216 C CA  . LEU A 1 409 ? 82.136 69.490  140.906 1.00 82.57  ? 409 LEU A CA  1 
ATOM 3217 C C   . LEU A 1 409 ? 81.077 68.970  139.942 1.00 82.24  ? 409 LEU A C   1 
ATOM 3218 O O   . LEU A 1 409 ? 80.075 69.643  139.694 1.00 81.68  ? 409 LEU A O   1 
ATOM 3219 C CB  . LEU A 1 409 ? 83.324 70.065  140.107 1.00 82.10  ? 409 LEU A CB  1 
ATOM 3220 C CG  . LEU A 1 409 ? 84.373 70.954  140.809 1.00 82.10  ? 409 LEU A CG  1 
ATOM 3221 C CD1 . LEU A 1 409 ? 85.144 71.742  139.738 1.00 81.18  ? 409 LEU A CD1 1 
ATOM 3222 C CD2 . LEU A 1 409 ? 83.691 71.918  141.785 1.00 82.23  ? 409 LEU A CD2 1 
ATOM 3223 N N   . ARG A 1 410 ? 81.294 67.757  139.432 1.00 82.36  ? 410 ARG A N   1 
ATOM 3224 C CA  . ARG A 1 410 ? 80.376 67.113  138.478 1.00 82.30  ? 410 ARG A CA  1 
ATOM 3225 C C   . ARG A 1 410 ? 78.977 66.924  139.064 1.00 82.50  ? 410 ARG A C   1 
ATOM 3226 O O   . ARG A 1 410 ? 77.961 67.279  138.443 1.00 81.64  ? 410 ARG A O   1 
ATOM 3227 C CB  . ARG A 1 410 ? 80.944 65.753  138.042 1.00 81.98  ? 410 ARG A CB  1 
ATOM 3228 C CG  . ARG A 1 410 ? 82.275 65.865  137.284 1.00 81.86  ? 410 ARG A CG  1 
ATOM 3229 C CD  . ARG A 1 410 ? 82.089 66.529  135.928 1.00 81.48  ? 410 ARG A CD  1 
ATOM 3230 N NE  . ARG A 1 410 ? 83.311 66.534  135.127 1.00 81.38  ? 410 ARG A NE  1 
ATOM 3231 C CZ  . ARG A 1 410 ? 83.353 66.906  133.848 1.00 81.88  ? 410 ARG A CZ  1 
ATOM 3232 N NH1 . ARG A 1 410 ? 82.236 67.303  133.237 1.00 82.19  ? 410 ARG A NH1 1 
ATOM 3233 N NH2 . ARG A 1 410 ? 84.501 66.879  133.172 1.00 81.64  ? 410 ARG A NH2 1 
ATOM 3234 N N   . ARG A 1 411 ? 78.942 66.353  140.264 1.00 82.95  ? 411 ARG A N   1 
ATOM 3235 C CA  . ARG A 1 411 ? 77.692 66.140  140.965 1.00 82.81  ? 411 ARG A CA  1 
ATOM 3236 C C   . ARG A 1 411 ? 77.147 67.487  141.553 1.00 83.40  ? 411 ARG A C   1 
ATOM 3237 O O   . ARG A 1 411 ? 75.922 67.650  141.671 1.00 83.64  ? 411 ARG A O   1 
ATOM 3238 C CB  . ARG A 1 411 ? 77.889 65.060  142.056 1.00 81.29  ? 411 ARG A CB  1 
ATOM 3239 C CG  . ARG A 1 411 ? 78.123 63.607  141.531 1.00 79.34  ? 411 ARG A CG  1 
ATOM 3240 C CD  . ARG A 1 411 ? 77.856 62.600  142.683 1.00 78.53  ? 411 ARG A CD  1 
ATOM 3241 N NE  . ARG A 1 411 ? 78.148 61.191  142.388 1.00 77.10  ? 411 ARG A NE  1 
ATOM 3242 C CZ  . ARG A 1 411 ? 77.920 60.175  143.229 1.00 75.51  ? 411 ARG A CZ  1 
ATOM 3243 N NH1 . ARG A 1 411 ? 77.396 60.389  144.421 1.00 74.29  ? 411 ARG A NH1 1 
ATOM 3244 N NH2 . ARG A 1 411 ? 78.224 58.933  142.888 1.00 74.56  ? 411 ARG A NH2 1 
ATOM 3245 N N   . GLN A 1 412 ? 78.029 68.446  141.902 1.00 83.47  ? 412 GLN A N   1 
ATOM 3246 C CA  . GLN A 1 412 ? 77.572 69.752  142.435 1.00 83.22  ? 412 GLN A CA  1 
ATOM 3247 C C   . GLN A 1 412 ? 76.825 70.430  141.286 1.00 83.12  ? 412 GLN A C   1 
ATOM 3248 O O   . GLN A 1 412 ? 76.035 71.352  141.481 1.00 82.14  ? 412 GLN A O   1 
ATOM 3249 C CB  . GLN A 1 412 ? 78.750 70.643  142.902 1.00 83.58  ? 412 GLN A CB  1 
ATOM 3250 C CG  . GLN A 1 412 ? 78.336 71.839  143.853 1.00 84.55  ? 412 GLN A CG  1 
ATOM 3251 C CD  . GLN A 1 412 ? 79.524 72.672  144.416 1.00 84.66  ? 412 GLN A CD  1 
ATOM 3252 O OE1 . GLN A 1 412 ? 80.688 72.264  144.313 1.00 85.04  ? 412 GLN A OE1 1 
ATOM 3253 N NE2 . GLN A 1 412 ? 79.218 73.833  145.025 1.00 83.16  ? 412 GLN A NE2 1 
ATOM 3254 N N   . VAL A 1 413 ? 77.094 69.935  140.083 1.00 83.74  ? 413 VAL A N   1 
ATOM 3255 C CA  . VAL A 1 413 ? 76.451 70.410  138.866 1.00 84.94  ? 413 VAL A CA  1 
ATOM 3256 C C   . VAL A 1 413 ? 75.079 69.742  138.804 1.00 85.66  ? 413 VAL A C   1 
ATOM 3257 O O   . VAL A 1 413 ? 74.109 70.312  138.300 1.00 86.00  ? 413 VAL A O   1 
ATOM 3258 C CB  . VAL A 1 413 ? 77.274 70.007  137.602 1.00 84.14  ? 413 VAL A CB  1 
ATOM 3259 C CG1 . VAL A 1 413 ? 76.528 70.392  136.318 1.00 83.60  ? 413 VAL A CG1 1 
ATOM 3260 C CG2 . VAL A 1 413 ? 78.632 70.690  137.645 1.00 84.64  ? 413 VAL A CG2 1 
ATOM 3261 N N   . ASN A 1 414 ? 75.011 68.529  139.338 1.00 86.76  ? 414 ASN A N   1 
ATOM 3262 C CA  . ASN A 1 414 ? 73.773 67.758  139.369 1.00 88.06  ? 414 ASN A CA  1 
ATOM 3263 C C   . ASN A 1 414 ? 72.710 68.489  140.184 1.00 88.92  ? 414 ASN A C   1 
ATOM 3264 O O   . ASN A 1 414 ? 71.527 68.486  139.832 1.00 88.65  ? 414 ASN A O   1 
ATOM 3265 C CB  . ASN A 1 414 ? 74.037 66.384  139.999 1.00 87.60  ? 414 ASN A CB  1 
ATOM 3266 C CG  . ASN A 1 414 ? 72.810 65.483  139.987 1.00 87.24  ? 414 ASN A CG  1 
ATOM 3267 O OD1 . ASN A 1 414 ? 71.680 65.966  139.896 1.00 87.00  ? 414 ASN A OD1 1 
ATOM 3268 N ND2 . ASN A 1 414 ? 73.028 64.163  140.093 1.00 85.95  ? 414 ASN A ND2 1 
ATOM 3269 N N   . GLU A 1 415 ? 73.142 69.090  141.291 1.00 90.85  ? 415 GLU A N   1 
ATOM 3270 C CA  . GLU A 1 415 ? 72.253 69.841  142.183 1.00 92.60  ? 415 GLU A CA  1 
ATOM 3271 C C   . GLU A 1 415 ? 71.920 71.226  141.591 1.00 92.58  ? 415 GLU A C   1 
ATOM 3272 O O   . GLU A 1 415 ? 70.779 71.706  141.705 1.00 92.86  ? 415 GLU A O   1 
ATOM 3273 C CB  . GLU A 1 415 ? 72.900 70.006  143.573 1.00 93.63  ? 415 GLU A CB  1 
ATOM 3274 C CG  . GLU A 1 415 ? 71.875 70.188  144.675 1.00 94.98  ? 415 GLU A CG  1 
ATOM 3275 C CD  . GLU A 1 415 ? 70.984 68.964  144.832 1.00 95.74  ? 415 GLU A CD  1 
ATOM 3276 O OE1 . GLU A 1 415 ? 70.788 68.221  143.838 1.00 95.82  ? 415 GLU A OE1 1 
ATOM 3277 O OE2 . GLU A 1 415 ? 70.467 68.752  145.951 1.00 96.50  ? 415 GLU A OE2 1 
ATOM 3278 N N   . VAL A 1 416 ? 72.915 71.860  140.961 1.00 92.35  ? 416 VAL A N   1 
ATOM 3279 C CA  . VAL A 1 416 ? 72.726 73.170  140.330 1.00 92.01  ? 416 VAL A CA  1 
ATOM 3280 C C   . VAL A 1 416 ? 71.755 73.036  139.144 1.00 91.53  ? 416 VAL A C   1 
ATOM 3281 O O   . VAL A 1 416 ? 70.686 73.658  139.125 1.00 91.61  ? 416 VAL A O   1 
ATOM 3282 C CB  . VAL A 1 416 ? 74.079 73.752  139.830 1.00 91.63  ? 416 VAL A CB  1 
ATOM 3283 C CG1 . VAL A 1 416 ? 73.854 75.118  139.176 1.00 91.97  ? 416 VAL A CG1 1 
ATOM 3284 C CG2 . VAL A 1 416 ? 75.056 73.882  140.998 1.00 91.22  ? 416 VAL A CG2 1 
ATOM 3285 N N   . ALA A 1 417 ? 72.144 72.226  138.163 1.00 91.27  ? 417 ALA A N   1 
ATOM 3286 C CA  . ALA A 1 417 ? 71.336 71.952  136.973 1.00 91.36  ? 417 ALA A CA  1 
ATOM 3287 C C   . ALA A 1 417 ? 70.000 71.362  137.412 1.00 91.75  ? 417 ALA A C   1 
ATOM 3288 O O   . ALA A 1 417 ? 68.943 71.669  136.789 1.00 91.25  ? 417 ALA A O   1 
ATOM 3289 C CB  . ALA A 1 417 ? 72.068 70.937  136.068 1.00 90.95  ? 417 ALA A CB  1 
ATOM 3290 O OXT . ALA A 1 417 ? 70.050 70.567  138.376 1.00 91.79  ? 417 ALA A OXT 1 
ATOM 3291 N N   . MET B 1 1   ? 52.335 98.207  184.229 1.00 84.65  ? 1   MET B N   1 
ATOM 3292 C CA  . MET B 1 1   ? 52.024 98.477  185.669 1.00 85.28  ? 1   MET B CA  1 
ATOM 3293 C C   . MET B 1 1   ? 50.566 98.096  185.943 1.00 85.52  ? 1   MET B C   1 
ATOM 3294 O O   . MET B 1 1   ? 49.769 98.097  185.026 1.00 85.00  ? 1   MET B O   1 
ATOM 3295 C CB  . MET B 1 1   ? 52.349 99.940  185.971 1.00 85.47  ? 1   MET B CB  1 
ATOM 3296 C CG  . MET B 1 1   ? 53.772 100.303 185.463 1.00 85.70  ? 1   MET B CG  1 
ATOM 3297 S SD  . MET B 1 1   ? 54.349 101.966 185.822 1.00 86.65  ? 1   MET B SD  1 
ATOM 3298 C CE  . MET B 1 1   ? 54.476 101.862 187.654 1.00 85.81  ? 1   MET B CE  1 
ATOM 3299 N N   . TYR B 1 2   ? 50.242 97.744  187.188 1.00 86.47  ? 2   TYR B N   1 
ATOM 3300 C CA  . TYR B 1 2   ? 48.900 97.264  187.561 1.00 87.93  ? 2   TYR B CA  1 
ATOM 3301 C C   . TYR B 1 2   ? 47.867 97.400  186.448 1.00 88.61  ? 2   TYR B C   1 
ATOM 3302 O O   . TYR B 1 2   ? 47.132 96.460  186.139 1.00 88.13  ? 2   TYR B O   1 
ATOM 3303 C CB  . TYR B 1 2   ? 48.404 97.938  188.853 1.00 88.16  ? 2   TYR B CB  1 
ATOM 3304 C CG  . TYR B 1 2   ? 47.671 99.248  188.682 1.00 87.83  ? 2   TYR B CG  1 
ATOM 3305 C CD1 . TYR B 1 2   ? 46.314 99.283  188.321 1.00 87.49  ? 2   TYR B CD1 1 
ATOM 3306 C CD2 . TYR B 1 2   ? 48.314 100.449 188.960 1.00 87.77  ? 2   TYR B CD2 1 
ATOM 3307 C CE1 . TYR B 1 2   ? 45.624 100.488 188.255 1.00 86.82  ? 2   TYR B CE1 1 
ATOM 3308 C CE2 . TYR B 1 2   ? 47.638 101.656 188.903 1.00 87.31  ? 2   TYR B CE2 1 
ATOM 3309 C CZ  . TYR B 1 2   ? 46.297 101.674 188.556 1.00 87.06  ? 2   TYR B CZ  1 
ATOM 3310 O OH  . TYR B 1 2   ? 45.647 102.887 188.572 1.00 86.23  ? 2   TYR B OH  1 
ATOM 3311 N N   . TYR B 1 3   ? 47.832 98.575  185.837 1.00 89.80  ? 3   TYR B N   1 
ATOM 3312 C CA  . TYR B 1 3   ? 46.914 98.850  184.748 1.00 90.95  ? 3   TYR B CA  1 
ATOM 3313 C C   . TYR B 1 3   ? 47.224 98.033  183.486 1.00 89.78  ? 3   TYR B C   1 
ATOM 3314 O O   . TYR B 1 3   ? 46.367 97.863  182.612 1.00 90.75  ? 3   TYR B O   1 
ATOM 3315 C CB  . TYR B 1 3   ? 46.935 100.354 184.444 1.00 92.94  ? 3   TYR B CB  1 
ATOM 3316 C CG  . TYR B 1 3   ? 48.242 101.063 184.776 1.00 95.04  ? 3   TYR B CG  1 
ATOM 3317 C CD1 . TYR B 1 3   ? 49.347 100.971 183.924 1.00 95.74  ? 3   TYR B CD1 1 
ATOM 3318 C CD2 . TYR B 1 3   ? 48.354 101.860 185.926 1.00 95.36  ? 3   TYR B CD2 1 
ATOM 3319 C CE1 . TYR B 1 3   ? 50.522 101.662 184.200 1.00 96.72  ? 3   TYR B CE1 1 
ATOM 3320 C CE2 . TYR B 1 3   ? 49.531 102.556 186.219 1.00 95.90  ? 3   TYR B CE2 1 
ATOM 3321 C CZ  . TYR B 1 3   ? 50.609 102.452 185.348 1.00 96.59  ? 3   TYR B CZ  1 
ATOM 3322 O OH  . TYR B 1 3   ? 51.780 103.140 185.593 1.00 96.62  ? 3   TYR B OH  1 
ATOM 3323 N N   . LEU B 1 4   ? 48.447 97.514  183.409 1.00 88.02  ? 4   LEU B N   1 
ATOM 3324 C CA  . LEU B 1 4   ? 48.892 96.711  182.267 1.00 85.06  ? 4   LEU B CA  1 
ATOM 3325 C C   . LEU B 1 4   ? 49.097 95.259  182.705 1.00 82.80  ? 4   LEU B C   1 
ATOM 3326 O O   . LEU B 1 4   ? 49.155 94.346  181.881 1.00 81.63  ? 4   LEU B O   1 
ATOM 3327 C CB  . LEU B 1 4   ? 50.204 97.285  181.692 1.00 86.13  ? 4   LEU B CB  1 
ATOM 3328 C CG  . LEU B 1 4   ? 50.264 98.725  181.147 1.00 86.01  ? 4   LEU B CG  1 
ATOM 3329 C CD1 . LEU B 1 4   ? 51.654 98.978  180.593 1.00 86.02  ? 4   LEU B CD1 1 
ATOM 3330 C CD2 . LEU B 1 4   ? 49.229 98.953  180.082 1.00 86.03  ? 4   LEU B CD2 1 
ATOM 3331 N N   . LYS B 1 5   ? 49.205 95.043  184.008 1.00 79.51  ? 5   LYS B N   1 
ATOM 3332 C CA  . LYS B 1 5   ? 49.415 93.692  184.488 1.00 76.70  ? 5   LYS B CA  1 
ATOM 3333 C C   . LYS B 1 5   ? 48.122 92.893  184.566 1.00 74.95  ? 5   LYS B C   1 
ATOM 3334 O O   . LYS B 1 5   ? 48.079 91.739  184.154 1.00 74.48  ? 5   LYS B O   1 
ATOM 3335 C CB  . LYS B 1 5   ? 50.058 93.718  185.874 1.00 76.55  ? 5   LYS B CB  1 
ATOM 3336 C CG  . LYS B 1 5   ? 51.296 94.581  186.015 1.00 76.07  ? 5   LYS B CG  1 
ATOM 3337 C CD  . LYS B 1 5   ? 51.772 94.607  187.476 1.00 76.16  ? 5   LYS B CD  1 
ATOM 3338 C CE  . LYS B 1 5   ? 53.079 95.386  187.619 1.00 76.64  ? 5   LYS B CE  1 
ATOM 3339 N NZ  . LYS B 1 5   ? 53.526 95.554  189.035 1.00 75.19  ? 5   LYS B NZ  1 
ATOM 3340 N N   . ASN B 1 6   ? 47.066 93.502  185.097 1.00 73.94  ? 6   ASN B N   1 
ATOM 3341 C CA  . ASN B 1 6   ? 45.789 92.797  185.275 1.00 72.72  ? 6   ASN B CA  1 
ATOM 3342 C C   . ASN B 1 6   ? 45.141 92.237  184.022 1.00 72.02  ? 6   ASN B C   1 
ATOM 3343 O O   . ASN B 1 6   ? 45.372 92.725  182.906 1.00 71.68  ? 6   ASN B O   1 
ATOM 3344 C CB  . ASN B 1 6   ? 44.778 93.703  185.956 1.00 72.97  ? 6   ASN B CB  1 
ATOM 3345 C CG  . ASN B 1 6   ? 44.315 94.806  185.051 1.00 72.60  ? 6   ASN B CG  1 
ATOM 3346 O OD1 . ASN B 1 6   ? 43.613 94.561  184.066 1.00 72.54  ? 6   ASN B OD1 1 
ATOM 3347 N ND2 . ASN B 1 6   ? 44.724 96.033  185.361 1.00 72.32  ? 6   ASN B ND2 1 
ATOM 3348 N N   . THR B 1 7   ? 44.285 91.240  184.248 1.00 70.37  ? 7   THR B N   1 
ATOM 3349 C CA  . THR B 1 7   ? 43.548 90.524  183.201 1.00 68.68  ? 7   THR B CA  1 
ATOM 3350 C C   . THR B 1 7   ? 42.670 91.366  182.268 1.00 67.10  ? 7   THR B C   1 
ATOM 3351 O O   . THR B 1 7   ? 42.968 91.524  181.072 1.00 66.99  ? 7   THR B O   1 
ATOM 3352 C CB  . THR B 1 7   ? 42.630 89.429  183.832 1.00 68.86  ? 7   THR B CB  1 
ATOM 3353 O OG1 . THR B 1 7   ? 43.429 88.494  184.571 1.00 69.43  ? 7   THR B OG1 1 
ATOM 3354 C CG2 . THR B 1 7   ? 41.833 88.686  182.744 1.00 68.29  ? 7   THR B CG2 1 
ATOM 3355 N N   . ASN B 1 8   ? 41.585 91.898  182.821 1.00 65.00  ? 8   ASN B N   1 
ATOM 3356 C CA  . ASN B 1 8   ? 40.617 92.663  182.041 1.00 62.65  ? 8   ASN B CA  1 
ATOM 3357 C C   . ASN B 1 8   ? 41.128 93.842  181.260 1.00 59.95  ? 8   ASN B C   1 
ATOM 3358 O O   . ASN B 1 8   ? 40.730 94.052  180.109 1.00 59.01  ? 8   ASN B O   1 
ATOM 3359 C CB  . ASN B 1 8   ? 39.490 93.071  182.957 1.00 63.75  ? 8   ASN B CB  1 
ATOM 3360 C CG  . ASN B 1 8   ? 38.973 91.898  183.731 1.00 64.56  ? 8   ASN B CG  1 
ATOM 3361 O OD1 . ASN B 1 8   ? 38.639 90.846  183.153 1.00 64.50  ? 8   ASN B OD1 1 
ATOM 3362 N ND2 . ASN B 1 8   ? 38.926 92.044  185.049 1.00 65.21  ? 8   ASN B ND2 1 
ATOM 3363 N N   . PHE B 1 9   ? 42.001 94.626  181.868 1.00 57.30  ? 9   PHE B N   1 
ATOM 3364 C CA  . PHE B 1 9   ? 42.517 95.727  181.098 1.00 54.57  ? 9   PHE B CA  1 
ATOM 3365 C C   . PHE B 1 9   ? 43.010 95.154  179.807 1.00 53.44  ? 9   PHE B C   1 
ATOM 3366 O O   . PHE B 1 9   ? 42.467 95.444  178.758 1.00 52.66  ? 9   PHE B O   1 
ATOM 3367 C CB  . PHE B 1 9   ? 43.708 96.360  181.704 1.00 53.84  ? 9   PHE B CB  1 
ATOM 3368 C CG  . PHE B 1 9   ? 44.370 97.306  180.794 1.00 52.95  ? 9   PHE B CG  1 
ATOM 3369 C CD1 . PHE B 1 9   ? 43.877 98.586  180.652 1.00 53.37  ? 9   PHE B CD1 1 
ATOM 3370 C CD2 . PHE B 1 9   ? 45.477 96.926  180.065 1.00 52.77  ? 9   PHE B CD2 1 
ATOM 3371 C CE1 . PHE B 1 9   ? 44.512 99.498  179.838 1.00 54.14  ? 9   PHE B CE1 1 
ATOM 3372 C CE2 . PHE B 1 9   ? 46.117 97.837  179.245 1.00 53.63  ? 9   PHE B CE2 1 
ATOM 3373 C CZ  . PHE B 1 9   ? 45.628 99.114  179.119 1.00 54.49  ? 9   PHE B CZ  1 
ATOM 3374 N N   . TRP B 1 10  ? 44.087 94.378  179.904 1.00 52.58  ? 10  TRP B N   1 
ATOM 3375 C CA  . TRP B 1 10  ? 44.673 93.750  178.738 1.00 52.17  ? 10  TRP B CA  1 
ATOM 3376 C C   . TRP B 1 10  ? 43.542 93.280  177.853 1.00 52.56  ? 10  TRP B C   1 
ATOM 3377 O O   . TRP B 1 10  ? 43.414 93.737  176.716 1.00 54.09  ? 10  TRP B O   1 
ATOM 3378 C CB  . TRP B 1 10  ? 45.573 92.549  179.111 1.00 50.87  ? 10  TRP B CB  1 
ATOM 3379 C CG  . TRP B 1 10  ? 47.029 92.658  178.542 1.00 50.57  ? 10  TRP B CG  1 
ATOM 3380 C CD1 . TRP B 1 10  ? 47.778 91.658  177.964 1.00 49.86  ? 10  TRP B CD1 1 
ATOM 3381 C CD2 . TRP B 1 10  ? 47.857 93.857  178.476 1.00 50.16  ? 10  TRP B CD2 1 
ATOM 3382 N NE1 . TRP B 1 10  ? 49.013 92.159  177.562 1.00 49.48  ? 10  TRP B NE1 1 
ATOM 3383 C CE2 . TRP B 1 10  ? 49.093 93.474  177.888 1.00 49.46  ? 10  TRP B CE2 1 
ATOM 3384 C CE3 . TRP B 1 10  ? 47.686 95.163  178.919 1.00 48.51  ? 10  TRP B CE3 1 
ATOM 3385 C CZ2 . TRP B 1 10  ? 50.120 94.428  177.661 1.00 48.27  ? 10  TRP B CZ2 1 
ATOM 3386 C CZ3 . TRP B 1 10  ? 48.690 96.070  178.696 1.00 47.22  ? 10  TRP B CZ3 1 
ATOM 3387 C CH2 . TRP B 1 10  ? 49.906 95.698  178.105 1.00 47.37  ? 10  TRP B CH2 1 
ATOM 3388 N N   . MET B 1 11  ? 42.688 92.413  178.388 1.00 52.55  ? 11  MET B N   1 
ATOM 3389 C CA  . MET B 1 11  ? 41.580 91.860  177.608 1.00 52.67  ? 11  MET B CA  1 
ATOM 3390 C C   . MET B 1 11  ? 40.690 92.847  176.897 1.00 51.69  ? 11  MET B C   1 
ATOM 3391 O O   . MET B 1 11  ? 40.696 92.937  175.661 1.00 51.84  ? 11  MET B O   1 
ATOM 3392 C CB  . MET B 1 11  ? 40.735 90.963  178.489 1.00 54.16  ? 11  MET B CB  1 
ATOM 3393 C CG  . MET B 1 11  ? 41.560 89.831  179.047 1.00 56.33  ? 11  MET B CG  1 
ATOM 3394 S SD  . MET B 1 11  ? 42.382 88.942  177.695 1.00 58.41  ? 11  MET B SD  1 
ATOM 3395 C CE  . MET B 1 11  ? 44.026 89.817  177.632 1.00 56.14  ? 11  MET B CE  1 
ATOM 3396 N N   . PHE B 1 12  ? 39.902 93.581  177.660 1.00 50.15  ? 12  PHE B N   1 
ATOM 3397 C CA  . PHE B 1 12  ? 39.040 94.537  177.014 1.00 48.94  ? 12  PHE B CA  1 
ATOM 3398 C C   . PHE B 1 12  ? 39.790 95.587  176.208 1.00 47.70  ? 12  PHE B C   1 
ATOM 3399 O O   . PHE B 1 12  ? 39.335 95.954  175.127 1.00 47.49  ? 12  PHE B O   1 
ATOM 3400 C CB  . PHE B 1 12  ? 38.121 95.191  178.040 1.00 49.69  ? 12  PHE B CB  1 
ATOM 3401 C CG  . PHE B 1 12  ? 36.910 94.367  178.360 1.00 50.07  ? 12  PHE B CG  1 
ATOM 3402 C CD1 . PHE B 1 12  ? 36.765 93.101  177.810 1.00 50.54  ? 12  PHE B CD1 1 
ATOM 3403 C CD2 . PHE B 1 12  ? 35.934 94.832  179.236 1.00 50.20  ? 12  PHE B CD2 1 
ATOM 3404 C CE1 . PHE B 1 12  ? 35.648 92.320  178.091 1.00 50.13  ? 12  PHE B CE1 1 
ATOM 3405 C CE2 . PHE B 1 12  ? 34.813 94.061  179.524 1.00 49.95  ? 12  PHE B CE2 1 
ATOM 3406 C CZ  . PHE B 1 12  ? 34.682 92.794  178.962 1.00 49.90  ? 12  PHE B CZ  1 
ATOM 3407 N N   . GLY B 1 13  ? 40.936 96.056  176.712 1.00 46.30  ? 13  GLY B N   1 
ATOM 3408 C CA  . GLY B 1 13  ? 41.712 97.069  175.998 1.00 43.68  ? 13  GLY B CA  1 
ATOM 3409 C C   . GLY B 1 13  ? 41.927 96.610  174.577 1.00 40.81  ? 13  GLY B C   1 
ATOM 3410 O O   . GLY B 1 13  ? 42.231 97.390  173.672 1.00 39.65  ? 13  GLY B O   1 
ATOM 3411 N N   . LEU B 1 14  ? 41.770 95.309  174.396 1.00 39.30  ? 14  LEU B N   1 
ATOM 3412 C CA  . LEU B 1 14  ? 41.900 94.730  173.090 1.00 38.99  ? 14  LEU B CA  1 
ATOM 3413 C C   . LEU B 1 14  ? 40.515 94.768  172.466 1.00 38.66  ? 14  LEU B C   1 
ATOM 3414 O O   . LEU B 1 14  ? 40.367 95.118  171.293 1.00 39.33  ? 14  LEU B O   1 
ATOM 3415 C CB  . LEU B 1 14  ? 42.412 93.291  173.173 1.00 38.99  ? 14  LEU B CB  1 
ATOM 3416 C CG  . LEU B 1 14  ? 43.886 93.102  173.563 1.00 39.44  ? 14  LEU B CG  1 
ATOM 3417 C CD1 . LEU B 1 14  ? 44.275 91.663  173.233 1.00 38.79  ? 14  LEU B CD1 1 
ATOM 3418 C CD2 . LEU B 1 14  ? 44.803 94.097  172.829 1.00 38.71  ? 14  LEU B CD2 1 
ATOM 3419 N N   . PHE B 1 15  ? 39.493 94.433  173.248 1.00 37.74  ? 15  PHE B N   1 
ATOM 3420 C CA  . PHE B 1 15  ? 38.149 94.457  172.710 1.00 36.87  ? 15  PHE B CA  1 
ATOM 3421 C C   . PHE B 1 15  ? 37.937 95.796  172.038 1.00 38.07  ? 15  PHE B C   1 
ATOM 3422 O O   . PHE B 1 15  ? 37.448 95.859  170.909 1.00 39.30  ? 15  PHE B O   1 
ATOM 3423 C CB  . PHE B 1 15  ? 37.117 94.261  173.790 1.00 34.18  ? 15  PHE B CB  1 
ATOM 3424 C CG  . PHE B 1 15  ? 35.852 93.697  173.264 1.00 33.16  ? 15  PHE B CG  1 
ATOM 3425 C CD1 . PHE B 1 15  ? 35.865 92.499  172.550 1.00 32.64  ? 15  PHE B CD1 1 
ATOM 3426 C CD2 . PHE B 1 15  ? 34.657 94.367  173.422 1.00 32.56  ? 15  PHE B CD2 1 
ATOM 3427 C CE1 . PHE B 1 15  ? 34.695 91.978  171.996 1.00 32.73  ? 15  PHE B CE1 1 
ATOM 3428 C CE2 . PHE B 1 15  ? 33.475 93.857  172.873 1.00 32.56  ? 15  PHE B CE2 1 
ATOM 3429 C CZ  . PHE B 1 15  ? 33.494 92.661  172.158 1.00 32.52  ? 15  PHE B CZ  1 
ATOM 3430 N N   . PHE B 1 16  ? 38.317 96.867  172.732 1.00 39.05  ? 16  PHE B N   1 
ATOM 3431 C CA  . PHE B 1 16  ? 38.228 98.221  172.178 1.00 39.97  ? 16  PHE B CA  1 
ATOM 3432 C C   . PHE B 1 16  ? 38.895 98.196  170.800 1.00 39.30  ? 16  PHE B C   1 
ATOM 3433 O O   . PHE B 1 16  ? 38.250 98.381  169.769 1.00 38.84  ? 16  PHE B O   1 
ATOM 3434 C CB  . PHE B 1 16  ? 38.983 99.212  173.081 1.00 41.56  ? 16  PHE B CB  1 
ATOM 3435 C CG  . PHE B 1 16  ? 38.090 100.003 174.022 1.00 42.84  ? 16  PHE B CG  1 
ATOM 3436 C CD1 . PHE B 1 16  ? 37.461 99.390  175.098 1.00 42.16  ? 16  PHE B CD1 1 
ATOM 3437 C CD2 . PHE B 1 16  ? 37.849 101.357 173.797 1.00 42.69  ? 16  PHE B CD2 1 
ATOM 3438 C CE1 . PHE B 1 16  ? 36.611 100.107 175.920 1.00 41.22  ? 16  PHE B CE1 1 
ATOM 3439 C CE2 . PHE B 1 16  ? 36.999 102.074 174.617 1.00 42.12  ? 16  PHE B CE2 1 
ATOM 3440 C CZ  . PHE B 1 16  ? 36.380 101.443 175.678 1.00 41.78  ? 16  PHE B CZ  1 
ATOM 3441 N N   . PHE B 1 17  ? 40.198 97.955  170.829 1.00 38.95  ? 17  PHE B N   1 
ATOM 3442 C CA  . PHE B 1 17  ? 41.064 97.875  169.663 1.00 39.49  ? 17  PHE B CA  1 
ATOM 3443 C C   . PHE B 1 17  ? 40.426 97.173  168.450 1.00 39.30  ? 17  PHE B C   1 
ATOM 3444 O O   . PHE B 1 17  ? 40.495 97.679  167.333 1.00 39.54  ? 17  PHE B O   1 
ATOM 3445 C CB  . PHE B 1 17  ? 42.361 97.180  170.106 1.00 40.43  ? 17  PHE B CB  1 
ATOM 3446 C CG  . PHE B 1 17  ? 43.400 97.030  169.027 1.00 41.00  ? 17  PHE B CG  1 
ATOM 3447 C CD1 . PHE B 1 17  ? 44.311 98.042  168.750 1.00 40.44  ? 17  PHE B CD1 1 
ATOM 3448 C CD2 . PHE B 1 17  ? 43.491 95.860  168.313 1.00 40.40  ? 17  PHE B CD2 1 
ATOM 3449 C CE1 . PHE B 1 17  ? 45.291 97.869  167.775 1.00 40.63  ? 17  PHE B CE1 1 
ATOM 3450 C CE2 . PHE B 1 17  ? 44.468 95.698  167.347 1.00 40.27  ? 17  PHE B CE2 1 
ATOM 3451 C CZ  . PHE B 1 17  ? 45.364 96.694  167.077 1.00 40.99  ? 17  PHE B CZ  1 
ATOM 3452 N N   . PHE B 1 18  ? 39.779 96.034  168.649 1.00 38.76  ? 18  PHE B N   1 
ATOM 3453 C CA  . PHE B 1 18  ? 39.195 95.370  167.508 1.00 38.75  ? 18  PHE B CA  1 
ATOM 3454 C C   . PHE B 1 18  ? 37.754 95.773  167.154 1.00 39.64  ? 18  PHE B C   1 
ATOM 3455 O O   . PHE B 1 18  ? 37.139 95.213  166.249 1.00 39.31  ? 18  PHE B O   1 
ATOM 3456 C CB  . PHE B 1 18  ? 39.364 93.877  167.694 1.00 37.67  ? 18  PHE B CB  1 
ATOM 3457 C CG  . PHE B 1 18  ? 40.803 93.433  167.633 1.00 36.21  ? 18  PHE B CG  1 
ATOM 3458 C CD1 . PHE B 1 18  ? 41.356 93.076  166.422 1.00 36.22  ? 18  PHE B CD1 1 
ATOM 3459 C CD2 . PHE B 1 18  ? 41.599 93.367  168.771 1.00 35.38  ? 18  PHE B CD2 1 
ATOM 3460 C CE1 . PHE B 1 18  ? 42.677 92.654  166.323 1.00 36.23  ? 18  PHE B CE1 1 
ATOM 3461 C CE2 . PHE B 1 18  ? 42.937 92.939  168.686 1.00 35.08  ? 18  PHE B CE2 1 
ATOM 3462 C CZ  . PHE B 1 18  ? 43.472 92.584  167.457 1.00 35.30  ? 18  PHE B CZ  1 
ATOM 3463 N N   . TYR B 1 19  ? 37.224 96.780  167.831 1.00 40.71  ? 19  TYR B N   1 
ATOM 3464 C CA  . TYR B 1 19  ? 35.894 97.239  167.495 1.00 42.95  ? 19  TYR B CA  1 
ATOM 3465 C C   . TYR B 1 19  ? 36.168 98.214  166.378 1.00 45.15  ? 19  TYR B C   1 
ATOM 3466 O O   . TYR B 1 19  ? 35.681 98.075  165.251 1.00 45.72  ? 19  TYR B O   1 
ATOM 3467 C CB  . TYR B 1 19  ? 35.281 97.960  168.667 1.00 42.16  ? 19  TYR B CB  1 
ATOM 3468 C CG  . TYR B 1 19  ? 33.806 98.123  168.508 1.00 42.57  ? 19  TYR B CG  1 
ATOM 3469 C CD1 . TYR B 1 19  ? 32.996 97.029  168.197 1.00 42.17  ? 19  TYR B CD1 1 
ATOM 3470 C CD2 . TYR B 1 19  ? 33.202 99.351  168.723 1.00 42.30  ? 19  TYR B CD2 1 
ATOM 3471 C CE1 . TYR B 1 19  ? 31.614 97.161  168.113 1.00 42.74  ? 19  TYR B CE1 1 
ATOM 3472 C CE2 . TYR B 1 19  ? 31.826 99.494  168.644 1.00 43.04  ? 19  TYR B CE2 1 
ATOM 3473 C CZ  . TYR B 1 19  ? 31.036 98.400  168.345 1.00 43.13  ? 19  TYR B CZ  1 
ATOM 3474 O OH  . TYR B 1 19  ? 29.673 98.555  168.318 1.00 43.31  ? 19  TYR B OH  1 
ATOM 3475 N N   . PHE B 1 20  ? 36.984 99.200  166.712 1.00 48.05  ? 20  PHE B N   1 
ATOM 3476 C CA  . PHE B 1 20  ? 37.407 100.203 165.756 1.00 50.36  ? 20  PHE B CA  1 
ATOM 3477 C C   . PHE B 1 20  ? 37.846 99.583  164.424 1.00 50.23  ? 20  PHE B C   1 
ATOM 3478 O O   . PHE B 1 20  ? 37.809 100.243 163.394 1.00 49.65  ? 20  PHE B O   1 
ATOM 3479 C CB  . PHE B 1 20  ? 38.570 100.976 166.336 1.00 53.29  ? 20  PHE B CB  1 
ATOM 3480 C CG  . PHE B 1 20  ? 38.227 101.747 167.577 1.00 56.35  ? 20  PHE B CG  1 
ATOM 3481 C CD1 . PHE B 1 20  ? 37.735 101.117 168.705 1.00 56.51  ? 20  PHE B CD1 1 
ATOM 3482 C CD2 . PHE B 1 20  ? 38.422 103.123 167.623 1.00 57.42  ? 20  PHE B CD2 1 
ATOM 3483 C CE1 . PHE B 1 20  ? 37.451 101.875 169.860 1.00 57.42  ? 20  PHE B CE1 1 
ATOM 3484 C CE2 . PHE B 1 20  ? 38.143 103.872 168.759 1.00 57.28  ? 20  PHE B CE2 1 
ATOM 3485 C CZ  . PHE B 1 20  ? 37.661 103.253 169.875 1.00 57.55  ? 20  PHE B CZ  1 
ATOM 3486 N N   . PHE B 1 21  ? 38.249 98.316  164.436 1.00 50.27  ? 21  PHE B N   1 
ATOM 3487 C CA  . PHE B 1 21  ? 38.694 97.684  163.201 1.00 51.88  ? 21  PHE B CA  1 
ATOM 3488 C C   . PHE B 1 21  ? 37.545 97.489  162.282 1.00 51.44  ? 21  PHE B C   1 
ATOM 3489 O O   . PHE B 1 21  ? 37.508 98.029  161.170 1.00 51.34  ? 21  PHE B O   1 
ATOM 3490 C CB  . PHE B 1 21  ? 39.293 96.296  163.418 1.00 54.67  ? 21  PHE B CB  1 
ATOM 3491 C CG  . PHE B 1 21  ? 40.792 96.247  163.314 1.00 57.98  ? 21  PHE B CG  1 
ATOM 3492 C CD1 . PHE B 1 21  ? 41.563 96.559  164.419 1.00 60.76  ? 21  PHE B CD1 1 
ATOM 3493 C CD2 . PHE B 1 21  ? 41.445 95.913  162.109 1.00 56.67  ? 21  PHE B CD2 1 
ATOM 3494 C CE1 . PHE B 1 21  ? 42.955 96.536  164.332 1.00 61.83  ? 21  PHE B CE1 1 
ATOM 3495 C CE2 . PHE B 1 21  ? 42.854 95.891  162.022 1.00 56.95  ? 21  PHE B CE2 1 
ATOM 3496 C CZ  . PHE B 1 21  ? 43.599 96.204  163.120 1.00 59.75  ? 21  PHE B CZ  1 
ATOM 3497 N N   . ILE B 1 22  ? 36.620 96.656  162.729 1.00 52.18  ? 22  ILE B N   1 
ATOM 3498 C CA  . ILE B 1 22  ? 35.480 96.399  161.899 1.00 53.36  ? 22  ILE B CA  1 
ATOM 3499 C C   . ILE B 1 22  ? 34.809 97.720  161.662 1.00 53.68  ? 22  ILE B C   1 
ATOM 3500 O O   . ILE B 1 22  ? 34.433 98.012  160.528 1.00 53.83  ? 22  ILE B O   1 
ATOM 3501 C CB  . ILE B 1 22  ? 34.445 95.510  162.543 1.00 53.78  ? 22  ILE B CB  1 
ATOM 3502 C CG1 . ILE B 1 22  ? 35.092 94.573  163.535 1.00 55.13  ? 22  ILE B CG1 1 
ATOM 3503 C CG2 . ILE B 1 22  ? 33.711 94.732  161.456 1.00 53.64  ? 22  ILE B CG2 1 
ATOM 3504 C CD1 . ILE B 1 22  ? 34.060 93.843  164.352 1.00 56.80  ? 22  ILE B CD1 1 
ATOM 3505 N N   . MET B 1 23  ? 34.651 98.520  162.717 1.00 53.76  ? 23  MET B N   1 
ATOM 3506 C CA  . MET B 1 23  ? 33.980 99.797  162.548 1.00 54.09  ? 23  MET B CA  1 
ATOM 3507 C C   . MET B 1 23  ? 34.753 100.556 161.503 1.00 53.64  ? 23  MET B C   1 
ATOM 3508 O O   . MET B 1 23  ? 34.174 101.096 160.548 1.00 54.90  ? 23  MET B O   1 
ATOM 3509 C CB  . MET B 1 23  ? 33.930 100.597 163.846 1.00 55.76  ? 23  MET B CB  1 
ATOM 3510 C CG  . MET B 1 23  ? 33.264 101.960 163.657 1.00 57.71  ? 23  MET B CG  1 
ATOM 3511 S SD  . MET B 1 23  ? 32.704 102.817 165.136 1.00 61.07  ? 23  MET B SD  1 
ATOM 3512 C CE  . MET B 1 23  ? 34.290 103.407 165.764 1.00 60.91  ? 23  MET B CE  1 
ATOM 3513 N N   . GLY B 1 24  ? 36.070 100.568 161.666 1.00 52.22  ? 24  GLY B N   1 
ATOM 3514 C CA  . GLY B 1 24  ? 36.899 101.245 160.693 1.00 50.49  ? 24  GLY B CA  1 
ATOM 3515 C C   . GLY B 1 24  ? 36.382 100.934 159.304 1.00 48.31  ? 24  GLY B C   1 
ATOM 3516 O O   . GLY B 1 24  ? 35.604 101.717 158.732 1.00 48.75  ? 24  GLY B O   1 
ATOM 3517 N N   . ALA B 1 25  ? 36.782 99.790  158.765 1.00 45.72  ? 25  ALA B N   1 
ATOM 3518 C CA  . ALA B 1 25  ? 36.333 99.424  157.433 1.00 43.09  ? 25  ALA B CA  1 
ATOM 3519 C C   . ALA B 1 25  ? 34.933 99.920  157.227 1.00 41.54  ? 25  ALA B C   1 
ATOM 3520 O O   . ALA B 1 25  ? 34.694 100.786 156.415 1.00 40.73  ? 25  ALA B O   1 
ATOM 3521 C CB  . ALA B 1 25  ? 36.355 97.932  157.259 1.00 43.95  ? 25  ALA B CB  1 
ATOM 3522 N N   . TYR B 1 26  ? 34.015 99.393  158.015 1.00 40.14  ? 26  TYR B N   1 
ATOM 3523 C CA  . TYR B 1 26  ? 32.633 99.784  157.893 1.00 39.81  ? 26  TYR B CA  1 
ATOM 3524 C C   . TYR B 1 26  ? 32.428 101.206 157.425 1.00 42.12  ? 26  TYR B C   1 
ATOM 3525 O O   . TYR B 1 26  ? 32.344 101.431 156.231 1.00 43.22  ? 26  TYR B O   1 
ATOM 3526 C CB  . TYR B 1 26  ? 31.880 99.600  159.203 1.00 37.30  ? 26  TYR B CB  1 
ATOM 3527 C CG  . TYR B 1 26  ? 30.421 100.037 159.141 1.00 35.58  ? 26  TYR B CG  1 
ATOM 3528 C CD1 . TYR B 1 26  ? 29.423 99.162  158.719 1.00 33.42  ? 26  TYR B CD1 1 
ATOM 3529 C CD2 . TYR B 1 26  ? 30.044 101.336 159.494 1.00 34.71  ? 26  TYR B CD2 1 
ATOM 3530 C CE1 . TYR B 1 26  ? 28.087 99.567  158.657 1.00 32.96  ? 26  TYR B CE1 1 
ATOM 3531 C CE2 . TYR B 1 26  ? 28.718 101.751 159.428 1.00 33.15  ? 26  TYR B CE2 1 
ATOM 3532 C CZ  . TYR B 1 26  ? 27.746 100.860 159.011 1.00 32.96  ? 26  TYR B CZ  1 
ATOM 3533 O OH  . TYR B 1 26  ? 26.435 101.261 158.954 1.00 32.48  ? 26  TYR B OH  1 
ATOM 3534 N N   . PHE B 1 27  ? 32.368 102.162 158.349 1.00 44.15  ? 27  PHE B N   1 
ATOM 3535 C CA  . PHE B 1 27  ? 32.074 103.543 157.997 1.00 46.90  ? 27  PHE B CA  1 
ATOM 3536 C C   . PHE B 1 27  ? 32.537 103.982 156.598 1.00 48.20  ? 27  PHE B C   1 
ATOM 3537 O O   . PHE B 1 27  ? 31.708 104.190 155.700 1.00 48.43  ? 27  PHE B O   1 
ATOM 3538 C CB  . PHE B 1 27  ? 32.596 104.486 159.064 1.00 49.23  ? 27  PHE B CB  1 
ATOM 3539 C CG  . PHE B 1 27  ? 32.011 105.845 158.965 1.00 54.02  ? 27  PHE B CG  1 
ATOM 3540 C CD1 . PHE B 1 27  ? 32.522 106.761 158.039 1.00 56.08  ? 27  PHE B CD1 1 
ATOM 3541 C CD2 . PHE B 1 27  ? 30.910 106.207 159.745 1.00 54.54  ? 27  PHE B CD2 1 
ATOM 3542 C CE1 . PHE B 1 27  ? 31.940 108.039 157.877 1.00 57.84  ? 27  PHE B CE1 1 
ATOM 3543 C CE2 . PHE B 1 27  ? 30.313 107.480 159.603 1.00 56.77  ? 27  PHE B CE2 1 
ATOM 3544 C CZ  . PHE B 1 27  ? 30.829 108.401 158.665 1.00 57.98  ? 27  PHE B CZ  1 
ATOM 3545 N N   . PRO B 1 28  ? 33.852 104.163 156.395 1.00 49.33  ? 28  PRO B N   1 
ATOM 3546 C CA  . PRO B 1 28  ? 34.351 104.565 155.068 1.00 48.82  ? 28  PRO B CA  1 
ATOM 3547 C C   . PRO B 1 28  ? 33.974 103.549 153.981 1.00 49.31  ? 28  PRO B C   1 
ATOM 3548 O O   . PRO B 1 28  ? 33.224 103.844 153.064 1.00 48.06  ? 28  PRO B O   1 
ATOM 3549 C CB  . PRO B 1 28  ? 35.866 104.647 155.275 1.00 49.68  ? 28  PRO B CB  1 
ATOM 3550 C CG  . PRO B 1 28  ? 36.107 104.040 156.646 1.00 49.42  ? 28  PRO B CG  1 
ATOM 3551 C CD  . PRO B 1 28  ? 34.893 104.341 157.419 1.00 48.26  ? 28  PRO B CD  1 
ATOM 3552 N N   . PHE B 1 29  ? 34.524 102.349 154.107 1.00 50.05  ? 29  PHE B N   1 
ATOM 3553 C CA  . PHE B 1 29  ? 34.262 101.249 153.178 1.00 50.95  ? 29  PHE B CA  1 
ATOM 3554 C C   . PHE B 1 29  ? 32.846 101.453 152.606 1.00 47.36  ? 29  PHE B C   1 
ATOM 3555 O O   . PHE B 1 29  ? 32.663 101.566 151.396 1.00 46.19  ? 29  PHE B O   1 
ATOM 3556 C CB  . PHE B 1 29  ? 34.405 99.896  153.964 1.00 57.26  ? 29  PHE B CB  1 
ATOM 3557 C CG  . PHE B 1 29  ? 34.295 98.615  153.114 1.00 63.17  ? 29  PHE B CG  1 
ATOM 3558 C CD1 . PHE B 1 29  ? 33.057 98.176  152.651 1.00 64.95  ? 29  PHE B CD1 1 
ATOM 3559 C CD2 . PHE B 1 29  ? 35.423 97.798  152.859 1.00 65.12  ? 29  PHE B CD2 1 
ATOM 3560 C CE1 . PHE B 1 29  ? 32.935 96.964  151.961 1.00 66.11  ? 29  PHE B CE1 1 
ATOM 3561 C CE2 . PHE B 1 29  ? 35.295 96.557  152.153 1.00 66.61  ? 29  PHE B CE2 1 
ATOM 3562 C CZ  . PHE B 1 29  ? 34.046 96.148  151.710 1.00 66.79  ? 29  PHE B CZ  1 
ATOM 3563 N N   . PHE B 1 30  ? 31.879 101.559 153.515 1.00 44.13  ? 30  PHE B N   1 
ATOM 3564 C CA  . PHE B 1 30  ? 30.478 101.715 153.197 1.00 40.47  ? 30  PHE B CA  1 
ATOM 3565 C C   . PHE B 1 30  ? 30.219 102.548 151.962 1.00 38.92  ? 30  PHE B C   1 
ATOM 3566 O O   . PHE B 1 30  ? 29.936 102.011 150.869 1.00 39.61  ? 30  PHE B O   1 
ATOM 3567 C CB  . PHE B 1 30  ? 29.756 102.300 154.397 1.00 37.75  ? 30  PHE B CB  1 
ATOM 3568 C CG  . PHE B 1 30  ? 28.307 102.048 154.397 1.00 35.57  ? 30  PHE B CG  1 
ATOM 3569 C CD1 . PHE B 1 30  ? 27.679 101.607 153.251 1.00 33.92  ? 30  PHE B CD1 1 
ATOM 3570 C CD2 . PHE B 1 30  ? 27.565 102.220 155.552 1.00 36.16  ? 30  PHE B CD2 1 
ATOM 3571 C CE1 . PHE B 1 30  ? 26.344 101.330 153.230 1.00 32.68  ? 30  PHE B CE1 1 
ATOM 3572 C CE2 . PHE B 1 30  ? 26.215 101.942 155.542 1.00 35.88  ? 30  PHE B CE2 1 
ATOM 3573 C CZ  . PHE B 1 30  ? 25.604 101.494 154.372 1.00 34.01  ? 30  PHE B CZ  1 
ATOM 3574 N N   . PRO B 1 31  ? 30.303 103.868 152.092 1.00 38.38  ? 31  PRO B N   1 
ATOM 3575 C CA  . PRO B 1 31  ? 30.039 104.619 150.860 1.00 38.46  ? 31  PRO B CA  1 
ATOM 3576 C C   . PRO B 1 31  ? 30.760 104.064 149.609 1.00 37.79  ? 31  PRO B C   1 
ATOM 3577 O O   . PRO B 1 31  ? 30.141 103.786 148.579 1.00 36.82  ? 31  PRO B O   1 
ATOM 3578 C CB  . PRO B 1 31  ? 30.497 106.027 151.219 1.00 38.71  ? 31  PRO B CB  1 
ATOM 3579 C CG  . PRO B 1 31  ? 30.240 106.110 152.704 1.00 38.81  ? 31  PRO B CG  1 
ATOM 3580 C CD  . PRO B 1 31  ? 30.694 104.755 153.200 1.00 38.11  ? 31  PRO B CD  1 
ATOM 3581 N N   . ILE B 1 32  ? 32.071 103.907 149.699 1.00 38.27  ? 32  ILE B N   1 
ATOM 3582 C CA  . ILE B 1 32  ? 32.815 103.401 148.567 1.00 39.15  ? 32  ILE B CA  1 
ATOM 3583 C C   . ILE B 1 32  ? 32.210 102.102 148.117 1.00 39.26  ? 32  ILE B C   1 
ATOM 3584 O O   . ILE B 1 32  ? 31.895 101.930 146.949 1.00 38.95  ? 32  ILE B O   1 
ATOM 3585 C CB  . ILE B 1 32  ? 34.252 103.112 148.930 1.00 40.14  ? 32  ILE B CB  1 
ATOM 3586 C CG1 . ILE B 1 32  ? 34.923 104.393 149.388 1.00 41.07  ? 32  ILE B CG1 1 
ATOM 3587 C CG2 . ILE B 1 32  ? 34.979 102.511 147.734 1.00 40.71  ? 32  ILE B CG2 1 
ATOM 3588 C CD1 . ILE B 1 32  ? 36.151 104.145 150.237 1.00 43.51  ? 32  ILE B CD1 1 
ATOM 3589 N N   . TRP B 1 33  ? 32.052 101.189 149.064 1.00 39.77  ? 33  TRP B N   1 
ATOM 3590 C CA  . TRP B 1 33  ? 31.521 99.875  148.781 1.00 40.96  ? 33  TRP B CA  1 
ATOM 3591 C C   . TRP B 1 33  ? 30.282 99.969  147.935 1.00 43.30  ? 33  TRP B C   1 
ATOM 3592 O O   . TRP B 1 33  ? 30.008 99.099  147.116 1.00 43.53  ? 33  TRP B O   1 
ATOM 3593 C CB  . TRP B 1 33  ? 31.192 99.165  150.075 1.00 38.91  ? 33  TRP B CB  1 
ATOM 3594 C CG  . TRP B 1 33  ? 30.702 97.778  149.903 1.00 37.70  ? 33  TRP B CG  1 
ATOM 3595 C CD1 . TRP B 1 33  ? 31.430 96.710  149.539 1.00 37.52  ? 33  TRP B CD1 1 
ATOM 3596 C CD2 . TRP B 1 33  ? 29.377 97.304  150.131 1.00 37.60  ? 33  TRP B CD2 1 
ATOM 3597 N NE1 . TRP B 1 33  ? 30.655 95.578  149.519 1.00 38.04  ? 33  TRP B NE1 1 
ATOM 3598 C CE2 . TRP B 1 33  ? 29.384 95.916  149.872 1.00 37.71  ? 33  TRP B CE2 1 
ATOM 3599 C CE3 . TRP B 1 33  ? 28.186 97.912  150.512 1.00 37.74  ? 33  TRP B CE3 1 
ATOM 3600 C CZ2 . TRP B 1 33  ? 28.241 95.124  150.005 1.00 38.25  ? 33  TRP B CZ2 1 
ATOM 3601 C CZ3 . TRP B 1 33  ? 27.051 97.131  150.643 1.00 38.01  ? 33  TRP B CZ3 1 
ATOM 3602 C CH2 . TRP B 1 33  ? 27.085 95.748  150.382 1.00 37.93  ? 33  TRP B CH2 1 
ATOM 3603 N N   . LEU B 1 34  ? 29.538 101.044 148.117 1.00 46.30  ? 34  LEU B N   1 
ATOM 3604 C CA  . LEU B 1 34  ? 28.318 101.234 147.358 1.00 49.97  ? 34  LEU B CA  1 
ATOM 3605 C C   . LEU B 1 34  ? 28.588 101.588 145.905 1.00 52.51  ? 34  LEU B C   1 
ATOM 3606 O O   . LEU B 1 34  ? 28.027 101.000 144.973 1.00 53.36  ? 34  LEU B O   1 
ATOM 3607 C CB  . LEU B 1 34  ? 27.522 102.338 148.002 1.00 49.75  ? 34  LEU B CB  1 
ATOM 3608 C CG  . LEU B 1 34  ? 27.033 101.967 149.386 1.00 50.92  ? 34  LEU B CG  1 
ATOM 3609 C CD1 . LEU B 1 34  ? 26.295 103.130 150.002 1.00 51.33  ? 34  LEU B CD1 1 
ATOM 3610 C CD2 . LEU B 1 34  ? 26.124 100.763 149.278 1.00 50.88  ? 34  LEU B CD2 1 
ATOM 3611 N N   . HIS B 1 35  ? 29.458 102.563 145.722 1.00 55.33  ? 35  HIS B N   1 
ATOM 3612 C CA  . HIS B 1 35  ? 29.793 103.008 144.397 1.00 57.40  ? 35  HIS B CA  1 
ATOM 3613 C C   . HIS B 1 35  ? 30.438 101.912 143.546 1.00 56.70  ? 35  HIS B C   1 
ATOM 3614 O O   . HIS B 1 35  ? 29.753 101.228 142.792 1.00 56.77  ? 35  HIS B O   1 
ATOM 3615 C CB  . HIS B 1 35  ? 30.706 104.218 144.521 1.00 60.82  ? 35  HIS B CB  1 
ATOM 3616 C CG  . HIS B 1 35  ? 30.780 105.045 143.283 1.00 63.93  ? 35  HIS B CG  1 
ATOM 3617 N ND1 . HIS B 1 35  ? 31.882 105.030 142.455 1.00 66.57  ? 35  HIS B ND1 1 
ATOM 3618 C CD2 . HIS B 1 35  ? 29.909 105.928 142.744 1.00 65.36  ? 35  HIS B CD2 1 
ATOM 3619 C CE1 . HIS B 1 35  ? 31.688 105.875 141.459 1.00 67.67  ? 35  HIS B CE1 1 
ATOM 3620 N NE2 . HIS B 1 35  ? 30.495 106.437 141.610 1.00 66.85  ? 35  HIS B NE2 1 
ATOM 3621 N N   . ASP B 1 36  ? 31.743 101.718 143.693 1.00 55.20  ? 36  ASP B N   1 
ATOM 3622 C CA  . ASP B 1 36  ? 32.442 100.728 142.884 1.00 53.52  ? 36  ASP B CA  1 
ATOM 3623 C C   . ASP B 1 36  ? 31.892 99.328  142.951 1.00 51.45  ? 36  ASP B C   1 
ATOM 3624 O O   . ASP B 1 36  ? 31.881 98.593  141.965 1.00 50.66  ? 36  ASP B O   1 
ATOM 3625 C CB  . ASP B 1 36  ? 33.916 100.686 143.262 1.00 55.52  ? 36  ASP B CB  1 
ATOM 3626 C CG  . ASP B 1 36  ? 34.594 102.035 143.111 1.00 57.13  ? 36  ASP B CG  1 
ATOM 3627 O OD1 . ASP B 1 36  ? 34.153 102.843 142.273 1.00 57.64  ? 36  ASP B OD1 1 
ATOM 3628 O OD2 . ASP B 1 36  ? 35.588 102.282 143.822 1.00 59.04  ? 36  ASP B OD2 1 
ATOM 3629 N N   . ILE B 1 37  ? 31.423 98.962  144.122 1.00 49.04  ? 37  ILE B N   1 
ATOM 3630 C CA  . ILE B 1 37  ? 30.942 97.628  144.297 1.00 47.54  ? 37  ILE B CA  1 
ATOM 3631 C C   . ILE B 1 37  ? 29.466 97.462  144.095 1.00 46.12  ? 37  ILE B C   1 
ATOM 3632 O O   . ILE B 1 37  ? 29.018 96.451  143.590 1.00 45.99  ? 37  ILE B O   1 
ATOM 3633 C CB  . ILE B 1 37  ? 31.345 97.140  145.682 1.00 48.86  ? 37  ILE B CB  1 
ATOM 3634 C CG1 . ILE B 1 37  ? 32.856 97.348  145.842 1.00 50.15  ? 37  ILE B CG1 1 
ATOM 3635 C CG2 . ILE B 1 37  ? 30.943 95.674  145.868 1.00 49.50  ? 37  ILE B CG2 1 
ATOM 3636 C CD1 . ILE B 1 37  ? 33.317 97.488  147.272 1.00 51.73  ? 37  ILE B CD1 1 
ATOM 3637 N N   . ASN B 1 38  ? 28.692 98.460  144.451 1.00 45.06  ? 38  ASN B N   1 
ATOM 3638 C CA  . ASN B 1 38  ? 27.278 98.265  144.317 1.00 45.16  ? 38  ASN B CA  1 
ATOM 3639 C C   . ASN B 1 38  ? 26.563 99.264  143.462 1.00 45.39  ? 38  ASN B C   1 
ATOM 3640 O O   . ASN B 1 38  ? 25.350 99.441  143.577 1.00 45.99  ? 38  ASN B O   1 
ATOM 3641 C CB  . ASN B 1 38  ? 26.649 98.196  145.700 1.00 44.91  ? 38  ASN B CB  1 
ATOM 3642 C CG  . ASN B 1 38  ? 27.195 97.048  146.513 1.00 44.89  ? 38  ASN B CG  1 
ATOM 3643 O OD1 . ASN B 1 38  ? 27.211 95.906  146.048 1.00 44.40  ? 38  ASN B OD1 1 
ATOM 3644 N ND2 . ASN B 1 38  ? 27.648 97.338  147.736 1.00 45.09  ? 38  ASN B ND2 1 
ATOM 3645 N N   . HIS B 1 39  ? 27.320 99.935  142.609 1.00 45.84  ? 39  HIS B N   1 
ATOM 3646 C CA  . HIS B 1 39  ? 26.746 100.919 141.695 1.00 46.37  ? 39  HIS B CA  1 
ATOM 3647 C C   . HIS B 1 39  ? 25.573 101.685 142.295 1.00 46.09  ? 39  HIS B C   1 
ATOM 3648 O O   . HIS B 1 39  ? 24.550 101.890 141.646 1.00 45.43  ? 39  HIS B O   1 
ATOM 3649 C CB  . HIS B 1 39  ? 26.281 100.182 140.448 1.00 47.94  ? 39  HIS B CB  1 
ATOM 3650 C CG  . HIS B 1 39  ? 27.333 99.332  139.830 1.00 49.28  ? 39  HIS B CG  1 
ATOM 3651 N ND1 . HIS B 1 39  ? 28.458 99.864  139.223 1.00 50.16  ? 39  HIS B ND1 1 
ATOM 3652 C CD2 . HIS B 1 39  ? 27.483 97.985  139.765 1.00 49.00  ? 39  HIS B CD2 1 
ATOM 3653 C CE1 . HIS B 1 39  ? 29.242 98.897  138.832 1.00 50.08  ? 39  HIS B CE1 1 
ATOM 3654 N NE2 . HIS B 1 39  ? 28.680 97.734  139.144 1.00 49.42  ? 39  HIS B NE2 1 
ATOM 3655 N N   . ILE B 1 40  ? 25.737 102.122 143.528 1.00 45.82  ? 40  ILE B N   1 
ATOM 3656 C CA  . ILE B 1 40  ? 24.667 102.818 144.186 1.00 46.72  ? 40  ILE B CA  1 
ATOM 3657 C C   . ILE B 1 40  ? 24.412 104.219 143.688 1.00 46.58  ? 40  ILE B C   1 
ATOM 3658 O O   . ILE B 1 40  ? 25.338 104.952 143.373 1.00 46.73  ? 40  ILE B O   1 
ATOM 3659 C CB  . ILE B 1 40  ? 24.940 102.899 145.655 1.00 47.89  ? 40  ILE B CB  1 
ATOM 3660 C CG1 . ILE B 1 40  ? 23.706 103.389 146.374 1.00 49.30  ? 40  ILE B CG1 1 
ATOM 3661 C CG2 . ILE B 1 40  ? 26.056 103.889 145.903 1.00 47.74  ? 40  ILE B CG2 1 
ATOM 3662 C CD1 . ILE B 1 40  ? 23.788 103.156 147.874 1.00 50.53  ? 40  ILE B CD1 1 
ATOM 3663 N N   . SER B 1 41  ? 23.142 104.578 143.595 1.00 47.36  ? 41  SER B N   1 
ATOM 3664 C CA  . SER B 1 41  ? 22.812 105.916 143.171 1.00 48.83  ? 41  SER B CA  1 
ATOM 3665 C C   . SER B 1 41  ? 22.551 106.696 144.439 1.00 50.01  ? 41  SER B C   1 
ATOM 3666 O O   . SER B 1 41  ? 22.819 106.217 145.536 1.00 49.83  ? 41  SER B O   1 
ATOM 3667 C CB  . SER B 1 41  ? 21.577 105.923 142.282 1.00 49.01  ? 41  SER B CB  1 
ATOM 3668 O OG  . SER B 1 41  ? 20.584 105.097 142.838 1.00 49.13  ? 41  SER B OG  1 
ATOM 3669 N N   . LYS B 1 42  ? 22.014 107.895 144.284 1.00 51.26  ? 42  LYS B N   1 
ATOM 3670 C CA  . LYS B 1 42  ? 21.729 108.767 145.412 1.00 52.51  ? 42  LYS B CA  1 
ATOM 3671 C C   . LYS B 1 42  ? 20.510 108.350 146.199 1.00 51.95  ? 42  LYS B C   1 
ATOM 3672 O O   . LYS B 1 42  ? 20.593 108.140 147.406 1.00 51.86  ? 42  LYS B O   1 
ATOM 3673 C CB  . LYS B 1 42  ? 21.547 110.195 144.916 1.00 55.40  ? 42  LYS B CB  1 
ATOM 3674 C CG  . LYS B 1 42  ? 22.709 110.704 144.057 1.00 57.79  ? 42  LYS B CG  1 
ATOM 3675 C CD  . LYS B 1 42  ? 24.025 110.698 144.827 1.00 59.39  ? 42  LYS B CD  1 
ATOM 3676 C CE  . LYS B 1 42  ? 25.123 111.320 144.002 1.00 59.50  ? 42  LYS B CE  1 
ATOM 3677 N NZ  . LYS B 1 42  ? 25.978 112.096 144.907 1.00 62.71  ? 42  LYS B NZ  1 
ATOM 3678 N N   . SER B 1 43  ? 19.369 108.262 145.525 1.00 52.21  ? 43  SER B N   1 
ATOM 3679 C CA  . SER B 1 43  ? 18.149 107.834 146.197 1.00 52.72  ? 43  SER B CA  1 
ATOM 3680 C C   . SER B 1 43  ? 18.529 106.638 147.089 1.00 52.08  ? 43  SER B C   1 
ATOM 3681 O O   . SER B 1 43  ? 18.203 106.613 148.287 1.00 52.48  ? 43  SER B O   1 
ATOM 3682 C CB  . SER B 1 43  ? 17.089 107.424 145.161 1.00 53.55  ? 43  SER B CB  1 
ATOM 3683 O OG  . SER B 1 43  ? 16.508 108.564 144.546 1.00 54.04  ? 43  SER B OG  1 
ATOM 3684 N N   . ASP B 1 44  ? 19.249 105.677 146.497 1.00 50.48  ? 44  ASP B N   1 
ATOM 3685 C CA  . ASP B 1 44  ? 19.700 104.475 147.197 1.00 48.03  ? 44  ASP B CA  1 
ATOM 3686 C C   . ASP B 1 44  ? 20.537 104.840 148.438 1.00 45.14  ? 44  ASP B C   1 
ATOM 3687 O O   . ASP B 1 44  ? 20.126 104.591 149.583 1.00 43.85  ? 44  ASP B O   1 
ATOM 3688 C CB  . ASP B 1 44  ? 20.509 103.566 146.241 1.00 50.67  ? 44  ASP B CB  1 
ATOM 3689 C CG  . ASP B 1 44  ? 19.751 103.202 144.947 1.00 51.02  ? 44  ASP B CG  1 
ATOM 3690 O OD1 . ASP B 1 44  ? 18.495 103.146 144.933 1.00 51.30  ? 44  ASP B OD1 1 
ATOM 3691 O OD2 . ASP B 1 44  ? 20.446 102.938 143.943 1.00 52.17  ? 44  ASP B OD2 1 
ATOM 3692 N N   . THR B 1 45  ? 21.695 105.452 148.204 1.00 42.20  ? 45  THR B N   1 
ATOM 3693 C CA  . THR B 1 45  ? 22.569 105.865 149.284 1.00 39.28  ? 45  THR B CA  1 
ATOM 3694 C C   . THR B 1 45  ? 21.686 106.548 150.308 1.00 37.85  ? 45  THR B C   1 
ATOM 3695 O O   . THR B 1 45  ? 21.454 106.034 151.409 1.00 37.67  ? 45  THR B O   1 
ATOM 3696 C CB  . THR B 1 45  ? 23.628 106.866 148.778 1.00 38.80  ? 45  THR B CB  1 
ATOM 3697 O OG1 . THR B 1 45  ? 22.983 108.003 148.205 1.00 38.89  ? 45  THR B OG1 1 
ATOM 3698 C CG2 . THR B 1 45  ? 24.505 106.253 147.713 1.00 38.39  ? 45  THR B CG2 1 
ATOM 3699 N N   . GLY B 1 46  ? 21.184 107.701 149.876 1.00 35.57  ? 46  GLY B N   1 
ATOM 3700 C CA  . GLY B 1 46  ? 20.315 108.550 150.658 1.00 32.27  ? 46  GLY B CA  1 
ATOM 3701 C C   . GLY B 1 46  ? 19.408 107.827 151.609 1.00 29.79  ? 46  GLY B C   1 
ATOM 3702 O O   . GLY B 1 46  ? 19.274 108.226 152.757 1.00 29.72  ? 46  GLY B O   1 
ATOM 3703 N N   . ILE B 1 47  ? 18.781 106.762 151.145 1.00 27.86  ? 47  ILE B N   1 
ATOM 3704 C CA  . ILE B 1 47  ? 17.905 106.029 152.017 1.00 26.35  ? 47  ILE B CA  1 
ATOM 3705 C C   . ILE B 1 47  ? 18.749 105.114 152.838 1.00 25.44  ? 47  ILE B C   1 
ATOM 3706 O O   . ILE B 1 47  ? 18.615 105.070 154.052 1.00 24.19  ? 47  ILE B O   1 
ATOM 3707 C CB  . ILE B 1 47  ? 16.903 105.224 151.243 1.00 25.75  ? 47  ILE B CB  1 
ATOM 3708 C CG1 . ILE B 1 47  ? 16.023 106.182 150.454 1.00 26.46  ? 47  ILE B CG1 1 
ATOM 3709 C CG2 . ILE B 1 47  ? 16.066 104.397 152.190 1.00 26.03  ? 47  ILE B CG2 1 
ATOM 3710 C CD1 . ILE B 1 47  ? 14.897 105.509 149.736 1.00 27.58  ? 47  ILE B CD1 1 
ATOM 3711 N N   . ILE B 1 48  ? 19.633 104.379 152.190 1.00 25.17  ? 48  ILE B N   1 
ATOM 3712 C CA  . ILE B 1 48  ? 20.472 103.510 152.964 1.00 25.47  ? 48  ILE B CA  1 
ATOM 3713 C C   . ILE B 1 48  ? 20.911 104.302 154.184 1.00 25.77  ? 48  ILE B C   1 
ATOM 3714 O O   . ILE B 1 48  ? 20.511 104.002 155.310 1.00 24.48  ? 48  ILE B O   1 
ATOM 3715 C CB  . ILE B 1 48  ? 21.671 103.070 152.161 1.00 25.39  ? 48  ILE B CB  1 
ATOM 3716 C CG1 . ILE B 1 48  ? 21.191 102.218 151.001 1.00 26.19  ? 48  ILE B CG1 1 
ATOM 3717 C CG2 . ILE B 1 48  ? 22.624 102.284 153.027 1.00 24.81  ? 48  ILE B CG2 1 
ATOM 3718 C CD1 . ILE B 1 48  ? 22.300 101.485 150.307 1.00 28.52  ? 48  ILE B CD1 1 
ATOM 3719 N N   . PHE B 1 49  ? 21.691 105.349 153.966 1.00 27.37  ? 49  PHE B N   1 
ATOM 3720 C CA  . PHE B 1 49  ? 22.152 106.124 155.098 1.00 29.79  ? 49  PHE B CA  1 
ATOM 3721 C C   . PHE B 1 49  ? 21.055 106.596 156.029 1.00 31.63  ? 49  PHE B C   1 
ATOM 3722 O O   . PHE B 1 49  ? 21.055 106.276 157.220 1.00 32.43  ? 49  PHE B O   1 
ATOM 3723 C CB  . PHE B 1 49  ? 22.978 107.303 154.637 1.00 28.84  ? 49  PHE B CB  1 
ATOM 3724 C CG  . PHE B 1 49  ? 24.415 106.994 154.561 1.00 29.04  ? 49  PHE B CG  1 
ATOM 3725 C CD1 . PHE B 1 49  ? 25.203 107.079 155.688 1.00 30.83  ? 49  PHE B CD1 1 
ATOM 3726 C CD2 . PHE B 1 49  ? 24.985 106.579 153.385 1.00 29.86  ? 49  PHE B CD2 1 
ATOM 3727 C CE1 . PHE B 1 49  ? 26.551 106.753 155.642 1.00 32.16  ? 49  PHE B CE1 1 
ATOM 3728 C CE2 . PHE B 1 49  ? 26.332 106.253 153.327 1.00 31.08  ? 49  PHE B CE2 1 
ATOM 3729 C CZ  . PHE B 1 49  ? 27.116 106.341 154.456 1.00 31.68  ? 49  PHE B CZ  1 
ATOM 3730 N N   . ALA B 1 50  ? 20.114 107.355 155.489 1.00 33.83  ? 50  ALA B N   1 
ATOM 3731 C CA  . ALA B 1 50  ? 19.019 107.869 156.297 1.00 34.50  ? 50  ALA B CA  1 
ATOM 3732 C C   . ALA B 1 50  ? 18.388 106.736 157.085 1.00 34.20  ? 50  ALA B C   1 
ATOM 3733 O O   . ALA B 1 50  ? 18.291 106.794 158.309 1.00 35.12  ? 50  ALA B O   1 
ATOM 3734 C CB  . ALA B 1 50  ? 17.977 108.531 155.411 1.00 35.56  ? 50  ALA B CB  1 
ATOM 3735 N N   . ALA B 1 51  ? 17.971 105.699 156.378 1.00 33.56  ? 51  ALA B N   1 
ATOM 3736 C CA  . ALA B 1 51  ? 17.333 104.584 157.028 1.00 33.57  ? 51  ALA B CA  1 
ATOM 3737 C C   . ALA B 1 51  ? 18.117 104.233 158.280 1.00 33.91  ? 51  ALA B C   1 
ATOM 3738 O O   . ALA B 1 51  ? 17.569 104.210 159.391 1.00 33.15  ? 51  ALA B O   1 
ATOM 3739 C CB  . ALA B 1 51  ? 17.277 103.436 156.083 1.00 33.86  ? 51  ALA B CB  1 
ATOM 3740 N N   . ILE B 1 52  ? 19.408 103.990 158.097 1.00 35.22  ? 52  ILE B N   1 
ATOM 3741 C CA  . ILE B 1 52  ? 20.272 103.649 159.208 1.00 37.94  ? 52  ILE B CA  1 
ATOM 3742 C C   . ILE B 1 52  ? 19.896 104.489 160.404 1.00 38.61  ? 52  ILE B C   1 
ATOM 3743 O O   . ILE B 1 52  ? 19.714 103.977 161.497 1.00 38.99  ? 52  ILE B O   1 
ATOM 3744 C CB  . ILE B 1 52  ? 21.737 103.907 158.872 1.00 38.62  ? 52  ILE B CB  1 
ATOM 3745 C CG1 . ILE B 1 52  ? 22.253 102.816 157.926 1.00 40.09  ? 52  ILE B CG1 1 
ATOM 3746 C CG2 . ILE B 1 52  ? 22.536 103.967 160.149 1.00 38.52  ? 52  ILE B CG2 1 
ATOM 3747 C CD1 . ILE B 1 52  ? 23.750 102.856 157.684 1.00 42.14  ? 52  ILE B CD1 1 
ATOM 3748 N N   . SER B 1 53  ? 19.777 105.787 160.188 1.00 40.19  ? 53  SER B N   1 
ATOM 3749 C CA  . SER B 1 53  ? 19.401 106.678 161.265 1.00 41.65  ? 53  SER B CA  1 
ATOM 3750 C C   . SER B 1 53  ? 18.175 106.140 162.004 1.00 41.46  ? 53  SER B C   1 
ATOM 3751 O O   . SER B 1 53  ? 18.188 106.069 163.236 1.00 41.92  ? 53  SER B O   1 
ATOM 3752 C CB  . SER B 1 53  ? 19.124 108.082 160.712 1.00 43.01  ? 53  SER B CB  1 
ATOM 3753 O OG  . SER B 1 53  ? 17.977 108.679 161.300 1.00 45.08  ? 53  SER B OG  1 
ATOM 3754 N N   . LEU B 1 54  ? 17.134 105.734 161.270 1.00 40.55  ? 54  LEU B N   1 
ATOM 3755 C CA  . LEU B 1 54  ? 15.923 105.238 161.923 1.00 40.09  ? 54  LEU B CA  1 
ATOM 3756 C C   . LEU B 1 54  ? 16.286 104.279 163.026 1.00 40.08  ? 54  LEU B C   1 
ATOM 3757 O O   . LEU B 1 54  ? 15.857 104.424 164.166 1.00 40.16  ? 54  LEU B O   1 
ATOM 3758 C CB  . LEU B 1 54  ? 14.986 104.527 160.955 1.00 39.49  ? 54  LEU B CB  1 
ATOM 3759 C CG  . LEU B 1 54  ? 13.766 104.034 161.742 1.00 39.69  ? 54  LEU B CG  1 
ATOM 3760 C CD1 . LEU B 1 54  ? 12.798 105.187 161.891 1.00 39.09  ? 54  LEU B CD1 1 
ATOM 3761 C CD2 . LEU B 1 54  ? 13.097 102.861 161.052 1.00 39.49  ? 54  LEU B CD2 1 
ATOM 3762 N N   . PHE B 1 55  ? 17.094 103.295 162.690 1.00 39.96  ? 55  PHE B N   1 
ATOM 3763 C CA  . PHE B 1 55  ? 17.490 102.357 163.695 1.00 39.62  ? 55  PHE B CA  1 
ATOM 3764 C C   . PHE B 1 55  ? 18.474 102.899 164.712 1.00 39.84  ? 55  PHE B C   1 
ATOM 3765 O O   . PHE B 1 55  ? 18.637 102.309 165.776 1.00 40.38  ? 55  PHE B O   1 
ATOM 3766 C CB  . PHE B 1 55  ? 17.996 101.107 163.018 1.00 38.96  ? 55  PHE B CB  1 
ATOM 3767 C CG  . PHE B 1 55  ? 16.921 100.367 162.326 1.00 38.09  ? 55  PHE B CG  1 
ATOM 3768 C CD1 . PHE B 1 55  ? 15.965 99.712  163.068 1.00 38.16  ? 55  PHE B CD1 1 
ATOM 3769 C CD2 . PHE B 1 55  ? 16.784 100.413 160.954 1.00 37.53  ? 55  PHE B CD2 1 
ATOM 3770 C CE1 . PHE B 1 55  ? 14.903 99.107  162.458 1.00 37.15  ? 55  PHE B CE1 1 
ATOM 3771 C CE2 . PHE B 1 55  ? 15.711 99.798  160.338 1.00 37.35  ? 55  PHE B CE2 1 
ATOM 3772 C CZ  . PHE B 1 55  ? 14.765 99.156  161.090 1.00 36.74  ? 55  PHE B CZ  1 
ATOM 3773 N N   . SER B 1 56  ? 19.110 104.030 164.407 1.00 40.06  ? 56  SER B N   1 
ATOM 3774 C CA  . SER B 1 56  ? 20.055 104.657 165.337 1.00 39.94  ? 56  SER B CA  1 
ATOM 3775 C C   . SER B 1 56  ? 19.208 105.530 166.214 1.00 40.09  ? 56  SER B C   1 
ATOM 3776 O O   . SER B 1 56  ? 19.702 106.280 167.049 1.00 39.75  ? 56  SER B O   1 
ATOM 3777 C CB  . SER B 1 56  ? 21.062 105.536 164.604 1.00 40.19  ? 56  SER B CB  1 
ATOM 3778 O OG  . SER B 1 56  ? 21.768 106.361 165.519 1.00 40.68  ? 56  SER B OG  1 
ATOM 3779 N N   . LEU B 1 57  ? 17.909 105.432 165.997 1.00 39.98  ? 57  LEU B N   1 
ATOM 3780 C CA  . LEU B 1 57  ? 16.987 106.207 166.773 1.00 40.17  ? 57  LEU B CA  1 
ATOM 3781 C C   . LEU B 1 57  ? 16.091 105.300 167.575 1.00 41.57  ? 57  LEU B C   1 
ATOM 3782 O O   . LEU B 1 57  ? 15.870 105.531 168.758 1.00 41.38  ? 57  LEU B O   1 
ATOM 3783 C CB  . LEU B 1 57  ? 16.174 107.094 165.847 1.00 39.14  ? 57  LEU B CB  1 
ATOM 3784 C CG  . LEU B 1 57  ? 14.831 107.594 166.370 1.00 39.22  ? 57  LEU B CG  1 
ATOM 3785 C CD1 . LEU B 1 57  ? 14.973 108.327 167.678 1.00 38.86  ? 57  LEU B CD1 1 
ATOM 3786 C CD2 . LEU B 1 57  ? 14.220 108.452 165.291 1.00 38.93  ? 57  LEU B CD2 1 
ATOM 3787 N N   . LEU B 1 58  ? 15.604 104.240 166.950 1.00 43.58  ? 58  LEU B N   1 
ATOM 3788 C CA  . LEU B 1 58  ? 14.697 103.347 167.652 1.00 46.43  ? 58  LEU B CA  1 
ATOM 3789 C C   . LEU B 1 58  ? 15.364 102.188 168.348 1.00 47.82  ? 58  LEU B C   1 
ATOM 3790 O O   . LEU B 1 58  ? 14.848 101.660 169.325 1.00 47.51  ? 58  LEU B O   1 
ATOM 3791 C CB  . LEU B 1 58  ? 13.643 102.808 166.687 1.00 47.68  ? 58  LEU B CB  1 
ATOM 3792 C CG  . LEU B 1 58  ? 12.780 103.832 165.916 1.00 48.06  ? 58  LEU B CG  1 
ATOM 3793 C CD1 . LEU B 1 58  ? 12.054 103.147 164.747 1.00 49.86  ? 58  LEU B CD1 1 
ATOM 3794 C CD2 . LEU B 1 58  ? 11.781 104.464 166.860 1.00 47.26  ? 58  LEU B CD2 1 
ATOM 3795 N N   . PHE B 1 59  ? 16.522 101.797 167.858 1.00 50.31  ? 59  PHE B N   1 
ATOM 3796 C CA  . PHE B 1 59  ? 17.206 100.665 168.446 1.00 52.99  ? 59  PHE B CA  1 
ATOM 3797 C C   . PHE B 1 59  ? 18.015 100.953 169.706 1.00 54.43  ? 59  PHE B C   1 
ATOM 3798 O O   . PHE B 1 59  ? 17.805 100.341 170.769 1.00 55.01  ? 59  PHE B O   1 
ATOM 3799 C CB  . PHE B 1 59  ? 18.121 100.047 167.402 1.00 52.66  ? 59  PHE B CB  1 
ATOM 3800 C CG  . PHE B 1 59  ? 17.856 98.612  167.155 1.00 52.94  ? 59  PHE B CG  1 
ATOM 3801 C CD1 . PHE B 1 59  ? 16.633 98.212  166.652 1.00 53.02  ? 59  PHE B CD1 1 
ATOM 3802 C CD2 . PHE B 1 59  ? 18.822 97.653  167.440 1.00 52.64  ? 59  PHE B CD2 1 
ATOM 3803 C CE1 . PHE B 1 59  ? 16.365 96.874  166.428 1.00 54.22  ? 59  PHE B CE1 1 
ATOM 3804 C CE2 . PHE B 1 59  ? 18.571 96.310  167.223 1.00 53.60  ? 59  PHE B CE2 1 
ATOM 3805 C CZ  . PHE B 1 59  ? 17.334 95.914  166.714 1.00 54.48  ? 59  PHE B CZ  1 
ATOM 3806 N N   . GLN B 1 60  ? 18.943 101.889 169.558 1.00 56.08  ? 60  GLN B N   1 
ATOM 3807 C CA  . GLN B 1 60  ? 19.879 102.284 170.606 1.00 57.28  ? 60  GLN B CA  1 
ATOM 3808 C C   . GLN B 1 60  ? 19.372 102.796 171.937 1.00 56.88  ? 60  GLN B C   1 
ATOM 3809 O O   . GLN B 1 60  ? 20.122 102.756 172.912 1.00 56.89  ? 60  GLN B O   1 
ATOM 3810 C CB  . GLN B 1 60  ? 20.880 103.297 170.028 1.00 59.40  ? 60  GLN B CB  1 
ATOM 3811 C CG  . GLN B 1 60  ? 21.781 104.009 171.056 1.00 60.96  ? 60  GLN B CG  1 
ATOM 3812 C CD  . GLN B 1 60  ? 22.474 105.236 170.447 1.00 63.27  ? 60  GLN B CD  1 
ATOM 3813 O OE1 . GLN B 1 60  ? 23.207 105.957 171.131 1.00 63.79  ? 60  GLN B OE1 1 
ATOM 3814 N NE2 . GLN B 1 60  ? 22.232 105.478 169.148 1.00 64.20  ? 60  GLN B NE2 1 
ATOM 3815 N N   . PRO B 1 61  ? 18.145 103.354 171.989 1.00 56.55  ? 61  PRO B N   1 
ATOM 3816 C CA  . PRO B 1 61  ? 17.710 103.817 173.314 1.00 56.56  ? 61  PRO B CA  1 
ATOM 3817 C C   . PRO B 1 61  ? 17.205 102.643 174.166 1.00 56.39  ? 61  PRO B C   1 
ATOM 3818 O O   . PRO B 1 61  ? 17.348 102.620 175.393 1.00 55.92  ? 61  PRO B O   1 
ATOM 3819 C CB  . PRO B 1 61  ? 16.565 104.777 173.003 1.00 56.67  ? 61  PRO B CB  1 
ATOM 3820 C CG  . PRO B 1 61  ? 16.838 105.245 171.641 1.00 56.02  ? 61  PRO B CG  1 
ATOM 3821 C CD  . PRO B 1 61  ? 17.353 104.010 170.932 1.00 56.11  ? 61  PRO B CD  1 
ATOM 3822 N N   . LEU B 1 62  ? 16.579 101.681 173.501 1.00 56.11  ? 62  LEU B N   1 
ATOM 3823 C CA  . LEU B 1 62  ? 16.059 100.522 174.186 1.00 55.74  ? 62  LEU B CA  1 
ATOM 3824 C C   . LEU B 1 62  ? 17.237 99.627  174.527 1.00 55.88  ? 62  LEU B C   1 
ATOM 3825 O O   . LEU B 1 62  ? 17.224 98.920  175.531 1.00 56.49  ? 62  LEU B O   1 
ATOM 3826 C CB  . LEU B 1 62  ? 15.029 99.829  173.285 1.00 55.25  ? 62  LEU B CB  1 
ATOM 3827 C CG  . LEU B 1 62  ? 15.192 98.400  172.773 1.00 54.39  ? 62  LEU B CG  1 
ATOM 3828 C CD1 . LEU B 1 62  ? 15.156 97.433  173.944 1.00 53.65  ? 62  LEU B CD1 1 
ATOM 3829 C CD2 . LEU B 1 62  ? 14.055 98.089  171.783 1.00 54.44  ? 62  LEU B CD2 1 
ATOM 3830 N N   . PHE B 1 63  ? 18.272 99.700  173.705 1.00 56.46  ? 63  PHE B N   1 
ATOM 3831 C CA  . PHE B 1 63  ? 19.463 98.923  173.907 1.00 57.73  ? 63  PHE B CA  1 
ATOM 3832 C C   . PHE B 1 63  ? 20.259 99.461  175.103 1.00 57.07  ? 63  PHE B C   1 
ATOM 3833 O O   . PHE B 1 63  ? 20.907 98.703  175.816 1.00 56.96  ? 63  PHE B O   1 
ATOM 3834 C CB  . PHE B 1 63  ? 20.271 98.964  172.621 1.00 60.35  ? 63  PHE B CB  1 
ATOM 3835 C CG  . PHE B 1 63  ? 21.634 98.475  172.790 1.00 64.76  ? 63  PHE B CG  1 
ATOM 3836 C CD1 . PHE B 1 63  ? 22.573 99.291  173.364 1.00 66.50  ? 63  PHE B CD1 1 
ATOM 3837 C CD2 . PHE B 1 63  ? 21.990 97.190  172.475 1.00 66.34  ? 63  PHE B CD2 1 
ATOM 3838 C CE1 . PHE B 1 63  ? 23.852 98.838  173.632 1.00 68.37  ? 63  PHE B CE1 1 
ATOM 3839 C CE2 . PHE B 1 63  ? 23.308 96.731  172.753 1.00 68.38  ? 63  PHE B CE2 1 
ATOM 3840 C CZ  . PHE B 1 63  ? 24.216 97.549  173.323 1.00 69.16  ? 63  PHE B CZ  1 
ATOM 3841 N N   . GLY B 1 64  ? 20.178 100.766 175.333 1.00 57.13  ? 64  GLY B N   1 
ATOM 3842 C CA  . GLY B 1 64  ? 20.870 101.365 176.459 1.00 57.60  ? 64  GLY B CA  1 
ATOM 3843 C C   . GLY B 1 64  ? 20.091 101.201 177.757 1.00 58.00  ? 64  GLY B C   1 
ATOM 3844 O O   . GLY B 1 64  ? 20.649 101.266 178.859 1.00 58.38  ? 64  GLY B O   1 
ATOM 3845 N N   . LEU B 1 65  ? 18.787 100.991 177.637 1.00 57.81  ? 65  LEU B N   1 
ATOM 3846 C CA  . LEU B 1 65  ? 17.976 100.804 178.826 1.00 57.48  ? 65  LEU B CA  1 
ATOM 3847 C C   . LEU B 1 65  ? 18.140 99.351  179.254 1.00 56.40  ? 65  LEU B C   1 
ATOM 3848 O O   . LEU B 1 65  ? 18.048 99.023  180.437 1.00 55.33  ? 65  LEU B O   1 
ATOM 3849 C CB  . LEU B 1 65  ? 16.505 101.155 178.538 1.00 58.08  ? 65  LEU B CB  1 
ATOM 3850 C CG  . LEU B 1 65  ? 16.184 102.574 177.984 1.00 58.30  ? 65  LEU B CG  1 
ATOM 3851 C CD1 . LEU B 1 65  ? 14.668 102.710 177.849 1.00 58.01  ? 65  LEU B CD1 1 
ATOM 3852 C CD2 . LEU B 1 65  ? 16.727 103.697 178.883 1.00 57.31  ? 65  LEU B CD2 1 
ATOM 3853 N N   . LEU B 1 66  ? 18.407 98.483  178.286 1.00 56.12  ? 66  LEU B N   1 
ATOM 3854 C CA  . LEU B 1 66  ? 18.614 97.085  178.602 1.00 56.80  ? 66  LEU B CA  1 
ATOM 3855 C C   . LEU B 1 66  ? 19.925 96.999  179.363 1.00 57.04  ? 66  LEU B C   1 
ATOM 3856 O O   . LEU B 1 66  ? 20.059 96.199  180.276 1.00 58.23  ? 66  LEU B O   1 
ATOM 3857 C CB  . LEU B 1 66  ? 18.674 96.217  177.334 1.00 55.71  ? 66  LEU B CB  1 
ATOM 3858 C CG  . LEU B 1 66  ? 17.381 96.029  176.518 1.00 56.34  ? 66  LEU B CG  1 
ATOM 3859 C CD1 . LEU B 1 66  ? 17.651 95.086  175.341 1.00 56.08  ? 66  LEU B CD1 1 
ATOM 3860 C CD2 . LEU B 1 66  ? 16.262 95.473  177.394 1.00 55.47  ? 66  LEU B CD2 1 
ATOM 3861 N N   . SER B 1 67  ? 20.889 97.841  179.021 1.00 57.92  ? 67  SER B N   1 
ATOM 3862 C CA  . SER B 1 67  ? 22.166 97.795  179.724 1.00 58.89  ? 67  SER B CA  1 
ATOM 3863 C C   . SER B 1 67  ? 22.047 97.910  181.238 1.00 59.69  ? 67  SER B C   1 
ATOM 3864 O O   . SER B 1 67  ? 22.866 97.369  181.978 1.00 60.06  ? 67  SER B O   1 
ATOM 3865 C CB  . SER B 1 67  ? 23.079 98.904  179.261 1.00 59.48  ? 67  SER B CB  1 
ATOM 3866 O OG  . SER B 1 67  ? 24.032 99.151  180.283 1.00 59.81  ? 67  SER B OG  1 
ATOM 3867 N N   . ASP B 1 68  ? 21.043 98.643  181.693 1.00 60.11  ? 68  ASP B N   1 
ATOM 3868 C CA  . ASP B 1 68  ? 20.834 98.814  183.113 1.00 59.92  ? 68  ASP B CA  1 
ATOM 3869 C C   . ASP B 1 68  ? 20.223 97.535  183.669 1.00 59.28  ? 68  ASP B C   1 
ATOM 3870 O O   . ASP B 1 68  ? 20.819 96.894  184.529 1.00 58.69  ? 68  ASP B O   1 
ATOM 3871 C CB  . ASP B 1 68  ? 19.924 100.017 183.356 1.00 61.71  ? 68  ASP B CB  1 
ATOM 3872 C CG  . ASP B 1 68  ? 20.233 101.169 182.414 1.00 63.30  ? 68  ASP B CG  1 
ATOM 3873 O OD1 . ASP B 1 68  ? 21.438 101.446 182.187 1.00 64.17  ? 68  ASP B OD1 1 
ATOM 3874 O OD2 . ASP B 1 68  ? 19.275 101.794 181.903 1.00 63.78  ? 68  ASP B OD2 1 
ATOM 3875 N N   . LYS B 1 69  ? 19.051 97.143  183.177 1.00 58.02  ? 69  LYS B N   1 
ATOM 3876 C CA  . LYS B 1 69  ? 18.434 95.917  183.676 1.00 57.28  ? 69  LYS B CA  1 
ATOM 3877 C C   . LYS B 1 69  ? 19.492 94.810  183.705 1.00 56.71  ? 69  LYS B C   1 
ATOM 3878 O O   . LYS B 1 69  ? 19.513 93.957  184.600 1.00 56.58  ? 69  LYS B O   1 
ATOM 3879 C CB  . LYS B 1 69  ? 17.269 95.499  182.777 1.00 57.44  ? 69  LYS B CB  1 
ATOM 3880 C CG  . LYS B 1 69  ? 16.522 94.254  183.276 1.00 59.12  ? 69  LYS B CG  1 
ATOM 3881 C CD  . LYS B 1 69  ? 15.469 93.771  182.264 1.00 59.89  ? 69  LYS B CD  1 
ATOM 3882 C CE  . LYS B 1 69  ? 14.831 92.442  182.688 1.00 60.74  ? 69  LYS B CE  1 
ATOM 3883 N NZ  . LYS B 1 69  ? 13.836 91.914  181.702 1.00 60.21  ? 69  LYS B NZ  1 
ATOM 3884 N N   . LEU B 1 70  ? 20.382 94.848  182.719 1.00 56.39  ? 70  LEU B N   1 
ATOM 3885 C CA  . LEU B 1 70  ? 21.456 93.861  182.594 1.00 56.12  ? 70  LEU B CA  1 
ATOM 3886 C C   . LEU B 1 70  ? 22.558 94.075  183.603 1.00 55.91  ? 70  LEU B C   1 
ATOM 3887 O O   . LEU B 1 70  ? 23.286 93.151  183.918 1.00 56.52  ? 70  LEU B O   1 
ATOM 3888 C CB  . LEU B 1 70  ? 22.119 93.933  181.220 1.00 55.61  ? 70  LEU B CB  1 
ATOM 3889 C CG  . LEU B 1 70  ? 21.353 93.689  179.924 1.00 55.69  ? 70  LEU B CG  1 
ATOM 3890 C CD1 . LEU B 1 70  ? 22.291 93.906  178.748 1.00 55.70  ? 70  LEU B CD1 1 
ATOM 3891 C CD2 . LEU B 1 70  ? 20.770 92.292  179.922 1.00 54.86  ? 70  LEU B CD2 1 
ATOM 3892 N N   . GLY B 1 71  ? 22.713 95.297  184.092 1.00 56.21  ? 71  GLY B N   1 
ATOM 3893 C CA  . GLY B 1 71  ? 23.793 95.535  185.024 1.00 56.90  ? 71  GLY B CA  1 
ATOM 3894 C C   . GLY B 1 71  ? 25.077 95.219  184.283 1.00 57.70  ? 71  GLY B C   1 
ATOM 3895 O O   . GLY B 1 71  ? 25.274 95.656  183.150 1.00 58.28  ? 71  GLY B O   1 
ATOM 3896 N N   . LEU B 1 72  ? 25.953 94.445  184.898 1.00 58.78  ? 72  LEU B N   1 
ATOM 3897 C CA  . LEU B 1 72  ? 27.203 94.116  184.242 1.00 60.60  ? 72  LEU B CA  1 
ATOM 3898 C C   . LEU B 1 72  ? 27.230 92.652  183.749 1.00 61.83  ? 72  LEU B C   1 
ATOM 3899 O O   . LEU B 1 72  ? 28.198 91.921  183.957 1.00 60.99  ? 72  LEU B O   1 
ATOM 3900 C CB  . LEU B 1 72  ? 28.350 94.450  185.206 1.00 59.97  ? 72  LEU B CB  1 
ATOM 3901 C CG  . LEU B 1 72  ? 29.787 93.966  185.018 1.00 59.17  ? 72  LEU B CG  1 
ATOM 3902 C CD1 . LEU B 1 72  ? 30.354 94.534  183.745 1.00 58.40  ? 72  LEU B CD1 1 
ATOM 3903 C CD2 . LEU B 1 72  ? 30.628 94.385  186.220 1.00 59.09  ? 72  LEU B CD2 1 
ATOM 3904 N N   . ARG B 1 73  ? 26.154 92.239  183.078 1.00 64.47  ? 73  ARG B N   1 
ATOM 3905 C CA  . ARG B 1 73  ? 26.043 90.887  182.518 1.00 67.48  ? 73  ARG B CA  1 
ATOM 3906 C C   . ARG B 1 73  ? 26.464 90.949  181.032 1.00 68.02  ? 73  ARG B C   1 
ATOM 3907 O O   . ARG B 1 73  ? 26.058 91.837  180.276 1.00 68.37  ? 73  ARG B O   1 
ATOM 3908 C CB  . ARG B 1 73  ? 24.600 90.367  182.682 1.00 69.03  ? 73  ARG B CB  1 
ATOM 3909 C CG  . ARG B 1 73  ? 24.151 90.268  184.176 1.00 72.23  ? 73  ARG B CG  1 
ATOM 3910 C CD  . ARG B 1 73  ? 22.609 90.136  184.395 1.00 75.03  ? 73  ARG B CD  1 
ATOM 3911 N NE  . ARG B 1 73  ? 22.196 90.445  185.774 1.00 76.70  ? 73  ARG B NE  1 
ATOM 3912 C CZ  . ARG B 1 73  ? 20.933 90.496  186.206 1.00 77.09  ? 73  ARG B CZ  1 
ATOM 3913 N NH1 . ARG B 1 73  ? 19.917 90.255  185.381 1.00 77.35  ? 73  ARG B NH1 1 
ATOM 3914 N NH2 . ARG B 1 73  ? 20.686 90.802  187.475 1.00 77.63  ? 73  ARG B NH2 1 
ATOM 3915 N N   . LYS B 1 74  ? 27.291 90.000  180.624 1.00 68.47  ? 74  LYS B N   1 
ATOM 3916 C CA  . LYS B 1 74  ? 27.825 89.958  179.265 1.00 68.27  ? 74  LYS B CA  1 
ATOM 3917 C C   . LYS B 1 74  ? 26.791 89.701  178.164 1.00 66.96  ? 74  LYS B C   1 
ATOM 3918 O O   . LYS B 1 74  ? 26.931 90.207  177.042 1.00 66.67  ? 74  LYS B O   1 
ATOM 3919 C CB  . LYS B 1 74  ? 28.943 88.891  179.206 1.00 69.60  ? 74  LYS B CB  1 
ATOM 3920 C CG  . LYS B 1 74  ? 30.112 89.107  180.197 1.00 71.20  ? 74  LYS B CG  1 
ATOM 3921 C CD  . LYS B 1 74  ? 29.640 89.092  181.660 1.00 72.66  ? 74  LYS B CD  1 
ATOM 3922 C CE  . LYS B 1 74  ? 30.753 89.445  182.643 1.00 73.88  ? 74  LYS B CE  1 
ATOM 3923 N NZ  . LYS B 1 74  ? 30.243 89.662  184.039 1.00 73.09  ? 74  LYS B NZ  1 
ATOM 3924 N N   . TYR B 1 75  ? 25.754 88.935  178.512 1.00 66.07  ? 75  TYR B N   1 
ATOM 3925 C CA  . TYR B 1 75  ? 24.687 88.523  177.590 1.00 64.62  ? 75  TYR B CA  1 
ATOM 3926 C C   . TYR B 1 75  ? 24.508 89.380  176.330 1.00 62.16  ? 75  TYR B C   1 
ATOM 3927 O O   . TYR B 1 75  ? 24.731 88.920  175.207 1.00 61.77  ? 75  TYR B O   1 
ATOM 3928 C CB  . TYR B 1 75  ? 23.344 88.402  178.351 1.00 67.08  ? 75  TYR B CB  1 
ATOM 3929 C CG  . TYR B 1 75  ? 22.260 87.697  177.560 1.00 69.31  ? 75  TYR B CG  1 
ATOM 3930 C CD1 . TYR B 1 75  ? 22.199 86.296  177.502 1.00 70.72  ? 75  TYR B CD1 1 
ATOM 3931 C CD2 . TYR B 1 75  ? 21.357 88.429  176.790 1.00 70.26  ? 75  TYR B CD2 1 
ATOM 3932 C CE1 . TYR B 1 75  ? 21.269 85.637  176.686 1.00 71.91  ? 75  TYR B CE1 1 
ATOM 3933 C CE2 . TYR B 1 75  ? 20.421 87.790  175.967 1.00 71.87  ? 75  TYR B CE2 1 
ATOM 3934 C CZ  . TYR B 1 75  ? 20.382 86.386  175.916 1.00 72.66  ? 75  TYR B CZ  1 
ATOM 3935 O OH  . TYR B 1 75  ? 19.484 85.730  175.084 1.00 73.07  ? 75  TYR B OH  1 
ATOM 3936 N N   . LEU B 1 76  ? 24.121 90.631  176.524 1.00 58.99  ? 76  LEU B N   1 
ATOM 3937 C CA  . LEU B 1 76  ? 23.908 91.520  175.398 1.00 56.02  ? 76  LEU B CA  1 
ATOM 3938 C C   . LEU B 1 76  ? 25.147 91.722  174.543 1.00 53.69  ? 76  LEU B C   1 
ATOM 3939 O O   . LEU B 1 76  ? 25.102 91.550  173.324 1.00 52.96  ? 76  LEU B O   1 
ATOM 3940 C CB  . LEU B 1 76  ? 23.411 92.868  175.882 1.00 56.02  ? 76  LEU B CB  1 
ATOM 3941 C CG  . LEU B 1 76  ? 23.000 93.826  174.793 1.00 56.14  ? 76  LEU B CG  1 
ATOM 3942 C CD1 . LEU B 1 76  ? 22.036 93.168  173.795 1.00 56.48  ? 76  LEU B CD1 1 
ATOM 3943 C CD2 . LEU B 1 76  ? 22.330 94.995  175.502 1.00 56.37  ? 76  LEU B CD2 1 
ATOM 3944 N N   . LEU B 1 77  ? 26.253 92.082  175.183 1.00 51.46  ? 77  LEU B N   1 
ATOM 3945 C CA  . LEU B 1 77  ? 27.482 92.307  174.457 1.00 50.31  ? 77  LEU B CA  1 
ATOM 3946 C C   . LEU B 1 77  ? 27.772 91.140  173.523 1.00 49.89  ? 77  LEU B C   1 
ATOM 3947 O O   . LEU B 1 77  ? 28.338 91.333  172.452 1.00 50.28  ? 77  LEU B O   1 
ATOM 3948 C CB  . LEU B 1 77  ? 28.647 92.515  175.417 1.00 48.70  ? 77  LEU B CB  1 
ATOM 3949 C CG  . LEU B 1 77  ? 29.888 93.101  174.740 1.00 47.85  ? 77  LEU B CG  1 
ATOM 3950 C CD1 . LEU B 1 77  ? 29.537 94.398  174.053 1.00 46.62  ? 77  LEU B CD1 1 
ATOM 3951 C CD2 . LEU B 1 77  ? 30.956 93.342  175.776 1.00 47.97  ? 77  LEU B CD2 1 
ATOM 3952 N N   . TRP B 1 78  ? 27.392 89.928  173.919 1.00 50.14  ? 78  TRP B N   1 
ATOM 3953 C CA  . TRP B 1 78  ? 27.614 88.787  173.041 1.00 50.36  ? 78  TRP B CA  1 
ATOM 3954 C C   . TRP B 1 78  ? 26.761 88.962  171.789 1.00 49.90  ? 78  TRP B C   1 
ATOM 3955 O O   . TRP B 1 78  ? 27.249 88.808  170.665 1.00 49.20  ? 78  TRP B O   1 
ATOM 3956 C CB  . TRP B 1 78  ? 27.212 87.448  173.682 1.00 51.84  ? 78  TRP B CB  1 
ATOM 3957 C CG  . TRP B 1 78  ? 28.177 86.876  174.687 1.00 53.76  ? 78  TRP B CG  1 
ATOM 3958 C CD1 . TRP B 1 78  ? 28.570 87.463  175.849 1.00 54.73  ? 78  TRP B CD1 1 
ATOM 3959 C CD2 . TRP B 1 78  ? 28.815 85.576  174.661 1.00 54.05  ? 78  TRP B CD2 1 
ATOM 3960 N NE1 . TRP B 1 78  ? 29.407 86.620  176.557 1.00 54.83  ? 78  TRP B NE1 1 
ATOM 3961 C CE2 . TRP B 1 78  ? 29.573 85.459  175.853 1.00 54.35  ? 78  TRP B CE2 1 
ATOM 3962 C CE3 . TRP B 1 78  ? 28.818 84.506  173.761 1.00 53.63  ? 78  TRP B CE3 1 
ATOM 3963 C CZ2 . TRP B 1 78  ? 30.323 84.322  176.161 1.00 53.57  ? 78  TRP B CZ2 1 
ATOM 3964 C CZ3 . TRP B 1 78  ? 29.568 83.373  174.075 1.00 53.52  ? 78  TRP B CZ3 1 
ATOM 3965 C CH2 . TRP B 1 78  ? 30.307 83.294  175.266 1.00 53.36  ? 78  TRP B CH2 1 
ATOM 3966 N N   . ILE B 1 79  ? 25.480 89.273  171.994 1.00 49.21  ? 79  ILE B N   1 
ATOM 3967 C CA  . ILE B 1 79  ? 24.511 89.462  170.907 1.00 48.42  ? 79  ILE B CA  1 
ATOM 3968 C C   . ILE B 1 79  ? 25.135 90.375  169.885 1.00 48.14  ? 79  ILE B C   1 
ATOM 3969 O O   . ILE B 1 79  ? 24.677 90.471  168.748 1.00 47.57  ? 79  ILE B O   1 
ATOM 3970 C CB  . ILE B 1 79  ? 23.181 90.113  171.424 1.00 49.31  ? 79  ILE B CB  1 
ATOM 3971 C CG1 . ILE B 1 79  ? 22.603 89.268  172.569 1.00 49.90  ? 79  ILE B CG1 1 
ATOM 3972 C CG2 . ILE B 1 79  ? 22.144 90.208  170.283 1.00 48.43  ? 79  ILE B CG2 1 
ATOM 3973 C CD1 . ILE B 1 79  ? 21.483 89.942  173.381 1.00 49.58  ? 79  ILE B CD1 1 
ATOM 3974 N N   . ILE B 1 80  ? 26.190 91.055  170.309 1.00 48.26  ? 80  ILE B N   1 
ATOM 3975 C CA  . ILE B 1 80  ? 26.900 91.961  169.431 1.00 48.26  ? 80  ILE B CA  1 
ATOM 3976 C C   . ILE B 1 80  ? 27.951 91.158  168.696 1.00 48.92  ? 80  ILE B C   1 
ATOM 3977 O O   . ILE B 1 80  ? 27.888 91.030  167.478 1.00 48.52  ? 80  ILE B O   1 
ATOM 3978 C CB  . ILE B 1 80  ? 27.596 93.092  170.212 1.00 47.79  ? 80  ILE B CB  1 
ATOM 3979 C CG1 . ILE B 1 80  ? 26.551 93.944  170.929 1.00 48.37  ? 80  ILE B CG1 1 
ATOM 3980 C CG2 . ILE B 1 80  ? 28.396 93.959  169.265 1.00 46.55  ? 80  ILE B CG2 1 
ATOM 3981 C CD1 . ILE B 1 80  ? 27.151 95.000  171.852 1.00 48.94  ? 80  ILE B CD1 1 
ATOM 3982 N N   . THR B 1 81  ? 28.915 90.608  169.422 1.00 49.41  ? 81  THR B N   1 
ATOM 3983 C CA  . THR B 1 81  ? 29.942 89.840  168.751 1.00 50.30  ? 81  THR B CA  1 
ATOM 3984 C C   . THR B 1 81  ? 29.294 88.877  167.781 1.00 52.29  ? 81  THR B C   1 
ATOM 3985 O O   . THR B 1 81  ? 29.805 88.646  166.678 1.00 51.85  ? 81  THR B O   1 
ATOM 3986 C CB  . THR B 1 81  ? 30.800 89.078  169.745 1.00 49.85  ? 81  THR B CB  1 
ATOM 3987 O OG1 . THR B 1 81  ? 31.694 90.002  170.378 1.00 48.42  ? 81  THR B OG1 1 
ATOM 3988 C CG2 . THR B 1 81  ? 31.595 87.984  169.037 1.00 49.86  ? 81  THR B CG2 1 
ATOM 3989 N N   . GLY B 1 82  ? 28.143 88.349  168.185 1.00 54.39  ? 82  GLY B N   1 
ATOM 3990 C CA  . GLY B 1 82  ? 27.424 87.408  167.341 1.00 58.13  ? 82  GLY B CA  1 
ATOM 3991 C C   . GLY B 1 82  ? 27.058 87.938  165.966 1.00 59.85  ? 82  GLY B C   1 
ATOM 3992 O O   . GLY B 1 82  ? 27.444 87.367  164.936 1.00 59.71  ? 82  GLY B O   1 
ATOM 3993 N N   . MET B 1 83  ? 26.308 89.034  165.942 1.00 61.93  ? 83  MET B N   1 
ATOM 3994 C CA  . MET B 1 83  ? 25.904 89.615  164.671 1.00 63.51  ? 83  MET B CA  1 
ATOM 3995 C C   . MET B 1 83  ? 27.084 90.264  163.975 1.00 64.22  ? 83  MET B C   1 
ATOM 3996 O O   . MET B 1 83  ? 27.106 90.369  162.748 1.00 64.34  ? 83  MET B O   1 
ATOM 3997 C CB  . MET B 1 83  ? 24.802 90.649  164.868 1.00 65.15  ? 83  MET B CB  1 
ATOM 3998 C CG  . MET B 1 83  ? 23.458 90.056  165.222 1.00 66.32  ? 83  MET B CG  1 
ATOM 3999 S SD  . MET B 1 83  ? 22.236 91.351  165.369 1.00 69.69  ? 83  MET B SD  1 
ATOM 4000 C CE  . MET B 1 83  ? 22.107 91.807  163.633 1.00 67.78  ? 83  MET B CE  1 
ATOM 4001 N N   . LEU B 1 84  ? 28.065 90.713  164.746 1.00 64.22  ? 84  LEU B N   1 
ATOM 4002 C CA  . LEU B 1 84  ? 29.222 91.329  164.124 1.00 64.38  ? 84  LEU B CA  1 
ATOM 4003 C C   . LEU B 1 84  ? 29.956 90.281  163.312 1.00 64.22  ? 84  LEU B C   1 
ATOM 4004 O O   . LEU B 1 84  ? 30.281 90.502  162.139 1.00 65.10  ? 84  LEU B O   1 
ATOM 4005 C CB  . LEU B 1 84  ? 30.141 91.941  165.177 1.00 64.73  ? 84  LEU B CB  1 
ATOM 4006 C CG  . LEU B 1 84  ? 29.566 93.270  165.699 1.00 65.56  ? 84  LEU B CG  1 
ATOM 4007 C CD1 . LEU B 1 84  ? 30.506 93.869  166.729 1.00 66.92  ? 84  LEU B CD1 1 
ATOM 4008 C CD2 . LEU B 1 84  ? 29.371 94.240  164.549 1.00 64.48  ? 84  LEU B CD2 1 
ATOM 4009 N N   . VAL B 1 85  ? 30.173 89.126  163.926 1.00 63.41  ? 85  VAL B N   1 
ATOM 4010 C CA  . VAL B 1 85  ? 30.868 88.046  163.263 1.00 63.23  ? 85  VAL B CA  1 
ATOM 4011 C C   . VAL B 1 85  ? 30.446 87.687  161.840 1.00 62.34  ? 85  VAL B C   1 
ATOM 4012 O O   . VAL B 1 85  ? 31.311 87.543  160.989 1.00 62.57  ? 85  VAL B O   1 
ATOM 4013 C CB  . VAL B 1 85  ? 30.815 86.790  164.094 1.00 63.69  ? 85  VAL B CB  1 
ATOM 4014 C CG1 . VAL B 1 85  ? 31.478 85.647  163.334 1.00 64.42  ? 85  VAL B CG1 1 
ATOM 4015 C CG2 . VAL B 1 85  ? 31.496 87.063  165.408 1.00 64.27  ? 85  VAL B CG2 1 
ATOM 4016 N N   . MET B 1 86  ? 29.158 87.534  161.547 1.00 61.04  ? 86  MET B N   1 
ATOM 4017 C CA  . MET B 1 86  ? 28.818 87.180  160.166 1.00 59.25  ? 86  MET B CA  1 
ATOM 4018 C C   . MET B 1 86  ? 28.838 88.376  159.187 1.00 57.41  ? 86  MET B C   1 
ATOM 4019 O O   . MET B 1 86  ? 28.149 88.379  158.151 1.00 56.97  ? 86  MET B O   1 
ATOM 4020 C CB  . MET B 1 86  ? 27.474 86.442  160.105 1.00 60.62  ? 86  MET B CB  1 
ATOM 4021 C CG  . MET B 1 86  ? 26.276 87.277  160.477 1.00 62.69  ? 86  MET B CG  1 
ATOM 4022 S SD  . MET B 1 86  ? 24.746 86.309  160.466 1.00 64.47  ? 86  MET B SD  1 
ATOM 4023 C CE  . MET B 1 86  ? 24.621 85.856  162.229 1.00 64.33  ? 86  MET B CE  1 
ATOM 4024 N N   . PHE B 1 87  ? 29.663 89.366  159.538 1.00 54.59  ? 87  PHE B N   1 
ATOM 4025 C CA  . PHE B 1 87  ? 29.853 90.596  158.781 1.00 52.22  ? 87  PHE B CA  1 
ATOM 4026 C C   . PHE B 1 87  ? 29.969 90.317  157.283 1.00 52.37  ? 87  PHE B C   1 
ATOM 4027 O O   . PHE B 1 87  ? 29.165 90.805  156.480 1.00 52.49  ? 87  PHE B O   1 
ATOM 4028 C CB  . PHE B 1 87  ? 31.124 91.310  159.273 1.00 50.19  ? 87  PHE B CB  1 
ATOM 4029 C CG  . PHE B 1 87  ? 31.228 92.750  158.827 1.00 48.52  ? 87  PHE B CG  1 
ATOM 4030 C CD1 . PHE B 1 87  ? 30.114 93.576  158.857 1.00 48.29  ? 87  PHE B CD1 1 
ATOM 4031 C CD2 . PHE B 1 87  ? 32.434 93.282  158.388 1.00 47.82  ? 87  PHE B CD2 1 
ATOM 4032 C CE1 . PHE B 1 87  ? 30.199 94.909  158.455 1.00 48.07  ? 87  PHE B CE1 1 
ATOM 4033 C CE2 . PHE B 1 87  ? 32.527 94.615  157.985 1.00 47.68  ? 87  PHE B CE2 1 
ATOM 4034 C CZ  . PHE B 1 87  ? 31.407 95.426  158.019 1.00 47.63  ? 87  PHE B CZ  1 
ATOM 4035 N N   . ALA B 1 88  ? 30.977 89.526  156.923 1.00 51.64  ? 88  ALA B N   1 
ATOM 4036 C CA  . ALA B 1 88  ? 31.256 89.176  155.530 1.00 50.59  ? 88  ALA B CA  1 
ATOM 4037 C C   . ALA B 1 88  ? 30.095 88.497  154.822 1.00 50.39  ? 88  ALA B C   1 
ATOM 4038 O O   . ALA B 1 88  ? 29.634 88.950  153.774 1.00 50.49  ? 88  ALA B O   1 
ATOM 4039 C CB  . ALA B 1 88  ? 32.490 88.277  155.459 1.00 50.59  ? 88  ALA B CB  1 
ATOM 4040 N N   . PRO B 1 89  ? 29.620 87.381  155.379 1.00 49.86  ? 89  PRO B N   1 
ATOM 4041 C CA  . PRO B 1 89  ? 28.508 86.646  154.776 1.00 50.23  ? 89  PRO B CA  1 
ATOM 4042 C C   . PRO B 1 89  ? 27.305 87.548  154.649 1.00 51.62  ? 89  PRO B C   1 
ATOM 4043 O O   . PRO B 1 89  ? 26.634 87.630  153.614 1.00 51.48  ? 89  PRO B O   1 
ATOM 4044 C CB  . PRO B 1 89  ? 28.250 85.542  155.780 1.00 49.78  ? 89  PRO B CB  1 
ATOM 4045 C CG  . PRO B 1 89  ? 29.567 85.363  156.447 1.00 49.61  ? 89  PRO B CG  1 
ATOM 4046 C CD  . PRO B 1 89  ? 30.070 86.739  156.622 1.00 49.32  ? 89  PRO B CD  1 
ATOM 4047 N N   . PHE B 1 90  ? 27.029 88.211  155.753 1.00 53.44  ? 90  PHE B N   1 
ATOM 4048 C CA  . PHE B 1 90  ? 25.920 89.129  155.829 1.00 55.45  ? 90  PHE B CA  1 
ATOM 4049 C C   . PHE B 1 90  ? 25.992 90.166  154.711 1.00 55.15  ? 90  PHE B C   1 
ATOM 4050 O O   . PHE B 1 90  ? 25.090 90.267  153.875 1.00 54.58  ? 90  PHE B O   1 
ATOM 4051 C CB  . PHE B 1 90  ? 25.987 89.819  157.170 1.00 58.16  ? 90  PHE B CB  1 
ATOM 4052 C CG  . PHE B 1 90  ? 25.076 90.986  157.290 1.00 61.41  ? 90  PHE B CG  1 
ATOM 4053 C CD1 . PHE B 1 90  ? 23.713 90.806  157.396 1.00 61.80  ? 90  PHE B CD1 1 
ATOM 4054 C CD2 . PHE B 1 90  ? 25.571 92.265  157.308 1.00 62.63  ? 90  PHE B CD2 1 
ATOM 4055 C CE1 . PHE B 1 90  ? 22.834 91.875  157.525 1.00 62.82  ? 90  PHE B CE1 1 
ATOM 4056 C CE2 . PHE B 1 90  ? 24.700 93.335  157.439 1.00 63.76  ? 90  PHE B CE2 1 
ATOM 4057 C CZ  . PHE B 1 90  ? 23.316 93.123  157.547 1.00 63.48  ? 90  PHE B CZ  1 
ATOM 4058 N N   . PHE B 1 91  ? 27.083 90.931  154.723 1.00 54.94  ? 91  PHE B N   1 
ATOM 4059 C CA  . PHE B 1 91  ? 27.327 91.982  153.744 1.00 54.22  ? 91  PHE B CA  1 
ATOM 4060 C C   . PHE B 1 91  ? 27.419 91.512  152.295 1.00 54.02  ? 91  PHE B C   1 
ATOM 4061 O O   . PHE B 1 91  ? 26.607 91.916  151.445 1.00 54.00  ? 91  PHE B O   1 
ATOM 4062 C CB  . PHE B 1 91  ? 28.606 92.733  154.091 1.00 53.94  ? 91  PHE B CB  1 
ATOM 4063 C CG  . PHE B 1 91  ? 28.367 94.118  154.575 1.00 53.22  ? 91  PHE B CG  1 
ATOM 4064 C CD1 . PHE B 1 91  ? 27.985 94.350  155.880 1.00 52.64  ? 91  PHE B CD1 1 
ATOM 4065 C CD2 . PHE B 1 91  ? 28.488 95.198  153.709 1.00 53.54  ? 91  PHE B CD2 1 
ATOM 4066 C CE1 . PHE B 1 91  ? 27.724 95.636  156.320 1.00 52.59  ? 91  PHE B CE1 1 
ATOM 4067 C CE2 . PHE B 1 91  ? 28.227 96.493  154.145 1.00 53.11  ? 91  PHE B CE2 1 
ATOM 4068 C CZ  . PHE B 1 91  ? 27.844 96.707  155.455 1.00 52.61  ? 91  PHE B CZ  1 
ATOM 4069 N N   . ILE B 1 92  ? 28.427 90.687  152.016 1.00 53.43  ? 92  ILE B N   1 
ATOM 4070 C CA  . ILE B 1 92  ? 28.635 90.145  150.681 1.00 52.68  ? 92  ILE B CA  1 
ATOM 4071 C C   . ILE B 1 92  ? 27.360 89.546  150.110 1.00 52.94  ? 92  ILE B C   1 
ATOM 4072 O O   . ILE B 1 92  ? 26.925 89.905  149.011 1.00 53.14  ? 92  ILE B O   1 
ATOM 4073 C CB  . ILE B 1 92  ? 29.682 89.010  150.673 1.00 51.92  ? 92  ILE B CB  1 
ATOM 4074 C CG1 . ILE B 1 92  ? 31.083 89.552  150.948 1.00 51.78  ? 92  ILE B CG1 1 
ATOM 4075 C CG2 . ILE B 1 92  ? 29.642 88.307  149.329 1.00 51.97  ? 92  ILE B CG2 1 
ATOM 4076 C CD1 . ILE B 1 92  ? 32.169 88.486  150.839 1.00 51.87  ? 92  ILE B CD1 1 
ATOM 4077 N N   . PHE B 1 93  ? 26.761 88.639  150.874 1.00 53.06  ? 93  PHE B N   1 
ATOM 4078 C CA  . PHE B 1 93  ? 25.564 87.933  150.440 1.00 53.63  ? 93  PHE B CA  1 
ATOM 4079 C C   . PHE B 1 93  ? 24.190 88.571  150.579 1.00 53.55  ? 93  PHE B C   1 
ATOM 4080 O O   . PHE B 1 93  ? 23.357 88.389  149.694 1.00 53.46  ? 93  PHE B O   1 
ATOM 4081 C CB  . PHE B 1 93  ? 25.567 86.557  151.088 1.00 53.62  ? 93  PHE B CB  1 
ATOM 4082 C CG  . PHE B 1 93  ? 26.782 85.760  150.744 1.00 53.91  ? 93  PHE B CG  1 
ATOM 4083 C CD1 . PHE B 1 93  ? 28.025 86.143  151.231 1.00 53.77  ? 93  PHE B CD1 1 
ATOM 4084 C CD2 . PHE B 1 93  ? 26.705 84.684  149.865 1.00 54.12  ? 93  PHE B CD2 1 
ATOM 4085 C CE1 . PHE B 1 93  ? 29.171 85.480  150.847 1.00 54.07  ? 93  PHE B CE1 1 
ATOM 4086 C CE2 . PHE B 1 93  ? 27.850 84.012  149.474 1.00 54.37  ? 93  PHE B CE2 1 
ATOM 4087 C CZ  . PHE B 1 93  ? 29.087 84.411  149.964 1.00 54.36  ? 93  PHE B CZ  1 
ATOM 4088 N N   . ILE B 1 94  ? 23.949 89.314  151.660 1.00 53.10  ? 94  ILE B N   1 
ATOM 4089 C CA  . ILE B 1 94  ? 22.644 89.947  151.851 1.00 52.63  ? 94  ILE B CA  1 
ATOM 4090 C C   . ILE B 1 94  ? 22.462 91.248  151.064 1.00 52.13  ? 94  ILE B C   1 
ATOM 4091 O O   . ILE B 1 94  ? 21.613 91.355  150.155 1.00 50.83  ? 94  ILE B O   1 
ATOM 4092 C CB  . ILE B 1 94  ? 22.412 90.254  153.312 1.00 52.64  ? 94  ILE B CB  1 
ATOM 4093 C CG1 . ILE B 1 94  ? 22.712 89.001  154.119 1.00 51.57  ? 94  ILE B CG1 1 
ATOM 4094 C CG2 . ILE B 1 94  ? 21.007 90.727  153.518 1.00 53.71  ? 94  ILE B CG2 1 
ATOM 4095 C CD1 . ILE B 1 94  ? 22.248 89.089  155.427 1.00 52.19  ? 94  ILE B CD1 1 
ATOM 4096 N N   . PHE B 1 95  ? 23.253 92.250  151.427 1.00 52.72  ? 95  PHE B N   1 
ATOM 4097 C CA  . PHE B 1 95  ? 23.154 93.526  150.738 1.00 54.16  ? 95  PHE B CA  1 
ATOM 4098 C C   . PHE B 1 95  ? 23.280 93.391  149.269 1.00 53.85  ? 95  PHE B C   1 
ATOM 4099 O O   . PHE B 1 95  ? 22.324 93.603  148.541 1.00 52.90  ? 95  PHE B O   1 
ATOM 4100 C CB  . PHE B 1 95  ? 24.235 94.509  151.143 1.00 56.43  ? 95  PHE B CB  1 
ATOM 4101 C CG  . PHE B 1 95  ? 24.068 95.042  152.495 1.00 58.96  ? 95  PHE B CG  1 
ATOM 4102 C CD1 . PHE B 1 95  ? 24.095 94.183  153.554 1.00 58.96  ? 95  PHE B CD1 1 
ATOM 4103 C CD2 . PHE B 1 95  ? 23.891 96.418  152.729 1.00 59.44  ? 95  PHE B CD2 1 
ATOM 4104 C CE1 . PHE B 1 95  ? 23.960 94.663  154.804 1.00 59.38  ? 95  PHE B CE1 1 
ATOM 4105 C CE2 . PHE B 1 95  ? 23.752 96.903  154.025 1.00 59.36  ? 95  PHE B CE2 1 
ATOM 4106 C CZ  . PHE B 1 95  ? 23.788 96.018  155.063 1.00 59.53  ? 95  PHE B CZ  1 
ATOM 4107 N N   . GLY B 1 96  ? 24.498 93.105  148.832 1.00 54.44  ? 96  GLY B N   1 
ATOM 4108 C CA  . GLY B 1 96  ? 24.738 92.974  147.413 1.00 55.41  ? 96  GLY B CA  1 
ATOM 4109 C C   . GLY B 1 96  ? 23.468 92.612  146.675 1.00 57.18  ? 96  GLY B C   1 
ATOM 4110 O O   . GLY B 1 96  ? 22.973 93.397  145.881 1.00 57.57  ? 96  GLY B O   1 
ATOM 4111 N N   . PRO B 1 97  ? 22.906 91.430  146.929 1.00 58.40  ? 97  PRO B N   1 
ATOM 4112 C CA  . PRO B 1 97  ? 21.683 90.906  146.315 1.00 59.60  ? 97  PRO B CA  1 
ATOM 4113 C C   . PRO B 1 97  ? 20.416 91.753  146.452 1.00 61.02  ? 97  PRO B C   1 
ATOM 4114 O O   . PRO B 1 97  ? 19.855 92.226  145.446 1.00 60.89  ? 97  PRO B O   1 
ATOM 4115 C CB  . PRO B 1 97  ? 21.515 89.543  146.985 1.00 59.75  ? 97  PRO B CB  1 
ATOM 4116 C CG  . PRO B 1 97  ? 22.903 89.105  147.191 1.00 58.82  ? 97  PRO B CG  1 
ATOM 4117 C CD  . PRO B 1 97  ? 23.588 90.379  147.691 1.00 58.12  ? 97  PRO B CD  1 
ATOM 4118 N N   . LEU B 1 98  ? 19.940 91.930  147.681 1.00 62.02  ? 98  LEU B N   1 
ATOM 4119 C CA  . LEU B 1 98  ? 18.728 92.701  147.850 1.00 63.19  ? 98  LEU B CA  1 
ATOM 4120 C C   . LEU B 1 98  ? 18.833 93.953  146.976 1.00 65.87  ? 98  LEU B C   1 
ATOM 4121 O O   . LEU B 1 98  ? 17.879 94.346  146.293 1.00 65.46  ? 98  LEU B O   1 
ATOM 4122 C CB  . LEU B 1 98  ? 18.528 93.017  149.329 1.00 61.66  ? 98  LEU B CB  1 
ATOM 4123 C CG  . LEU B 1 98  ? 18.143 91.803  150.167 1.00 60.13  ? 98  LEU B CG  1 
ATOM 4124 C CD1 . LEU B 1 98  ? 17.931 92.189  151.616 1.00 59.77  ? 98  LEU B CD1 1 
ATOM 4125 C CD2 . LEU B 1 98  ? 16.858 91.224  149.596 1.00 59.84  ? 98  LEU B CD2 1 
ATOM 4126 N N   . LEU B 1 99  ? 20.027 94.528  146.950 1.00 70.12  ? 99  LEU B N   1 
ATOM 4127 C CA  . LEU B 1 99  ? 20.294 95.714  146.159 1.00 75.14  ? 99  LEU B CA  1 
ATOM 4128 C C   . LEU B 1 99  ? 20.504 95.397  144.673 1.00 79.05  ? 99  LEU B C   1 
ATOM 4129 O O   . LEU B 1 99  ? 19.643 95.682  143.832 1.00 78.84  ? 99  LEU B O   1 
ATOM 4130 C CB  . LEU B 1 99  ? 21.528 96.413  146.727 1.00 75.06  ? 99  LEU B CB  1 
ATOM 4131 C CG  . LEU B 1 99  ? 21.293 96.885  148.161 1.00 75.83  ? 99  LEU B CG  1 
ATOM 4132 C CD1 . LEU B 1 99  ? 22.572 97.406  148.820 1.00 76.10  ? 99  LEU B CD1 1 
ATOM 4133 C CD2 . LEU B 1 99  ? 20.226 97.960  148.097 1.00 76.15  ? 99  LEU B CD2 1 
ATOM 4134 N N   . GLN B 1 100 ? 21.651 94.790  144.368 1.00 83.77  ? 100 GLN B N   1 
ATOM 4135 C CA  . GLN B 1 100 ? 22.034 94.444  143.000 1.00 88.20  ? 100 GLN B CA  1 
ATOM 4136 C C   . GLN B 1 100 ? 20.970 93.742  142.172 1.00 90.42  ? 100 GLN B C   1 
ATOM 4137 O O   . GLN B 1 100 ? 20.837 94.045  140.976 1.00 91.57  ? 100 GLN B O   1 
ATOM 4138 C CB  . GLN B 1 100 ? 23.309 93.587  142.991 1.00 90.04  ? 100 GLN B CB  1 
ATOM 4139 C CG  . GLN B 1 100 ? 24.611 94.333  143.322 1.00 92.76  ? 100 GLN B CG  1 
ATOM 4140 C CD  . GLN B 1 100 ? 24.555 95.836  143.069 1.00 93.70  ? 100 GLN B CD  1 
ATOM 4141 O OE1 . GLN B 1 100 ? 24.095 96.307  142.013 1.00 93.68  ? 100 GLN B OE1 1 
ATOM 4142 N NE2 . GLN B 1 100 ? 25.038 96.597  144.041 1.00 94.65  ? 100 GLN B NE2 1 
ATOM 4143 N N   . TYR B 1 101 ? 20.231 92.811  142.791 1.00 91.66  ? 101 TYR B N   1 
ATOM 4144 C CA  . TYR B 1 101 ? 19.171 92.065  142.101 1.00 92.22  ? 101 TYR B CA  1 
ATOM 4145 C C   . TYR B 1 101 ? 18.062 93.091  141.778 1.00 91.16  ? 101 TYR B C   1 
ATOM 4146 O O   . TYR B 1 101 ? 17.042 92.776  141.124 1.00 91.97  ? 101 TYR B O   1 
ATOM 4147 C CB  . TYR B 1 101 ? 18.657 90.934  142.998 1.00 95.52  ? 101 TYR B CB  1 
ATOM 4148 C CG  . TYR B 1 101 ? 17.979 89.807  142.246 1.00 99.09  ? 101 TYR B CG  1 
ATOM 4149 C CD1 . TYR B 1 101 ? 18.710 88.920  141.447 1.00 100.73 ? 101 TYR B CD1 1 
ATOM 4150 C CD2 . TYR B 1 101 ? 16.591 89.647  142.312 1.00 100.74 ? 101 TYR B CD2 1 
ATOM 4151 C CE1 . TYR B 1 101 ? 18.059 87.898  140.728 1.00 102.60 ? 101 TYR B CE1 1 
ATOM 4152 C CE2 . TYR B 1 101 ? 15.935 88.636  141.601 1.00 101.74 ? 101 TYR B CE2 1 
ATOM 4153 C CZ  . TYR B 1 101 ? 16.667 87.767  140.810 1.00 102.54 ? 101 TYR B CZ  1 
ATOM 4154 O OH  . TYR B 1 101 ? 16.001 86.797  140.081 1.00 103.19 ? 101 TYR B OH  1 
ATOM 4155 N N   . ASN B 1 102 ? 18.317 94.325  142.238 1.00 87.66  ? 102 ASN B N   1 
ATOM 4156 C CA  . ASN B 1 102 ? 17.464 95.472  141.990 1.00 83.18  ? 102 ASN B CA  1 
ATOM 4157 C C   . ASN B 1 102 ? 16.242 95.556  142.917 1.00 79.73  ? 102 ASN B C   1 
ATOM 4158 O O   . ASN B 1 102 ? 15.117 95.476  142.435 1.00 79.68  ? 102 ASN B O   1 
ATOM 4159 C CB  . ASN B 1 102 ? 17.009 95.457  140.501 1.00 84.25  ? 102 ASN B CB  1 
ATOM 4160 C CG  . ASN B 1 102 ? 18.193 95.473  139.496 1.00 84.56  ? 102 ASN B CG  1 
ATOM 4161 O OD1 . ASN B 1 102 ? 18.089 94.947  138.378 1.00 84.42  ? 102 ASN B OD1 1 
ATOM 4162 N ND2 . ASN B 1 102 ? 19.306 96.097  139.893 1.00 84.27  ? 102 ASN B ND2 1 
ATOM 4163 N N   . ILE B 1 103 ? 16.445 95.703  144.229 1.00 75.01  ? 103 ILE B N   1 
ATOM 4164 C CA  . ILE B 1 103 ? 15.322 95.844  145.180 1.00 69.55  ? 103 ILE B CA  1 
ATOM 4165 C C   . ILE B 1 103 ? 15.777 96.595  146.442 1.00 66.49  ? 103 ILE B C   1 
ATOM 4166 O O   . ILE B 1 103 ? 15.687 96.090  147.568 1.00 65.71  ? 103 ILE B O   1 
ATOM 4167 C CB  . ILE B 1 103 ? 14.755 94.487  145.646 1.00 69.66  ? 103 ILE B CB  1 
ATOM 4168 C CG1 . ILE B 1 103 ? 14.538 93.551  144.459 1.00 69.13  ? 103 ILE B CG1 1 
ATOM 4169 C CG2 . ILE B 1 103 ? 13.437 94.728  146.406 1.00 69.36  ? 103 ILE B CG2 1 
ATOM 4170 C CD1 . ILE B 1 103 ? 13.921 92.247  144.872 1.00 69.80  ? 103 ILE B CD1 1 
ATOM 4171 N N   . LEU B 1 104 ? 16.243 97.816  146.234 1.00 61.79  ? 104 LEU B N   1 
ATOM 4172 C CA  . LEU B 1 104 ? 16.767 98.671  147.287 1.00 57.22  ? 104 LEU B CA  1 
ATOM 4173 C C   . LEU B 1 104 ? 16.051 98.810  148.636 1.00 54.92  ? 104 LEU B C   1 
ATOM 4174 O O   . LEU B 1 104 ? 16.607 98.440  149.669 1.00 53.89  ? 104 LEU B O   1 
ATOM 4175 C CB  . LEU B 1 104 ? 16.987 100.059 146.710 1.00 56.54  ? 104 LEU B CB  1 
ATOM 4176 C CG  . LEU B 1 104 ? 17.671 100.966 147.706 1.00 55.34  ? 104 LEU B CG  1 
ATOM 4177 C CD1 . LEU B 1 104 ? 19.170 100.856 147.575 1.00 54.69  ? 104 LEU B CD1 1 
ATOM 4178 C CD2 . LEU B 1 104 ? 17.202 102.360 147.465 1.00 55.80  ? 104 LEU B CD2 1 
ATOM 4179 N N   . VAL B 1 105 ? 14.836 99.351  148.638 1.00 53.09  ? 105 VAL B N   1 
ATOM 4180 C CA  . VAL B 1 105 ? 14.134 99.566  149.895 1.00 50.82  ? 105 VAL B CA  1 
ATOM 4181 C C   . VAL B 1 105 ? 14.259 98.438  150.894 1.00 50.76  ? 105 VAL B C   1 
ATOM 4182 O O   . VAL B 1 105 ? 14.383 98.701  152.084 1.00 51.22  ? 105 VAL B O   1 
ATOM 4183 C CB  . VAL B 1 105 ? 12.634 99.850  149.714 1.00 50.11  ? 105 VAL B CB  1 
ATOM 4184 C CG1 . VAL B 1 105 ? 12.093 100.480 150.984 1.00 48.44  ? 105 VAL B CG1 1 
ATOM 4185 C CG2 . VAL B 1 105 ? 12.399 100.771 148.546 1.00 49.90  ? 105 VAL B CG2 1 
ATOM 4186 N N   . GLY B 1 106 ? 14.224 97.191  150.431 1.00 49.59  ? 106 GLY B N   1 
ATOM 4187 C CA  . GLY B 1 106 ? 14.331 96.073  151.356 1.00 48.68  ? 106 GLY B CA  1 
ATOM 4188 C C   . GLY B 1 106 ? 15.707 95.929  151.986 1.00 48.70  ? 106 GLY B C   1 
ATOM 4189 O O   . GLY B 1 106 ? 15.863 95.925  153.214 1.00 48.70  ? 106 GLY B O   1 
ATOM 4190 N N   . SER B 1 107 ? 16.716 95.815  151.132 1.00 48.19  ? 107 SER B N   1 
ATOM 4191 C CA  . SER B 1 107 ? 18.096 95.658  151.582 1.00 46.88  ? 107 SER B CA  1 
ATOM 4192 C C   . SER B 1 107 ? 18.395 96.645  152.691 1.00 45.04  ? 107 SER B C   1 
ATOM 4193 O O   . SER B 1 107 ? 18.973 96.298  153.711 1.00 44.39  ? 107 SER B O   1 
ATOM 4194 C CB  . SER B 1 107 ? 19.055 95.894  150.416 1.00 47.56  ? 107 SER B CB  1 
ATOM 4195 O OG  . SER B 1 107 ? 20.219 95.078  150.507 1.00 47.35  ? 107 SER B OG  1 
ATOM 4196 N N   . ILE B 1 108 ? 17.993 97.885  152.481 1.00 42.92  ? 108 ILE B N   1 
ATOM 4197 C CA  . ILE B 1 108 ? 18.224 98.905  153.470 1.00 40.90  ? 108 ILE B CA  1 
ATOM 4198 C C   . ILE B 1 108 ? 17.544 98.479  154.752 1.00 39.04  ? 108 ILE B C   1 
ATOM 4199 O O   . ILE B 1 108 ? 18.153 97.856  155.603 1.00 37.69  ? 108 ILE B O   1 
ATOM 4200 C CB  . ILE B 1 108 ? 17.656 100.233 152.988 1.00 41.28  ? 108 ILE B CB  1 
ATOM 4201 C CG1 . ILE B 1 108 ? 18.047 100.436 151.526 1.00 42.06  ? 108 ILE B CG1 1 
ATOM 4202 C CG2 . ILE B 1 108 ? 18.200 101.355 153.819 1.00 42.11  ? 108 ILE B CG2 1 
ATOM 4203 C CD1 . ILE B 1 108 ? 17.829 101.823 151.018 1.00 43.74  ? 108 ILE B CD1 1 
ATOM 4204 N N   . VAL B 1 109 ? 16.268 98.795  154.872 1.00 37.94  ? 109 VAL B N   1 
ATOM 4205 C CA  . VAL B 1 109 ? 15.538 98.450  156.068 1.00 37.58  ? 109 VAL B CA  1 
ATOM 4206 C C   . VAL B 1 109 ? 16.037 97.132  156.636 1.00 38.16  ? 109 VAL B C   1 
ATOM 4207 O O   . VAL B 1 109 ? 16.500 97.071  157.769 1.00 37.63  ? 109 VAL B O   1 
ATOM 4208 C CB  . VAL B 1 109 ? 14.038 98.343  155.777 1.00 37.51  ? 109 VAL B CB  1 
ATOM 4209 C CG1 . VAL B 1 109 ? 13.270 98.155  157.058 1.00 37.22  ? 109 VAL B CG1 1 
ATOM 4210 C CG2 . VAL B 1 109 ? 13.575 99.584  155.058 1.00 36.29  ? 109 VAL B CG2 1 
ATOM 4211 N N   . GLY B 1 110 ? 15.968 96.081  155.834 1.00 38.83  ? 110 GLY B N   1 
ATOM 4212 C CA  . GLY B 1 110 ? 16.411 94.785  156.305 1.00 40.38  ? 110 GLY B CA  1 
ATOM 4213 C C   . GLY B 1 110 ? 17.897 94.744  156.565 1.00 40.73  ? 110 GLY B C   1 
ATOM 4214 O O   . GLY B 1 110 ? 18.377 93.944  157.361 1.00 41.27  ? 110 GLY B O   1 
ATOM 4215 N N   . GLY B 1 111 ? 18.624 95.631  155.910 1.00 41.56  ? 111 GLY B N   1 
ATOM 4216 C CA  . GLY B 1 111 ? 20.060 95.638  156.068 1.00 43.93  ? 111 GLY B CA  1 
ATOM 4217 C C   . GLY B 1 111 ? 20.622 96.430  157.220 1.00 45.28  ? 111 GLY B C   1 
ATOM 4218 O O   . GLY B 1 111 ? 21.783 96.260  157.600 1.00 44.48  ? 111 GLY B O   1 
ATOM 4219 N N   . ILE B 1 112 ? 19.809 97.280  157.816 1.00 46.64  ? 112 ILE B N   1 
ATOM 4220 C CA  . ILE B 1 112 ? 20.331 98.084  158.896 1.00 47.96  ? 112 ILE B CA  1 
ATOM 4221 C C   . ILE B 1 112 ? 20.160 97.503  160.283 1.00 49.16  ? 112 ILE B C   1 
ATOM 4222 O O   . ILE B 1 112 ? 19.784 98.207  161.220 1.00 48.64  ? 112 ILE B O   1 
ATOM 4223 C CB  . ILE B 1 112 ? 19.723 99.455  158.866 1.00 48.21  ? 112 ILE B CB  1 
ATOM 4224 C CG1 . ILE B 1 112 ? 19.684 99.936  157.417 1.00 48.38  ? 112 ILE B CG1 1 
ATOM 4225 C CG2 . ILE B 1 112 ? 20.553 100.379 159.712 1.00 48.05  ? 112 ILE B CG2 1 
ATOM 4226 C CD1 . ILE B 1 112 ? 18.885 101.141 157.219 1.00 48.46  ? 112 ILE B CD1 1 
ATOM 4227 N N   . TYR B 1 113 ? 20.430 96.210  160.405 1.00 51.52  ? 113 TYR B N   1 
ATOM 4228 C CA  . TYR B 1 113 ? 20.361 95.530  161.687 1.00 54.05  ? 113 TYR B CA  1 
ATOM 4229 C C   . TYR B 1 113 ? 21.755 95.042  162.058 1.00 54.95  ? 113 TYR B C   1 
ATOM 4230 O O   . TYR B 1 113 ? 22.288 95.424  163.103 1.00 54.49  ? 113 TYR B O   1 
ATOM 4231 C CB  . TYR B 1 113 ? 19.346 94.397  161.633 1.00 56.61  ? 113 TYR B CB  1 
ATOM 4232 C CG  . TYR B 1 113 ? 17.971 94.914  161.912 1.00 59.19  ? 113 TYR B CG  1 
ATOM 4233 C CD1 . TYR B 1 113 ? 17.421 95.937  161.148 1.00 59.85  ? 113 TYR B CD1 1 
ATOM 4234 C CD2 . TYR B 1 113 ? 17.233 94.409  162.972 1.00 61.94  ? 113 TYR B CD2 1 
ATOM 4235 C CE1 . TYR B 1 113 ? 16.167 96.434  161.430 1.00 61.51  ? 113 TYR B CE1 1 
ATOM 4236 C CE2 . TYR B 1 113 ? 15.973 94.902  163.273 1.00 63.81  ? 113 TYR B CE2 1 
ATOM 4237 C CZ  . TYR B 1 113 ? 15.437 95.913  162.501 1.00 63.62  ? 113 TYR B CZ  1 
ATOM 4238 O OH  . TYR B 1 113 ? 14.159 96.353  162.800 1.00 64.90  ? 113 TYR B OH  1 
ATOM 4239 N N   . LEU B 1 114 ? 22.370 94.217  161.214 1.00 55.22  ? 114 LEU B N   1 
ATOM 4240 C CA  . LEU B 1 114 ? 23.736 93.797  161.513 1.00 55.40  ? 114 LEU B CA  1 
ATOM 4241 C C   . LEU B 1 114 ? 24.454 95.138  161.368 1.00 56.40  ? 114 LEU B C   1 
ATOM 4242 O O   . LEU B 1 114 ? 25.576 95.321  161.854 1.00 56.46  ? 114 LEU B O   1 
ATOM 4243 C CB  . LEU B 1 114 ? 24.262 92.781  160.488 1.00 54.17  ? 114 LEU B CB  1 
ATOM 4244 C CG  . LEU B 1 114 ? 25.668 92.236  160.790 1.00 53.68  ? 114 LEU B CG  1 
ATOM 4245 C CD1 . LEU B 1 114 ? 25.807 90.818  160.317 1.00 53.78  ? 114 LEU B CD1 1 
ATOM 4246 C CD2 . LEU B 1 114 ? 26.721 93.121  160.159 1.00 53.49  ? 114 LEU B CD2 1 
ATOM 4247 N N   . GLY B 1 115 ? 23.749 96.082  160.725 1.00 57.12  ? 115 GLY B N   1 
ATOM 4248 C CA  . GLY B 1 115 ? 24.251 97.437  160.496 1.00 57.12  ? 115 GLY B CA  1 
ATOM 4249 C C   . GLY B 1 115 ? 24.087 98.356  161.698 1.00 57.08  ? 115 GLY B C   1 
ATOM 4250 O O   . GLY B 1 115 ? 24.609 99.475  161.709 1.00 57.02  ? 115 GLY B O   1 
ATOM 4251 N N   . PHE B 1 116 ? 23.373 97.875  162.716 1.00 56.74  ? 116 PHE B N   1 
ATOM 4252 C CA  . PHE B 1 116 ? 23.140 98.639  163.945 1.00 55.51  ? 116 PHE B CA  1 
ATOM 4253 C C   . PHE B 1 116 ? 24.306 98.431  164.891 1.00 55.35  ? 116 PHE B C   1 
ATOM 4254 O O   . PHE B 1 116 ? 24.684 99.332  165.639 1.00 55.05  ? 116 PHE B O   1 
ATOM 4255 C CB  . PHE B 1 116 ? 21.897 98.133  164.646 1.00 54.84  ? 116 PHE B CB  1 
ATOM 4256 C CG  . PHE B 1 116 ? 22.180 97.254  165.835 1.00 54.68  ? 116 PHE B CG  1 
ATOM 4257 C CD1 . PHE B 1 116 ? 22.555 97.813  167.051 1.00 55.38  ? 116 PHE B CD1 1 
ATOM 4258 C CD2 . PHE B 1 116 ? 22.032 95.873  165.753 1.00 54.93  ? 116 PHE B CD2 1 
ATOM 4259 C CE1 . PHE B 1 116 ? 22.771 97.019  168.171 1.00 56.39  ? 116 PHE B CE1 1 
ATOM 4260 C CE2 . PHE B 1 116 ? 22.246 95.069  166.869 1.00 55.62  ? 116 PHE B CE2 1 
ATOM 4261 C CZ  . PHE B 1 116 ? 22.614 95.641  168.081 1.00 56.09  ? 116 PHE B CZ  1 
ATOM 4262 N N   . CYS B 1 117 ? 24.809 97.196  164.894 1.00 55.23  ? 117 CYS B N   1 
ATOM 4263 C CA  . CYS B 1 117 ? 25.927 96.768  165.731 1.00 54.71  ? 117 CYS B CA  1 
ATOM 4264 C C   . CYS B 1 117 ? 27.095 97.730  165.725 1.00 55.16  ? 117 CYS B C   1 
ATOM 4265 O O   . CYS B 1 117 ? 28.109 97.432  166.348 1.00 55.12  ? 117 CYS B O   1 
ATOM 4266 C CB  . CYS B 1 117 ? 26.422 95.403  165.264 1.00 53.51  ? 117 CYS B CB  1 
ATOM 4267 S SG  . CYS B 1 117 ? 25.089 94.138  165.340 1.00 51.20  ? 117 CYS B SG  1 
ATOM 4268 N N   . PHE B 1 118 ? 26.977 98.855  165.014 1.00 54.92  ? 118 PHE B N   1 
ATOM 4269 C CA  . PHE B 1 118 ? 28.062 99.819  164.958 1.00 54.25  ? 118 PHE B CA  1 
ATOM 4270 C C   . PHE B 1 118 ? 27.687 101.231 165.343 1.00 53.10  ? 118 PHE B C   1 
ATOM 4271 O O   . PHE B 1 118 ? 28.523 102.135 165.327 1.00 53.73  ? 118 PHE B O   1 
ATOM 4272 C CB  . PHE B 1 118 ? 28.737 99.772  163.580 1.00 54.22  ? 118 PHE B CB  1 
ATOM 4273 C CG  . PHE B 1 118 ? 29.840 98.758  163.510 1.00 54.22  ? 118 PHE B CG  1 
ATOM 4274 C CD1 . PHE B 1 118 ? 30.611 98.493  164.644 1.00 54.79  ? 118 PHE B CD1 1 
ATOM 4275 C CD2 . PHE B 1 118 ? 30.067 98.026  162.365 1.00 54.99  ? 118 PHE B CD2 1 
ATOM 4276 C CE1 . PHE B 1 118 ? 31.577 97.504  164.647 1.00 55.52  ? 118 PHE B CE1 1 
ATOM 4277 C CE2 . PHE B 1 118 ? 31.040 97.024  162.353 1.00 56.30  ? 118 PHE B CE2 1 
ATOM 4278 C CZ  . PHE B 1 118 ? 31.794 96.768  163.505 1.00 56.43  ? 118 PHE B CZ  1 
ATOM 4279 N N   . ASN B 1 119 ? 26.431 101.432 165.698 1.00 51.52  ? 119 ASN B N   1 
ATOM 4280 C CA  . ASN B 1 119 ? 26.046 102.746 166.144 1.00 50.37  ? 119 ASN B CA  1 
ATOM 4281 C C   . ASN B 1 119 ? 25.700 102.630 167.628 1.00 49.42  ? 119 ASN B C   1 
ATOM 4282 O O   . ASN B 1 119 ? 26.182 103.409 168.453 1.00 49.46  ? 119 ASN B O   1 
ATOM 4283 C CB  . ASN B 1 119 ? 24.869 103.288 165.341 1.00 50.82  ? 119 ASN B CB  1 
ATOM 4284 C CG  . ASN B 1 119 ? 24.714 104.791 165.509 1.00 52.48  ? 119 ASN B CG  1 
ATOM 4285 O OD1 . ASN B 1 119 ? 25.153 105.364 166.517 1.00 53.60  ? 119 ASN B OD1 1 
ATOM 4286 N ND2 . ASN B 1 119 ? 24.091 105.438 164.533 1.00 52.50  ? 119 ASN B ND2 1 
ATOM 4287 N N   . ALA B 1 120 ? 24.886 101.640 167.975 1.00 47.74  ? 120 ALA B N   1 
ATOM 4288 C CA  . ALA B 1 120 ? 24.522 101.445 169.371 1.00 45.69  ? 120 ALA B CA  1 
ATOM 4289 C C   . ALA B 1 120 ? 25.733 100.844 170.053 1.00 44.04  ? 120 ALA B C   1 
ATOM 4290 O O   . ALA B 1 120 ? 26.251 101.386 171.033 1.00 43.72  ? 120 ALA B O   1 
ATOM 4291 C CB  . ALA B 1 120 ? 23.343 100.492 169.477 1.00 45.72  ? 120 ALA B CB  1 
ATOM 4292 N N   . GLY B 1 121 ? 26.170 99.721  169.495 1.00 42.32  ? 121 GLY B N   1 
ATOM 4293 C CA  . GLY B 1 121 ? 27.307 99.011  170.021 1.00 41.05  ? 121 GLY B CA  1 
ATOM 4294 C C   . GLY B 1 121 ? 28.391 99.945  170.481 1.00 39.77  ? 121 GLY B C   1 
ATOM 4295 O O   . GLY B 1 121 ? 29.006 99.745  171.525 1.00 39.59  ? 121 GLY B O   1 
ATOM 4296 N N   . ALA B 1 122 ? 28.637 100.983 169.704 1.00 38.46  ? 122 ALA B N   1 
ATOM 4297 C CA  . ALA B 1 122 ? 29.668 101.912 170.104 1.00 36.90  ? 122 ALA B CA  1 
ATOM 4298 C C   . ALA B 1 122 ? 29.371 102.372 171.527 1.00 35.93  ? 122 ALA B C   1 
ATOM 4299 O O   . ALA B 1 122 ? 30.074 101.986 172.448 1.00 35.36  ? 122 ALA B O   1 
ATOM 4300 C CB  . ALA B 1 122 ? 29.724 103.068 169.153 1.00 37.66  ? 122 ALA B CB  1 
ATOM 4301 N N   . PRO B 1 123 ? 28.327 103.195 171.734 1.00 35.15  ? 123 PRO B N   1 
ATOM 4302 C CA  . PRO B 1 123 ? 28.085 103.594 173.119 1.00 34.75  ? 123 PRO B CA  1 
ATOM 4303 C C   . PRO B 1 123 ? 27.948 102.393 173.997 1.00 35.07  ? 123 PRO B C   1 
ATOM 4304 O O   . PRO B 1 123 ? 28.139 102.464 175.208 1.00 35.38  ? 123 PRO B O   1 
ATOM 4305 C CB  . PRO B 1 123 ? 26.809 104.430 173.040 1.00 34.45  ? 123 PRO B CB  1 
ATOM 4306 C CG  . PRO B 1 123 ? 26.291 104.229 171.638 1.00 34.42  ? 123 PRO B CG  1 
ATOM 4307 C CD  . PRO B 1 123 ? 27.527 104.026 170.826 1.00 35.46  ? 123 PRO B CD  1 
ATOM 4308 N N   . ALA B 1 124 ? 27.608 101.281 173.365 1.00 36.06  ? 124 ALA B N   1 
ATOM 4309 C CA  . ALA B 1 124 ? 27.504 100.009 174.061 1.00 36.60  ? 124 ALA B CA  1 
ATOM 4310 C C   . ALA B 1 124 ? 28.904 99.579  174.581 1.00 36.96  ? 124 ALA B C   1 
ATOM 4311 O O   . ALA B 1 124 ? 29.173 99.832  175.736 1.00 37.06  ? 124 ALA B O   1 
ATOM 4312 C CB  . ALA B 1 124 ? 26.905 98.993  173.129 1.00 36.13  ? 124 ALA B CB  1 
ATOM 4313 N N   . VAL B 1 125 ? 29.778 98.970  173.765 1.00 37.70  ? 125 VAL B N   1 
ATOM 4314 C CA  . VAL B 1 125 ? 31.150 98.579  174.196 1.00 40.36  ? 125 VAL B CA  1 
ATOM 4315 C C   . VAL B 1 125 ? 31.756 99.731  174.982 1.00 42.22  ? 125 VAL B C   1 
ATOM 4316 O O   . VAL B 1 125 ? 32.280 99.551  176.086 1.00 42.49  ? 125 VAL B O   1 
ATOM 4317 C CB  . VAL B 1 125 ? 32.068 98.316  172.950 1.00 40.83  ? 125 VAL B CB  1 
ATOM 4318 C CG1 . VAL B 1 125 ? 33.549 98.010  173.309 1.00 40.71  ? 125 VAL B CG1 1 
ATOM 4319 C CG2 . VAL B 1 125 ? 31.448 97.204  172.139 1.00 41.16  ? 125 VAL B CG2 1 
ATOM 4320 N N   . GLU B 1 126 ? 31.644 100.929 174.410 1.00 44.23  ? 126 GLU B N   1 
ATOM 4321 C CA  . GLU B 1 126 ? 32.134 102.147 175.060 1.00 46.11  ? 126 GLU B CA  1 
ATOM 4322 C C   . GLU B 1 126 ? 31.597 102.126 176.498 1.00 46.31  ? 126 GLU B C   1 
ATOM 4323 O O   . GLU B 1 126 ? 32.314 102.443 177.451 1.00 47.36  ? 126 GLU B O   1 
ATOM 4324 C CB  . GLU B 1 126 ? 31.615 103.414 174.340 1.00 46.31  ? 126 GLU B CB  1 
ATOM 4325 C CG  . GLU B 1 126 ? 32.321 103.752 173.008 1.00 48.35  ? 126 GLU B CG  1 
ATOM 4326 C CD  . GLU B 1 126 ? 32.081 105.199 172.542 1.00 49.72  ? 126 GLU B CD  1 
ATOM 4327 O OE1 . GLU B 1 126 ? 30.906 105.580 172.315 1.00 50.04  ? 126 GLU B OE1 1 
ATOM 4328 O OE2 . GLU B 1 126 ? 33.079 105.957 172.409 1.00 51.17  ? 126 GLU B OE2 1 
ATOM 4329 N N   . ALA B 1 127 ? 30.350 101.701 176.653 1.00 46.19  ? 127 ALA B N   1 
ATOM 4330 C CA  . ALA B 1 127 ? 29.754 101.662 177.968 1.00 45.76  ? 127 ALA B CA  1 
ATOM 4331 C C   . ALA B 1 127 ? 30.261 100.502 178.809 1.00 45.46  ? 127 ALA B C   1 
ATOM 4332 O O   . ALA B 1 127 ? 31.151 100.659 179.656 1.00 44.60  ? 127 ALA B O   1 
ATOM 4333 C CB  . ALA B 1 127 ? 28.254 101.555 177.842 1.00 46.14  ? 127 ALA B CB  1 
ATOM 4334 N N   . PHE B 1 128 ? 29.677 99.334  178.571 1.00 45.07  ? 128 PHE B N   1 
ATOM 4335 C CA  . PHE B 1 128 ? 30.036 98.182  179.351 1.00 44.22  ? 128 PHE B CA  1 
ATOM 4336 C C   . PHE B 1 128 ? 31.432 98.230  179.873 1.00 43.90  ? 128 PHE B C   1 
ATOM 4337 O O   . PHE B 1 128 ? 31.663 98.200  181.069 1.00 43.17  ? 128 PHE B O   1 
ATOM 4338 C CB  . PHE B 1 128 ? 29.887 96.937  178.545 1.00 43.99  ? 128 PHE B CB  1 
ATOM 4339 C CG  . PHE B 1 128 ? 30.149 95.704  179.318 1.00 44.87  ? 128 PHE B CG  1 
ATOM 4340 C CD1 . PHE B 1 128 ? 31.434 95.379  179.742 1.00 44.60  ? 128 PHE B CD1 1 
ATOM 4341 C CD2 . PHE B 1 128 ? 29.121 94.809  179.542 1.00 44.88  ? 128 PHE B CD2 1 
ATOM 4342 C CE1 . PHE B 1 128 ? 31.676 94.173  180.361 1.00 44.91  ? 128 PHE B CE1 1 
ATOM 4343 C CE2 . PHE B 1 128 ? 29.359 93.602  180.160 1.00 44.77  ? 128 PHE B CE2 1 
ATOM 4344 C CZ  . PHE B 1 128 ? 30.634 93.280  180.567 1.00 44.97  ? 128 PHE B CZ  1 
ATOM 4345 N N   . ILE B 1 129 ? 32.372 98.260  178.951 1.00 44.65  ? 129 ILE B N   1 
ATOM 4346 C CA  . ILE B 1 129 ? 33.768 98.291  179.319 1.00 46.39  ? 129 ILE B CA  1 
ATOM 4347 C C   . ILE B 1 129 ? 34.011 99.334  180.399 1.00 47.31  ? 129 ILE B C   1 
ATOM 4348 O O   . ILE B 1 129 ? 34.739 99.103  181.365 1.00 47.31  ? 129 ILE B O   1 
ATOM 4349 C CB  . ILE B 1 129 ? 34.624 98.583  178.091 1.00 46.68  ? 129 ILE B CB  1 
ATOM 4350 C CG1 . ILE B 1 129 ? 34.262 97.577  176.995 1.00 47.62  ? 129 ILE B CG1 1 
ATOM 4351 C CG2 . ILE B 1 129 ? 36.087 98.486  178.443 1.00 46.05  ? 129 ILE B CG2 1 
ATOM 4352 C CD1 . ILE B 1 129 ? 35.396 97.214  176.056 1.00 49.26  ? 129 ILE B CD1 1 
ATOM 4353 N N   . GLU B 1 130 ? 33.383 100.486 180.237 1.00 48.65  ? 130 GLU B N   1 
ATOM 4354 C CA  . GLU B 1 130 ? 33.529 101.544 181.215 1.00 50.31  ? 130 GLU B CA  1 
ATOM 4355 C C   . GLU B 1 130 ? 33.200 101.001 182.585 1.00 50.45  ? 130 GLU B C   1 
ATOM 4356 O O   . GLU B 1 130 ? 33.969 101.183 183.526 1.00 50.08  ? 130 GLU B O   1 
ATOM 4357 C CB  . GLU B 1 130 ? 32.606 102.709 180.886 1.00 52.01  ? 130 GLU B CB  1 
ATOM 4358 C CG  . GLU B 1 130 ? 32.491 103.777 181.979 1.00 54.84  ? 130 GLU B CG  1 
ATOM 4359 C CD  . GLU B 1 130 ? 32.012 105.123 181.424 1.00 57.28  ? 130 GLU B CD  1 
ATOM 4360 O OE1 . GLU B 1 130 ? 31.542 105.164 180.256 1.00 58.75  ? 130 GLU B OE1 1 
ATOM 4361 O OE2 . GLU B 1 130 ? 32.103 106.145 182.152 1.00 57.86  ? 130 GLU B OE2 1 
ATOM 4362 N N   . LYS B 1 131 ? 32.062 100.326 182.702 1.00 51.08  ? 131 LYS B N   1 
ATOM 4363 C CA  . LYS B 1 131 ? 31.684 99.770  183.992 1.00 51.68  ? 131 LYS B CA  1 
ATOM 4364 C C   . LYS B 1 131 ? 32.780 98.825  184.469 1.00 50.65  ? 131 LYS B C   1 
ATOM 4365 O O   . LYS B 1 131 ? 33.083 98.778  185.649 1.00 50.23  ? 131 LYS B O   1 
ATOM 4366 C CB  . LYS B 1 131 ? 30.313 99.054  183.930 1.00 52.77  ? 131 LYS B CB  1 
ATOM 4367 C CG  . LYS B 1 131 ? 29.111 100.011 184.121 1.00 54.03  ? 131 LYS B CG  1 
ATOM 4368 C CD  . LYS B 1 131 ? 27.738 99.330  184.025 1.00 55.21  ? 131 LYS B CD  1 
ATOM 4369 C CE  . LYS B 1 131 ? 26.659 100.415 183.835 1.00 55.83  ? 131 LYS B CE  1 
ATOM 4370 N NZ  . LYS B 1 131 ? 25.272 99.894  183.592 1.00 55.24  ? 131 LYS B NZ  1 
ATOM 4371 N N   . VAL B 1 132 ? 33.415 98.099  183.564 1.00 50.36  ? 132 VAL B N   1 
ATOM 4372 C CA  . VAL B 1 132 ? 34.464 97.200  184.008 1.00 50.90  ? 132 VAL B CA  1 
ATOM 4373 C C   . VAL B 1 132 ? 35.697 97.991  184.425 1.00 51.02  ? 132 VAL B C   1 
ATOM 4374 O O   . VAL B 1 132 ? 36.572 97.463  185.108 1.00 51.82  ? 132 VAL B O   1 
ATOM 4375 C CB  . VAL B 1 132 ? 34.823 96.174  182.916 1.00 50.69  ? 132 VAL B CB  1 
ATOM 4376 C CG1 . VAL B 1 132 ? 35.571 94.968  183.529 1.00 50.75  ? 132 VAL B CG1 1 
ATOM 4377 C CG2 . VAL B 1 132 ? 33.544 95.729  182.233 1.00 49.99  ? 132 VAL B CG2 1 
ATOM 4378 N N   . SER B 1 133 ? 35.775 99.261  184.054 1.00 51.36  ? 133 SER B N   1 
ATOM 4379 C CA  . SER B 1 133 ? 36.941 100.016 184.476 1.00 52.84  ? 133 SER B CA  1 
ATOM 4380 C C   . SER B 1 133 ? 36.828 100.370 185.958 1.00 54.10  ? 133 SER B C   1 
ATOM 4381 O O   . SER B 1 133 ? 37.839 100.503 186.648 1.00 54.04  ? 133 SER B O   1 
ATOM 4382 C CB  . SER B 1 133 ? 37.107 101.288 183.660 1.00 52.58  ? 133 SER B CB  1 
ATOM 4383 O OG  . SER B 1 133 ? 38.162 102.049 184.217 1.00 52.28  ? 133 SER B OG  1 
ATOM 4384 N N   . ARG B 1 134 ? 35.594 100.517 186.438 1.00 56.23  ? 134 ARG B N   1 
ATOM 4385 C CA  . ARG B 1 134 ? 35.331 100.833 187.847 1.00 57.99  ? 134 ARG B CA  1 
ATOM 4386 C C   . ARG B 1 134 ? 35.510 99.566  188.716 1.00 58.78  ? 134 ARG B C   1 
ATOM 4387 O O   . ARG B 1 134 ? 35.639 99.652  189.947 1.00 59.20  ? 134 ARG B O   1 
ATOM 4388 C CB  . ARG B 1 134 ? 33.895 101.381 188.026 1.00 58.22  ? 134 ARG B CB  1 
ATOM 4389 C CG  . ARG B 1 134 ? 33.696 102.877 187.708 1.00 57.68  ? 134 ARG B CG  1 
ATOM 4390 C CD  . ARG B 1 134 ? 32.211 103.254 187.671 1.00 57.85  ? 134 ARG B CD  1 
ATOM 4391 N NE  . ARG B 1 134 ? 31.986 104.693 187.610 1.00 57.34  ? 134 ARG B NE  1 
ATOM 4392 C CZ  . ARG B 1 134 ? 30.799 105.243 187.390 1.00 57.09  ? 134 ARG B CZ  1 
ATOM 4393 N NH1 . ARG B 1 134 ? 29.743 104.467 187.207 1.00 56.31  ? 134 ARG B NH1 1 
ATOM 4394 N NH2 . ARG B 1 134 ? 30.662 106.561 187.359 1.00 56.58  ? 134 ARG B NH2 1 
ATOM 4395 N N   . ARG B 1 135 ? 35.518 98.397  188.071 1.00 59.48  ? 135 ARG B N   1 
ATOM 4396 C CA  . ARG B 1 135 ? 35.676 97.138  188.793 1.00 60.06  ? 135 ARG B CA  1 
ATOM 4397 C C   . ARG B 1 135 ? 37.133 96.835  189.074 1.00 60.14  ? 135 ARG B C   1 
ATOM 4398 O O   . ARG B 1 135 ? 37.475 96.419  190.169 1.00 60.75  ? 135 ARG B O   1 
ATOM 4399 C CB  . ARG B 1 135 ? 35.073 95.958  188.012 1.00 60.93  ? 135 ARG B CB  1 
ATOM 4400 C CG  . ARG B 1 135 ? 34.597 94.780  188.896 1.00 62.18  ? 135 ARG B CG  1 
ATOM 4401 C CD  . ARG B 1 135 ? 35.730 94.165  189.734 1.00 65.08  ? 135 ARG B CD  1 
ATOM 4402 N NE  . ARG B 1 135 ? 35.317 93.038  190.575 1.00 67.12  ? 135 ARG B NE  1 
ATOM 4403 C CZ  . ARG B 1 135 ? 36.107 92.417  191.463 1.00 68.08  ? 135 ARG B CZ  1 
ATOM 4404 N NH1 . ARG B 1 135 ? 37.364 92.802  191.649 1.00 68.26  ? 135 ARG B NH1 1 
ATOM 4405 N NH2 . ARG B 1 135 ? 35.656 91.383  192.167 1.00 68.19  ? 135 ARG B NH2 1 
ATOM 4406 N N   . SER B 1 136 ? 37.996 97.064  188.099 1.00 59.53  ? 136 SER B N   1 
ATOM 4407 C CA  . SER B 1 136 ? 39.398 96.755  188.275 1.00 59.64  ? 136 SER B CA  1 
ATOM 4408 C C   . SER B 1 136 ? 40.325 97.878  188.682 1.00 59.57  ? 136 SER B C   1 
ATOM 4409 O O   . SER B 1 136 ? 41.354 97.631  189.287 1.00 60.20  ? 136 SER B O   1 
ATOM 4410 C CB  . SER B 1 136 ? 39.937 96.112  187.008 1.00 59.98  ? 136 SER B CB  1 
ATOM 4411 O OG  . SER B 1 136 ? 41.239 96.600  186.731 1.00 60.29  ? 136 SER B OG  1 
ATOM 4412 N N   . ASN B 1 137 ? 39.985 99.101  188.322 1.00 60.06  ? 137 ASN B N   1 
ATOM 4413 C CA  . ASN B 1 137 ? 40.799 100.261 188.660 1.00 60.80  ? 137 ASN B CA  1 
ATOM 4414 C C   . ASN B 1 137 ? 41.239 101.083 187.465 1.00 61.16  ? 137 ASN B C   1 
ATOM 4415 O O   . ASN B 1 137 ? 41.401 102.287 187.622 1.00 61.60  ? 137 ASN B O   1 
ATOM 4416 C CB  . ASN B 1 137 ? 42.051 99.894  189.479 1.00 61.08  ? 137 ASN B CB  1 
ATOM 4417 C CG  . ASN B 1 137 ? 42.859 101.123 189.916 1.00 61.71  ? 137 ASN B CG  1 
ATOM 4418 O OD1 . ASN B 1 137 ? 42.420 102.267 189.773 1.00 62.39  ? 137 ASN B OD1 1 
ATOM 4419 N ND2 . ASN B 1 137 ? 44.044 100.883 190.464 1.00 61.72  ? 137 ASN B ND2 1 
ATOM 4420 N N   . PHE B 1 138 ? 41.461 100.510 186.277 1.00 60.82  ? 138 PHE B N   1 
ATOM 4421 C CA  . PHE B 1 138 ? 41.854 101.472 185.265 1.00 60.20  ? 138 PHE B CA  1 
ATOM 4422 C C   . PHE B 1 138 ? 40.869 102.005 184.299 1.00 59.89  ? 138 PHE B C   1 
ATOM 4423 O O   . PHE B 1 138 ? 40.317 101.303 183.446 1.00 58.63  ? 138 PHE B O   1 
ATOM 4424 C CB  . PHE B 1 138 ? 43.134 101.139 184.512 1.00 60.24  ? 138 PHE B CB  1 
ATOM 4425 C CG  . PHE B 1 138 ? 44.026 102.359 184.327 1.00 59.64  ? 138 PHE B CG  1 
ATOM 4426 C CD1 . PHE B 1 138 ? 43.966 103.412 185.241 1.00 57.94  ? 138 PHE B CD1 1 
ATOM 4427 C CD2 . PHE B 1 138 ? 44.959 102.436 183.302 1.00 59.84  ? 138 PHE B CD2 1 
ATOM 4428 C CE1 . PHE B 1 138 ? 44.816 104.510 185.159 1.00 56.87  ? 138 PHE B CE1 1 
ATOM 4429 C CE2 . PHE B 1 138 ? 45.821 103.546 183.220 1.00 59.13  ? 138 PHE B CE2 1 
ATOM 4430 C CZ  . PHE B 1 138 ? 45.743 104.581 184.152 1.00 57.78  ? 138 PHE B CZ  1 
ATOM 4431 N N   . GLU B 1 139 ? 40.700 103.313 184.479 1.00 61.08  ? 139 GLU B N   1 
ATOM 4432 C CA  . GLU B 1 139 ? 39.802 104.154 183.725 1.00 62.70  ? 139 GLU B CA  1 
ATOM 4433 C C   . GLU B 1 139 ? 39.753 103.860 182.241 1.00 64.20  ? 139 GLU B C   1 
ATOM 4434 O O   . GLU B 1 139 ? 40.761 103.553 181.585 1.00 63.43  ? 139 GLU B O   1 
ATOM 4435 C CB  . GLU B 1 139 ? 40.137 105.629 183.989 1.00 62.17  ? 139 GLU B CB  1 
ATOM 4436 C CG  . GLU B 1 139 ? 41.617 105.969 183.995 1.00 61.32  ? 139 GLU B CG  1 
ATOM 4437 C CD  . GLU B 1 139 ? 41.862 107.433 184.301 1.00 61.48  ? 139 GLU B CD  1 
ATOM 4438 O OE1 . GLU B 1 139 ? 41.257 107.959 185.272 1.00 61.01  ? 139 GLU B OE1 1 
ATOM 4439 O OE2 . GLU B 1 139 ? 42.667 108.056 183.570 1.00 61.07  ? 139 GLU B OE2 1 
ATOM 4440 N N   . PHE B 1 140 ? 38.547 103.936 181.709 1.00 65.73  ? 140 PHE B N   1 
ATOM 4441 C CA  . PHE B 1 140 ? 38.369 103.689 180.302 1.00 67.93  ? 140 PHE B CA  1 
ATOM 4442 C C   . PHE B 1 140 ? 39.183 104.776 179.608 1.00 69.19  ? 140 PHE B C   1 
ATOM 4443 O O   . PHE B 1 140 ? 39.494 104.669 178.421 1.00 70.18  ? 140 PHE B O   1 
ATOM 4444 C CB  . PHE B 1 140 ? 36.893 103.799 179.969 1.00 68.10  ? 140 PHE B CB  1 
ATOM 4445 C CG  . PHE B 1 140 ? 36.340 105.173 180.102 1.00 69.09  ? 140 PHE B CG  1 
ATOM 4446 C CD1 . PHE B 1 140 ? 35.923 105.649 181.340 1.00 70.09  ? 140 PHE B CD1 1 
ATOM 4447 C CD2 . PHE B 1 140 ? 36.211 105.987 178.979 1.00 69.44  ? 140 PHE B CD2 1 
ATOM 4448 C CE1 . PHE B 1 140 ? 35.378 106.932 181.461 1.00 71.61  ? 140 PHE B CE1 1 
ATOM 4449 C CE2 . PHE B 1 140 ? 35.672 107.266 179.081 1.00 70.42  ? 140 PHE B CE2 1 
ATOM 4450 C CZ  . PHE B 1 140 ? 35.252 107.744 180.324 1.00 71.32  ? 140 PHE B CZ  1 
ATOM 4451 N N   . GLY B 1 141 ? 39.537 105.811 180.379 1.00 70.79  ? 141 GLY B N   1 
ATOM 4452 C CA  . GLY B 1 141 ? 40.308 106.926 179.858 1.00 72.55  ? 141 GLY B CA  1 
ATOM 4453 C C   . GLY B 1 141 ? 41.450 106.455 178.991 1.00 74.06  ? 141 GLY B C   1 
ATOM 4454 O O   . GLY B 1 141 ? 41.667 106.972 177.898 1.00 74.14  ? 141 GLY B O   1 
ATOM 4455 N N   . ARG B 1 142 ? 42.177 105.453 179.466 1.00 75.03  ? 142 ARG B N   1 
ATOM 4456 C CA  . ARG B 1 142 ? 43.301 104.947 178.702 1.00 75.90  ? 142 ARG B CA  1 
ATOM 4457 C C   . ARG B 1 142 ? 42.860 103.778 177.842 1.00 75.24  ? 142 ARG B C   1 
ATOM 4458 O O   . ARG B 1 142 ? 43.518 103.446 176.862 1.00 75.29  ? 142 ARG B O   1 
ATOM 4459 C CB  . ARG B 1 142 ? 44.447 104.564 179.646 1.00 77.62  ? 142 ARG B CB  1 
ATOM 4460 C CG  . ARG B 1 142 ? 44.738 105.691 180.670 1.00 79.70  ? 142 ARG B CG  1 
ATOM 4461 C CD  . ARG B 1 142 ? 46.206 106.134 180.732 1.00 80.80  ? 142 ARG B CD  1 
ATOM 4462 N NE  . ARG B 1 142 ? 46.359 107.411 181.439 1.00 82.51  ? 142 ARG B NE  1 
ATOM 4463 C CZ  . ARG B 1 142 ? 47.497 107.845 181.981 1.00 83.04  ? 142 ARG B CZ  1 
ATOM 4464 N NH1 . ARG B 1 142 ? 48.598 107.100 181.905 1.00 83.95  ? 142 ARG B NH1 1 
ATOM 4465 N NH2 . ARG B 1 142 ? 47.538 109.026 182.600 1.00 83.07  ? 142 ARG B NH2 1 
ATOM 4466 N N   . ALA B 1 143 ? 41.736 103.167 178.192 1.00 74.97  ? 143 ALA B N   1 
ATOM 4467 C CA  . ALA B 1 143 ? 41.216 102.058 177.404 1.00 75.46  ? 143 ALA B CA  1 
ATOM 4468 C C   . ALA B 1 143 ? 40.852 102.561 176.017 1.00 76.31  ? 143 ALA B C   1 
ATOM 4469 O O   . ALA B 1 143 ? 41.146 101.904 175.020 1.00 75.12  ? 143 ALA B O   1 
ATOM 4470 C CB  . ALA B 1 143 ? 39.989 101.485 178.058 1.00 75.48  ? 143 ALA B CB  1 
ATOM 4471 N N   . ARG B 1 144 ? 40.199 103.726 175.969 1.00 77.67  ? 144 ARG B N   1 
ATOM 4472 C CA  . ARG B 1 144 ? 39.779 104.350 174.707 1.00 78.67  ? 144 ARG B CA  1 
ATOM 4473 C C   . ARG B 1 144 ? 41.017 104.713 173.908 1.00 77.96  ? 144 ARG B C   1 
ATOM 4474 O O   . ARG B 1 144 ? 41.098 104.434 172.707 1.00 78.25  ? 144 ARG B O   1 
ATOM 4475 C CB  . ARG B 1 144 ? 38.932 105.619 174.976 1.00 80.89  ? 144 ARG B CB  1 
ATOM 4476 C CG  . ARG B 1 144 ? 38.823 106.643 173.805 1.00 83.21  ? 144 ARG B CG  1 
ATOM 4477 C CD  . ARG B 1 144 ? 37.817 106.250 172.692 1.00 84.82  ? 144 ARG B CD  1 
ATOM 4478 N NE  . ARG B 1 144 ? 37.875 107.163 171.539 1.00 86.62  ? 144 ARG B NE  1 
ATOM 4479 C CZ  . ARG B 1 144 ? 37.196 106.989 170.401 1.00 87.01  ? 144 ARG B CZ  1 
ATOM 4480 N NH1 . ARG B 1 144 ? 36.400 105.932 170.270 1.00 87.35  ? 144 ARG B NH1 1 
ATOM 4481 N NH2 . ARG B 1 144 ? 37.322 107.852 169.384 1.00 87.63  ? 144 ARG B NH2 1 
ATOM 4482 N N   . MET B 1 145 ? 41.981 105.335 174.582 1.00 77.11  ? 145 MET B N   1 
ATOM 4483 C CA  . MET B 1 145 ? 43.218 105.729 173.929 1.00 75.87  ? 145 MET B CA  1 
ATOM 4484 C C   . MET B 1 145 ? 43.897 104.478 173.389 1.00 73.99  ? 145 MET B C   1 
ATOM 4485 O O   . MET B 1 145 ? 44.605 104.534 172.381 1.00 74.02  ? 145 MET B O   1 
ATOM 4486 C CB  . MET B 1 145 ? 44.122 106.463 174.911 1.00 76.97  ? 145 MET B CB  1 
ATOM 4487 C CG  . MET B 1 145 ? 43.438 107.657 175.552 1.00 77.70  ? 145 MET B CG  1 
ATOM 4488 S SD  . MET B 1 145 ? 44.622 108.669 176.473 1.00 79.90  ? 145 MET B SD  1 
ATOM 4489 C CE  . MET B 1 145 ? 44.401 110.320 175.579 1.00 78.28  ? 145 MET B CE  1 
ATOM 4490 N N   . PHE B 1 146 ? 43.677 103.343 174.049 1.00 71.66  ? 146 PHE B N   1 
ATOM 4491 C CA  . PHE B 1 146 ? 44.258 102.112 173.550 1.00 68.99  ? 146 PHE B CA  1 
ATOM 4492 C C   . PHE B 1 146 ? 43.370 101.558 172.454 1.00 66.34  ? 146 PHE B C   1 
ATOM 4493 O O   . PHE B 1 146 ? 43.850 101.004 171.451 1.00 66.69  ? 146 PHE B O   1 
ATOM 4494 C CB  . PHE B 1 146 ? 44.362 101.061 174.620 1.00 69.15  ? 146 PHE B CB  1 
ATOM 4495 C CG  . PHE B 1 146 ? 45.175 99.915  174.189 1.00 70.40  ? 146 PHE B CG  1 
ATOM 4496 C CD1 . PHE B 1 146 ? 46.556 100.059 174.076 1.00 70.57  ? 146 PHE B CD1 1 
ATOM 4497 C CD2 . PHE B 1 146 ? 44.573 98.723  173.794 1.00 70.76  ? 146 PHE B CD2 1 
ATOM 4498 C CE1 . PHE B 1 146 ? 47.331 99.038  173.578 1.00 71.18  ? 146 PHE B CE1 1 
ATOM 4499 C CE2 . PHE B 1 146 ? 45.338 97.684  173.291 1.00 71.23  ? 146 PHE B CE2 1 
ATOM 4500 C CZ  . PHE B 1 146 ? 46.726 97.843  173.179 1.00 71.50  ? 146 PHE B CZ  1 
ATOM 4501 N N   . GLY B 1 147 ? 42.068 101.682 172.688 1.00 63.21  ? 147 GLY B N   1 
ATOM 4502 C CA  . GLY B 1 147 ? 41.098 101.232 171.727 1.00 59.60  ? 147 GLY B CA  1 
ATOM 4503 C C   . GLY B 1 147 ? 41.143 102.029 170.447 1.00 57.44  ? 147 GLY B C   1 
ATOM 4504 O O   . GLY B 1 147 ? 40.882 101.455 169.424 1.00 57.01  ? 147 GLY B O   1 
ATOM 4505 N N   . CYS B 1 148 ? 41.485 103.315 170.465 1.00 55.67  ? 148 CYS B N   1 
ATOM 4506 C CA  . CYS B 1 148 ? 41.505 104.079 169.211 1.00 53.90  ? 148 CYS B CA  1 
ATOM 4507 C C   . CYS B 1 148 ? 42.581 103.713 168.169 1.00 52.09  ? 148 CYS B C   1 
ATOM 4508 O O   . CYS B 1 148 ? 42.525 104.130 167.004 1.00 50.94  ? 148 CYS B O   1 
ATOM 4509 C CB  . CYS B 1 148 ? 41.616 105.573 169.475 1.00 54.09  ? 148 CYS B CB  1 
ATOM 4510 S SG  . CYS B 1 148 ? 41.662 106.454 167.880 1.00 57.25  ? 148 CYS B SG  1 
ATOM 4511 N N   . VAL B 1 149 ? 43.576 102.950 168.584 1.00 50.68  ? 149 VAL B N   1 
ATOM 4512 C CA  . VAL B 1 149 ? 44.636 102.529 167.675 1.00 49.30  ? 149 VAL B CA  1 
ATOM 4513 C C   . VAL B 1 149 ? 44.030 101.766 166.490 1.00 48.63  ? 149 VAL B C   1 
ATOM 4514 O O   . VAL B 1 149 ? 44.223 102.129 165.326 1.00 47.95  ? 149 VAL B O   1 
ATOM 4515 C CB  . VAL B 1 149 ? 45.623 101.610 168.424 1.00 49.49  ? 149 VAL B CB  1 
ATOM 4516 C CG1 . VAL B 1 149 ? 46.587 100.959 167.454 1.00 49.31  ? 149 VAL B CG1 1 
ATOM 4517 C CG2 . VAL B 1 149 ? 46.359 102.408 169.462 1.00 48.50  ? 149 VAL B CG2 1 
ATOM 4518 N N   . GLY B 1 150 ? 43.299 100.699 166.822 1.00 48.14  ? 150 GLY B N   1 
ATOM 4519 C CA  . GLY B 1 150 ? 42.634 99.847  165.841 1.00 47.23  ? 150 GLY B CA  1 
ATOM 4520 C C   . GLY B 1 150 ? 41.943 100.621 164.746 1.00 47.00  ? 150 GLY B C   1 
ATOM 4521 O O   . GLY B 1 150 ? 42.034 100.269 163.574 1.00 45.79  ? 150 GLY B O   1 
ATOM 4522 N N   . TRP B 1 151 ? 41.240 101.671 165.150 1.00 47.64  ? 151 TRP B N   1 
ATOM 4523 C CA  . TRP B 1 151 ? 40.541 102.570 164.242 1.00 48.66  ? 151 TRP B CA  1 
ATOM 4524 C C   . TRP B 1 151 ? 41.613 103.069 163.300 1.00 48.36  ? 151 TRP B C   1 
ATOM 4525 O O   . TRP B 1 151 ? 41.537 102.894 162.091 1.00 48.28  ? 151 TRP B O   1 
ATOM 4526 C CB  . TRP B 1 151 ? 39.964 103.733 165.065 1.00 50.84  ? 151 TRP B CB  1 
ATOM 4527 C CG  . TRP B 1 151 ? 39.383 104.911 164.311 1.00 53.97  ? 151 TRP B CG  1 
ATOM 4528 C CD1 . TRP B 1 151 ? 39.920 106.162 164.205 1.00 54.97  ? 151 TRP B CD1 1 
ATOM 4529 C CD2 . TRP B 1 151 ? 38.157 104.935 163.565 1.00 55.31  ? 151 TRP B CD2 1 
ATOM 4530 N NE1 . TRP B 1 151 ? 39.111 106.963 163.427 1.00 56.08  ? 151 TRP B NE1 1 
ATOM 4531 C CE2 . TRP B 1 151 ? 38.037 106.233 163.010 1.00 56.28  ? 151 TRP B CE2 1 
ATOM 4532 C CE3 . TRP B 1 151 ? 37.176 103.974 163.291 1.00 54.95  ? 151 TRP B CE3 1 
ATOM 4533 C CZ2 . TRP B 1 151 ? 36.937 106.602 162.218 1.00 56.94  ? 151 TRP B CZ2 1 
ATOM 4534 C CZ3 . TRP B 1 151 ? 36.089 104.343 162.506 1.00 55.93  ? 151 TRP B CZ3 1 
ATOM 4535 C CH2 . TRP B 1 151 ? 35.986 105.645 161.964 1.00 56.99  ? 151 TRP B CH2 1 
ATOM 4536 N N   . ALA B 1 152 ? 42.645 103.667 163.871 1.00 48.55  ? 152 ALA B N   1 
ATOM 4537 C CA  . ALA B 1 152 ? 43.716 104.205 163.049 1.00 48.40  ? 152 ALA B CA  1 
ATOM 4538 C C   . ALA B 1 152 ? 44.315 103.165 162.096 1.00 48.20  ? 152 ALA B C   1 
ATOM 4539 O O   . ALA B 1 152 ? 44.391 103.380 160.893 1.00 47.08  ? 152 ALA B O   1 
ATOM 4540 C CB  . ALA B 1 152 ? 44.800 104.803 163.952 1.00 49.18  ? 152 ALA B CB  1 
ATOM 4541 N N   . LEU B 1 153 ? 44.715 102.028 162.649 1.00 48.61  ? 153 LEU B N   1 
ATOM 4542 C CA  . LEU B 1 153 ? 45.329 100.963 161.873 1.00 48.81  ? 153 LEU B CA  1 
ATOM 4543 C C   . LEU B 1 153 ? 44.457 100.408 160.726 1.00 47.95  ? 153 LEU B C   1 
ATOM 4544 O O   . LEU B 1 153 ? 44.871 100.419 159.560 1.00 48.01  ? 153 LEU B O   1 
ATOM 4545 C CB  . LEU B 1 153 ? 45.744 99.848  162.836 1.00 49.39  ? 153 LEU B CB  1 
ATOM 4546 C CG  . LEU B 1 153 ? 46.752 98.823  162.303 1.00 49.70  ? 153 LEU B CG  1 
ATOM 4547 C CD1 . LEU B 1 153 ? 48.029 99.556  161.881 1.00 49.70  ? 153 LEU B CD1 1 
ATOM 4548 C CD2 . LEU B 1 153 ? 47.052 97.767  163.373 1.00 49.39  ? 153 LEU B CD2 1 
ATOM 4549 N N   . GLY B 1 154 ? 43.261 99.936  161.066 1.00 46.93  ? 154 GLY B N   1 
ATOM 4550 C CA  . GLY B 1 154 ? 42.358 99.384  160.071 1.00 47.32  ? 154 GLY B CA  1 
ATOM 4551 C C   . GLY B 1 154 ? 42.188 100.259 158.844 1.00 47.30  ? 154 GLY B C   1 
ATOM 4552 O O   . GLY B 1 154 ? 42.505 99.863  157.717 1.00 46.94  ? 154 GLY B O   1 
ATOM 4553 N N   . ALA B 1 155 ? 41.667 101.457 159.074 1.00 47.20  ? 155 ALA B N   1 
ATOM 4554 C CA  . ALA B 1 155 ? 41.463 102.420 158.010 1.00 47.62  ? 155 ALA B CA  1 
ATOM 4555 C C   . ALA B 1 155 ? 42.590 102.289 156.985 1.00 48.48  ? 155 ALA B C   1 
ATOM 4556 O O   . ALA B 1 155 ? 42.356 101.927 155.835 1.00 48.00  ? 155 ALA B O   1 
ATOM 4557 C CB  . ALA B 1 155 ? 41.447 103.821 158.585 1.00 47.01  ? 155 ALA B CB  1 
ATOM 4558 N N   . SER B 1 156 ? 43.818 102.566 157.410 1.00 50.16  ? 156 SER B N   1 
ATOM 4559 C CA  . SER B 1 156 ? 44.952 102.497 156.500 1.00 51.35  ? 156 SER B CA  1 
ATOM 4560 C C   . SER B 1 156 ? 44.972 101.175 155.760 1.00 51.92  ? 156 SER B C   1 
ATOM 4561 O O   . SER B 1 156 ? 45.157 101.138 154.545 1.00 51.80  ? 156 SER B O   1 
ATOM 4562 C CB  . SER B 1 156 ? 46.271 102.706 157.250 1.00 52.04  ? 156 SER B CB  1 
ATOM 4563 O OG  . SER B 1 156 ? 46.377 104.052 157.699 1.00 53.85  ? 156 SER B OG  1 
ATOM 4564 N N   . ILE B 1 157 ? 44.761 100.085 156.475 1.00 52.20  ? 157 ILE B N   1 
ATOM 4565 C CA  . ILE B 1 157 ? 44.768 98.803  155.818 1.00 53.31  ? 157 ILE B CA  1 
ATOM 4566 C C   . ILE B 1 157 ? 43.597 98.650  154.866 1.00 53.92  ? 157 ILE B C   1 
ATOM 4567 O O   . ILE B 1 157 ? 43.733 98.024  153.815 1.00 54.30  ? 157 ILE B O   1 
ATOM 4568 C CB  . ILE B 1 157 ? 44.777 97.695  156.840 1.00 54.04  ? 157 ILE B CB  1 
ATOM 4569 C CG1 . ILE B 1 157 ? 46.127 97.755  157.566 1.00 55.27  ? 157 ILE B CG1 1 
ATOM 4570 C CG2 . ILE B 1 157 ? 44.492 96.349  156.176 1.00 53.76  ? 157 ILE B CG2 1 
ATOM 4571 C CD1 . ILE B 1 157 ? 46.458 96.552  158.410 1.00 56.71  ? 157 ILE B CD1 1 
ATOM 4572 N N   . VAL B 1 158 ? 42.452 99.228  155.218 1.00 54.64  ? 158 VAL B N   1 
ATOM 4573 C CA  . VAL B 1 158 ? 41.266 99.171  154.352 1.00 55.15  ? 158 VAL B CA  1 
ATOM 4574 C C   . VAL B 1 158 ? 41.562 99.690  152.944 1.00 54.98  ? 158 VAL B C   1 
ATOM 4575 O O   . VAL B 1 158 ? 41.519 98.930  151.975 1.00 54.78  ? 158 VAL B O   1 
ATOM 4576 C CB  . VAL B 1 158 ? 40.094 99.998  154.944 1.00 55.75  ? 158 VAL B CB  1 
ATOM 4577 C CG1 . VAL B 1 158 ? 38.986 100.226 153.876 1.00 55.21  ? 158 VAL B CG1 1 
ATOM 4578 C CG2 . VAL B 1 158 ? 39.530 99.253  156.143 1.00 56.64  ? 158 VAL B CG2 1 
ATOM 4579 N N   . GLY B 1 159 ? 41.839 100.990 152.836 1.00 54.65  ? 159 GLY B N   1 
ATOM 4580 C CA  . GLY B 1 159 ? 42.144 101.573 151.540 1.00 53.79  ? 159 GLY B CA  1 
ATOM 4581 C C   . GLY B 1 159 ? 42.960 100.628 150.681 1.00 53.07  ? 159 GLY B C   1 
ATOM 4582 O O   . GLY B 1 159 ? 42.497 100.167 149.641 1.00 52.43  ? 159 GLY B O   1 
ATOM 4583 N N   . ILE B 1 160 ? 44.176 100.334 151.122 1.00 52.33  ? 160 ILE B N   1 
ATOM 4584 C CA  . ILE B 1 160 ? 45.053 99.433  150.397 1.00 51.42  ? 160 ILE B CA  1 
ATOM 4585 C C   . ILE B 1 160 ? 44.295 98.154  150.066 1.00 50.99  ? 160 ILE B C   1 
ATOM 4586 O O   . ILE B 1 160 ? 43.765 97.986  148.970 1.00 50.41  ? 160 ILE B O   1 
ATOM 4587 C CB  . ILE B 1 160 ? 46.316 99.138  151.252 1.00 51.13  ? 160 ILE B CB  1 
ATOM 4588 C CG1 . ILE B 1 160 ? 47.049 100.468 151.474 1.00 50.82  ? 160 ILE B CG1 1 
ATOM 4589 C CG2 . ILE B 1 160 ? 47.217 98.071  150.581 1.00 51.39  ? 160 ILE B CG2 1 
ATOM 4590 C CD1 . ILE B 1 160 ? 48.319 100.388 152.278 1.00 51.40  ? 160 ILE B CD1 1 
ATOM 4591 N N   . MET B 1 161 ? 44.222 97.269  151.040 1.00 51.38  ? 161 MET B N   1 
ATOM 4592 C CA  . MET B 1 161 ? 43.533 96.005  150.879 1.00 52.12  ? 161 MET B CA  1 
ATOM 4593 C C   . MET B 1 161 ? 42.163 96.106  150.222 1.00 52.76  ? 161 MET B C   1 
ATOM 4594 O O   . MET B 1 161 ? 41.752 95.192  149.500 1.00 51.72  ? 161 MET B O   1 
ATOM 4595 C CB  . MET B 1 161 ? 43.367 95.344  152.247 1.00 52.83  ? 161 MET B CB  1 
ATOM 4596 C CG  . MET B 1 161 ? 44.661 95.174  153.017 1.00 53.09  ? 161 MET B CG  1 
ATOM 4597 S SD  . MET B 1 161 ? 45.643 93.747  152.520 1.00 53.62  ? 161 MET B SD  1 
ATOM 4598 C CE  . MET B 1 161 ? 46.685 94.472  151.167 1.00 53.25  ? 161 MET B CE  1 
ATOM 4599 N N   . PHE B 1 162 ? 41.436 97.192  150.466 1.00 53.71  ? 162 PHE B N   1 
ATOM 4600 C CA  . PHE B 1 162 ? 40.105 97.266  149.887 1.00 55.13  ? 162 PHE B CA  1 
ATOM 4601 C C   . PHE B 1 162 ? 40.064 97.110  148.392 1.00 55.71  ? 162 PHE B C   1 
ATOM 4602 O O   . PHE B 1 162 ? 39.510 96.141  147.867 1.00 55.33  ? 162 PHE B O   1 
ATOM 4603 C CB  . PHE B 1 162 ? 39.390 98.568  150.197 1.00 55.11  ? 162 PHE B CB  1 
ATOM 4604 C CG  . PHE B 1 162 ? 38.127 98.738  149.391 1.00 55.98  ? 162 PHE B CG  1 
ATOM 4605 C CD1 . PHE B 1 162 ? 37.005 97.957  149.657 1.00 56.05  ? 162 PHE B CD1 1 
ATOM 4606 C CD2 . PHE B 1 162 ? 38.067 99.656  148.349 1.00 56.68  ? 162 PHE B CD2 1 
ATOM 4607 C CE1 . PHE B 1 162 ? 35.844 98.088  148.908 1.00 56.16  ? 162 PHE B CE1 1 
ATOM 4608 C CE2 . PHE B 1 162 ? 36.908 99.797  147.587 1.00 57.33  ? 162 PHE B CE2 1 
ATOM 4609 C CZ  . PHE B 1 162 ? 35.794 99.013  147.872 1.00 57.03  ? 162 PHE B CZ  1 
ATOM 4610 N N   . THR B 1 163 ? 40.622 98.110  147.719 1.00 57.31  ? 163 THR B N   1 
ATOM 4611 C CA  . THR B 1 163 ? 40.633 98.160  146.268 1.00 59.04  ? 163 THR B CA  1 
ATOM 4612 C C   . THR B 1 163 ? 41.248 96.917  145.655 1.00 60.33  ? 163 THR B C   1 
ATOM 4613 O O   . THR B 1 163 ? 40.927 96.551  144.518 1.00 59.90  ? 163 THR B O   1 
ATOM 4614 C CB  . THR B 1 163 ? 41.437 99.374  145.735 1.00 59.43  ? 163 THR B CB  1 
ATOM 4615 O OG1 . THR B 1 163 ? 41.306 100.479 146.637 1.00 59.85  ? 163 THR B OG1 1 
ATOM 4616 C CG2 . THR B 1 163 ? 40.923 99.775  144.342 1.00 58.60  ? 163 THR B CG2 1 
ATOM 4617 N N   . ILE B 1 164 ? 42.128 96.260  146.406 1.00 61.15  ? 164 ILE B N   1 
ATOM 4618 C CA  . ILE B 1 164 ? 42.803 95.073  145.891 1.00 61.73  ? 164 ILE B CA  1 
ATOM 4619 C C   . ILE B 1 164 ? 41.878 93.880  145.775 1.00 61.59  ? 164 ILE B C   1 
ATOM 4620 O O   . ILE B 1 164 ? 42.042 93.023  144.896 1.00 62.10  ? 164 ILE B O   1 
ATOM 4621 C CB  . ILE B 1 164 ? 44.018 94.701  146.755 1.00 62.19  ? 164 ILE B CB  1 
ATOM 4622 C CG1 . ILE B 1 164 ? 45.026 95.859  146.736 1.00 62.56  ? 164 ILE B CG1 1 
ATOM 4623 C CG2 . ILE B 1 164 ? 44.649 93.404  146.218 1.00 62.42  ? 164 ILE B CG2 1 
ATOM 4624 C CD1 . ILE B 1 164 ? 46.281 95.633  147.563 1.00 62.75  ? 164 ILE B CD1 1 
ATOM 4625 N N   . ASN B 1 165 ? 40.918 93.838  146.688 1.00 61.08  ? 165 ASN B N   1 
ATOM 4626 C CA  . ASN B 1 165 ? 39.916 92.794  146.734 1.00 60.51  ? 165 ASN B CA  1 
ATOM 4627 C C   . ASN B 1 165 ? 39.003 93.090  147.918 1.00 60.41  ? 165 ASN B C   1 
ATOM 4628 O O   . ASN B 1 165 ? 39.238 92.630  149.027 1.00 60.79  ? 165 ASN B O   1 
ATOM 4629 C CB  . ASN B 1 165 ? 40.565 91.418  146.896 1.00 59.62  ? 165 ASN B CB  1 
ATOM 4630 C CG  . ASN B 1 165 ? 39.541 90.311  146.947 1.00 59.44  ? 165 ASN B CG  1 
ATOM 4631 O OD1 . ASN B 1 165 ? 38.328 90.567  146.947 1.00 58.10  ? 165 ASN B OD1 1 
ATOM 4632 N ND2 . ASN B 1 165 ? 40.014 89.075  146.994 1.00 59.99  ? 165 ASN B ND2 1 
ATOM 4633 N N   . ASN B 1 166 ? 37.974 93.888  147.677 1.00 59.84  ? 166 ASN B N   1 
ATOM 4634 C CA  . ASN B 1 166 ? 37.034 94.239  148.727 1.00 59.70  ? 166 ASN B CA  1 
ATOM 4635 C C   . ASN B 1 166 ? 36.519 92.974  149.466 1.00 60.06  ? 166 ASN B C   1 
ATOM 4636 O O   . ASN B 1 166 ? 36.453 92.958  150.704 1.00 60.37  ? 166 ASN B O   1 
ATOM 4637 C CB  . ASN B 1 166 ? 35.869 94.996  148.120 1.00 58.99  ? 166 ASN B CB  1 
ATOM 4638 C CG  . ASN B 1 166 ? 34.959 94.089  147.377 1.00 58.92  ? 166 ASN B CG  1 
ATOM 4639 O OD1 . ASN B 1 166 ? 35.357 92.991  146.984 1.00 58.17  ? 166 ASN B OD1 1 
ATOM 4640 N ND2 . ASN B 1 166 ? 33.732 94.519  147.173 1.00 59.02  ? 166 ASN B ND2 1 
ATOM 4641 N N   . GLN B 1 167 ? 36.167 91.922  148.717 1.00 59.86  ? 167 GLN B N   1 
ATOM 4642 C CA  . GLN B 1 167 ? 35.677 90.661  149.297 1.00 59.71  ? 167 GLN B CA  1 
ATOM 4643 C C   . GLN B 1 167 ? 36.600 90.173  150.436 1.00 59.08  ? 167 GLN B C   1 
ATOM 4644 O O   . GLN B 1 167 ? 36.181 89.479  151.378 1.00 58.71  ? 167 GLN B O   1 
ATOM 4645 C CB  . GLN B 1 167 ? 35.591 89.594  148.195 1.00 60.72  ? 167 GLN B CB  1 
ATOM 4646 C CG  . GLN B 1 167 ? 35.114 88.207  148.654 1.00 62.74  ? 167 GLN B CG  1 
ATOM 4647 C CD  . GLN B 1 167 ? 34.861 87.246  147.482 1.00 63.61  ? 167 GLN B CD  1 
ATOM 4648 O OE1 . GLN B 1 167 ? 35.446 87.385  146.394 1.00 62.93  ? 167 GLN B OE1 1 
ATOM 4649 N NE2 . GLN B 1 167 ? 33.994 86.253  147.710 1.00 64.72  ? 167 GLN B NE2 1 
ATOM 4650 N N   . PHE B 1 168 ? 37.866 90.554  150.339 1.00 57.87  ? 168 PHE B N   1 
ATOM 4651 C CA  . PHE B 1 168 ? 38.889 90.186  151.316 1.00 56.21  ? 168 PHE B CA  1 
ATOM 4652 C C   . PHE B 1 168 ? 38.741 90.891  152.667 1.00 56.01  ? 168 PHE B C   1 
ATOM 4653 O O   . PHE B 1 168 ? 38.508 90.224  153.667 1.00 56.39  ? 168 PHE B O   1 
ATOM 4654 C CB  . PHE B 1 168 ? 40.273 90.473  150.715 1.00 55.37  ? 168 PHE B CB  1 
ATOM 4655 C CG  . PHE B 1 168 ? 41.358 90.722  151.732 1.00 53.57  ? 168 PHE B CG  1 
ATOM 4656 C CD1 . PHE B 1 168 ? 41.943 89.670  152.410 1.00 52.53  ? 168 PHE B CD1 1 
ATOM 4657 C CD2 . PHE B 1 168 ? 41.824 92.016  151.975 1.00 52.30  ? 168 PHE B CD2 1 
ATOM 4658 C CE1 . PHE B 1 168 ? 42.983 89.904  153.309 1.00 52.83  ? 168 PHE B CE1 1 
ATOM 4659 C CE2 . PHE B 1 168 ? 42.861 92.250  152.872 1.00 51.56  ? 168 PHE B CE2 1 
ATOM 4660 C CZ  . PHE B 1 168 ? 43.442 91.199  153.535 1.00 52.26  ? 168 PHE B CZ  1 
ATOM 4661 N N   . VAL B 1 169 ? 38.889 92.223  152.681 1.00 55.35  ? 169 VAL B N   1 
ATOM 4662 C CA  . VAL B 1 169 ? 38.792 93.051  153.894 1.00 54.70  ? 169 VAL B CA  1 
ATOM 4663 C C   . VAL B 1 169 ? 37.721 92.581  154.848 1.00 55.01  ? 169 VAL B C   1 
ATOM 4664 O O   . VAL B 1 169 ? 37.949 92.445  156.049 1.00 53.66  ? 169 VAL B O   1 
ATOM 4665 C CB  . VAL B 1 169 ? 38.458 94.514  153.569 1.00 54.71  ? 169 VAL B CB  1 
ATOM 4666 C CG1 . VAL B 1 169 ? 38.431 95.329  154.856 1.00 54.21  ? 169 VAL B CG1 1 
ATOM 4667 C CG2 . VAL B 1 169 ? 39.467 95.072  152.598 1.00 54.94  ? 169 VAL B CG2 1 
ATOM 4668 N N   . PHE B 1 170 ? 36.530 92.377  154.309 1.00 55.60  ? 170 PHE B N   1 
ATOM 4669 C CA  . PHE B 1 170 ? 35.427 91.892  155.118 1.00 56.59  ? 170 PHE B CA  1 
ATOM 4670 C C   . PHE B 1 170 ? 35.905 90.663  155.847 1.00 57.39  ? 170 PHE B C   1 
ATOM 4671 O O   . PHE B 1 170 ? 35.778 90.540  157.068 1.00 56.59  ? 170 PHE B O   1 
ATOM 4672 C CB  . PHE B 1 170 ? 34.251 91.521  154.226 1.00 56.19  ? 170 PHE B CB  1 
ATOM 4673 C CG  . PHE B 1 170 ? 33.358 92.673  153.901 1.00 55.54  ? 170 PHE B CG  1 
ATOM 4674 C CD1 . PHE B 1 170 ? 33.455 93.863  154.614 1.00 54.85  ? 170 PHE B CD1 1 
ATOM 4675 C CD2 . PHE B 1 170 ? 32.358 92.541  152.942 1.00 54.66  ? 170 PHE B CD2 1 
ATOM 4676 C CE1 . PHE B 1 170 ? 32.562 94.889  154.383 1.00 53.74  ? 170 PHE B CE1 1 
ATOM 4677 C CE2 . PHE B 1 170 ? 31.455 93.570  152.701 1.00 53.63  ? 170 PHE B CE2 1 
ATOM 4678 C CZ  . PHE B 1 170 ? 31.550 94.735  153.416 1.00 53.21  ? 170 PHE B CZ  1 
ATOM 4679 N N   . TRP B 1 171 ? 36.450 89.744  155.065 1.00 58.88  ? 171 TRP B N   1 
ATOM 4680 C CA  . TRP B 1 171 ? 36.991 88.526  155.610 1.00 60.23  ? 171 TRP B CA  1 
ATOM 4681 C C   . TRP B 1 171 ? 37.836 88.835  156.852 1.00 60.99  ? 171 TRP B C   1 
ATOM 4682 O O   . TRP B 1 171 ? 37.494 88.383  157.940 1.00 61.41  ? 171 TRP B O   1 
ATOM 4683 C CB  . TRP B 1 171 ? 37.835 87.824  154.552 1.00 60.94  ? 171 TRP B CB  1 
ATOM 4684 C CG  . TRP B 1 171 ? 37.143 86.724  153.834 1.00 62.43  ? 171 TRP B CG  1 
ATOM 4685 C CD1 . TRP B 1 171 ? 37.512 86.175  152.638 1.00 63.45  ? 171 TRP B CD1 1 
ATOM 4686 C CD2 . TRP B 1 171 ? 36.016 85.965  154.292 1.00 63.09  ? 171 TRP B CD2 1 
ATOM 4687 N NE1 . TRP B 1 171 ? 36.689 85.119  152.326 1.00 64.23  ? 171 TRP B NE1 1 
ATOM 4688 C CE2 . TRP B 1 171 ? 35.763 84.969  153.325 1.00 63.55  ? 171 TRP B CE2 1 
ATOM 4689 C CE3 . TRP B 1 171 ? 35.201 86.025  155.426 1.00 62.64  ? 171 TRP B CE3 1 
ATOM 4690 C CZ2 . TRP B 1 171 ? 34.724 84.040  153.459 1.00 63.60  ? 171 TRP B CZ2 1 
ATOM 4691 C CZ3 . TRP B 1 171 ? 34.172 85.101  155.560 1.00 62.66  ? 171 TRP B CZ3 1 
ATOM 4692 C CH2 . TRP B 1 171 ? 33.943 84.123  154.583 1.00 63.20  ? 171 TRP B CH2 1 
ATOM 4693 N N   . LEU B 1 172 ? 38.913 89.613  156.714 1.00 61.48  ? 172 LEU B N   1 
ATOM 4694 C CA  . LEU B 1 172 ? 39.762 89.905  157.876 1.00 61.77  ? 172 LEU B CA  1 
ATOM 4695 C C   . LEU B 1 172 ? 39.068 90.761  158.910 1.00 61.10  ? 172 LEU B C   1 
ATOM 4696 O O   . LEU B 1 172 ? 39.209 90.535  160.123 1.00 61.47  ? 172 LEU B O   1 
ATOM 4697 C CB  . LEU B 1 172 ? 41.088 90.581  157.481 1.00 62.84  ? 172 LEU B CB  1 
ATOM 4698 C CG  . LEU B 1 172 ? 42.279 89.699  157.018 1.00 64.25  ? 172 LEU B CG  1 
ATOM 4699 C CD1 . LEU B 1 172 ? 43.564 90.548  156.939 1.00 64.20  ? 172 LEU B CD1 1 
ATOM 4700 C CD2 . LEU B 1 172 ? 42.496 88.530  157.981 1.00 63.64  ? 172 LEU B CD2 1 
ATOM 4701 N N   . GLY B 1 173 ? 38.324 91.754  158.445 1.00 59.77  ? 173 GLY B N   1 
ATOM 4702 C CA  . GLY B 1 173 ? 37.621 92.589  159.394 1.00 59.02  ? 173 GLY B CA  1 
ATOM 4703 C C   . GLY B 1 173 ? 36.816 91.679  160.294 1.00 57.93  ? 173 GLY B C   1 
ATOM 4704 O O   . GLY B 1 173 ? 37.077 91.585  161.493 1.00 56.74  ? 173 GLY B O   1 
ATOM 4705 N N   . SER B 1 174 ? 35.863 90.978  159.679 1.00 57.79  ? 174 SER B N   1 
ATOM 4706 C CA  . SER B 1 174 ? 34.947 90.055  160.359 1.00 57.34  ? 174 SER B CA  1 
ATOM 4707 C C   . SER B 1 174 ? 35.694 88.965  161.087 1.00 57.35  ? 174 SER B C   1 
ATOM 4708 O O   . SER B 1 174 ? 35.312 88.528  162.177 1.00 56.40  ? 174 SER B O   1 
ATOM 4709 C CB  . SER B 1 174 ? 34.000 89.418  159.331 1.00 57.21  ? 174 SER B CB  1 
ATOM 4710 O OG  . SER B 1 174 ? 33.207 88.397  159.916 1.00 56.26  ? 174 SER B OG  1 
ATOM 4711 N N   . GLY B 1 175 ? 36.773 88.532  160.461 1.00 57.69  ? 175 GLY B N   1 
ATOM 4712 C CA  . GLY B 1 175 ? 37.561 87.486  161.052 1.00 58.68  ? 175 GLY B CA  1 
ATOM 4713 C C   . GLY B 1 175 ? 38.236 87.860  162.354 1.00 58.97  ? 175 GLY B C   1 
ATOM 4714 O O   . GLY B 1 175 ? 37.799 87.444  163.441 1.00 59.39  ? 175 GLY B O   1 
ATOM 4715 N N   . CYS B 1 176 ? 39.309 88.638  162.265 1.00 58.80  ? 176 CYS B N   1 
ATOM 4716 C CA  . CYS B 1 176 ? 40.014 88.984  163.482 1.00 59.30  ? 176 CYS B CA  1 
ATOM 4717 C C   . CYS B 1 176 ? 38.978 89.418  164.509 1.00 59.54  ? 176 CYS B C   1 
ATOM 4718 O O   . CYS B 1 176 ? 39.104 89.144  165.709 1.00 59.81  ? 176 CYS B O   1 
ATOM 4719 C CB  . CYS B 1 176 ? 41.043 90.070  163.212 1.00 58.78  ? 176 CYS B CB  1 
ATOM 4720 S SG  . CYS B 1 176 ? 40.357 91.482  162.520 1.00 59.05  ? 176 CYS B SG  1 
ATOM 4721 N N   . ALA B 1 177 ? 37.920 90.041  164.003 1.00 59.43  ? 177 ALA B N   1 
ATOM 4722 C CA  . ALA B 1 177 ? 36.820 90.519  164.825 1.00 59.37  ? 177 ALA B CA  1 
ATOM 4723 C C   . ALA B 1 177 ? 36.195 89.407  165.645 1.00 59.19  ? 177 ALA B C   1 
ATOM 4724 O O   . ALA B 1 177 ? 36.141 89.489  166.860 1.00 58.91  ? 177 ALA B O   1 
ATOM 4725 C CB  . ALA B 1 177 ? 35.779 91.136  163.942 1.00 59.17  ? 177 ALA B CB  1 
ATOM 4726 N N   . LEU B 1 178 ? 35.718 88.373  164.964 1.00 59.68  ? 178 LEU B N   1 
ATOM 4727 C CA  . LEU B 1 178 ? 35.090 87.253  165.637 1.00 60.42  ? 178 LEU B CA  1 
ATOM 4728 C C   . LEU B 1 178 ? 36.091 86.532  166.506 1.00 59.84  ? 178 LEU B C   1 
ATOM 4729 O O   . LEU B 1 178 ? 35.933 86.497  167.722 1.00 59.55  ? 178 LEU B O   1 
ATOM 4730 C CB  . LEU B 1 178 ? 34.517 86.251  164.633 1.00 62.00  ? 178 LEU B CB  1 
ATOM 4731 C CG  . LEU B 1 178 ? 34.424 84.817  165.200 1.00 62.40  ? 178 LEU B CG  1 
ATOM 4732 C CD1 . LEU B 1 178 ? 33.333 84.729  166.251 1.00 63.32  ? 178 LEU B CD1 1 
ATOM 4733 C CD2 . LEU B 1 178 ? 34.167 83.818  164.082 1.00 62.81  ? 178 LEU B CD2 1 
ATOM 4734 N N   . ILE B 1 179 ? 37.111 85.951  165.873 1.00 59.37  ? 179 ILE B N   1 
ATOM 4735 C CA  . ILE B 1 179 ? 38.126 85.205  166.597 1.00 58.70  ? 179 ILE B CA  1 
ATOM 4736 C C   . ILE B 1 179 ? 38.509 85.926  167.893 1.00 58.51  ? 179 ILE B C   1 
ATOM 4737 O O   . ILE B 1 179 ? 38.247 85.428  168.996 1.00 59.60  ? 179 ILE B O   1 
ATOM 4738 C CB  . ILE B 1 179 ? 39.396 84.972  165.728 1.00 57.95  ? 179 ILE B CB  1 
ATOM 4739 C CG1 . ILE B 1 179 ? 38.996 84.263  164.437 1.00 59.10  ? 179 ILE B CG1 1 
ATOM 4740 C CG2 . ILE B 1 179 ? 40.411 84.089  166.476 1.00 57.58  ? 179 ILE B CG2 1 
ATOM 4741 C CD1 . ILE B 1 179 ? 40.154 84.005  163.475 1.00 59.94  ? 179 ILE B CD1 1 
ATOM 4742 N N   . LEU B 1 180 ? 39.093 87.112  167.776 1.00 57.03  ? 180 LEU B N   1 
ATOM 4743 C CA  . LEU B 1 180 ? 39.508 87.841  168.963 1.00 55.91  ? 180 LEU B CA  1 
ATOM 4744 C C   . LEU B 1 180 ? 38.341 88.272  169.858 1.00 56.06  ? 180 LEU B C   1 
ATOM 4745 O O   . LEU B 1 180 ? 38.501 88.427  171.066 1.00 55.53  ? 180 LEU B O   1 
ATOM 4746 C CB  . LEU B 1 180 ? 40.382 89.019  168.532 1.00 55.63  ? 180 LEU B CB  1 
ATOM 4747 C CG  . LEU B 1 180 ? 41.618 88.577  167.723 1.00 54.09  ? 180 LEU B CG  1 
ATOM 4748 C CD1 . LEU B 1 180 ? 42.489 89.766  167.460 1.00 53.68  ? 180 LEU B CD1 1 
ATOM 4749 C CD2 . LEU B 1 180 ? 42.422 87.513  168.477 1.00 54.05  ? 180 LEU B CD2 1 
ATOM 4750 N N   . ALA B 1 181 ? 37.165 88.446  169.265 1.00 55.75  ? 181 ALA B N   1 
ATOM 4751 C CA  . ALA B 1 181 ? 35.983 88.819  170.037 1.00 55.57  ? 181 ALA B CA  1 
ATOM 4752 C C   . ALA B 1 181 ? 35.713 87.696  171.037 1.00 55.75  ? 181 ALA B C   1 
ATOM 4753 O O   . ALA B 1 181 ? 35.903 87.878  172.239 1.00 54.85  ? 181 ALA B O   1 
ATOM 4754 C CB  . ALA B 1 181 ? 34.777 89.006  169.112 1.00 56.30  ? 181 ALA B CB  1 
ATOM 4755 N N   . VAL B 1 182 ? 35.292 86.534  170.534 1.00 56.52  ? 182 VAL B N   1 
ATOM 4756 C CA  . VAL B 1 182 ? 35.010 85.380  171.399 1.00 57.77  ? 182 VAL B CA  1 
ATOM 4757 C C   . VAL B 1 182 ? 36.240 85.092  172.263 1.00 58.46  ? 182 VAL B C   1 
ATOM 4758 O O   . VAL B 1 182 ? 36.118 84.828  173.459 1.00 58.71  ? 182 VAL B O   1 
ATOM 4759 C CB  . VAL B 1 182 ? 34.611 84.082  170.571 1.00 58.32  ? 182 VAL B CB  1 
ATOM 4760 C CG1 . VAL B 1 182 ? 34.579 82.835  171.481 1.00 57.35  ? 182 VAL B CG1 1 
ATOM 4761 C CG2 . VAL B 1 182 ? 33.221 84.283  169.923 1.00 57.88  ? 182 VAL B CG2 1 
ATOM 4762 N N   . LEU B 1 183 ? 37.422 85.180  171.658 1.00 59.37  ? 183 LEU B N   1 
ATOM 4763 C CA  . LEU B 1 183 ? 38.659 84.937  172.376 1.00 61.21  ? 183 LEU B CA  1 
ATOM 4764 C C   . LEU B 1 183 ? 38.595 85.758  173.670 1.00 62.48  ? 183 LEU B C   1 
ATOM 4765 O O   . LEU B 1 183 ? 38.919 85.263  174.755 1.00 62.99  ? 183 LEU B O   1 
ATOM 4766 C CB  . LEU B 1 183 ? 39.880 85.355  171.525 1.00 61.05  ? 183 LEU B CB  1 
ATOM 4767 C CG  . LEU B 1 183 ? 41.179 84.511  171.663 1.00 61.31  ? 183 LEU B CG  1 
ATOM 4768 C CD1 . LEU B 1 183 ? 41.077 83.287  170.750 1.00 60.80  ? 183 LEU B CD1 1 
ATOM 4769 C CD2 . LEU B 1 183 ? 42.438 85.319  171.287 1.00 60.40  ? 183 LEU B CD2 1 
ATOM 4770 N N   . LEU B 1 184 ? 38.111 86.990  173.567 1.00 64.00  ? 184 LEU B N   1 
ATOM 4771 C CA  . LEU B 1 184 ? 38.042 87.869  174.729 1.00 65.63  ? 184 LEU B CA  1 
ATOM 4772 C C   . LEU B 1 184 ? 36.944 87.639  175.784 1.00 67.25  ? 184 LEU B C   1 
ATOM 4773 O O   . LEU B 1 184 ? 37.066 88.125  176.918 1.00 66.25  ? 184 LEU B O   1 
ATOM 4774 C CB  . LEU B 1 184 ? 38.021 89.317  174.235 1.00 66.08  ? 184 LEU B CB  1 
ATOM 4775 C CG  . LEU B 1 184 ? 39.184 89.609  173.270 1.00 66.56  ? 184 LEU B CG  1 
ATOM 4776 C CD1 . LEU B 1 184 ? 39.183 91.084  172.840 1.00 67.29  ? 184 LEU B CD1 1 
ATOM 4777 C CD2 . LEU B 1 184 ? 40.506 89.229  173.937 1.00 66.07  ? 184 LEU B CD2 1 
ATOM 4778 N N   . PHE B 1 185 ? 35.889 86.903  175.424 1.00 69.34  ? 185 PHE B N   1 
ATOM 4779 C CA  . PHE B 1 185 ? 34.796 86.602  176.367 1.00 72.00  ? 185 PHE B CA  1 
ATOM 4780 C C   . PHE B 1 185 ? 35.186 85.541  177.394 1.00 73.05  ? 185 PHE B C   1 
ATOM 4781 O O   . PHE B 1 185 ? 34.914 85.689  178.591 1.00 73.08  ? 185 PHE B O   1 
ATOM 4782 C CB  . PHE B 1 185 ? 33.524 86.111  175.642 1.00 73.31  ? 185 PHE B CB  1 
ATOM 4783 C CG  . PHE B 1 185 ? 32.650 87.223  175.132 1.00 74.68  ? 185 PHE B CG  1 
ATOM 4784 C CD1 . PHE B 1 185 ? 31.876 87.975  176.014 1.00 75.13  ? 185 PHE B CD1 1 
ATOM 4785 C CD2 . PHE B 1 185 ? 32.661 87.576  173.786 1.00 76.41  ? 185 PHE B CD2 1 
ATOM 4786 C CE1 . PHE B 1 185 ? 31.127 89.071  175.570 1.00 76.34  ? 185 PHE B CE1 1 
ATOM 4787 C CE2 . PHE B 1 185 ? 31.912 88.676  173.326 1.00 78.09  ? 185 PHE B CE2 1 
ATOM 4788 C CZ  . PHE B 1 185 ? 31.144 89.426  174.229 1.00 77.45  ? 185 PHE B CZ  1 
ATOM 4789 N N   . PHE B 1 186 ? 35.831 84.473  176.937 1.00 74.60  ? 186 PHE B N   1 
ATOM 4790 C CA  . PHE B 1 186 ? 36.190 83.409  177.856 1.00 75.76  ? 186 PHE B CA  1 
ATOM 4791 C C   . PHE B 1 186 ? 37.056 83.800  179.022 1.00 76.06  ? 186 PHE B C   1 
ATOM 4792 O O   . PHE B 1 186 ? 37.171 83.043  179.983 1.00 76.69  ? 186 PHE B O   1 
ATOM 4793 C CB  . PHE B 1 186 ? 36.772 82.218  177.111 1.00 76.61  ? 186 PHE B CB  1 
ATOM 4794 C CG  . PHE B 1 186 ? 35.738 81.447  176.383 1.00 77.99  ? 186 PHE B CG  1 
ATOM 4795 C CD1 . PHE B 1 186 ? 34.895 80.569  177.070 1.00 78.27  ? 186 PHE B CD1 1 
ATOM 4796 C CD2 . PHE B 1 186 ? 35.557 81.636  175.021 1.00 79.54  ? 186 PHE B CD2 1 
ATOM 4797 C CE1 . PHE B 1 186 ? 33.885 79.887  176.404 1.00 79.38  ? 186 PHE B CE1 1 
ATOM 4798 C CE2 . PHE B 1 186 ? 34.555 80.964  174.338 1.00 81.02  ? 186 PHE B CE2 1 
ATOM 4799 C CZ  . PHE B 1 186 ? 33.711 80.084  175.027 1.00 80.81  ? 186 PHE B CZ  1 
ATOM 4800 N N   . ALA B 1 187 ? 37.629 84.998  178.953 1.00 75.79  ? 187 ALA B N   1 
ATOM 4801 C CA  . ALA B 1 187 ? 38.439 85.523  180.048 1.00 76.12  ? 187 ALA B CA  1 
ATOM 4802 C C   . ALA B 1 187 ? 37.770 86.819  180.589 1.00 76.66  ? 187 ALA B C   1 
ATOM 4803 O O   . ALA B 1 187 ? 38.130 87.930  180.191 1.00 77.01  ? 187 ALA B O   1 
ATOM 4804 C CB  . ALA B 1 187 ? 39.856 85.795  179.563 1.00 75.18  ? 187 ALA B CB  1 
ATOM 4805 N N   . LYS B 1 188 ? 36.820 86.664  181.521 1.00 76.81  ? 188 LYS B N   1 
ATOM 4806 C CA  . LYS B 1 188 ? 36.066 87.800  182.073 1.00 76.55  ? 188 LYS B CA  1 
ATOM 4807 C C   . LYS B 1 188 ? 36.188 88.193  183.569 1.00 77.13  ? 188 LYS B C   1 
ATOM 4808 O O   . LYS B 1 188 ? 37.184 87.884  184.230 1.00 77.23  ? 188 LYS B O   1 
ATOM 4809 C CB  . LYS B 1 188 ? 34.579 87.608  181.714 1.00 75.17  ? 188 LYS B CB  1 
ATOM 4810 C CG  . LYS B 1 188 ? 33.965 86.258  182.109 1.00 72.47  ? 188 LYS B CG  1 
ATOM 4811 C CD  . LYS B 1 188 ? 32.597 86.080  181.458 1.00 71.49  ? 188 LYS B CD  1 
ATOM 4812 C CE  . LYS B 1 188 ? 31.943 84.768  181.852 1.00 70.88  ? 188 LYS B CE  1 
ATOM 4813 N NZ  . LYS B 1 188 ? 30.696 84.505  181.077 1.00 70.56  ? 188 LYS B NZ  1 
ATOM 4814 N N   . THR B 1 189 ? 35.156 88.892  184.069 1.00 78.09  ? 189 THR B N   1 
ATOM 4815 C CA  . THR B 1 189 ? 35.058 89.369  185.468 1.00 79.30  ? 189 THR B CA  1 
ATOM 4816 C C   . THR B 1 189 ? 33.582 89.257  185.969 1.00 81.33  ? 189 THR B C   1 
ATOM 4817 O O   . THR B 1 189 ? 32.730 90.041  185.554 1.00 80.92  ? 189 THR B O   1 
ATOM 4818 C CB  . THR B 1 189 ? 35.516 90.854  185.566 1.00 78.78  ? 189 THR B CB  1 
ATOM 4819 O OG1 . THR B 1 189 ? 36.717 91.034  184.809 1.00 78.37  ? 189 THR B OG1 1 
ATOM 4820 C CG2 . THR B 1 189 ? 35.787 91.245  187.014 1.00 78.24  ? 189 THR B CG2 1 
ATOM 4821 N N   . ASP B 1 190 ? 33.304 88.317  186.884 1.00 83.52  ? 190 ASP B N   1 
ATOM 4822 C CA  . ASP B 1 190 ? 31.937 88.057  187.381 1.00 85.67  ? 190 ASP B CA  1 
ATOM 4823 C C   . ASP B 1 190 ? 31.396 88.502  188.743 1.00 87.89  ? 190 ASP B C   1 
ATOM 4824 O O   . ASP B 1 190 ? 30.239 88.919  188.828 1.00 87.53  ? 190 ASP B O   1 
ATOM 4825 C CB  . ASP B 1 190 ? 31.613 86.555  187.253 1.00 84.20  ? 190 ASP B CB  1 
ATOM 4826 C CG  . ASP B 1 190 ? 31.269 86.166  185.845 1.00 83.95  ? 190 ASP B CG  1 
ATOM 4827 O OD1 . ASP B 1 190 ? 31.163 87.092  185.014 1.00 83.98  ? 190 ASP B OD1 1 
ATOM 4828 O OD2 . ASP B 1 190 ? 31.092 84.956  185.553 1.00 82.46  ? 190 ASP B OD2 1 
ATOM 4829 N N   . ALA B 1 191 ? 32.192 88.383  189.803 1.00 90.04  ? 191 ALA B N   1 
ATOM 4830 C CA  . ALA B 1 191 ? 31.749 88.746  191.156 1.00 92.08  ? 191 ALA B CA  1 
ATOM 4831 C C   . ALA B 1 191 ? 32.654 89.782  191.804 1.00 93.97  ? 191 ALA B C   1 
ATOM 4832 O O   . ALA B 1 191 ? 33.751 90.038  191.313 1.00 93.75  ? 191 ALA B O   1 
ATOM 4833 C CB  . ALA B 1 191 ? 31.697 87.489  192.038 1.00 90.99  ? 191 ALA B CB  1 
ATOM 4834 N N   . PRO B 1 192 ? 32.193 90.417  192.905 1.00 95.28  ? 192 PRO B N   1 
ATOM 4835 C CA  . PRO B 1 192 ? 33.078 91.414  193.533 1.00 96.74  ? 192 PRO B CA  1 
ATOM 4836 C C   . PRO B 1 192 ? 34.163 90.804  194.422 1.00 98.03  ? 192 PRO B C   1 
ATOM 4837 O O   . PRO B 1 192 ? 34.289 89.566  194.542 1.00 97.92  ? 192 PRO B O   1 
ATOM 4838 C CB  . PRO B 1 192 ? 32.124 92.273  194.379 1.00 96.01  ? 192 PRO B CB  1 
ATOM 4839 C CG  . PRO B 1 192 ? 30.806 92.100  193.732 1.00 95.62  ? 192 PRO B CG  1 
ATOM 4840 C CD  . PRO B 1 192 ? 30.795 90.635  193.334 1.00 95.34  ? 192 PRO B CD  1 
ATOM 4841 N N   . SER B 1 193 ? 34.926 91.726  195.028 1.00 99.09  ? 193 SER B N   1 
ATOM 4842 C CA  . SER B 1 193 ? 36.025 91.472  195.977 1.00 100.16 ? 193 SER B CA  1 
ATOM 4843 C C   . SER B 1 193 ? 36.277 92.796  196.728 1.00 100.51 ? 193 SER B C   1 
ATOM 4844 O O   . SER B 1 193 ? 37.375 93.375  196.664 1.00 100.56 ? 193 SER B O   1 
ATOM 4845 C CB  . SER B 1 193 ? 37.308 91.034  195.249 1.00 100.22 ? 193 SER B CB  1 
ATOM 4846 O OG  . SER B 1 193 ? 37.719 92.007  194.304 1.00 100.68 ? 193 SER B OG  1 
ATOM 4847 N N   . SER B 1 194 ? 35.230 93.250  197.425 1.00 101.52 ? 194 SER B N   1 
ATOM 4848 C CA  . SER B 1 194 ? 35.193 94.496  198.215 1.00 102.13 ? 194 SER B CA  1 
ATOM 4849 C C   . SER B 1 194 ? 34.534 95.668  197.436 1.00 103.20 ? 194 SER B C   1 
ATOM 4850 O O   . SER B 1 194 ? 34.319 96.757  197.997 1.00 102.73 ? 194 SER B O   1 
ATOM 4851 C CB  . SER B 1 194 ? 36.606 94.900  198.688 1.00 101.49 ? 194 SER B CB  1 
ATOM 4852 O OG  . SER B 1 194 ? 36.562 95.944  199.647 1.00 100.48 ? 194 SER B OG  1 
ATOM 4853 N N   . ALA B 1 195 ? 34.209 95.436  196.157 1.00 104.16 ? 195 ALA B N   1 
ATOM 4854 C CA  . ALA B 1 195 ? 33.574 96.458  195.300 1.00 104.50 ? 195 ALA B CA  1 
ATOM 4855 C C   . ALA B 1 195 ? 32.030 96.328  195.239 1.00 104.41 ? 195 ALA B C   1 
ATOM 4856 O O   . ALA B 1 195 ? 31.406 96.528  194.179 1.00 104.81 ? 195 ALA B O   1 
ATOM 4857 C CB  . ALA B 1 195 ? 34.179 96.400  193.876 1.00 104.31 ? 195 ALA B CB  1 
ATOM 4858 N N   . THR B 1 196 ? 31.441 95.994  196.392 1.00 103.77 ? 196 THR B N   1 
ATOM 4859 C CA  . THR B 1 196 ? 29.993 95.809  196.577 1.00 102.60 ? 196 THR B CA  1 
ATOM 4860 C C   . THR B 1 196 ? 29.294 94.745  195.695 1.00 102.16 ? 196 THR B C   1 
ATOM 4861 O O   . THR B 1 196 ? 29.563 94.640  194.485 1.00 101.91 ? 196 THR B O   1 
ATOM 4862 C CB  . THR B 1 196 ? 29.233 97.138  196.415 1.00 102.36 ? 196 THR B CB  1 
ATOM 4863 O OG1 . THR B 1 196 ? 27.916 96.988  196.966 1.00 102.15 ? 196 THR B OG1 1 
ATOM 4864 C CG2 . THR B 1 196 ? 29.129 97.526  194.935 1.00 101.86 ? 196 THR B CG2 1 
ATOM 4865 N N   . VAL B 1 197 ? 28.380 93.989  196.331 1.00 101.20 ? 197 VAL B N   1 
ATOM 4866 C CA  . VAL B 1 197 ? 27.582 92.895  195.726 1.00 100.21 ? 197 VAL B CA  1 
ATOM 4867 C C   . VAL B 1 197 ? 26.536 93.332  194.680 1.00 99.18  ? 197 VAL B C   1 
ATOM 4868 O O   . VAL B 1 197 ? 26.459 92.721  193.609 1.00 99.53  ? 197 VAL B O   1 
ATOM 4869 C CB  . VAL B 1 197 ? 26.794 92.052  196.822 1.00 99.24  ? 197 VAL B CB  1 
ATOM 4870 C CG1 . VAL B 1 197 ? 25.954 90.959  196.143 1.00 99.01  ? 197 VAL B CG1 1 
ATOM 4871 C CG2 . VAL B 1 197 ? 27.762 91.431  197.855 1.00 99.16  ? 197 VAL B CG2 1 
ATOM 4872 N N   . ALA B 1 198 ? 25.725 94.353  195.003 1.00 97.85  ? 198 ALA B N   1 
ATOM 4873 C CA  . ALA B 1 198 ? 24.673 94.857  194.096 1.00 96.51  ? 198 ALA B CA  1 
ATOM 4874 C C   . ALA B 1 198 ? 25.205 95.672  192.899 1.00 95.51  ? 198 ALA B C   1 
ATOM 4875 O O   . ALA B 1 198 ? 26.138 96.487  193.055 1.00 95.26  ? 198 ALA B O   1 
ATOM 4876 C CB  . ALA B 1 198 ? 23.621 95.700  194.890 1.00 94.55  ? 198 ALA B CB  1 
ATOM 4877 N N   . ASN B 1 199 ? 24.611 95.434  191.717 1.00 94.13  ? 199 ASN B N   1 
ATOM 4878 C CA  . ASN B 1 199 ? 24.962 96.117  190.455 1.00 92.53  ? 199 ASN B CA  1 
ATOM 4879 C C   . ASN B 1 199 ? 24.590 97.603  190.489 1.00 92.65  ? 199 ASN B C   1 
ATOM 4880 O O   . ASN B 1 199 ? 25.108 98.410  189.700 1.00 91.88  ? 199 ASN B O   1 
ATOM 4881 C CB  . ASN B 1 199 ? 24.236 95.450  189.280 1.00 90.62  ? 199 ASN B CB  1 
ATOM 4882 C CG  . ASN B 1 199 ? 22.713 95.607  189.351 1.00 89.89  ? 199 ASN B CG  1 
ATOM 4883 O OD1 . ASN B 1 199 ? 22.123 95.650  190.434 1.00 88.78  ? 199 ASN B OD1 1 
ATOM 4884 N ND2 . ASN B 1 199 ? 22.074 95.661  188.188 1.00 89.12  ? 199 ASN B ND2 1 
ATOM 4885 N N   . ALA B 1 200 ? 23.679 97.951  191.398 1.00 92.76  ? 200 ALA B N   1 
ATOM 4886 C CA  . ALA B 1 200 ? 23.226 99.326  191.567 1.00 92.35  ? 200 ALA B CA  1 
ATOM 4887 C C   . ALA B 1 200 ? 24.116 100.135 192.513 1.00 91.89  ? 200 ALA B C   1 
ATOM 4888 O O   . ALA B 1 200 ? 23.864 101.321 192.721 1.00 92.12  ? 200 ALA B O   1 
ATOM 4889 C CB  . ALA B 1 200 ? 21.787 99.326  192.116 1.00 90.52  ? 200 ALA B CB  1 
ATOM 4890 N N   . VAL B 1 201 ? 25.178 99.531  193.043 1.00 91.48  ? 201 VAL B N   1 
ATOM 4891 C CA  . VAL B 1 201 ? 26.028 100.218 194.025 1.00 90.63  ? 201 VAL B CA  1 
ATOM 4892 C C   . VAL B 1 201 ? 27.240 101.070 193.597 1.00 88.97  ? 201 VAL B C   1 
ATOM 4893 O O   . VAL B 1 201 ? 27.458 102.190 194.101 1.00 88.15  ? 201 VAL B O   1 
ATOM 4894 C CB  . VAL B 1 201 ? 26.512 99.176  195.084 1.00 90.56  ? 201 VAL B CB  1 
ATOM 4895 C CG1 . VAL B 1 201 ? 27.161 99.879  196.281 1.00 90.79  ? 201 VAL B CG1 1 
ATOM 4896 C CG2 . VAL B 1 201 ? 25.331 98.297  195.546 1.00 89.35  ? 201 VAL B CG2 1 
ATOM 4897 N N   . GLY B 1 202 ? 28.015 100.530 192.666 1.00 88.35  ? 202 GLY B N   1 
ATOM 4898 C CA  . GLY B 1 202 ? 29.200 101.211 192.181 1.00 87.65  ? 202 GLY B CA  1 
ATOM 4899 C C   . GLY B 1 202 ? 29.003 102.252 191.088 1.00 87.30  ? 202 GLY B C   1 
ATOM 4900 O O   . GLY B 1 202 ? 29.381 103.417 191.299 1.00 87.59  ? 202 GLY B O   1 
ATOM 4901 N N   . ALA B 1 203 ? 28.429 101.843 189.941 1.00 86.55  ? 203 ALA B N   1 
ATOM 4902 C CA  . ALA B 1 203 ? 28.194 102.734 188.775 1.00 84.92  ? 203 ALA B CA  1 
ATOM 4903 C C   . ALA B 1 203 ? 26.950 103.653 188.809 1.00 83.48  ? 203 ALA B C   1 
ATOM 4904 O O   . ALA B 1 203 ? 26.864 104.612 188.020 1.00 82.73  ? 203 ALA B O   1 
ATOM 4905 C CB  . ALA B 1 203 ? 28.193 101.908 187.469 1.00 84.08  ? 203 ALA B CB  1 
ATOM 4906 N N   . ASN B 1 204 ? 25.995 103.349 189.699 1.00 81.51  ? 204 ASN B N   1 
ATOM 4907 C CA  . ASN B 1 204 ? 24.774 104.155 189.871 1.00 79.00  ? 204 ASN B CA  1 
ATOM 4908 C C   . ASN B 1 204 ? 24.036 104.384 188.540 1.00 76.86  ? 204 ASN B C   1 
ATOM 4909 O O   . ASN B 1 204 ? 24.334 103.734 187.538 1.00 77.06  ? 204 ASN B O   1 
ATOM 4910 C CB  . ASN B 1 204 ? 25.137 105.516 190.502 1.00 79.04  ? 204 ASN B CB  1 
ATOM 4911 C CG  . ASN B 1 204 ? 25.772 105.396 191.906 1.00 79.07  ? 204 ASN B CG  1 
ATOM 4912 O OD1 . ASN B 1 204 ? 26.299 106.386 192.434 1.00 78.56  ? 204 ASN B OD1 1 
ATOM 4913 N ND2 . ASN B 1 204 ? 25.714 104.203 192.510 1.00 78.76  ? 204 ASN B ND2 1 
ATOM 4914 N N   . HIS B 1 205 ? 23.080 105.306 188.508 1.00 74.50  ? 205 HIS B N   1 
ATOM 4915 C CA  . HIS B 1 205 ? 22.384 105.532 187.247 1.00 72.05  ? 205 HIS B CA  1 
ATOM 4916 C C   . HIS B 1 205 ? 21.816 106.962 187.105 1.00 69.94  ? 205 HIS B C   1 
ATOM 4917 O O   . HIS B 1 205 ? 22.010 107.806 187.980 1.00 70.02  ? 205 HIS B O   1 
ATOM 4918 C CB  . HIS B 1 205 ? 21.293 104.452 187.097 1.00 72.59  ? 205 HIS B CB  1 
ATOM 4919 C CG  . HIS B 1 205 ? 20.879 104.195 185.680 1.00 73.94  ? 205 HIS B CG  1 
ATOM 4920 N ND1 . HIS B 1 205 ? 19.552 104.147 185.297 1.00 73.89  ? 205 HIS B ND1 1 
ATOM 4921 C CD2 . HIS B 1 205 ? 21.602 103.987 184.556 1.00 74.32  ? 205 HIS B CD2 1 
ATOM 4922 C CE1 . HIS B 1 205 ? 19.480 103.925 183.999 1.00 74.63  ? 205 HIS B CE1 1 
ATOM 4923 N NE2 . HIS B 1 205 ? 20.711 103.825 183.523 1.00 74.93  ? 205 HIS B NE2 1 
ATOM 4924 N N   . SER B 1 206 ? 21.164 107.232 185.976 1.00 66.64  ? 206 SER B N   1 
ATOM 4925 C CA  . SER B 1 206 ? 20.552 108.530 185.689 1.00 63.09  ? 206 SER B CA  1 
ATOM 4926 C C   . SER B 1 206 ? 19.147 108.209 185.143 1.00 60.81  ? 206 SER B C   1 
ATOM 4927 O O   . SER B 1 206 ? 18.942 107.135 184.570 1.00 60.19  ? 206 SER B O   1 
ATOM 4928 C CB  . SER B 1 206 ? 21.400 109.281 184.650 1.00 62.87  ? 206 SER B CB  1 
ATOM 4929 O OG  . SER B 1 206 ? 22.712 109.523 185.145 1.00 62.32  ? 206 SER B OG  1 
ATOM 4930 N N   . ALA B 1 207 ? 18.174 109.102 185.326 1.00 58.57  ? 207 ALA B N   1 
ATOM 4931 C CA  . ALA B 1 207 ? 16.820 108.802 184.841 1.00 56.29  ? 207 ALA B CA  1 
ATOM 4932 C C   . ALA B 1 207 ? 16.066 109.975 184.209 1.00 54.76  ? 207 ALA B C   1 
ATOM 4933 O O   . ALA B 1 207 ? 16.507 111.120 184.293 1.00 53.56  ? 207 ALA B O   1 
ATOM 4934 C CB  . ALA B 1 207 ? 15.996 108.202 185.967 1.00 56.30  ? 207 ALA B CB  1 
ATOM 4935 N N   . PHE B 1 208 ? 14.927 109.672 183.580 1.00 53.18  ? 208 PHE B N   1 
ATOM 4936 C CA  . PHE B 1 208 ? 14.129 110.686 182.894 1.00 51.91  ? 208 PHE B CA  1 
ATOM 4937 C C   . PHE B 1 208 ? 12.628 110.430 182.841 1.00 50.29  ? 208 PHE B C   1 
ATOM 4938 O O   . PHE B 1 208 ? 12.172 109.307 183.095 1.00 50.01  ? 208 PHE B O   1 
ATOM 4939 C CB  . PHE B 1 208 ? 14.656 110.892 181.459 1.00 53.31  ? 208 PHE B CB  1 
ATOM 4940 C CG  . PHE B 1 208 ? 14.729 109.628 180.637 1.00 54.77  ? 208 PHE B CG  1 
ATOM 4941 C CD1 . PHE B 1 208 ? 15.684 108.651 180.919 1.00 55.87  ? 208 PHE B CD1 1 
ATOM 4942 C CD2 . PHE B 1 208 ? 13.860 109.421 179.570 1.00 55.94  ? 208 PHE B CD2 1 
ATOM 4943 C CE1 . PHE B 1 208 ? 15.787 107.483 180.135 1.00 57.12  ? 208 PHE B CE1 1 
ATOM 4944 C CE2 . PHE B 1 208 ? 13.946 108.258 178.771 1.00 57.01  ? 208 PHE B CE2 1 
ATOM 4945 C CZ  . PHE B 1 208 ? 14.913 107.282 179.057 1.00 57.26  ? 208 PHE B CZ  1 
ATOM 4946 N N   . SER B 1 209 ? 11.873 111.473 182.472 1.00 48.35  ? 209 SER B N   1 
ATOM 4947 C CA  . SER B 1 209 ? 10.420 111.369 182.425 1.00 46.82  ? 209 SER B CA  1 
ATOM 4948 C C   . SER B 1 209 ? 9.685  112.588 181.915 1.00 45.05  ? 209 SER B C   1 
ATOM 4949 O O   . SER B 1 209 ? 10.236 113.675 181.844 1.00 43.97  ? 209 SER B O   1 
ATOM 4950 C CB  . SER B 1 209 ? 9.914  111.136 183.814 1.00 48.38  ? 209 SER B CB  1 
ATOM 4951 O OG  . SER B 1 209 ? 10.362 112.241 184.577 1.00 49.90  ? 209 SER B OG  1 
ATOM 4952 N N   . LEU B 1 210 ? 8.401  112.366 181.647 1.00 43.48  ? 210 LEU B N   1 
ATOM 4953 C CA  . LEU B 1 210 ? 7.466  113.357 181.143 1.00 42.28  ? 210 LEU B CA  1 
ATOM 4954 C C   . LEU B 1 210 ? 7.596  114.738 181.751 1.00 41.68  ? 210 LEU B C   1 
ATOM 4955 O O   . LEU B 1 210 ? 7.674  115.729 181.030 1.00 41.28  ? 210 LEU B O   1 
ATOM 4956 C CB  . LEU B 1 210 ? 6.028  112.881 181.346 1.00 42.20  ? 210 LEU B CB  1 
ATOM 4957 C CG  . LEU B 1 210 ? 4.958  113.897 180.938 1.00 42.32  ? 210 LEU B CG  1 
ATOM 4958 C CD1 . LEU B 1 210 ? 4.958  113.964 179.431 1.00 42.28  ? 210 LEU B CD1 1 
ATOM 4959 C CD2 . LEU B 1 210 ? 3.560  113.521 181.466 1.00 42.61  ? 210 LEU B CD2 1 
ATOM 4960 N N   . LYS B 1 211 ? 7.600  114.830 183.074 1.00 41.15  ? 211 LYS B N   1 
ATOM 4961 C CA  . LYS B 1 211 ? 7.700  116.156 183.666 1.00 40.94  ? 211 LYS B CA  1 
ATOM 4962 C C   . LYS B 1 211 ? 9.038  116.780 183.320 1.00 40.10  ? 211 LYS B C   1 
ATOM 4963 O O   . LYS B 1 211 ? 9.093  117.940 182.901 1.00 40.30  ? 211 LYS B O   1 
ATOM 4964 C CB  . LYS B 1 211 ? 7.496  116.135 185.194 1.00 41.60  ? 211 LYS B CB  1 
ATOM 4965 C CG  . LYS B 1 211 ? 6.035  115.970 185.657 1.00 41.66  ? 211 LYS B CG  1 
ATOM 4966 C CD  . LYS B 1 211 ? 5.152  117.157 185.277 1.00 41.10  ? 211 LYS B CD  1 
ATOM 4967 C CE  . LYS B 1 211 ? 3.686  116.778 185.393 1.00 40.69  ? 211 LYS B CE  1 
ATOM 4968 N NZ  . LYS B 1 211 ? 2.801  117.855 184.873 1.00 40.13  ? 211 LYS B NZ  1 
ATOM 4969 N N   . LEU B 1 212 ? 10.117 116.019 183.479 1.00 39.35  ? 212 LEU B N   1 
ATOM 4970 C CA  . LEU B 1 212 ? 11.426 116.559 183.146 1.00 38.84  ? 212 LEU B CA  1 
ATOM 4971 C C   . LEU B 1 212 ? 11.282 117.125 181.769 1.00 37.54  ? 212 LEU B C   1 
ATOM 4972 O O   . LEU B 1 212 ? 11.611 118.274 181.488 1.00 35.66  ? 212 LEU B O   1 
ATOM 4973 C CB  . LEU B 1 212 ? 12.475 115.457 183.114 1.00 39.15  ? 212 LEU B CB  1 
ATOM 4974 C CG  . LEU B 1 212 ? 13.095 115.080 184.458 1.00 40.34  ? 212 LEU B CG  1 
ATOM 4975 C CD1 . LEU B 1 212 ? 14.213 114.076 184.188 1.00 39.76  ? 212 LEU B CD1 1 
ATOM 4976 C CD2 . LEU B 1 212 ? 13.628 116.340 185.186 1.00 40.62  ? 212 LEU B CD2 1 
ATOM 4977 N N   . ALA B 1 213 ? 10.756 116.264 180.920 1.00 37.68  ? 213 ALA B N   1 
ATOM 4978 C CA  . ALA B 1 213 ? 10.524 116.578 179.542 1.00 37.91  ? 213 ALA B CA  1 
ATOM 4979 C C   . ALA B 1 213 ? 9.731  117.851 179.484 1.00 38.17  ? 213 ALA B C   1 
ATOM 4980 O O   . ALA B 1 213 ? 10.259 118.890 179.117 1.00 38.15  ? 213 ALA B O   1 
ATOM 4981 C CB  . ALA B 1 213 ? 9.756  115.448 178.884 1.00 37.74  ? 213 ALA B CB  1 
ATOM 4982 N N   . LEU B 1 214 ? 8.466  117.763 179.874 1.00 38.82  ? 214 LEU B N   1 
ATOM 4983 C CA  . LEU B 1 214 ? 7.572  118.906 179.849 1.00 40.18  ? 214 LEU B CA  1 
ATOM 4984 C C   . LEU B 1 214 ? 8.214  120.145 180.418 1.00 41.31  ? 214 LEU B C   1 
ATOM 4985 O O   . LEU B 1 214 ? 7.952  121.270 179.975 1.00 40.86  ? 214 LEU B O   1 
ATOM 4986 C CB  . LEU B 1 214 ? 6.294  118.589 180.616 1.00 39.78  ? 214 LEU B CB  1 
ATOM 4987 C CG  . LEU B 1 214 ? 5.412  117.581 179.885 1.00 40.04  ? 214 LEU B CG  1 
ATOM 4988 C CD1 . LEU B 1 214 ? 4.086  117.435 180.608 1.00 40.15  ? 214 LEU B CD1 1 
ATOM 4989 C CD2 . LEU B 1 214 ? 5.187  118.063 178.455 1.00 40.43  ? 214 LEU B CD2 1 
ATOM 4990 N N   . GLU B 1 215 ? 9.069  119.953 181.402 1.00 42.62  ? 215 GLU B N   1 
ATOM 4991 C CA  . GLU B 1 215 ? 9.705  121.106 181.963 1.00 44.28  ? 215 GLU B CA  1 
ATOM 4992 C C   . GLU B 1 215 ? 10.699 121.632 180.924 1.00 44.50  ? 215 GLU B C   1 
ATOM 4993 O O   . GLU B 1 215 ? 10.743 122.831 180.667 1.00 44.91  ? 215 GLU B O   1 
ATOM 4994 C CB  . GLU B 1 215 ? 10.367 120.720 183.273 1.00 45.83  ? 215 GLU B CB  1 
ATOM 4995 C CG  . GLU B 1 215 ? 10.921 121.889 184.012 1.00 47.78  ? 215 GLU B CG  1 
ATOM 4996 C CD  . GLU B 1 215 ? 12.170 122.402 183.355 1.00 49.40  ? 215 GLU B CD  1 
ATOM 4997 O OE1 . GLU B 1 215 ? 12.661 121.725 182.422 1.00 51.03  ? 215 GLU B OE1 1 
ATOM 4998 O OE2 . GLU B 1 215 ? 12.666 123.468 183.776 1.00 50.11  ? 215 GLU B OE2 1 
ATOM 4999 N N   . LEU B 1 216 ? 11.468 120.723 180.319 1.00 44.95  ? 216 LEU B N   1 
ATOM 5000 C CA  . LEU B 1 216 ? 12.460 121.056 179.292 1.00 45.58  ? 216 LEU B CA  1 
ATOM 5001 C C   . LEU B 1 216 ? 11.796 121.821 178.179 1.00 46.68  ? 216 LEU B C   1 
ATOM 5002 O O   . LEU B 1 216 ? 12.273 122.866 177.763 1.00 45.61  ? 216 LEU B O   1 
ATOM 5003 C CB  . LEU B 1 216 ? 13.099 119.787 178.712 1.00 44.77  ? 216 LEU B CB  1 
ATOM 5004 C CG  . LEU B 1 216 ? 14.359 119.313 179.444 1.00 44.01  ? 216 LEU B CG  1 
ATOM 5005 C CD1 . LEU B 1 216 ? 14.941 118.099 178.785 1.00 43.14  ? 216 LEU B CD1 1 
ATOM 5006 C CD2 . LEU B 1 216 ? 15.372 120.425 179.412 1.00 43.32  ? 216 LEU B CD2 1 
ATOM 5007 N N   . PHE B 1 217 ? 10.680 121.303 177.694 1.00 49.22  ? 217 PHE B N   1 
ATOM 5008 C CA  . PHE B 1 217 ? 9.988  122.010 176.636 1.00 52.04  ? 217 PHE B CA  1 
ATOM 5009 C C   . PHE B 1 217 ? 9.500  123.369 177.117 1.00 52.37  ? 217 PHE B C   1 
ATOM 5010 O O   . PHE B 1 217 ? 9.268  124.268 176.310 1.00 52.08  ? 217 PHE B O   1 
ATOM 5011 C CB  . PHE B 1 217 ? 8.814  121.196 176.084 1.00 53.58  ? 217 PHE B CB  1 
ATOM 5012 C CG  . PHE B 1 217 ? 9.233  119.959 175.343 1.00 54.08  ? 217 PHE B CG  1 
ATOM 5013 C CD1 . PHE B 1 217 ? 9.638  118.833 176.036 1.00 54.10  ? 217 PHE B CD1 1 
ATOM 5014 C CD2 . PHE B 1 217 ? 9.208  119.922 173.947 1.00 54.15  ? 217 PHE B CD2 1 
ATOM 5015 C CE1 . PHE B 1 217 ? 10.004 117.686 175.358 1.00 54.09  ? 217 PHE B CE1 1 
ATOM 5016 C CE2 . PHE B 1 217 ? 9.574  118.781 173.259 1.00 53.39  ? 217 PHE B CE2 1 
ATOM 5017 C CZ  . PHE B 1 217 ? 9.973  117.659 173.966 1.00 53.64  ? 217 PHE B CZ  1 
ATOM 5018 N N   . ARG B 1 218 ? 9.334  123.520 178.424 1.00 53.50  ? 218 ARG B N   1 
ATOM 5019 C CA  . ARG B 1 218 ? 8.910  124.799 178.968 1.00 55.12  ? 218 ARG B CA  1 
ATOM 5020 C C   . ARG B 1 218 ? 10.080 125.735 178.691 1.00 54.17  ? 218 ARG B C   1 
ATOM 5021 O O   . ARG B 1 218 ? 9.904  126.906 178.362 1.00 53.88  ? 218 ARG B O   1 
ATOM 5022 C CB  . ARG B 1 218 ? 8.671  124.661 180.481 1.00 57.95  ? 218 ARG B CB  1 
ATOM 5023 C CG  . ARG B 1 218 ? 8.487  125.968 181.257 1.00 62.39  ? 218 ARG B CG  1 
ATOM 5024 C CD  . ARG B 1 218 ? 8.792  125.757 182.741 1.00 66.01  ? 218 ARG B CD  1 
ATOM 5025 N NE  . ARG B 1 218 ? 8.641  126.986 183.514 1.00 69.87  ? 218 ARG B NE  1 
ATOM 5026 C CZ  . ARG B 1 218 ? 8.846  127.072 184.827 1.00 71.44  ? 218 ARG B CZ  1 
ATOM 5027 N NH1 . ARG B 1 218 ? 9.214  125.997 185.506 1.00 73.15  ? 218 ARG B NH1 1 
ATOM 5028 N NH2 . ARG B 1 218 ? 8.672  128.226 185.468 1.00 72.79  ? 218 ARG B NH2 1 
ATOM 5029 N N   . GLN B 1 219 ? 11.284 125.184 178.792 1.00 53.30  ? 219 GLN B N   1 
ATOM 5030 C CA  . GLN B 1 219 ? 12.494 125.969 178.606 1.00 53.05  ? 219 GLN B CA  1 
ATOM 5031 C C   . GLN B 1 219 ? 12.675 126.438 177.186 1.00 52.33  ? 219 GLN B C   1 
ATOM 5032 O O   . GLN B 1 219 ? 12.330 125.729 176.240 1.00 53.56  ? 219 GLN B O   1 
ATOM 5033 C CB  . GLN B 1 219 ? 13.713 125.156 178.997 1.00 52.90  ? 219 GLN B CB  1 
ATOM 5034 C CG  . GLN B 1 219 ? 13.669 124.534 180.378 1.00 53.81  ? 219 GLN B CG  1 
ATOM 5035 C CD  . GLN B 1 219 ? 14.943 123.796 180.671 1.00 54.27  ? 219 GLN B CD  1 
ATOM 5036 O OE1 . GLN B 1 219 ? 15.445 123.081 179.804 1.00 55.87  ? 219 GLN B OE1 1 
ATOM 5037 N NE2 . GLN B 1 219 ? 15.483 123.957 181.885 1.00 54.40  ? 219 GLN B NE2 1 
ATOM 5038 N N   . PRO B 1 220 ? 13.206 127.655 177.011 1.00 50.63  ? 220 PRO B N   1 
ATOM 5039 C CA  . PRO B 1 220 ? 13.430 128.195 175.667 1.00 50.20  ? 220 PRO B CA  1 
ATOM 5040 C C   . PRO B 1 220 ? 14.805 127.788 175.167 1.00 48.62  ? 220 PRO B C   1 
ATOM 5041 O O   . PRO B 1 220 ? 15.002 127.577 173.978 1.00 48.80  ? 220 PRO B O   1 
ATOM 5042 C CB  . PRO B 1 220 ? 13.333 129.698 175.873 1.00 49.83  ? 220 PRO B CB  1 
ATOM 5043 C CG  . PRO B 1 220 ? 13.911 129.863 177.230 1.00 50.20  ? 220 PRO B CG  1 
ATOM 5044 C CD  . PRO B 1 220 ? 13.306 128.717 178.024 1.00 50.98  ? 220 PRO B CD  1 
ATOM 5045 N N   . LYS B 1 221 ? 15.755 127.666 176.085 1.00 47.25  ? 221 LYS B N   1 
ATOM 5046 C CA  . LYS B 1 221 ? 17.099 127.305 175.697 1.00 46.96  ? 221 LYS B CA  1 
ATOM 5047 C C   . LYS B 1 221 ? 17.148 126.047 174.877 1.00 46.77  ? 221 LYS B C   1 
ATOM 5048 O O   . LYS B 1 221 ? 17.989 125.937 173.996 1.00 46.91  ? 221 LYS B O   1 
ATOM 5049 C CB  . LYS B 1 221 ? 18.017 127.154 176.911 1.00 47.24  ? 221 LYS B CB  1 
ATOM 5050 C CG  . LYS B 1 221 ? 17.390 126.450 178.117 1.00 47.46  ? 221 LYS B CG  1 
ATOM 5051 C CD  . LYS B 1 221 ? 18.375 126.331 179.317 1.00 46.33  ? 221 LYS B CD  1 
ATOM 5052 C CE  . LYS B 1 221 ? 17.759 125.526 180.474 1.00 45.50  ? 221 LYS B CE  1 
ATOM 5053 N NZ  . LYS B 1 221 ? 18.738 124.945 181.442 1.00 45.44  ? 221 LYS B NZ  1 
ATOM 5054 N N   . LEU B 1 222 ? 16.260 125.097 175.144 1.00 47.89  ? 222 LEU B N   1 
ATOM 5055 C CA  . LEU B 1 222 ? 16.289 123.877 174.360 1.00 48.87  ? 222 LEU B CA  1 
ATOM 5056 C C   . LEU B 1 222 ? 16.049 124.252 172.913 1.00 49.35  ? 222 LEU B C   1 
ATOM 5057 O O   . LEU B 1 222 ? 16.872 123.966 172.043 1.00 48.98  ? 222 LEU B O   1 
ATOM 5058 C CB  . LEU B 1 222 ? 15.212 122.873 174.793 1.00 49.20  ? 222 LEU B CB  1 
ATOM 5059 C CG  . LEU B 1 222 ? 15.168 121.605 173.907 1.00 49.84  ? 222 LEU B CG  1 
ATOM 5060 C CD1 . LEU B 1 222 ? 16.456 120.794 174.124 1.00 49.99  ? 222 LEU B CD1 1 
ATOM 5061 C CD2 . LEU B 1 222 ? 13.933 120.756 174.219 1.00 49.41  ? 222 LEU B CD2 1 
ATOM 5062 N N   . TRP B 1 223 ? 14.927 124.914 172.667 1.00 49.48  ? 223 TRP B N   1 
ATOM 5063 C CA  . TRP B 1 223 ? 14.568 125.299 171.320 1.00 50.19  ? 223 TRP B CA  1 
ATOM 5064 C C   . TRP B 1 223 ? 15.765 125.828 170.563 1.00 48.96  ? 223 TRP B C   1 
ATOM 5065 O O   . TRP B 1 223 ? 16.056 125.419 169.436 1.00 49.88  ? 223 TRP B O   1 
ATOM 5066 C CB  . TRP B 1 223 ? 13.484 126.363 171.358 1.00 54.42  ? 223 TRP B CB  1 
ATOM 5067 C CG  . TRP B 1 223 ? 12.182 125.889 171.948 1.00 58.52  ? 223 TRP B CG  1 
ATOM 5068 C CD1 . TRP B 1 223 ? 11.247 126.660 172.581 1.00 59.86  ? 223 TRP B CD1 1 
ATOM 5069 C CD2 . TRP B 1 223 ? 11.633 124.559 171.891 1.00 60.22  ? 223 TRP B CD2 1 
ATOM 5070 N NE1 . TRP B 1 223 ? 10.154 125.899 172.917 1.00 61.60  ? 223 TRP B NE1 1 
ATOM 5071 C CE2 . TRP B 1 223 ? 10.362 124.610 172.509 1.00 61.56  ? 223 TRP B CE2 1 
ATOM 5072 C CE3 . TRP B 1 223 ? 12.093 123.337 171.382 1.00 60.52  ? 223 TRP B CE3 1 
ATOM 5073 C CZ2 . TRP B 1 223 ? 9.540  123.483 172.624 1.00 62.15  ? 223 TRP B CZ2 1 
ATOM 5074 C CZ3 . TRP B 1 223 ? 11.274 122.220 171.500 1.00 61.57  ? 223 TRP B CZ3 1 
ATOM 5075 C CH2 . TRP B 1 223 ? 10.014 122.304 172.117 1.00 62.34  ? 223 TRP B CH2 1 
ATOM 5076 N N   . PHE B 1 224 ? 16.477 126.731 171.204 1.00 46.93  ? 224 PHE B N   1 
ATOM 5077 C CA  . PHE B 1 224 ? 17.608 127.329 170.573 1.00 44.75  ? 224 PHE B CA  1 
ATOM 5078 C C   . PHE B 1 224 ? 18.816 126.431 170.559 1.00 42.84  ? 224 PHE B C   1 
ATOM 5079 O O   . PHE B 1 224 ? 19.650 126.541 169.661 1.00 43.15  ? 224 PHE B O   1 
ATOM 5080 C CB  . PHE B 1 224 ? 17.835 128.687 171.212 1.00 45.16  ? 224 PHE B CB  1 
ATOM 5081 C CG  . PHE B 1 224 ? 16.692 129.636 170.959 1.00 45.98  ? 224 PHE B CG  1 
ATOM 5082 C CD1 . PHE B 1 224 ? 15.477 129.189 170.443 1.00 46.16  ? 224 PHE B CD1 1 
ATOM 5083 C CD2 . PHE B 1 224 ? 16.822 130.961 171.215 1.00 46.11  ? 224 PHE B CD2 1 
ATOM 5084 C CE1 . PHE B 1 224 ? 14.430 130.084 170.197 1.00 46.10  ? 224 PHE B CE1 1 
ATOM 5085 C CE2 . PHE B 1 224 ? 15.782 131.848 170.967 1.00 47.04  ? 224 PHE B CE2 1 
ATOM 5086 C CZ  . PHE B 1 224 ? 14.597 131.411 170.463 1.00 46.74  ? 224 PHE B CZ  1 
ATOM 5087 N N   . LEU B 1 225 ? 18.903 125.495 171.494 1.00 39.39  ? 225 LEU B N   1 
ATOM 5088 C CA  . LEU B 1 225 ? 20.034 124.592 171.432 1.00 36.63  ? 225 LEU B CA  1 
ATOM 5089 C C   . LEU B 1 225 ? 19.757 123.606 170.322 1.00 33.99  ? 225 LEU B C   1 
ATOM 5090 O O   . LEU B 1 225 ? 20.570 123.419 169.427 1.00 34.32  ? 225 LEU B O   1 
ATOM 5091 C CB  . LEU B 1 225 ? 20.235 123.801 172.711 1.00 37.40  ? 225 LEU B CB  1 
ATOM 5092 C CG  . LEU B 1 225 ? 21.438 122.905 172.393 1.00 38.28  ? 225 LEU B CG  1 
ATOM 5093 C CD1 . LEU B 1 225 ? 22.736 123.718 172.472 1.00 38.43  ? 225 LEU B CD1 1 
ATOM 5094 C CD2 . LEU B 1 225 ? 21.474 121.752 173.333 1.00 38.52  ? 225 LEU B CD2 1 
ATOM 5095 N N   . SER B 1 226 ? 18.603 122.963 170.385 1.00 31.48  ? 226 SER B N   1 
ATOM 5096 C CA  . SER B 1 226 ? 18.265 122.010 169.349 1.00 28.78  ? 226 SER B CA  1 
ATOM 5097 C C   . SER B 1 226 ? 18.476 122.597 167.951 1.00 26.90  ? 226 SER B C   1 
ATOM 5098 O O   . SER B 1 226 ? 19.035 121.927 167.097 1.00 26.74  ? 226 SER B O   1 
ATOM 5099 C CB  . SER B 1 226 ? 16.828 121.516 169.508 1.00 28.96  ? 226 SER B CB  1 
ATOM 5100 O OG  . SER B 1 226 ? 16.742 120.586 170.568 1.00 28.92  ? 226 SER B OG  1 
ATOM 5101 N N   . LEU B 1 227 ? 18.044 123.832 167.701 1.00 24.28  ? 227 LEU B N   1 
ATOM 5102 C CA  . LEU B 1 227 ? 18.266 124.388 166.380 1.00 21.50  ? 227 LEU B CA  1 
ATOM 5103 C C   . LEU B 1 227 ? 19.696 124.081 166.041 1.00 20.04  ? 227 LEU B C   1 
ATOM 5104 O O   . LEU B 1 227 ? 19.984 123.366 165.081 1.00 20.16  ? 227 LEU B O   1 
ATOM 5105 C CB  . LEU B 1 227 ? 18.080 125.902 166.322 1.00 21.04  ? 227 LEU B CB  1 
ATOM 5106 C CG  . LEU B 1 227 ? 16.657 126.385 166.026 1.00 20.35  ? 227 LEU B CG  1 
ATOM 5107 C CD1 . LEU B 1 227 ? 16.661 127.874 165.782 1.00 19.76  ? 227 LEU B CD1 1 
ATOM 5108 C CD2 . LEU B 1 227 ? 16.133 125.648 164.817 1.00 20.08  ? 227 LEU B CD2 1 
ATOM 5109 N N   . TYR B 1 228 ? 20.606 124.602 166.851 1.00 17.77  ? 228 TYR B N   1 
ATOM 5110 C CA  . TYR B 1 228 ? 22.020 124.395 166.596 1.00 16.64  ? 228 TYR B CA  1 
ATOM 5111 C C   . TYR B 1 228 ? 22.267 122.954 166.264 1.00 18.12  ? 228 TYR B C   1 
ATOM 5112 O O   . TYR B 1 228 ? 22.455 122.577 165.096 1.00 17.26  ? 228 TYR B O   1 
ATOM 5113 C CB  . TYR B 1 228 ? 22.874 124.728 167.804 1.00 14.45  ? 228 TYR B CB  1 
ATOM 5114 C CG  . TYR B 1 228 ? 24.357 124.619 167.523 1.00 11.37  ? 228 TYR B CG  1 
ATOM 5115 C CD1 . TYR B 1 228 ? 25.020 123.415 167.690 1.00 9.85   ? 228 TYR B CD1 1 
ATOM 5116 C CD2 . TYR B 1 228 ? 25.089 125.714 167.088 1.00 9.96   ? 228 TYR B CD2 1 
ATOM 5117 C CE1 . TYR B 1 228 ? 26.340 123.295 167.415 1.00 8.93   ? 228 TYR B CE1 1 
ATOM 5118 C CE2 . TYR B 1 228 ? 26.430 125.598 166.815 1.00 8.31   ? 228 TYR B CE2 1 
ATOM 5119 C CZ  . TYR B 1 228 ? 27.046 124.386 166.996 1.00 8.45   ? 228 TYR B CZ  1 
ATOM 5120 O OH  . TYR B 1 228 ? 28.380 124.238 166.778 1.00 9.52   ? 228 TYR B OH  1 
ATOM 5121 N N   . VAL B 1 229 ? 22.302 122.121 167.283 1.00 19.98  ? 229 VAL B N   1 
ATOM 5122 C CA  . VAL B 1 229 ? 22.555 120.720 167.050 1.00 22.51  ? 229 VAL B CA  1 
ATOM 5123 C C   . VAL B 1 229 ? 21.786 120.225 165.829 1.00 23.01  ? 229 VAL B C   1 
ATOM 5124 O O   . VAL B 1 229 ? 22.394 119.905 164.835 1.00 22.61  ? 229 VAL B O   1 
ATOM 5125 C CB  . VAL B 1 229 ? 22.088 119.839 168.285 1.00 24.51  ? 229 VAL B CB  1 
ATOM 5126 C CG1 . VAL B 1 229 ? 22.298 118.366 167.893 1.00 24.80  ? 229 VAL B CG1 1 
ATOM 5127 C CG2 . VAL B 1 229 ? 22.914 120.215 169.571 1.00 26.00  ? 229 VAL B CG2 1 
ATOM 5128 N N   . ILE B 1 230 ? 20.454 120.151 165.924 1.00 24.56  ? 230 ILE B N   1 
ATOM 5129 C CA  . ILE B 1 230 ? 19.641 119.630 164.815 1.00 26.97  ? 230 ILE B CA  1 
ATOM 5130 C C   . ILE B 1 230 ? 19.960 120.199 163.461 1.00 27.52  ? 230 ILE B C   1 
ATOM 5131 O O   . ILE B 1 230 ? 20.080 119.468 162.487 1.00 27.37  ? 230 ILE B O   1 
ATOM 5132 C CB  . ILE B 1 230 ? 18.126 119.848 165.036 1.00 28.37  ? 230 ILE B CB  1 
ATOM 5133 C CG1 . ILE B 1 230 ? 17.704 119.089 166.287 1.00 30.21  ? 230 ILE B CG1 1 
ATOM 5134 C CG2 . ILE B 1 230 ? 17.310 119.362 163.819 1.00 28.36  ? 230 ILE B CG2 1 
ATOM 5135 C CD1 . ILE B 1 230 ? 16.240 119.102 166.633 1.00 32.30  ? 230 ILE B CD1 1 
ATOM 5136 N N   . GLY B 1 231 ? 20.063 121.516 163.407 1.00 27.73  ? 231 GLY B N   1 
ATOM 5137 C CA  . GLY B 1 231 ? 20.358 122.172 162.155 1.00 27.76  ? 231 GLY B CA  1 
ATOM 5138 C C   . GLY B 1 231 ? 21.739 121.830 161.646 1.00 27.13  ? 231 GLY B C   1 
ATOM 5139 O O   . GLY B 1 231 ? 21.894 121.197 160.595 1.00 27.95  ? 231 GLY B O   1 
ATOM 5140 N N   . VAL B 1 232 ? 22.740 122.213 162.425 1.00 26.60  ? 232 VAL B N   1 
ATOM 5141 C CA  . VAL B 1 232 ? 24.118 121.985 162.063 1.00 26.53  ? 232 VAL B CA  1 
ATOM 5142 C C   . VAL B 1 232 ? 24.554 120.523 161.996 1.00 25.91  ? 232 VAL B C   1 
ATOM 5143 O O   . VAL B 1 232 ? 25.086 120.099 160.972 1.00 26.73  ? 232 VAL B O   1 
ATOM 5144 C CB  . VAL B 1 232 ? 25.044 122.792 162.982 1.00 26.48  ? 232 VAL B CB  1 
ATOM 5145 C CG1 . VAL B 1 232 ? 26.480 122.561 162.618 1.00 26.41  ? 232 VAL B CG1 1 
ATOM 5146 C CG2 . VAL B 1 232 ? 24.726 124.274 162.824 1.00 25.73  ? 232 VAL B CG2 1 
ATOM 5147 N N   . SER B 1 233 ? 24.322 119.743 163.046 1.00 24.24  ? 233 SER B N   1 
ATOM 5148 C CA  . SER B 1 233 ? 24.695 118.333 162.998 1.00 22.97  ? 233 SER B CA  1 
ATOM 5149 C C   . SER B 1 233 ? 24.086 117.664 161.768 1.00 22.17  ? 233 SER B C   1 
ATOM 5150 O O   . SER B 1 233 ? 24.798 117.188 160.884 1.00 22.92  ? 233 SER B O   1 
ATOM 5151 C CB  . SER B 1 233 ? 24.224 117.616 164.252 1.00 22.14  ? 233 SER B CB  1 
ATOM 5152 O OG  . SER B 1 233 ? 24.972 118.062 165.354 1.00 22.13  ? 233 SER B OG  1 
ATOM 5153 N N   . CYS B 1 234 ? 22.762 117.638 161.715 1.00 21.20  ? 234 CYS B N   1 
ATOM 5154 C CA  . CYS B 1 234 ? 22.037 117.039 160.596 1.00 20.25  ? 234 CYS B CA  1 
ATOM 5155 C C   . CYS B 1 234 ? 22.787 117.386 159.316 1.00 19.06  ? 234 CYS B C   1 
ATOM 5156 O O   . CYS B 1 234 ? 23.408 116.536 158.661 1.00 19.00  ? 234 CYS B O   1 
ATOM 5157 C CB  . CYS B 1 234 ? 20.642 117.640 160.572 1.00 21.76  ? 234 CYS B CB  1 
ATOM 5158 S SG  . CYS B 1 234 ? 19.389 116.942 159.496 1.00 23.26  ? 234 CYS B SG  1 
ATOM 5159 N N   . THR B 1 235 ? 22.713 118.659 158.984 1.00 16.20  ? 235 THR B N   1 
ATOM 5160 C CA  . THR B 1 235 ? 23.374 119.190 157.847 1.00 14.35  ? 235 THR B CA  1 
ATOM 5161 C C   . THR B 1 235 ? 24.779 118.587 157.707 1.00 13.93  ? 235 THR B C   1 
ATOM 5162 O O   . THR B 1 235 ? 25.024 117.752 156.834 1.00 13.35  ? 235 THR B O   1 
ATOM 5163 C CB  . THR B 1 235 ? 23.407 120.680 158.032 1.00 13.63  ? 235 THR B CB  1 
ATOM 5164 O OG1 . THR B 1 235 ? 22.062 121.136 158.170 1.00 12.92  ? 235 THR B OG1 1 
ATOM 5165 C CG2 . THR B 1 235 ? 24.040 121.365 156.873 1.00 15.95  ? 235 THR B CG2 1 
ATOM 5166 N N   . TYR B 1 236 ? 25.690 118.970 158.594 1.00 13.89  ? 236 TYR B N   1 
ATOM 5167 C CA  . TYR B 1 236 ? 27.071 118.491 158.522 1.00 14.82  ? 236 TYR B CA  1 
ATOM 5168 C C   . TYR B 1 236 ? 27.193 116.996 158.418 1.00 15.11  ? 236 TYR B C   1 
ATOM 5169 O O   . TYR B 1 236 ? 27.930 116.484 157.591 1.00 16.39  ? 236 TYR B O   1 
ATOM 5170 C CB  . TYR B 1 236 ? 27.881 118.963 159.724 1.00 15.25  ? 236 TYR B CB  1 
ATOM 5171 C CG  . TYR B 1 236 ? 29.327 118.517 159.710 1.00 15.61  ? 236 TYR B CG  1 
ATOM 5172 C CD1 . TYR B 1 236 ? 30.276 119.171 158.932 1.00 14.93  ? 236 TYR B CD1 1 
ATOM 5173 C CD2 . TYR B 1 236 ? 29.750 117.457 160.508 1.00 16.20  ? 236 TYR B CD2 1 
ATOM 5174 C CE1 . TYR B 1 236 ? 31.611 118.786 158.959 1.00 15.29  ? 236 TYR B CE1 1 
ATOM 5175 C CE2 . TYR B 1 236 ? 31.078 117.064 160.538 1.00 15.93  ? 236 TYR B CE2 1 
ATOM 5176 C CZ  . TYR B 1 236 ? 32.000 117.732 159.766 1.00 15.68  ? 236 TYR B CZ  1 
ATOM 5177 O OH  . TYR B 1 236 ? 33.311 117.345 159.815 1.00 14.76  ? 236 TYR B OH  1 
ATOM 5178 N N   . ASP B 1 237 ? 26.494 116.280 159.270 1.00 14.75  ? 237 ASP B N   1 
ATOM 5179 C CA  . ASP B 1 237 ? 26.579 114.855 159.191 1.00 14.92  ? 237 ASP B CA  1 
ATOM 5180 C C   . ASP B 1 237 ? 26.195 114.402 157.794 1.00 14.30  ? 237 ASP B C   1 
ATOM 5181 O O   . ASP B 1 237 ? 27.018 113.831 157.077 1.00 14.64  ? 237 ASP B O   1 
ATOM 5182 C CB  . ASP B 1 237 ? 25.683 114.237 160.259 1.00 16.74  ? 237 ASP B CB  1 
ATOM 5183 C CG  . ASP B 1 237 ? 26.319 114.281 161.625 1.00 19.46  ? 237 ASP B CG  1 
ATOM 5184 O OD1 . ASP B 1 237 ? 27.003 115.291 161.899 1.00 21.49  ? 237 ASP B OD1 1 
ATOM 5185 O OD2 . ASP B 1 237 ? 26.149 113.329 162.424 1.00 19.50  ? 237 ASP B OD2 1 
ATOM 5186 N N   . VAL B 1 238 ? 24.967 114.687 157.381 1.00 13.77  ? 238 VAL B N   1 
ATOM 5187 C CA  . VAL B 1 238 ? 24.551 114.263 156.059 1.00 13.75  ? 238 VAL B CA  1 
ATOM 5188 C C   . VAL B 1 238 ? 25.751 114.389 155.175 1.00 13.81  ? 238 VAL B C   1 
ATOM 5189 O O   . VAL B 1 238 ? 26.264 113.410 154.648 1.00 13.19  ? 238 VAL B O   1 
ATOM 5190 C CB  . VAL B 1 238 ? 23.444 115.138 155.482 1.00 13.98  ? 238 VAL B CB  1 
ATOM 5191 C CG1 . VAL B 1 238 ? 23.248 114.785 154.047 1.00 13.70  ? 238 VAL B CG1 1 
ATOM 5192 C CG2 . VAL B 1 238 ? 22.154 114.883 156.200 1.00 13.24  ? 238 VAL B CG2 1 
ATOM 5193 N N   . PHE B 1 239 ? 26.204 115.620 155.057 1.00 14.38  ? 239 PHE B N   1 
ATOM 5194 C CA  . PHE B 1 239 ? 27.353 115.938 154.259 1.00 15.98  ? 239 PHE B CA  1 
ATOM 5195 C C   . PHE B 1 239 ? 28.466 114.874 154.412 1.00 17.72  ? 239 PHE B C   1 
ATOM 5196 O O   . PHE B 1 239 ? 28.687 114.076 153.505 1.00 19.69  ? 239 PHE B O   1 
ATOM 5197 C CB  . PHE B 1 239 ? 27.801 117.332 154.665 1.00 13.97  ? 239 PHE B CB  1 
ATOM 5198 C CG  . PHE B 1 239 ? 29.049 117.779 154.022 1.00 13.32  ? 239 PHE B CG  1 
ATOM 5199 C CD1 . PHE B 1 239 ? 30.172 117.000 154.032 1.00 13.17  ? 239 PHE B CD1 1 
ATOM 5200 C CD2 . PHE B 1 239 ? 29.135 119.023 153.488 1.00 13.04  ? 239 PHE B CD2 1 
ATOM 5201 C CE1 . PHE B 1 239 ? 31.349 117.453 153.519 1.00 13.48  ? 239 PHE B CE1 1 
ATOM 5202 C CE2 . PHE B 1 239 ? 30.329 119.478 152.970 1.00 13.86  ? 239 PHE B CE2 1 
ATOM 5203 C CZ  . PHE B 1 239 ? 31.430 118.695 152.992 1.00 14.15  ? 239 PHE B CZ  1 
ATOM 5204 N N   . ASP B 1 240 ? 29.152 114.843 155.547 1.00 18.73  ? 240 ASP B N   1 
ATOM 5205 C CA  . ASP B 1 240 ? 30.233 113.888 155.751 1.00 19.99  ? 240 ASP B CA  1 
ATOM 5206 C C   . ASP B 1 240 ? 29.870 112.454 155.419 1.00 20.36  ? 240 ASP B C   1 
ATOM 5207 O O   . ASP B 1 240 ? 30.741 111.640 155.137 1.00 20.02  ? 240 ASP B O   1 
ATOM 5208 C CB  . ASP B 1 240 ? 30.726 113.948 157.199 1.00 21.97  ? 240 ASP B CB  1 
ATOM 5209 C CG  . ASP B 1 240 ? 31.843 112.950 157.485 1.00 24.30  ? 240 ASP B CG  1 
ATOM 5210 O OD1 . ASP B 1 240 ? 32.769 112.849 156.657 1.00 24.92  ? 240 ASP B OD1 1 
ATOM 5211 O OD2 . ASP B 1 240 ? 31.806 112.274 158.546 1.00 25.27  ? 240 ASP B OD2 1 
ATOM 5212 N N   . GLN B 1 241 ? 28.592 112.124 155.416 1.00 21.55  ? 241 GLN B N   1 
ATOM 5213 C CA  . GLN B 1 241 ? 28.244 110.734 155.159 1.00 23.23  ? 241 GLN B CA  1 
ATOM 5214 C C   . GLN B 1 241 ? 28.398 110.275 153.715 1.00 22.92  ? 241 GLN B C   1 
ATOM 5215 O O   . GLN B 1 241 ? 28.411 109.085 153.419 1.00 21.90  ? 241 GLN B O   1 
ATOM 5216 C CB  . GLN B 1 241 ? 26.816 110.465 155.625 1.00 25.37  ? 241 GLN B CB  1 
ATOM 5217 C CG  . GLN B 1 241 ? 25.794 110.423 154.497 1.00 27.44  ? 241 GLN B CG  1 
ATOM 5218 C CD  . GLN B 1 241 ? 24.367 110.554 154.993 1.00 27.95  ? 241 GLN B CD  1 
ATOM 5219 O OE1 . GLN B 1 241 ? 23.864 109.706 155.732 1.00 27.80  ? 241 GLN B OE1 1 
ATOM 5220 N NE2 . GLN B 1 241 ? 23.706 111.630 154.587 1.00 28.23  ? 241 GLN B NE2 1 
ATOM 5221 N N   . GLN B 1 242 ? 28.508 111.218 152.803 1.00 23.28  ? 242 GLN B N   1 
ATOM 5222 C CA  . GLN B 1 242 ? 28.631 110.851 151.404 1.00 24.27  ? 242 GLN B CA  1 
ATOM 5223 C C   . GLN B 1 242 ? 29.714 111.694 150.784 1.00 23.74  ? 242 GLN B C   1 
ATOM 5224 O O   . GLN B 1 242 ? 30.047 111.555 149.618 1.00 22.50  ? 242 GLN B O   1 
ATOM 5225 C CB  . GLN B 1 242 ? 27.302 111.102 150.706 1.00 26.41  ? 242 GLN B CB  1 
ATOM 5226 C CG  . GLN B 1 242 ? 27.150 110.553 149.310 1.00 28.08  ? 242 GLN B CG  1 
ATOM 5227 C CD  . GLN B 1 242 ? 25.692 110.342 148.975 1.00 29.34  ? 242 GLN B CD  1 
ATOM 5228 O OE1 . GLN B 1 242 ? 25.335 110.066 147.839 1.00 29.83  ? 242 GLN B OE1 1 
ATOM 5229 N NE2 . GLN B 1 242 ? 24.838 110.461 149.982 1.00 29.19  ? 242 GLN B NE2 1 
ATOM 5230 N N   . PHE B 1 243 ? 30.259 112.584 151.586 1.00 23.66  ? 243 PHE B N   1 
ATOM 5231 C CA  . PHE B 1 243 ? 31.309 113.449 151.121 1.00 23.73  ? 243 PHE B CA  1 
ATOM 5232 C C   . PHE B 1 243 ? 32.389 112.618 150.480 1.00 21.88  ? 243 PHE B C   1 
ATOM 5233 O O   . PHE B 1 243 ? 32.850 112.933 149.403 1.00 22.34  ? 243 PHE B O   1 
ATOM 5234 C CB  . PHE B 1 243 ? 31.882 114.226 152.291 1.00 26.99  ? 243 PHE B CB  1 
ATOM 5235 C CG  . PHE B 1 243 ? 33.190 114.905 151.998 1.00 31.53  ? 243 PHE B CG  1 
ATOM 5236 C CD1 . PHE B 1 243 ? 33.240 116.144 151.335 1.00 32.95  ? 243 PHE B CD1 1 
ATOM 5237 C CD2 . PHE B 1 243 ? 34.378 114.319 152.416 1.00 32.60  ? 243 PHE B CD2 1 
ATOM 5238 C CE1 . PHE B 1 243 ? 34.463 116.790 151.098 1.00 34.61  ? 243 PHE B CE1 1 
ATOM 5239 C CE2 . PHE B 1 243 ? 35.600 114.950 152.185 1.00 35.46  ? 243 PHE B CE2 1 
ATOM 5240 C CZ  . PHE B 1 243 ? 35.644 116.193 151.524 1.00 35.99  ? 243 PHE B CZ  1 
ATOM 5241 N N   . ALA B 1 244 ? 32.793 111.546 151.137 1.00 19.70  ? 244 ALA B N   1 
ATOM 5242 C CA  . ALA B 1 244 ? 33.842 110.697 150.596 1.00 17.06  ? 244 ALA B CA  1 
ATOM 5243 C C   . ALA B 1 244 ? 33.728 110.415 149.092 1.00 14.97  ? 244 ALA B C   1 
ATOM 5244 O O   . ALA B 1 244 ? 34.613 110.773 148.309 1.00 14.78  ? 244 ALA B O   1 
ATOM 5245 C CB  . ALA B 1 244 ? 33.883 109.403 151.364 1.00 17.75  ? 244 ALA B CB  1 
ATOM 5246 N N   . ASN B 1 245 ? 32.647 109.763 148.683 1.00 11.94  ? 245 ASN B N   1 
ATOM 5247 C CA  . ASN B 1 245 ? 32.469 109.431 147.273 1.00 9.47   ? 245 ASN B CA  1 
ATOM 5248 C C   . ASN B 1 245 ? 32.942 110.598 146.427 1.00 8.23   ? 245 ASN B C   1 
ATOM 5249 O O   . ASN B 1 245 ? 33.680 110.432 145.477 1.00 8.04   ? 245 ASN B O   1 
ATOM 5250 C CB  . ASN B 1 245 ? 31.003 109.111 146.976 1.00 11.37  ? 245 ASN B CB  1 
ATOM 5251 C CG  . ASN B 1 245 ? 30.687 107.629 147.112 1.00 12.85  ? 245 ASN B CG  1 
ATOM 5252 O OD1 . ASN B 1 245 ? 31.566 106.810 147.381 1.00 14.72  ? 245 ASN B OD1 1 
ATOM 5253 N ND2 . ASN B 1 245 ? 29.426 107.278 146.917 1.00 13.39  ? 245 ASN B ND2 1 
ATOM 5254 N N   . PHE B 1 246 ? 32.517 111.789 146.794 1.00 6.51   ? 246 PHE B N   1 
ATOM 5255 C CA  . PHE B 1 246 ? 32.907 112.983 146.092 1.00 4.55   ? 246 PHE B CA  1 
ATOM 5256 C C   . PHE B 1 246 ? 34.408 113.126 146.078 1.00 4.69   ? 246 PHE B C   1 
ATOM 5257 O O   . PHE B 1 246 ? 35.009 113.389 145.054 1.00 2.07   ? 246 PHE B O   1 
ATOM 5258 C CB  . PHE B 1 246 ? 32.288 114.144 146.815 1.00 3.30   ? 246 PHE B CB  1 
ATOM 5259 C CG  . PHE B 1 246 ? 32.899 115.438 146.499 1.00 3.14   ? 246 PHE B CG  1 
ATOM 5260 C CD1 . PHE B 1 246 ? 34.251 115.667 146.680 1.00 2.88   ? 246 PHE B CD1 1 
ATOM 5261 C CD2 . PHE B 1 246 ? 32.092 116.479 146.139 1.00 4.06   ? 246 PHE B CD2 1 
ATOM 5262 C CE1 . PHE B 1 246 ? 34.788 116.886 146.449 1.00 2.81   ? 246 PHE B CE1 1 
ATOM 5263 C CE2 . PHE B 1 246 ? 32.622 117.706 145.905 1.00 5.51   ? 246 PHE B CE2 1 
ATOM 5264 C CZ  . PHE B 1 246 ? 33.968 117.923 146.087 1.00 4.71   ? 246 PHE B CZ  1 
ATOM 5265 N N   . PHE B 1 247 ? 34.997 113.017 147.257 1.00 6.39   ? 247 PHE B N   1 
ATOM 5266 C CA  . PHE B 1 247 ? 36.433 113.129 147.478 1.00 8.78   ? 247 PHE B CA  1 
ATOM 5267 C C   . PHE B 1 247 ? 37.058 112.170 146.500 1.00 9.60   ? 247 PHE B C   1 
ATOM 5268 O O   . PHE B 1 247 ? 38.116 112.423 145.953 1.00 9.22   ? 247 PHE B O   1 
ATOM 5269 C CB  . PHE B 1 247 ? 36.733 112.714 148.933 1.00 10.17  ? 247 PHE B CB  1 
ATOM 5270 C CG  . PHE B 1 247 ? 38.208 112.703 149.309 1.00 11.48  ? 247 PHE B CG  1 
ATOM 5271 C CD1 . PHE B 1 247 ? 38.964 111.578 149.168 1.00 11.93  ? 247 PHE B CD1 1 
ATOM 5272 C CD2 . PHE B 1 247 ? 38.822 113.810 149.843 1.00 11.66  ? 247 PHE B CD2 1 
ATOM 5273 C CE1 . PHE B 1 247 ? 40.298 111.562 149.576 1.00 11.36  ? 247 PHE B CE1 1 
ATOM 5274 C CE2 . PHE B 1 247 ? 40.160 113.796 150.250 1.00 12.12  ? 247 PHE B CE2 1 
ATOM 5275 C CZ  . PHE B 1 247 ? 40.887 112.679 150.111 1.00 11.97  ? 247 PHE B CZ  1 
ATOM 5276 N N   . THR B 1 248 ? 36.346 111.090 146.235 1.00 11.41  ? 248 THR B N   1 
ATOM 5277 C CA  . THR B 1 248 ? 36.859 110.080 145.338 1.00 14.53  ? 248 THR B CA  1 
ATOM 5278 C C   . THR B 1 248 ? 36.901 110.434 143.840 1.00 17.13  ? 248 THR B C   1 
ATOM 5279 O O   . THR B 1 248 ? 37.568 109.766 143.038 1.00 17.88  ? 248 THR B O   1 
ATOM 5280 C CB  . THR B 1 248 ? 36.100 108.801 145.580 1.00 14.21  ? 248 THR B CB  1 
ATOM 5281 O OG1 . THR B 1 248 ? 36.175 108.509 146.979 1.00 13.12  ? 248 THR B OG1 1 
ATOM 5282 C CG2 . THR B 1 248 ? 36.700 107.647 144.778 1.00 15.65  ? 248 THR B CG2 1 
ATOM 5283 N N   . SER B 1 249 ? 36.193 111.481 143.449 1.00 18.78  ? 249 SER B N   1 
ATOM 5284 C CA  . SER B 1 249 ? 36.222 111.861 142.056 1.00 20.25  ? 249 SER B CA  1 
ATOM 5285 C C   . SER B 1 249 ? 37.584 112.461 141.763 1.00 21.22  ? 249 SER B C   1 
ATOM 5286 O O   . SER B 1 249 ? 38.186 112.156 140.754 1.00 21.06  ? 249 SER B O   1 
ATOM 5287 C CB  . SER B 1 249 ? 35.115 112.875 141.756 1.00 20.94  ? 249 SER B CB  1 
ATOM 5288 O OG  . SER B 1 249 ? 33.939 112.231 141.280 1.00 22.78  ? 249 SER B OG  1 
ATOM 5289 N N   . PHE B 1 250 ? 38.081 113.275 142.686 1.00 22.79  ? 250 PHE B N   1 
ATOM 5290 C CA  . PHE B 1 250 ? 39.351 113.984 142.541 1.00 25.40  ? 250 PHE B CA  1 
ATOM 5291 C C   . PHE B 1 250 ? 40.653 113.235 142.369 1.00 28.79  ? 250 PHE B C   1 
ATOM 5292 O O   . PHE B 1 250 ? 41.715 113.855 142.379 1.00 28.70  ? 250 PHE B O   1 
ATOM 5293 C CB  . PHE B 1 250 ? 39.536 114.948 143.707 1.00 23.42  ? 250 PHE B CB  1 
ATOM 5294 C CG  . PHE B 1 250 ? 38.575 116.079 143.704 1.00 22.12  ? 250 PHE B CG  1 
ATOM 5295 C CD1 . PHE B 1 250 ? 37.221 115.836 143.673 1.00 21.72  ? 250 PHE B CD1 1 
ATOM 5296 C CD2 . PHE B 1 250 ? 39.017 117.390 143.752 1.00 21.39  ? 250 PHE B CD2 1 
ATOM 5297 C CE1 . PHE B 1 250 ? 36.316 116.872 143.685 1.00 21.75  ? 250 PHE B CE1 1 
ATOM 5298 C CE2 . PHE B 1 250 ? 38.113 118.440 143.767 1.00 21.40  ? 250 PHE B CE2 1 
ATOM 5299 C CZ  . PHE B 1 250 ? 36.757 118.176 143.735 1.00 21.83  ? 250 PHE B CZ  1 
ATOM 5300 N N   . PHE B 1 251 ? 40.628 111.924 142.211 1.00 33.00  ? 251 PHE B N   1 
ATOM 5301 C CA  . PHE B 1 251 ? 41.920 111.277 142.063 1.00 38.43  ? 251 PHE B CA  1 
ATOM 5302 C C   . PHE B 1 251 ? 42.373 110.676 140.792 1.00 41.23  ? 251 PHE B C   1 
ATOM 5303 O O   . PHE B 1 251 ? 41.614 110.512 139.861 1.00 42.72  ? 251 PHE B O   1 
ATOM 5304 C CB  . PHE B 1 251 ? 42.135 110.261 143.136 1.00 40.39  ? 251 PHE B CB  1 
ATOM 5305 C CG  . PHE B 1 251 ? 42.397 110.875 144.398 1.00 43.09  ? 251 PHE B CG  1 
ATOM 5306 C CD1 . PHE B 1 251 ? 41.345 111.374 145.137 1.00 44.61  ? 251 PHE B CD1 1 
ATOM 5307 C CD2 . PHE B 1 251 ? 43.693 111.042 144.828 1.00 43.61  ? 251 PHE B CD2 1 
ATOM 5308 C CE1 . PHE B 1 251 ? 41.569 112.043 146.302 1.00 46.66  ? 251 PHE B CE1 1 
ATOM 5309 C CE2 . PHE B 1 251 ? 43.942 111.711 145.989 1.00 46.21  ? 251 PHE B CE2 1 
ATOM 5310 C CZ  . PHE B 1 251 ? 42.872 112.218 146.742 1.00 47.28  ? 251 PHE B CZ  1 
ATOM 5311 N N   . ALA B 1 252 ? 43.647 110.321 140.777 1.00 44.35  ? 252 ALA B N   1 
ATOM 5312 C CA  . ALA B 1 252 ? 44.237 109.763 139.588 1.00 47.48  ? 252 ALA B CA  1 
ATOM 5313 C C   . ALA B 1 252 ? 43.462 108.556 139.136 1.00 49.95  ? 252 ALA B C   1 
ATOM 5314 O O   . ALA B 1 252 ? 43.336 108.305 137.941 1.00 51.36  ? 252 ALA B O   1 
ATOM 5315 C CB  . ALA B 1 252 ? 45.664 109.408 139.853 1.00 47.68  ? 252 ALA B CB  1 
ATOM 5316 N N   . THR B 1 253 ? 42.926 107.820 140.104 1.00 51.73  ? 253 THR B N   1 
ATOM 5317 C CA  . THR B 1 253 ? 42.147 106.627 139.817 1.00 53.60  ? 253 THR B CA  1 
ATOM 5318 C C   . THR B 1 253 ? 41.341 106.188 141.013 1.00 55.11  ? 253 THR B C   1 
ATOM 5319 O O   . THR B 1 253 ? 41.648 106.542 142.152 1.00 55.80  ? 253 THR B O   1 
ATOM 5320 C CB  . THR B 1 253 ? 43.051 105.492 139.431 1.00 54.67  ? 253 THR B CB  1 
ATOM 5321 O OG1 . THR B 1 253 ? 43.834 105.889 138.304 1.00 56.70  ? 253 THR B OG1 1 
ATOM 5322 C CG2 . THR B 1 253 ? 42.235 104.268 139.051 1.00 55.14  ? 253 THR B CG2 1 
ATOM 5323 N N   . GLY B 1 254 ? 40.307 105.405 140.711 1.00 56.10  ? 254 GLY B N   1 
ATOM 5324 C CA  . GLY B 1 254 ? 39.415 104.852 141.713 1.00 57.50  ? 254 GLY B CA  1 
ATOM 5325 C C   . GLY B 1 254 ? 40.283 104.254 142.804 1.00 58.36  ? 254 GLY B C   1 
ATOM 5326 O O   . GLY B 1 254 ? 40.105 104.550 143.984 1.00 58.26  ? 254 GLY B O   1 
ATOM 5327 N N   . GLU B 1 255 ? 41.232 103.414 142.389 1.00 59.45  ? 255 GLU B N   1 
ATOM 5328 C CA  . GLU B 1 255 ? 42.168 102.760 143.298 1.00 60.35  ? 255 GLU B CA  1 
ATOM 5329 C C   . GLU B 1 255 ? 42.879 103.784 144.231 1.00 59.62  ? 255 GLU B C   1 
ATOM 5330 O O   . GLU B 1 255 ? 42.645 103.776 145.437 1.00 58.69  ? 255 GLU B O   1 
ATOM 5331 C CB  . GLU B 1 255 ? 43.208 101.910 142.505 1.00 62.43  ? 255 GLU B CB  1 
ATOM 5332 C CG  . GLU B 1 255 ? 43.803 100.665 143.246 1.00 64.62  ? 255 GLU B CG  1 
ATOM 5333 C CD  . GLU B 1 255 ? 44.369 99.575  142.323 1.00 66.04  ? 255 GLU B CD  1 
ATOM 5334 O OE1 . GLU B 1 255 ? 44.235 99.700  141.086 1.00 66.99  ? 255 GLU B OE1 1 
ATOM 5335 O OE2 . GLU B 1 255 ? 44.937 98.575  142.841 1.00 66.43  ? 255 GLU B OE2 1 
ATOM 5336 N N   . GLN B 1 256 ? 43.705 104.684 143.691 1.00 59.07  ? 256 GLN B N   1 
ATOM 5337 C CA  . GLN B 1 256 ? 44.434 105.657 144.527 1.00 57.91  ? 256 GLN B CA  1 
ATOM 5338 C C   . GLN B 1 256 ? 43.554 106.546 145.374 1.00 55.88  ? 256 GLN B C   1 
ATOM 5339 O O   . GLN B 1 256 ? 43.893 106.894 146.504 1.00 56.28  ? 256 GLN B O   1 
ATOM 5340 C CB  . GLN B 1 256 ? 45.346 106.578 143.695 1.00 59.56  ? 256 GLN B CB  1 
ATOM 5341 C CG  . GLN B 1 256 ? 46.313 107.453 144.563 1.00 61.36  ? 256 GLN B CG  1 
ATOM 5342 C CD  . GLN B 1 256 ? 47.423 106.628 145.286 1.00 62.16  ? 256 GLN B CD  1 
ATOM 5343 O OE1 . GLN B 1 256 ? 47.329 105.398 145.404 1.00 62.94  ? 256 GLN B OE1 1 
ATOM 5344 N NE2 . GLN B 1 256 ? 48.467 107.314 145.769 1.00 61.50  ? 256 GLN B NE2 1 
ATOM 5345 N N   . GLY B 1 257 ? 42.431 106.955 144.820 1.00 53.25  ? 257 GLY B N   1 
ATOM 5346 C CA  . GLY B 1 257 ? 41.552 107.791 145.600 1.00 50.97  ? 257 GLY B CA  1 
ATOM 5347 C C   . GLY B 1 257 ? 41.338 107.154 146.953 1.00 48.27  ? 257 GLY B C   1 
ATOM 5348 O O   . GLY B 1 257 ? 41.784 107.680 147.981 1.00 47.57  ? 257 GLY B O   1 
ATOM 5349 N N   . THR B 1 258 ? 40.670 106.002 146.933 1.00 46.12  ? 258 THR B N   1 
ATOM 5350 C CA  . THR B 1 258 ? 40.351 105.230 148.133 1.00 44.93  ? 258 THR B CA  1 
ATOM 5351 C C   . THR B 1 258 ? 41.489 105.226 149.147 1.00 44.92  ? 258 THR B C   1 
ATOM 5352 O O   . THR B 1 258 ? 41.279 105.515 150.327 1.00 44.99  ? 258 THR B O   1 
ATOM 5353 C CB  . THR B 1 258 ? 40.004 103.784 147.761 1.00 43.72  ? 258 THR B CB  1 
ATOM 5354 O OG1 . THR B 1 258 ? 38.975 103.804 146.768 1.00 42.58  ? 258 THR B OG1 1 
ATOM 5355 C CG2 . THR B 1 258 ? 39.513 103.010 148.976 1.00 42.57  ? 258 THR B CG2 1 
ATOM 5356 N N   . ARG B 1 259 ? 42.694 104.906 148.684 1.00 45.12  ? 259 ARG B N   1 
ATOM 5357 C CA  . ARG B 1 259 ? 43.862 104.893 149.561 1.00 45.17  ? 259 ARG B CA  1 
ATOM 5358 C C   . ARG B 1 259 ? 43.880 106.170 150.382 1.00 44.08  ? 259 ARG B C   1 
ATOM 5359 O O   . ARG B 1 259 ? 43.776 106.131 151.594 1.00 43.89  ? 259 ARG B O   1 
ATOM 5360 C CB  . ARG B 1 259 ? 45.166 104.857 148.762 1.00 47.11  ? 259 ARG B CB  1 
ATOM 5361 C CG  . ARG B 1 259 ? 45.636 103.507 148.212 1.00 49.57  ? 259 ARG B CG  1 
ATOM 5362 C CD  . ARG B 1 259 ? 46.963 103.694 147.430 1.00 50.95  ? 259 ARG B CD  1 
ATOM 5363 N NE  . ARG B 1 259 ? 47.493 102.468 146.832 1.00 52.76  ? 259 ARG B NE  1 
ATOM 5364 C CZ  . ARG B 1 259 ? 48.648 102.407 146.176 1.00 53.03  ? 259 ARG B CZ  1 
ATOM 5365 N NH1 . ARG B 1 259 ? 49.378 103.508 146.037 1.00 53.40  ? 259 ARG B NH1 1 
ATOM 5366 N NH2 . ARG B 1 259 ? 49.081 101.254 145.672 1.00 53.79  ? 259 ARG B NH2 1 
ATOM 5367 N N   . VAL B 1 260 ? 44.025 107.297 149.696 1.00 42.84  ? 260 VAL B N   1 
ATOM 5368 C CA  . VAL B 1 260 ? 44.092 108.581 150.349 1.00 41.98  ? 260 VAL B CA  1 
ATOM 5369 C C   . VAL B 1 260 ? 43.110 108.656 151.479 1.00 42.25  ? 260 VAL B C   1 
ATOM 5370 O O   . VAL B 1 260 ? 43.472 108.991 152.616 1.00 42.15  ? 260 VAL B O   1 
ATOM 5371 C CB  . VAL B 1 260 ? 43.781 109.697 149.371 1.00 42.08  ? 260 VAL B CB  1 
ATOM 5372 C CG1 . VAL B 1 260 ? 43.868 111.072 150.056 1.00 42.00  ? 260 VAL B CG1 1 
ATOM 5373 C CG2 . VAL B 1 260 ? 44.741 109.589 148.218 1.00 42.09  ? 260 VAL B CG2 1 
ATOM 5374 N N   . PHE B 1 261 ? 41.861 108.338 151.186 1.00 42.14  ? 261 PHE B N   1 
ATOM 5375 C CA  . PHE B 1 261 ? 40.893 108.418 152.240 1.00 42.48  ? 261 PHE B CA  1 
ATOM 5376 C C   . PHE B 1 261 ? 41.458 107.677 153.476 1.00 42.39  ? 261 PHE B C   1 
ATOM 5377 O O   . PHE B 1 261 ? 41.522 108.251 154.569 1.00 42.96  ? 261 PHE B O   1 
ATOM 5378 C CB  . PHE B 1 261 ? 39.549 107.861 151.758 1.00 42.23  ? 261 PHE B CB  1 
ATOM 5379 C CG  . PHE B 1 261 ? 38.375 108.522 152.403 1.00 43.01  ? 261 PHE B CG  1 
ATOM 5380 C CD1 . PHE B 1 261 ? 38.257 109.921 152.441 1.00 43.78  ? 261 PHE B CD1 1 
ATOM 5381 C CD2 . PHE B 1 261 ? 37.440 107.759 153.055 1.00 43.79  ? 261 PHE B CD2 1 
ATOM 5382 C CE1 . PHE B 1 261 ? 37.219 110.533 153.144 1.00 44.46  ? 261 PHE B CE1 1 
ATOM 5383 C CE2 . PHE B 1 261 ? 36.400 108.355 153.758 1.00 45.30  ? 261 PHE B CE2 1 
ATOM 5384 C CZ  . PHE B 1 261 ? 36.288 109.742 153.808 1.00 45.06  ? 261 PHE B CZ  1 
ATOM 5385 N N   . GLY B 1 262 ? 41.943 106.452 153.265 1.00 42.44  ? 262 GLY B N   1 
ATOM 5386 C CA  . GLY B 1 262 ? 42.514 105.644 154.334 1.00 41.94  ? 262 GLY B CA  1 
ATOM 5387 C C   . GLY B 1 262 ? 43.576 106.353 155.148 1.00 41.64  ? 262 GLY B C   1 
ATOM 5388 O O   . GLY B 1 262 ? 43.563 106.335 156.382 1.00 41.68  ? 262 GLY B O   1 
ATOM 5389 N N   . TYR B 1 263 ? 44.515 106.973 154.451 1.00 41.66  ? 263 TYR B N   1 
ATOM 5390 C CA  . TYR B 1 263 ? 45.560 107.718 155.119 1.00 41.47  ? 263 TYR B CA  1 
ATOM 5391 C C   . TYR B 1 263 ? 44.866 108.766 155.952 1.00 40.34  ? 263 TYR B C   1 
ATOM 5392 O O   . TYR B 1 263 ? 44.912 108.705 157.183 1.00 40.60  ? 263 TYR B O   1 
ATOM 5393 C CB  . TYR B 1 263 ? 46.471 108.366 154.089 1.00 43.33  ? 263 TYR B CB  1 
ATOM 5394 C CG  . TYR B 1 263 ? 47.221 107.327 153.301 1.00 46.36  ? 263 TYR B CG  1 
ATOM 5395 C CD1 . TYR B 1 263 ? 46.536 106.273 152.683 1.00 47.50  ? 263 TYR B CD1 1 
ATOM 5396 C CD2 . TYR B 1 263 ? 48.607 107.371 153.186 1.00 46.86  ? 263 TYR B CD2 1 
ATOM 5397 C CE1 . TYR B 1 263 ? 47.208 105.284 151.967 1.00 48.48  ? 263 TYR B CE1 1 
ATOM 5398 C CE2 . TYR B 1 263 ? 49.293 106.387 152.472 1.00 48.03  ? 263 TYR B CE2 1 
ATOM 5399 C CZ  . TYR B 1 263 ? 48.580 105.345 151.865 1.00 48.76  ? 263 TYR B CZ  1 
ATOM 5400 O OH  . TYR B 1 263 ? 49.218 104.359 151.145 1.00 48.62  ? 263 TYR B OH  1 
ATOM 5401 N N   . VAL B 1 264 ? 44.202 109.705 155.280 1.00 38.77  ? 264 VAL B N   1 
ATOM 5402 C CA  . VAL B 1 264 ? 43.479 110.777 155.959 1.00 37.87  ? 264 VAL B CA  1 
ATOM 5403 C C   . VAL B 1 264 ? 42.883 110.337 157.293 1.00 37.94  ? 264 VAL B C   1 
ATOM 5404 O O   . VAL B 1 264 ? 43.457 110.579 158.362 1.00 38.25  ? 264 VAL B O   1 
ATOM 5405 C CB  . VAL B 1 264 ? 42.325 111.313 155.091 1.00 38.00  ? 264 VAL B CB  1 
ATOM 5406 C CG1 . VAL B 1 264 ? 41.541 112.413 155.842 1.00 37.80  ? 264 VAL B CG1 1 
ATOM 5407 C CG2 . VAL B 1 264 ? 42.884 111.831 153.791 1.00 38.30  ? 264 VAL B CG2 1 
ATOM 5408 N N   . THR B 1 265 ? 41.726 109.694 157.229 1.00 37.41  ? 265 THR B N   1 
ATOM 5409 C CA  . THR B 1 265 ? 41.068 109.245 158.434 1.00 36.95  ? 265 THR B CA  1 
ATOM 5410 C C   . THR B 1 265 ? 42.121 108.882 159.449 1.00 37.00  ? 265 THR B C   1 
ATOM 5411 O O   . THR B 1 265 ? 42.211 109.503 160.502 1.00 36.56  ? 265 THR B O   1 
ATOM 5412 C CB  . THR B 1 265 ? 40.171 108.049 158.148 1.00 37.28  ? 265 THR B CB  1 
ATOM 5413 O OG1 . THR B 1 265 ? 39.175 108.447 157.197 1.00 37.20  ? 265 THR B OG1 1 
ATOM 5414 C CG2 . THR B 1 265 ? 39.480 107.578 159.425 1.00 36.77  ? 265 THR B CG2 1 
ATOM 5415 N N   . THR B 1 266 ? 42.958 107.915 159.108 1.00 37.26  ? 266 THR B N   1 
ATOM 5416 C CA  . THR B 1 266 ? 44.005 107.501 160.021 1.00 38.76  ? 266 THR B CA  1 
ATOM 5417 C C   . THR B 1 266 ? 44.915 108.619 160.532 1.00 39.84  ? 266 THR B C   1 
ATOM 5418 O O   . THR B 1 266 ? 45.217 108.672 161.715 1.00 39.97  ? 266 THR B O   1 
ATOM 5419 C CB  . THR B 1 266 ? 44.885 106.414 159.398 1.00 38.65  ? 266 THR B CB  1 
ATOM 5420 O OG1 . THR B 1 266 ? 44.198 105.155 159.427 1.00 38.80  ? 266 THR B OG1 1 
ATOM 5421 C CG2 . THR B 1 266 ? 46.169 106.281 160.172 1.00 38.28  ? 266 THR B CG2 1 
ATOM 5422 N N   . MET B 1 267 ? 45.366 109.508 159.659 1.00 41.73  ? 267 MET B N   1 
ATOM 5423 C CA  . MET B 1 267 ? 46.276 110.582 160.088 1.00 43.84  ? 267 MET B CA  1 
ATOM 5424 C C   . MET B 1 267 ? 45.504 111.598 160.894 1.00 44.52  ? 267 MET B C   1 
ATOM 5425 O O   . MET B 1 267 ? 46.075 112.448 161.599 1.00 44.43  ? 267 MET B O   1 
ATOM 5426 C CB  . MET B 1 267 ? 46.892 111.293 158.885 1.00 45.93  ? 267 MET B CB  1 
ATOM 5427 C CG  . MET B 1 267 ? 48.161 112.107 159.177 1.00 46.65  ? 267 MET B CG  1 
ATOM 5428 S SD  . MET B 1 267 ? 49.651 111.095 159.475 1.00 49.47  ? 267 MET B SD  1 
ATOM 5429 C CE  . MET B 1 267 ? 50.184 110.676 157.842 1.00 46.82  ? 267 MET B CE  1 
ATOM 5430 N N   . GLY B 1 268 ? 44.188 111.480 160.782 1.00 45.75  ? 268 GLY B N   1 
ATOM 5431 C CA  . GLY B 1 268 ? 43.278 112.366 161.473 1.00 47.95  ? 268 GLY B CA  1 
ATOM 5432 C C   . GLY B 1 268 ? 43.315 112.246 162.977 1.00 49.06  ? 268 GLY B C   1 
ATOM 5433 O O   . GLY B 1 268 ? 43.655 113.206 163.657 1.00 49.24  ? 268 GLY B O   1 
ATOM 5434 N N   . GLU B 1 269 ? 42.975 111.081 163.511 1.00 50.30  ? 269 GLU B N   1 
ATOM 5435 C CA  . GLU B 1 269 ? 42.950 110.925 164.961 1.00 51.16  ? 269 GLU B CA  1 
ATOM 5436 C C   . GLU B 1 269 ? 44.196 111.446 165.656 1.00 50.13  ? 269 GLU B C   1 
ATOM 5437 O O   . GLU B 1 269 ? 44.128 111.894 166.797 1.00 49.79  ? 269 GLU B O   1 
ATOM 5438 C CB  . GLU B 1 269 ? 42.676 109.454 165.327 1.00 53.64  ? 269 GLU B CB  1 
ATOM 5439 C CG  . GLU B 1 269 ? 41.335 108.938 164.769 1.00 57.75  ? 269 GLU B CG  1 
ATOM 5440 C CD  . GLU B 1 269 ? 40.128 109.805 165.179 1.00 60.76  ? 269 GLU B CD  1 
ATOM 5441 O OE1 . GLU B 1 269 ? 39.749 109.775 166.380 1.00 62.55  ? 269 GLU B OE1 1 
ATOM 5442 O OE2 . GLU B 1 269 ? 39.565 110.516 164.293 1.00 62.58  ? 269 GLU B OE2 1 
ATOM 5443 N N   . LEU B 1 270 ? 45.330 111.410 164.966 1.00 49.13  ? 270 LEU B N   1 
ATOM 5444 C CA  . LEU B 1 270 ? 46.557 111.906 165.568 1.00 48.53  ? 270 LEU B CA  1 
ATOM 5445 C C   . LEU B 1 270 ? 46.382 113.393 165.785 1.00 47.97  ? 270 LEU B C   1 
ATOM 5446 O O   . LEU B 1 270 ? 47.032 113.997 166.644 1.00 47.63  ? 270 LEU B O   1 
ATOM 5447 C CB  . LEU B 1 270 ? 47.754 111.611 164.676 1.00 48.25  ? 270 LEU B CB  1 
ATOM 5448 C CG  . LEU B 1 270 ? 48.171 110.130 164.651 1.00 48.82  ? 270 LEU B CG  1 
ATOM 5449 C CD1 . LEU B 1 270 ? 49.464 110.007 163.871 1.00 48.65  ? 270 LEU B CD1 1 
ATOM 5450 C CD2 . LEU B 1 270 ? 48.367 109.589 166.065 1.00 47.54  ? 270 LEU B CD2 1 
ATOM 5451 N N   . LEU B 1 271 ? 45.484 113.987 165.018 1.00 48.23  ? 271 LEU B N   1 
ATOM 5452 C CA  . LEU B 1 271 ? 45.221 115.401 165.181 1.00 48.68  ? 271 LEU B CA  1 
ATOM 5453 C C   . LEU B 1 271 ? 44.205 115.532 166.330 1.00 49.34  ? 271 LEU B C   1 
ATOM 5454 O O   . LEU B 1 271 ? 44.349 116.358 167.221 1.00 49.39  ? 271 LEU B O   1 
ATOM 5455 C CB  . LEU B 1 271 ? 44.668 115.981 163.867 1.00 48.84  ? 271 LEU B CB  1 
ATOM 5456 C CG  . LEU B 1 271 ? 44.154 117.436 163.908 1.00 48.84  ? 271 LEU B CG  1 
ATOM 5457 C CD1 . LEU B 1 271 ? 45.352 118.316 164.075 1.00 48.91  ? 271 LEU B CD1 1 
ATOM 5458 C CD2 . LEU B 1 271 ? 43.417 117.812 162.634 1.00 48.79  ? 271 LEU B CD2 1 
ATOM 5459 N N   . ASN B 1 272 ? 43.207 114.663 166.324 1.00 50.32  ? 272 ASN B N   1 
ATOM 5460 C CA  . ASN B 1 272 ? 42.172 114.656 167.344 1.00 52.14  ? 272 ASN B CA  1 
ATOM 5461 C C   . ASN B 1 272 ? 42.805 114.814 168.757 1.00 53.12  ? 272 ASN B C   1 
ATOM 5462 O O   . ASN B 1 272 ? 42.388 115.656 169.568 1.00 52.36  ? 272 ASN B O   1 
ATOM 5463 C CB  . ASN B 1 272 ? 41.445 113.325 167.197 1.00 51.24  ? 272 ASN B CB  1 
ATOM 5464 C CG  . ASN B 1 272 ? 40.086 113.301 167.879 1.00 52.15  ? 272 ASN B CG  1 
ATOM 5465 O OD1 . ASN B 1 272 ? 39.237 114.171 167.649 1.00 52.13  ? 272 ASN B OD1 1 
ATOM 5466 N ND2 . ASN B 1 272 ? 39.861 112.282 168.710 1.00 52.18  ? 272 ASN B ND2 1 
ATOM 5467 N N   . ALA B 1 273 ? 43.830 114.001 169.005 1.00 54.76  ? 273 ALA B N   1 
ATOM 5468 C CA  . ALA B 1 273 ? 44.537 113.971 170.267 1.00 56.10  ? 273 ALA B CA  1 
ATOM 5469 C C   . ALA B 1 273 ? 45.085 115.339 170.596 1.00 56.84  ? 273 ALA B C   1 
ATOM 5470 O O   . ALA B 1 273 ? 44.705 115.965 171.592 1.00 55.89  ? 273 ALA B O   1 
ATOM 5471 C CB  . ALA B 1 273 ? 45.667 112.959 170.200 1.00 55.53  ? 273 ALA B CB  1 
ATOM 5472 N N   . SER B 1 274 ? 46.001 115.792 169.754 1.00 58.57  ? 274 SER B N   1 
ATOM 5473 C CA  . SER B 1 274 ? 46.604 117.087 169.951 1.00 60.85  ? 274 SER B CA  1 
ATOM 5474 C C   . SER B 1 274 ? 45.528 118.091 170.356 1.00 61.90  ? 274 SER B C   1 
ATOM 5475 O O   . SER B 1 274 ? 45.674 118.823 171.340 1.00 62.00  ? 274 SER B O   1 
ATOM 5476 C CB  . SER B 1 274 ? 47.313 117.528 168.664 1.00 60.20  ? 274 SER B CB  1 
ATOM 5477 O OG  . SER B 1 274 ? 46.541 117.204 167.522 1.00 60.45  ? 274 SER B OG  1 
ATOM 5478 N N   . ILE B 1 275 ? 44.425 118.097 169.622 1.00 63.53  ? 275 ILE B N   1 
ATOM 5479 C CA  . ILE B 1 275 ? 43.369 119.033 169.925 1.00 65.42  ? 275 ILE B CA  1 
ATOM 5480 C C   . ILE B 1 275 ? 42.783 118.853 171.320 1.00 66.56  ? 275 ILE B C   1 
ATOM 5481 O O   . ILE B 1 275 ? 42.928 119.729 172.185 1.00 67.07  ? 275 ILE B O   1 
ATOM 5482 C CB  . ILE B 1 275 ? 42.261 118.940 168.894 1.00 65.44  ? 275 ILE B CB  1 
ATOM 5483 C CG1 . ILE B 1 275 ? 42.877 119.047 167.501 1.00 66.18  ? 275 ILE B CG1 1 
ATOM 5484 C CG2 . ILE B 1 275 ? 41.276 120.076 169.104 1.00 65.85  ? 275 ILE B CG2 1 
ATOM 5485 C CD1 . ILE B 1 275 ? 41.923 118.782 166.372 1.00 67.63  ? 275 ILE B CD1 1 
ATOM 5486 N N   . MET B 1 276 ? 42.148 117.715 171.558 1.00 68.06  ? 276 MET B N   1 
ATOM 5487 C CA  . MET B 1 276 ? 41.525 117.477 172.847 1.00 69.29  ? 276 MET B CA  1 
ATOM 5488 C C   . MET B 1 276 ? 42.420 117.680 174.080 1.00 68.50  ? 276 MET B C   1 
ATOM 5489 O O   . MET B 1 276 ? 41.951 118.139 175.135 1.00 68.32  ? 276 MET B O   1 
ATOM 5490 C CB  . MET B 1 276 ? 40.936 116.080 172.843 1.00 72.07  ? 276 MET B CB  1 
ATOM 5491 C CG  . MET B 1 276 ? 40.110 115.793 174.055 1.00 76.29  ? 276 MET B CG  1 
ATOM 5492 S SD  . MET B 1 276 ? 39.256 114.230 173.834 1.00 81.88  ? 276 MET B SD  1 
ATOM 5493 C CE  . MET B 1 276 ? 40.530 112.957 174.556 1.00 79.72  ? 276 MET B CE  1 
ATOM 5494 N N   . PHE B 1 277 ? 43.700 117.348 173.936 1.00 67.17  ? 277 PHE B N   1 
ATOM 5495 C CA  . PHE B 1 277 ? 44.667 117.501 175.014 1.00 66.04  ? 277 PHE B CA  1 
ATOM 5496 C C   . PHE B 1 277 ? 44.584 118.959 175.503 1.00 64.03  ? 277 PHE B C   1 
ATOM 5497 O O   . PHE B 1 277 ? 44.986 119.263 176.619 1.00 63.93  ? 277 PHE B O   1 
ATOM 5498 C CB  . PHE B 1 277 ? 46.078 117.198 174.472 1.00 67.17  ? 277 PHE B CB  1 
ATOM 5499 C CG  . PHE B 1 277 ? 47.109 116.902 175.538 1.00 68.25  ? 277 PHE B CG  1 
ATOM 5500 C CD1 . PHE B 1 277 ? 47.167 115.647 176.156 1.00 69.07  ? 277 PHE B CD1 1 
ATOM 5501 C CD2 . PHE B 1 277 ? 48.022 117.880 175.924 1.00 68.46  ? 277 PHE B CD2 1 
ATOM 5502 C CE1 . PHE B 1 277 ? 48.126 115.380 177.141 1.00 69.16  ? 277 PHE B CE1 1 
ATOM 5503 C CE2 . PHE B 1 277 ? 48.980 117.629 176.902 1.00 68.75  ? 277 PHE B CE2 1 
ATOM 5504 C CZ  . PHE B 1 277 ? 49.038 116.380 177.515 1.00 69.00  ? 277 PHE B CZ  1 
ATOM 5505 N N   . PHE B 1 278 ? 44.013 119.839 174.677 1.00 61.92  ? 278 PHE B N   1 
ATOM 5506 C CA  . PHE B 1 278 ? 43.916 121.267 174.993 1.00 59.68  ? 278 PHE B CA  1 
ATOM 5507 C C   . PHE B 1 278 ? 42.463 121.740 175.103 1.00 57.30  ? 278 PHE B C   1 
ATOM 5508 O O   . PHE B 1 278 ? 42.151 122.792 175.675 1.00 57.18  ? 278 PHE B O   1 
ATOM 5509 C CB  . PHE B 1 278 ? 44.625 122.082 173.906 1.00 59.68  ? 278 PHE B CB  1 
ATOM 5510 C CG  . PHE B 1 278 ? 46.079 121.705 173.685 1.00 59.95  ? 278 PHE B CG  1 
ATOM 5511 C CD1 . PHE B 1 278 ? 46.578 120.414 173.954 1.00 60.19  ? 278 PHE B CD1 1 
ATOM 5512 C CD2 . PHE B 1 278 ? 46.952 122.657 173.176 1.00 59.80  ? 278 PHE B CD2 1 
ATOM 5513 C CE1 . PHE B 1 278 ? 47.931 120.096 173.714 1.00 60.49  ? 278 PHE B CE1 1 
ATOM 5514 C CE2 . PHE B 1 278 ? 48.301 122.357 172.933 1.00 60.13  ? 278 PHE B CE2 1 
ATOM 5515 C CZ  . PHE B 1 278 ? 48.793 121.076 173.200 1.00 60.45  ? 278 PHE B CZ  1 
ATOM 5516 N N   . ALA B 1 279 ? 41.590 120.940 174.519 1.00 54.98  ? 279 ALA B N   1 
ATOM 5517 C CA  . ALA B 1 279 ? 40.182 121.200 174.510 1.00 52.68  ? 279 ALA B CA  1 
ATOM 5518 C C   . ALA B 1 279 ? 39.689 121.857 175.805 1.00 51.12  ? 279 ALA B C   1 
ATOM 5519 O O   . ALA B 1 279 ? 39.356 123.050 175.789 1.00 49.60  ? 279 ALA B O   1 
ATOM 5520 C CB  . ALA B 1 279 ? 39.452 119.904 174.246 1.00 53.82  ? 279 ALA B CB  1 
ATOM 5521 N N   . PRO B 1 280 ? 39.652 121.099 176.937 1.00 50.20  ? 280 PRO B N   1 
ATOM 5522 C CA  . PRO B 1 280 ? 39.187 121.627 178.216 1.00 49.77  ? 280 PRO B CA  1 
ATOM 5523 C C   . PRO B 1 280 ? 39.636 123.016 178.435 1.00 49.06  ? 280 PRO B C   1 
ATOM 5524 O O   . PRO B 1 280 ? 38.831 123.934 178.537 1.00 49.02  ? 280 PRO B O   1 
ATOM 5525 C CB  . PRO B 1 280 ? 39.800 120.643 179.205 1.00 49.57  ? 280 PRO B CB  1 
ATOM 5526 C CG  . PRO B 1 280 ? 39.507 119.398 178.523 1.00 49.83  ? 280 PRO B CG  1 
ATOM 5527 C CD  . PRO B 1 280 ? 40.234 119.766 177.202 1.00 50.03  ? 280 PRO B CD  1 
ATOM 5528 N N   . LEU B 1 281 ? 40.947 123.162 178.488 1.00 48.14  ? 281 LEU B N   1 
ATOM 5529 C CA  . LEU B 1 281 ? 41.525 124.467 178.731 1.00 47.74  ? 281 LEU B CA  1 
ATOM 5530 C C   . LEU B 1 281 ? 40.878 125.458 177.792 1.00 47.12  ? 281 LEU B C   1 
ATOM 5531 O O   . LEU B 1 281 ? 40.268 126.441 178.211 1.00 46.53  ? 281 LEU B O   1 
ATOM 5532 C CB  . LEU B 1 281 ? 43.036 124.436 178.486 1.00 48.32  ? 281 LEU B CB  1 
ATOM 5533 C CG  . LEU B 1 281 ? 43.979 123.513 179.303 1.00 49.24  ? 281 LEU B CG  1 
ATOM 5534 C CD1 . LEU B 1 281 ? 45.438 123.837 178.920 1.00 49.00  ? 281 LEU B CD1 1 
ATOM 5535 C CD2 . LEU B 1 281 ? 43.787 123.704 180.816 1.00 49.10  ? 281 LEU B CD2 1 
ATOM 5536 N N   . ILE B 1 282 ? 41.020 125.164 176.512 1.00 47.16  ? 282 ILE B N   1 
ATOM 5537 C CA  . ILE B 1 282 ? 40.482 125.981 175.457 1.00 47.42  ? 282 ILE B CA  1 
ATOM 5538 C C   . ILE B 1 282 ? 39.062 126.413 175.787 1.00 48.42  ? 282 ILE B C   1 
ATOM 5539 O O   . ILE B 1 282 ? 38.741 127.605 175.875 1.00 47.38  ? 282 ILE B O   1 
ATOM 5540 C CB  . ILE B 1 282 ? 40.503 125.165 174.177 1.00 46.85  ? 282 ILE B CB  1 
ATOM 5541 C CG1 . ILE B 1 282 ? 41.955 124.838 173.816 1.00 45.93  ? 282 ILE B CG1 1 
ATOM 5542 C CG2 . ILE B 1 282 ? 39.793 125.904 173.088 1.00 46.72  ? 282 ILE B CG2 1 
ATOM 5543 C CD1 . ILE B 1 282 ? 42.113 123.893 172.662 1.00 45.12  ? 282 ILE B CD1 1 
ATOM 5544 N N   . ILE B 1 283 ? 38.224 125.408 175.982 1.00 49.96  ? 283 ILE B N   1 
ATOM 5545 C CA  . ILE B 1 283 ? 36.829 125.609 176.298 1.00 52.08  ? 283 ILE B CA  1 
ATOM 5546 C C   . ILE B 1 283 ? 36.620 126.512 177.479 1.00 54.36  ? 283 ILE B C   1 
ATOM 5547 O O   . ILE B 1 283 ? 36.076 127.587 177.338 1.00 54.30  ? 283 ILE B O   1 
ATOM 5548 C CB  . ILE B 1 283 ? 36.157 124.280 176.587 1.00 52.07  ? 283 ILE B CB  1 
ATOM 5549 C CG1 . ILE B 1 283 ? 36.435 123.333 175.424 1.00 51.67  ? 283 ILE B CG1 1 
ATOM 5550 C CG2 . ILE B 1 283 ? 34.660 124.496 176.805 1.00 52.03  ? 283 ILE B CG2 1 
ATOM 5551 C CD1 . ILE B 1 283 ? 36.047 123.892 174.084 1.00 51.82  ? 283 ILE B CD1 1 
ATOM 5552 N N   . ASN B 1 284 ? 37.053 126.072 178.649 1.00 57.36  ? 284 ASN B N   1 
ATOM 5553 C CA  . ASN B 1 284 ? 36.861 126.884 179.837 1.00 60.41  ? 284 ASN B CA  1 
ATOM 5554 C C   . ASN B 1 284 ? 37.438 128.286 179.666 1.00 62.05  ? 284 ASN B C   1 
ATOM 5555 O O   . ASN B 1 284 ? 36.882 129.271 180.175 1.00 62.25  ? 284 ASN B O   1 
ATOM 5556 C CB  . ASN B 1 284 ? 37.483 126.218 181.065 1.00 61.69  ? 284 ASN B CB  1 
ATOM 5557 C CG  . ASN B 1 284 ? 36.819 124.901 181.406 1.00 62.70  ? 284 ASN B CG  1 
ATOM 5558 O OD1 . ASN B 1 284 ? 35.594 124.760 181.297 1.00 63.26  ? 284 ASN B OD1 1 
ATOM 5559 N ND2 . ASN B 1 284 ? 37.620 123.926 181.828 1.00 62.82  ? 284 ASN B ND2 1 
ATOM 5560 N N   . ARG B 1 285 ? 38.558 128.389 178.966 1.00 63.13  ? 285 ARG B N   1 
ATOM 5561 C CA  . ARG B 1 285 ? 39.135 129.699 178.772 1.00 64.34  ? 285 ARG B CA  1 
ATOM 5562 C C   . ARG B 1 285 ? 38.147 130.488 177.928 1.00 63.31  ? 285 ARG B C   1 
ATOM 5563 O O   . ARG B 1 285 ? 37.931 131.689 178.145 1.00 63.07  ? 285 ARG B O   1 
ATOM 5564 C CB  . ARG B 1 285 ? 40.483 129.592 178.054 1.00 67.40  ? 285 ARG B CB  1 
ATOM 5565 C CG  . ARG B 1 285 ? 41.670 129.183 178.954 1.00 71.57  ? 285 ARG B CG  1 
ATOM 5566 C CD  . ARG B 1 285 ? 42.965 128.961 178.105 1.00 76.80  ? 285 ARG B CD  1 
ATOM 5567 N NE  . ARG B 1 285 ? 44.173 128.623 178.885 1.00 80.43  ? 285 ARG B NE  1 
ATOM 5568 C CZ  . ARG B 1 285 ? 45.343 128.231 178.360 1.00 81.82  ? 285 ARG B CZ  1 
ATOM 5569 N NH1 . ARG B 1 285 ? 45.492 128.115 177.039 1.00 82.57  ? 285 ARG B NH1 1 
ATOM 5570 N NH2 . ARG B 1 285 ? 46.375 127.957 179.159 1.00 81.59  ? 285 ARG B NH2 1 
ATOM 5571 N N   . ILE B 1 286 ? 37.512 129.788 176.990 1.00 62.60  ? 286 ILE B N   1 
ATOM 5572 C CA  . ILE B 1 286 ? 36.555 130.408 176.075 1.00 61.35  ? 286 ILE B CA  1 
ATOM 5573 C C   . ILE B 1 286 ? 35.118 130.417 176.554 1.00 60.65  ? 286 ILE B C   1 
ATOM 5574 O O   . ILE B 1 286 ? 34.550 131.474 176.823 1.00 61.05  ? 286 ILE B O   1 
ATOM 5575 C CB  . ILE B 1 286 ? 36.570 129.714 174.735 1.00 61.01  ? 286 ILE B CB  1 
ATOM 5576 C CG1 . ILE B 1 286 ? 37.998 129.655 174.210 1.00 60.76  ? 286 ILE B CG1 1 
ATOM 5577 C CG2 . ILE B 1 286 ? 35.643 130.453 173.790 1.00 60.35  ? 286 ILE B CG2 1 
ATOM 5578 C CD1 . ILE B 1 286 ? 38.173 128.792 173.009 1.00 60.96  ? 286 ILE B CD1 1 
ATOM 5579 N N   . GLY B 1 287 ? 34.531 129.229 176.618 1.00 59.07  ? 287 GLY B N   1 
ATOM 5580 C CA  . GLY B 1 287 ? 33.155 129.110 177.039 1.00 56.71  ? 287 GLY B CA  1 
ATOM 5581 C C   . GLY B 1 287 ? 32.408 128.241 176.059 1.00 54.40  ? 287 GLY B C   1 
ATOM 5582 O O   . GLY B 1 287 ? 32.752 128.184 174.883 1.00 54.21  ? 287 GLY B O   1 
ATOM 5583 N N   . GLY B 1 288 ? 31.381 127.565 176.545 1.00 52.43  ? 288 GLY B N   1 
ATOM 5584 C CA  . GLY B 1 288 ? 30.613 126.700 175.683 1.00 50.47  ? 288 GLY B CA  1 
ATOM 5585 C C   . GLY B 1 288 ? 30.010 127.398 174.479 1.00 48.58  ? 288 GLY B C   1 
ATOM 5586 O O   . GLY B 1 288 ? 30.426 127.152 173.336 1.00 47.96  ? 288 GLY B O   1 
ATOM 5587 N N   . LYS B 1 289 ? 29.029 128.266 174.729 1.00 46.58  ? 289 LYS B N   1 
ATOM 5588 C CA  . LYS B 1 289 ? 28.350 128.985 173.653 1.00 44.31  ? 289 LYS B CA  1 
ATOM 5589 C C   . LYS B 1 289 ? 29.289 129.191 172.478 1.00 42.66  ? 289 LYS B C   1 
ATOM 5590 O O   . LYS B 1 289 ? 28.945 128.950 171.333 1.00 42.44  ? 289 LYS B O   1 
ATOM 5591 C CB  . LYS B 1 289 ? 27.812 130.333 174.150 1.00 44.54  ? 289 LYS B CB  1 
ATOM 5592 C CG  . LYS B 1 289 ? 27.276 131.196 173.023 1.00 44.83  ? 289 LYS B CG  1 
ATOM 5593 C CD  . LYS B 1 289 ? 26.355 132.302 173.494 1.00 45.88  ? 289 LYS B CD  1 
ATOM 5594 C CE  . LYS B 1 289 ? 25.693 133.001 172.299 1.00 45.71  ? 289 LYS B CE  1 
ATOM 5595 N NZ  . LYS B 1 289 ? 24.857 134.177 172.698 1.00 45.71  ? 289 LYS B NZ  1 
ATOM 5596 N N   . ASN B 1 290 ? 30.502 129.593 172.783 1.00 41.19  ? 290 ASN B N   1 
ATOM 5597 C CA  . ASN B 1 290 ? 31.486 129.820 171.770 1.00 40.41  ? 290 ASN B CA  1 
ATOM 5598 C C   . ASN B 1 290 ? 31.949 128.546 171.121 1.00 39.51  ? 290 ASN B C   1 
ATOM 5599 O O   . ASN B 1 290 ? 31.810 128.372 169.918 1.00 39.10  ? 290 ASN B O   1 
ATOM 5600 C CB  . ASN B 1 290 ? 32.626 130.545 172.421 1.00 40.99  ? 290 ASN B CB  1 
ATOM 5601 C CG  . ASN B 1 290 ? 32.164 131.803 173.060 1.00 42.38  ? 290 ASN B CG  1 
ATOM 5602 O OD1 . ASN B 1 290 ? 32.201 132.870 172.449 1.00 42.91  ? 290 ASN B OD1 1 
ATOM 5603 N ND2 . ASN B 1 290 ? 31.651 131.688 174.273 1.00 42.95  ? 290 ASN B ND2 1 
ATOM 5604 N N   . ALA B 1 291 ? 32.485 127.648 171.930 1.00 38.86  ? 291 ALA B N   1 
ATOM 5605 C CA  . ALA B 1 291 ? 32.967 126.372 171.427 1.00 37.75  ? 291 ALA B CA  1 
ATOM 5606 C C   . ALA B 1 291 ? 32.154 125.916 170.213 1.00 36.33  ? 291 ALA B C   1 
ATOM 5607 O O   . ALA B 1 291 ? 32.682 125.759 169.103 1.00 35.63  ? 291 ALA B O   1 
ATOM 5608 C CB  . ALA B 1 291 ? 32.889 125.313 172.538 1.00 38.99  ? 291 ALA B CB  1 
ATOM 5609 N N   . LEU B 1 292 ? 30.857 125.730 170.435 1.00 34.87  ? 292 LEU B N   1 
ATOM 5610 C CA  . LEU B 1 292 ? 29.958 125.268 169.394 1.00 33.20  ? 292 LEU B CA  1 
ATOM 5611 C C   . LEU B 1 292 ? 30.055 126.100 168.141 1.00 32.16  ? 292 LEU B C   1 
ATOM 5612 O O   . LEU B 1 292 ? 30.261 125.587 167.044 1.00 31.90  ? 292 LEU B O   1 
ATOM 5613 C CB  . LEU B 1 292 ? 28.522 125.282 169.902 1.00 34.00  ? 292 LEU B CB  1 
ATOM 5614 C CG  . LEU B 1 292 ? 28.286 124.501 171.196 1.00 34.80  ? 292 LEU B CG  1 
ATOM 5615 C CD1 . LEU B 1 292 ? 26.788 124.373 171.435 1.00 34.59  ? 292 LEU B CD1 1 
ATOM 5616 C CD2 . LEU B 1 292 ? 28.940 123.136 171.118 1.00 35.48  ? 292 LEU B CD2 1 
ATOM 5617 N N   . LEU B 1 293 ? 29.898 127.397 168.317 1.00 30.67  ? 293 LEU B N   1 
ATOM 5618 C CA  . LEU B 1 293 ? 29.968 128.314 167.212 1.00 29.80  ? 293 LEU B CA  1 
ATOM 5619 C C   . LEU B 1 293 ? 31.251 128.111 166.423 1.00 29.73  ? 293 LEU B C   1 
ATOM 5620 O O   . LEU B 1 293 ? 31.206 127.722 165.264 1.00 29.37  ? 293 LEU B O   1 
ATOM 5621 C CB  . LEU B 1 293 ? 29.872 129.722 167.750 1.00 29.57  ? 293 LEU B CB  1 
ATOM 5622 C CG  . LEU B 1 293 ? 28.613 129.856 168.605 1.00 30.64  ? 293 LEU B CG  1 
ATOM 5623 C CD1 . LEU B 1 293 ? 28.641 131.152 169.391 1.00 31.42  ? 293 LEU B CD1 1 
ATOM 5624 C CD2 . LEU B 1 293 ? 27.394 129.789 167.716 1.00 29.75  ? 293 LEU B CD2 1 
ATOM 5625 N N   . LEU B 1 294 ? 32.402 128.352 167.033 1.00 30.36  ? 294 LEU B N   1 
ATOM 5626 C CA  . LEU B 1 294 ? 33.650 128.165 166.300 1.00 30.76  ? 294 LEU B CA  1 
ATOM 5627 C C   . LEU B 1 294 ? 33.633 126.816 165.579 1.00 30.59  ? 294 LEU B C   1 
ATOM 5628 O O   . LEU B 1 294 ? 34.001 126.724 164.414 1.00 30.65  ? 294 LEU B O   1 
ATOM 5629 C CB  . LEU B 1 294 ? 34.854 128.229 167.240 1.00 32.26  ? 294 LEU B CB  1 
ATOM 5630 C CG  . LEU B 1 294 ? 36.189 128.209 166.486 1.00 32.03  ? 294 LEU B CG  1 
ATOM 5631 C CD1 . LEU B 1 294 ? 36.394 129.567 165.848 1.00 33.05  ? 294 LEU B CD1 1 
ATOM 5632 C CD2 . LEU B 1 294 ? 37.342 127.902 167.412 1.00 32.09  ? 294 LEU B CD2 1 
ATOM 5633 N N   . ALA B 1 295 ? 33.194 125.776 166.277 1.00 30.56  ? 295 ALA B N   1 
ATOM 5634 C CA  . ALA B 1 295 ? 33.108 124.444 165.698 1.00 30.77  ? 295 ALA B CA  1 
ATOM 5635 C C   . ALA B 1 295 ? 32.210 124.466 164.460 1.00 30.88  ? 295 ALA B C   1 
ATOM 5636 O O   . ALA B 1 295 ? 32.617 124.055 163.372 1.00 30.51  ? 295 ALA B O   1 
ATOM 5637 C CB  . ALA B 1 295 ? 32.555 123.484 166.738 1.00 32.00  ? 295 ALA B CB  1 
ATOM 5638 N N   . GLY B 1 296 ? 30.986 124.955 164.636 1.00 30.93  ? 296 GLY B N   1 
ATOM 5639 C CA  . GLY B 1 296 ? 30.031 125.042 163.536 1.00 31.19  ? 296 GLY B CA  1 
ATOM 5640 C C   . GLY B 1 296 ? 30.515 125.879 162.360 1.00 30.97  ? 296 GLY B C   1 
ATOM 5641 O O   . GLY B 1 296 ? 30.303 125.508 161.203 1.00 30.95  ? 296 GLY B O   1 
ATOM 5642 N N   . THR B 1 297 ? 31.143 127.017 162.650 1.00 30.26  ? 297 THR B N   1 
ATOM 5643 C CA  . THR B 1 297 ? 31.683 127.871 161.604 1.00 29.21  ? 297 THR B CA  1 
ATOM 5644 C C   . THR B 1 297 ? 32.594 126.982 160.765 1.00 27.94  ? 297 THR B C   1 
ATOM 5645 O O   . THR B 1 297 ? 32.488 126.940 159.541 1.00 26.79  ? 297 THR B O   1 
ATOM 5646 C CB  . THR B 1 297 ? 32.505 129.031 162.208 1.00 29.32  ? 297 THR B CB  1 
ATOM 5647 O OG1 . THR B 1 297 ? 31.631 129.926 162.899 1.00 30.08  ? 297 THR B OG1 1 
ATOM 5648 C CG2 . THR B 1 297 ? 33.210 129.809 161.134 1.00 29.71  ? 297 THR B CG2 1 
ATOM 5649 N N   . ILE B 1 298 ? 33.469 126.243 161.437 1.00 26.86  ? 298 ILE B N   1 
ATOM 5650 C CA  . ILE B 1 298 ? 34.390 125.355 160.744 1.00 27.03  ? 298 ILE B CA  1 
ATOM 5651 C C   . ILE B 1 298 ? 33.675 124.532 159.680 1.00 26.65  ? 298 ILE B C   1 
ATOM 5652 O O   . ILE B 1 298 ? 33.991 124.615 158.490 1.00 26.73  ? 298 ILE B O   1 
ATOM 5653 C CB  . ILE B 1 298 ? 35.079 124.390 161.716 1.00 26.73  ? 298 ILE B CB  1 
ATOM 5654 C CG1 . ILE B 1 298 ? 35.917 125.172 162.728 1.00 27.65  ? 298 ILE B CG1 1 
ATOM 5655 C CG2 . ILE B 1 298 ? 35.963 123.424 160.933 1.00 27.09  ? 298 ILE B CG2 1 
ATOM 5656 C CD1 . ILE B 1 298 ? 36.643 124.298 163.744 1.00 28.49  ? 298 ILE B CD1 1 
ATOM 5657 N N   . MET B 1 299 ? 32.716 123.729 160.122 1.00 26.96  ? 299 MET B N   1 
ATOM 5658 C CA  . MET B 1 299 ? 31.950 122.884 159.220 1.00 26.44  ? 299 MET B CA  1 
ATOM 5659 C C   . MET B 1 299 ? 31.413 123.697 158.058 1.00 26.33  ? 299 MET B C   1 
ATOM 5660 O O   . MET B 1 299 ? 31.626 123.354 156.894 1.00 26.03  ? 299 MET B O   1 
ATOM 5661 C CB  . MET B 1 299 ? 30.806 122.240 159.975 1.00 26.17  ? 299 MET B CB  1 
ATOM 5662 C CG  . MET B 1 299 ? 31.297 121.353 161.063 1.00 26.49  ? 299 MET B CG  1 
ATOM 5663 S SD  . MET B 1 299 ? 29.937 120.573 161.868 1.00 28.34  ? 299 MET B SD  1 
ATOM 5664 C CE  . MET B 1 299 ? 29.761 121.622 163.291 1.00 26.81  ? 299 MET B CE  1 
ATOM 5665 N N   . SER B 1 300 ? 30.710 124.775 158.374 1.00 25.68  ? 300 SER B N   1 
ATOM 5666 C CA  . SER B 1 300 ? 30.187 125.612 157.328 1.00 24.64  ? 300 SER B CA  1 
ATOM 5667 C C   . SER B 1 300 ? 31.329 125.805 156.324 1.00 24.27  ? 300 SER B C   1 
ATOM 5668 O O   . SER B 1 300 ? 31.229 125.383 155.173 1.00 24.32  ? 300 SER B O   1 
ATOM 5669 C CB  . SER B 1 300 ? 29.711 126.962 157.894 1.00 23.91  ? 300 SER B CB  1 
ATOM 5670 O OG  . SER B 1 300 ? 28.426 126.875 158.503 1.00 21.82  ? 300 SER B OG  1 
ATOM 5671 N N   . VAL B 1 301 ? 32.433 126.392 156.764 1.00 23.57  ? 301 VAL B N   1 
ATOM 5672 C CA  . VAL B 1 301 ? 33.527 126.604 155.851 1.00 24.02  ? 301 VAL B CA  1 
ATOM 5673 C C   . VAL B 1 301 ? 33.966 125.317 155.200 1.00 25.12  ? 301 VAL B C   1 
ATOM 5674 O O   . VAL B 1 301 ? 34.474 125.338 154.097 1.00 26.00  ? 301 VAL B O   1 
ATOM 5675 C CB  . VAL B 1 301 ? 34.718 127.255 156.537 1.00 23.07  ? 301 VAL B CB  1 
ATOM 5676 C CG1 . VAL B 1 301 ? 35.947 127.172 155.657 1.00 22.58  ? 301 VAL B CG1 1 
ATOM 5677 C CG2 . VAL B 1 301 ? 34.402 128.703 156.809 1.00 22.76  ? 301 VAL B CG2 1 
ATOM 5678 N N   . ARG B 1 302 ? 33.763 124.180 155.847 1.00 26.50  ? 302 ARG B N   1 
ATOM 5679 C CA  . ARG B 1 302 ? 34.171 122.929 155.205 1.00 27.80  ? 302 ARG B CA  1 
ATOM 5680 C C   . ARG B 1 302 ? 33.280 122.583 154.030 1.00 26.87  ? 302 ARG B C   1 
ATOM 5681 O O   . ARG B 1 302 ? 33.694 121.897 153.101 1.00 26.37  ? 302 ARG B O   1 
ATOM 5682 C CB  . ARG B 1 302 ? 34.131 121.750 156.167 1.00 30.65  ? 302 ARG B CB  1 
ATOM 5683 C CG  . ARG B 1 302 ? 34.591 120.446 155.504 1.00 33.37  ? 302 ARG B CG  1 
ATOM 5684 C CD  . ARG B 1 302 ? 34.288 119.257 156.375 1.00 35.84  ? 302 ARG B CD  1 
ATOM 5685 N NE  . ARG B 1 302 ? 34.736 117.997 155.802 1.00 37.85  ? 302 ARG B NE  1 
ATOM 5686 C CZ  . ARG B 1 302 ? 34.432 116.808 156.321 1.00 39.24  ? 302 ARG B CZ  1 
ATOM 5687 N NH1 . ARG B 1 302 ? 33.683 116.730 157.414 1.00 39.77  ? 302 ARG B NH1 1 
ATOM 5688 N NH2 . ARG B 1 302 ? 34.874 115.688 155.759 1.00 39.30  ? 302 ARG B NH2 1 
ATOM 5689 N N   . ILE B 1 303 ? 32.042 123.046 154.082 1.00 26.55  ? 303 ILE B N   1 
ATOM 5690 C CA  . ILE B 1 303 ? 31.063 122.756 153.040 1.00 27.57  ? 303 ILE B CA  1 
ATOM 5691 C C   . ILE B 1 303 ? 31.215 123.711 151.911 1.00 28.33  ? 303 ILE B C   1 
ATOM 5692 O O   . ILE B 1 303 ? 31.466 123.362 150.759 1.00 28.73  ? 303 ILE B O   1 
ATOM 5693 C CB  . ILE B 1 303 ? 29.668 122.912 153.602 1.00 27.63  ? 303 ILE B CB  1 
ATOM 5694 C CG1 . ILE B 1 303 ? 29.558 122.071 154.870 1.00 28.24  ? 303 ILE B CG1 1 
ATOM 5695 C CG2 . ILE B 1 303 ? 28.658 122.496 152.585 1.00 27.71  ? 303 ILE B CG2 1 
ATOM 5696 C CD1 . ILE B 1 303 ? 28.178 122.006 155.443 1.00 29.74  ? 303 ILE B CD1 1 
ATOM 5697 N N   . ILE B 1 304 ? 31.017 124.961 152.265 1.00 28.88  ? 304 ILE B N   1 
ATOM 5698 C CA  . ILE B 1 304 ? 31.124 126.025 151.297 1.00 29.20  ? 304 ILE B CA  1 
ATOM 5699 C C   . ILE B 1 304 ? 32.459 125.850 150.604 1.00 30.21  ? 304 ILE B C   1 
ATOM 5700 O O   . ILE B 1 304 ? 32.617 126.194 149.443 1.00 30.17  ? 304 ILE B O   1 
ATOM 5701 C CB  . ILE B 1 304 ? 31.028 127.309 152.016 1.00 28.51  ? 304 ILE B CB  1 
ATOM 5702 C CG1 . ILE B 1 304 ? 29.656 127.475 152.582 1.00 27.52  ? 304 ILE B CG1 1 
ATOM 5703 C CG2 . ILE B 1 304 ? 31.502 128.428 151.088 1.00 28.76  ? 304 ILE B CG2 1 
ATOM 5704 C CD1 . ILE B 1 304 ? 29.329 128.847 153.060 1.00 28.89  ? 304 ILE B CD1 1 
ATOM 5705 N N   . GLY B 1 305 ? 33.396 125.279 151.343 1.00 31.30  ? 305 GLY B N   1 
ATOM 5706 C CA  . GLY B 1 305 ? 34.698 125.046 150.788 1.00 33.30  ? 305 GLY B CA  1 
ATOM 5707 C C   . GLY B 1 305 ? 34.696 123.878 149.830 1.00 34.87  ? 305 GLY B C   1 
ATOM 5708 O O   . GLY B 1 305 ? 35.763 123.461 149.384 1.00 35.94  ? 305 GLY B O   1 
ATOM 5709 N N   . SER B 1 306 ? 33.524 123.337 149.510 1.00 35.43  ? 306 SER B N   1 
ATOM 5710 C CA  . SER B 1 306 ? 33.481 122.222 148.579 1.00 36.18  ? 306 SER B CA  1 
ATOM 5711 C C   . SER B 1 306 ? 32.909 122.596 147.219 1.00 36.08  ? 306 SER B C   1 
ATOM 5712 O O   . SER B 1 306 ? 33.297 122.030 146.198 1.00 35.86  ? 306 SER B O   1 
ATOM 5713 C CB  . SER B 1 306 ? 32.736 121.049 149.205 1.00 36.78  ? 306 SER B CB  1 
ATOM 5714 O OG  . SER B 1 306 ? 33.493 120.520 150.286 1.00 38.45  ? 306 SER B OG  1 
ATOM 5715 N N   . SER B 1 307 ? 32.014 123.575 147.189 1.00 36.95  ? 307 SER B N   1 
ATOM 5716 C CA  . SER B 1 307 ? 31.450 124.003 145.913 1.00 37.68  ? 307 SER B CA  1 
ATOM 5717 C C   . SER B 1 307 ? 32.460 124.821 145.110 1.00 37.77  ? 307 SER B C   1 
ATOM 5718 O O   . SER B 1 307 ? 32.266 125.062 143.928 1.00 38.36  ? 307 SER B O   1 
ATOM 5719 C CB  . SER B 1 307 ? 30.207 124.859 146.122 1.00 38.08  ? 307 SER B CB  1 
ATOM 5720 O OG  . SER B 1 307 ? 30.573 126.223 146.218 1.00 37.49  ? 307 SER B OG  1 
ATOM 5721 N N   . PHE B 1 308 ? 33.533 125.253 145.748 1.00 37.33  ? 308 PHE B N   1 
ATOM 5722 C CA  . PHE B 1 308 ? 34.528 126.051 145.060 1.00 37.20  ? 308 PHE B CA  1 
ATOM 5723 C C   . PHE B 1 308 ? 35.837 125.299 144.966 1.00 36.50  ? 308 PHE B C   1 
ATOM 5724 O O   . PHE B 1 308 ? 36.907 125.884 144.775 1.00 36.47  ? 308 PHE B O   1 
ATOM 5725 C CB  . PHE B 1 308 ? 34.715 127.368 145.813 1.00 37.93  ? 308 PHE B CB  1 
ATOM 5726 C CG  . PHE B 1 308 ? 33.619 128.367 145.561 1.00 39.55  ? 308 PHE B CG  1 
ATOM 5727 C CD1 . PHE B 1 308 ? 32.883 128.324 144.388 1.00 39.54  ? 308 PHE B CD1 1 
ATOM 5728 C CD2 . PHE B 1 308 ? 33.362 129.387 146.461 1.00 39.97  ? 308 PHE B CD2 1 
ATOM 5729 C CE1 . PHE B 1 308 ? 31.926 129.279 144.126 1.00 39.60  ? 308 PHE B CE1 1 
ATOM 5730 C CE2 . PHE B 1 308 ? 32.395 130.352 146.198 1.00 40.93  ? 308 PHE B CE2 1 
ATOM 5731 C CZ  . PHE B 1 308 ? 31.678 130.299 145.032 1.00 40.92  ? 308 PHE B CZ  1 
ATOM 5732 N N   . ALA B 1 309 ? 35.744 123.985 145.060 1.00 35.92  ? 309 ALA B N   1 
ATOM 5733 C CA  . ALA B 1 309 ? 36.936 123.179 145.034 1.00 36.26  ? 309 ALA B CA  1 
ATOM 5734 C C   . ALA B 1 309 ? 37.156 122.459 143.750 1.00 36.43  ? 309 ALA B C   1 
ATOM 5735 O O   . ALA B 1 309 ? 36.208 122.022 143.132 1.00 36.38  ? 309 ALA B O   1 
ATOM 5736 C CB  . ALA B 1 309 ? 36.886 122.192 146.147 1.00 37.69  ? 309 ALA B CB  1 
ATOM 5737 N N   . THR B 1 310 ? 38.422 122.295 143.391 1.00 37.43  ? 310 THR B N   1 
ATOM 5738 C CA  . THR B 1 310 ? 38.776 121.628 142.166 1.00 39.76  ? 310 THR B CA  1 
ATOM 5739 C C   . THR B 1 310 ? 39.794 120.494 142.280 1.00 40.30  ? 310 THR B C   1 
ATOM 5740 O O   . THR B 1 310 ? 39.606 119.437 141.690 1.00 40.34  ? 310 THR B O   1 
ATOM 5741 C CB  . THR B 1 310 ? 39.306 122.641 141.144 1.00 41.04  ? 310 THR B CB  1 
ATOM 5742 O OG1 . THR B 1 310 ? 40.304 123.456 141.767 1.00 42.43  ? 310 THR B OG1 1 
ATOM 5743 C CG2 . THR B 1 310 ? 38.195 123.532 140.646 1.00 42.17  ? 310 THR B CG2 1 
ATOM 5744 N N   . SER B 1 311 ? 40.862 120.683 143.039 1.00 40.78  ? 311 SER B N   1 
ATOM 5745 C CA  . SER B 1 311 ? 41.887 119.645 143.119 1.00 41.86  ? 311 SER B CA  1 
ATOM 5746 C C   . SER B 1 311 ? 41.805 118.705 144.293 1.00 42.08  ? 311 SER B C   1 
ATOM 5747 O O   . SER B 1 311 ? 41.206 119.030 145.317 1.00 42.93  ? 311 SER B O   1 
ATOM 5748 C CB  . SER B 1 311 ? 43.273 120.282 143.117 1.00 42.72  ? 311 SER B CB  1 
ATOM 5749 O OG  . SER B 1 311 ? 43.404 121.172 144.220 1.00 43.04  ? 311 SER B OG  1 
ATOM 5750 N N   . ALA B 1 312 ? 42.438 117.545 144.144 1.00 42.36  ? 312 ALA B N   1 
ATOM 5751 C CA  . ALA B 1 312 ? 42.461 116.546 145.199 1.00 42.81  ? 312 ALA B CA  1 
ATOM 5752 C C   . ALA B 1 312 ? 43.097 117.154 146.421 1.00 42.32  ? 312 ALA B C   1 
ATOM 5753 O O   . ALA B 1 312 ? 42.509 117.182 147.497 1.00 42.18  ? 312 ALA B O   1 
ATOM 5754 C CB  . ALA B 1 312 ? 43.267 115.348 144.757 1.00 43.53  ? 312 ALA B CB  1 
ATOM 5755 N N   . LEU B 1 313 ? 44.311 117.645 146.244 1.00 42.08  ? 313 LEU B N   1 
ATOM 5756 C CA  . LEU B 1 313 ? 45.015 118.256 147.348 1.00 42.73  ? 313 LEU B CA  1 
ATOM 5757 C C   . LEU B 1 313 ? 44.090 119.254 148.037 1.00 41.19  ? 313 LEU B C   1 
ATOM 5758 O O   . LEU B 1 313 ? 44.083 119.377 149.264 1.00 41.82  ? 313 LEU B O   1 
ATOM 5759 C CB  . LEU B 1 313 ? 46.278 118.932 146.823 1.00 44.65  ? 313 LEU B CB  1 
ATOM 5760 C CG  . LEU B 1 313 ? 47.252 117.944 146.153 1.00 46.59  ? 313 LEU B CG  1 
ATOM 5761 C CD1 . LEU B 1 313 ? 48.361 118.697 145.411 1.00 47.33  ? 313 LEU B CD1 1 
ATOM 5762 C CD2 . LEU B 1 313 ? 47.844 117.026 147.234 1.00 47.60  ? 313 LEU B CD2 1 
ATOM 5763 N N   . GLU B 1 314 ? 43.281 119.941 147.247 1.00 40.46  ? 314 GLU B N   1 
ATOM 5764 C CA  . GLU B 1 314 ? 42.358 120.906 147.806 1.00 39.23  ? 314 GLU B CA  1 
ATOM 5765 C C   . GLU B 1 314 ? 41.385 120.205 148.759 1.00 37.29  ? 314 GLU B C   1 
ATOM 5766 O O   . GLU B 1 314 ? 41.088 120.726 149.832 1.00 35.91  ? 314 GLU B O   1 
ATOM 5767 C CB  . GLU B 1 314 ? 41.602 121.609 146.681 1.00 41.13  ? 314 GLU B CB  1 
ATOM 5768 C CG  . GLU B 1 314 ? 40.738 122.752 147.152 1.00 44.17  ? 314 GLU B CG  1 
ATOM 5769 C CD  . GLU B 1 314 ? 40.507 123.806 146.084 1.00 46.17  ? 314 GLU B CD  1 
ATOM 5770 O OE1 . GLU B 1 314 ? 40.618 123.480 144.869 1.00 47.55  ? 314 GLU B OE1 1 
ATOM 5771 O OE2 . GLU B 1 314 ? 40.195 124.963 146.471 1.00 45.60  ? 314 GLU B OE2 1 
ATOM 5772 N N   . VAL B 1 315 ? 40.927 119.010 148.378 1.00 35.53  ? 315 VAL B N   1 
ATOM 5773 C CA  . VAL B 1 315 ? 40.005 118.224 149.201 1.00 34.28  ? 315 VAL B CA  1 
ATOM 5774 C C   . VAL B 1 315 ? 40.666 117.755 150.478 1.00 32.36  ? 315 VAL B C   1 
ATOM 5775 O O   . VAL B 1 315 ? 40.077 117.832 151.556 1.00 32.33  ? 315 VAL B O   1 
ATOM 5776 C CB  . VAL B 1 315 ? 39.517 116.965 148.512 1.00 34.66  ? 315 VAL B CB  1 
ATOM 5777 C CG1 . VAL B 1 315 ? 38.136 116.664 149.018 1.00 34.20  ? 315 VAL B CG1 1 
ATOM 5778 C CG2 . VAL B 1 315 ? 39.529 117.139 147.025 1.00 35.74  ? 315 VAL B CG2 1 
ATOM 5779 N N   . VAL B 1 316 ? 41.873 117.225 150.341 1.00 30.58  ? 316 VAL B N   1 
ATOM 5780 C CA  . VAL B 1 316 ? 42.603 116.786 151.496 1.00 29.67  ? 316 VAL B CA  1 
ATOM 5781 C C   . VAL B 1 316 ? 42.423 117.909 152.510 1.00 29.50  ? 316 VAL B C   1 
ATOM 5782 O O   . VAL B 1 316 ? 41.880 117.677 153.586 1.00 29.67  ? 316 VAL B O   1 
ATOM 5783 C CB  . VAL B 1 316 ? 44.101 116.613 151.190 1.00 29.11  ? 316 VAL B CB  1 
ATOM 5784 C CG1 . VAL B 1 316 ? 44.879 116.489 152.474 1.00 28.84  ? 316 VAL B CG1 1 
ATOM 5785 C CG2 . VAL B 1 316 ? 44.329 115.374 150.335 1.00 28.71  ? 316 VAL B CG2 1 
ATOM 5786 N N   . ILE B 1 317 ? 42.815 119.136 152.156 1.00 29.63  ? 317 ILE B N   1 
ATOM 5787 C CA  . ILE B 1 317 ? 42.680 120.263 153.092 1.00 30.35  ? 317 ILE B CA  1 
ATOM 5788 C C   . ILE B 1 317 ? 41.259 120.454 153.644 1.00 29.91  ? 317 ILE B C   1 
ATOM 5789 O O   . ILE B 1 317 ? 41.074 120.909 154.774 1.00 30.41  ? 317 ILE B O   1 
ATOM 5790 C CB  . ILE B 1 317 ? 43.185 121.612 152.477 1.00 29.74  ? 317 ILE B CB  1 
ATOM 5791 C CG1 . ILE B 1 317 ? 44.695 121.537 152.226 1.00 30.88  ? 317 ILE B CG1 1 
ATOM 5792 C CG2 . ILE B 1 317 ? 42.962 122.768 153.463 1.00 30.06  ? 317 ILE B CG2 1 
ATOM 5793 C CD1 . ILE B 1 317 ? 45.287 122.840 151.659 1.00 32.13  ? 317 ILE B CD1 1 
ATOM 5794 N N   . LEU B 1 318 ? 40.254 120.086 152.863 1.00 29.58  ? 318 LEU B N   1 
ATOM 5795 C CA  . LEU B 1 318 ? 38.874 120.206 153.301 1.00 29.03  ? 318 LEU B CA  1 
ATOM 5796 C C   . LEU B 1 318 ? 38.461 119.102 154.259 1.00 29.49  ? 318 LEU B C   1 
ATOM 5797 O O   . LEU B 1 318 ? 37.653 119.340 155.154 1.00 28.84  ? 318 LEU B O   1 
ATOM 5798 C CB  . LEU B 1 318 ? 37.965 120.203 152.094 1.00 28.87  ? 318 LEU B CB  1 
ATOM 5799 C CG  . LEU B 1 318 ? 38.248 121.328 151.111 1.00 26.97  ? 318 LEU B CG  1 
ATOM 5800 C CD1 . LEU B 1 318 ? 37.277 121.198 149.975 1.00 26.88  ? 318 LEU B CD1 1 
ATOM 5801 C CD2 . LEU B 1 318 ? 38.102 122.666 151.790 1.00 25.72  ? 318 LEU B CD2 1 
ATOM 5802 N N   . LYS B 1 319 ? 38.975 117.890 154.075 1.00 30.44  ? 319 LYS B N   1 
ATOM 5803 C CA  . LYS B 1 319 ? 38.625 116.789 154.986 1.00 31.35  ? 319 LYS B CA  1 
ATOM 5804 C C   . LYS B 1 319 ? 39.147 117.172 156.349 1.00 31.38  ? 319 LYS B C   1 
ATOM 5805 O O   . LYS B 1 319 ? 38.383 117.511 157.248 1.00 30.24  ? 319 LYS B O   1 
ATOM 5806 C CB  . LYS B 1 319 ? 39.298 115.470 154.563 1.00 32.20  ? 319 LYS B CB  1 
ATOM 5807 C CG  . LYS B 1 319 ? 38.989 114.301 155.494 1.00 32.54  ? 319 LYS B CG  1 
ATOM 5808 C CD  . LYS B 1 319 ? 37.535 113.909 155.413 1.00 33.62  ? 319 LYS B CD  1 
ATOM 5809 C CE  . LYS B 1 319 ? 37.279 112.555 156.026 1.00 34.03  ? 319 LYS B CE  1 
ATOM 5810 N NZ  . LYS B 1 319 ? 35.820 112.309 155.938 1.00 34.53  ? 319 LYS B NZ  1 
ATOM 5811 N N   . THR B 1 320 ? 40.465 117.092 156.484 1.00 31.74  ? 320 THR B N   1 
ATOM 5812 C CA  . THR B 1 320 ? 41.166 117.491 157.700 1.00 34.04  ? 320 THR B CA  1 
ATOM 5813 C C   . THR B 1 320 ? 40.268 118.241 158.656 1.00 35.12  ? 320 THR B C   1 
ATOM 5814 O O   . THR B 1 320 ? 40.026 117.802 159.766 1.00 35.93  ? 320 THR B O   1 
ATOM 5815 C CB  . THR B 1 320 ? 42.344 118.401 157.300 1.00 34.60  ? 320 THR B CB  1 
ATOM 5816 O OG1 . THR B 1 320 ? 43.298 117.617 156.553 1.00 34.89  ? 320 THR B OG1 1 
ATOM 5817 C CG2 . THR B 1 320 ? 43.010 118.996 158.528 1.00 35.80  ? 320 THR B CG2 1 
ATOM 5818 N N   . LEU B 1 321 ? 39.778 119.385 158.187 1.00 36.93  ? 321 LEU B N   1 
ATOM 5819 C CA  . LEU B 1 321 ? 38.895 120.263 158.960 1.00 39.01  ? 321 LEU B CA  1 
ATOM 5820 C C   . LEU B 1 321 ? 37.864 119.495 159.735 1.00 40.45  ? 321 LEU B C   1 
ATOM 5821 O O   . LEU B 1 321 ? 37.246 120.044 160.647 1.00 40.06  ? 321 LEU B O   1 
ATOM 5822 C CB  . LEU B 1 321 ? 38.194 121.260 158.042 1.00 38.64  ? 321 LEU B CB  1 
ATOM 5823 C CG  . LEU B 1 321 ? 39.131 122.220 157.371 1.00 39.04  ? 321 LEU B CG  1 
ATOM 5824 C CD1 . LEU B 1 321 ? 38.358 123.358 156.726 1.00 38.68  ? 321 LEU B CD1 1 
ATOM 5825 C CD2 . LEU B 1 321 ? 40.123 122.791 158.382 1.00 38.67  ? 321 LEU B CD2 1 
ATOM 5826 N N   . HIS B 1 322 ? 37.667 118.236 159.326 1.00 42.34  ? 322 HIS B N   1 
ATOM 5827 C CA  . HIS B 1 322 ? 36.722 117.334 160.002 1.00 44.59  ? 322 HIS B CA  1 
ATOM 5828 C C   . HIS B 1 322 ? 37.231 117.243 161.432 1.00 44.71  ? 322 HIS B C   1 
ATOM 5829 O O   . HIS B 1 322 ? 36.491 117.537 162.372 1.00 45.61  ? 322 HIS B O   1 
ATOM 5830 C CB  . HIS B 1 322 ? 36.689 115.891 159.406 1.00 45.97  ? 322 HIS B CB  1 
ATOM 5831 C CG  . HIS B 1 322 ? 35.747 114.938 160.118 1.00 47.17  ? 322 HIS B CG  1 
ATOM 5832 N ND1 . HIS B 1 322 ? 34.383 115.134 160.154 1.00 47.53  ? 322 HIS B ND1 1 
ATOM 5833 C CD2 . HIS B 1 322 ? 35.978 113.801 160.811 1.00 47.33  ? 322 HIS B CD2 1 
ATOM 5834 C CE1 . HIS B 1 322 ? 33.813 114.166 160.844 1.00 47.99  ? 322 HIS B CE1 1 
ATOM 5835 N NE2 . HIS B 1 322 ? 34.767 113.333 161.262 1.00 47.75  ? 322 HIS B NE2 1 
ATOM 5836 N N   . MET B 1 323 ? 38.497 116.856 161.591 1.00 44.68  ? 323 MET B N   1 
ATOM 5837 C CA  . MET B 1 323 ? 39.089 116.703 162.909 1.00 44.24  ? 323 MET B CA  1 
ATOM 5838 C C   . MET B 1 323 ? 39.030 117.958 163.725 1.00 43.01  ? 323 MET B C   1 
ATOM 5839 O O   . MET B 1 323 ? 38.829 117.891 164.924 1.00 43.50  ? 323 MET B O   1 
ATOM 5840 C CB  . MET B 1 323 ? 40.541 116.235 162.809 1.00 45.78  ? 323 MET B CB  1 
ATOM 5841 C CG  . MET B 1 323 ? 40.692 114.818 162.279 1.00 48.19  ? 323 MET B CG  1 
ATOM 5842 S SD  . MET B 1 323 ? 39.533 114.455 160.932 1.00 50.14  ? 323 MET B SD  1 
ATOM 5843 C CE  . MET B 1 323 ? 40.014 112.754 160.478 1.00 49.48  ? 323 MET B CE  1 
ATOM 5844 N N   . PHE B 1 324 ? 39.202 119.098 163.074 1.00 41.22  ? 324 PHE B N   1 
ATOM 5845 C CA  . PHE B 1 324 ? 39.160 120.362 163.767 1.00 40.60  ? 324 PHE B CA  1 
ATOM 5846 C C   . PHE B 1 324 ? 37.855 120.600 164.457 1.00 39.86  ? 324 PHE B C   1 
ATOM 5847 O O   . PHE B 1 324 ? 37.795 121.362 165.390 1.00 39.14  ? 324 PHE B O   1 
ATOM 5848 C CB  . PHE B 1 324 ? 39.374 121.521 162.813 1.00 41.17  ? 324 PHE B CB  1 
ATOM 5849 C CG  . PHE B 1 324 ? 40.740 122.104 162.892 1.00 41.93  ? 324 PHE B CG  1 
ATOM 5850 C CD1 . PHE B 1 324 ? 41.825 121.268 163.094 1.00 41.16  ? 324 PHE B CD1 1 
ATOM 5851 C CD2 . PHE B 1 324 ? 40.953 123.477 162.765 1.00 41.71  ? 324 PHE B CD2 1 
ATOM 5852 C CE1 . PHE B 1 324 ? 43.106 121.769 163.172 1.00 41.44  ? 324 PHE B CE1 1 
ATOM 5853 C CE2 . PHE B 1 324 ? 42.244 124.000 162.843 1.00 41.99  ? 324 PHE B CE2 1 
ATOM 5854 C CZ  . PHE B 1 324 ? 43.326 123.136 163.047 1.00 42.24  ? 324 PHE B CZ  1 
ATOM 5855 N N   . GLU B 1 325 ? 36.796 119.955 164.016 1.00 40.62  ? 325 GLU B N   1 
ATOM 5856 C CA  . GLU B 1 325 ? 35.524 120.230 164.645 1.00 41.55  ? 325 GLU B CA  1 
ATOM 5857 C C   . GLU B 1 325 ? 35.202 119.226 165.713 1.00 41.84  ? 325 GLU B C   1 
ATOM 5858 O O   . GLU B 1 325 ? 34.556 119.553 166.719 1.00 41.91  ? 325 GLU B O   1 
ATOM 5859 C CB  . GLU B 1 325 ? 34.430 120.280 163.573 1.00 42.29  ? 325 GLU B CB  1 
ATOM 5860 C CG  . GLU B 1 325 ? 32.999 120.106 164.042 1.00 43.64  ? 325 GLU B CG  1 
ATOM 5861 C CD  . GLU B 1 325 ? 32.456 118.768 163.611 1.00 44.34  ? 325 GLU B CD  1 
ATOM 5862 O OE1 . GLU B 1 325 ? 33.223 117.792 163.719 1.00 44.58  ? 325 GLU B OE1 1 
ATOM 5863 O OE2 . GLU B 1 325 ? 31.284 118.680 163.172 1.00 45.99  ? 325 GLU B OE2 1 
ATOM 5864 N N   . VAL B 1 326 ? 35.679 118.009 165.497 1.00 42.06  ? 326 VAL B N   1 
ATOM 5865 C CA  . VAL B 1 326 ? 35.424 116.927 166.411 1.00 43.72  ? 326 VAL B CA  1 
ATOM 5866 C C   . VAL B 1 326 ? 35.553 117.414 167.830 1.00 44.00  ? 326 VAL B C   1 
ATOM 5867 O O   . VAL B 1 326 ? 34.560 117.843 168.449 1.00 44.11  ? 326 VAL B O   1 
ATOM 5868 C CB  . VAL B 1 326 ? 36.392 115.769 166.193 1.00 42.61  ? 326 VAL B CB  1 
ATOM 5869 C CG1 . VAL B 1 326 ? 35.893 114.524 166.925 1.00 41.11  ? 326 VAL B CG1 1 
ATOM 5870 C CG2 . VAL B 1 326 ? 36.539 115.519 164.723 1.00 43.02  ? 326 VAL B CG2 1 
ATOM 5871 N N   . PRO B 1 327 ? 36.784 117.394 168.360 1.00 44.73  ? 327 PRO B N   1 
ATOM 5872 C CA  . PRO B 1 327 ? 36.943 117.851 169.737 1.00 45.30  ? 327 PRO B CA  1 
ATOM 5873 C C   . PRO B 1 327 ? 35.943 118.945 170.059 1.00 43.51  ? 327 PRO B C   1 
ATOM 5874 O O   . PRO B 1 327 ? 35.003 118.718 170.814 1.00 43.35  ? 327 PRO B O   1 
ATOM 5875 C CB  . PRO B 1 327 ? 38.381 118.341 169.761 1.00 45.04  ? 327 PRO B CB  1 
ATOM 5876 C CG  . PRO B 1 327 ? 38.625 118.707 168.288 1.00 45.41  ? 327 PRO B CG  1 
ATOM 5877 C CD  . PRO B 1 327 ? 38.051 117.550 167.622 1.00 45.61  ? 327 PRO B CD  1 
ATOM 5878 N N   . PHE B 1 328 ? 36.124 120.109 169.443 1.00 41.98  ? 328 PHE B N   1 
ATOM 5879 C CA  . PHE B 1 328 ? 35.259 121.240 169.725 1.00 41.69  ? 328 PHE B CA  1 
ATOM 5880 C C   . PHE B 1 328 ? 33.793 120.925 169.889 1.00 40.63  ? 328 PHE B C   1 
ATOM 5881 O O   . PHE B 1 328 ? 33.165 121.423 170.823 1.00 40.50  ? 328 PHE B O   1 
ATOM 5882 C CB  . PHE B 1 328 ? 35.426 122.347 168.695 1.00 43.50  ? 328 PHE B CB  1 
ATOM 5883 C CG  . PHE B 1 328 ? 36.782 122.993 168.728 1.00 44.98  ? 328 PHE B CG  1 
ATOM 5884 C CD1 . PHE B 1 328 ? 37.902 122.276 168.338 1.00 45.48  ? 328 PHE B CD1 1 
ATOM 5885 C CD2 . PHE B 1 328 ? 36.953 124.302 169.173 1.00 44.47  ? 328 PHE B CD2 1 
ATOM 5886 C CE1 . PHE B 1 328 ? 39.181 122.846 168.386 1.00 45.46  ? 328 PHE B CE1 1 
ATOM 5887 C CE2 . PHE B 1 328 ? 38.229 124.877 169.224 1.00 44.36  ? 328 PHE B CE2 1 
ATOM 5888 C CZ  . PHE B 1 328 ? 39.343 124.145 168.829 1.00 44.75  ? 328 PHE B CZ  1 
ATOM 5889 N N   . LEU B 1 329 ? 33.221 120.097 169.028 1.00 39.51  ? 329 LEU B N   1 
ATOM 5890 C CA  . LEU B 1 329 ? 31.814 119.844 169.226 1.00 38.66  ? 329 LEU B CA  1 
ATOM 5891 C C   . LEU B 1 329 ? 31.539 118.958 170.401 1.00 39.12  ? 329 LEU B C   1 
ATOM 5892 O O   . LEU B 1 329 ? 30.753 119.310 171.268 1.00 39.21  ? 329 LEU B O   1 
ATOM 5893 C CB  . LEU B 1 329 ? 31.134 119.247 168.003 1.00 37.68  ? 329 LEU B CB  1 
ATOM 5894 C CG  . LEU B 1 329 ? 29.631 119.425 168.246 1.00 37.43  ? 329 LEU B CG  1 
ATOM 5895 C CD1 . LEU B 1 329 ? 29.362 120.889 168.347 1.00 36.90  ? 329 LEU B CD1 1 
ATOM 5896 C CD2 . LEU B 1 329 ? 28.795 118.830 167.148 1.00 37.65  ? 329 LEU B CD2 1 
ATOM 5897 N N   . LEU B 1 330 ? 32.176 117.803 170.446 1.00 39.58  ? 330 LEU B N   1 
ATOM 5898 C CA  . LEU B 1 330 ? 31.939 116.894 171.554 1.00 40.42  ? 330 LEU B CA  1 
ATOM 5899 C C   . LEU B 1 330 ? 32.058 117.662 172.864 1.00 40.80  ? 330 LEU B C   1 
ATOM 5900 O O   . LEU B 1 330 ? 31.116 117.756 173.659 1.00 40.07  ? 330 LEU B O   1 
ATOM 5901 C CB  . LEU B 1 330 ? 32.971 115.775 171.520 1.00 41.54  ? 330 LEU B CB  1 
ATOM 5902 C CG  . LEU B 1 330 ? 32.751 114.630 172.512 1.00 42.86  ? 330 LEU B CG  1 
ATOM 5903 C CD1 . LEU B 1 330 ? 31.475 113.849 172.160 1.00 42.34  ? 330 LEU B CD1 1 
ATOM 5904 C CD2 . LEU B 1 330 ? 33.969 113.722 172.471 1.00 42.44  ? 330 LEU B CD2 1 
ATOM 5905 N N   . VAL B 1 331 ? 33.242 118.216 173.060 1.00 40.60  ? 331 VAL B N   1 
ATOM 5906 C CA  . VAL B 1 331 ? 33.566 118.983 174.245 1.00 39.98  ? 331 VAL B CA  1 
ATOM 5907 C C   . VAL B 1 331 ? 32.551 120.093 174.508 1.00 40.95  ? 331 VAL B C   1 
ATOM 5908 O O   . VAL B 1 331 ? 31.863 120.088 175.529 1.00 40.36  ? 331 VAL B O   1 
ATOM 5909 C CB  . VAL B 1 331 ? 34.955 119.595 174.076 1.00 39.60  ? 331 VAL B CB  1 
ATOM 5910 C CG1 . VAL B 1 331 ? 35.336 120.332 175.303 1.00 38.83  ? 331 VAL B CG1 1 
ATOM 5911 C CG2 . VAL B 1 331 ? 35.970 118.499 173.757 1.00 39.21  ? 331 VAL B CG2 1 
ATOM 5912 N N   . GLY B 1 332 ? 32.480 121.043 173.577 1.00 42.31  ? 332 GLY B N   1 
ATOM 5913 C CA  . GLY B 1 332 ? 31.557 122.156 173.688 1.00 43.94  ? 332 GLY B CA  1 
ATOM 5914 C C   . GLY B 1 332 ? 30.157 121.679 173.994 1.00 45.39  ? 332 GLY B C   1 
ATOM 5915 O O   . GLY B 1 332 ? 29.644 121.939 175.079 1.00 46.11  ? 332 GLY B O   1 
ATOM 5916 N N   . CYS B 1 333 ? 29.534 120.988 173.047 1.00 46.40  ? 333 CYS B N   1 
ATOM 5917 C CA  . CYS B 1 333 ? 28.189 120.474 173.244 1.00 48.06  ? 333 CYS B CA  1 
ATOM 5918 C C   . CYS B 1 333 ? 28.001 120.051 174.709 1.00 49.55  ? 333 CYS B C   1 
ATOM 5919 O O   . CYS B 1 333 ? 27.098 120.519 175.403 1.00 49.73  ? 333 CYS B O   1 
ATOM 5920 C CB  . CYS B 1 333 ? 28.018 119.285 172.314 1.00 47.90  ? 333 CYS B CB  1 
ATOM 5921 S SG  . CYS B 1 333 ? 26.851 119.452 170.891 1.00 48.24  ? 333 CYS B SG  1 
ATOM 5922 N N   . PHE B 1 334 ? 28.898 119.182 175.159 1.00 51.41  ? 334 PHE B N   1 
ATOM 5923 C CA  . PHE B 1 334 ? 28.907 118.619 176.504 1.00 52.83  ? 334 PHE B CA  1 
ATOM 5924 C C   . PHE B 1 334 ? 28.988 119.654 177.633 1.00 52.28  ? 334 PHE B C   1 
ATOM 5925 O O   . PHE B 1 334 ? 28.171 119.660 178.568 1.00 52.43  ? 334 PHE B O   1 
ATOM 5926 C CB  . PHE B 1 334 ? 30.083 117.635 176.561 1.00 54.85  ? 334 PHE B CB  1 
ATOM 5927 C CG  . PHE B 1 334 ? 30.364 117.075 177.916 1.00 57.06  ? 334 PHE B CG  1 
ATOM 5928 C CD1 . PHE B 1 334 ? 29.407 116.336 178.608 1.00 57.38  ? 334 PHE B CD1 1 
ATOM 5929 C CD2 . PHE B 1 334 ? 31.614 117.261 178.484 1.00 57.56  ? 334 PHE B CD2 1 
ATOM 5930 C CE1 . PHE B 1 334 ? 29.700 115.793 179.842 1.00 57.80  ? 334 PHE B CE1 1 
ATOM 5931 C CE2 . PHE B 1 334 ? 31.917 116.724 179.716 1.00 58.48  ? 334 PHE B CE2 1 
ATOM 5932 C CZ  . PHE B 1 334 ? 30.960 115.987 180.400 1.00 58.51  ? 334 PHE B CZ  1 
ATOM 5933 N N   . LYS B 1 335 ? 29.977 120.530 177.534 1.00 51.58  ? 335 LYS B N   1 
ATOM 5934 C CA  . LYS B 1 335 ? 30.181 121.555 178.539 1.00 51.11  ? 335 LYS B CA  1 
ATOM 5935 C C   . LYS B 1 335 ? 29.105 122.618 178.447 1.00 49.24  ? 335 LYS B C   1 
ATOM 5936 O O   . LYS B 1 335 ? 28.754 123.227 179.442 1.00 49.50  ? 335 LYS B O   1 
ATOM 5937 C CB  . LYS B 1 335 ? 31.551 122.207 178.358 1.00 53.29  ? 335 LYS B CB  1 
ATOM 5938 C CG  . LYS B 1 335 ? 32.746 121.265 178.520 1.00 55.00  ? 335 LYS B CG  1 
ATOM 5939 C CD  . LYS B 1 335 ? 33.146 121.026 179.966 1.00 55.78  ? 335 LYS B CD  1 
ATOM 5940 C CE  . LYS B 1 335 ? 34.468 120.264 179.996 1.00 56.44  ? 335 LYS B CE  1 
ATOM 5941 N NZ  . LYS B 1 335 ? 34.995 120.056 181.375 1.00 56.97  ? 335 LYS B NZ  1 
ATOM 5942 N N   . TYR B 1 336 ? 28.576 122.848 177.256 1.00 46.63  ? 336 TYR B N   1 
ATOM 5943 C CA  . TYR B 1 336 ? 27.555 123.857 177.131 1.00 44.25  ? 336 TYR B CA  1 
ATOM 5944 C C   . TYR B 1 336 ? 26.306 123.396 177.798 1.00 43.51  ? 336 TYR B C   1 
ATOM 5945 O O   . TYR B 1 336 ? 25.491 124.198 178.242 1.00 43.36  ? 336 TYR B O   1 
ATOM 5946 C CB  . TYR B 1 336 ? 27.204 124.145 175.701 1.00 43.85  ? 336 TYR B CB  1 
ATOM 5947 C CG  . TYR B 1 336 ? 26.043 125.076 175.634 1.00 43.34  ? 336 TYR B CG  1 
ATOM 5948 C CD1 . TYR B 1 336 ? 26.103 126.312 176.261 1.00 43.42  ? 336 TYR B CD1 1 
ATOM 5949 C CD2 . TYR B 1 336 ? 24.893 124.738 174.951 1.00 42.76  ? 336 TYR B CD2 1 
ATOM 5950 C CE1 . TYR B 1 336 ? 25.055 127.190 176.207 1.00 43.38  ? 336 TYR B CE1 1 
ATOM 5951 C CE2 . TYR B 1 336 ? 23.832 125.616 174.888 1.00 43.00  ? 336 TYR B CE2 1 
ATOM 5952 C CZ  . TYR B 1 336 ? 23.921 126.839 175.519 1.00 43.15  ? 336 TYR B CZ  1 
ATOM 5953 O OH  . TYR B 1 336 ? 22.890 127.732 175.454 1.00 43.08  ? 336 TYR B OH  1 
ATOM 5954 N N   . ILE B 1 337 ? 26.124 122.093 177.837 1.00 43.45  ? 337 ILE B N   1 
ATOM 5955 C CA  . ILE B 1 337 ? 24.959 121.563 178.502 1.00 44.09  ? 337 ILE B CA  1 
ATOM 5956 C C   . ILE B 1 337 ? 25.160 121.817 179.986 1.00 45.03  ? 337 ILE B C   1 
ATOM 5957 O O   . ILE B 1 337 ? 24.405 122.553 180.627 1.00 44.46  ? 337 ILE B O   1 
ATOM 5958 C CB  . ILE B 1 337 ? 24.830 120.062 178.264 1.00 43.96  ? 337 ILE B CB  1 
ATOM 5959 C CG1 . ILE B 1 337 ? 24.657 119.811 176.770 1.00 44.48  ? 337 ILE B CG1 1 
ATOM 5960 C CG2 . ILE B 1 337 ? 23.652 119.521 179.045 1.00 44.13  ? 337 ILE B CG2 1 
ATOM 5961 C CD1 . ILE B 1 337 ? 24.489 118.365 176.410 1.00 45.02  ? 337 ILE B CD1 1 
ATOM 5962 N N   . THR B 1 338 ? 26.206 121.215 180.523 1.00 45.62  ? 338 THR B N   1 
ATOM 5963 C CA  . THR B 1 338 ? 26.498 121.383 181.920 1.00 46.41  ? 338 THR B CA  1 
ATOM 5964 C C   . THR B 1 338 ? 26.353 122.847 182.334 1.00 46.20  ? 338 THR B C   1 
ATOM 5965 O O   . THR B 1 338 ? 25.632 123.150 183.263 1.00 47.11  ? 338 THR B O   1 
ATOM 5966 C CB  . THR B 1 338 ? 27.919 120.890 182.232 1.00 47.52  ? 338 THR B CB  1 
ATOM 5967 O OG1 . THR B 1 338 ? 27.990 120.483 183.599 1.00 48.41  ? 338 THR B OG1 1 
ATOM 5968 C CG2 . THR B 1 338 ? 28.931 121.992 181.996 1.00 47.51  ? 338 THR B CG2 1 
ATOM 5969 N N   . SER B 1 339 ? 26.999 123.754 181.612 1.00 46.26  ? 339 SER B N   1 
ATOM 5970 C CA  . SER B 1 339 ? 26.966 125.170 181.960 1.00 46.78  ? 339 SER B CA  1 
ATOM 5971 C C   . SER B 1 339 ? 25.625 125.910 181.969 1.00 46.54  ? 339 SER B C   1 
ATOM 5972 O O   . SER B 1 339 ? 25.421 126.795 182.794 1.00 47.15  ? 339 SER B O   1 
ATOM 5973 C CB  . SER B 1 339 ? 27.967 125.943 181.095 1.00 47.45  ? 339 SER B CB  1 
ATOM 5974 O OG  . SER B 1 339 ? 29.305 125.573 181.414 1.00 48.75  ? 339 SER B OG  1 
ATOM 5975 N N   . GLN B 1 340 ? 24.704 125.598 181.075 1.00 45.45  ? 340 GLN B N   1 
ATOM 5976 C CA  . GLN B 1 340 ? 23.449 126.333 181.134 1.00 44.72  ? 340 GLN B CA  1 
ATOM 5977 C C   . GLN B 1 340 ? 22.288 125.401 181.424 1.00 41.74  ? 340 GLN B C   1 
ATOM 5978 O O   . GLN B 1 340 ? 21.128 125.704 181.150 1.00 41.58  ? 340 GLN B O   1 
ATOM 5979 C CB  . GLN B 1 340 ? 23.222 127.101 179.825 1.00 48.34  ? 340 GLN B CB  1 
ATOM 5980 C CG  . GLN B 1 340 ? 22.090 128.161 179.830 1.00 52.56  ? 340 GLN B CG  1 
ATOM 5981 C CD  . GLN B 1 340 ? 22.409 129.420 180.638 1.00 54.71  ? 340 GLN B CD  1 
ATOM 5982 O OE1 . GLN B 1 340 ? 22.353 129.423 181.871 1.00 56.53  ? 340 GLN B OE1 1 
ATOM 5983 N NE2 . GLN B 1 340 ? 22.742 130.505 179.931 1.00 56.46  ? 340 GLN B NE2 1 
ATOM 5984 N N   . PHE B 1 341 ? 22.604 124.257 182.000 1.00 39.94  ? 341 PHE B N   1 
ATOM 5985 C CA  . PHE B 1 341 ? 21.563 123.300 182.294 1.00 38.20  ? 341 PHE B CA  1 
ATOM 5986 C C   . PHE B 1 341 ? 21.625 122.544 183.590 1.00 37.05  ? 341 PHE B C   1 
ATOM 5987 O O   . PHE B 1 341 ? 22.671 122.045 184.017 1.00 36.37  ? 341 PHE B O   1 
ATOM 5988 C CB  . PHE B 1 341 ? 21.471 122.292 181.172 1.00 38.08  ? 341 PHE B CB  1 
ATOM 5989 C CG  . PHE B 1 341 ? 20.911 122.844 179.936 1.00 36.57  ? 341 PHE B CG  1 
ATOM 5990 C CD1 . PHE B 1 341 ? 21.678 123.617 179.090 1.00 36.11  ? 341 PHE B CD1 1 
ATOM 5991 C CD2 . PHE B 1 341 ? 19.614 122.560 179.597 1.00 35.96  ? 341 PHE B CD2 1 
ATOM 5992 C CE1 . PHE B 1 341 ? 21.145 124.104 177.926 1.00 35.44  ? 341 PHE B CE1 1 
ATOM 5993 C CE2 . PHE B 1 341 ? 19.078 123.042 178.440 1.00 35.03  ? 341 PHE B CE2 1 
ATOM 5994 C CZ  . PHE B 1 341 ? 19.841 123.808 177.595 1.00 35.06  ? 341 PHE B CZ  1 
ATOM 5995 N N   . GLU B 1 342 ? 20.454 122.434 184.184 1.00 34.38  ? 342 GLU B N   1 
ATOM 5996 C CA  . GLU B 1 342 ? 20.298 121.746 185.430 1.00 32.39  ? 342 GLU B CA  1 
ATOM 5997 C C   . GLU B 1 342 ? 20.735 120.306 185.244 1.00 30.85  ? 342 GLU B C   1 
ATOM 5998 O O   . GLU B 1 342 ? 20.063 119.520 184.586 1.00 32.02  ? 342 GLU B O   1 
ATOM 5999 C CB  . GLU B 1 342 ? 18.841 121.859 185.818 1.00 33.67  ? 342 GLU B CB  1 
ATOM 6000 C CG  . GLU B 1 342 ? 18.308 123.242 185.474 1.00 35.26  ? 342 GLU B CG  1 
ATOM 6001 C CD  . GLU B 1 342 ? 16.808 123.345 185.627 1.00 36.64  ? 342 GLU B CD  1 
ATOM 6002 O OE1 . GLU B 1 342 ? 16.241 122.602 186.434 1.00 37.27  ? 342 GLU B OE1 1 
ATOM 6003 O OE2 . GLU B 1 342 ? 16.179 124.182 184.959 1.00 36.32  ? 342 GLU B OE2 1 
ATOM 6004 N N   . VAL B 1 343 ? 21.886 119.976 185.816 1.00 28.64  ? 343 VAL B N   1 
ATOM 6005 C CA  . VAL B 1 343 ? 22.454 118.634 185.726 1.00 27.10  ? 343 VAL B CA  1 
ATOM 6006 C C   . VAL B 1 343 ? 21.441 117.494 185.707 1.00 26.82  ? 343 VAL B C   1 
ATOM 6007 O O   . VAL B 1 343 ? 21.671 116.450 185.117 1.00 25.46  ? 343 VAL B O   1 
ATOM 6008 C CB  . VAL B 1 343 ? 23.417 118.359 186.869 1.00 26.20  ? 343 VAL B CB  1 
ATOM 6009 C CG1 . VAL B 1 343 ? 24.077 117.048 186.639 1.00 26.20  ? 343 VAL B CG1 1 
ATOM 6010 C CG2 . VAL B 1 343 ? 24.451 119.447 186.956 1.00 25.58  ? 343 VAL B CG2 1 
ATOM 6011 N N   . ARG B 1 344 ? 20.316 117.685 186.362 1.00 26.63  ? 344 ARG B N   1 
ATOM 6012 C CA  . ARG B 1 344 ? 19.307 116.648 186.375 1.00 27.19  ? 344 ARG B CA  1 
ATOM 6013 C C   . ARG B 1 344 ? 18.775 116.407 184.974 1.00 27.11  ? 344 ARG B C   1 
ATOM 6014 O O   . ARG B 1 344 ? 18.196 115.383 184.674 1.00 26.76  ? 344 ARG B O   1 
ATOM 6015 C CB  . ARG B 1 344 ? 18.148 117.052 187.299 1.00 28.52  ? 344 ARG B CB  1 
ATOM 6016 C CG  . ARG B 1 344 ? 17.403 118.320 186.892 1.00 29.46  ? 344 ARG B CG  1 
ATOM 6017 C CD  . ARG B 1 344 ? 16.334 118.717 187.920 1.00 30.07  ? 344 ARG B CD  1 
ATOM 6018 N NE  . ARG B 1 344 ? 15.250 119.503 187.325 1.00 31.74  ? 344 ARG B NE  1 
ATOM 6019 C CZ  . ARG B 1 344 ? 14.327 120.155 188.021 1.00 31.96  ? 344 ARG B CZ  1 
ATOM 6020 N NH1 . ARG B 1 344 ? 14.361 120.118 189.338 1.00 34.03  ? 344 ARG B NH1 1 
ATOM 6021 N NH2 . ARG B 1 344 ? 13.370 120.836 187.404 1.00 30.21  ? 344 ARG B NH2 1 
ATOM 6022 N N   . PHE B 1 345 ? 18.990 117.342 184.085 1.00 28.29  ? 345 PHE B N   1 
ATOM 6023 C CA  . PHE B 1 345 ? 18.444 117.145 182.775 1.00 29.59  ? 345 PHE B CA  1 
ATOM 6024 C C   . PHE B 1 345 ? 19.327 116.437 181.775 1.00 31.13  ? 345 PHE B C   1 
ATOM 6025 O O   . PHE B 1 345 ? 18.845 116.023 180.725 1.00 30.12  ? 345 PHE B O   1 
ATOM 6026 C CB  . PHE B 1 345 ? 17.983 118.485 182.220 1.00 28.72  ? 345 PHE B CB  1 
ATOM 6027 C CG  . PHE B 1 345 ? 16.706 118.975 182.833 1.00 28.02  ? 345 PHE B CG  1 
ATOM 6028 C CD1 . PHE B 1 345 ? 15.530 118.252 182.700 1.00 27.61  ? 345 PHE B CD1 1 
ATOM 6029 C CD2 . PHE B 1 345 ? 16.657 120.159 183.511 1.00 26.98  ? 345 PHE B CD2 1 
ATOM 6030 C CE1 . PHE B 1 345 ? 14.344 118.717 183.229 1.00 27.24  ? 345 PHE B CE1 1 
ATOM 6031 C CE2 . PHE B 1 345 ? 15.459 120.604 184.034 1.00 26.92  ? 345 PHE B CE2 1 
ATOM 6032 C CZ  . PHE B 1 345 ? 14.319 119.895 183.896 1.00 27.46  ? 345 PHE B CZ  1 
ATOM 6033 N N   . SER B 1 346 ? 20.604 116.267 182.098 1.00 32.84  ? 346 SER B N   1 
ATOM 6034 C CA  . SER B 1 346 ? 21.535 115.619 181.175 1.00 34.56  ? 346 SER B CA  1 
ATOM 6035 C C   . SER B 1 346 ? 20.868 114.515 180.367 1.00 34.29  ? 346 SER B C   1 
ATOM 6036 O O   . SER B 1 346 ? 20.459 114.734 179.235 1.00 33.76  ? 346 SER B O   1 
ATOM 6037 C CB  . SER B 1 346 ? 22.731 115.037 181.930 1.00 36.59  ? 346 SER B CB  1 
ATOM 6038 O OG  . SER B 1 346 ? 22.363 113.852 182.615 1.00 40.45  ? 346 SER B OG  1 
ATOM 6039 N N   . ALA B 1 347 ? 20.753 113.334 180.962 1.00 35.02  ? 347 ALA B N   1 
ATOM 6040 C CA  . ALA B 1 347 ? 20.157 112.195 180.287 1.00 35.91  ? 347 ALA B CA  1 
ATOM 6041 C C   . ALA B 1 347 ? 19.011 112.613 179.395 1.00 36.62  ? 347 ALA B C   1 
ATOM 6042 O O   . ALA B 1 347 ? 18.997 112.307 178.205 1.00 36.84  ? 347 ALA B O   1 
ATOM 6043 C CB  . ALA B 1 347 ? 19.674 111.173 181.296 1.00 35.18  ? 347 ALA B CB  1 
ATOM 6044 N N   . THR B 1 348 ? 18.052 113.323 179.962 1.00 37.30  ? 348 THR B N   1 
ATOM 6045 C CA  . THR B 1 348 ? 16.918 113.734 179.174 1.00 38.84  ? 348 THR B CA  1 
ATOM 6046 C C   . THR B 1 348 ? 17.352 114.493 177.930 1.00 38.28  ? 348 THR B C   1 
ATOM 6047 O O   . THR B 1 348 ? 16.971 114.144 176.811 1.00 38.26  ? 348 THR B O   1 
ATOM 6048 C CB  . THR B 1 348 ? 15.980 114.609 179.985 1.00 40.66  ? 348 THR B CB  1 
ATOM 6049 O OG1 . THR B 1 348 ? 15.771 114.018 181.277 1.00 42.66  ? 348 THR B OG1 1 
ATOM 6050 C CG2 . THR B 1 348 ? 14.649 114.733 179.262 1.00 41.42  ? 348 THR B CG2 1 
ATOM 6051 N N   . ILE B 1 349 ? 18.161 115.527 178.126 1.00 38.38  ? 349 ILE B N   1 
ATOM 6052 C CA  . ILE B 1 349 ? 18.630 116.332 177.007 1.00 37.60  ? 349 ILE B CA  1 
ATOM 6053 C C   . ILE B 1 349 ? 19.060 115.436 175.853 1.00 36.19  ? 349 ILE B C   1 
ATOM 6054 O O   . ILE B 1 349 ? 18.495 115.510 174.763 1.00 35.73  ? 349 ILE B O   1 
ATOM 6055 C CB  . ILE B 1 349 ? 19.785 117.268 177.448 1.00 38.46  ? 349 ILE B CB  1 
ATOM 6056 C CG1 . ILE B 1 349 ? 19.194 118.436 178.243 1.00 39.10  ? 349 ILE B CG1 1 
ATOM 6057 C CG2 . ILE B 1 349 ? 20.557 117.769 176.252 1.00 37.82  ? 349 ILE B CG2 1 
ATOM 6058 C CD1 . ILE B 1 349 ? 20.221 119.385 178.852 1.00 40.89  ? 349 ILE B CD1 1 
ATOM 6059 N N   . TYR B 1 350 ? 20.030 114.565 176.100 1.00 34.57  ? 350 TYR B N   1 
ATOM 6060 C CA  . TYR B 1 350 ? 20.499 113.676 175.058 1.00 33.72  ? 350 TYR B CA  1 
ATOM 6061 C C   . TYR B 1 350 ? 19.325 112.960 174.441 1.00 33.86  ? 350 TYR B C   1 
ATOM 6062 O O   . TYR B 1 350 ? 19.048 113.110 173.263 1.00 33.96  ? 350 TYR B O   1 
ATOM 6063 C CB  . TYR B 1 350 ? 21.502 112.673 175.615 1.00 32.81  ? 350 TYR B CB  1 
ATOM 6064 C CG  . TYR B 1 350 ? 22.829 113.308 175.946 1.00 33.27  ? 350 TYR B CG  1 
ATOM 6065 C CD1 . TYR B 1 350 ? 23.002 114.684 175.863 1.00 33.70  ? 350 TYR B CD1 1 
ATOM 6066 C CD2 . TYR B 1 350 ? 23.909 112.543 176.365 1.00 33.64  ? 350 TYR B CD2 1 
ATOM 6067 C CE1 . TYR B 1 350 ? 24.220 115.286 176.192 1.00 33.97  ? 350 TYR B CE1 1 
ATOM 6068 C CE2 . TYR B 1 350 ? 25.140 113.140 176.702 1.00 34.22  ? 350 TYR B CE2 1 
ATOM 6069 C CZ  . TYR B 1 350 ? 25.285 114.514 176.615 1.00 33.86  ? 350 TYR B CZ  1 
ATOM 6070 O OH  . TYR B 1 350 ? 26.474 115.113 176.975 1.00 32.81  ? 350 TYR B OH  1 
ATOM 6071 N N   . LEU B 1 351 ? 18.615 112.196 175.249 1.00 33.71  ? 351 LEU B N   1 
ATOM 6072 C CA  . LEU B 1 351 ? 17.471 111.458 174.761 1.00 33.84  ? 351 LEU B CA  1 
ATOM 6073 C C   . LEU B 1 351 ? 16.588 112.254 173.839 1.00 33.78  ? 351 LEU B C   1 
ATOM 6074 O O   . LEU B 1 351 ? 16.307 111.832 172.737 1.00 33.81  ? 351 LEU B O   1 
ATOM 6075 C CB  . LEU B 1 351 ? 16.633 110.983 175.922 1.00 35.51  ? 351 LEU B CB  1 
ATOM 6076 C CG  . LEU B 1 351 ? 17.528 110.271 176.924 1.00 38.26  ? 351 LEU B CG  1 
ATOM 6077 C CD1 . LEU B 1 351 ? 16.859 110.217 178.280 1.00 39.47  ? 351 LEU B CD1 1 
ATOM 6078 C CD2 . LEU B 1 351 ? 17.861 108.904 176.378 1.00 38.71  ? 351 LEU B CD2 1 
ATOM 6079 N N   . VAL B 1 352 ? 16.147 113.420 174.277 1.00 33.76  ? 352 VAL B N   1 
ATOM 6080 C CA  . VAL B 1 352 ? 15.257 114.209 173.445 1.00 34.18  ? 352 VAL B CA  1 
ATOM 6081 C C   . VAL B 1 352 ? 15.915 115.064 172.382 1.00 34.60  ? 352 VAL B C   1 
ATOM 6082 O O   . VAL B 1 352 ? 15.494 115.045 171.221 1.00 34.44  ? 352 VAL B O   1 
ATOM 6083 C CB  . VAL B 1 352 ? 14.387 115.107 174.286 1.00 35.32  ? 352 VAL B CB  1 
ATOM 6084 C CG1 . VAL B 1 352 ? 13.559 115.999 173.392 1.00 36.00  ? 352 VAL B CG1 1 
ATOM 6085 C CG2 . VAL B 1 352 ? 13.496 114.271 175.153 1.00 35.91  ? 352 VAL B CG2 1 
ATOM 6086 N N   . CYS B 1 353 ? 16.924 115.833 172.778 1.00 34.84  ? 353 CYS B N   1 
ATOM 6087 C CA  . CYS B 1 353 ? 17.634 116.697 171.842 1.00 35.16  ? 353 CYS B CA  1 
ATOM 6088 C C   . CYS B 1 353 ? 18.569 115.946 170.886 1.00 35.82  ? 353 CYS B C   1 
ATOM 6089 O O   . CYS B 1 353 ? 18.672 116.332 169.740 1.00 36.10  ? 353 CYS B O   1 
ATOM 6090 C CB  . CYS B 1 353 ? 18.442 117.766 172.601 1.00 34.97  ? 353 CYS B CB  1 
ATOM 6091 S SG  . CYS B 1 353 ? 19.289 119.021 171.574 1.00 33.67  ? 353 CYS B SG  1 
ATOM 6092 N N   . PHE B 1 354 ? 19.225 114.872 171.327 1.00 36.43  ? 354 PHE B N   1 
ATOM 6093 C CA  . PHE B 1 354 ? 20.166 114.155 170.456 1.00 36.65  ? 354 PHE B CA  1 
ATOM 6094 C C   . PHE B 1 354 ? 19.750 112.859 169.772 1.00 37.21  ? 354 PHE B C   1 
ATOM 6095 O O   . PHE B 1 354 ? 20.314 112.506 168.746 1.00 37.88  ? 354 PHE B O   1 
ATOM 6096 C CB  . PHE B 1 354 ? 21.494 113.919 171.186 1.00 36.90  ? 354 PHE B CB  1 
ATOM 6097 C CG  . PHE B 1 354 ? 22.387 115.128 171.191 1.00 37.56  ? 354 PHE B CG  1 
ATOM 6098 C CD1 . PHE B 1 354 ? 21.938 116.330 171.746 1.00 36.03  ? 354 PHE B CD1 1 
ATOM 6099 C CD2 . PHE B 1 354 ? 23.646 115.096 170.584 1.00 38.89  ? 354 PHE B CD2 1 
ATOM 6100 C CE1 . PHE B 1 354 ? 22.708 117.488 171.683 1.00 35.13  ? 354 PHE B CE1 1 
ATOM 6101 C CE2 . PHE B 1 354 ? 24.442 116.265 170.512 1.00 38.58  ? 354 PHE B CE2 1 
ATOM 6102 C CZ  . PHE B 1 354 ? 23.962 117.458 171.069 1.00 36.82  ? 354 PHE B CZ  1 
ATOM 6103 N N   . CYS B 1 355 ? 18.792 112.140 170.329 1.00 36.87  ? 355 CYS B N   1 
ATOM 6104 C CA  . CYS B 1 355 ? 18.361 110.917 169.704 1.00 36.83  ? 355 CYS B CA  1 
ATOM 6105 C C   . CYS B 1 355 ? 16.987 111.097 169.062 1.00 38.04  ? 355 CYS B C   1 
ATOM 6106 O O   . CYS B 1 355 ? 16.846 110.831 167.891 1.00 38.57  ? 355 CYS B O   1 
ATOM 6107 C CB  . CYS B 1 355 ? 18.354 109.791 170.724 1.00 36.02  ? 355 CYS B CB  1 
ATOM 6108 S SG  . CYS B 1 355 ? 19.526 108.481 170.423 1.00 31.55  ? 355 CYS B SG  1 
ATOM 6109 N N   . PHE B 1 356 ? 15.980 111.583 169.778 1.00 38.77  ? 356 PHE B N   1 
ATOM 6110 C CA  . PHE B 1 356 ? 14.691 111.717 169.130 1.00 39.51  ? 356 PHE B CA  1 
ATOM 6111 C C   . PHE B 1 356 ? 14.657 112.909 168.196 1.00 40.31  ? 356 PHE B C   1 
ATOM 6112 O O   . PHE B 1 356 ? 13.817 112.960 167.310 1.00 41.30  ? 356 PHE B O   1 
ATOM 6113 C CB  . PHE B 1 356 ? 13.563 111.832 170.144 1.00 37.97  ? 356 PHE B CB  1 
ATOM 6114 C CG  . PHE B 1 356 ? 12.284 112.271 169.539 1.00 37.31  ? 356 PHE B CG  1 
ATOM 6115 C CD1 . PHE B 1 356 ? 11.483 111.395 168.845 1.00 37.00  ? 356 PHE B CD1 1 
ATOM 6116 C CD2 . PHE B 1 356 ? 11.945 113.596 169.543 1.00 36.09  ? 356 PHE B CD2 1 
ATOM 6117 C CE1 . PHE B 1 356 ? 10.360 111.863 168.154 1.00 37.38  ? 356 PHE B CE1 1 
ATOM 6118 C CE2 . PHE B 1 356 ? 10.832 114.055 168.858 1.00 35.90  ? 356 PHE B CE2 1 
ATOM 6119 C CZ  . PHE B 1 356 ? 10.046 113.203 168.166 1.00 36.94  ? 356 PHE B CZ  1 
ATOM 6120 N N   . PHE B 1 357 ? 15.573 113.852 168.349 1.00 41.32  ? 357 PHE B N   1 
ATOM 6121 C CA  . PHE B 1 357 ? 15.507 114.983 167.463 1.00 41.96  ? 357 PHE B CA  1 
ATOM 6122 C C   . PHE B 1 357 ? 16.543 115.190 166.378 1.00 41.30  ? 357 PHE B C   1 
ATOM 6123 O O   . PHE B 1 357 ? 16.304 115.886 165.388 1.00 40.74  ? 357 PHE B O   1 
ATOM 6124 C CB  . PHE B 1 357 ? 15.350 116.230 168.296 1.00 44.24  ? 357 PHE B CB  1 
ATOM 6125 C CG  . PHE B 1 357 ? 13.950 116.621 168.459 1.00 46.68  ? 357 PHE B CG  1 
ATOM 6126 C CD1 . PHE B 1 357 ? 13.240 117.057 167.357 1.00 47.55  ? 357 PHE B CD1 1 
ATOM 6127 C CD2 . PHE B 1 357 ? 13.322 116.541 169.683 1.00 47.74  ? 357 PHE B CD2 1 
ATOM 6128 C CE1 . PHE B 1 357 ? 11.922 117.418 167.456 1.00 48.63  ? 357 PHE B CE1 1 
ATOM 6129 C CE2 . PHE B 1 357 ? 11.992 116.902 169.801 1.00 49.75  ? 357 PHE B CE2 1 
ATOM 6130 C CZ  . PHE B 1 357 ? 11.284 117.343 168.678 1.00 49.71  ? 357 PHE B CZ  1 
ATOM 6131 N N   . LYS B 1 358 ? 17.698 114.585 166.548 1.00 40.07  ? 358 LYS B N   1 
ATOM 6132 C CA  . LYS B 1 358 ? 18.736 114.722 165.547 1.00 39.31  ? 358 LYS B CA  1 
ATOM 6133 C C   . LYS B 1 358 ? 18.519 113.654 164.505 1.00 37.96  ? 358 LYS B C   1 
ATOM 6134 O O   . LYS B 1 358 ? 18.281 113.957 163.349 1.00 37.56  ? 358 LYS B O   1 
ATOM 6135 C CB  . LYS B 1 358 ? 20.110 114.560 166.184 1.00 40.78  ? 358 LYS B CB  1 
ATOM 6136 C CG  . LYS B 1 358 ? 21.236 114.227 165.219 1.00 42.38  ? 358 LYS B CG  1 
ATOM 6137 C CD  . LYS B 1 358 ? 22.474 113.789 166.013 1.00 45.23  ? 358 LYS B CD  1 
ATOM 6138 C CE  . LYS B 1 358 ? 23.646 113.317 165.144 1.00 47.68  ? 358 LYS B CE  1 
ATOM 6139 N NZ  . LYS B 1 358 ? 24.782 112.816 165.983 1.00 48.31  ? 358 LYS B NZ  1 
ATOM 6140 N N   . GLN B 1 359 ? 18.594 112.401 164.924 1.00 37.33  ? 359 GLN B N   1 
ATOM 6141 C CA  . GLN B 1 359 ? 18.406 111.288 164.021 1.00 37.40  ? 359 GLN B CA  1 
ATOM 6142 C C   . GLN B 1 359 ? 17.193 111.530 163.125 1.00 37.38  ? 359 GLN B C   1 
ATOM 6143 O O   . GLN B 1 359 ? 17.259 111.334 161.907 1.00 37.72  ? 359 GLN B O   1 
ATOM 6144 C CB  . GLN B 1 359 ? 18.222 109.993 164.816 1.00 37.83  ? 359 GLN B CB  1 
ATOM 6145 C CG  . GLN B 1 359 ? 19.374 109.670 165.786 1.00 40.07  ? 359 GLN B CG  1 
ATOM 6146 C CD  . GLN B 1 359 ? 20.715 109.579 165.084 1.00 40.60  ? 359 GLN B CD  1 
ATOM 6147 O OE1 . GLN B 1 359 ? 20.781 109.748 163.877 1.00 41.25  ? 359 GLN B OE1 1 
ATOM 6148 N NE2 . GLN B 1 359 ? 21.789 109.306 165.834 1.00 40.64  ? 359 GLN B NE2 1 
ATOM 6149 N N   . LEU B 1 360 ? 16.088 111.978 163.710 1.00 36.65  ? 360 LEU B N   1 
ATOM 6150 C CA  . LEU B 1 360 ? 14.885 112.212 162.912 1.00 36.10  ? 360 LEU B CA  1 
ATOM 6151 C C   . LEU B 1 360 ? 15.197 113.108 161.728 1.00 34.93  ? 360 LEU B C   1 
ATOM 6152 O O   . LEU B 1 360 ? 14.921 112.764 160.577 1.00 35.38  ? 360 LEU B O   1 
ATOM 6153 C CB  . LEU B 1 360 ? 13.767 112.843 163.756 1.00 36.42  ? 360 LEU B CB  1 
ATOM 6154 C CG  . LEU B 1 360 ? 12.539 113.217 162.914 1.00 36.58  ? 360 LEU B CG  1 
ATOM 6155 C CD1 . LEU B 1 360 ? 12.013 111.974 162.212 1.00 36.49  ? 360 LEU B CD1 1 
ATOM 6156 C CD2 . LEU B 1 360 ? 11.468 113.845 163.785 1.00 36.08  ? 360 LEU B CD2 1 
ATOM 6157 N N   . ALA B 1 361 ? 15.782 114.259 162.025 1.00 33.51  ? 361 ALA B N   1 
ATOM 6158 C CA  . ALA B 1 361 ? 16.139 115.205 160.994 1.00 32.33  ? 361 ALA B CA  1 
ATOM 6159 C C   . ALA B 1 361 ? 16.893 114.495 159.910 1.00 31.64  ? 361 ALA B C   1 
ATOM 6160 O O   . ALA B 1 361 ? 16.599 114.661 158.736 1.00 32.52  ? 361 ALA B O   1 
ATOM 6161 C CB  . ALA B 1 361 ? 16.994 116.295 161.567 1.00 32.72  ? 361 ALA B CB  1 
ATOM 6162 N N   . MET B 1 362 ? 17.861 113.685 160.293 1.00 30.60  ? 362 MET B N   1 
ATOM 6163 C CA  . MET B 1 362 ? 18.642 112.998 159.288 1.00 29.89  ? 362 MET B CA  1 
ATOM 6164 C C   . MET B 1 362 ? 17.820 112.133 158.324 1.00 28.93  ? 362 MET B C   1 
ATOM 6165 O O   . MET B 1 362 ? 17.927 112.285 157.107 1.00 28.73  ? 362 MET B O   1 
ATOM 6166 C CB  . MET B 1 362 ? 19.754 112.223 159.976 1.00 30.51  ? 362 MET B CB  1 
ATOM 6167 C CG  . MET B 1 362 ? 20.570 113.153 160.884 1.00 31.63  ? 362 MET B CG  1 
ATOM 6168 S SD  . MET B 1 362 ? 22.172 112.517 161.375 1.00 33.69  ? 362 MET B SD  1 
ATOM 6169 C CE  . MET B 1 362 ? 22.806 112.020 159.750 1.00 34.95  ? 362 MET B CE  1 
ATOM 6170 N N   . ILE B 1 363 ? 16.971 111.257 158.830 1.00 27.49  ? 363 ILE B N   1 
ATOM 6171 C CA  . ILE B 1 363 ? 16.182 110.459 157.909 1.00 26.84  ? 363 ILE B CA  1 
ATOM 6172 C C   . ILE B 1 363 ? 15.621 111.325 156.792 1.00 26.66  ? 363 ILE B C   1 
ATOM 6173 O O   . ILE B 1 363 ? 15.564 110.909 155.652 1.00 26.33  ? 363 ILE B O   1 
ATOM 6174 C CB  . ILE B 1 363 ? 15.030 109.783 158.617 1.00 25.86  ? 363 ILE B CB  1 
ATOM 6175 C CG1 . ILE B 1 363 ? 15.581 108.898 159.731 1.00 24.94  ? 363 ILE B CG1 1 
ATOM 6176 C CG2 . ILE B 1 363 ? 14.225 108.981 157.624 1.00 25.17  ? 363 ILE B CG2 1 
ATOM 6177 C CD1 . ILE B 1 363 ? 14.527 108.199 160.548 1.00 24.32  ? 363 ILE B CD1 1 
ATOM 6178 N N   . PHE B 1 364 ? 15.213 112.539 157.107 1.00 27.33  ? 364 PHE B N   1 
ATOM 6179 C CA  . PHE B 1 364 ? 14.681 113.372 156.058 1.00 28.63  ? 364 PHE B CA  1 
ATOM 6180 C C   . PHE B 1 364 ? 15.727 114.056 155.212 1.00 28.86  ? 364 PHE B C   1 
ATOM 6181 O O   . PHE B 1 364 ? 15.788 113.845 154.001 1.00 28.40  ? 364 PHE B O   1 
ATOM 6182 C CB  . PHE B 1 364 ? 13.748 114.417 156.631 1.00 29.91  ? 364 PHE B CB  1 
ATOM 6183 C CG  . PHE B 1 364 ? 12.380 113.923 156.855 1.00 31.81  ? 364 PHE B CG  1 
ATOM 6184 C CD1 . PHE B 1 364 ? 12.120 112.568 156.858 1.00 32.92  ? 364 PHE B CD1 1 
ATOM 6185 C CD2 . PHE B 1 364 ? 11.336 114.811 157.044 1.00 32.51  ? 364 PHE B CD2 1 
ATOM 6186 C CE1 . PHE B 1 364 ? 10.831 112.095 157.045 1.00 34.22  ? 364 PHE B CE1 1 
ATOM 6187 C CE2 . PHE B 1 364 ? 10.038 114.353 157.232 1.00 33.81  ? 364 PHE B CE2 1 
ATOM 6188 C CZ  . PHE B 1 364 ? 9.782  112.991 157.233 1.00 34.23  ? 364 PHE B CZ  1 
ATOM 6189 N N   . MET B 1 365 ? 16.548 114.885 155.846 1.00 29.32  ? 365 MET B N   1 
ATOM 6190 C CA  . MET B 1 365 ? 17.566 115.625 155.120 1.00 29.98  ? 365 MET B CA  1 
ATOM 6191 C C   . MET B 1 365 ? 18.433 114.689 154.300 1.00 30.60  ? 365 MET B C   1 
ATOM 6192 O O   . MET B 1 365 ? 18.825 115.032 153.187 1.00 31.55  ? 365 MET B O   1 
ATOM 6193 C CB  . MET B 1 365 ? 18.421 116.482 156.074 1.00 29.91  ? 365 MET B CB  1 
ATOM 6194 C CG  . MET B 1 365 ? 17.648 117.642 156.711 1.00 29.05  ? 365 MET B CG  1 
ATOM 6195 S SD  . MET B 1 365 ? 18.594 118.787 157.677 1.00 29.73  ? 365 MET B SD  1 
ATOM 6196 C CE  . MET B 1 365 ? 19.225 119.774 156.468 1.00 29.43  ? 365 MET B CE  1 
ATOM 6197 N N   . SER B 1 366 ? 18.708 113.495 154.822 1.00 30.47  ? 366 SER B N   1 
ATOM 6198 C CA  . SER B 1 366 ? 19.539 112.523 154.090 1.00 30.25  ? 366 SER B CA  1 
ATOM 6199 C C   . SER B 1 366 ? 18.957 112.303 152.706 1.00 30.21  ? 366 SER B C   1 
ATOM 6200 O O   . SER B 1 366 ? 19.631 112.458 151.689 1.00 29.81  ? 366 SER B O   1 
ATOM 6201 C CB  . SER B 1 366 ? 19.579 111.158 154.787 1.00 29.65  ? 366 SER B CB  1 
ATOM 6202 O OG  . SER B 1 366 ? 20.079 111.229 156.109 1.00 30.84  ? 366 SER B OG  1 
ATOM 6203 N N   . VAL B 1 367 ? 17.691 111.924 152.698 1.00 30.41  ? 367 VAL B N   1 
ATOM 6204 C CA  . VAL B 1 367 ? 16.982 111.672 151.477 1.00 31.43  ? 367 VAL B CA  1 
ATOM 6205 C C   . VAL B 1 367 ? 16.998 112.940 150.620 1.00 31.89  ? 367 VAL B C   1 
ATOM 6206 O O   . VAL B 1 367 ? 17.468 112.911 149.482 1.00 32.30  ? 367 VAL B O   1 
ATOM 6207 C CB  . VAL B 1 367 ? 15.546 111.190 151.813 1.00 31.76  ? 367 VAL B CB  1 
ATOM 6208 C CG1 . VAL B 1 367 ? 14.741 110.977 150.569 1.00 32.56  ? 367 VAL B CG1 1 
ATOM 6209 C CG2 . VAL B 1 367 ? 15.626 109.879 152.588 1.00 31.36  ? 367 VAL B CG2 1 
ATOM 6210 N N   . LEU B 1 368 ? 16.535 114.062 151.159 1.00 32.66  ? 368 LEU B N   1 
ATOM 6211 C CA  . LEU B 1 368 ? 16.542 115.295 150.378 1.00 34.09  ? 368 LEU B CA  1 
ATOM 6212 C C   . LEU B 1 368 ? 17.922 115.428 149.761 1.00 34.52  ? 368 LEU B C   1 
ATOM 6213 O O   . LEU B 1 368 ? 18.077 115.582 148.553 1.00 33.83  ? 368 LEU B O   1 
ATOM 6214 C CB  . LEU B 1 368 ? 16.272 116.514 151.259 1.00 34.14  ? 368 LEU B CB  1 
ATOM 6215 C CG  . LEU B 1 368 ? 16.201 117.828 150.472 1.00 34.87  ? 368 LEU B CG  1 
ATOM 6216 C CD1 . LEU B 1 368 ? 14.858 117.889 149.764 1.00 34.88  ? 368 LEU B CD1 1 
ATOM 6217 C CD2 . LEU B 1 368 ? 16.363 119.035 151.378 1.00 34.24  ? 368 LEU B CD2 1 
ATOM 6218 N N   . ALA B 1 369 ? 18.929 115.337 150.611 1.00 35.92  ? 369 ALA B N   1 
ATOM 6219 C CA  . ALA B 1 369 ? 20.313 115.441 150.184 1.00 37.73  ? 369 ALA B CA  1 
ATOM 6220 C C   . ALA B 1 369 ? 20.551 114.547 149.007 1.00 38.98  ? 369 ALA B C   1 
ATOM 6221 O O   . ALA B 1 369 ? 20.904 115.015 147.932 1.00 39.52  ? 369 ALA B O   1 
ATOM 6222 C CB  . ALA B 1 369 ? 21.222 115.024 151.303 1.00 39.57  ? 369 ALA B CB  1 
ATOM 6223 N N   . GLY B 1 370 ? 20.380 113.250 149.240 1.00 40.42  ? 370 GLY B N   1 
ATOM 6224 C CA  . GLY B 1 370 ? 20.570 112.276 148.187 1.00 42.76  ? 370 GLY B CA  1 
ATOM 6225 C C   . GLY B 1 370 ? 20.051 112.833 146.880 1.00 43.86  ? 370 GLY B C   1 
ATOM 6226 O O   . GLY B 1 370 ? 20.820 113.218 146.001 1.00 43.93  ? 370 GLY B O   1 
ATOM 6227 N N   . ASN B 1 371 ? 18.735 112.886 146.751 1.00 44.60  ? 371 ASN B N   1 
ATOM 6228 C CA  . ASN B 1 371 ? 18.117 113.421 145.552 1.00 46.11  ? 371 ASN B CA  1 
ATOM 6229 C C   . ASN B 1 371 ? 18.882 114.622 145.045 1.00 46.63  ? 371 ASN B C   1 
ATOM 6230 O O   . ASN B 1 371 ? 19.400 114.600 143.939 1.00 46.50  ? 371 ASN B O   1 
ATOM 6231 C CB  . ASN B 1 371 ? 16.691 113.813 145.870 1.00 47.67  ? 371 ASN B CB  1 
ATOM 6232 C CG  . ASN B 1 371 ? 15.899 112.654 146.423 1.00 49.69  ? 371 ASN B CG  1 
ATOM 6233 O OD1 . ASN B 1 371 ? 15.165 112.800 147.401 1.00 52.02  ? 371 ASN B OD1 1 
ATOM 6234 N ND2 . ASN B 1 371 ? 16.049 111.482 145.803 1.00 49.95  ? 371 ASN B ND2 1 
ATOM 6235 N N   . MET B 1 372 ? 18.953 115.668 145.859 1.00 47.51  ? 372 MET B N   1 
ATOM 6236 C CA  . MET B 1 372 ? 19.678 116.880 145.487 1.00 47.91  ? 372 MET B CA  1 
ATOM 6237 C C   . MET B 1 372 ? 20.947 116.533 144.710 1.00 47.45  ? 372 MET B C   1 
ATOM 6238 O O   . MET B 1 372 ? 21.210 117.080 143.631 1.00 47.29  ? 372 MET B O   1 
ATOM 6239 C CB  . MET B 1 372 ? 20.073 117.650 146.745 1.00 49.15  ? 372 MET B CB  1 
ATOM 6240 C CG  . MET B 1 372 ? 18.926 118.201 147.561 1.00 50.59  ? 372 MET B CG  1 
ATOM 6241 S SD  . MET B 1 372 ? 19.575 119.300 148.826 1.00 51.23  ? 372 MET B SD  1 
ATOM 6242 C CE  . MET B 1 372 ? 19.866 120.804 147.813 1.00 49.99  ? 372 MET B CE  1 
ATOM 6243 N N   . TYR B 1 373 ? 21.741 115.633 145.285 1.00 46.90  ? 373 TYR B N   1 
ATOM 6244 C CA  . TYR B 1 373 ? 22.994 115.188 144.670 1.00 46.27  ? 373 TYR B CA  1 
ATOM 6245 C C   . TYR B 1 373 ? 22.705 114.711 143.237 1.00 47.15  ? 373 TYR B C   1 
ATOM 6246 O O   . TYR B 1 373 ? 23.167 115.302 142.255 1.00 46.80  ? 373 TYR B O   1 
ATOM 6247 C CB  . TYR B 1 373 ? 23.587 114.019 145.484 1.00 43.69  ? 373 TYR B CB  1 
ATOM 6248 C CG  . TYR B 1 373 ? 24.182 114.317 146.856 1.00 39.51  ? 373 TYR B CG  1 
ATOM 6249 C CD1 . TYR B 1 373 ? 25.313 115.084 146.990 1.00 38.26  ? 373 TYR B CD1 1 
ATOM 6250 C CD2 . TYR B 1 373 ? 23.679 113.731 148.000 1.00 37.45  ? 373 TYR B CD2 1 
ATOM 6251 C CE1 . TYR B 1 373 ? 25.932 115.251 148.231 1.00 36.49  ? 373 TYR B CE1 1 
ATOM 6252 C CE2 . TYR B 1 373 ? 24.299 113.900 149.232 1.00 35.91  ? 373 TYR B CE2 1 
ATOM 6253 C CZ  . TYR B 1 373 ? 25.427 114.656 149.334 1.00 35.40  ? 373 TYR B CZ  1 
ATOM 6254 O OH  . TYR B 1 373 ? 26.085 114.789 150.524 1.00 34.16  ? 373 TYR B OH  1 
ATOM 6255 N N   . GLU B 1 374 ? 21.929 113.634 143.154 1.00 48.18  ? 374 GLU B N   1 
ATOM 6256 C CA  . GLU B 1 374 ? 21.549 113.019 141.887 1.00 49.27  ? 374 GLU B CA  1 
ATOM 6257 C C   . GLU B 1 374 ? 21.078 114.059 140.889 1.00 48.52  ? 374 GLU B C   1 
ATOM 6258 O O   . GLU B 1 374 ? 21.587 114.138 139.776 1.00 48.95  ? 374 GLU B O   1 
ATOM 6259 C CB  . GLU B 1 374 ? 20.396 112.053 142.110 1.00 51.05  ? 374 GLU B CB  1 
ATOM 6260 C CG  . GLU B 1 374 ? 20.168 111.009 141.023 1.00 53.31  ? 374 GLU B CG  1 
ATOM 6261 C CD  . GLU B 1 374 ? 18.961 110.137 141.333 1.00 55.51  ? 374 GLU B CD  1 
ATOM 6262 O OE1 . GLU B 1 374 ? 18.848 109.712 142.515 1.00 57.29  ? 374 GLU B OE1 1 
ATOM 6263 O OE2 . GLU B 1 374 ? 18.130 109.869 140.422 1.00 56.16  ? 374 GLU B OE2 1 
ATOM 6264 N N   . SER B 1 375 ? 20.099 114.853 141.323 1.00 48.06  ? 375 SER B N   1 
ATOM 6265 C CA  . SER B 1 375 ? 19.471 115.872 140.491 1.00 46.40  ? 375 SER B CA  1 
ATOM 6266 C C   . SER B 1 375 ? 20.180 117.184 140.351 1.00 44.82  ? 375 SER B C   1 
ATOM 6267 O O   . SER B 1 375 ? 19.782 118.011 139.539 1.00 44.56  ? 375 SER B O   1 
ATOM 6268 C CB  . SER B 1 375 ? 18.059 116.176 140.978 1.00 47.33  ? 375 SER B CB  1 
ATOM 6269 O OG  . SER B 1 375 ? 18.061 116.674 142.326 1.00 47.60  ? 375 SER B OG  1 
ATOM 6270 N N   . ILE B 1 376 ? 21.222 117.412 141.126 1.00 42.18  ? 376 ILE B N   1 
ATOM 6271 C CA  . ILE B 1 376 ? 21.889 118.687 141.013 1.00 40.12  ? 376 ILE B CA  1 
ATOM 6272 C C   . ILE B 1 376 ? 23.374 118.570 140.955 1.00 38.44  ? 376 ILE B C   1 
ATOM 6273 O O   . ILE B 1 376 ? 24.027 119.433 140.390 1.00 39.23  ? 376 ILE B O   1 
ATOM 6274 C CB  . ILE B 1 376 ? 21.494 119.598 142.172 1.00 41.66  ? 376 ILE B CB  1 
ATOM 6275 C CG1 . ILE B 1 376 ? 20.012 119.952 142.023 1.00 43.13  ? 376 ILE B CG1 1 
ATOM 6276 C CG2 . ILE B 1 376 ? 22.386 120.834 142.193 1.00 41.42  ? 376 ILE B CG2 1 
ATOM 6277 C CD1 . ILE B 1 376 ? 19.473 120.911 143.086 1.00 44.46  ? 376 ILE B CD1 1 
ATOM 6278 N N   . GLY B 1 377 ? 23.910 117.512 141.544 1.00 36.05  ? 377 GLY B N   1 
ATOM 6279 C CA  . GLY B 1 377 ? 25.348 117.337 141.529 1.00 33.81  ? 377 GLY B CA  1 
ATOM 6280 C C   . GLY B 1 377 ? 25.949 117.710 142.860 1.00 30.93  ? 377 GLY B C   1 
ATOM 6281 O O   . GLY B 1 377 ? 25.513 118.655 143.494 1.00 30.25  ? 377 GLY B O   1 
ATOM 6282 N N   . PHE B 1 378 ? 26.957 116.966 143.275 1.00 28.69  ? 378 PHE B N   1 
ATOM 6283 C CA  . PHE B 1 378 ? 27.599 117.210 144.541 1.00 27.09  ? 378 PHE B CA  1 
ATOM 6284 C C   . PHE B 1 378 ? 27.761 118.658 144.931 1.00 27.22  ? 378 PHE B C   1 
ATOM 6285 O O   . PHE B 1 378 ? 27.062 119.164 145.813 1.00 26.50  ? 378 PHE B O   1 
ATOM 6286 C CB  . PHE B 1 378 ? 28.969 116.568 144.564 1.00 25.68  ? 378 PHE B CB  1 
ATOM 6287 C CG  . PHE B 1 378 ? 28.938 115.079 144.697 1.00 23.41  ? 378 PHE B CG  1 
ATOM 6288 C CD1 . PHE B 1 378 ? 28.395 114.288 143.710 1.00 22.70  ? 378 PHE B CD1 1 
ATOM 6289 C CD2 . PHE B 1 378 ? 29.476 114.467 145.802 1.00 21.02  ? 378 PHE B CD2 1 
ATOM 6290 C CE1 . PHE B 1 378 ? 28.397 112.915 143.834 1.00 21.38  ? 378 PHE B CE1 1 
ATOM 6291 C CE2 . PHE B 1 378 ? 29.477 113.104 145.925 1.00 19.89  ? 378 PHE B CE2 1 
ATOM 6292 C CZ  . PHE B 1 378 ? 28.937 112.333 144.936 1.00 20.61  ? 378 PHE B CZ  1 
ATOM 6293 N N   . GLN B 1 379 ? 28.698 119.329 144.277 1.00 28.06  ? 379 GLN B N   1 
ATOM 6294 C CA  . GLN B 1 379 ? 28.958 120.714 144.617 1.00 28.94  ? 379 GLN B CA  1 
ATOM 6295 C C   . GLN B 1 379 ? 27.685 121.525 144.573 1.00 28.84  ? 379 GLN B C   1 
ATOM 6296 O O   . GLN B 1 379 ? 27.460 122.396 145.412 1.00 28.22  ? 379 GLN B O   1 
ATOM 6297 C CB  . GLN B 1 379 ? 30.015 121.305 143.687 1.00 30.22  ? 379 GLN B CB  1 
ATOM 6298 C CG  . GLN B 1 379 ? 31.281 120.468 143.617 1.00 32.74  ? 379 GLN B CG  1 
ATOM 6299 C CD  . GLN B 1 379 ? 32.584 121.272 143.731 1.00 34.57  ? 379 GLN B CD  1 
ATOM 6300 O OE1 . GLN B 1 379 ? 33.675 120.709 143.717 1.00 35.76  ? 379 GLN B OE1 1 
ATOM 6301 N NE2 . GLN B 1 379 ? 32.471 122.576 143.854 1.00 35.60  ? 379 GLN B NE2 1 
ATOM 6302 N N   . GLY B 1 380 ? 26.839 121.209 143.604 1.00 29.03  ? 380 GLY B N   1 
ATOM 6303 C CA  . GLY B 1 380 ? 25.586 121.922 143.471 1.00 30.08  ? 380 GLY B CA  1 
ATOM 6304 C C   . GLY B 1 380 ? 24.825 121.933 144.778 1.00 29.62  ? 380 GLY B C   1 
ATOM 6305 O O   . GLY B 1 380 ? 24.691 122.970 145.424 1.00 29.43  ? 380 GLY B O   1 
ATOM 6306 N N   . ALA B 1 381 ? 24.329 120.768 145.174 1.00 29.10  ? 381 ALA B N   1 
ATOM 6307 C CA  . ALA B 1 381 ? 23.580 120.655 146.413 1.00 27.49  ? 381 ALA B CA  1 
ATOM 6308 C C   . ALA B 1 381 ? 24.294 121.429 147.495 1.00 26.03  ? 381 ALA B C   1 
ATOM 6309 O O   . ALA B 1 381 ? 23.708 122.258 148.189 1.00 25.41  ? 381 ALA B O   1 
ATOM 6310 C CB  . ALA B 1 381 ? 23.467 119.208 146.806 1.00 27.99  ? 381 ALA B CB  1 
ATOM 6311 N N   . TYR B 1 382 ? 25.580 121.155 147.608 1.00 24.68  ? 382 TYR B N   1 
ATOM 6312 C CA  . TYR B 1 382 ? 26.400 121.780 148.610 1.00 25.14  ? 382 TYR B CA  1 
ATOM 6313 C C   . TYR B 1 382 ? 26.012 123.200 148.927 1.00 24.00  ? 382 TYR B C   1 
ATOM 6314 O O   . TYR B 1 382 ? 25.783 123.540 150.073 1.00 23.63  ? 382 TYR B O   1 
ATOM 6315 C CB  . TYR B 1 382 ? 27.851 121.632 148.197 1.00 26.59  ? 382 TYR B CB  1 
ATOM 6316 C CG  . TYR B 1 382 ? 28.286 120.183 148.351 1.00 29.13  ? 382 TYR B CG  1 
ATOM 6317 C CD1 . TYR B 1 382 ? 27.350 119.164 148.556 1.00 29.59  ? 382 TYR B CD1 1 
ATOM 6318 C CD2 . TYR B 1 382 ? 29.626 119.831 148.362 1.00 31.07  ? 382 TYR B CD2 1 
ATOM 6319 C CE1 . TYR B 1 382 ? 27.754 117.832 148.777 1.00 30.95  ? 382 TYR B CE1 1 
ATOM 6320 C CE2 . TYR B 1 382 ? 30.035 118.499 148.585 1.00 31.67  ? 382 TYR B CE2 1 
ATOM 6321 C CZ  . TYR B 1 382 ? 29.100 117.513 148.791 1.00 31.18  ? 382 TYR B CZ  1 
ATOM 6322 O OH  . TYR B 1 382 ? 29.541 116.223 149.011 1.00 32.46  ? 382 TYR B OH  1 
ATOM 6323 N N   . LEU B 1 383 ? 25.897 124.047 147.934 1.00 22.98  ? 383 LEU B N   1 
ATOM 6324 C CA  . LEU B 1 383 ? 25.483 125.383 148.278 1.00 22.12  ? 383 LEU B CA  1 
ATOM 6325 C C   . LEU B 1 383 ? 24.306 125.336 149.221 1.00 21.03  ? 383 LEU B C   1 
ATOM 6326 O O   . LEU B 1 383 ? 24.345 125.902 150.294 1.00 20.33  ? 383 LEU B O   1 
ATOM 6327 C CB  . LEU B 1 383 ? 25.065 126.138 147.053 1.00 23.73  ? 383 LEU B CB  1 
ATOM 6328 C CG  . LEU B 1 383 ? 26.220 126.534 146.162 1.00 26.42  ? 383 LEU B CG  1 
ATOM 6329 C CD1 . LEU B 1 383 ? 25.689 127.211 144.886 1.00 28.39  ? 383 LEU B CD1 1 
ATOM 6330 C CD2 . LEU B 1 383 ? 27.119 127.448 146.955 1.00 25.61  ? 383 LEU B CD2 1 
ATOM 6331 N N   . VAL B 1 384 ? 23.247 124.660 148.824 1.00 20.83  ? 384 VAL B N   1 
ATOM 6332 C CA  . VAL B 1 384 ? 22.082 124.610 149.671 1.00 21.35  ? 384 VAL B CA  1 
ATOM 6333 C C   . VAL B 1 384 ? 22.469 124.265 151.086 1.00 21.39  ? 384 VAL B C   1 
ATOM 6334 O O   . VAL B 1 384 ? 22.156 124.998 152.014 1.00 23.08  ? 384 VAL B O   1 
ATOM 6335 C CB  . VAL B 1 384 ? 21.068 123.579 149.163 1.00 22.55  ? 384 VAL B CB  1 
ATOM 6336 C CG1 . VAL B 1 384 ? 19.883 123.476 150.118 1.00 24.66  ? 384 VAL B CG1 1 
ATOM 6337 C CG2 . VAL B 1 384 ? 20.585 123.999 147.807 1.00 22.32  ? 384 VAL B CG2 1 
ATOM 6338 N N   . LEU B 1 385 ? 23.185 123.170 151.267 1.00 20.01  ? 385 LEU B N   1 
ATOM 6339 C CA  . LEU B 1 385 ? 23.548 122.778 152.619 1.00 18.44  ? 385 LEU B CA  1 
ATOM 6340 C C   . LEU B 1 385 ? 24.496 123.734 153.304 1.00 18.24  ? 385 LEU B C   1 
ATOM 6341 O O   . LEU B 1 385 ? 24.146 124.384 154.293 1.00 17.08  ? 385 LEU B O   1 
ATOM 6342 C CB  . LEU B 1 385 ? 24.146 121.395 152.601 1.00 16.84  ? 385 LEU B CB  1 
ATOM 6343 C CG  . LEU B 1 385 ? 23.196 120.341 152.049 1.00 16.00  ? 385 LEU B CG  1 
ATOM 6344 C CD1 . LEU B 1 385 ? 23.898 119.017 152.167 1.00 15.37  ? 385 LEU B CD1 1 
ATOM 6345 C CD2 . LEU B 1 385 ? 21.868 120.333 152.799 1.00 15.80  ? 385 LEU B CD2 1 
ATOM 6346 N N   . GLY B 1 386 ? 25.709 123.803 152.783 1.00 18.67  ? 386 GLY B N   1 
ATOM 6347 C CA  . GLY B 1 386 ? 26.688 124.694 153.355 1.00 19.12  ? 386 GLY B CA  1 
ATOM 6348 C C   . GLY B 1 386 ? 26.087 126.042 153.668 1.00 19.91  ? 386 GLY B C   1 
ATOM 6349 O O   . GLY B 1 386 ? 26.411 126.622 154.691 1.00 20.33  ? 386 GLY B O   1 
ATOM 6350 N N   . LEU B 1 387 ? 25.205 126.541 152.805 1.00 20.72  ? 387 LEU B N   1 
ATOM 6351 C CA  . LEU B 1 387 ? 24.596 127.850 153.035 1.00 22.20  ? 387 LEU B CA  1 
ATOM 6352 C C   . LEU B 1 387 ? 23.709 127.728 154.235 1.00 22.61  ? 387 LEU B C   1 
ATOM 6353 O O   . LEU B 1 387 ? 23.924 128.395 155.250 1.00 22.79  ? 387 LEU B O   1 
ATOM 6354 C CB  . LEU B 1 387 ? 23.746 128.338 151.849 1.00 22.36  ? 387 LEU B CB  1 
ATOM 6355 C CG  . LEU B 1 387 ? 23.290 129.817 151.918 1.00 24.00  ? 387 LEU B CG  1 
ATOM 6356 C CD1 . LEU B 1 387 ? 24.510 130.735 151.795 1.00 23.77  ? 387 LEU B CD1 1 
ATOM 6357 C CD2 . LEU B 1 387 ? 22.282 130.139 150.807 1.00 24.43  ? 387 LEU B CD2 1 
ATOM 6358 N N   . VAL B 1 388 ? 22.705 126.870 154.124 1.00 23.29  ? 388 VAL B N   1 
ATOM 6359 C CA  . VAL B 1 388 ? 21.804 126.669 155.235 1.00 25.17  ? 388 VAL B CA  1 
ATOM 6360 C C   . VAL B 1 388 ? 22.624 126.469 156.501 1.00 25.42  ? 388 VAL B C   1 
ATOM 6361 O O   . VAL B 1 388 ? 22.223 126.911 157.578 1.00 26.39  ? 388 VAL B O   1 
ATOM 6362 C CB  . VAL B 1 388 ? 20.922 125.441 155.039 1.00 25.64  ? 388 VAL B CB  1 
ATOM 6363 C CG1 . VAL B 1 388 ? 20.341 125.018 156.375 1.00 26.68  ? 388 VAL B CG1 1 
ATOM 6364 C CG2 . VAL B 1 388 ? 19.796 125.768 154.072 1.00 26.19  ? 388 VAL B CG2 1 
ATOM 6365 N N   . ALA B 1 389 ? 23.773 125.812 156.375 1.00 25.47  ? 389 ALA B N   1 
ATOM 6366 C CA  . ALA B 1 389 ? 24.631 125.587 157.533 1.00 25.96  ? 389 ALA B CA  1 
ATOM 6367 C C   . ALA B 1 389 ? 25.136 126.893 158.129 1.00 26.40  ? 389 ALA B C   1 
ATOM 6368 O O   . ALA B 1 389 ? 24.862 127.196 159.288 1.00 26.58  ? 389 ALA B O   1 
ATOM 6369 C CB  . ALA B 1 389 ? 25.808 124.719 157.154 1.00 25.99  ? 389 ALA B CB  1 
ATOM 6370 N N   . LEU B 1 390 ? 25.877 127.664 157.339 1.00 26.93  ? 390 LEU B N   1 
ATOM 6371 C CA  . LEU B 1 390 ? 26.394 128.926 157.829 1.00 28.51  ? 390 LEU B CA  1 
ATOM 6372 C C   . LEU B 1 390 ? 25.305 129.789 158.413 1.00 30.40  ? 390 LEU B C   1 
ATOM 6373 O O   . LEU B 1 390 ? 25.480 130.352 159.484 1.00 30.60  ? 390 LEU B O   1 
ATOM 6374 C CB  . LEU B 1 390 ? 27.089 129.734 156.742 1.00 28.04  ? 390 LEU B CB  1 
ATOM 6375 C CG  . LEU B 1 390 ? 27.595 131.065 157.334 1.00 28.76  ? 390 LEU B CG  1 
ATOM 6376 C CD1 . LEU B 1 390 ? 28.869 131.486 156.644 1.00 28.38  ? 390 LEU B CD1 1 
ATOM 6377 C CD2 . LEU B 1 390 ? 26.533 132.151 157.232 1.00 28.38  ? 390 LEU B CD2 1 
ATOM 6378 N N   . GLY B 1 391 ? 24.191 129.927 157.706 1.00 31.33  ? 391 GLY B N   1 
ATOM 6379 C CA  . GLY B 1 391 ? 23.116 130.755 158.228 1.00 32.62  ? 391 GLY B CA  1 
ATOM 6380 C C   . GLY B 1 391 ? 22.674 130.328 159.617 1.00 32.94  ? 391 GLY B C   1 
ATOM 6381 O O   . GLY B 1 391 ? 22.484 131.138 160.533 1.00 32.55  ? 391 GLY B O   1 
ATOM 6382 N N   . PHE B 1 392 ? 22.502 129.027 159.777 1.00 33.61  ? 392 PHE B N   1 
ATOM 6383 C CA  . PHE B 1 392 ? 22.090 128.513 161.059 1.00 33.97  ? 392 PHE B CA  1 
ATOM 6384 C C   . PHE B 1 392 ? 23.219 128.756 162.047 1.00 33.66  ? 392 PHE B C   1 
ATOM 6385 O O   . PHE B 1 392 ? 22.962 129.090 163.190 1.00 34.00  ? 392 PHE B O   1 
ATOM 6386 C CB  . PHE B 1 392 ? 21.687 127.024 160.949 1.00 35.03  ? 392 PHE B CB  1 
ATOM 6387 C CG  . PHE B 1 392 ? 20.190 126.814 160.726 1.00 36.54  ? 392 PHE B CG  1 
ATOM 6388 C CD1 . PHE B 1 392 ? 19.342 127.908 160.587 1.00 37.62  ? 392 PHE B CD1 1 
ATOM 6389 C CD2 . PHE B 1 392 ? 19.626 125.541 160.696 1.00 36.46  ? 392 PHE B CD2 1 
ATOM 6390 C CE1 . PHE B 1 392 ? 17.965 127.742 160.425 1.00 38.08  ? 392 PHE B CE1 1 
ATOM 6391 C CE2 . PHE B 1 392 ? 18.235 125.370 160.533 1.00 36.83  ? 392 PHE B CE2 1 
ATOM 6392 C CZ  . PHE B 1 392 ? 17.410 126.473 160.399 1.00 37.15  ? 392 PHE B CZ  1 
ATOM 6393 N N   . THR B 1 393 ? 24.469 128.641 161.616 1.00 33.91  ? 393 THR B N   1 
ATOM 6394 C CA  . THR B 1 393 ? 25.576 128.896 162.538 1.00 34.97  ? 393 THR B CA  1 
ATOM 6395 C C   . THR B 1 393 ? 25.483 130.336 163.011 1.00 35.63  ? 393 THR B C   1 
ATOM 6396 O O   . THR B 1 393 ? 25.623 130.632 164.197 1.00 35.65  ? 393 THR B O   1 
ATOM 6397 C CB  . THR B 1 393 ? 26.954 128.697 161.867 1.00 34.79  ? 393 THR B CB  1 
ATOM 6398 O OG1 . THR B 1 393 ? 27.160 127.306 161.599 1.00 35.83  ? 393 THR B OG1 1 
ATOM 6399 C CG2 . THR B 1 393 ? 28.066 129.193 162.772 1.00 34.44  ? 393 THR B CG2 1 
ATOM 6400 N N   . LEU B 1 394 ? 25.229 131.233 162.070 1.00 36.00  ? 394 LEU B N   1 
ATOM 6401 C CA  . LEU B 1 394 ? 25.114 132.637 162.402 1.00 35.83  ? 394 LEU B CA  1 
ATOM 6402 C C   . LEU B 1 394 ? 24.020 132.857 163.432 1.00 35.02  ? 394 LEU B C   1 
ATOM 6403 O O   . LEU B 1 394 ? 24.289 133.354 164.528 1.00 34.46  ? 394 LEU B O   1 
ATOM 6404 C CB  . LEU B 1 394 ? 24.794 133.446 161.152 1.00 37.46  ? 394 LEU B CB  1 
ATOM 6405 C CG  . LEU B 1 394 ? 24.824 134.963 161.349 1.00 38.74  ? 394 LEU B CG  1 
ATOM 6406 C CD1 . LEU B 1 394 ? 26.286 135.397 161.401 1.00 39.62  ? 394 LEU B CD1 1 
ATOM 6407 C CD2 . LEU B 1 394 ? 24.086 135.683 160.219 1.00 38.57  ? 394 LEU B CD2 1 
ATOM 6408 N N   . ILE B 1 395 ? 22.794 132.477 163.073 1.00 35.06  ? 395 ILE B N   1 
ATOM 6409 C CA  . ILE B 1 395 ? 21.640 132.654 163.947 1.00 36.63  ? 395 ILE B CA  1 
ATOM 6410 C C   . ILE B 1 395 ? 21.941 132.253 165.381 1.00 38.34  ? 395 ILE B C   1 
ATOM 6411 O O   . ILE B 1 395 ? 21.595 132.974 166.310 1.00 39.01  ? 395 ILE B O   1 
ATOM 6412 C CB  . ILE B 1 395 ? 20.401 131.881 163.415 1.00 35.93  ? 395 ILE B CB  1 
ATOM 6413 C CG1 . ILE B 1 395 ? 20.053 132.398 162.023 1.00 36.83  ? 395 ILE B CG1 1 
ATOM 6414 C CG2 . ILE B 1 395 ? 19.195 132.117 164.298 1.00 35.67  ? 395 ILE B CG2 1 
ATOM 6415 C CD1 . ILE B 1 395 ? 18.671 131.993 161.512 1.00 36.86  ? 395 ILE B CD1 1 
ATOM 6416 N N   . SER B 1 396 ? 22.609 131.120 165.564 1.00 40.16  ? 396 SER B N   1 
ATOM 6417 C CA  . SER B 1 396 ? 22.958 130.649 166.901 1.00 41.86  ? 396 SER B CA  1 
ATOM 6418 C C   . SER B 1 396 ? 23.841 131.664 167.602 1.00 43.28  ? 396 SER B C   1 
ATOM 6419 O O   . SER B 1 396 ? 23.644 131.967 168.773 1.00 43.83  ? 396 SER B O   1 
ATOM 6420 C CB  . SER B 1 396 ? 23.682 129.306 166.825 1.00 41.14  ? 396 SER B CB  1 
ATOM 6421 O OG  . SER B 1 396 ? 22.751 128.237 166.872 1.00 40.21  ? 396 SER B OG  1 
ATOM 6422 N N   . VAL B 1 397 ? 24.818 132.190 166.882 1.00 45.31  ? 397 VAL B N   1 
ATOM 6423 C CA  . VAL B 1 397 ? 25.697 133.176 167.462 1.00 47.76  ? 397 VAL B CA  1 
ATOM 6424 C C   . VAL B 1 397 ? 24.892 134.290 168.090 1.00 50.25  ? 397 VAL B C   1 
ATOM 6425 O O   . VAL B 1 397 ? 25.081 134.618 169.255 1.00 50.06  ? 397 VAL B O   1 
ATOM 6426 C CB  . VAL B 1 397 ? 26.596 133.781 166.412 1.00 47.20  ? 397 VAL B CB  1 
ATOM 6427 C CG1 . VAL B 1 397 ? 27.324 134.987 166.977 1.00 46.56  ? 397 VAL B CG1 1 
ATOM 6428 C CG2 . VAL B 1 397 ? 27.569 132.736 165.942 1.00 48.03  ? 397 VAL B CG2 1 
ATOM 6429 N N   . PHE B 1 398 ? 23.995 134.868 167.301 1.00 53.50  ? 398 PHE B N   1 
ATOM 6430 C CA  . PHE B 1 398 ? 23.143 135.969 167.753 1.00 57.21  ? 398 PHE B CA  1 
ATOM 6431 C C   . PHE B 1 398 ? 22.047 135.460 168.703 1.00 58.09  ? 398 PHE B C   1 
ATOM 6432 O O   . PHE B 1 398 ? 21.399 136.253 169.368 1.00 58.62  ? 398 PHE B O   1 
ATOM 6433 C CB  . PHE B 1 398 ? 22.465 136.686 166.537 1.00 59.36  ? 398 PHE B CB  1 
ATOM 6434 C CG  . PHE B 1 398 ? 22.922 138.139 166.292 1.00 61.79  ? 398 PHE B CG  1 
ATOM 6435 C CD1 . PHE B 1 398 ? 24.237 138.428 165.893 1.00 62.69  ? 398 PHE B CD1 1 
ATOM 6436 C CD2 . PHE B 1 398 ? 22.050 139.216 166.516 1.00 62.43  ? 398 PHE B CD2 1 
ATOM 6437 C CE1 . PHE B 1 398 ? 24.664 139.762 165.689 1.00 63.18  ? 398 PHE B CE1 1 
ATOM 6438 C CE2 . PHE B 1 398 ? 22.466 140.556 166.314 1.00 63.01  ? 398 PHE B CE2 1 
ATOM 6439 C CZ  . PHE B 1 398 ? 23.781 140.822 165.918 1.00 63.29  ? 398 PHE B CZ  1 
ATOM 6440 N N   . THR B 1 399 ? 21.863 134.150 168.807 1.00 59.16  ? 399 THR B N   1 
ATOM 6441 C CA  . THR B 1 399 ? 20.775 133.635 169.627 1.00 60.16  ? 399 THR B CA  1 
ATOM 6442 C C   . THR B 1 399 ? 21.035 132.634 170.751 1.00 60.97  ? 399 THR B C   1 
ATOM 6443 O O   . THR B 1 399 ? 20.250 132.552 171.694 1.00 61.32  ? 399 THR B O   1 
ATOM 6444 C CB  . THR B 1 399 ? 19.708 133.039 168.716 1.00 60.03  ? 399 THR B CB  1 
ATOM 6445 O OG1 . THR B 1 399 ? 19.146 134.077 167.903 1.00 60.43  ? 399 THR B OG1 1 
ATOM 6446 C CG2 . THR B 1 399 ? 18.644 132.371 169.518 1.00 59.14  ? 399 THR B CG2 1 
ATOM 6447 N N   . LEU B 1 400 ? 22.116 131.873 170.655 1.00 61.43  ? 400 LEU B N   1 
ATOM 6448 C CA  . LEU B 1 400 ? 22.452 130.879 171.664 1.00 61.95  ? 400 LEU B CA  1 
ATOM 6449 C C   . LEU B 1 400 ? 22.450 131.483 173.061 1.00 62.73  ? 400 LEU B C   1 
ATOM 6450 O O   . LEU B 1 400 ? 22.383 132.695 173.207 1.00 63.35  ? 400 LEU B O   1 
ATOM 6451 C CB  . LEU B 1 400 ? 23.821 130.264 171.363 1.00 62.86  ? 400 LEU B CB  1 
ATOM 6452 C CG  . LEU B 1 400 ? 24.330 129.231 172.381 1.00 63.89  ? 400 LEU B CG  1 
ATOM 6453 C CD1 . LEU B 1 400 ? 23.345 128.048 172.465 1.00 64.03  ? 400 LEU B CD1 1 
ATOM 6454 C CD2 . LEU B 1 400 ? 25.718 128.727 171.968 1.00 64.44  ? 400 LEU B CD2 1 
ATOM 6455 N N   . SER B 1 401 ? 22.530 130.640 174.087 1.00 63.78  ? 401 SER B N   1 
ATOM 6456 C CA  . SER B 1 401 ? 22.496 131.104 175.472 1.00 65.60  ? 401 SER B CA  1 
ATOM 6457 C C   . SER B 1 401 ? 23.802 131.667 176.008 1.00 67.42  ? 401 SER B C   1 
ATOM 6458 O O   . SER B 1 401 ? 24.878 131.089 175.830 1.00 66.40  ? 401 SER B O   1 
ATOM 6459 C CB  . SER B 1 401 ? 22.030 129.978 176.389 1.00 65.16  ? 401 SER B CB  1 
ATOM 6460 O OG  . SER B 1 401 ? 21.177 130.445 177.414 1.00 64.52  ? 401 SER B OG  1 
ATOM 6461 N N   . GLY B 1 402 ? 23.655 132.793 176.707 1.00 70.04  ? 402 GLY B N   1 
ATOM 6462 C CA  . GLY B 1 402 ? 24.757 133.519 177.309 1.00 71.36  ? 402 GLY B CA  1 
ATOM 6463 C C   . GLY B 1 402 ? 26.019 132.737 177.543 1.00 73.50  ? 402 GLY B C   1 
ATOM 6464 O O   . GLY B 1 402 ? 26.005 131.625 178.069 1.00 73.29  ? 402 GLY B O   1 
ATOM 6465 N N   . PRO B 1 403 ? 27.144 133.318 177.137 1.00 75.38  ? 403 PRO B N   1 
ATOM 6466 C CA  . PRO B 1 403 ? 28.446 132.681 177.300 1.00 76.83  ? 403 PRO B CA  1 
ATOM 6467 C C   . PRO B 1 403 ? 28.764 132.674 178.791 1.00 78.24  ? 403 PRO B C   1 
ATOM 6468 O O   . PRO B 1 403 ? 29.577 131.882 179.277 1.00 78.35  ? 403 PRO B O   1 
ATOM 6469 C CB  . PRO B 1 403 ? 29.385 133.595 176.508 1.00 76.77  ? 403 PRO B CB  1 
ATOM 6470 C CG  . PRO B 1 403 ? 28.472 134.321 175.533 1.00 76.59  ? 403 PRO B CG  1 
ATOM 6471 C CD  . PRO B 1 403 ? 27.240 134.559 176.350 1.00 75.69  ? 403 PRO B CD  1 
ATOM 6472 N N   . GLY B 1 404 ? 28.100 133.573 179.508 1.00 79.86  ? 404 GLY B N   1 
ATOM 6473 C CA  . GLY B 1 404 ? 28.283 133.694 180.946 1.00 82.51  ? 404 GLY B CA  1 
ATOM 6474 C C   . GLY B 1 404 ? 26.933 134.073 181.515 1.00 83.71  ? 404 GLY B C   1 
ATOM 6475 O O   . GLY B 1 404 ? 26.707 135.236 181.898 1.00 84.21  ? 404 GLY B O   1 
ATOM 6476 N N   . PRO B 1 405 ? 26.019 133.091 181.588 1.00 84.25  ? 405 PRO B N   1 
ATOM 6477 C CA  . PRO B 1 405 ? 24.656 133.225 182.086 1.00 85.40  ? 405 PRO B CA  1 
ATOM 6478 C C   . PRO B 1 405 ? 24.609 134.050 183.330 1.00 86.30  ? 405 PRO B C   1 
ATOM 6479 O O   . PRO B 1 405 ? 25.656 134.428 183.880 1.00 86.78  ? 405 PRO B O   1 
ATOM 6480 C CB  . PRO B 1 405 ? 24.229 131.787 182.332 1.00 85.23  ? 405 PRO B CB  1 
ATOM 6481 C CG  . PRO B 1 405 ? 25.515 131.114 182.679 1.00 85.16  ? 405 PRO B CG  1 
ATOM 6482 C CD  . PRO B 1 405 ? 26.440 131.683 181.639 1.00 84.72  ? 405 PRO B CD  1 
ATOM 6483 N N   . LEU B 1 406 ? 23.380 134.309 183.767 1.00 86.85  ? 406 LEU B N   1 
ATOM 6484 C CA  . LEU B 1 406 ? 23.116 135.121 184.946 1.00 86.80  ? 406 LEU B CA  1 
ATOM 6485 C C   . LEU B 1 406 ? 23.860 134.770 186.259 1.00 87.01  ? 406 LEU B C   1 
ATOM 6486 O O   . LEU B 1 406 ? 23.471 135.264 187.311 1.00 86.68  ? 406 LEU B O   1 
ATOM 6487 C CB  . LEU B 1 406 ? 21.594 135.203 185.178 1.00 86.02  ? 406 LEU B CB  1 
ATOM 6488 C CG  . LEU B 1 406 ? 20.772 135.983 184.131 1.00 85.43  ? 406 LEU B CG  1 
ATOM 6489 C CD1 . LEU B 1 406 ? 19.412 135.335 184.017 1.00 84.90  ? 406 LEU B CD1 1 
ATOM 6490 C CD2 . LEU B 1 406 ? 20.643 137.460 184.509 1.00 85.49  ? 406 LEU B CD2 1 
ATOM 6491 N N   . SER B 1 407 ? 24.915 133.941 186.194 1.00 86.49  ? 407 SER B N   1 
ATOM 6492 C CA  . SER B 1 407 ? 25.763 133.581 187.357 1.00 85.58  ? 407 SER B CA  1 
ATOM 6493 C C   . SER B 1 407 ? 26.856 132.583 186.957 1.00 85.26  ? 407 SER B C   1 
ATOM 6494 O O   . SER B 1 407 ? 26.807 131.419 187.377 1.00 84.58  ? 407 SER B O   1 
ATOM 6495 C CB  . SER B 1 407 ? 24.933 132.971 188.498 1.00 85.39  ? 407 SER B CB  1 
ATOM 6496 O OG  . SER B 1 407 ? 25.791 132.375 189.461 1.00 84.41  ? 407 SER B OG  1 
ATOM 6497 N N   . LEU B 1 408 ? 27.839 133.035 186.164 1.00 85.05  ? 408 LEU B N   1 
ATOM 6498 C CA  . LEU B 1 408 ? 28.904 132.138 185.686 1.00 84.23  ? 408 LEU B CA  1 
ATOM 6499 C C   . LEU B 1 408 ? 29.947 131.650 186.691 1.00 83.69  ? 408 LEU B C   1 
ATOM 6500 O O   . LEU B 1 408 ? 30.249 130.461 186.719 1.00 82.77  ? 408 LEU B O   1 
ATOM 6501 C CB  . LEU B 1 408 ? 29.667 132.734 184.473 1.00 83.90  ? 408 LEU B CB  1 
ATOM 6502 C CG  . LEU B 1 408 ? 30.679 131.775 183.784 1.00 84.68  ? 408 LEU B CG  1 
ATOM 6503 C CD1 . LEU B 1 408 ? 29.945 130.739 182.904 1.00 84.22  ? 408 LEU B CD1 1 
ATOM 6504 C CD2 . LEU B 1 408 ? 31.674 132.581 182.932 1.00 84.86  ? 408 LEU B CD2 1 
ATOM 6505 N N   . LEU B 1 409 ? 30.519 132.552 187.488 1.00 82.88  ? 409 LEU B N   1 
ATOM 6506 C CA  . LEU B 1 409 ? 31.550 132.136 188.437 1.00 82.53  ? 409 LEU B CA  1 
ATOM 6507 C C   . LEU B 1 409 ? 31.012 131.093 189.410 1.00 82.41  ? 409 LEU B C   1 
ATOM 6508 O O   . LEU B 1 409 ? 31.711 130.121 189.721 1.00 81.96  ? 409 LEU B O   1 
ATOM 6509 C CB  . LEU B 1 409 ? 32.128 133.333 189.235 1.00 82.62  ? 409 LEU B CB  1 
ATOM 6510 C CG  . LEU B 1 409 ? 33.002 134.413 188.562 1.00 82.10  ? 409 LEU B CG  1 
ATOM 6511 C CD1 . LEU B 1 409 ? 33.747 135.204 189.640 1.00 81.28  ? 409 LEU B CD1 1 
ATOM 6512 C CD2 . LEU B 1 409 ? 34.002 133.758 187.613 1.00 82.87  ? 409 LEU B CD2 1 
ATOM 6513 N N   . ARG B 1 410 ? 29.768 131.293 189.862 1.00 82.68  ? 410 ARG B N   1 
ATOM 6514 C CA  . ARG B 1 410 ? 29.100 130.398 190.820 1.00 82.08  ? 410 ARG B CA  1 
ATOM 6515 C C   . ARG B 1 410 ? 28.877 129.002 190.232 1.00 82.33  ? 410 ARG B C   1 
ATOM 6516 O O   . ARG B 1 410 ? 29.167 127.984 190.873 1.00 81.82  ? 410 ARG B O   1 
ATOM 6517 C CB  . ARG B 1 410 ? 27.759 131.004 191.246 1.00 81.07  ? 410 ARG B CB  1 
ATOM 6518 C CG  . ARG B 1 410 ? 27.885 132.327 192.006 1.00 80.83  ? 410 ARG B CG  1 
ATOM 6519 C CD  . ARG B 1 410 ? 28.508 132.108 193.375 1.00 80.54  ? 410 ARG B CD  1 
ATOM 6520 N NE  . ARG B 1 410 ? 28.547 133.322 194.193 1.00 81.05  ? 410 ARG B NE  1 
ATOM 6521 C CZ  . ARG B 1 410 ? 28.903 133.343 195.479 1.00 80.84  ? 410 ARG B CZ  1 
ATOM 6522 N NH1 . ARG B 1 410 ? 29.249 132.218 196.092 1.00 81.57  ? 410 ARG B NH1 1 
ATOM 6523 N NH2 . ARG B 1 410 ? 28.909 134.481 196.163 1.00 81.11  ? 410 ARG B NH2 1 
ATOM 6524 N N   . ARG B 1 411 ? 28.357 128.965 189.010 1.00 82.07  ? 411 ARG B N   1 
ATOM 6525 C CA  . ARG B 1 411 ? 28.140 127.707 188.331 1.00 81.95  ? 411 ARG B CA  1 
ATOM 6526 C C   . ARG B 1 411 ? 29.483 127.163 187.758 1.00 83.01  ? 411 ARG B C   1 
ATOM 6527 O O   . ARG B 1 411 ? 29.634 125.932 187.635 1.00 82.44  ? 411 ARG B O   1 
ATOM 6528 C CB  . ARG B 1 411 ? 27.090 127.886 187.230 1.00 80.95  ? 411 ARG B CB  1 
ATOM 6529 C CG  . ARG B 1 411 ? 25.656 128.119 187.739 1.00 79.97  ? 411 ARG B CG  1 
ATOM 6530 C CD  . ARG B 1 411 ? 24.662 127.884 186.575 1.00 79.78  ? 411 ARG B CD  1 
ATOM 6531 N NE  . ARG B 1 411 ? 23.253 128.192 186.863 1.00 78.28  ? 411 ARG B NE  1 
ATOM 6532 C CZ  . ARG B 1 411 ? 22.234 127.929 186.035 1.00 76.90  ? 411 ARG B CZ  1 
ATOM 6533 N NH1 . ARG B 1 411 ? 22.445 127.352 184.862 1.00 76.28  ? 411 ARG B NH1 1 
ATOM 6534 N NH2 . ARG B 1 411 ? 20.993 128.242 186.375 1.00 75.87  ? 411 ARG B NH2 1 
ATOM 6535 N N   . GLN B 1 412 ? 30.446 128.052 187.418 1.00 83.52  ? 412 GLN B N   1 
ATOM 6536 C CA  . GLN B 1 412 ? 31.778 127.616 186.906 1.00 83.38  ? 412 GLN B CA  1 
ATOM 6537 C C   . GLN B 1 412 ? 32.490 126.878 188.053 1.00 83.48  ? 412 GLN B C   1 
ATOM 6538 O O   . GLN B 1 412 ? 33.449 126.123 187.848 1.00 82.70  ? 412 GLN B O   1 
ATOM 6539 C CB  . GLN B 1 412 ? 32.654 128.803 186.434 1.00 83.86  ? 412 GLN B CB  1 
ATOM 6540 C CG  . GLN B 1 412 ? 33.930 128.378 185.620 1.00 84.43  ? 412 GLN B CG  1 
ATOM 6541 C CD  . GLN B 1 412 ? 34.722 129.564 185.034 1.00 84.30  ? 412 GLN B CD  1 
ATOM 6542 O OE1 . GLN B 1 412 ? 34.309 130.723 185.165 1.00 84.28  ? 412 GLN B OE1 1 
ATOM 6543 N NE2 . GLN B 1 412 ? 35.859 129.271 184.381 1.00 83.38  ? 412 GLN B NE2 1 
ATOM 6544 N N   . VAL B 1 413 ? 31.993 127.127 189.262 1.00 83.89  ? 413 VAL B N   1 
ATOM 6545 C CA  . VAL B 1 413 ? 32.480 126.489 190.471 1.00 84.29  ? 413 VAL B CA  1 
ATOM 6546 C C   . VAL B 1 413 ? 31.788 125.126 190.533 1.00 85.73  ? 413 VAL B C   1 
ATOM 6547 O O   . VAL B 1 413 ? 32.326 124.177 191.101 1.00 85.36  ? 413 VAL B O   1 
ATOM 6548 C CB  . VAL B 1 413 ? 32.101 127.315 191.726 1.00 84.26  ? 413 VAL B CB  1 
ATOM 6549 C CG1 . VAL B 1 413 ? 32.481 126.562 193.002 1.00 83.85  ? 413 VAL B CG1 1 
ATOM 6550 C CG2 . VAL B 1 413 ? 32.799 128.661 191.674 1.00 83.96  ? 413 VAL B CG2 1 
ATOM 6551 N N   . ASN B 1 414 ? 30.600 125.043 189.930 1.00 86.85  ? 414 ASN B N   1 
ATOM 6552 C CA  . ASN B 1 414 ? 29.808 123.813 189.891 1.00 88.17  ? 414 ASN B CA  1 
ATOM 6553 C C   . ASN B 1 414 ? 30.513 122.736 189.065 1.00 89.63  ? 414 ASN B C   1 
ATOM 6554 O O   . ASN B 1 414 ? 30.461 121.542 189.395 1.00 89.79  ? 414 ASN B O   1 
ATOM 6555 C CB  . ASN B 1 414 ? 28.433 124.096 189.270 1.00 87.53  ? 414 ASN B CB  1 
ATOM 6556 C CG  . ASN B 1 414 ? 27.527 122.871 189.259 1.00 87.18  ? 414 ASN B CG  1 
ATOM 6557 O OD1 . ASN B 1 414 ? 27.994 121.744 189.407 1.00 86.79  ? 414 ASN B OD1 1 
ATOM 6558 N ND2 . ASN B 1 414 ? 26.224 123.091 189.076 1.00 86.15  ? 414 ASN B ND2 1 
ATOM 6559 N N   . GLU B 1 415 ? 31.144 123.163 187.973 1.00 91.10  ? 415 GLU B N   1 
ATOM 6560 C CA  . GLU B 1 415 ? 31.881 122.259 187.081 1.00 92.08  ? 415 GLU B CA  1 
ATOM 6561 C C   . GLU B 1 415 ? 33.257 121.907 187.666 1.00 92.58  ? 415 GLU B C   1 
ATOM 6562 O O   . GLU B 1 415 ? 33.727 120.769 187.527 1.00 92.02  ? 415 GLU B O   1 
ATOM 6563 C CB  . GLU B 1 415 ? 32.075 122.904 185.703 1.00 93.10  ? 415 GLU B CB  1 
ATOM 6564 C CG  . GLU B 1 415 ? 32.286 121.885 184.626 1.00 94.06  ? 415 GLU B CG  1 
ATOM 6565 C CD  . GLU B 1 415 ? 31.083 120.965 184.491 1.00 94.89  ? 415 GLU B CD  1 
ATOM 6566 O OE1 . GLU B 1 415 ? 30.406 120.692 185.515 1.00 94.37  ? 415 GLU B OE1 1 
ATOM 6567 O OE2 . GLU B 1 415 ? 30.821 120.501 183.359 1.00 95.69  ? 415 GLU B OE2 1 
ATOM 6568 N N   . VAL B 1 416 ? 33.896 122.895 188.306 1.00 92.63  ? 416 VAL B N   1 
ATOM 6569 C CA  . VAL B 1 416 ? 35.205 122.715 188.945 1.00 92.05  ? 416 VAL B CA  1 
ATOM 6570 C C   . VAL B 1 416 ? 35.051 121.739 190.137 1.00 92.55  ? 416 VAL B C   1 
ATOM 6571 O O   . VAL B 1 416 ? 35.629 120.636 190.133 1.00 92.57  ? 416 VAL B O   1 
ATOM 6572 C CB  . VAL B 1 416 ? 35.777 124.085 189.439 1.00 92.14  ? 416 VAL B CB  1 
ATOM 6573 C CG1 . VAL B 1 416 ? 37.128 123.873 190.107 1.00 92.49  ? 416 VAL B CG1 1 
ATOM 6574 C CG2 . VAL B 1 416 ? 35.932 125.055 188.264 1.00 91.09  ? 416 VAL B CG2 1 
ATOM 6575 N N   . ALA B 1 417 ? 34.274 122.154 191.141 1.00 92.35  ? 417 ALA B N   1 
ATOM 6576 C CA  . ALA B 1 417 ? 33.991 121.340 192.325 1.00 92.03  ? 417 ALA B CA  1 
ATOM 6577 C C   . ALA B 1 417 ? 33.376 120.015 191.841 1.00 92.25  ? 417 ALA B C   1 
ATOM 6578 O O   . ALA B 1 417 ? 33.717 118.941 192.404 1.00 92.22  ? 417 ALA B O   1 
ATOM 6579 C CB  . ALA B 1 417 ? 32.992 122.085 193.260 1.00 91.71  ? 417 ALA B CB  1 
ATOM 6580 O OXT . ALA B 1 417 ? 32.549 120.064 190.903 1.00 92.07  ? 417 ALA B OXT 1 
# 



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.