data_8XQV
# 
_entry.id   8XQV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8XQV         pdb_00008xqv 10.2210/pdb8xqv/pdb 
WWPDB D_1300043839 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8XQV 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gfyang@mail.ccnu.edu.cn 
_pdbx_contact_author.name_first         Guang-Fu 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4384-2593 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dong, J.'    1 ? 
'Lin, H.-Y.'  2 ? 
'Yang, G.-F.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of AtHPPD-YH23025 complex' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dong, J.'    1 ? 
primary 'Lin, H.-Y.'  2 ? 
primary 'Yang, G.-F.' 3 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '4-hydroxyphenylpyruvate dioxygenase' 44442.934 2  1.13.11.27 ? ? ? 
2 non-polymer syn 'COBALT (II) ION' 58.933    2  ?          ? ? ? 
3 non-polymer syn 
;4-[[1,6-dimethyl-2,5-bis(oxidanylidene)-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-3~{H}-1,4-benzodiazepin-4-yl]methyl]benzenecarbonitrile
;
457.478   2  ?          ? ? ? 
4 water       nat water 18.015    77 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '4-hydroxyphenylpyruvic acid oxidase,4HPPD,HPD,HPPDase' 
# 
_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       
;KNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEIKP
TTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSYKA
EDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLASND
EMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGDVL
SDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELFKSIEEY
EKT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;KNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEIKP
TTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSYKA
EDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLASND
EMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGDVL
SDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELFKSIEEY
EKT
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COBALT (II) ION' CO    
3 
;4-[[1,6-dimethyl-2,5-bis(oxidanylidene)-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-3~{H}-1,4-benzodiazepin-4-yl]methyl]benzenecarbonitrile
;
A1LWU 
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LYS n 
1 2   ASN n 
1 3   PRO n 
1 4   LYS n 
1 5   SER n 
1 6   ASP n 
1 7   LYS n 
1 8   PHE n 
1 9   LYS n 
1 10  VAL n 
1 11  LYS n 
1 12  ARG n 
1 13  PHE n 
1 14  HIS n 
1 15  HIS n 
1 16  ILE n 
1 17  GLU n 
1 18  PHE n 
1 19  TRP n 
1 20  CYS n 
1 21  GLY n 
1 22  ASP n 
1 23  ALA n 
1 24  THR n 
1 25  ASN n 
1 26  VAL n 
1 27  ALA n 
1 28  ARG n 
1 29  ARG n 
1 30  PHE n 
1 31  SER n 
1 32  TRP n 
1 33  GLY n 
1 34  LEU n 
1 35  GLY n 
1 36  MET n 
1 37  ARG n 
1 38  PHE n 
1 39  SER n 
1 40  ALA n 
1 41  LYS n 
1 42  SER n 
1 43  ASP n 
1 44  LEU n 
1 45  SER n 
1 46  THR n 
1 47  GLY n 
1 48  ASN n 
1 49  MET n 
1 50  VAL n 
1 51  HIS n 
1 52  ALA n 
1 53  SER n 
1 54  TYR n 
1 55  LEU n 
1 56  LEU n 
1 57  THR n 
1 58  SER n 
1 59  GLY n 
1 60  ASP n 
1 61  LEU n 
1 62  ARG n 
1 63  PHE n 
1 64  LEU n 
1 65  PHE n 
1 66  THR n 
1 67  ALA n 
1 68  PRO n 
1 69  TYR n 
1 70  SER n 
1 71  PRO n 
1 72  SER n 
1 73  LEU n 
1 74  SER n 
1 75  ALA n 
1 76  GLY n 
1 77  GLU n 
1 78  ILE n 
1 79  LYS n 
1 80  PRO n 
1 81  THR n 
1 82  THR n 
1 83  THR n 
1 84  ALA n 
1 85  SER n 
1 86  ILE n 
1 87  PRO n 
1 88  SER n 
1 89  PHE n 
1 90  ASP n 
1 91  HIS n 
1 92  GLY n 
1 93  SER n 
1 94  CYS n 
1 95  ARG n 
1 96  SER n 
1 97  PHE n 
1 98  PHE n 
1 99  SER n 
1 100 SER n 
1 101 HIS n 
1 102 GLY n 
1 103 LEU n 
1 104 GLY n 
1 105 VAL n 
1 106 ARG n 
1 107 ALA n 
1 108 VAL n 
1 109 ALA n 
1 110 ILE n 
1 111 GLU n 
1 112 VAL n 
1 113 GLU n 
1 114 ASP n 
1 115 ALA n 
1 116 GLU n 
1 117 SER n 
1 118 ALA n 
1 119 PHE n 
1 120 SER n 
1 121 ILE n 
1 122 SER n 
1 123 VAL n 
1 124 ALA n 
1 125 ASN n 
1 126 GLY n 
1 127 ALA n 
1 128 ILE n 
1 129 PRO n 
1 130 SER n 
1 131 SER n 
1 132 PRO n 
1 133 PRO n 
1 134 ILE n 
1 135 VAL n 
1 136 LEU n 
1 137 ASN n 
1 138 GLU n 
1 139 ALA n 
1 140 VAL n 
1 141 THR n 
1 142 ILE n 
1 143 ALA n 
1 144 GLU n 
1 145 VAL n 
1 146 LYS n 
1 147 LEU n 
1 148 TYR n 
1 149 GLY n 
1 150 ASP n 
1 151 VAL n 
1 152 VAL n 
1 153 LEU n 
1 154 ARG n 
1 155 TYR n 
1 156 VAL n 
1 157 SER n 
1 158 TYR n 
1 159 LYS n 
1 160 ALA n 
1 161 GLU n 
1 162 ASP n 
1 163 THR n 
1 164 GLU n 
1 165 LYS n 
1 166 SER n 
1 167 GLU n 
1 168 PHE n 
1 169 LEU n 
1 170 PRO n 
1 171 GLY n 
1 172 PHE n 
1 173 GLU n 
1 174 ARG n 
1 175 VAL n 
1 176 GLU n 
1 177 ASP n 
1 178 ALA n 
1 179 SER n 
1 180 SER n 
1 181 PHE n 
1 182 PRO n 
1 183 LEU n 
1 184 ASP n 
1 185 TYR n 
1 186 GLY n 
1 187 ILE n 
1 188 ARG n 
1 189 ARG n 
1 190 LEU n 
1 191 ASP n 
1 192 HIS n 
1 193 ALA n 
1 194 VAL n 
1 195 GLY n 
1 196 ASN n 
1 197 VAL n 
1 198 PRO n 
1 199 GLU n 
1 200 LEU n 
1 201 GLY n 
1 202 PRO n 
1 203 ALA n 
1 204 LEU n 
1 205 THR n 
1 206 TYR n 
1 207 VAL n 
1 208 ALA n 
1 209 GLY n 
1 210 PHE n 
1 211 THR n 
1 212 GLY n 
1 213 PHE n 
1 214 HIS n 
1 215 GLN n 
1 216 PHE n 
1 217 ALA n 
1 218 GLU n 
1 219 PHE n 
1 220 THR n 
1 221 ALA n 
1 222 ASP n 
1 223 ASP n 
1 224 VAL n 
1 225 GLY n 
1 226 THR n 
1 227 ALA n 
1 228 GLU n 
1 229 SER n 
1 230 GLY n 
1 231 LEU n 
1 232 ASN n 
1 233 SER n 
1 234 ALA n 
1 235 VAL n 
1 236 LEU n 
1 237 ALA n 
1 238 SER n 
1 239 ASN n 
1 240 ASP n 
1 241 GLU n 
1 242 MET n 
1 243 VAL n 
1 244 LEU n 
1 245 LEU n 
1 246 PRO n 
1 247 ILE n 
1 248 ASN n 
1 249 GLU n 
1 250 PRO n 
1 251 VAL n 
1 252 HIS n 
1 253 GLY n 
1 254 THR n 
1 255 LYS n 
1 256 ARG n 
1 257 LYS n 
1 258 SER n 
1 259 GLN n 
1 260 ILE n 
1 261 GLN n 
1 262 THR n 
1 263 TYR n 
1 264 LEU n 
1 265 GLU n 
1 266 HIS n 
1 267 ASN n 
1 268 GLU n 
1 269 GLY n 
1 270 ALA n 
1 271 GLY n 
1 272 LEU n 
1 273 GLN n 
1 274 HIS n 
1 275 LEU n 
1 276 ALA n 
1 277 LEU n 
1 278 MET n 
1 279 SER n 
1 280 GLU n 
1 281 ASP n 
1 282 ILE n 
1 283 PHE n 
1 284 ARG n 
1 285 THR n 
1 286 LEU n 
1 287 ARG n 
1 288 GLU n 
1 289 MET n 
1 290 ARG n 
1 291 LYS n 
1 292 ARG n 
1 293 SER n 
1 294 SER n 
1 295 ILE n 
1 296 GLY n 
1 297 GLY n 
1 298 PHE n 
1 299 ASP n 
1 300 PHE n 
1 301 MET n 
1 302 PRO n 
1 303 SER n 
1 304 PRO n 
1 305 PRO n 
1 306 PRO n 
1 307 THR n 
1 308 TYR n 
1 309 TYR n 
1 310 GLN n 
1 311 ASN n 
1 312 LEU n 
1 313 LYS n 
1 314 LYS n 
1 315 ARG n 
1 316 VAL n 
1 317 GLY n 
1 318 ASP n 
1 319 VAL n 
1 320 LEU n 
1 321 SER n 
1 322 ASP n 
1 323 ASP n 
1 324 GLN n 
1 325 ILE n 
1 326 LYS n 
1 327 GLU n 
1 328 CYS n 
1 329 GLU n 
1 330 GLU n 
1 331 LEU n 
1 332 GLY n 
1 333 ILE n 
1 334 LEU n 
1 335 VAL n 
1 336 ASP n 
1 337 ARG n 
1 338 ASP n 
1 339 ASP n 
1 340 GLN n 
1 341 GLY n 
1 342 THR n 
1 343 LEU n 
1 344 LEU n 
1 345 GLN n 
1 346 ILE n 
1 347 PHE n 
1 348 THR n 
1 349 LYS n 
1 350 PRO n 
1 351 LEU n 
1 352 GLY n 
1 353 ASP n 
1 354 ARG n 
1 355 PRO n 
1 356 THR n 
1 357 ILE n 
1 358 PHE n 
1 359 ILE n 
1 360 GLU n 
1 361 ILE n 
1 362 ILE n 
1 363 GLN n 
1 364 ARG n 
1 365 VAL n 
1 366 GLY n 
1 367 CYS n 
1 368 MET n 
1 369 MET n 
1 370 LYS n 
1 371 ASP n 
1 372 GLU n 
1 373 GLU n 
1 374 GLY n 
1 375 LYS n 
1 376 ALA n 
1 377 TYR n 
1 378 GLN n 
1 379 SER n 
1 380 GLY n 
1 381 GLY n 
1 382 CYS n 
1 383 GLY n 
1 384 GLY n 
1 385 PHE n 
1 386 GLY n 
1 387 LYS n 
1 388 GLY n 
1 389 ASN n 
1 390 PHE n 
1 391 SER n 
1 392 GLU n 
1 393 LEU n 
1 394 PHE n 
1 395 LYS n 
1 396 SER n 
1 397 ILE n 
1 398 GLU n 
1 399 GLU n 
1 400 TYR n 
1 401 GLU n 
1 402 LYS n 
1 403 THR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   403 
_entity_src_gen.gene_src_common_name               'thale cress' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HPD, PDS1, At1g06570, F12K11.9' 
_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      'Arabidopsis thaliana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1LWU non-polymer         . 
;4-[[1,6-dimethyl-2,5-bis(oxidanylidene)-7-(2-oxidanyl-6-oxidanylidene-cyclohexen-1-yl)carbonyl-3~{H}-1,4-benzodiazepin-4-yl]methyl]benzenecarbonitrile
;
? 'C26 H23 N3 O5'  457.478 
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 
CO    non-polymer         . 'COBALT (II) ION' ? 'Co 2'           58.933  
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
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   LYS 1   35  35  LYS LYS A . n 
A 1 2   ASN 2   36  36  ASN ASN A . n 
A 1 3   PRO 3   37  37  PRO PRO A . n 
A 1 4   LYS 4   38  38  LYS LYS A . n 
A 1 5   SER 5   39  39  SER SER A . n 
A 1 6   ASP 6   40  40  ASP ASP A . n 
A 1 7   LYS 7   41  41  LYS LYS A . n 
A 1 8   PHE 8   42  42  PHE PHE A . n 
A 1 9   LYS 9   43  43  LYS LYS A . n 
A 1 10  VAL 10  44  44  VAL VAL A . n 
A 1 11  LYS 11  45  45  LYS LYS A . n 
A 1 12  ARG 12  46  46  ARG ARG A . n 
A 1 13  PHE 13  47  47  PHE PHE A . n 
A 1 14  HIS 14  48  48  HIS HIS A . n 
A 1 15  HIS 15  49  49  HIS HIS A . n 
A 1 16  ILE 16  50  50  ILE ILE A . n 
A 1 17  GLU 17  51  51  GLU GLU A . n 
A 1 18  PHE 18  52  52  PHE PHE A . n 
A 1 19  TRP 19  53  53  TRP TRP A . n 
A 1 20  CYS 20  54  54  CYS CYS A . n 
A 1 21  GLY 21  55  55  GLY GLY A . n 
A 1 22  ASP 22  56  56  ASP ASP A . n 
A 1 23  ALA 23  57  57  ALA ALA A . n 
A 1 24  THR 24  58  58  THR THR A . n 
A 1 25  ASN 25  59  59  ASN ASN A . n 
A 1 26  VAL 26  60  60  VAL VAL A . n 
A 1 27  ALA 27  61  61  ALA ALA A . n 
A 1 28  ARG 28  62  62  ARG ARG A . n 
A 1 29  ARG 29  63  63  ARG ARG A . n 
A 1 30  PHE 30  64  64  PHE PHE A . n 
A 1 31  SER 31  65  65  SER SER A . n 
A 1 32  TRP 32  66  66  TRP TRP A . n 
A 1 33  GLY 33  67  67  GLY GLY A . n 
A 1 34  LEU 34  68  68  LEU LEU A . n 
A 1 35  GLY 35  69  69  GLY GLY A . n 
A 1 36  MET 36  70  70  MET MET A . n 
A 1 37  ARG 37  71  71  ARG ARG A . n 
A 1 38  PHE 38  72  72  PHE PHE A . n 
A 1 39  SER 39  73  73  SER SER A . n 
A 1 40  ALA 40  74  74  ALA ALA A . n 
A 1 41  LYS 41  75  75  LYS LYS A . n 
A 1 42  SER 42  76  76  SER SER A . n 
A 1 43  ASP 43  77  77  ASP ASP A . n 
A 1 44  LEU 44  78  78  LEU LEU A . n 
A 1 45  SER 45  79  79  SER SER A . n 
A 1 46  THR 46  80  80  THR THR A . n 
A 1 47  GLY 47  81  81  GLY GLY A . n 
A 1 48  ASN 48  82  82  ASN ASN A . n 
A 1 49  MET 49  83  83  MET MET A . n 
A 1 50  VAL 50  84  84  VAL VAL A . n 
A 1 51  HIS 51  85  85  HIS HIS A . n 
A 1 52  ALA 52  86  86  ALA ALA A . n 
A 1 53  SER 53  87  87  SER SER A . n 
A 1 54  TYR 54  88  88  TYR TYR A . n 
A 1 55  LEU 55  89  89  LEU LEU A . n 
A 1 56  LEU 56  90  90  LEU LEU A . n 
A 1 57  THR 57  91  91  THR THR A . n 
A 1 58  SER 58  92  92  SER SER A . n 
A 1 59  GLY 59  93  93  GLY GLY A . n 
A 1 60  ASP 60  94  94  ASP ASP A . n 
A 1 61  LEU 61  95  95  LEU LEU A . n 
A 1 62  ARG 62  96  96  ARG ARG A . n 
A 1 63  PHE 63  97  97  PHE PHE A . n 
A 1 64  LEU 64  98  98  LEU LEU A . n 
A 1 65  PHE 65  99  99  PHE PHE A . n 
A 1 66  THR 66  100 100 THR THR A . n 
A 1 67  ALA 67  101 101 ALA ALA A . n 
A 1 68  PRO 68  102 102 PRO PRO A . n 
A 1 69  TYR 69  103 103 TYR TYR A . n 
A 1 70  SER 70  104 104 SER SER A . n 
A 1 71  PRO 71  105 105 PRO PRO A . n 
A 1 72  SER 72  106 106 SER SER A . n 
A 1 73  LEU 73  107 107 LEU LEU A . n 
A 1 74  SER 74  108 108 SER SER A . n 
A 1 75  ALA 75  109 109 ALA ALA A . n 
A 1 76  GLY 76  110 110 GLY GLY A . n 
A 1 77  GLU 77  111 111 GLU GLU A . n 
A 1 78  ILE 78  112 112 ILE ILE A . n 
A 1 79  LYS 79  113 113 LYS LYS A . n 
A 1 80  PRO 80  114 114 PRO PRO A . n 
A 1 81  THR 81  115 115 THR THR A . n 
A 1 82  THR 82  116 116 THR THR A . n 
A 1 83  THR 83  117 117 THR THR A . n 
A 1 84  ALA 84  118 118 ALA ALA A . n 
A 1 85  SER 85  119 119 SER SER A . n 
A 1 86  ILE 86  120 120 ILE ILE A . n 
A 1 87  PRO 87  121 121 PRO PRO A . n 
A 1 88  SER 88  122 122 SER SER A . n 
A 1 89  PHE 89  123 123 PHE PHE A . n 
A 1 90  ASP 90  124 124 ASP ASP A . n 
A 1 91  HIS 91  125 125 HIS HIS A . n 
A 1 92  GLY 92  126 126 GLY GLY A . n 
A 1 93  SER 93  127 127 SER SER A . n 
A 1 94  CYS 94  128 128 CYS CYS A . n 
A 1 95  ARG 95  129 129 ARG ARG A . n 
A 1 96  SER 96  130 130 SER SER A . n 
A 1 97  PHE 97  131 131 PHE PHE A . n 
A 1 98  PHE 98  132 132 PHE PHE A . n 
A 1 99  SER 99  133 133 SER SER A . n 
A 1 100 SER 100 134 134 SER SER A . n 
A 1 101 HIS 101 135 135 HIS HIS A . n 
A 1 102 GLY 102 136 136 GLY GLY A . n 
A 1 103 LEU 103 137 137 LEU LEU A . n 
A 1 104 GLY 104 138 138 GLY GLY A . n 
A 1 105 VAL 105 139 139 VAL VAL A . n 
A 1 106 ARG 106 140 140 ARG ARG A . n 
A 1 107 ALA 107 141 141 ALA ALA A . n 
A 1 108 VAL 108 142 142 VAL VAL A . n 
A 1 109 ALA 109 143 143 ALA ALA A . n 
A 1 110 ILE 110 144 144 ILE ILE A . n 
A 1 111 GLU 111 145 145 GLU GLU A . n 
A 1 112 VAL 112 146 146 VAL VAL A . n 
A 1 113 GLU 113 147 147 GLU GLU A . n 
A 1 114 ASP 114 148 148 ASP ASP A . n 
A 1 115 ALA 115 149 149 ALA ALA A . n 
A 1 116 GLU 116 150 150 GLU GLU A . n 
A 1 117 SER 117 151 151 SER SER A . n 
A 1 118 ALA 118 152 152 ALA ALA A . n 
A 1 119 PHE 119 153 153 PHE PHE A . n 
A 1 120 SER 120 154 154 SER SER A . n 
A 1 121 ILE 121 155 155 ILE ILE A . n 
A 1 122 SER 122 156 156 SER SER A . n 
A 1 123 VAL 123 157 157 VAL VAL A . n 
A 1 124 ALA 124 158 158 ALA ALA A . n 
A 1 125 ASN 125 159 159 ASN ASN A . n 
A 1 126 GLY 126 160 160 GLY GLY A . n 
A 1 127 ALA 127 161 161 ALA ALA A . n 
A 1 128 ILE 128 162 162 ILE ILE A . n 
A 1 129 PRO 129 163 163 PRO PRO A . n 
A 1 130 SER 130 164 164 SER SER A . n 
A 1 131 SER 131 165 165 SER SER A . n 
A 1 132 PRO 132 166 166 PRO PRO A . n 
A 1 133 PRO 133 167 167 PRO PRO A . n 
A 1 134 ILE 134 168 168 ILE ILE A . n 
A 1 135 VAL 135 169 169 VAL VAL A . n 
A 1 136 LEU 136 170 170 LEU LEU A . n 
A 1 137 ASN 137 171 171 ASN ASN A . n 
A 1 138 GLU 138 172 172 GLU GLU A . n 
A 1 139 ALA 139 173 173 ALA ALA A . n 
A 1 140 VAL 140 174 174 VAL VAL A . n 
A 1 141 THR 141 175 175 THR THR A . n 
A 1 142 ILE 142 176 176 ILE ILE A . n 
A 1 143 ALA 143 177 177 ALA ALA A . n 
A 1 144 GLU 144 178 178 GLU GLU A . n 
A 1 145 VAL 145 179 179 VAL VAL A . n 
A 1 146 LYS 146 180 180 LYS LYS A . n 
A 1 147 LEU 147 181 181 LEU LEU A . n 
A 1 148 TYR 148 182 182 TYR TYR A . n 
A 1 149 GLY 149 183 183 GLY GLY A . n 
A 1 150 ASP 150 184 184 ASP ASP A . n 
A 1 151 VAL 151 185 185 VAL VAL A . n 
A 1 152 VAL 152 186 186 VAL VAL A . n 
A 1 153 LEU 153 187 187 LEU LEU A . n 
A 1 154 ARG 154 188 188 ARG ARG A . n 
A 1 155 TYR 155 189 189 TYR TYR A . n 
A 1 156 VAL 156 190 190 VAL VAL A . n 
A 1 157 SER 157 191 191 SER SER A . n 
A 1 158 TYR 158 192 192 TYR TYR A . n 
A 1 159 LYS 159 193 193 LYS LYS A . n 
A 1 160 ALA 160 194 194 ALA ALA A . n 
A 1 161 GLU 161 195 ?   ?   ?   A . n 
A 1 162 ASP 162 196 ?   ?   ?   A . n 
A 1 163 THR 163 197 ?   ?   ?   A . n 
A 1 164 GLU 164 198 ?   ?   ?   A . n 
A 1 165 LYS 165 199 ?   ?   ?   A . n 
A 1 166 SER 166 200 ?   ?   ?   A . n 
A 1 167 GLU 167 201 ?   ?   ?   A . n 
A 1 168 PHE 168 202 202 PHE PHE A . n 
A 1 169 LEU 169 203 203 LEU LEU A . n 
A 1 170 PRO 170 204 204 PRO PRO A . n 
A 1 171 GLY 171 205 205 GLY GLY A . n 
A 1 172 PHE 172 206 206 PHE PHE A . n 
A 1 173 GLU 173 207 207 GLU GLU A . n 
A 1 174 ARG 174 208 208 ARG ARG A . n 
A 1 175 VAL 175 209 209 VAL VAL A . n 
A 1 176 GLU 176 210 210 GLU GLU A . n 
A 1 177 ASP 177 211 211 ASP ASP A . n 
A 1 178 ALA 178 212 212 ALA ALA A . n 
A 1 179 SER 179 213 213 SER SER A . n 
A 1 180 SER 180 214 214 SER SER A . n 
A 1 181 PHE 181 215 215 PHE PHE A . n 
A 1 182 PRO 182 216 216 PRO PRO A . n 
A 1 183 LEU 183 217 217 LEU LEU A . n 
A 1 184 ASP 184 218 218 ASP ASP A . n 
A 1 185 TYR 185 219 219 TYR TYR A . n 
A 1 186 GLY 186 220 220 GLY GLY A . n 
A 1 187 ILE 187 221 221 ILE ILE A . n 
A 1 188 ARG 188 222 222 ARG ARG A . n 
A 1 189 ARG 189 223 223 ARG ARG A . n 
A 1 190 LEU 190 224 224 LEU LEU A . n 
A 1 191 ASP 191 225 225 ASP ASP A . n 
A 1 192 HIS 192 226 226 HIS HIS A . n 
A 1 193 ALA 193 227 227 ALA ALA A . n 
A 1 194 VAL 194 228 228 VAL VAL A . n 
A 1 195 GLY 195 229 229 GLY GLY A . n 
A 1 196 ASN 196 230 230 ASN ASN A . n 
A 1 197 VAL 197 231 231 VAL VAL A . n 
A 1 198 PRO 198 232 232 PRO PRO A . n 
A 1 199 GLU 199 233 233 GLU GLU A . n 
A 1 200 LEU 200 234 234 LEU LEU A . n 
A 1 201 GLY 201 235 235 GLY GLY A . n 
A 1 202 PRO 202 236 236 PRO PRO A . n 
A 1 203 ALA 203 237 237 ALA ALA A . n 
A 1 204 LEU 204 238 238 LEU LEU A . n 
A 1 205 THR 205 239 239 THR THR A . n 
A 1 206 TYR 206 240 240 TYR TYR A . n 
A 1 207 VAL 207 241 241 VAL VAL A . n 
A 1 208 ALA 208 242 242 ALA ALA A . n 
A 1 209 GLY 209 243 243 GLY GLY A . n 
A 1 210 PHE 210 244 244 PHE PHE A . n 
A 1 211 THR 211 245 245 THR THR A . n 
A 1 212 GLY 212 246 246 GLY GLY A . n 
A 1 213 PHE 213 247 247 PHE PHE A . n 
A 1 214 HIS 214 248 248 HIS HIS A . n 
A 1 215 GLN 215 249 249 GLN GLN A . n 
A 1 216 PHE 216 250 250 PHE PHE A . n 
A 1 217 ALA 217 251 251 ALA ALA A . n 
A 1 218 GLU 218 252 ?   ?   ?   A . n 
A 1 219 PHE 219 253 ?   ?   ?   A . n 
A 1 220 THR 220 254 ?   ?   ?   A . n 
A 1 221 ALA 221 255 ?   ?   ?   A . n 
A 1 222 ASP 222 256 ?   ?   ?   A . n 
A 1 223 ASP 223 257 ?   ?   ?   A . n 
A 1 224 VAL 224 258 ?   ?   ?   A . n 
A 1 225 GLY 225 259 ?   ?   ?   A . n 
A 1 226 THR 226 260 ?   ?   ?   A . n 
A 1 227 ALA 227 261 ?   ?   ?   A . n 
A 1 228 GLU 228 262 262 GLU GLU A . n 
A 1 229 SER 229 263 263 SER SER A . n 
A 1 230 GLY 230 264 264 GLY GLY A . n 
A 1 231 LEU 231 265 265 LEU LEU A . n 
A 1 232 ASN 232 266 266 ASN ASN A . n 
A 1 233 SER 233 267 267 SER SER A . n 
A 1 234 ALA 234 268 268 ALA ALA A . n 
A 1 235 VAL 235 269 269 VAL VAL A . n 
A 1 236 LEU 236 270 270 LEU LEU A . n 
A 1 237 ALA 237 271 271 ALA ALA A . n 
A 1 238 SER 238 272 272 SER SER A . n 
A 1 239 ASN 239 273 273 ASN ASN A . n 
A 1 240 ASP 240 274 274 ASP ASP A . n 
A 1 241 GLU 241 275 275 GLU GLU A . n 
A 1 242 MET 242 276 276 MET MET A . n 
A 1 243 VAL 243 277 277 VAL VAL A . n 
A 1 244 LEU 244 278 278 LEU LEU A . n 
A 1 245 LEU 245 279 279 LEU LEU A . n 
A 1 246 PRO 246 280 280 PRO PRO A . n 
A 1 247 ILE 247 281 281 ILE ILE A . n 
A 1 248 ASN 248 282 282 ASN ASN A . n 
A 1 249 GLU 249 283 283 GLU GLU A . n 
A 1 250 PRO 250 284 284 PRO PRO A . n 
A 1 251 VAL 251 285 285 VAL VAL A . n 
A 1 252 HIS 252 286 286 HIS HIS A . n 
A 1 253 GLY 253 287 287 GLY GLY A . n 
A 1 254 THR 254 288 288 THR THR A . n 
A 1 255 LYS 255 289 289 LYS LYS A . n 
A 1 256 ARG 256 290 290 ARG ARG A . n 
A 1 257 LYS 257 291 291 LYS LYS A . n 
A 1 258 SER 258 292 292 SER SER A . n 
A 1 259 GLN 259 293 293 GLN GLN A . n 
A 1 260 ILE 260 294 294 ILE ILE A . n 
A 1 261 GLN 261 295 295 GLN GLN A . n 
A 1 262 THR 262 296 296 THR THR A . n 
A 1 263 TYR 263 297 297 TYR TYR A . n 
A 1 264 LEU 264 298 298 LEU LEU A . n 
A 1 265 GLU 265 299 299 GLU GLU A . n 
A 1 266 HIS 266 300 300 HIS HIS A . n 
A 1 267 ASN 267 301 301 ASN ASN A . n 
A 1 268 GLU 268 302 302 GLU GLU A . n 
A 1 269 GLY 269 303 303 GLY GLY A . n 
A 1 270 ALA 270 304 304 ALA ALA A . n 
A 1 271 GLY 271 305 305 GLY GLY A . n 
A 1 272 LEU 272 306 306 LEU LEU A . n 
A 1 273 GLN 273 307 307 GLN GLN A . n 
A 1 274 HIS 274 308 308 HIS HIS A . n 
A 1 275 LEU 275 309 309 LEU LEU A . n 
A 1 276 ALA 276 310 310 ALA ALA A . n 
A 1 277 LEU 277 311 311 LEU LEU A . n 
A 1 278 MET 278 312 312 MET MET A . n 
A 1 279 SER 279 313 313 SER SER A . n 
A 1 280 GLU 280 314 314 GLU GLU A . n 
A 1 281 ASP 281 315 315 ASP ASP A . n 
A 1 282 ILE 282 316 316 ILE ILE A . n 
A 1 283 PHE 283 317 317 PHE PHE A . n 
A 1 284 ARG 284 318 318 ARG ARG A . n 
A 1 285 THR 285 319 319 THR THR A . n 
A 1 286 LEU 286 320 320 LEU LEU A . n 
A 1 287 ARG 287 321 321 ARG ARG A . n 
A 1 288 GLU 288 322 322 GLU GLU A . n 
A 1 289 MET 289 323 323 MET MET A . n 
A 1 290 ARG 290 324 324 ARG ARG A . n 
A 1 291 LYS 291 325 325 LYS LYS A . n 
A 1 292 ARG 292 326 326 ARG ARG A . n 
A 1 293 SER 293 327 327 SER SER A . n 
A 1 294 SER 294 328 328 SER SER A . n 
A 1 295 ILE 295 329 329 ILE ILE A . n 
A 1 296 GLY 296 330 330 GLY GLY A . n 
A 1 297 GLY 297 331 331 GLY GLY A . n 
A 1 298 PHE 298 332 332 PHE PHE A . n 
A 1 299 ASP 299 333 333 ASP ASP A . n 
A 1 300 PHE 300 334 334 PHE PHE A . n 
A 1 301 MET 301 335 335 MET MET A . n 
A 1 302 PRO 302 336 336 PRO PRO A . n 
A 1 303 SER 303 337 337 SER SER A . n 
A 1 304 PRO 304 338 338 PRO PRO A . n 
A 1 305 PRO 305 339 339 PRO PRO A . n 
A 1 306 PRO 306 340 340 PRO PRO A . n 
A 1 307 THR 307 341 341 THR THR A . n 
A 1 308 TYR 308 342 342 TYR TYR A . n 
A 1 309 TYR 309 343 343 TYR TYR A . n 
A 1 310 GLN 310 344 344 GLN GLN A . n 
A 1 311 ASN 311 345 345 ASN ASN A . n 
A 1 312 LEU 312 346 346 LEU LEU A . n 
A 1 313 LYS 313 347 347 LYS LYS A . n 
A 1 314 LYS 314 348 348 LYS LYS A . n 
A 1 315 ARG 315 349 349 ARG ARG A . n 
A 1 316 VAL 316 350 350 VAL VAL A . n 
A 1 317 GLY 317 351 351 GLY GLY A . n 
A 1 318 ASP 318 352 352 ASP ASP A . n 
A 1 319 VAL 319 353 353 VAL VAL A . n 
A 1 320 LEU 320 354 354 LEU LEU A . n 
A 1 321 SER 321 355 355 SER SER A . n 
A 1 322 ASP 322 356 356 ASP ASP A . n 
A 1 323 ASP 323 357 357 ASP ASP A . n 
A 1 324 GLN 324 358 358 GLN GLN A . n 
A 1 325 ILE 325 359 359 ILE ILE A . n 
A 1 326 LYS 326 360 360 LYS LYS A . n 
A 1 327 GLU 327 361 361 GLU GLU A . n 
A 1 328 CYS 328 362 362 CYS CYS A . n 
A 1 329 GLU 329 363 363 GLU GLU A . n 
A 1 330 GLU 330 364 364 GLU GLU A . n 
A 1 331 LEU 331 365 365 LEU LEU A . n 
A 1 332 GLY 332 366 366 GLY GLY A . n 
A 1 333 ILE 333 367 367 ILE ILE A . n 
A 1 334 LEU 334 368 368 LEU LEU A . n 
A 1 335 VAL 335 369 369 VAL VAL A . n 
A 1 336 ASP 336 370 370 ASP ASP A . n 
A 1 337 ARG 337 371 371 ARG ARG A . n 
A 1 338 ASP 338 372 372 ASP ASP A . n 
A 1 339 ASP 339 373 373 ASP ASP A . n 
A 1 340 GLN 340 374 374 GLN GLN A . n 
A 1 341 GLY 341 375 375 GLY GLY A . n 
A 1 342 THR 342 376 376 THR THR A . n 
A 1 343 LEU 343 377 377 LEU LEU A . n 
A 1 344 LEU 344 378 378 LEU LEU A . n 
A 1 345 GLN 345 379 379 GLN GLN A . n 
A 1 346 ILE 346 380 380 ILE ILE A . n 
A 1 347 PHE 347 381 381 PHE PHE A . n 
A 1 348 THR 348 382 382 THR THR A . n 
A 1 349 LYS 349 383 383 LYS LYS A . n 
A 1 350 PRO 350 384 384 PRO PRO A . n 
A 1 351 LEU 351 385 385 LEU LEU A . n 
A 1 352 GLY 352 386 386 GLY GLY A . n 
A 1 353 ASP 353 387 387 ASP ASP A . n 
A 1 354 ARG 354 388 388 ARG ARG A . n 
A 1 355 PRO 355 389 389 PRO PRO A . n 
A 1 356 THR 356 390 390 THR THR A . n 
A 1 357 ILE 357 391 391 ILE ILE A . n 
A 1 358 PHE 358 392 392 PHE PHE A . n 
A 1 359 ILE 359 393 393 ILE ILE A . n 
A 1 360 GLU 360 394 394 GLU GLU A . n 
A 1 361 ILE 361 395 395 ILE ILE A . n 
A 1 362 ILE 362 396 396 ILE ILE A . n 
A 1 363 GLN 363 397 397 GLN GLN A . n 
A 1 364 ARG 364 398 398 ARG ARG A . n 
A 1 365 VAL 365 399 399 VAL VAL A . n 
A 1 366 GLY 366 400 400 GLY GLY A . n 
A 1 367 CYS 367 401 401 CYS CYS A . n 
A 1 368 MET 368 402 402 MET MET A . n 
A 1 369 MET 369 403 ?   ?   ?   A . n 
A 1 370 LYS 370 404 ?   ?   ?   A . n 
A 1 371 ASP 371 405 ?   ?   ?   A . n 
A 1 372 GLU 372 406 ?   ?   ?   A . n 
A 1 373 GLU 373 407 ?   ?   ?   A . n 
A 1 374 GLY 374 408 ?   ?   ?   A . n 
A 1 375 LYS 375 409 ?   ?   ?   A . n 
A 1 376 ALA 376 410 ?   ?   ?   A . n 
A 1 377 TYR 377 411 411 TYR TYR A . n 
A 1 378 GLN 378 412 412 GLN GLN A . n 
A 1 379 SER 379 413 413 SER SER A . n 
A 1 380 GLY 380 414 414 GLY GLY A . n 
A 1 381 GLY 381 415 415 GLY GLY A . n 
A 1 382 CYS 382 416 416 CYS CYS A . n 
A 1 383 GLY 383 417 417 GLY GLY A . n 
A 1 384 GLY 384 418 418 GLY GLY A . n 
A 1 385 PHE 385 419 419 PHE PHE A . n 
A 1 386 GLY 386 420 420 GLY GLY A . n 
A 1 387 LYS 387 421 421 LYS LYS A . n 
A 1 388 GLY 388 422 422 GLY GLY A . n 
A 1 389 ASN 389 423 423 ASN ASN A . n 
A 1 390 PHE 390 424 424 PHE PHE A . n 
A 1 391 SER 391 425 425 SER SER A . n 
A 1 392 GLU 392 426 426 GLU GLU A . n 
A 1 393 LEU 393 427 427 LEU LEU A . n 
A 1 394 PHE 394 428 428 PHE PHE A . n 
A 1 395 LYS 395 429 429 LYS LYS A . n 
A 1 396 SER 396 430 430 SER SER A . n 
A 1 397 ILE 397 431 431 ILE ILE A . n 
A 1 398 GLU 398 432 432 GLU GLU A . n 
A 1 399 GLU 399 433 433 GLU GLU A . n 
A 1 400 TYR 400 434 434 TYR TYR A . n 
A 1 401 GLU 401 435 435 GLU GLU A . n 
A 1 402 LYS 402 436 436 LYS LYS A . n 
A 1 403 THR 403 437 ?   ?   ?   A . n 
B 1 1   LYS 1   35  ?   ?   ?   B . n 
B 1 2   ASN 2   36  36  ASN ASN B . n 
B 1 3   PRO 3   37  37  PRO PRO B . n 
B 1 4   LYS 4   38  38  LYS LYS B . n 
B 1 5   SER 5   39  39  SER SER B . n 
B 1 6   ASP 6   40  40  ASP ASP B . n 
B 1 7   LYS 7   41  41  LYS LYS B . n 
B 1 8   PHE 8   42  42  PHE PHE B . n 
B 1 9   LYS 9   43  43  LYS LYS B . n 
B 1 10  VAL 10  44  44  VAL VAL B . n 
B 1 11  LYS 11  45  45  LYS LYS B . n 
B 1 12  ARG 12  46  46  ARG ARG B . n 
B 1 13  PHE 13  47  47  PHE PHE B . n 
B 1 14  HIS 14  48  48  HIS HIS B . n 
B 1 15  HIS 15  49  49  HIS HIS B . n 
B 1 16  ILE 16  50  50  ILE ILE B . n 
B 1 17  GLU 17  51  51  GLU GLU B . n 
B 1 18  PHE 18  52  52  PHE PHE B . n 
B 1 19  TRP 19  53  53  TRP TRP B . n 
B 1 20  CYS 20  54  54  CYS CYS B . n 
B 1 21  GLY 21  55  55  GLY GLY B . n 
B 1 22  ASP 22  56  56  ASP ASP B . n 
B 1 23  ALA 23  57  57  ALA ALA B . n 
B 1 24  THR 24  58  58  THR THR B . n 
B 1 25  ASN 25  59  59  ASN ASN B . n 
B 1 26  VAL 26  60  60  VAL VAL B . n 
B 1 27  ALA 27  61  61  ALA ALA B . n 
B 1 28  ARG 28  62  62  ARG ARG B . n 
B 1 29  ARG 29  63  63  ARG ARG B . n 
B 1 30  PHE 30  64  64  PHE PHE B . n 
B 1 31  SER 31  65  65  SER SER B . n 
B 1 32  TRP 32  66  66  TRP TRP B . n 
B 1 33  GLY 33  67  67  GLY GLY B . n 
B 1 34  LEU 34  68  68  LEU LEU B . n 
B 1 35  GLY 35  69  69  GLY GLY B . n 
B 1 36  MET 36  70  70  MET MET B . n 
B 1 37  ARG 37  71  71  ARG ARG B . n 
B 1 38  PHE 38  72  72  PHE PHE B . n 
B 1 39  SER 39  73  73  SER SER B . n 
B 1 40  ALA 40  74  74  ALA ALA B . n 
B 1 41  LYS 41  75  75  LYS LYS B . n 
B 1 42  SER 42  76  76  SER SER B . n 
B 1 43  ASP 43  77  77  ASP ASP B . n 
B 1 44  LEU 44  78  78  LEU LEU B . n 
B 1 45  SER 45  79  79  SER SER B . n 
B 1 46  THR 46  80  80  THR THR B . n 
B 1 47  GLY 47  81  81  GLY GLY B . n 
B 1 48  ASN 48  82  82  ASN ASN B . n 
B 1 49  MET 49  83  83  MET MET B . n 
B 1 50  VAL 50  84  84  VAL VAL B . n 
B 1 51  HIS 51  85  85  HIS HIS B . n 
B 1 52  ALA 52  86  86  ALA ALA B . n 
B 1 53  SER 53  87  87  SER SER B . n 
B 1 54  TYR 54  88  88  TYR TYR B . n 
B 1 55  LEU 55  89  89  LEU LEU B . n 
B 1 56  LEU 56  90  90  LEU LEU B . n 
B 1 57  THR 57  91  91  THR THR B . n 
B 1 58  SER 58  92  92  SER SER B . n 
B 1 59  GLY 59  93  93  GLY GLY B . n 
B 1 60  ASP 60  94  94  ASP ASP B . n 
B 1 61  LEU 61  95  95  LEU LEU B . n 
B 1 62  ARG 62  96  96  ARG ARG B . n 
B 1 63  PHE 63  97  97  PHE PHE B . n 
B 1 64  LEU 64  98  98  LEU LEU B . n 
B 1 65  PHE 65  99  99  PHE PHE B . n 
B 1 66  THR 66  100 100 THR THR B . n 
B 1 67  ALA 67  101 101 ALA ALA B . n 
B 1 68  PRO 68  102 102 PRO PRO B . n 
B 1 69  TYR 69  103 103 TYR TYR B . n 
B 1 70  SER 70  104 104 SER SER B . n 
B 1 71  PRO 71  105 105 PRO PRO B . n 
B 1 72  SER 72  106 106 SER SER B . n 
B 1 73  LEU 73  107 107 LEU LEU B . n 
B 1 74  SER 74  108 108 SER SER B . n 
B 1 75  ALA 75  109 109 ALA ALA B . n 
B 1 76  GLY 76  110 110 GLY GLY B . n 
B 1 77  GLU 77  111 111 GLU GLU B . n 
B 1 78  ILE 78  112 112 ILE ILE B . n 
B 1 79  LYS 79  113 113 LYS LYS B . n 
B 1 80  PRO 80  114 114 PRO PRO B . n 
B 1 81  THR 81  115 115 THR THR B . n 
B 1 82  THR 82  116 116 THR THR B . n 
B 1 83  THR 83  117 117 THR THR B . n 
B 1 84  ALA 84  118 118 ALA ALA B . n 
B 1 85  SER 85  119 119 SER SER B . n 
B 1 86  ILE 86  120 120 ILE ILE B . n 
B 1 87  PRO 87  121 121 PRO PRO B . n 
B 1 88  SER 88  122 122 SER SER B . n 
B 1 89  PHE 89  123 123 PHE PHE B . n 
B 1 90  ASP 90  124 124 ASP ASP B . n 
B 1 91  HIS 91  125 125 HIS HIS B . n 
B 1 92  GLY 92  126 126 GLY GLY B . n 
B 1 93  SER 93  127 127 SER SER B . n 
B 1 94  CYS 94  128 128 CYS CYS B . n 
B 1 95  ARG 95  129 129 ARG ARG B . n 
B 1 96  SER 96  130 130 SER SER B . n 
B 1 97  PHE 97  131 131 PHE PHE B . n 
B 1 98  PHE 98  132 132 PHE PHE B . n 
B 1 99  SER 99  133 133 SER SER B . n 
B 1 100 SER 100 134 134 SER SER B . n 
B 1 101 HIS 101 135 135 HIS HIS B . n 
B 1 102 GLY 102 136 136 GLY GLY B . n 
B 1 103 LEU 103 137 137 LEU LEU B . n 
B 1 104 GLY 104 138 138 GLY GLY B . n 
B 1 105 VAL 105 139 139 VAL VAL B . n 
B 1 106 ARG 106 140 140 ARG ARG B . n 
B 1 107 ALA 107 141 141 ALA ALA B . n 
B 1 108 VAL 108 142 142 VAL VAL B . n 
B 1 109 ALA 109 143 143 ALA ALA B . n 
B 1 110 ILE 110 144 144 ILE ILE B . n 
B 1 111 GLU 111 145 145 GLU GLU B . n 
B 1 112 VAL 112 146 146 VAL VAL B . n 
B 1 113 GLU 113 147 147 GLU GLU B . n 
B 1 114 ASP 114 148 148 ASP ASP B . n 
B 1 115 ALA 115 149 149 ALA ALA B . n 
B 1 116 GLU 116 150 150 GLU GLU B . n 
B 1 117 SER 117 151 151 SER SER B . n 
B 1 118 ALA 118 152 152 ALA ALA B . n 
B 1 119 PHE 119 153 153 PHE PHE B . n 
B 1 120 SER 120 154 154 SER SER B . n 
B 1 121 ILE 121 155 155 ILE ILE B . n 
B 1 122 SER 122 156 156 SER SER B . n 
B 1 123 VAL 123 157 157 VAL VAL B . n 
B 1 124 ALA 124 158 158 ALA ALA B . n 
B 1 125 ASN 125 159 159 ASN ASN B . n 
B 1 126 GLY 126 160 160 GLY GLY B . n 
B 1 127 ALA 127 161 161 ALA ALA B . n 
B 1 128 ILE 128 162 162 ILE ILE B . n 
B 1 129 PRO 129 163 163 PRO PRO B . n 
B 1 130 SER 130 164 164 SER SER B . n 
B 1 131 SER 131 165 165 SER SER B . n 
B 1 132 PRO 132 166 166 PRO PRO B . n 
B 1 133 PRO 133 167 167 PRO PRO B . n 
B 1 134 ILE 134 168 168 ILE ILE B . n 
B 1 135 VAL 135 169 169 VAL VAL B . n 
B 1 136 LEU 136 170 170 LEU LEU B . n 
B 1 137 ASN 137 171 171 ASN ASN B . n 
B 1 138 GLU 138 172 172 GLU GLU B . n 
B 1 139 ALA 139 173 173 ALA ALA B . n 
B 1 140 VAL 140 174 174 VAL VAL B . n 
B 1 141 THR 141 175 175 THR THR B . n 
B 1 142 ILE 142 176 176 ILE ILE B . n 
B 1 143 ALA 143 177 177 ALA ALA B . n 
B 1 144 GLU 144 178 178 GLU GLU B . n 
B 1 145 VAL 145 179 179 VAL VAL B . n 
B 1 146 LYS 146 180 180 LYS LYS B . n 
B 1 147 LEU 147 181 181 LEU LEU B . n 
B 1 148 TYR 148 182 182 TYR TYR B . n 
B 1 149 GLY 149 183 183 GLY GLY B . n 
B 1 150 ASP 150 184 184 ASP ASP B . n 
B 1 151 VAL 151 185 185 VAL VAL B . n 
B 1 152 VAL 152 186 186 VAL VAL B . n 
B 1 153 LEU 153 187 187 LEU LEU B . n 
B 1 154 ARG 154 188 188 ARG ARG B . n 
B 1 155 TYR 155 189 189 TYR TYR B . n 
B 1 156 VAL 156 190 190 VAL VAL B . n 
B 1 157 SER 157 191 191 SER SER B . n 
B 1 158 TYR 158 192 192 TYR TYR B . n 
B 1 159 LYS 159 193 193 LYS LYS B . n 
B 1 160 ALA 160 194 194 ALA ALA B . n 
B 1 161 GLU 161 195 ?   ?   ?   B . n 
B 1 162 ASP 162 196 ?   ?   ?   B . n 
B 1 163 THR 163 197 ?   ?   ?   B . n 
B 1 164 GLU 164 198 ?   ?   ?   B . n 
B 1 165 LYS 165 199 ?   ?   ?   B . n 
B 1 166 SER 166 200 ?   ?   ?   B . n 
B 1 167 GLU 167 201 201 GLU GLU B . n 
B 1 168 PHE 168 202 202 PHE PHE B . n 
B 1 169 LEU 169 203 203 LEU LEU B . n 
B 1 170 PRO 170 204 204 PRO PRO B . n 
B 1 171 GLY 171 205 205 GLY GLY B . n 
B 1 172 PHE 172 206 206 PHE PHE B . n 
B 1 173 GLU 173 207 207 GLU GLU B . n 
B 1 174 ARG 174 208 208 ARG ARG B . n 
B 1 175 VAL 175 209 209 VAL VAL B . n 
B 1 176 GLU 176 210 210 GLU GLU B . n 
B 1 177 ASP 177 211 211 ASP ASP B . n 
B 1 178 ALA 178 212 212 ALA ALA B . n 
B 1 179 SER 179 213 213 SER SER B . n 
B 1 180 SER 180 214 214 SER SER B . n 
B 1 181 PHE 181 215 215 PHE PHE B . n 
B 1 182 PRO 182 216 216 PRO PRO B . n 
B 1 183 LEU 183 217 217 LEU LEU B . n 
B 1 184 ASP 184 218 218 ASP ASP B . n 
B 1 185 TYR 185 219 219 TYR TYR B . n 
B 1 186 GLY 186 220 220 GLY GLY B . n 
B 1 187 ILE 187 221 221 ILE ILE B . n 
B 1 188 ARG 188 222 222 ARG ARG B . n 
B 1 189 ARG 189 223 223 ARG ARG B . n 
B 1 190 LEU 190 224 224 LEU LEU B . n 
B 1 191 ASP 191 225 225 ASP ASP B . n 
B 1 192 HIS 192 226 226 HIS HIS B . n 
B 1 193 ALA 193 227 227 ALA ALA B . n 
B 1 194 VAL 194 228 228 VAL VAL B . n 
B 1 195 GLY 195 229 229 GLY GLY B . n 
B 1 196 ASN 196 230 230 ASN ASN B . n 
B 1 197 VAL 197 231 231 VAL VAL B . n 
B 1 198 PRO 198 232 232 PRO PRO B . n 
B 1 199 GLU 199 233 233 GLU GLU B . n 
B 1 200 LEU 200 234 234 LEU LEU B . n 
B 1 201 GLY 201 235 235 GLY GLY B . n 
B 1 202 PRO 202 236 236 PRO PRO B . n 
B 1 203 ALA 203 237 237 ALA ALA B . n 
B 1 204 LEU 204 238 238 LEU LEU B . n 
B 1 205 THR 205 239 239 THR THR B . n 
B 1 206 TYR 206 240 240 TYR TYR B . n 
B 1 207 VAL 207 241 241 VAL VAL B . n 
B 1 208 ALA 208 242 242 ALA ALA B . n 
B 1 209 GLY 209 243 243 GLY GLY B . n 
B 1 210 PHE 210 244 244 PHE PHE B . n 
B 1 211 THR 211 245 245 THR THR B . n 
B 1 212 GLY 212 246 246 GLY GLY B . n 
B 1 213 PHE 213 247 247 PHE PHE B . n 
B 1 214 HIS 214 248 248 HIS HIS B . n 
B 1 215 GLN 215 249 249 GLN GLN B . n 
B 1 216 PHE 216 250 250 PHE PHE B . n 
B 1 217 ALA 217 251 251 ALA ALA B . n 
B 1 218 GLU 218 252 ?   ?   ?   B . n 
B 1 219 PHE 219 253 ?   ?   ?   B . n 
B 1 220 THR 220 254 ?   ?   ?   B . n 
B 1 221 ALA 221 255 ?   ?   ?   B . n 
B 1 222 ASP 222 256 ?   ?   ?   B . n 
B 1 223 ASP 223 257 ?   ?   ?   B . n 
B 1 224 VAL 224 258 ?   ?   ?   B . n 
B 1 225 GLY 225 259 ?   ?   ?   B . n 
B 1 226 THR 226 260 ?   ?   ?   B . n 
B 1 227 ALA 227 261 ?   ?   ?   B . n 
B 1 228 GLU 228 262 262 GLU GLU B . n 
B 1 229 SER 229 263 263 SER SER B . n 
B 1 230 GLY 230 264 264 GLY GLY B . n 
B 1 231 LEU 231 265 265 LEU LEU B . n 
B 1 232 ASN 232 266 266 ASN ASN B . n 
B 1 233 SER 233 267 267 SER SER B . n 
B 1 234 ALA 234 268 268 ALA ALA B . n 
B 1 235 VAL 235 269 269 VAL VAL B . n 
B 1 236 LEU 236 270 270 LEU LEU B . n 
B 1 237 ALA 237 271 271 ALA ALA B . n 
B 1 238 SER 238 272 272 SER SER B . n 
B 1 239 ASN 239 273 273 ASN ASN B . n 
B 1 240 ASP 240 274 274 ASP ASP B . n 
B 1 241 GLU 241 275 275 GLU GLU B . n 
B 1 242 MET 242 276 276 MET MET B . n 
B 1 243 VAL 243 277 277 VAL VAL B . n 
B 1 244 LEU 244 278 278 LEU LEU B . n 
B 1 245 LEU 245 279 279 LEU LEU B . n 
B 1 246 PRO 246 280 280 PRO PRO B . n 
B 1 247 ILE 247 281 281 ILE ILE B . n 
B 1 248 ASN 248 282 282 ASN ASN B . n 
B 1 249 GLU 249 283 283 GLU GLU B . n 
B 1 250 PRO 250 284 284 PRO PRO B . n 
B 1 251 VAL 251 285 285 VAL VAL B . n 
B 1 252 HIS 252 286 286 HIS HIS B . n 
B 1 253 GLY 253 287 287 GLY GLY B . n 
B 1 254 THR 254 288 288 THR THR B . n 
B 1 255 LYS 255 289 289 LYS LYS B . n 
B 1 256 ARG 256 290 290 ARG ARG B . n 
B 1 257 LYS 257 291 291 LYS LYS B . n 
B 1 258 SER 258 292 292 SER SER B . n 
B 1 259 GLN 259 293 293 GLN GLN B . n 
B 1 260 ILE 260 294 294 ILE ILE B . n 
B 1 261 GLN 261 295 295 GLN GLN B . n 
B 1 262 THR 262 296 296 THR THR B . n 
B 1 263 TYR 263 297 297 TYR TYR B . n 
B 1 264 LEU 264 298 298 LEU LEU B . n 
B 1 265 GLU 265 299 299 GLU GLU B . n 
B 1 266 HIS 266 300 300 HIS HIS B . n 
B 1 267 ASN 267 301 301 ASN ASN B . n 
B 1 268 GLU 268 302 302 GLU GLU B . n 
B 1 269 GLY 269 303 303 GLY GLY B . n 
B 1 270 ALA 270 304 304 ALA ALA B . n 
B 1 271 GLY 271 305 305 GLY GLY B . n 
B 1 272 LEU 272 306 306 LEU LEU B . n 
B 1 273 GLN 273 307 307 GLN GLN B . n 
B 1 274 HIS 274 308 308 HIS HIS B . n 
B 1 275 LEU 275 309 309 LEU LEU B . n 
B 1 276 ALA 276 310 310 ALA ALA B . n 
B 1 277 LEU 277 311 311 LEU LEU B . n 
B 1 278 MET 278 312 312 MET MET B . n 
B 1 279 SER 279 313 313 SER SER B . n 
B 1 280 GLU 280 314 314 GLU GLU B . n 
B 1 281 ASP 281 315 315 ASP ASP B . n 
B 1 282 ILE 282 316 316 ILE ILE B . n 
B 1 283 PHE 283 317 317 PHE PHE B . n 
B 1 284 ARG 284 318 318 ARG ARG B . n 
B 1 285 THR 285 319 319 THR THR B . n 
B 1 286 LEU 286 320 320 LEU LEU B . n 
B 1 287 ARG 287 321 321 ARG ARG B . n 
B 1 288 GLU 288 322 322 GLU GLU B . n 
B 1 289 MET 289 323 323 MET MET B . n 
B 1 290 ARG 290 324 324 ARG ARG B . n 
B 1 291 LYS 291 325 325 LYS LYS B . n 
B 1 292 ARG 292 326 326 ARG ARG B . n 
B 1 293 SER 293 327 327 SER SER B . n 
B 1 294 SER 294 328 328 SER SER B . n 
B 1 295 ILE 295 329 329 ILE ILE B . n 
B 1 296 GLY 296 330 330 GLY GLY B . n 
B 1 297 GLY 297 331 331 GLY GLY B . n 
B 1 298 PHE 298 332 332 PHE PHE B . n 
B 1 299 ASP 299 333 333 ASP ASP B . n 
B 1 300 PHE 300 334 334 PHE PHE B . n 
B 1 301 MET 301 335 335 MET MET B . n 
B 1 302 PRO 302 336 336 PRO PRO B . n 
B 1 303 SER 303 337 337 SER SER B . n 
B 1 304 PRO 304 338 338 PRO PRO B . n 
B 1 305 PRO 305 339 339 PRO PRO B . n 
B 1 306 PRO 306 340 340 PRO PRO B . n 
B 1 307 THR 307 341 341 THR THR B . n 
B 1 308 TYR 308 342 342 TYR TYR B . n 
B 1 309 TYR 309 343 343 TYR TYR B . n 
B 1 310 GLN 310 344 344 GLN GLN B . n 
B 1 311 ASN 311 345 345 ASN ASN B . n 
B 1 312 LEU 312 346 346 LEU LEU B . n 
B 1 313 LYS 313 347 347 LYS LYS B . n 
B 1 314 LYS 314 348 348 LYS LYS B . n 
B 1 315 ARG 315 349 349 ARG ARG B . n 
B 1 316 VAL 316 350 350 VAL VAL B . n 
B 1 317 GLY 317 351 351 GLY GLY B . n 
B 1 318 ASP 318 352 352 ASP ASP B . n 
B 1 319 VAL 319 353 353 VAL VAL B . n 
B 1 320 LEU 320 354 354 LEU LEU B . n 
B 1 321 SER 321 355 355 SER SER B . n 
B 1 322 ASP 322 356 356 ASP ASP B . n 
B 1 323 ASP 323 357 357 ASP ASP B . n 
B 1 324 GLN 324 358 358 GLN GLN B . n 
B 1 325 ILE 325 359 359 ILE ILE B . n 
B 1 326 LYS 326 360 360 LYS LYS B . n 
B 1 327 GLU 327 361 361 GLU GLU B . n 
B 1 328 CYS 328 362 362 CYS CYS B . n 
B 1 329 GLU 329 363 363 GLU GLU B . n 
B 1 330 GLU 330 364 364 GLU GLU B . n 
B 1 331 LEU 331 365 365 LEU LEU B . n 
B 1 332 GLY 332 366 366 GLY GLY B . n 
B 1 333 ILE 333 367 367 ILE ILE B . n 
B 1 334 LEU 334 368 368 LEU LEU B . n 
B 1 335 VAL 335 369 369 VAL VAL B . n 
B 1 336 ASP 336 370 370 ASP ASP B . n 
B 1 337 ARG 337 371 371 ARG ARG B . n 
B 1 338 ASP 338 372 372 ASP ASP B . n 
B 1 339 ASP 339 373 373 ASP ASP B . n 
B 1 340 GLN 340 374 374 GLN GLN B . n 
B 1 341 GLY 341 375 375 GLY GLY B . n 
B 1 342 THR 342 376 376 THR THR B . n 
B 1 343 LEU 343 377 377 LEU LEU B . n 
B 1 344 LEU 344 378 378 LEU LEU B . n 
B 1 345 GLN 345 379 379 GLN GLN B . n 
B 1 346 ILE 346 380 380 ILE ILE B . n 
B 1 347 PHE 347 381 381 PHE PHE B . n 
B 1 348 THR 348 382 382 THR THR B . n 
B 1 349 LYS 349 383 383 LYS LYS B . n 
B 1 350 PRO 350 384 384 PRO PRO B . n 
B 1 351 LEU 351 385 385 LEU LEU B . n 
B 1 352 GLY 352 386 386 GLY GLY B . n 
B 1 353 ASP 353 387 387 ASP ASP B . n 
B 1 354 ARG 354 388 388 ARG ARG B . n 
B 1 355 PRO 355 389 389 PRO PRO B . n 
B 1 356 THR 356 390 390 THR THR B . n 
B 1 357 ILE 357 391 391 ILE ILE B . n 
B 1 358 PHE 358 392 392 PHE PHE B . n 
B 1 359 ILE 359 393 393 ILE ILE B . n 
B 1 360 GLU 360 394 394 GLU GLU B . n 
B 1 361 ILE 361 395 395 ILE ILE B . n 
B 1 362 ILE 362 396 396 ILE ILE B . n 
B 1 363 GLN 363 397 397 GLN GLN B . n 
B 1 364 ARG 364 398 398 ARG ARG B . n 
B 1 365 VAL 365 399 399 VAL VAL B . n 
B 1 366 GLY 366 400 400 GLY GLY B . n 
B 1 367 CYS 367 401 401 CYS CYS B . n 
B 1 368 MET 368 402 402 MET MET B . n 
B 1 369 MET 369 403 ?   ?   ?   B . n 
B 1 370 LYS 370 404 ?   ?   ?   B . n 
B 1 371 ASP 371 405 ?   ?   ?   B . n 
B 1 372 GLU 372 406 ?   ?   ?   B . n 
B 1 373 GLU 373 407 ?   ?   ?   B . n 
B 1 374 GLY 374 408 ?   ?   ?   B . n 
B 1 375 LYS 375 409 ?   ?   ?   B . n 
B 1 376 ALA 376 410 ?   ?   ?   B . n 
B 1 377 TYR 377 411 411 TYR TYR B . n 
B 1 378 GLN 378 412 412 GLN GLN B . n 
B 1 379 SER 379 413 413 SER SER B . n 
B 1 380 GLY 380 414 414 GLY GLY B . n 
B 1 381 GLY 381 415 415 GLY GLY B . n 
B 1 382 CYS 382 416 416 CYS CYS B . n 
B 1 383 GLY 383 417 417 GLY GLY B . n 
B 1 384 GLY 384 418 418 GLY GLY B . n 
B 1 385 PHE 385 419 419 PHE PHE B . n 
B 1 386 GLY 386 420 420 GLY GLY B . n 
B 1 387 LYS 387 421 421 LYS LYS B . n 
B 1 388 GLY 388 422 422 GLY GLY B . n 
B 1 389 ASN 389 423 423 ASN ASN B . n 
B 1 390 PHE 390 424 424 PHE PHE B . n 
B 1 391 SER 391 425 425 SER SER B . n 
B 1 392 GLU 392 426 426 GLU GLU B . n 
B 1 393 LEU 393 427 427 LEU LEU B . n 
B 1 394 PHE 394 428 428 PHE PHE B . n 
B 1 395 LYS 395 429 429 LYS LYS B . n 
B 1 396 SER 396 430 430 SER SER B . n 
B 1 397 ILE 397 431 431 ILE ILE B . n 
B 1 398 GLU 398 432 432 GLU GLU B . n 
B 1 399 GLU 399 433 433 GLU GLU B . n 
B 1 400 TYR 400 434 434 TYR TYR B . n 
B 1 401 GLU 401 435 435 GLU GLU B . n 
B 1 402 LYS 402 436 436 LYS LYS B . n 
B 1 403 THR 403 437 437 THR THR B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CO    1  501 1   CO    CO  A . 
D 3 A1LWU 1  502 501 A1LWU LIG A . 
E 2 CO    1  501 2   CO    CO  B . 
F 3 A1LWU 1  502 1   A1LWU LIG B . 
G 4 HOH   1  601 63  HOH   HOH A . 
G 4 HOH   2  602 79  HOH   HOH A . 
G 4 HOH   3  603 67  HOH   HOH A . 
G 4 HOH   4  604 38  HOH   HOH A . 
G 4 HOH   5  605 75  HOH   HOH A . 
G 4 HOH   6  606 31  HOH   HOH A . 
G 4 HOH   7  607 20  HOH   HOH A . 
G 4 HOH   8  608 1   HOH   HOH A . 
G 4 HOH   9  609 15  HOH   HOH A . 
G 4 HOH   10 610 53  HOH   HOH A . 
G 4 HOH   11 611 54  HOH   HOH A . 
G 4 HOH   12 612 58  HOH   HOH A . 
G 4 HOH   13 613 74  HOH   HOH A . 
G 4 HOH   14 614 14  HOH   HOH A . 
G 4 HOH   15 615 2   HOH   HOH A . 
G 4 HOH   16 616 7   HOH   HOH A . 
G 4 HOH   17 617 43  HOH   HOH A . 
G 4 HOH   18 618 68  HOH   HOH A . 
G 4 HOH   19 619 5   HOH   HOH A . 
G 4 HOH   20 620 46  HOH   HOH A . 
G 4 HOH   21 621 39  HOH   HOH A . 
G 4 HOH   22 622 19  HOH   HOH A . 
G 4 HOH   23 623 34  HOH   HOH A . 
G 4 HOH   24 624 24  HOH   HOH A . 
G 4 HOH   25 625 55  HOH   HOH A . 
G 4 HOH   26 626 9   HOH   HOH A . 
G 4 HOH   27 627 12  HOH   HOH A . 
G 4 HOH   28 628 78  HOH   HOH A . 
G 4 HOH   29 629 72  HOH   HOH A . 
G 4 HOH   30 630 57  HOH   HOH A . 
G 4 HOH   31 631 32  HOH   HOH A . 
G 4 HOH   32 632 4   HOH   HOH A . 
G 4 HOH   33 633 66  HOH   HOH A . 
G 4 HOH   34 634 8   HOH   HOH A . 
G 4 HOH   35 635 77  HOH   HOH A . 
G 4 HOH   36 636 56  HOH   HOH A . 
G 4 HOH   37 637 76  HOH   HOH A . 
G 4 HOH   38 638 27  HOH   HOH A . 
G 4 HOH   39 639 23  HOH   HOH A . 
G 4 HOH   40 640 6   HOH   HOH A . 
G 4 HOH   41 641 42  HOH   HOH A . 
G 4 HOH   42 642 52  HOH   HOH A . 
G 4 HOH   43 643 61  HOH   HOH A . 
G 4 HOH   44 644 48  HOH   HOH A . 
G 4 HOH   45 645 60  HOH   HOH A . 
G 4 HOH   46 646 59  HOH   HOH A . 
G 4 HOH   47 647 70  HOH   HOH A . 
G 4 HOH   48 648 10  HOH   HOH A . 
G 4 HOH   49 649 13  HOH   HOH A . 
H 4 HOH   1  601 22  HOH   HOH B . 
H 4 HOH   2  602 36  HOH   HOH B . 
H 4 HOH   3  603 28  HOH   HOH B . 
H 4 HOH   4  604 29  HOH   HOH B . 
H 4 HOH   5  605 44  HOH   HOH B . 
H 4 HOH   6  606 16  HOH   HOH B . 
H 4 HOH   7  607 45  HOH   HOH B . 
H 4 HOH   8  608 51  HOH   HOH B . 
H 4 HOH   9  609 17  HOH   HOH B . 
H 4 HOH   10 610 65  HOH   HOH B . 
H 4 HOH   11 611 11  HOH   HOH B . 
H 4 HOH   12 612 69  HOH   HOH B . 
H 4 HOH   13 613 41  HOH   HOH B . 
H 4 HOH   14 614 50  HOH   HOH B . 
H 4 HOH   15 615 35  HOH   HOH B . 
H 4 HOH   16 616 33  HOH   HOH B . 
H 4 HOH   17 617 3   HOH   HOH B . 
H 4 HOH   18 618 25  HOH   HOH B . 
H 4 HOH   19 619 26  HOH   HOH B . 
H 4 HOH   20 620 49  HOH   HOH B . 
H 4 HOH   21 621 21  HOH   HOH B . 
H 4 HOH   22 622 40  HOH   HOH B . 
H 4 HOH   23 623 64  HOH   HOH B . 
H 4 HOH   24 624 71  HOH   HOH B . 
H 4 HOH   25 625 47  HOH   HOH B . 
H 4 HOH   26 626 18  HOH   HOH B . 
H 4 HOH   27 627 62  HOH   HOH B . 
H 4 HOH   28 628 73  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 35  ? CG  ? A LYS 1   CG  
2   1 Y 1 A LYS 35  ? CD  ? A LYS 1   CD  
3   1 Y 1 A LYS 35  ? CE  ? A LYS 1   CE  
4   1 Y 1 A LYS 35  ? NZ  ? A LYS 1   NZ  
5   1 Y 1 A ASN 171 ? CG  ? A ASN 137 CG  
6   1 Y 1 A ASN 171 ? OD1 ? A ASN 137 OD1 
7   1 Y 1 A ASN 171 ? ND2 ? A ASN 137 ND2 
8   1 Y 1 A LYS 193 ? CG  ? A LYS 159 CG  
9   1 Y 1 A LYS 193 ? CD  ? A LYS 159 CD  
10  1 Y 1 A LYS 193 ? CE  ? A LYS 159 CE  
11  1 Y 1 A LYS 193 ? NZ  ? A LYS 159 NZ  
12  1 Y 1 A GLU 210 ? CG  ? A GLU 176 CG  
13  1 Y 1 A GLU 210 ? CD  ? A GLU 176 CD  
14  1 Y 1 A GLU 210 ? OE1 ? A GLU 176 OE1 
15  1 Y 1 A GLU 210 ? OE2 ? A GLU 176 OE2 
16  1 Y 1 A ARG 290 ? CG  ? A ARG 256 CG  
17  1 Y 1 A ARG 290 ? CD  ? A ARG 256 CD  
18  1 Y 1 A ARG 290 ? NE  ? A ARG 256 NE  
19  1 Y 1 A ARG 290 ? CZ  ? A ARG 256 CZ  
20  1 Y 1 A ARG 290 ? NH1 ? A ARG 256 NH1 
21  1 Y 1 A ARG 290 ? NH2 ? A ARG 256 NH2 
22  1 Y 1 A GLN 344 ? CG  ? A GLN 310 CG  
23  1 Y 1 A GLN 344 ? CD  ? A GLN 310 CD  
24  1 Y 1 A GLN 344 ? OE1 ? A GLN 310 OE1 
25  1 Y 1 A GLN 344 ? NE2 ? A GLN 310 NE2 
26  1 Y 1 A LYS 348 ? CG  ? A LYS 314 CG  
27  1 Y 1 A LYS 348 ? CD  ? A LYS 314 CD  
28  1 Y 1 A LYS 348 ? CE  ? A LYS 314 CE  
29  1 Y 1 A LYS 348 ? NZ  ? A LYS 314 NZ  
30  1 Y 1 A TYR 411 ? CG  ? A TYR 377 CG  
31  1 Y 1 A TYR 411 ? CD1 ? A TYR 377 CD1 
32  1 Y 1 A TYR 411 ? CD2 ? A TYR 377 CD2 
33  1 Y 1 A TYR 411 ? CE1 ? A TYR 377 CE1 
34  1 Y 1 A TYR 411 ? CE2 ? A TYR 377 CE2 
35  1 Y 1 A TYR 411 ? CZ  ? A TYR 377 CZ  
36  1 Y 1 A TYR 411 ? OH  ? A TYR 377 OH  
37  1 Y 1 A LYS 429 ? CG  ? A LYS 395 CG  
38  1 Y 1 A LYS 429 ? CD  ? A LYS 395 CD  
39  1 Y 1 A LYS 429 ? CE  ? A LYS 395 CE  
40  1 Y 1 A LYS 429 ? NZ  ? A LYS 395 NZ  
41  1 Y 1 A GLU 432 ? CG  ? A GLU 398 CG  
42  1 Y 1 A GLU 432 ? CD  ? A GLU 398 CD  
43  1 Y 1 A GLU 432 ? OE1 ? A GLU 398 OE1 
44  1 Y 1 A GLU 432 ? OE2 ? A GLU 398 OE2 
45  1 Y 1 A GLU 433 ? CG  ? A GLU 399 CG  
46  1 Y 1 A GLU 433 ? CD  ? A GLU 399 CD  
47  1 Y 1 A GLU 433 ? OE1 ? A GLU 399 OE1 
48  1 Y 1 A GLU 433 ? OE2 ? A GLU 399 OE2 
49  1 Y 1 A GLU 435 ? CG  ? A GLU 401 CG  
50  1 Y 1 A GLU 435 ? CD  ? A GLU 401 CD  
51  1 Y 1 A GLU 435 ? OE1 ? A GLU 401 OE1 
52  1 Y 1 A GLU 435 ? OE2 ? A GLU 401 OE2 
53  1 Y 1 A LYS 436 ? CG  ? A LYS 402 CG  
54  1 Y 1 A LYS 436 ? CD  ? A LYS 402 CD  
55  1 Y 1 A LYS 436 ? CE  ? A LYS 402 CE  
56  1 Y 1 A LYS 436 ? NZ  ? A LYS 402 NZ  
57  1 Y 1 B LYS 43  ? CG  ? B LYS 9   CG  
58  1 Y 1 B LYS 43  ? CD  ? B LYS 9   CD  
59  1 Y 1 B LYS 43  ? CE  ? B LYS 9   CE  
60  1 Y 1 B LYS 43  ? NZ  ? B LYS 9   NZ  
61  1 Y 1 B ARG 71  ? CG  ? B ARG 37  CG  
62  1 Y 1 B ARG 71  ? CD  ? B ARG 37  CD  
63  1 Y 1 B ARG 71  ? NE  ? B ARG 37  NE  
64  1 Y 1 B ARG 71  ? CZ  ? B ARG 37  CZ  
65  1 Y 1 B ARG 71  ? NH1 ? B ARG 37  NH1 
66  1 Y 1 B ARG 71  ? NH2 ? B ARG 37  NH2 
67  1 Y 1 B GLU 111 ? CG  ? B GLU 77  CG  
68  1 Y 1 B GLU 111 ? CD  ? B GLU 77  CD  
69  1 Y 1 B GLU 111 ? OE1 ? B GLU 77  OE1 
70  1 Y 1 B GLU 111 ? OE2 ? B GLU 77  OE2 
71  1 Y 1 B GLU 172 ? CG  ? B GLU 138 CG  
72  1 Y 1 B GLU 172 ? CD  ? B GLU 138 CD  
73  1 Y 1 B GLU 172 ? OE1 ? B GLU 138 OE1 
74  1 Y 1 B GLU 172 ? OE2 ? B GLU 138 OE2 
75  1 Y 1 B LYS 193 ? CG  ? B LYS 159 CG  
76  1 Y 1 B LYS 193 ? CD  ? B LYS 159 CD  
77  1 Y 1 B LYS 193 ? CE  ? B LYS 159 CE  
78  1 Y 1 B LYS 193 ? NZ  ? B LYS 159 NZ  
79  1 Y 1 B GLU 201 ? CG  ? B GLU 167 CG  
80  1 Y 1 B GLU 201 ? CD  ? B GLU 167 CD  
81  1 Y 1 B GLU 201 ? OE1 ? B GLU 167 OE1 
82  1 Y 1 B GLU 201 ? OE2 ? B GLU 167 OE2 
83  1 Y 1 B ARG 208 ? CG  ? B ARG 174 CG  
84  1 Y 1 B ARG 208 ? CD  ? B ARG 174 CD  
85  1 Y 1 B ARG 208 ? NE  ? B ARG 174 NE  
86  1 Y 1 B ARG 208 ? CZ  ? B ARG 174 CZ  
87  1 Y 1 B ARG 208 ? NH1 ? B ARG 174 NH1 
88  1 Y 1 B ARG 208 ? NH2 ? B ARG 174 NH2 
89  1 Y 1 B GLU 210 ? CG  ? B GLU 176 CG  
90  1 Y 1 B GLU 210 ? CD  ? B GLU 176 CD  
91  1 Y 1 B GLU 210 ? OE1 ? B GLU 176 OE1 
92  1 Y 1 B GLU 210 ? OE2 ? B GLU 176 OE2 
93  1 Y 1 B GLU 262 ? CG  ? B GLU 228 CG  
94  1 Y 1 B GLU 262 ? CD  ? B GLU 228 CD  
95  1 Y 1 B GLU 262 ? OE1 ? B GLU 228 OE1 
96  1 Y 1 B GLU 262 ? OE2 ? B GLU 228 OE2 
97  1 Y 1 B LYS 289 ? CG  ? B LYS 255 CG  
98  1 Y 1 B LYS 289 ? CD  ? B LYS 255 CD  
99  1 Y 1 B LYS 289 ? CE  ? B LYS 255 CE  
100 1 Y 1 B LYS 289 ? NZ  ? B LYS 255 NZ  
101 1 Y 1 B ARG 290 ? CG  ? B ARG 256 CG  
102 1 Y 1 B ARG 290 ? CD  ? B ARG 256 CD  
103 1 Y 1 B ARG 290 ? NE  ? B ARG 256 NE  
104 1 Y 1 B ARG 290 ? CZ  ? B ARG 256 CZ  
105 1 Y 1 B ARG 290 ? NH1 ? B ARG 256 NH1 
106 1 Y 1 B ARG 290 ? NH2 ? B ARG 256 NH2 
107 1 Y 1 B LYS 291 ? CG  ? B LYS 257 CG  
108 1 Y 1 B LYS 291 ? CD  ? B LYS 257 CD  
109 1 Y 1 B LYS 291 ? CE  ? B LYS 257 CE  
110 1 Y 1 B LYS 291 ? NZ  ? B LYS 257 NZ  
111 1 Y 1 B GLN 344 ? CG  ? B GLN 310 CG  
112 1 Y 1 B GLN 344 ? CD  ? B GLN 310 CD  
113 1 Y 1 B GLN 344 ? OE1 ? B GLN 310 OE1 
114 1 Y 1 B GLN 344 ? NE2 ? B GLN 310 NE2 
115 1 Y 1 B LYS 347 ? CG  ? B LYS 313 CG  
116 1 Y 1 B LYS 347 ? CD  ? B LYS 313 CD  
117 1 Y 1 B LYS 347 ? CE  ? B LYS 313 CE  
118 1 Y 1 B LYS 347 ? NZ  ? B LYS 313 NZ  
119 1 Y 1 B LYS 348 ? CG  ? B LYS 314 CG  
120 1 Y 1 B LYS 348 ? CD  ? B LYS 314 CD  
121 1 Y 1 B LYS 348 ? CE  ? B LYS 314 CE  
122 1 Y 1 B LYS 348 ? NZ  ? B LYS 314 NZ  
123 1 Y 1 B ASP 357 ? CG  ? B ASP 323 CG  
124 1 Y 1 B ASP 357 ? OD1 ? B ASP 323 OD1 
125 1 Y 1 B ASP 357 ? OD2 ? B ASP 323 OD2 
126 1 Y 1 B LYS 360 ? CG  ? B LYS 326 CG  
127 1 Y 1 B LYS 360 ? CD  ? B LYS 326 CD  
128 1 Y 1 B LYS 360 ? CE  ? B LYS 326 CE  
129 1 Y 1 B LYS 360 ? NZ  ? B LYS 326 NZ  
130 1 Y 1 B PHE 428 ? CG  ? B PHE 394 CG  
131 1 Y 1 B PHE 428 ? CD1 ? B PHE 394 CD1 
132 1 Y 1 B PHE 428 ? CD2 ? B PHE 394 CD2 
133 1 Y 1 B PHE 428 ? CE1 ? B PHE 394 CE1 
134 1 Y 1 B PHE 428 ? CE2 ? B PHE 394 CE2 
135 1 Y 1 B PHE 428 ? CZ  ? B PHE 394 CZ  
136 1 Y 1 B LYS 429 ? CG  ? B LYS 395 CG  
137 1 Y 1 B LYS 429 ? CD  ? B LYS 395 CD  
138 1 Y 1 B LYS 429 ? CE  ? B LYS 395 CE  
139 1 Y 1 B LYS 429 ? NZ  ? B LYS 395 NZ  
140 1 Y 1 B ILE 431 ? CG1 ? B ILE 397 CG1 
141 1 Y 1 B ILE 431 ? CG2 ? B ILE 397 CG2 
142 1 Y 1 B ILE 431 ? CD1 ? B ILE 397 CD1 
143 1 Y 1 B GLU 432 ? CG  ? B GLU 398 CG  
144 1 Y 1 B GLU 432 ? CD  ? B GLU 398 CD  
145 1 Y 1 B GLU 432 ? OE1 ? B GLU 398 OE1 
146 1 Y 1 B GLU 432 ? OE2 ? B GLU 398 OE2 
147 1 Y 1 B GLU 433 ? CG  ? B GLU 399 CG  
148 1 Y 1 B GLU 433 ? CD  ? B GLU 399 CD  
149 1 Y 1 B GLU 433 ? OE1 ? B GLU 399 OE1 
150 1 Y 1 B GLU 433 ? OE2 ? B GLU 399 OE2 
151 1 Y 1 B GLU 435 ? CG  ? B GLU 401 CG  
152 1 Y 1 B GLU 435 ? CD  ? B GLU 401 CD  
153 1 Y 1 B GLU 435 ? OE1 ? B GLU 401 OE1 
154 1 Y 1 B GLU 435 ? OE2 ? B GLU 401 OE2 
155 1 Y 1 B LYS 436 ? CG  ? B LYS 402 CG  
156 1 Y 1 B LYS 436 ? CD  ? B LYS 402 CD  
157 1 Y 1 B LYS 436 ? CE  ? B LYS 402 CE  
158 1 Y 1 B LYS 436 ? NZ  ? B LYS 402 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.10.1_2155: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XQV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     59.453 
_cell.length_a_esd                 ? 
_cell.length_b                     83.849 
_cell.length_b_esd                 ? 
_cell.length_c                     75.052 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8XQV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8XQV 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.02 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.13 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.1M Tris/Bicine pH 8.5, 15% (v/v) MPD, 15% (w/v) PEG 1000, 15% (w/v) PEG 3350, 0.03M NaBr, 0.03M NaF, 0.03M NaI' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XQV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.698 
_reflns.d_resolution_low                               34.179 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     20064 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96.07 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.17 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.73 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.981 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.70 
_reflns_shell.d_res_low                                     2.86 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6038 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.781 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8XQV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.698 
_refine.ls_d_res_low                             34.179 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     20064 
_refine.ls_number_reflns_R_free                  1003 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.07 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1899 
_refine.ls_R_factor_R_free                       0.2603 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1862 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 28.80 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.36 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.698 
_refine_hist.d_res_low                        34.179 
_refine_hist.number_atoms_solvent             77 
_refine_hist.number_atoms_total               5858 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5711 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         70 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 5922 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.227  ? 8036 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.422 ? 3473 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.056  ? 877  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 1046 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.6981 2.8402 . . 139 2638 97.00  . . . . 0.2286 . . . . . . . . . . . 0.3438 
'X-RAY DIFFRACTION' 2.8402 3.0181 . . 144 2729 100.00 . . . . 0.2156 . . . . . . . . . . . 0.3348 
'X-RAY DIFFRACTION' 3.0181 3.2510 . . 142 2708 99.00  . . . . 0.2005 . . . . . . . . . . . 0.2903 
'X-RAY DIFFRACTION' 3.2510 3.5778 . . 144 2722 99.00  . . . . 0.1906 . . . . . . . . . . . 0.3148 
'X-RAY DIFFRACTION' 3.5778 4.0948 . . 144 2739 100.00 . . . . 0.1736 . . . . . . . . . . . 0.2223 
'X-RAY DIFFRACTION' 4.0948 5.1561 . . 144 2741 99.00  . . . . 0.1540 . . . . . . . . . . . 0.2342 
'X-RAY DIFFRACTION' 5.1561 8      . . 146 2784 99.00  . . . . 0.1935 . . . . . . . . . . . 0.2153 
# 
_struct.entry_id                     8XQV 
_struct.title                        'Crystal structure of AtHPPD-YH23025 complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8XQV 
_struct_keywords.text            'Complex, Inhibitor, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HPPD_ARATH 
_struct_ref.pdbx_db_accession          P93836 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEIKP
TTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSYKA
EDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLASND
EMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGDVL
SDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELFKSIEEY
EKT
;
_struct_ref.pdbx_align_begin           35 
# 
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 8XQV A 1 ? 403 ? P93836 35 ? 437 ? 35 437 
2 1 8XQV B 1 ? 403 ? P93836 35 ? 437 ? 35 437 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3240  ? 
1 MORE         -11   ? 
1 'SSA (A^2)'  28350 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? GLY A 35  ? ASP A 56  GLY A 69  1 ? 14 
HELX_P HELX_P2  AA2 ASP A 43  ? GLY A 47  ? ASP A 77  GLY A 81  5 ? 5  
HELX_P HELX_P3  AA3 SER A 70  ? ALA A 75  ? SER A 104 ALA A 109 5 ? 6  
HELX_P HELX_P4  AA4 ILE A 78  ? THR A 82  ? ILE A 112 THR A 116 5 ? 5  
HELX_P HELX_P5  AA5 ASP A 90  ? GLY A 102 ? ASP A 124 GLY A 136 1 ? 13 
HELX_P HELX_P6  AA6 ASP A 114 ? ALA A 124 ? ASP A 148 ALA A 158 1 ? 11 
HELX_P HELX_P7  AA7 GLU A 176 ? SER A 180 ? GLU A 210 SER A 214 5 ? 5  
HELX_P HELX_P8  AA8 GLU A 199 ? GLY A 212 ? GLU A 233 GLY A 246 1 ? 14 
HELX_P HELX_P9  AA9 SER A 258 ? GLU A 268 ? SER A 292 GLU A 302 1 ? 11 
HELX_P HELX_P10 AB1 ASP A 281 ? SER A 293 ? ASP A 315 SER A 327 1 ? 13 
HELX_P HELX_P11 AB2 SER A 294 ? GLY A 296 ? SER A 328 GLY A 330 5 ? 3  
HELX_P HELX_P12 AB3 PRO A 305 ? ASN A 311 ? PRO A 339 ASN A 345 1 ? 7  
HELX_P HELX_P13 AB4 ASN A 311 ? GLY A 317 ? ASN A 345 GLY A 351 1 ? 7  
HELX_P HELX_P14 AB5 SER A 321 ? GLY A 332 ? SER A 355 GLY A 366 1 ? 12 
HELX_P HELX_P15 AB6 GLY A 388 ? LYS A 402 ? GLY A 422 LYS A 436 1 ? 15 
HELX_P HELX_P16 AB7 ASP B 22  ? GLY B 35  ? ASP B 56  GLY B 69  1 ? 14 
HELX_P HELX_P17 AB8 ASP B 43  ? GLY B 47  ? ASP B 77  GLY B 81  5 ? 5  
HELX_P HELX_P18 AB9 SER B 70  ? ALA B 75  ? SER B 104 ALA B 109 5 ? 6  
HELX_P HELX_P19 AC1 ASP B 90  ? GLY B 102 ? ASP B 124 GLY B 136 1 ? 13 
HELX_P HELX_P20 AC2 ASP B 114 ? ASN B 125 ? ASP B 148 ASN B 159 1 ? 12 
HELX_P HELX_P21 AC3 GLU B 199 ? GLY B 212 ? GLU B 233 GLY B 246 1 ? 14 
HELX_P HELX_P22 AC4 SER B 258 ? GLU B 268 ? SER B 292 GLU B 302 1 ? 11 
HELX_P HELX_P23 AC5 ASP B 281 ? SER B 293 ? ASP B 315 SER B 327 1 ? 13 
HELX_P HELX_P24 AC6 SER B 294 ? GLY B 296 ? SER B 328 GLY B 330 5 ? 3  
HELX_P HELX_P25 AC7 PRO B 305 ? GLY B 317 ? PRO B 339 GLY B 351 1 ? 13 
HELX_P HELX_P26 AC8 SER B 321 ? GLY B 332 ? SER B 355 GLY B 366 1 ? 12 
HELX_P HELX_P27 AC9 GLY B 388 ? LYS B 402 ? GLY B 422 LYS B 436 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 367 SG  ? ? ? 1_555 A CYS   382 SG  ? ? A CYS 401 A CYS   416 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf2  disulf ? ? B CYS 367 SG  ? ? ? 1_555 B CYS   382 SG  ? ? B CYS 401 B CYS   416 1_555 ? ? ? ? ? ? ? 1.957 ? ? 
metalc1  metalc ? ? A HIS 192 NE2 ? ? ? 1_555 C CO    .   CO  ? ? A HIS 226 A CO    501 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc2  metalc ? ? A HIS 274 NE2 ? ? ? 1_555 C CO    .   CO  ? ? A HIS 308 A CO    501 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc3  metalc ? ? A GLU 360 OE1 ? ? ? 1_555 C CO    .   CO  ? ? A GLU 394 A CO    501 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc4  metalc ? ? C CO  .   CO  ? ? ? 1_555 D A1LWU .   O21 ? ? A CO  501 A A1LWU 502 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc5  metalc ? ? C CO  .   CO  ? ? ? 1_555 D A1LWU .   O15 ? ? A CO  501 A A1LWU 502 1_555 ? ? ? ? ? ? ? 1.823 ? ? 
metalc6  metalc ? ? B HIS 192 NE2 ? ? ? 1_555 E CO    .   CO  ? ? B HIS 226 B CO    501 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc7  metalc ? ? B HIS 274 NE2 ? ? ? 1_555 E CO    .   CO  ? ? B HIS 308 B CO    501 1_555 ? ? ? ? ? ? ? 2.442 ? ? 
metalc8  metalc ? ? B GLU 360 OE1 ? ? ? 1_555 E CO    .   CO  ? ? B GLU 394 B CO    501 1_555 ? ? ? ? ? ? ? 2.247 ? ? 
metalc9  metalc ? ? E CO  .   CO  ? ? ? 1_555 F A1LWU .   O15 ? ? B CO  501 B A1LWU 502 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
metalc10 metalc ? ? E CO  .   CO  ? ? ? 1_555 F A1LWU .   O21 ? ? B CO  501 B A1LWU 502 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS   192 ? A HIS   226 ? 1_555 CO ? C CO . ? A CO 501 ? 1_555 NE2 ? A HIS   274 ? A HIS   308 ? 1_555 109.8 ? 
2  NE2 ? A HIS   192 ? A HIS   226 ? 1_555 CO ? C CO . ? A CO 501 ? 1_555 OE1 ? A GLU   360 ? A GLU   394 ? 1_555 95.6  ? 
3  NE2 ? A HIS   274 ? A HIS   308 ? 1_555 CO ? C CO . ? A CO 501 ? 1_555 OE1 ? A GLU   360 ? A GLU   394 ? 1_555 78.8  ? 
4  NE2 ? A HIS   192 ? A HIS   226 ? 1_555 CO ? C CO . ? A CO 501 ? 1_555 O21 ? D A1LWU .   ? A A1LWU 502 ? 1_555 90.1  ? 
5  NE2 ? A HIS   274 ? A HIS   308 ? 1_555 CO ? C CO . ? A CO 501 ? 1_555 O21 ? D A1LWU .   ? A A1LWU 502 ? 1_555 104.4 ? 
6  OE1 ? A GLU   360 ? A GLU   394 ? 1_555 CO ? C CO . ? A CO 501 ? 1_555 O21 ? D A1LWU .   ? A A1LWU 502 ? 1_555 172.1 ? 
7  NE2 ? A HIS   192 ? A HIS   226 ? 1_555 CO ? C CO . ? A CO 501 ? 1_555 O15 ? D A1LWU .   ? A A1LWU 502 ? 1_555 156.5 ? 
8  NE2 ? A HIS   274 ? A HIS   308 ? 1_555 CO ? C CO . ? A CO 501 ? 1_555 O15 ? D A1LWU .   ? A A1LWU 502 ? 1_555 85.3  ? 
9  OE1 ? A GLU   360 ? A GLU   394 ? 1_555 CO ? C CO . ? A CO 501 ? 1_555 O15 ? D A1LWU .   ? A A1LWU 502 ? 1_555 105.2 ? 
10 O21 ? D A1LWU .   ? A A1LWU 502 ? 1_555 CO ? C CO . ? A CO 501 ? 1_555 O15 ? D A1LWU .   ? A A1LWU 502 ? 1_555 68.2  ? 
11 NE2 ? B HIS   192 ? B HIS   226 ? 1_555 CO ? E CO . ? B CO 501 ? 1_555 NE2 ? B HIS   274 ? B HIS   308 ? 1_555 102.6 ? 
12 NE2 ? B HIS   192 ? B HIS   226 ? 1_555 CO ? E CO . ? B CO 501 ? 1_555 OE1 ? B GLU   360 ? B GLU   394 ? 1_555 92.5  ? 
13 NE2 ? B HIS   274 ? B HIS   308 ? 1_555 CO ? E CO . ? B CO 501 ? 1_555 OE1 ? B GLU   360 ? B GLU   394 ? 1_555 81.5  ? 
14 NE2 ? B HIS   192 ? B HIS   226 ? 1_555 CO ? E CO . ? B CO 501 ? 1_555 O15 ? F A1LWU .   ? B A1LWU 502 ? 1_555 149.5 ? 
15 NE2 ? B HIS   274 ? B HIS   308 ? 1_555 CO ? E CO . ? B CO 501 ? 1_555 O15 ? F A1LWU .   ? B A1LWU 502 ? 1_555 96.6  ? 
16 OE1 ? B GLU   360 ? B GLU   394 ? 1_555 CO ? E CO . ? B CO 501 ? 1_555 O15 ? F A1LWU .   ? B A1LWU 502 ? 1_555 113.8 ? 
17 NE2 ? B HIS   192 ? B HIS   226 ? 1_555 CO ? E CO . ? B CO 501 ? 1_555 O21 ? F A1LWU .   ? B A1LWU 502 ? 1_555 92.1  ? 
18 NE2 ? B HIS   274 ? B HIS   308 ? 1_555 CO ? E CO . ? B CO 501 ? 1_555 O21 ? F A1LWU .   ? B A1LWU 502 ? 1_555 94.9  ? 
19 OE1 ? B GLU   360 ? B GLU   394 ? 1_555 CO ? E CO . ? B CO 501 ? 1_555 O21 ? F A1LWU .   ? B A1LWU 502 ? 1_555 174.6 ? 
20 O15 ? F A1LWU .   ? B A1LWU 502 ? 1_555 CO ? E CO . ? B CO 501 ? 1_555 O21 ? F A1LWU .   ? B A1LWU 502 ? 1_555 62.5  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 367 ? CYS A 382 ? CYS A 401 ? 1_555 CYS A 416 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 367 ? CYS B 382 ? CYS B 401 ? 1_555 CYS B 416 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 8 ? 
AA3 ? 9 ? 
AA4 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA3 5 6 ? parallel      
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA3 8 9 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? parallel      
AA4 4 5 ? anti-parallel 
AA4 5 6 ? parallel      
AA4 6 7 ? anti-parallel 
AA4 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PRO A 129 ? LEU A 136 ? PRO A 163 LEU A 170 
AA1 2 VAL A 140 ? TYR A 148 ? VAL A 174 TYR A 182 
AA1 3 VAL A 151 ? TYR A 158 ? VAL A 185 TYR A 192 
AA1 4 GLY A 104 ? VAL A 112 ? GLY A 138 VAL A 146 
AA1 5 VAL A 10  ? TRP A 19  ? VAL A 44  TRP A 53  
AA1 6 LEU A 61  ? PRO A 68  ? LEU A 95  PRO A 102 
AA1 7 HIS A 51  ? SER A 58  ? HIS A 85  SER A 92  
AA1 8 ARG A 37  ? SER A 42  ? ARG A 71  SER A 76  
AA1 9 GLU A 173 ? ARG A 174 ? GLU A 207 ARG A 208 
AA2 1 HIS A 214 ? GLN A 215 ? HIS A 248 GLN A 249 
AA2 2 LEU A 231 ? ALA A 237 ? LEU A 265 ALA A 271 
AA2 3 LEU A 244 ? PRO A 250 ? LEU A 278 PRO A 284 
AA2 4 ILE A 187 ? ASN A 196 ? ILE A 221 ASN A 230 
AA2 5 GLY A 271 ? SER A 279 ? GLY A 305 SER A 313 
AA2 6 PHE A 358 ? GLY A 366 ? PHE A 392 GLY A 400 
AA2 7 GLY A 341 ? PHE A 347 ? GLY A 375 PHE A 381 
AA2 8 LEU A 334 ? ARG A 337 ? LEU A 368 ARG A 371 
AA3 1 PRO B 129 ? LEU B 136 ? PRO B 163 LEU B 170 
AA3 2 VAL B 140 ? TYR B 148 ? VAL B 174 TYR B 182 
AA3 3 VAL B 151 ? TYR B 158 ? VAL B 185 TYR B 192 
AA3 4 GLY B 104 ? VAL B 112 ? GLY B 138 VAL B 146 
AA3 5 VAL B 10  ? TRP B 19  ? VAL B 44  TRP B 53  
AA3 6 LEU B 61  ? PRO B 68  ? LEU B 95  PRO B 102 
AA3 7 HIS B 51  ? SER B 58  ? HIS B 85  SER B 92  
AA3 8 ARG B 37  ? SER B 42  ? ARG B 71  SER B 76  
AA3 9 GLU B 173 ? ARG B 174 ? GLU B 207 ARG B 208 
AA4 1 HIS B 214 ? GLN B 215 ? HIS B 248 GLN B 249 
AA4 2 LEU B 231 ? ALA B 237 ? LEU B 265 ALA B 271 
AA4 3 LEU B 244 ? PRO B 250 ? LEU B 278 PRO B 284 
AA4 4 ILE B 187 ? ASN B 196 ? ILE B 221 ASN B 230 
AA4 5 GLY B 271 ? SER B 279 ? GLY B 305 SER B 313 
AA4 6 PHE B 358 ? VAL B 365 ? PHE B 392 VAL B 399 
AA4 7 THR B 342 ? PRO B 350 ? THR B 376 PRO B 384 
AA4 8 LEU B 334 ? ARG B 337 ? LEU B 368 ARG B 371 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N SER A 131 ? N SER A 165 O GLU A 144 ? O GLU A 178 
AA1 2 3 N ALA A 143 ? N ALA A 177 O TYR A 155 ? O TYR A 189 
AA1 3 4 O VAL A 156 ? O VAL A 190 N VAL A 112 ? N VAL A 146 
AA1 4 5 O ALA A 109 ? O ALA A 143 N HIS A 14  ? N HIS A 48  
AA1 5 6 N ILE A 16  ? N ILE A 50  O LEU A 64  ? O LEU A 98  
AA1 6 7 O PHE A 63  ? O PHE A 97  N LEU A 56  ? N LEU A 90  
AA1 7 8 O THR A 57  ? O THR A 91  N ARG A 37  ? N ARG A 71  
AA1 8 9 N LYS A 41  ? N LYS A 75  O GLU A 173 ? O GLU A 207 
AA2 1 2 N HIS A 214 ? N HIS A 248 O ALA A 237 ? O ALA A 271 
AA2 2 3 N LEU A 236 ? N LEU A 270 O LEU A 245 ? O LEU A 279 
AA2 3 4 O ASN A 248 ? O ASN A 282 N GLY A 195 ? N GLY A 229 
AA2 4 5 N ARG A 188 ? N ARG A 222 O MET A 278 ? O MET A 312 
AA2 5 6 N LEU A 277 ? N LEU A 311 O GLU A 360 ? O GLU A 394 
AA2 6 7 O VAL A 365 ? O VAL A 399 N THR A 342 ? N THR A 376 
AA2 7 8 O LEU A 343 ? O LEU A 377 N ASP A 336 ? N ASP A 370 
AA3 1 2 N LEU B 136 ? N LEU B 170 O VAL B 140 ? O VAL B 174 
AA3 2 3 N TYR B 148 ? N TYR B 182 O VAL B 151 ? O VAL B 185 
AA3 3 4 O ARG B 154 ? O ARG B 188 N ILE B 110 ? N ILE B 144 
AA3 4 5 O ALA B 109 ? O ALA B 143 N HIS B 14  ? N HIS B 48  
AA3 5 6 N PHE B 18  ? N PHE B 52  O LEU B 64  ? O LEU B 98  
AA3 6 7 O PHE B 63  ? O PHE B 97  N LEU B 56  ? N LEU B 90  
AA3 7 8 O LEU B 55  ? O LEU B 89  N ALA B 40  ? N ALA B 74  
AA3 8 9 N LYS B 41  ? N LYS B 75  O GLU B 173 ? O GLU B 207 
AA4 1 2 N HIS B 214 ? N HIS B 248 O ALA B 237 ? O ALA B 271 
AA4 2 3 N LEU B 236 ? N LEU B 270 O LEU B 245 ? O LEU B 279 
AA4 3 4 O ASN B 248 ? O ASN B 282 N GLY B 195 ? N GLY B 229 
AA4 4 5 N ARG B 189 ? N ARG B 223 O MET B 278 ? O MET B 312 
AA4 5 6 N SER B 279 ? N SER B 313 O ILE B 362 ? O ILE B 396 
AA4 6 7 O ILE B 359 ? O ILE B 393 N THR B 348 ? N THR B 382 
AA4 7 8 O LEU B 343 ? O LEU B 377 N ASP B 336 ? N ASP B 370 
# 
_pdbx_entry_details.entry_id                   8XQV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 LYS A 41  ? ? -63.91  0.63    
2  1 LYS A 45  ? ? -85.18  -92.35  
3  1 ASP A 77  ? ? -166.06 -163.98 
4  1 ASP A 124 ? ? -171.66 111.01  
5  1 ASN A 171 ? ? 51.17   -121.81 
6  1 GLU A 172 ? ? -141.64 30.67   
7  1 LEU A 181 ? ? -107.74 -71.28  
8  1 ASP A 218 ? ? -172.12 106.51  
9  1 GLU A 302 ? ? 73.02   45.26   
10 1 ASP A 315 ? ? -163.71 87.27   
11 1 THR A 390 ? ? -127.41 -95.52  
12 1 ARG B 46  ? ? 69.17   155.47  
13 1 VAL B 84  ? ? -104.83 -62.85  
14 1 ILE B 112 ? ? -109.45 -167.20 
15 1 ASP B 124 ? ? -165.69 119.85  
16 1 ALA B 173 ? ? -135.03 -56.43  
17 1 LEU B 181 ? ? -107.04 -71.80  
18 1 LYS B 193 ? ? -83.27  -80.07  
19 1 PHE B 202 ? ? -86.37  -76.59  
20 1 SER B 213 ? ? -140.33 -8.00   
21 1 PRO B 216 ? ? -53.30  90.04   
22 1 ASP B 218 ? ? -165.60 116.78  
23 1 ALA B 304 ? ? -38.83  143.34  
24 1 ASP B 315 ? ? -164.94 90.39   
25 1 PRO B 389 ? ? -68.28  69.23   
26 1 THR B 390 ? ? -125.48 -79.96  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 195 ? A GLU 161 
2  1 Y 1 A ASP 196 ? A ASP 162 
3  1 Y 1 A THR 197 ? A THR 163 
4  1 Y 1 A GLU 198 ? A GLU 164 
5  1 Y 1 A LYS 199 ? A LYS 165 
6  1 Y 1 A SER 200 ? A SER 166 
7  1 Y 1 A GLU 201 ? A GLU 167 
8  1 Y 1 A GLU 252 ? A GLU 218 
9  1 Y 1 A PHE 253 ? A PHE 219 
10 1 Y 1 A THR 254 ? A THR 220 
11 1 Y 1 A ALA 255 ? A ALA 221 
12 1 Y 1 A ASP 256 ? A ASP 222 
13 1 Y 1 A ASP 257 ? A ASP 223 
14 1 Y 1 A VAL 258 ? A VAL 224 
15 1 Y 1 A GLY 259 ? A GLY 225 
16 1 Y 1 A THR 260 ? A THR 226 
17 1 Y 1 A ALA 261 ? A ALA 227 
18 1 Y 1 A MET 403 ? A MET 369 
19 1 Y 1 A LYS 404 ? A LYS 370 
20 1 Y 1 A ASP 405 ? A ASP 371 
21 1 Y 1 A GLU 406 ? A GLU 372 
22 1 Y 1 A GLU 407 ? A GLU 373 
23 1 Y 1 A GLY 408 ? A GLY 374 
24 1 Y 1 A LYS 409 ? A LYS 375 
25 1 Y 1 A ALA 410 ? A ALA 376 
26 1 Y 1 A THR 437 ? A THR 403 
27 1 Y 1 B LYS 35  ? B LYS 1   
28 1 Y 1 B GLU 195 ? B GLU 161 
29 1 Y 1 B ASP 196 ? B ASP 162 
30 1 Y 1 B THR 197 ? B THR 163 
31 1 Y 1 B GLU 198 ? B GLU 164 
32 1 Y 1 B LYS 199 ? B LYS 165 
33 1 Y 1 B SER 200 ? B SER 166 
34 1 Y 1 B GLU 252 ? B GLU 218 
35 1 Y 1 B PHE 253 ? B PHE 219 
36 1 Y 1 B THR 254 ? B THR 220 
37 1 Y 1 B ALA 255 ? B ALA 221 
38 1 Y 1 B ASP 256 ? B ASP 222 
39 1 Y 1 B ASP 257 ? B ASP 223 
40 1 Y 1 B VAL 258 ? B VAL 224 
41 1 Y 1 B GLY 259 ? B GLY 225 
42 1 Y 1 B THR 260 ? B THR 226 
43 1 Y 1 B ALA 261 ? B ALA 227 
44 1 Y 1 B MET 403 ? B MET 369 
45 1 Y 1 B LYS 404 ? B LYS 370 
46 1 Y 1 B ASP 405 ? B ASP 371 
47 1 Y 1 B GLU 406 ? B GLU 372 
48 1 Y 1 B GLU 407 ? B GLU 373 
49 1 Y 1 B GLY 408 ? B GLY 374 
50 1 Y 1 B LYS 409 ? B LYS 375 
51 1 Y 1 B ALA 410 ? B ALA 376 
# 
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 
A1LWU C13  C  N N 1   
A1LWU C17  C  N N 2   
A1LWU C20  C  N N 3   
A1LWU C24  C  N N 4   
A1LWU C26  C  N N 5   
A1LWU C28  C  Y N 6   
A1LWU C01  C  Y N 7   
A1LWU C02  C  Y N 8   
A1LWU C03  C  Y N 9   
A1LWU C04  C  Y N 10  
A1LWU C05  C  Y N 11  
A1LWU C06  C  Y N 12  
A1LWU N07  N  N N 13  
A1LWU C08  C  N N 14  
A1LWU C09  C  N N 15  
A1LWU N10  N  N N 16  
A1LWU C11  C  N N 17  
A1LWU C12  C  N N 18  
A1LWU C14  C  N N 19  
A1LWU O15  O  N N 20  
A1LWU C16  C  N N 21  
A1LWU C18  C  N N 22  
A1LWU C19  C  N N 23  
A1LWU O21  O  N N 24  
A1LWU O22  O  N N 25  
A1LWU O23  O  N N 26  
A1LWU O25  O  N N 27  
A1LWU C27  C  Y N 28  
A1LWU C29  C  Y N 29  
A1LWU C30  C  Y N 30  
A1LWU C31  C  Y N 31  
A1LWU C32  C  Y N 32  
A1LWU C33  C  N N 33  
A1LWU N34  N  N N 34  
A1LWU H1   H  N N 35  
A1LWU H2   H  N N 36  
A1LWU H3   H  N N 37  
A1LWU H4   H  N N 38  
A1LWU H5   H  N N 39  
A1LWU H6   H  N N 40  
A1LWU H7   H  N N 41  
A1LWU H8   H  N N 42  
A1LWU H9   H  N N 43  
A1LWU H10  H  N N 44  
A1LWU H13  H  N N 45  
A1LWU H14  H  N N 46  
A1LWU H15  H  N N 47  
A1LWU H16  H  N N 48  
A1LWU H17  H  N N 49  
A1LWU H20  H  N N 50  
A1LWU H21  H  N N 51  
A1LWU H22  H  N N 52  
A1LWU H23  H  N N 53  
A1LWU H24  H  N N 54  
A1LWU H25  H  N N 55  
A1LWU H26  H  N N 56  
A1LWU H27  H  N N 57  
ALA   N    N  N N 58  
ALA   CA   C  N S 59  
ALA   C    C  N N 60  
ALA   O    O  N N 61  
ALA   CB   C  N N 62  
ALA   OXT  O  N N 63  
ALA   H    H  N N 64  
ALA   H2   H  N N 65  
ALA   HA   H  N N 66  
ALA   HB1  H  N N 67  
ALA   HB2  H  N N 68  
ALA   HB3  H  N N 69  
ALA   HXT  H  N N 70  
ARG   N    N  N N 71  
ARG   CA   C  N S 72  
ARG   C    C  N N 73  
ARG   O    O  N N 74  
ARG   CB   C  N N 75  
ARG   CG   C  N N 76  
ARG   CD   C  N N 77  
ARG   NE   N  N N 78  
ARG   CZ   C  N N 79  
ARG   NH1  N  N N 80  
ARG   NH2  N  N N 81  
ARG   OXT  O  N N 82  
ARG   H    H  N N 83  
ARG   H2   H  N N 84  
ARG   HA   H  N N 85  
ARG   HB2  H  N N 86  
ARG   HB3  H  N N 87  
ARG   HG2  H  N N 88  
ARG   HG3  H  N N 89  
ARG   HD2  H  N N 90  
ARG   HD3  H  N N 91  
ARG   HE   H  N N 92  
ARG   HH11 H  N N 93  
ARG   HH12 H  N N 94  
ARG   HH21 H  N N 95  
ARG   HH22 H  N N 96  
ARG   HXT  H  N N 97  
ASN   N    N  N N 98  
ASN   CA   C  N S 99  
ASN   C    C  N N 100 
ASN   O    O  N N 101 
ASN   CB   C  N N 102 
ASN   CG   C  N N 103 
ASN   OD1  O  N N 104 
ASN   ND2  N  N N 105 
ASN   OXT  O  N N 106 
ASN   H    H  N N 107 
ASN   H2   H  N N 108 
ASN   HA   H  N N 109 
ASN   HB2  H  N N 110 
ASN   HB3  H  N N 111 
ASN   HD21 H  N N 112 
ASN   HD22 H  N N 113 
ASN   HXT  H  N N 114 
ASP   N    N  N N 115 
ASP   CA   C  N S 116 
ASP   C    C  N N 117 
ASP   O    O  N N 118 
ASP   CB   C  N N 119 
ASP   CG   C  N N 120 
ASP   OD1  O  N N 121 
ASP   OD2  O  N N 122 
ASP   OXT  O  N N 123 
ASP   H    H  N N 124 
ASP   H2   H  N N 125 
ASP   HA   H  N N 126 
ASP   HB2  H  N N 127 
ASP   HB3  H  N N 128 
ASP   HD2  H  N N 129 
ASP   HXT  H  N N 130 
CO    CO   CO N N 131 
CYS   N    N  N N 132 
CYS   CA   C  N R 133 
CYS   C    C  N N 134 
CYS   O    O  N N 135 
CYS   CB   C  N N 136 
CYS   SG   S  N N 137 
CYS   OXT  O  N N 138 
CYS   H    H  N N 139 
CYS   H2   H  N N 140 
CYS   HA   H  N N 141 
CYS   HB2  H  N N 142 
CYS   HB3  H  N N 143 
CYS   HG   H  N N 144 
CYS   HXT  H  N N 145 
GLN   N    N  N N 146 
GLN   CA   C  N S 147 
GLN   C    C  N N 148 
GLN   O    O  N N 149 
GLN   CB   C  N N 150 
GLN   CG   C  N N 151 
GLN   CD   C  N N 152 
GLN   OE1  O  N N 153 
GLN   NE2  N  N N 154 
GLN   OXT  O  N N 155 
GLN   H    H  N N 156 
GLN   H2   H  N N 157 
GLN   HA   H  N N 158 
GLN   HB2  H  N N 159 
GLN   HB3  H  N N 160 
GLN   HG2  H  N N 161 
GLN   HG3  H  N N 162 
GLN   HE21 H  N N 163 
GLN   HE22 H  N N 164 
GLN   HXT  H  N N 165 
GLU   N    N  N N 166 
GLU   CA   C  N S 167 
GLU   C    C  N N 168 
GLU   O    O  N N 169 
GLU   CB   C  N N 170 
GLU   CG   C  N N 171 
GLU   CD   C  N N 172 
GLU   OE1  O  N N 173 
GLU   OE2  O  N N 174 
GLU   OXT  O  N N 175 
GLU   H    H  N N 176 
GLU   H2   H  N N 177 
GLU   HA   H  N N 178 
GLU   HB2  H  N N 179 
GLU   HB3  H  N N 180 
GLU   HG2  H  N N 181 
GLU   HG3  H  N N 182 
GLU   HE2  H  N N 183 
GLU   HXT  H  N N 184 
GLY   N    N  N N 185 
GLY   CA   C  N N 186 
GLY   C    C  N N 187 
GLY   O    O  N N 188 
GLY   OXT  O  N N 189 
GLY   H    H  N N 190 
GLY   H2   H  N N 191 
GLY   HA2  H  N N 192 
GLY   HA3  H  N N 193 
GLY   HXT  H  N N 194 
HIS   N    N  N N 195 
HIS   CA   C  N S 196 
HIS   C    C  N N 197 
HIS   O    O  N N 198 
HIS   CB   C  N N 199 
HIS   CG   C  Y N 200 
HIS   ND1  N  Y N 201 
HIS   CD2  C  Y N 202 
HIS   CE1  C  Y N 203 
HIS   NE2  N  Y N 204 
HIS   OXT  O  N N 205 
HIS   H    H  N N 206 
HIS   H2   H  N N 207 
HIS   HA   H  N N 208 
HIS   HB2  H  N N 209 
HIS   HB3  H  N N 210 
HIS   HD1  H  N N 211 
HIS   HD2  H  N N 212 
HIS   HE1  H  N N 213 
HIS   HE2  H  N N 214 
HIS   HXT  H  N N 215 
HOH   O    O  N N 216 
HOH   H1   H  N N 217 
HOH   H2   H  N N 218 
ILE   N    N  N N 219 
ILE   CA   C  N S 220 
ILE   C    C  N N 221 
ILE   O    O  N N 222 
ILE   CB   C  N S 223 
ILE   CG1  C  N N 224 
ILE   CG2  C  N N 225 
ILE   CD1  C  N N 226 
ILE   OXT  O  N N 227 
ILE   H    H  N N 228 
ILE   H2   H  N N 229 
ILE   HA   H  N N 230 
ILE   HB   H  N N 231 
ILE   HG12 H  N N 232 
ILE   HG13 H  N N 233 
ILE   HG21 H  N N 234 
ILE   HG22 H  N N 235 
ILE   HG23 H  N N 236 
ILE   HD11 H  N N 237 
ILE   HD12 H  N N 238 
ILE   HD13 H  N N 239 
ILE   HXT  H  N N 240 
LEU   N    N  N N 241 
LEU   CA   C  N S 242 
LEU   C    C  N N 243 
LEU   O    O  N N 244 
LEU   CB   C  N N 245 
LEU   CG   C  N N 246 
LEU   CD1  C  N N 247 
LEU   CD2  C  N N 248 
LEU   OXT  O  N N 249 
LEU   H    H  N N 250 
LEU   H2   H  N N 251 
LEU   HA   H  N N 252 
LEU   HB2  H  N N 253 
LEU   HB3  H  N N 254 
LEU   HG   H  N N 255 
LEU   HD11 H  N N 256 
LEU   HD12 H  N N 257 
LEU   HD13 H  N N 258 
LEU   HD21 H  N N 259 
LEU   HD22 H  N N 260 
LEU   HD23 H  N N 261 
LEU   HXT  H  N N 262 
LYS   N    N  N N 263 
LYS   CA   C  N S 264 
LYS   C    C  N N 265 
LYS   O    O  N N 266 
LYS   CB   C  N N 267 
LYS   CG   C  N N 268 
LYS   CD   C  N N 269 
LYS   CE   C  N N 270 
LYS   NZ   N  N N 271 
LYS   OXT  O  N N 272 
LYS   H    H  N N 273 
LYS   H2   H  N N 274 
LYS   HA   H  N N 275 
LYS   HB2  H  N N 276 
LYS   HB3  H  N N 277 
LYS   HG2  H  N N 278 
LYS   HG3  H  N N 279 
LYS   HD2  H  N N 280 
LYS   HD3  H  N N 281 
LYS   HE2  H  N N 282 
LYS   HE3  H  N N 283 
LYS   HZ1  H  N N 284 
LYS   HZ2  H  N N 285 
LYS   HZ3  H  N N 286 
LYS   HXT  H  N N 287 
MET   N    N  N N 288 
MET   CA   C  N S 289 
MET   C    C  N N 290 
MET   O    O  N N 291 
MET   CB   C  N N 292 
MET   CG   C  N N 293 
MET   SD   S  N N 294 
MET   CE   C  N N 295 
MET   OXT  O  N N 296 
MET   H    H  N N 297 
MET   H2   H  N N 298 
MET   HA   H  N N 299 
MET   HB2  H  N N 300 
MET   HB3  H  N N 301 
MET   HG2  H  N N 302 
MET   HG3  H  N N 303 
MET   HE1  H  N N 304 
MET   HE2  H  N N 305 
MET   HE3  H  N N 306 
MET   HXT  H  N N 307 
PHE   N    N  N N 308 
PHE   CA   C  N S 309 
PHE   C    C  N N 310 
PHE   O    O  N N 311 
PHE   CB   C  N N 312 
PHE   CG   C  Y N 313 
PHE   CD1  C  Y N 314 
PHE   CD2  C  Y N 315 
PHE   CE1  C  Y N 316 
PHE   CE2  C  Y N 317 
PHE   CZ   C  Y N 318 
PHE   OXT  O  N N 319 
PHE   H    H  N N 320 
PHE   H2   H  N N 321 
PHE   HA   H  N N 322 
PHE   HB2  H  N N 323 
PHE   HB3  H  N N 324 
PHE   HD1  H  N N 325 
PHE   HD2  H  N N 326 
PHE   HE1  H  N N 327 
PHE   HE2  H  N N 328 
PHE   HZ   H  N N 329 
PHE   HXT  H  N N 330 
PRO   N    N  N N 331 
PRO   CA   C  N S 332 
PRO   C    C  N N 333 
PRO   O    O  N N 334 
PRO   CB   C  N N 335 
PRO   CG   C  N N 336 
PRO   CD   C  N N 337 
PRO   OXT  O  N N 338 
PRO   H    H  N N 339 
PRO   HA   H  N N 340 
PRO   HB2  H  N N 341 
PRO   HB3  H  N N 342 
PRO   HG2  H  N N 343 
PRO   HG3  H  N N 344 
PRO   HD2  H  N N 345 
PRO   HD3  H  N N 346 
PRO   HXT  H  N N 347 
SER   N    N  N N 348 
SER   CA   C  N S 349 
SER   C    C  N N 350 
SER   O    O  N N 351 
SER   CB   C  N N 352 
SER   OG   O  N N 353 
SER   OXT  O  N N 354 
SER   H    H  N N 355 
SER   H2   H  N N 356 
SER   HA   H  N N 357 
SER   HB2  H  N N 358 
SER   HB3  H  N N 359 
SER   HG   H  N N 360 
SER   HXT  H  N N 361 
THR   N    N  N N 362 
THR   CA   C  N S 363 
THR   C    C  N N 364 
THR   O    O  N N 365 
THR   CB   C  N R 366 
THR   OG1  O  N N 367 
THR   CG2  C  N N 368 
THR   OXT  O  N N 369 
THR   H    H  N N 370 
THR   H2   H  N N 371 
THR   HA   H  N N 372 
THR   HB   H  N N 373 
THR   HG1  H  N N 374 
THR   HG21 H  N N 375 
THR   HG22 H  N N 376 
THR   HG23 H  N N 377 
THR   HXT  H  N N 378 
TRP   N    N  N N 379 
TRP   CA   C  N S 380 
TRP   C    C  N N 381 
TRP   O    O  N N 382 
TRP   CB   C  N N 383 
TRP   CG   C  Y N 384 
TRP   CD1  C  Y N 385 
TRP   CD2  C  Y N 386 
TRP   NE1  N  Y N 387 
TRP   CE2  C  Y N 388 
TRP   CE3  C  Y N 389 
TRP   CZ2  C  Y N 390 
TRP   CZ3  C  Y N 391 
TRP   CH2  C  Y N 392 
TRP   OXT  O  N N 393 
TRP   H    H  N N 394 
TRP   H2   H  N N 395 
TRP   HA   H  N N 396 
TRP   HB2  H  N N 397 
TRP   HB3  H  N N 398 
TRP   HD1  H  N N 399 
TRP   HE1  H  N N 400 
TRP   HE3  H  N N 401 
TRP   HZ2  H  N N 402 
TRP   HZ3  H  N N 403 
TRP   HH2  H  N N 404 
TRP   HXT  H  N N 405 
TYR   N    N  N N 406 
TYR   CA   C  N S 407 
TYR   C    C  N N 408 
TYR   O    O  N N 409 
TYR   CB   C  N N 410 
TYR   CG   C  Y N 411 
TYR   CD1  C  Y N 412 
TYR   CD2  C  Y N 413 
TYR   CE1  C  Y N 414 
TYR   CE2  C  Y N 415 
TYR   CZ   C  Y N 416 
TYR   OH   O  N N 417 
TYR   OXT  O  N N 418 
TYR   H    H  N N 419 
TYR   H2   H  N N 420 
TYR   HA   H  N N 421 
TYR   HB2  H  N N 422 
TYR   HB3  H  N N 423 
TYR   HD1  H  N N 424 
TYR   HD2  H  N N 425 
TYR   HE1  H  N N 426 
TYR   HE2  H  N N 427 
TYR   HH   H  N N 428 
TYR   HXT  H  N N 429 
VAL   N    N  N N 430 
VAL   CA   C  N S 431 
VAL   C    C  N N 432 
VAL   O    O  N N 433 
VAL   CB   C  N N 434 
VAL   CG1  C  N N 435 
VAL   CG2  C  N N 436 
VAL   OXT  O  N N 437 
VAL   H    H  N N 438 
VAL   H2   H  N N 439 
VAL   HA   H  N N 440 
VAL   HB   H  N N 441 
VAL   HG11 H  N N 442 
VAL   HG12 H  N N 443 
VAL   HG13 H  N N 444 
VAL   HG21 H  N N 445 
VAL   HG22 H  N N 446 
VAL   HG23 H  N N 447 
VAL   HXT  H  N N 448 
# 
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 
A1LWU C13 C01  sing N N 1   
A1LWU C13 C14  sing N N 2   
A1LWU C13 O15  doub N N 3   
A1LWU C17 C16  sing N N 4   
A1LWU C17 C18  sing N N 5   
A1LWU C20 C14  sing N N 6   
A1LWU C20 C19  sing N N 7   
A1LWU C20 O22  doub N N 8   
A1LWU C24 N10  sing N N 9   
A1LWU C24 C27  sing N N 10  
A1LWU C26 N07  sing N N 11  
A1LWU C28 C27  doub Y N 12  
A1LWU C28 C29  sing Y N 13  
A1LWU C01 C02  doub Y N 14  
A1LWU C01 C06  sing Y N 15  
A1LWU C02 C03  sing Y N 16  
A1LWU C03 C04  doub Y N 17  
A1LWU C04 C05  sing Y N 18  
A1LWU C05 C06  doub Y N 19  
A1LWU C05 C11  sing N N 20  
A1LWU C06 C12  sing N N 21  
A1LWU N07 C08  sing N N 22  
A1LWU C08 C09  sing N N 23  
A1LWU C08 O25  doub N N 24  
A1LWU C09 N10  sing N N 25  
A1LWU N10 C11  sing N N 26  
A1LWU C11 O23  doub N N 27  
A1LWU C14 C16  doub N N 28  
A1LWU C16 O21  sing N N 29  
A1LWU C18 C19  sing N N 30  
A1LWU C27 C32  sing Y N 31  
A1LWU C29 C30  doub Y N 32  
A1LWU C30 C31  sing Y N 33  
A1LWU C30 C33  sing N N 34  
A1LWU C31 C32  doub Y N 35  
A1LWU C33 N34  trip N N 36  
A1LWU C17 H1   sing N N 37  
A1LWU C17 H2   sing N N 38  
A1LWU C24 H3   sing N N 39  
A1LWU C24 H4   sing N N 40  
A1LWU C26 H5   sing N N 41  
A1LWU C26 H6   sing N N 42  
A1LWU C26 H7   sing N N 43  
A1LWU C28 H8   sing N N 44  
A1LWU C02 H9   sing N N 45  
A1LWU C03 H10  sing N N 46  
A1LWU C09 H13  sing N N 47  
A1LWU C09 H14  sing N N 48  
A1LWU C12 H15  sing N N 49  
A1LWU C12 H16  sing N N 50  
A1LWU C12 H17  sing N N 51  
A1LWU C18 H20  sing N N 52  
A1LWU C18 H21  sing N N 53  
A1LWU C19 H22  sing N N 54  
A1LWU C19 H23  sing N N 55  
A1LWU O21 H24  sing N N 56  
A1LWU C29 H25  sing N N 57  
A1LWU C31 H26  sing N N 58  
A1LWU C32 H27  sing N N 59  
A1LWU N07 C04  sing N N 60  
ALA   N   CA   sing N N 61  
ALA   N   H    sing N N 62  
ALA   N   H2   sing N N 63  
ALA   CA  C    sing N N 64  
ALA   CA  CB   sing N N 65  
ALA   CA  HA   sing N N 66  
ALA   C   O    doub N N 67  
ALA   C   OXT  sing N N 68  
ALA   CB  HB1  sing N N 69  
ALA   CB  HB2  sing N N 70  
ALA   CB  HB3  sing N N 71  
ALA   OXT HXT  sing N N 72  
ARG   N   CA   sing N N 73  
ARG   N   H    sing N N 74  
ARG   N   H2   sing N N 75  
ARG   CA  C    sing N N 76  
ARG   CA  CB   sing N N 77  
ARG   CA  HA   sing N N 78  
ARG   C   O    doub N N 79  
ARG   C   OXT  sing N N 80  
ARG   CB  CG   sing N N 81  
ARG   CB  HB2  sing N N 82  
ARG   CB  HB3  sing N N 83  
ARG   CG  CD   sing N N 84  
ARG   CG  HG2  sing N N 85  
ARG   CG  HG3  sing N N 86  
ARG   CD  NE   sing N N 87  
ARG   CD  HD2  sing N N 88  
ARG   CD  HD3  sing N N 89  
ARG   NE  CZ   sing N N 90  
ARG   NE  HE   sing N N 91  
ARG   CZ  NH1  sing N N 92  
ARG   CZ  NH2  doub N N 93  
ARG   NH1 HH11 sing N N 94  
ARG   NH1 HH12 sing N N 95  
ARG   NH2 HH21 sing N N 96  
ARG   NH2 HH22 sing N N 97  
ARG   OXT HXT  sing N N 98  
ASN   N   CA   sing N N 99  
ASN   N   H    sing N N 100 
ASN   N   H2   sing N N 101 
ASN   CA  C    sing N N 102 
ASN   CA  CB   sing N N 103 
ASN   CA  HA   sing N N 104 
ASN   C   O    doub N N 105 
ASN   C   OXT  sing N N 106 
ASN   CB  CG   sing N N 107 
ASN   CB  HB2  sing N N 108 
ASN   CB  HB3  sing N N 109 
ASN   CG  OD1  doub N N 110 
ASN   CG  ND2  sing N N 111 
ASN   ND2 HD21 sing N N 112 
ASN   ND2 HD22 sing N N 113 
ASN   OXT HXT  sing N N 114 
ASP   N   CA   sing N N 115 
ASP   N   H    sing N N 116 
ASP   N   H2   sing N N 117 
ASP   CA  C    sing N N 118 
ASP   CA  CB   sing N N 119 
ASP   CA  HA   sing N N 120 
ASP   C   O    doub N N 121 
ASP   C   OXT  sing N N 122 
ASP   CB  CG   sing N N 123 
ASP   CB  HB2  sing N N 124 
ASP   CB  HB3  sing N N 125 
ASP   CG  OD1  doub N N 126 
ASP   CG  OD2  sing N N 127 
ASP   OD2 HD2  sing N N 128 
ASP   OXT HXT  sing N N 129 
CYS   N   CA   sing N N 130 
CYS   N   H    sing N N 131 
CYS   N   H2   sing N N 132 
CYS   CA  C    sing N N 133 
CYS   CA  CB   sing N N 134 
CYS   CA  HA   sing N N 135 
CYS   C   O    doub N N 136 
CYS   C   OXT  sing N N 137 
CYS   CB  SG   sing N N 138 
CYS   CB  HB2  sing N N 139 
CYS   CB  HB3  sing N N 140 
CYS   SG  HG   sing N N 141 
CYS   OXT HXT  sing N N 142 
GLN   N   CA   sing N N 143 
GLN   N   H    sing N N 144 
GLN   N   H2   sing N N 145 
GLN   CA  C    sing N N 146 
GLN   CA  CB   sing N N 147 
GLN   CA  HA   sing N N 148 
GLN   C   O    doub N N 149 
GLN   C   OXT  sing N N 150 
GLN   CB  CG   sing N N 151 
GLN   CB  HB2  sing N N 152 
GLN   CB  HB3  sing N N 153 
GLN   CG  CD   sing N N 154 
GLN   CG  HG2  sing N N 155 
GLN   CG  HG3  sing N N 156 
GLN   CD  OE1  doub N N 157 
GLN   CD  NE2  sing N N 158 
GLN   NE2 HE21 sing N N 159 
GLN   NE2 HE22 sing N N 160 
GLN   OXT HXT  sing N N 161 
GLU   N   CA   sing N N 162 
GLU   N   H    sing N N 163 
GLU   N   H2   sing N N 164 
GLU   CA  C    sing N N 165 
GLU   CA  CB   sing N N 166 
GLU   CA  HA   sing N N 167 
GLU   C   O    doub N N 168 
GLU   C   OXT  sing N N 169 
GLU   CB  CG   sing N N 170 
GLU   CB  HB2  sing N N 171 
GLU   CB  HB3  sing N N 172 
GLU   CG  CD   sing N N 173 
GLU   CG  HG2  sing N N 174 
GLU   CG  HG3  sing N N 175 
GLU   CD  OE1  doub N N 176 
GLU   CD  OE2  sing N N 177 
GLU   OE2 HE2  sing N N 178 
GLU   OXT HXT  sing N N 179 
GLY   N   CA   sing N N 180 
GLY   N   H    sing N N 181 
GLY   N   H2   sing N N 182 
GLY   CA  C    sing N N 183 
GLY   CA  HA2  sing N N 184 
GLY   CA  HA3  sing N N 185 
GLY   C   O    doub N N 186 
GLY   C   OXT  sing N N 187 
GLY   OXT HXT  sing N N 188 
HIS   N   CA   sing N N 189 
HIS   N   H    sing N N 190 
HIS   N   H2   sing N N 191 
HIS   CA  C    sing N N 192 
HIS   CA  CB   sing N N 193 
HIS   CA  HA   sing N N 194 
HIS   C   O    doub N N 195 
HIS   C   OXT  sing N N 196 
HIS   CB  CG   sing N N 197 
HIS   CB  HB2  sing N N 198 
HIS   CB  HB3  sing N N 199 
HIS   CG  ND1  sing Y N 200 
HIS   CG  CD2  doub Y N 201 
HIS   ND1 CE1  doub Y N 202 
HIS   ND1 HD1  sing N N 203 
HIS   CD2 NE2  sing Y N 204 
HIS   CD2 HD2  sing N N 205 
HIS   CE1 NE2  sing Y N 206 
HIS   CE1 HE1  sing N N 207 
HIS   NE2 HE2  sing N N 208 
HIS   OXT HXT  sing N N 209 
HOH   O   H1   sing N N 210 
HOH   O   H2   sing N N 211 
ILE   N   CA   sing N N 212 
ILE   N   H    sing N N 213 
ILE   N   H2   sing N N 214 
ILE   CA  C    sing N N 215 
ILE   CA  CB   sing N N 216 
ILE   CA  HA   sing N N 217 
ILE   C   O    doub N N 218 
ILE   C   OXT  sing N N 219 
ILE   CB  CG1  sing N N 220 
ILE   CB  CG2  sing N N 221 
ILE   CB  HB   sing N N 222 
ILE   CG1 CD1  sing N N 223 
ILE   CG1 HG12 sing N N 224 
ILE   CG1 HG13 sing N N 225 
ILE   CG2 HG21 sing N N 226 
ILE   CG2 HG22 sing N N 227 
ILE   CG2 HG23 sing N N 228 
ILE   CD1 HD11 sing N N 229 
ILE   CD1 HD12 sing N N 230 
ILE   CD1 HD13 sing N N 231 
ILE   OXT HXT  sing N N 232 
LEU   N   CA   sing N N 233 
LEU   N   H    sing N N 234 
LEU   N   H2   sing N N 235 
LEU   CA  C    sing N N 236 
LEU   CA  CB   sing N N 237 
LEU   CA  HA   sing N N 238 
LEU   C   O    doub N N 239 
LEU   C   OXT  sing N N 240 
LEU   CB  CG   sing N N 241 
LEU   CB  HB2  sing N N 242 
LEU   CB  HB3  sing N N 243 
LEU   CG  CD1  sing N N 244 
LEU   CG  CD2  sing N N 245 
LEU   CG  HG   sing N N 246 
LEU   CD1 HD11 sing N N 247 
LEU   CD1 HD12 sing N N 248 
LEU   CD1 HD13 sing N N 249 
LEU   CD2 HD21 sing N N 250 
LEU   CD2 HD22 sing N N 251 
LEU   CD2 HD23 sing N N 252 
LEU   OXT HXT  sing N N 253 
LYS   N   CA   sing N N 254 
LYS   N   H    sing N N 255 
LYS   N   H2   sing N N 256 
LYS   CA  C    sing N N 257 
LYS   CA  CB   sing N N 258 
LYS   CA  HA   sing N N 259 
LYS   C   O    doub N N 260 
LYS   C   OXT  sing N N 261 
LYS   CB  CG   sing N N 262 
LYS   CB  HB2  sing N N 263 
LYS   CB  HB3  sing N N 264 
LYS   CG  CD   sing N N 265 
LYS   CG  HG2  sing N N 266 
LYS   CG  HG3  sing N N 267 
LYS   CD  CE   sing N N 268 
LYS   CD  HD2  sing N N 269 
LYS   CD  HD3  sing N N 270 
LYS   CE  NZ   sing N N 271 
LYS   CE  HE2  sing N N 272 
LYS   CE  HE3  sing N N 273 
LYS   NZ  HZ1  sing N N 274 
LYS   NZ  HZ2  sing N N 275 
LYS   NZ  HZ3  sing N N 276 
LYS   OXT HXT  sing N N 277 
MET   N   CA   sing N N 278 
MET   N   H    sing N N 279 
MET   N   H2   sing N N 280 
MET   CA  C    sing N N 281 
MET   CA  CB   sing N N 282 
MET   CA  HA   sing N N 283 
MET   C   O    doub N N 284 
MET   C   OXT  sing N N 285 
MET   CB  CG   sing N N 286 
MET   CB  HB2  sing N N 287 
MET   CB  HB3  sing N N 288 
MET   CG  SD   sing N N 289 
MET   CG  HG2  sing N N 290 
MET   CG  HG3  sing N N 291 
MET   SD  CE   sing N N 292 
MET   CE  HE1  sing N N 293 
MET   CE  HE2  sing N N 294 
MET   CE  HE3  sing N N 295 
MET   OXT HXT  sing N N 296 
PHE   N   CA   sing N N 297 
PHE   N   H    sing N N 298 
PHE   N   H2   sing N N 299 
PHE   CA  C    sing N N 300 
PHE   CA  CB   sing N N 301 
PHE   CA  HA   sing N N 302 
PHE   C   O    doub N N 303 
PHE   C   OXT  sing N N 304 
PHE   CB  CG   sing N N 305 
PHE   CB  HB2  sing N N 306 
PHE   CB  HB3  sing N N 307 
PHE   CG  CD1  doub Y N 308 
PHE   CG  CD2  sing Y N 309 
PHE   CD1 CE1  sing Y N 310 
PHE   CD1 HD1  sing N N 311 
PHE   CD2 CE2  doub Y N 312 
PHE   CD2 HD2  sing N N 313 
PHE   CE1 CZ   doub Y N 314 
PHE   CE1 HE1  sing N N 315 
PHE   CE2 CZ   sing Y N 316 
PHE   CE2 HE2  sing N N 317 
PHE   CZ  HZ   sing N N 318 
PHE   OXT HXT  sing N N 319 
PRO   N   CA   sing N N 320 
PRO   N   CD   sing N N 321 
PRO   N   H    sing N N 322 
PRO   CA  C    sing N N 323 
PRO   CA  CB   sing N N 324 
PRO   CA  HA   sing N N 325 
PRO   C   O    doub N N 326 
PRO   C   OXT  sing N N 327 
PRO   CB  CG   sing N N 328 
PRO   CB  HB2  sing N N 329 
PRO   CB  HB3  sing N N 330 
PRO   CG  CD   sing N N 331 
PRO   CG  HG2  sing N N 332 
PRO   CG  HG3  sing N N 333 
PRO   CD  HD2  sing N N 334 
PRO   CD  HD3  sing N N 335 
PRO   OXT HXT  sing N N 336 
SER   N   CA   sing N N 337 
SER   N   H    sing N N 338 
SER   N   H2   sing N N 339 
SER   CA  C    sing N N 340 
SER   CA  CB   sing N N 341 
SER   CA  HA   sing N N 342 
SER   C   O    doub N N 343 
SER   C   OXT  sing N N 344 
SER   CB  OG   sing N N 345 
SER   CB  HB2  sing N N 346 
SER   CB  HB3  sing N N 347 
SER   OG  HG   sing N N 348 
SER   OXT HXT  sing N N 349 
THR   N   CA   sing N N 350 
THR   N   H    sing N N 351 
THR   N   H2   sing N N 352 
THR   CA  C    sing N N 353 
THR   CA  CB   sing N N 354 
THR   CA  HA   sing N N 355 
THR   C   O    doub N N 356 
THR   C   OXT  sing N N 357 
THR   CB  OG1  sing N N 358 
THR   CB  CG2  sing N N 359 
THR   CB  HB   sing N N 360 
THR   OG1 HG1  sing N N 361 
THR   CG2 HG21 sing N N 362 
THR   CG2 HG22 sing N N 363 
THR   CG2 HG23 sing N N 364 
THR   OXT HXT  sing N N 365 
TRP   N   CA   sing N N 366 
TRP   N   H    sing N N 367 
TRP   N   H2   sing N N 368 
TRP   CA  C    sing N N 369 
TRP   CA  CB   sing N N 370 
TRP   CA  HA   sing N N 371 
TRP   C   O    doub N N 372 
TRP   C   OXT  sing N N 373 
TRP   CB  CG   sing N N 374 
TRP   CB  HB2  sing N N 375 
TRP   CB  HB3  sing N N 376 
TRP   CG  CD1  doub Y N 377 
TRP   CG  CD2  sing Y N 378 
TRP   CD1 NE1  sing Y N 379 
TRP   CD1 HD1  sing N N 380 
TRP   CD2 CE2  doub Y N 381 
TRP   CD2 CE3  sing Y N 382 
TRP   NE1 CE2  sing Y N 383 
TRP   NE1 HE1  sing N N 384 
TRP   CE2 CZ2  sing Y N 385 
TRP   CE3 CZ3  doub Y N 386 
TRP   CE3 HE3  sing N N 387 
TRP   CZ2 CH2  doub Y N 388 
TRP   CZ2 HZ2  sing N N 389 
TRP   CZ3 CH2  sing Y N 390 
TRP   CZ3 HZ3  sing N N 391 
TRP   CH2 HH2  sing N N 392 
TRP   OXT HXT  sing N N 393 
TYR   N   CA   sing N N 394 
TYR   N   H    sing N N 395 
TYR   N   H2   sing N N 396 
TYR   CA  C    sing N N 397 
TYR   CA  CB   sing N N 398 
TYR   CA  HA   sing N N 399 
TYR   C   O    doub N N 400 
TYR   C   OXT  sing N N 401 
TYR   CB  CG   sing N N 402 
TYR   CB  HB2  sing N N 403 
TYR   CB  HB3  sing N N 404 
TYR   CG  CD1  doub Y N 405 
TYR   CG  CD2  sing Y N 406 
TYR   CD1 CE1  sing Y N 407 
TYR   CD1 HD1  sing N N 408 
TYR   CD2 CE2  doub Y N 409 
TYR   CD2 HD2  sing N N 410 
TYR   CE1 CZ   doub Y N 411 
TYR   CE1 HE1  sing N N 412 
TYR   CE2 CZ   sing Y N 413 
TYR   CE2 HE2  sing N N 414 
TYR   CZ  OH   sing N N 415 
TYR   OH  HH   sing N N 416 
TYR   OXT HXT  sing N N 417 
VAL   N   CA   sing N N 418 
VAL   N   H    sing N N 419 
VAL   N   H2   sing N N 420 
VAL   CA  C    sing N N 421 
VAL   CA  CB   sing N N 422 
VAL   CA  HA   sing N N 423 
VAL   C   O    doub N N 424 
VAL   C   OXT  sing N N 425 
VAL   CB  CG1  sing N N 426 
VAL   CB  CG2  sing N N 427 
VAL   CB  HB   sing N N 428 
VAL   CG1 HG11 sing N N 429 
VAL   CG1 HG12 sing N N 430 
VAL   CG1 HG13 sing N N 431 
VAL   CG2 HG21 sing N N 432 
VAL   CG2 HG22 sing N N 433 
VAL   CG2 HG23 sing N N 434 
VAL   OXT HXT  sing N N 435 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5YY6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XQV 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.016820 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002035 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011926 
_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]   0.013421 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CO 
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   . LYS   A 1 1   ? 6.908   3.955   -20.021 1.00 70.00 ? 35  LYS   A N   1 
ATOM   2    C  CA  . LYS   A 1 1   ? 7.413   5.273   -20.393 1.00 72.34 ? 35  LYS   A CA  1 
ATOM   3    C  C   . LYS   A 1 1   ? 8.596   5.681   -19.506 1.00 74.77 ? 35  LYS   A C   1 
ATOM   4    O  O   . LYS   A 1 1   ? 8.407   6.142   -18.378 1.00 74.37 ? 35  LYS   A O   1 
ATOM   5    C  CB  . LYS   A 1 1   ? 6.297   6.318   -20.305 1.00 56.41 ? 35  LYS   A CB  1 
ATOM   6    N  N   . ASN   A 1 2   ? 9.815   5.500   -20.022 1.00 62.95 ? 36  ASN   A N   1 
ATOM   7    C  CA  . ASN   A 1 2   ? 11.051  5.877   -19.336 1.00 51.87 ? 36  ASN   A CA  1 
ATOM   8    C  C   . ASN   A 1 2   ? 11.725  6.948   -20.183 1.00 55.83 ? 36  ASN   A C   1 
ATOM   9    O  O   . ASN   A 1 2   ? 12.522  6.626   -21.079 1.00 56.81 ? 36  ASN   A O   1 
ATOM   10   C  CB  . ASN   A 1 2   ? 11.951  4.657   -19.132 1.00 57.15 ? 36  ASN   A CB  1 
ATOM   11   C  CG  . ASN   A 1 2   ? 13.289  5.000   -18.495 1.00 50.75 ? 36  ASN   A CG  1 
ATOM   12   O  OD1 . ASN   A 1 2   ? 13.531  6.133   -18.093 1.00 47.84 ? 36  ASN   A OD1 1 
ATOM   13   N  ND2 . ASN   A 1 2   ? 14.158  4.002   -18.382 1.00 55.56 ? 36  ASN   A ND2 1 
ATOM   14   N  N   . PRO   A 1 3   ? 11.447  8.236   -19.929 1.00 56.61 ? 37  PRO   A N   1 
ATOM   15   C  CA  . PRO   A 1 3   ? 11.880  9.292   -20.863 1.00 52.86 ? 37  PRO   A CA  1 
ATOM   16   C  C   . PRO   A 1 3   ? 13.380  9.571   -20.886 1.00 58.77 ? 37  PRO   A C   1 
ATOM   17   O  O   . PRO   A 1 3   ? 13.812  10.360  -21.744 1.00 60.16 ? 37  PRO   A O   1 
ATOM   18   C  CB  . PRO   A 1 3   ? 11.098  10.524  -20.386 1.00 47.26 ? 37  PRO   A CB  1 
ATOM   19   C  CG  . PRO   A 1 3   ? 10.801  10.259  -18.979 1.00 50.95 ? 37  PRO   A CG  1 
ATOM   20   C  CD  . PRO   A 1 3   ? 10.562  8.777   -18.886 1.00 58.03 ? 37  PRO   A CD  1 
ATOM   21   N  N   . LYS   A 1 4   ? 14.179  8.965   -20.004 1.00 50.35 ? 38  LYS   A N   1 
ATOM   22   C  CA  . LYS   A 1 4   ? 15.643  9.070   -20.058 1.00 49.98 ? 38  LYS   A CA  1 
ATOM   23   C  C   . LYS   A 1 4   ? 16.106  10.526  -20.165 1.00 51.18 ? 38  LYS   A C   1 
ATOM   24   O  O   . LYS   A 1 4   ? 16.806  10.914  -21.102 1.00 45.14 ? 38  LYS   A O   1 
ATOM   25   C  CB  . LYS   A 1 4   ? 16.228  8.251   -21.221 1.00 51.29 ? 38  LYS   A CB  1 
ATOM   26   C  CG  . LYS   A 1 4   ? 16.119  6.727   -21.113 1.00 53.88 ? 38  LYS   A CG  1 
ATOM   27   C  CD  . LYS   A 1 4   ? 17.416  6.066   -21.553 1.00 48.21 ? 38  LYS   A CD  1 
ATOM   28   C  CE  . LYS   A 1 4   ? 17.215  4.600   -21.886 1.00 61.93 ? 38  LYS   A CE  1 
ATOM   29   N  NZ  . LYS   A 1 4   ? 17.143  4.374   -23.357 1.00 73.16 ? 38  LYS   A NZ  1 
ATOM   30   N  N   . SER   A 1 5   ? 15.716  11.336  -19.176 1.00 50.54 ? 39  SER   A N   1 
ATOM   31   C  CA  . SER   A 1 5   ? 16.012  12.765  -19.185 1.00 38.34 ? 39  SER   A CA  1 
ATOM   32   C  C   . SER   A 1 5   ? 17.097  13.178  -18.186 1.00 32.46 ? 39  SER   A C   1 
ATOM   33   O  O   . SER   A 1 5   ? 17.082  14.308  -17.709 1.00 33.78 ? 39  SER   A O   1 
ATOM   34   C  CB  . SER   A 1 5   ? 14.735  13.567  -18.935 1.00 39.61 ? 39  SER   A CB  1 
ATOM   35   O  OG  . SER   A 1 5   ? 13.879  12.950  -17.992 1.00 41.42 ? 39  SER   A OG  1 
ATOM   36   N  N   . ASP   A 1 6   ? 18.054  12.293  -17.871 1.00 39.35 ? 40  ASP   A N   1 
ATOM   37   C  CA  . ASP   A 1 6   ? 19.144  12.623  -16.947 1.00 37.52 ? 40  ASP   A CA  1 
ATOM   38   C  C   . ASP   A 1 6   ? 19.986  13.771  -17.481 1.00 40.32 ? 40  ASP   A C   1 
ATOM   39   O  O   . ASP   A 1 6   ? 20.718  13.601  -18.459 1.00 43.76 ? 40  ASP   A O   1 
ATOM   40   C  CB  . ASP   A 1 6   ? 20.084  11.434  -16.706 1.00 33.73 ? 40  ASP   A CB  1 
ATOM   41   C  CG  . ASP   A 1 6   ? 19.524  10.392  -15.725 1.00 48.32 ? 40  ASP   A CG  1 
ATOM   42   O  OD1 . ASP   A 1 6   ? 18.472  10.649  -15.082 1.00 45.58 ? 40  ASP   A OD1 1 
ATOM   43   O  OD2 . ASP   A 1 6   ? 20.152  9.299   -15.606 1.00 44.31 ? 40  ASP   A OD2 1 
ATOM   44   N  N   . LYS   A 1 7   ? 19.928  14.924  -16.826 1.00 38.53 ? 41  LYS   A N   1 
ATOM   45   C  CA  . LYS   A 1 7   ? 20.761  16.062  -17.192 1.00 36.93 ? 41  LYS   A CA  1 
ATOM   46   C  C   . LYS   A 1 7   ? 22.276  15.825  -17.019 1.00 37.96 ? 41  LYS   A C   1 
ATOM   47   O  O   . LYS   A 1 7   ? 23.045  16.761  -17.272 1.00 38.30 ? 41  LYS   A O   1 
ATOM   48   C  CB  . LYS   A 1 7   ? 20.341  17.280  -16.371 1.00 36.32 ? 41  LYS   A CB  1 
ATOM   49   C  CG  . LYS   A 1 7   ? 18.935  17.771  -16.645 1.00 36.82 ? 41  LYS   A CG  1 
ATOM   50   C  CD  . LYS   A 1 7   ? 18.773  19.187  -16.091 1.00 39.32 ? 41  LYS   A CD  1 
ATOM   51   C  CE  . LYS   A 1 7   ? 17.399  19.766  -16.399 1.00 37.46 ? 41  LYS   A CE  1 
ATOM   52   N  NZ  . LYS   A 1 7   ? 16.339  18.989  -15.718 1.00 38.93 ? 41  LYS   A NZ  1 
ATOM   53   N  N   . PHE   A 1 8   ? 22.727  14.649  -16.579 1.00 35.79 ? 42  PHE   A N   1 
ATOM   54   C  CA  . PHE   A 1 8   ? 24.145  14.287  -16.549 1.00 31.41 ? 42  PHE   A CA  1 
ATOM   55   C  C   . PHE   A 1 8   ? 24.218  12.784  -16.319 1.00 39.87 ? 42  PHE   A C   1 
ATOM   56   O  O   . PHE   A 1 8   ? 23.207  12.144  -16.022 1.00 45.13 ? 42  PHE   A O   1 
ATOM   57   C  CB  . PHE   A 1 8   ? 24.944  15.064  -15.488 1.00 34.23 ? 42  PHE   A CB  1 
ATOM   58   C  CG  . PHE   A 1 8   ? 24.221  15.259  -14.176 1.00 33.38 ? 42  PHE   A CG  1 
ATOM   59   C  CD1 . PHE   A 1 8   ? 24.147  14.240  -13.241 1.00 33.08 ? 42  PHE   A CD1 1 
ATOM   60   C  CD2 . PHE   A 1 8   ? 23.638  16.485  -13.871 1.00 37.99 ? 42  PHE   A CD2 1 
ATOM   61   C  CE1 . PHE   A 1 8   ? 23.476  14.431  -12.031 1.00 35.21 ? 42  PHE   A CE1 1 
ATOM   62   C  CE2 . PHE   A 1 8   ? 22.970  16.685  -12.667 1.00 36.14 ? 42  PHE   A CE2 1 
ATOM   63   C  CZ  . PHE   A 1 8   ? 22.891  15.660  -11.744 1.00 34.16 ? 42  PHE   A CZ  1 
ATOM   64   N  N   . LYS   A 1 9   ? 25.415  12.214  -16.481 1.00 39.01 ? 43  LYS   A N   1 
ATOM   65   C  CA  . LYS   A 1 9   ? 25.556  10.761  -16.427 1.00 41.58 ? 43  LYS   A CA  1 
ATOM   66   C  C   . LYS   A 1 9   ? 25.626  10.291  -14.975 1.00 43.50 ? 43  LYS   A C   1 
ATOM   67   O  O   . LYS   A 1 9   ? 26.409  10.818  -14.177 1.00 45.34 ? 43  LYS   A O   1 
ATOM   68   C  CB  . LYS   A 1 9   ? 26.796  10.307  -17.209 1.00 43.10 ? 43  LYS   A CB  1 
ATOM   69   C  CG  . LYS   A 1 9   ? 27.072  8.781   -17.197 1.00 44.32 ? 43  LYS   A CG  1 
ATOM   70   C  CD  . LYS   A 1 9   ? 26.306  7.999   -18.268 1.00 43.05 ? 43  LYS   A CD  1 
ATOM   71   C  CE  . LYS   A 1 9   ? 26.629  8.529   -19.677 1.00 54.43 ? 43  LYS   A CE  1 
ATOM   72   N  NZ  . LYS   A 1 9   ? 26.253  7.596   -20.793 1.00 55.38 ? 43  LYS   A NZ  1 
ATOM   73   N  N   . VAL   A 1 10  ? 24.812  9.293   -14.638 1.00 40.89 ? 44  VAL   A N   1 
ATOM   74   C  CA  . VAL   A 1 10  ? 24.702  8.787   -13.274 1.00 44.91 ? 44  VAL   A CA  1 
ATOM   75   C  C   . VAL   A 1 10  ? 24.904  7.273   -13.302 1.00 43.12 ? 44  VAL   A C   1 
ATOM   76   O  O   . VAL   A 1 10  ? 24.207  6.575   -14.044 1.00 41.53 ? 44  VAL   A O   1 
ATOM   77   C  CB  . VAL   A 1 10  ? 23.333  9.148   -12.659 1.00 44.03 ? 44  VAL   A CB  1 
ATOM   78   C  CG1 . VAL   A 1 10  ? 23.159  8.478   -11.309 1.00 46.90 ? 44  VAL   A CG1 1 
ATOM   79   C  CG2 . VAL   A 1 10  ? 23.177  10.657  -12.549 1.00 36.55 ? 44  VAL   A CG2 1 
ATOM   80   N  N   . LYS   A 1 11  ? 25.856  6.758   -12.507 1.00 42.83 ? 45  LYS   A N   1 
ATOM   81   C  CA  . LYS   A 1 11  ? 26.012  5.304   -12.493 1.00 39.51 ? 45  LYS   A CA  1 
ATOM   82   C  C   . LYS   A 1 11  ? 25.048  4.657   -11.507 1.00 35.46 ? 45  LYS   A C   1 
ATOM   83   O  O   . LYS   A 1 11  ? 23.918  4.344   -11.897 1.00 47.12 ? 45  LYS   A O   1 
ATOM   84   C  CB  . LYS   A 1 11  ? 27.460  4.855   -12.241 1.00 42.61 ? 45  LYS   A CB  1 
ATOM   85   C  CG  . LYS   A 1 11  ? 28.143  5.277   -10.947 1.00 51.88 ? 45  LYS   A CG  1 
ATOM   86   C  CD  . LYS   A 1 11  ? 28.934  4.121   -10.245 1.00 52.90 ? 45  LYS   A CD  1 
ATOM   87   C  CE  . LYS   A 1 11  ? 28.092  3.085   -9.509  1.00 47.57 ? 45  LYS   A CE  1 
ATOM   88   N  NZ  . LYS   A 1 11  ? 28.871  1.830   -9.337  1.00 48.11 ? 45  LYS   A NZ  1 
ATOM   89   N  N   . ARG   A 1 12  ? 25.464  4.437   -10.259 1.00 32.87 ? 46  ARG   A N   1 
ATOM   90   C  CA  . ARG   A 1 12  ? 24.622  3.835   -9.230  1.00 39.39 ? 46  ARG   A CA  1 
ATOM   91   C  C   . ARG   A 1 12  ? 24.836  4.576   -7.920  1.00 40.72 ? 46  ARG   A C   1 
ATOM   92   O  O   . ARG   A 1 12  ? 25.571  5.570   -7.849  1.00 40.17 ? 46  ARG   A O   1 
ATOM   93   C  CB  . ARG   A 1 12  ? 24.923  2.346   -9.027  1.00 36.98 ? 46  ARG   A CB  1 
ATOM   94   C  CG  . ARG   A 1 12  ? 25.147  1.572   -10.322 1.00 45.37 ? 46  ARG   A CG  1 
ATOM   95   C  CD  . ARG   A 1 12  ? 24.137  0.476   -10.504 1.00 45.30 ? 46  ARG   A CD  1 
ATOM   96   N  NE  . ARG   A 1 12  ? 24.239  -0.160  -11.814 1.00 60.45 ? 46  ARG   A NE  1 
ATOM   97   C  CZ  . ARG   A 1 12  ? 24.773  -1.360  -12.030 1.00 61.53 ? 46  ARG   A CZ  1 
ATOM   98   N  NH1 . ARG   A 1 12  ? 25.269  -2.063  -11.018 1.00 57.29 ? 46  ARG   A NH1 1 
ATOM   99   N  NH2 . ARG   A 1 12  ? 24.804  -1.861  -13.262 1.00 54.30 ? 46  ARG   A NH2 1 
ATOM   100  N  N   . PHE   A 1 13  ? 24.201  4.081   -6.865  1.00 34.00 ? 47  PHE   A N   1 
ATOM   101  C  CA  . PHE   A 1 13  ? 24.510  4.597   -5.541  1.00 29.49 ? 47  PHE   A CA  1 
ATOM   102  C  C   . PHE   A 1 13  ? 25.981  4.342   -5.221  1.00 30.71 ? 47  PHE   A C   1 
ATOM   103  O  O   . PHE   A 1 13  ? 26.549  3.313   -5.603  1.00 33.18 ? 47  PHE   A O   1 
ATOM   104  C  CB  . PHE   A 1 13  ? 23.595  3.951   -4.498  1.00 26.14 ? 47  PHE   A CB  1 
ATOM   105  C  CG  . PHE   A 1 13  ? 22.190  4.467   -4.536  1.00 24.20 ? 47  PHE   A CG  1 
ATOM   106  C  CD1 . PHE   A 1 13  ? 21.923  5.804   -4.282  1.00 25.59 ? 47  PHE   A CD1 1 
ATOM   107  C  CD2 . PHE   A 1 13  ? 21.134  3.625   -4.810  1.00 21.25 ? 47  PHE   A CD2 1 
ATOM   108  C  CE1 . PHE   A 1 13  ? 20.621  6.280   -4.313  1.00 25.79 ? 47  PHE   A CE1 1 
ATOM   109  C  CE2 . PHE   A 1 13  ? 19.842  4.105   -4.853  1.00 22.63 ? 47  PHE   A CE2 1 
ATOM   110  C  CZ  . PHE   A 1 13  ? 19.582  5.428   -4.602  1.00 20.87 ? 47  PHE   A CZ  1 
ATOM   111  N  N   . HIS   A 1 14  ? 26.618  5.301   -4.544  1.00 29.88 ? 48  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 14  ? 28.022  5.145   -4.170  1.00 31.85 ? 48  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 14  ? 28.202  4.785   -2.695  1.00 30.72 ? 48  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 14  ? 28.826  3.767   -2.382  1.00 31.03 ? 48  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 14  ? 28.838  6.400   -4.515  1.00 27.11 ? 48  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 14  ? 30.316  6.199   -4.353  1.00 35.56 ? 48  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 14  ? 30.986  6.480   -3.179  1.00 34.70 ? 48  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 14  ? 31.248  5.702   -5.201  1.00 35.33 ? 48  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 14  ? 32.265  6.185   -3.316  1.00 32.09 ? 48  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 14  ? 32.451  5.714   -4.535  1.00 32.45 ? 48  HIS   A NE2 1 
ATOM   121  N  N   . HIS   A 1 15  ? 27.702  5.612   -1.777  1.00 26.81 ? 49  HIS   A N   1 
ATOM   122  C  CA  . HIS   A 1 15  ? 27.705  5.240   -0.366  1.00 28.68 ? 49  HIS   A CA  1 
ATOM   123  C  C   . HIS   A 1 15  ? 26.630  6.051   0.335   1.00 24.22 ? 49  HIS   A C   1 
ATOM   124  O  O   . HIS   A 1 15  ? 25.911  6.824   -0.295  1.00 24.32 ? 49  HIS   A O   1 
ATOM   125  C  CB  . HIS   A 1 15  ? 29.082  5.441   0.283   1.00 28.16 ? 49  HIS   A CB  1 
ATOM   126  C  CG  . HIS   A 1 15  ? 29.549  6.857   0.280   1.00 28.86 ? 49  HIS   A CG  1 
ATOM   127  N  ND1 . HIS   A 1 15  ? 30.199  7.422   -0.795  1.00 34.03 ? 49  HIS   A ND1 1 
ATOM   128  C  CD2 . HIS   A 1 15  ? 29.443  7.839   1.210   1.00 33.30 ? 49  HIS   A CD2 1 
ATOM   129  C  CE1 . HIS   A 1 15  ? 30.473  8.690   -0.530  1.00 32.40 ? 49  HIS   A CE1 1 
ATOM   130  N  NE2 . HIS   A 1 15  ? 30.026  8.969   0.680   1.00 26.08 ? 49  HIS   A NE2 1 
ATOM   131  N  N   . ILE   A 1 16  ? 26.517  5.850   1.651   1.00 26.71 ? 50  ILE   A N   1 
ATOM   132  C  CA  . ILE   A 1 16  ? 25.665  6.656   2.529   1.00 23.01 ? 50  ILE   A CA  1 
ATOM   133  C  C   . ILE   A 1 16  ? 26.504  7.140   3.713   1.00 24.01 ? 50  ILE   A C   1 
ATOM   134  O  O   . ILE   A 1 16  ? 27.246  6.358   4.319   1.00 24.02 ? 50  ILE   A O   1 
ATOM   135  C  CB  . ILE   A 1 16  ? 24.443  5.863   3.034   1.00 22.18 ? 50  ILE   A CB  1 
ATOM   136  C  CG1 . ILE   A 1 16  ? 23.544  5.414   1.865   1.00 20.21 ? 50  ILE   A CG1 1 
ATOM   137  C  CG2 . ILE   A 1 16  ? 23.697  6.657   4.115   1.00 18.59 ? 50  ILE   A CG2 1 
ATOM   138  C  CD1 . ILE   A 1 16  ? 22.480  6.407   1.433   1.00 18.72 ? 50  ILE   A CD1 1 
ATOM   139  N  N   . GLU   A 1 17  ? 26.399  8.423   4.042   1.00 26.29 ? 51  GLU   A N   1 
ATOM   140  C  CA  . GLU   A 1 17  ? 27.069  8.970   5.216   1.00 25.88 ? 51  GLU   A CA  1 
ATOM   141  C  C   . GLU   A 1 17  ? 26.061  9.264   6.312   1.00 24.25 ? 51  GLU   A C   1 
ATOM   142  O  O   . GLU   A 1 17  ? 25.085  9.991   6.089   1.00 24.92 ? 51  GLU   A O   1 
ATOM   143  C  CB  . GLU   A 1 17  ? 27.854  10.256  4.914   1.00 30.52 ? 51  GLU   A CB  1 
ATOM   144  C  CG  . GLU   A 1 17  ? 28.956  10.506  5.967   1.00 26.57 ? 51  GLU   A CG  1 
ATOM   145  C  CD  . GLU   A 1 17  ? 29.795  11.722  5.716   1.00 28.38 ? 51  GLU   A CD  1 
ATOM   146  O  OE1 . GLU   A 1 17  ? 29.905  12.181  4.562   1.00 35.16 ? 51  GLU   A OE1 1 
ATOM   147  O  OE2 . GLU   A 1 17  ? 30.386  12.216  6.686   1.00 34.57 ? 51  GLU   A OE2 1 
ATOM   148  N  N   . PHE   A 1 18  ? 26.327  8.706   7.491   1.00 25.42 ? 52  PHE   A N   1 
ATOM   149  C  CA  . PHE   A 1 18  ? 25.699  9.087   8.745   1.00 22.42 ? 52  PHE   A CA  1 
ATOM   150  C  C   . PHE   A 1 18  ? 26.622  10.050  9.468   1.00 22.57 ? 52  PHE   A C   1 
ATOM   151  O  O   . PHE   A 1 18  ? 27.841  9.877   9.462   1.00 23.28 ? 52  PHE   A O   1 
ATOM   152  C  CB  . PHE   A 1 18  ? 25.440  7.868   9.652   1.00 27.94 ? 52  PHE   A CB  1 
ATOM   153  C  CG  . PHE   A 1 18  ? 24.619  6.758   9.008   1.00 18.26 ? 52  PHE   A CG  1 
ATOM   154  C  CD1 . PHE   A 1 18  ? 23.297  6.566   9.364   1.00 15.34 ? 52  PHE   A CD1 1 
ATOM   155  C  CD2 . PHE   A 1 18  ? 25.184  5.902   8.078   1.00 18.10 ? 52  PHE   A CD2 1 
ATOM   156  C  CE1 . PHE   A 1 18  ? 22.542  5.555   8.785   1.00 20.36 ? 52  PHE   A CE1 1 
ATOM   157  C  CE2 . PHE   A 1 18  ? 24.435  4.881   7.487   1.00 21.95 ? 52  PHE   A CE2 1 
ATOM   158  C  CZ  . PHE   A 1 18  ? 23.113  4.706   7.837   1.00 19.93 ? 52  PHE   A CZ  1 
ATOM   159  N  N   . TRP   A 1 19  ? 26.042  11.072  10.080  1.00 29.12 ? 53  TRP   A N   1 
ATOM   160  C  CA  . TRP   A 1 19  ? 26.766  11.938  11.001  1.00 25.58 ? 53  TRP   A CA  1 
ATOM   161  C  C   . TRP   A 1 19  ? 26.354  11.538  12.408  1.00 21.09 ? 53  TRP   A C   1 
ATOM   162  O  O   . TRP   A 1 19  ? 25.162  11.394  12.687  1.00 19.71 ? 53  TRP   A O   1 
ATOM   163  C  CB  . TRP   A 1 19  ? 26.464  13.424  10.739  1.00 27.32 ? 53  TRP   A CB  1 
ATOM   164  C  CG  . TRP   A 1 19  ? 27.396  14.091  9.736   1.00 24.28 ? 53  TRP   A CG  1 
ATOM   165  C  CD1 . TRP   A 1 19  ? 28.449  13.517  9.092   1.00 24.10 ? 53  TRP   A CD1 1 
ATOM   166  C  CD2 . TRP   A 1 19  ? 27.342  15.449  9.274   1.00 26.49 ? 53  TRP   A CD2 1 
ATOM   167  N  NE1 . TRP   A 1 19  ? 29.053  14.422  8.256   1.00 25.49 ? 53  TRP   A NE1 1 
ATOM   168  C  CE2 . TRP   A 1 19  ? 28.399  15.620  8.353   1.00 30.08 ? 53  TRP   A CE2 1 
ATOM   169  C  CE3 . TRP   A 1 19  ? 26.510  16.536  9.553   1.00 25.81 ? 53  TRP   A CE3 1 
ATOM   170  C  CZ2 . TRP   A 1 19  ? 28.645  16.836  7.712   1.00 24.37 ? 53  TRP   A CZ2 1 
ATOM   171  C  CZ3 . TRP   A 1 19  ? 26.747  17.727  8.914   1.00 25.97 ? 53  TRP   A CZ3 1 
ATOM   172  C  CH2 . TRP   A 1 19  ? 27.808  17.871  8.004   1.00 25.19 ? 53  TRP   A CH2 1 
ATOM   173  N  N   . CYS   A 1 20  ? 27.330  11.316  13.282  1.00 25.00 ? 54  CYS   A N   1 
ATOM   174  C  CA  . CYS   A 1 20  ? 27.007  10.908  14.643  1.00 26.50 ? 54  CYS   A CA  1 
ATOM   175  C  C   . CYS   A 1 20  ? 27.848  11.669  15.651  1.00 28.40 ? 54  CYS   A C   1 
ATOM   176  O  O   . CYS   A 1 20  ? 28.806  12.371  15.308  1.00 26.83 ? 54  CYS   A O   1 
ATOM   177  C  CB  . CYS   A 1 20  ? 27.197  9.396   14.879  1.00 27.63 ? 54  CYS   A CB  1 
ATOM   178  S  SG  . CYS   A 1 20  ? 27.757  8.411   13.481  1.00 31.98 ? 54  CYS   A SG  1 
ATOM   179  N  N   . GLY   A 1 21  ? 27.450  11.517  16.916  1.00 26.33 ? 55  GLY   A N   1 
ATOM   180  C  CA  . GLY   A 1 21  ? 28.264  11.917  18.036  1.00 21.39 ? 55  GLY   A CA  1 
ATOM   181  C  C   . GLY   A 1 21  ? 29.509  11.072  18.117  1.00 26.34 ? 55  GLY   A C   1 
ATOM   182  O  O   . GLY   A 1 21  ? 30.624  11.609  18.131  1.00 30.70 ? 55  GLY   A O   1 
ATOM   183  N  N   . ASP   A 1 22  ? 29.349  9.745   18.157  1.00 27.57 ? 56  ASP   A N   1 
ATOM   184  C  CA  . ASP   A 1 22  ? 30.494  8.843   18.271  1.00 23.35 ? 56  ASP   A CA  1 
ATOM   185  C  C   . ASP   A 1 22  ? 30.507  7.850   17.113  1.00 20.35 ? 56  ASP   A C   1 
ATOM   186  O  O   . ASP   A 1 22  ? 29.721  6.894   17.095  1.00 21.21 ? 56  ASP   A O   1 
ATOM   187  C  CB  . ASP   A 1 22  ? 30.497  8.113   19.609  1.00 15.88 ? 56  ASP   A CB  1 
ATOM   188  C  CG  . ASP   A 1 22  ? 31.790  7.367   19.829  1.00 21.99 ? 56  ASP   A CG  1 
ATOM   189  O  OD1 . ASP   A 1 22  ? 31.795  6.131   19.732  1.00 26.25 ? 56  ASP   A OD1 1 
ATOM   190  O  OD2 . ASP   A 1 22  ? 32.834  8.009   20.045  1.00 23.83 ? 56  ASP   A OD2 1 
ATOM   191  N  N   . ALA   A 1 23  ? 31.433  8.051   16.172  1.00 21.15 ? 57  ALA   A N   1 
ATOM   192  C  CA  . ALA   A 1 23  ? 31.485  7.193   14.988  1.00 22.73 ? 57  ALA   A CA  1 
ATOM   193  C  C   . ALA   A 1 23  ? 31.708  5.743   15.380  1.00 19.54 ? 57  ALA   A C   1 
ATOM   194  O  O   . ALA   A 1 23  ? 30.972  4.855   14.945  1.00 18.58 ? 57  ALA   A O   1 
ATOM   195  C  CB  . ALA   A 1 23  ? 32.580  7.663   14.031  1.00 20.38 ? 57  ALA   A CB  1 
ATOM   196  N  N   . THR   A 1 24  ? 32.690  5.508   16.251  1.00 21.92 ? 58  THR   A N   1 
ATOM   197  C  CA  . THR   A 1 24  ? 33.111  4.161   16.617  1.00 20.93 ? 58  THR   A CA  1 
ATOM   198  C  C   . THR   A 1 24  ? 31.936  3.280   16.994  1.00 17.53 ? 58  THR   A C   1 
ATOM   199  O  O   . THR   A 1 24  ? 31.764  2.196   16.436  1.00 23.28 ? 58  THR   A O   1 
ATOM   200  C  CB  . THR   A 1 24  ? 34.109  4.221   17.773  1.00 20.84 ? 58  THR   A CB  1 
ATOM   201  O  OG1 . THR   A 1 24  ? 35.389  4.648   17.283  1.00 25.01 ? 58  THR   A OG1 1 
ATOM   202  C  CG2 . THR   A 1 24  ? 34.240  2.871   18.398  1.00 16.53 ? 58  THR   A CG2 1 
ATOM   203  N  N   . ASN   A 1 25  ? 31.102  3.745   17.921  1.00 17.79 ? 59  ASN   A N   1 
ATOM   204  C  CA  . ASN   A 1 25  ? 30.066  2.901   18.495  1.00 16.14 ? 59  ASN   A CA  1 
ATOM   205  C  C   . ASN   A 1 25  ? 28.922  2.660   17.537  1.00 19.97 ? 59  ASN   A C   1 
ATOM   206  O  O   . ASN   A 1 25  ? 28.301  1.597   17.585  1.00 24.86 ? 59  ASN   A O   1 
ATOM   207  C  CB  . ASN   A 1 25  ? 29.524  3.523   19.778  1.00 18.65 ? 59  ASN   A CB  1 
ATOM   208  C  CG  . ASN   A 1 25  ? 30.290  3.091   20.996  1.00 19.96 ? 59  ASN   A CG  1 
ATOM   209  O  OD1 . ASN   A 1 25  ? 29.885  2.163   21.706  1.00 20.77 ? 59  ASN   A OD1 1 
ATOM   210  N  ND2 . ASN   A 1 25  ? 31.418  3.741   21.237  1.00 16.52 ? 59  ASN   A ND2 1 
ATOM   211  N  N   . VAL   A 1 26  ? 28.603  3.629   16.685  1.00 22.33 ? 60  VAL   A N   1 
ATOM   212  C  CA  . VAL   A 1 26  ? 27.548  3.385   15.716  1.00 21.38 ? 60  VAL   A CA  1 
ATOM   213  C  C   . VAL   A 1 26  ? 27.990  2.319   14.737  1.00 21.03 ? 60  VAL   A C   1 
ATOM   214  O  O   . VAL   A 1 26  ? 27.188  1.484   14.303  1.00 21.99 ? 60  VAL   A O   1 
ATOM   215  C  CB  . VAL   A 1 26  ? 27.150  4.675   14.976  1.00 21.98 ? 60  VAL   A CB  1 
ATOM   216  C  CG1 . VAL   A 1 26  ? 25.982  4.365   14.059  1.00 17.72 ? 60  VAL   A CG1 1 
ATOM   217  C  CG2 . VAL   A 1 26  ? 26.771  5.802   15.959  1.00 21.08 ? 60  VAL   A CG2 1 
ATOM   218  N  N   . ALA   A 1 27  ? 29.270  2.338   14.364  1.00 17.94 ? 61  ALA   A N   1 
ATOM   219  C  CA  . ALA   A 1 27  ? 29.712  1.495   13.266  1.00 18.50 ? 61  ALA   A CA  1 
ATOM   220  C  C   . ALA   A 1 27  ? 29.820  0.049   13.728  1.00 22.57 ? 61  ALA   A C   1 
ATOM   221  O  O   . ALA   A 1 27  ? 29.477  -0.882  12.990  1.00 20.53 ? 61  ALA   A O   1 
ATOM   222  C  CB  . ALA   A 1 27  ? 31.041  2.007   12.714  1.00 14.83 ? 61  ALA   A CB  1 
ATOM   223  N  N   . ARG   A 1 28  ? 30.259  -0.145  14.963  1.00 18.83 ? 62  ARG   A N   1 
ATOM   224  C  CA  . ARG   A 1 28  ? 30.317  -1.486  15.497  1.00 17.78 ? 62  ARG   A CA  1 
ATOM   225  C  C   . ARG   A 1 28  ? 28.928  -2.030  15.774  1.00 18.31 ? 62  ARG   A C   1 
ATOM   226  O  O   . ARG   A 1 28  ? 28.688  -3.221  15.579  1.00 20.67 ? 62  ARG   A O   1 
ATOM   227  C  CB  . ARG   A 1 28  ? 31.200  -1.499  16.739  1.00 19.40 ? 62  ARG   A CB  1 
ATOM   228  C  CG  . ARG   A 1 28  ? 32.631  -1.469  16.307  1.00 20.94 ? 62  ARG   A CG  1 
ATOM   229  C  CD  . ARG   A 1 28  ? 33.580  -1.358  17.413  1.00 18.05 ? 62  ARG   A CD  1 
ATOM   230  N  NE  . ARG   A 1 28  ? 34.908  -1.230  16.847  1.00 18.04 ? 62  ARG   A NE  1 
ATOM   231  C  CZ  . ARG   A 1 28  ? 35.954  -1.997  17.124  1.00 20.77 ? 62  ARG   A CZ  1 
ATOM   232  N  NH1 . ARG   A 1 28  ? 37.101  -1.745  16.511  1.00 24.74 ? 62  ARG   A NH1 1 
ATOM   233  N  NH2 . ARG   A 1 28  ? 35.878  -2.984  18.021  1.00 21.98 ? 62  ARG   A NH2 1 
ATOM   234  N  N   . ARG   A 1 29  ? 27.994  -1.189  16.209  1.00 15.46 ? 63  ARG   A N   1 
ATOM   235  C  CA  . ARG   A 1 29  ? 26.626  -1.670  16.313  1.00 17.79 ? 63  ARG   A CA  1 
ATOM   236  C  C   . ARG   A 1 29  ? 26.094  -2.094  14.939  1.00 20.12 ? 63  ARG   A C   1 
ATOM   237  O  O   . ARG   A 1 29  ? 25.528  -3.183  14.800  1.00 20.90 ? 63  ARG   A O   1 
ATOM   238  C  CB  . ARG   A 1 29  ? 25.738  -0.610  16.973  1.00 17.61 ? 63  ARG   A CB  1 
ATOM   239  C  CG  . ARG   A 1 29  ? 24.314  -1.073  17.367  1.00 17.86 ? 63  ARG   A CG  1 
ATOM   240  C  CD  . ARG   A 1 29  ? 23.369  -1.138  16.149  1.00 18.75 ? 63  ARG   A CD  1 
ATOM   241  N  NE  . ARG   A 1 29  ? 22.067  -1.684  16.489  1.00 19.57 ? 63  ARG   A NE  1 
ATOM   242  C  CZ  . ARG   A 1 29  ? 20.980  -0.954  16.689  1.00 20.84 ? 63  ARG   A CZ  1 
ATOM   243  N  NH1 . ARG   A 1 29  ? 19.825  -1.543  17.005  1.00 19.03 ? 63  ARG   A NH1 1 
ATOM   244  N  NH2 . ARG   A 1 29  ? 21.051  0.367   16.557  1.00 18.41 ? 63  ARG   A NH2 1 
ATOM   245  N  N   . PHE   A 1 30  ? 26.282  -1.253  13.910  1.00 17.73 ? 64  PHE   A N   1 
ATOM   246  C  CA  . PHE   A 1 30  ? 25.721  -1.529  12.582  1.00 17.39 ? 64  PHE   A CA  1 
ATOM   247  C  C   . PHE   A 1 30  ? 26.415  -2.709  11.916  1.00 20.39 ? 64  PHE   A C   1 
ATOM   248  O  O   . PHE   A 1 30  ? 25.789  -3.473  11.177  1.00 21.34 ? 64  PHE   A O   1 
ATOM   249  C  CB  . PHE   A 1 30  ? 25.857  -0.298  11.677  1.00 20.32 ? 64  PHE   A CB  1 
ATOM   250  C  CG  . PHE   A 1 30  ? 24.735  0.705   11.805  1.00 20.37 ? 64  PHE   A CG  1 
ATOM   251  C  CD1 . PHE   A 1 30  ? 24.479  1.347   13.014  1.00 18.72 ? 64  PHE   A CD1 1 
ATOM   252  C  CD2 . PHE   A 1 30  ? 23.971  1.048   10.696  1.00 21.62 ? 64  PHE   A CD2 1 
ATOM   253  C  CE1 . PHE   A 1 30  ? 23.449  2.281   13.131  1.00 19.66 ? 64  PHE   A CE1 1 
ATOM   254  C  CE2 . PHE   A 1 30  ? 22.941  1.998   10.792  1.00 24.04 ? 64  PHE   A CE2 1 
ATOM   255  C  CZ  . PHE   A 1 30  ? 22.676  2.617   12.016  1.00 21.19 ? 64  PHE   A CZ  1 
ATOM   256  N  N   . SER   A 1 31  ? 27.725  -2.829  12.116  1.00 22.86 ? 65  SER   A N   1 
ATOM   257  C  CA  . SER   A 1 31  ? 28.480  -3.932  11.543  1.00 21.82 ? 65  SER   A CA  1 
ATOM   258  C  C   . SER   A 1 31  ? 27.901  -5.262  12.000  1.00 25.95 ? 65  SER   A C   1 
ATOM   259  O  O   . SER   A 1 31  ? 27.531  -6.121  11.182  1.00 22.69 ? 65  SER   A O   1 
ATOM   260  C  CB  . SER   A 1 31  ? 29.945  -3.792  11.957  1.00 17.84 ? 65  SER   A CB  1 
ATOM   261  O  OG  . SER   A 1 31  ? 30.718  -4.885  11.534  1.00 23.05 ? 65  SER   A OG  1 
ATOM   262  N  N   . TRP   A 1 32  ? 27.772  -5.416  13.319  1.00 25.13 ? 66  TRP   A N   1 
ATOM   263  C  CA  . TRP   A 1 32  ? 27.222  -6.622  13.928  1.00 20.83 ? 66  TRP   A CA  1 
ATOM   264  C  C   . TRP   A 1 32  ? 25.748  -6.798  13.593  1.00 21.34 ? 66  TRP   A C   1 
ATOM   265  O  O   . TRP   A 1 32  ? 25.315  -7.899  13.245  1.00 28.26 ? 66  TRP   A O   1 
ATOM   266  C  CB  . TRP   A 1 32  ? 27.445  -6.548  15.440  1.00 21.35 ? 66  TRP   A CB  1 
ATOM   267  C  CG  . TRP   A 1 32  ? 26.885  -7.631  16.242  1.00 19.95 ? 66  TRP   A CG  1 
ATOM   268  C  CD1 . TRP   A 1 32  ? 25.999  -7.505  17.271  1.00 22.90 ? 66  TRP   A CD1 1 
ATOM   269  C  CD2 . TRP   A 1 32  ? 27.175  -9.024  16.124  1.00 21.40 ? 66  TRP   A CD2 1 
ATOM   270  N  NE1 . TRP   A 1 32  ? 25.725  -8.731  17.806  1.00 25.66 ? 66  TRP   A NE1 1 
ATOM   271  C  CE2 . TRP   A 1 32  ? 26.414  -9.688  17.102  1.00 22.36 ? 66  TRP   A CE2 1 
ATOM   272  C  CE3 . TRP   A 1 32  ? 27.987  -9.781  15.266  1.00 21.98 ? 66  TRP   A CE3 1 
ATOM   273  C  CZ2 . TRP   A 1 32  ? 26.445  -11.073 17.258  1.00 21.47 ? 66  TRP   A CZ2 1 
ATOM   274  C  CZ3 . TRP   A 1 32  ? 28.032  -11.149 15.424  1.00 19.47 ? 66  TRP   A CZ3 1 
ATOM   275  C  CH2 . TRP   A 1 32  ? 27.270  -11.786 16.422  1.00 21.66 ? 66  TRP   A CH2 1 
ATOM   276  N  N   . GLY   A 1 33  ? 24.956  -5.734  13.667  1.00 18.23 ? 67  GLY   A N   1 
ATOM   277  C  CA  . GLY   A 1 33  ? 23.536  -5.912  13.426  1.00 20.22 ? 67  GLY   A CA  1 
ATOM   278  C  C   . GLY   A 1 33  ? 23.180  -6.213  11.983  1.00 24.00 ? 67  GLY   A C   1 
ATOM   279  O  O   . GLY   A 1 33  ? 22.123  -6.803  11.721  1.00 21.56 ? 67  GLY   A O   1 
ATOM   280  N  N   . LEU   A 1 34  ? 24.040  -5.825  11.040  1.00 21.66 ? 68  LEU   A N   1 
ATOM   281  C  CA  . LEU   A 1 34  ? 23.723  -5.921  9.625   1.00 21.95 ? 68  LEU   A CA  1 
ATOM   282  C  C   . LEU   A 1 34  ? 24.609  -6.882  8.847   1.00 24.62 ? 68  LEU   A C   1 
ATOM   283  O  O   . LEU   A 1 34  ? 24.202  -7.333  7.771   1.00 20.90 ? 68  LEU   A O   1 
ATOM   284  C  CB  . LEU   A 1 34  ? 23.812  -4.537  8.967   1.00 20.33 ? 68  LEU   A CB  1 
ATOM   285  C  CG  . LEU   A 1 34  ? 22.622  -3.619  9.208   1.00 23.14 ? 68  LEU   A CG  1 
ATOM   286  C  CD1 . LEU   A 1 34  ? 23.047  -2.153  9.005   1.00 23.14 ? 68  LEU   A CD1 1 
ATOM   287  C  CD2 . LEU   A 1 34  ? 21.417  -3.995  8.292   1.00 17.30 ? 68  LEU   A CD2 1 
ATOM   288  N  N   . GLY   A 1 35  ? 25.797  -7.201  9.345   1.00 23.08 ? 69  GLY   A N   1 
ATOM   289  C  CA  . GLY   A 1 35  ? 26.655  -8.127  8.650   1.00 22.08 ? 69  GLY   A CA  1 
ATOM   290  C  C   . GLY   A 1 35  ? 27.579  -7.422  7.690   1.00 24.30 ? 69  GLY   A C   1 
ATOM   291  O  O   . GLY   A 1 35  ? 27.801  -7.910  6.577   1.00 28.94 ? 69  GLY   A O   1 
ATOM   292  N  N   . MET   A 1 36  ? 28.134  -6.283  8.101   1.00 22.88 ? 70  MET   A N   1 
ATOM   293  C  CA  . MET   A 1 36  ? 28.962  -5.467  7.224   1.00 24.21 ? 70  MET   A CA  1 
ATOM   294  C  C   . MET   A 1 36  ? 30.406  -5.447  7.722   1.00 25.51 ? 70  MET   A C   1 
ATOM   295  O  O   . MET   A 1 36  ? 30.649  -5.438  8.933   1.00 27.65 ? 70  MET   A O   1 
ATOM   296  C  CB  . MET   A 1 36  ? 28.371  -4.054  7.118   1.00 24.29 ? 70  MET   A CB  1 
ATOM   297  C  CG  . MET   A 1 36  ? 26.988  -4.070  6.454   1.00 23.39 ? 70  MET   A CG  1 
ATOM   298  S  SD  . MET   A 1 36  ? 26.117  -2.501  6.330   1.00 29.15 ? 70  MET   A SD  1 
ATOM   299  C  CE  . MET   A 1 36  ? 27.128  -1.660  5.090   1.00 25.57 ? 70  MET   A CE  1 
ATOM   300  N  N   . ARG   A 1 37  ? 31.353  -5.472  6.776   1.00 21.79 ? 71  ARG   A N   1 
ATOM   301  C  CA  . ARG   A 1 37  ? 32.785  -5.531  7.052   1.00 22.36 ? 71  ARG   A CA  1 
ATOM   302  C  C   . ARG   A 1 37  ? 33.342  -4.159  7.410   1.00 32.90 ? 71  ARG   A C   1 
ATOM   303  O  O   . ARG   A 1 37  ? 32.998  -3.150  6.786   1.00 35.48 ? 71  ARG   A O   1 
ATOM   304  C  CB  . ARG   A 1 37  ? 33.544  -6.004  5.820   1.00 22.94 ? 71  ARG   A CB  1 
ATOM   305  C  CG  . ARG   A 1 37  ? 32.865  -7.126  5.071   1.00 43.28 ? 71  ARG   A CG  1 
ATOM   306  C  CD  . ARG   A 1 37  ? 33.837  -8.033  4.414   1.00 46.45 ? 71  ARG   A CD  1 
ATOM   307  N  NE  . ARG   A 1 37  ? 33.349  -9.406  4.291   1.00 54.24 ? 71  ARG   A NE  1 
ATOM   308  C  CZ  . ARG   A 1 37  ? 33.510  -10.210 3.255   1.00 49.25 ? 71  ARG   A CZ  1 
ATOM   309  N  NH1 . ARG   A 1 37  ? 33.010  -11.447 3.309   1.00 54.68 ? 71  ARG   A NH1 1 
ATOM   310  N  NH2 . ARG   A 1 37  ? 34.192  -9.793  2.208   1.00 58.78 ? 71  ARG   A NH2 1 
ATOM   311  N  N   . PHE   A 1 38  ? 34.289  -4.150  8.342   1.00 31.76 ? 72  PHE   A N   1 
ATOM   312  C  CA  . PHE   A 1 38  ? 35.120  -2.993  8.677   1.00 34.62 ? 72  PHE   A CA  1 
ATOM   313  C  C   . PHE   A 1 38  ? 36.250  -2.919  7.646   1.00 35.19 ? 72  PHE   A C   1 
ATOM   314  O  O   . PHE   A 1 38  ? 37.206  -3.692  7.700   1.00 36.48 ? 72  PHE   A O   1 
ATOM   315  C  CB  . PHE   A 1 38  ? 35.638  -3.184  10.096  1.00 36.04 ? 72  PHE   A CB  1 
ATOM   316  C  CG  . PHE   A 1 38  ? 36.263  -1.985  10.710  1.00 37.10 ? 72  PHE   A CG  1 
ATOM   317  C  CD1 . PHE   A 1 38  ? 35.932  -0.707  10.311  1.00 42.30 ? 72  PHE   A CD1 1 
ATOM   318  C  CD2 . PHE   A 1 38  ? 37.168  -2.145  11.755  1.00 45.53 ? 72  PHE   A CD2 1 
ATOM   319  C  CE1 . PHE   A 1 38  ? 36.519  0.406   10.937  1.00 37.20 ? 72  PHE   A CE1 1 
ATOM   320  C  CE2 . PHE   A 1 38  ? 37.759  -1.051  12.395  1.00 35.61 ? 72  PHE   A CE2 1 
ATOM   321  C  CZ  . PHE   A 1 38  ? 37.437  0.226   11.981  1.00 38.84 ? 72  PHE   A CZ  1 
ATOM   322  N  N   . SER   A 1 39  ? 36.152  -1.997  6.687   1.00 34.31 ? 73  SER   A N   1 
ATOM   323  C  CA  . SER   A 1 39  ? 37.007  -2.060  5.506   1.00 33.04 ? 73  SER   A CA  1 
ATOM   324  C  C   . SER   A 1 39  ? 37.862  -0.822  5.230   1.00 36.36 ? 73  SER   A C   1 
ATOM   325  O  O   . SER   A 1 39  ? 38.834  -0.943  4.474   1.00 40.87 ? 73  SER   A O   1 
ATOM   326  C  CB  . SER   A 1 39  ? 36.160  -2.354  4.259   1.00 33.50 ? 73  SER   A CB  1 
ATOM   327  O  OG  . SER   A 1 39  ? 35.214  -1.318  4.046   1.00 41.55 ? 73  SER   A OG  1 
ATOM   328  N  N   . ALA   A 1 40  ? 37.555  0.342   5.813   1.00 29.78 ? 74  ALA   A N   1 
ATOM   329  C  CA  . ALA   A 1 40  ? 38.374  1.529   5.592   1.00 27.42 ? 74  ALA   A CA  1 
ATOM   330  C  C   . ALA   A 1 40  ? 38.135  2.552   6.703   1.00 31.61 ? 74  ALA   A C   1 
ATOM   331  O  O   . ALA   A 1 40  ? 37.060  2.588   7.319   1.00 26.61 ? 74  ALA   A O   1 
ATOM   332  C  CB  . ALA   A 1 40  ? 38.089  2.146   4.225   1.00 22.24 ? 74  ALA   A CB  1 
ATOM   333  N  N   . LYS   A 1 41  ? 39.147  3.389   6.952   1.00 26.23 ? 75  LYS   A N   1 
ATOM   334  C  CA  . LYS   A 1 41  ? 39.051  4.334   8.057   1.00 29.21 ? 75  LYS   A CA  1 
ATOM   335  C  C   . LYS   A 1 41  ? 39.816  5.624   7.769   1.00 27.86 ? 75  LYS   A C   1 
ATOM   336  O  O   . LYS   A 1 41  ? 40.800  5.649   7.027   1.00 31.33 ? 75  LYS   A O   1 
ATOM   337  C  CB  . LYS   A 1 41  ? 39.572  3.720   9.360   1.00 26.09 ? 75  LYS   A CB  1 
ATOM   338  C  CG  . LYS   A 1 41  ? 40.998  3.260   9.233   1.00 30.80 ? 75  LYS   A CG  1 
ATOM   339  C  CD  . LYS   A 1 41  ? 41.648  3.109   10.584  1.00 36.10 ? 75  LYS   A CD  1 
ATOM   340  C  CE  . LYS   A 1 41  ? 43.087  2.664   10.435  1.00 38.85 ? 75  LYS   A CE  1 
ATOM   341  N  NZ  . LYS   A 1 41  ? 43.596  2.078   11.709  1.00 47.71 ? 75  LYS   A NZ  1 
ATOM   342  N  N   . SER   A 1 42  ? 39.364  6.697   8.404   1.00 24.24 ? 76  SER   A N   1 
ATOM   343  C  CA  . SER   A 1 42  ? 40.096  7.954   8.393   1.00 26.56 ? 76  SER   A CA  1 
ATOM   344  C  C   . SER   A 1 42  ? 39.921  8.590   9.765   1.00 24.26 ? 76  SER   A C   1 
ATOM   345  O  O   . SER   A 1 42  ? 38.792  8.888   10.166  1.00 22.27 ? 76  SER   A O   1 
ATOM   346  C  CB  . SER   A 1 42  ? 39.585  8.861   7.266   1.00 27.37 ? 76  SER   A CB  1 
ATOM   347  O  OG  . SER   A 1 42  ? 40.359  10.037  7.144   1.00 31.51 ? 76  SER   A OG  1 
ATOM   348  N  N   . ASP   A 1 43  ? 41.014  8.749   10.501  1.00 23.98 ? 77  ASP   A N   1 
ATOM   349  C  CA  . ASP   A 1 43  ? 40.935  9.200   11.893  1.00 26.60 ? 77  ASP   A CA  1 
ATOM   350  C  C   . ASP   A 1 43  ? 42.329  9.616   12.353  1.00 29.46 ? 77  ASP   A C   1 
ATOM   351  O  O   . ASP   A 1 43  ? 43.235  9.816   11.532  1.00 27.98 ? 77  ASP   A O   1 
ATOM   352  C  CB  . ASP   A 1 43  ? 40.328  8.125   12.806  1.00 20.96 ? 77  ASP   A CB  1 
ATOM   353  C  CG  . ASP   A 1 43  ? 41.159  6.835   12.871  1.00 25.25 ? 77  ASP   A CG  1 
ATOM   354  O  OD1 . ASP   A 1 43  ? 42.328  6.821   12.417  1.00 27.47 ? 77  ASP   A OD1 1 
ATOM   355  O  OD2 . ASP   A 1 43  ? 40.646  5.827   13.422  1.00 23.47 ? 77  ASP   A OD2 1 
ATOM   356  N  N   . LEU   A 1 44  ? 42.498  9.735   13.682  1.00 27.89 ? 78  LEU   A N   1 
ATOM   357  C  CA  . LEU   A 1 44  ? 43.788  10.134  14.247  1.00 27.57 ? 78  LEU   A CA  1 
ATOM   358  C  C   . LEU   A 1 44  ? 44.889  9.159   13.861  1.00 27.53 ? 78  LEU   A C   1 
ATOM   359  O  O   . LEU   A 1 44  ? 46.037  9.558   13.625  1.00 28.58 ? 78  LEU   A O   1 
ATOM   360  C  CB  . LEU   A 1 44  ? 43.694  10.220  15.766  1.00 25.64 ? 78  LEU   A CB  1 
ATOM   361  C  CG  . LEU   A 1 44  ? 42.706  11.183  16.404  1.00 27.06 ? 78  LEU   A CG  1 
ATOM   362  C  CD1 . LEU   A 1 44  ? 42.680  10.928  17.905  1.00 26.10 ? 78  LEU   A CD1 1 
ATOM   363  C  CD2 . LEU   A 1 44  ? 43.103  12.619  16.094  1.00 27.07 ? 78  LEU   A CD2 1 
ATOM   364  N  N   . SER   A 1 45  ? 44.561  7.871   13.811  1.00 26.05 ? 79  SER   A N   1 
ATOM   365  C  CA  . SER   A 1 45  ? 45.553  6.861   13.489  1.00 28.81 ? 79  SER   A CA  1 
ATOM   366  C  C   . SER   A 1 45  ? 46.054  6.973   12.058  1.00 32.29 ? 79  SER   A C   1 
ATOM   367  O  O   . SER   A 1 45  ? 47.106  6.408   11.744  1.00 36.22 ? 79  SER   A O   1 
ATOM   368  C  CB  . SER   A 1 45  ? 44.967  5.481   13.705  1.00 24.47 ? 79  SER   A CB  1 
ATOM   369  O  OG  . SER   A 1 45  ? 44.155  5.160   12.594  1.00 27.87 ? 79  SER   A OG  1 
ATOM   370  N  N   . THR   A 1 46  ? 45.314  7.657   11.182  1.00 28.16 ? 80  THR   A N   1 
ATOM   371  C  CA  . THR   A 1 46  ? 45.739  7.906   9.810   1.00 30.77 ? 80  THR   A CA  1 
ATOM   372  C  C   . THR   A 1 46  ? 45.964  9.394   9.545   1.00 29.21 ? 80  THR   A C   1 
ATOM   373  O  O   . THR   A 1 46  ? 45.992  9.818   8.392   1.00 33.90 ? 80  THR   A O   1 
ATOM   374  C  CB  . THR   A 1 46  ? 44.722  7.336   8.814   1.00 32.66 ? 80  THR   A CB  1 
ATOM   375  O  OG1 . THR   A 1 46  ? 43.662  8.280   8.611   1.00 35.16 ? 80  THR   A OG1 1 
ATOM   376  C  CG2 . THR   A 1 46  ? 44.112  6.058   9.340   1.00 35.58 ? 80  THR   A CG2 1 
ATOM   377  N  N   . GLY   A 1 47  ? 46.097  10.203  10.587  1.00 34.06 ? 81  GLY   A N   1 
ATOM   378  C  CA  . GLY   A 1 47  ? 46.431  11.601  10.426  1.00 32.56 ? 81  GLY   A CA  1 
ATOM   379  C  C   . GLY   A 1 47  ? 45.273  12.570  10.307  1.00 29.80 ? 81  GLY   A C   1 
ATOM   380  O  O   . GLY   A 1 47  ? 45.515  13.758  10.112  1.00 27.47 ? 81  GLY   A O   1 
ATOM   381  N  N   . ASN   A 1 48  ? 44.027  12.119  10.410  1.00 26.99 ? 82  ASN   A N   1 
ATOM   382  C  CA  . ASN   A 1 48  ? 42.906  13.044  10.350  1.00 24.51 ? 82  ASN   A CA  1 
ATOM   383  C  C   . ASN   A 1 48  ? 42.693  13.651  11.734  1.00 28.03 ? 82  ASN   A C   1 
ATOM   384  O  O   . ASN   A 1 48  ? 42.344  12.940  12.685  1.00 23.96 ? 82  ASN   A O   1 
ATOM   385  C  CB  . ASN   A 1 48  ? 41.653  12.326  9.852   1.00 27.88 ? 82  ASN   A CB  1 
ATOM   386  C  CG  . ASN   A 1 48  ? 40.538  13.277  9.490   1.00 24.56 ? 82  ASN   A CG  1 
ATOM   387  O  OD1 . ASN   A 1 48  ? 40.422  14.363  10.055  1.00 22.95 ? 82  ASN   A OD1 1 
ATOM   388  N  ND2 . ASN   A 1 48  ? 39.701  12.866  8.544   1.00 26.26 ? 82  ASN   A ND2 1 
ATOM   389  N  N   . MET   A 1 49  ? 42.914  14.964  11.845  1.00 25.03 ? 83  MET   A N   1 
ATOM   390  C  CA  . MET   A 1 49  ? 42.744  15.697  13.087  1.00 21.15 ? 83  MET   A CA  1 
ATOM   391  C  C   . MET   A 1 49  ? 41.362  16.286  13.223  1.00 21.19 ? 83  MET   A C   1 
ATOM   392  O  O   . MET   A 1 49  ? 41.061  16.908  14.244  1.00 20.88 ? 83  MET   A O   1 
ATOM   393  C  CB  . MET   A 1 49  ? 43.756  16.832  13.188  1.00 25.42 ? 83  MET   A CB  1 
ATOM   394  C  CG  . MET   A 1 49  ? 45.195  16.450  12.973  1.00 22.44 ? 83  MET   A CG  1 
ATOM   395  S  SD  . MET   A 1 49  ? 45.743  15.483  14.360  1.00 40.62 ? 83  MET   A SD  1 
ATOM   396  C  CE  . MET   A 1 49  ? 45.740  13.847  13.641  1.00 28.76 ? 83  MET   A CE  1 
ATOM   397  N  N   . VAL   A 1 50  ? 40.522  16.124  12.216  1.00 24.51 ? 84  VAL   A N   1 
ATOM   398  C  CA  . VAL   A 1 50  ? 39.285  16.886  12.169  1.00 24.76 ? 84  VAL   A CA  1 
ATOM   399  C  C   . VAL   A 1 50  ? 38.138  15.971  12.533  1.00 21.11 ? 84  VAL   A C   1 
ATOM   400  O  O   . VAL   A 1 50  ? 37.407  16.225  13.494  1.00 24.46 ? 84  VAL   A O   1 
ATOM   401  C  CB  . VAL   A 1 50  ? 39.062  17.527  10.783  1.00 24.05 ? 84  VAL   A CB  1 
ATOM   402  C  CG1 . VAL   A 1 50  ? 37.691  18.158  10.726  1.00 22.99 ? 84  VAL   A CG1 1 
ATOM   403  C  CG2 . VAL   A 1 50  ? 40.145  18.551  10.475  1.00 19.84 ? 84  VAL   A CG2 1 
ATOM   404  N  N   . HIS   A 1 51  ? 37.966  14.909  11.764  1.00 22.35 ? 85  HIS   A N   1 
ATOM   405  C  CA  . HIS   A 1 51  ? 36.858  13.998  11.973  1.00 23.40 ? 85  HIS   A CA  1 
ATOM   406  C  C   . HIS   A 1 51  ? 37.371  12.576  11.984  1.00 25.80 ? 85  HIS   A C   1 
ATOM   407  O  O   . HIS   A 1 51  ? 38.414  12.276  11.397  1.00 28.39 ? 85  HIS   A O   1 
ATOM   408  C  CB  . HIS   A 1 51  ? 35.776  14.143  10.900  1.00 23.57 ? 85  HIS   A CB  1 
ATOM   409  C  CG  . HIS   A 1 51  ? 36.257  13.878  9.506   1.00 29.34 ? 85  HIS   A CG  1 
ATOM   410  N  ND1 . HIS   A 1 51  ? 36.359  12.609  8.980   1.00 25.98 ? 85  HIS   A ND1 1 
ATOM   411  C  CD2 . HIS   A 1 51  ? 36.641  14.725  8.519   1.00 28.83 ? 85  HIS   A CD2 1 
ATOM   412  C  CE1 . HIS   A 1 51  ? 36.795  12.684  7.735   1.00 27.82 ? 85  HIS   A CE1 1 
ATOM   413  N  NE2 . HIS   A 1 51  ? 36.978  13.957  7.433   1.00 28.38 ? 85  HIS   A NE2 1 
ATOM   414  N  N   . ALA   A 1 52  ? 36.640  11.719  12.695  1.00 25.00 ? 86  ALA   A N   1 
ATOM   415  C  CA  . ALA   A 1 52  ? 36.741  10.276  12.562  1.00 22.57 ? 86  ALA   A CA  1 
ATOM   416  C  C   . ALA   A 1 52  ? 35.673  9.797   11.589  1.00 24.15 ? 86  ALA   A C   1 
ATOM   417  O  O   . ALA   A 1 52  ? 34.519  10.236  11.652  1.00 21.35 ? 86  ALA   A O   1 
ATOM   418  C  CB  . ALA   A 1 52  ? 36.563  9.581   13.909  1.00 22.12 ? 86  ALA   A CB  1 
ATOM   419  N  N   . SER   A 1 53  ? 36.062  8.886   10.701  1.00 22.33 ? 87  SER   A N   1 
ATOM   420  C  CA  . SER   A 1 53  ? 35.152  8.343   9.696   1.00 23.70 ? 87  SER   A CA  1 
ATOM   421  C  C   . SER   A 1 53  ? 35.477  6.872   9.457   1.00 23.75 ? 87  SER   A C   1 
ATOM   422  O  O   . SER   A 1 53  ? 36.589  6.546   9.029   1.00 26.50 ? 87  SER   A O   1 
ATOM   423  C  CB  . SER   A 1 53  ? 35.248  9.144   8.377   1.00 27.43 ? 87  SER   A CB  1 
ATOM   424  O  OG  . SER   A 1 53  ? 34.839  10.496  8.535   1.00 27.88 ? 87  SER   A OG  1 
ATOM   425  N  N   . TYR   A 1 54  ? 34.510  5.990   9.710   1.00 22.89 ? 88  TYR   A N   1 
ATOM   426  C  CA  . TYR   A 1 54  ? 34.676  4.549   9.522   1.00 24.34 ? 88  TYR   A CA  1 
ATOM   427  C  C   . TYR   A 1 54  ? 33.648  4.045   8.514   1.00 25.67 ? 88  TYR   A C   1 
ATOM   428  O  O   . TYR   A 1 54  ? 32.496  4.496   8.507   1.00 25.82 ? 88  TYR   A O   1 
ATOM   429  C  CB  . TYR   A 1 54  ? 34.548  3.774   10.855  1.00 19.44 ? 88  TYR   A CB  1 
ATOM   430  C  CG  . TYR   A 1 54  ? 35.493  4.298   11.901  1.00 20.98 ? 88  TYR   A CG  1 
ATOM   431  C  CD1 . TYR   A 1 54  ? 36.858  4.052   11.822  1.00 21.84 ? 88  TYR   A CD1 1 
ATOM   432  C  CD2 . TYR   A 1 54  ? 35.030  5.079   12.946  1.00 21.78 ? 88  TYR   A CD2 1 
ATOM   433  C  CE1 . TYR   A 1 54  ? 37.726  4.550   12.761  1.00 18.53 ? 88  TYR   A CE1 1 
ATOM   434  C  CE2 . TYR   A 1 54  ? 35.895  5.592   13.882  1.00 22.76 ? 88  TYR   A CE2 1 
ATOM   435  C  CZ  . TYR   A 1 54  ? 37.241  5.323   13.778  1.00 21.96 ? 88  TYR   A CZ  1 
ATOM   436  O  OH  . TYR   A 1 54  ? 38.100  5.823   14.719  1.00 31.66 ? 88  TYR   A OH  1 
ATOM   437  N  N   . LEU   A 1 55  ? 34.076  3.100   7.675   1.00 25.97 ? 89  LEU   A N   1 
ATOM   438  C  CA  . LEU   A 1 55  ? 33.323  2.648   6.513   1.00 21.33 ? 89  LEU   A CA  1 
ATOM   439  C  C   . LEU   A 1 55  ? 33.078  1.146   6.606   1.00 28.96 ? 89  LEU   A C   1 
ATOM   440  O  O   . LEU   A 1 55  ? 34.028  0.352   6.618   1.00 30.28 ? 89  LEU   A O   1 
ATOM   441  C  CB  . LEU   A 1 55  ? 34.080  2.994   5.236   1.00 21.38 ? 89  LEU   A CB  1 
ATOM   442  C  CG  . LEU   A 1 55  ? 33.467  2.559   3.911   1.00 29.82 ? 89  LEU   A CG  1 
ATOM   443  C  CD1 . LEU   A 1 55  ? 32.231  3.374   3.592   1.00 24.28 ? 89  LEU   A CD1 1 
ATOM   444  C  CD2 . LEU   A 1 55  ? 34.491  2.684   2.806   1.00 29.88 ? 89  LEU   A CD2 1 
ATOM   445  N  N   . LEU   A 1 56  ? 31.806  0.760   6.664   1.00 27.51 ? 90  LEU   A N   1 
ATOM   446  C  CA  . LEU   A 1 56  ? 31.405  -0.634  6.575   1.00 27.26 ? 90  LEU   A CA  1 
ATOM   447  C  C   . LEU   A 1 56  ? 30.939  -0.922  5.160   1.00 26.50 ? 90  LEU   A C   1 
ATOM   448  O  O   . LEU   A 1 56  ? 30.327  -0.066  4.515   1.00 23.84 ? 90  LEU   A O   1 
ATOM   449  C  CB  . LEU   A 1 56  ? 30.279  -0.973  7.555   1.00 25.32 ? 90  LEU   A CB  1 
ATOM   450  C  CG  . LEU   A 1 56  ? 30.308  -0.371  8.955   1.00 22.24 ? 90  LEU   A CG  1 
ATOM   451  C  CD1 . LEU   A 1 56  ? 29.076  -0.836  9.706   1.00 22.80 ? 90  LEU   A CD1 1 
ATOM   452  C  CD2 . LEU   A 1 56  ? 31.584  -0.745  9.690   1.00 22.58 ? 90  LEU   A CD2 1 
ATOM   453  N  N   . THR   A 1 57  ? 31.225  -2.138  4.684   1.00 24.76 ? 91  THR   A N   1 
ATOM   454  C  CA  . THR   A 1 57  ? 30.817  -2.545  3.347   1.00 22.27 ? 91  THR   A CA  1 
ATOM   455  C  C   . THR   A 1 57  ? 30.195  -3.929  3.394   1.00 25.98 ? 91  THR   A C   1 
ATOM   456  O  O   . THR   A 1 57  ? 30.639  -4.798  4.149   1.00 25.17 ? 91  THR   A O   1 
ATOM   457  C  CB  . THR   A 1 57  ? 31.987  -2.571  2.339   1.00 18.45 ? 91  THR   A CB  1 
ATOM   458  O  OG1 . THR   A 1 57  ? 32.963  -3.521  2.765   1.00 26.33 ? 91  THR   A OG1 1 
ATOM   459  C  CG2 . THR   A 1 57  ? 32.653  -1.213  2.207   1.00 21.93 ? 91  THR   A CG2 1 
ATOM   460  N  N   . SER   A 1 58  ? 29.169  -4.125  2.568   1.00 28.21 ? 92  SER   A N   1 
ATOM   461  C  CA  . SER   A 1 58  ? 28.644  -5.454  2.266   1.00 24.47 ? 92  SER   A CA  1 
ATOM   462  C  C   . SER   A 1 58  ? 28.319  -5.469  0.782   1.00 27.79 ? 92  SER   A C   1 
ATOM   463  O  O   . SER   A 1 58  ? 27.407  -4.757  0.346   1.00 33.02 ? 92  SER   A O   1 
ATOM   464  C  CB  . SER   A 1 58  ? 27.409  -5.787  3.107   1.00 29.65 ? 92  SER   A CB  1 
ATOM   465  O  OG  . SER   A 1 58  ? 27.038  -7.154  2.933   1.00 33.96 ? 92  SER   A OG  1 
ATOM   466  N  N   . GLY   A 1 59  ? 29.062  -6.262  0.007   1.00 27.36 ? 93  GLY   A N   1 
ATOM   467  C  CA  . GLY   A 1 59  ? 28.955  -6.190  -1.444  1.00 24.06 ? 93  GLY   A CA  1 
ATOM   468  C  C   . GLY   A 1 59  ? 29.285  -4.794  -1.962  1.00 25.87 ? 93  GLY   A C   1 
ATOM   469  O  O   . GLY   A 1 59  ? 30.391  -4.276  -1.764  1.00 25.26 ? 93  GLY   A O   1 
ATOM   470  N  N   . ASP   A 1 60  ? 28.314  -4.179  -2.641  1.00 26.05 ? 94  ASP   A N   1 
ATOM   471  C  CA  . ASP   A 1 60  ? 28.396  -2.809  -3.144  1.00 32.18 ? 94  ASP   A CA  1 
ATOM   472  C  C   . ASP   A 1 60  ? 27.824  -1.791  -2.170  1.00 30.42 ? 94  ASP   A C   1 
ATOM   473  O  O   . ASP   A 1 60  ? 27.936  -0.576  -2.412  1.00 26.83 ? 94  ASP   A O   1 
ATOM   474  C  CB  . ASP   A 1 60  ? 27.637  -2.655  -4.486  1.00 36.65 ? 94  ASP   A CB  1 
ATOM   475  C  CG  . ASP   A 1 60  ? 28.295  -3.399  -5.652  1.00 43.24 ? 94  ASP   A CG  1 
ATOM   476  O  OD1 . ASP   A 1 60  ? 29.533  -3.608  -5.635  1.00 48.27 ? 94  ASP   A OD1 1 
ATOM   477  O  OD2 . ASP   A 1 60  ? 27.561  -3.748  -6.607  1.00 46.87 ? 94  ASP   A OD2 1 
ATOM   478  N  N   . LEU   A 1 61  ? 27.159  -2.258  -1.114  1.00 30.76 ? 95  LEU   A N   1 
ATOM   479  C  CA  . LEU   A 1 61  ? 26.653  -1.350  -0.100  1.00 29.00 ? 95  LEU   A CA  1 
ATOM   480  C  C   . LEU   A 1 61  ? 27.829  -0.840  0.727   1.00 27.96 ? 95  LEU   A C   1 
ATOM   481  O  O   . LEU   A 1 61  ? 28.699  -1.615  1.155   1.00 22.90 ? 95  LEU   A O   1 
ATOM   482  C  CB  . LEU   A 1 61  ? 25.610  -2.043  0.781   1.00 24.83 ? 95  LEU   A CB  1 
ATOM   483  C  CG  . LEU   A 1 61  ? 25.009  -1.082  1.814   1.00 25.27 ? 95  LEU   A CG  1 
ATOM   484  C  CD1 . LEU   A 1 61  ? 24.375  0.094   1.094   1.00 18.74 ? 95  LEU   A CD1 1 
ATOM   485  C  CD2 . LEU   A 1 61  ? 24.025  -1.739  2.788   1.00 20.99 ? 95  LEU   A CD2 1 
ATOM   486  N  N   . ARG   A 1 62  ? 27.881  0.474   0.895   1.00 23.20 ? 96  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 62  ? 28.910  1.122   1.691   1.00 25.82 ? 96  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 62  ? 28.227  2.070   2.662   1.00 26.46 ? 96  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 62  ? 27.507  2.985   2.239   1.00 25.84 ? 96  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 62  ? 29.909  1.872   0.802   1.00 30.45 ? 96  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 62  ? 30.756  0.986   -0.116  1.00 26.17 ? 96  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 62  ? 31.429  1.812   -1.219  1.00 29.88 ? 96  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 62  ? 31.463  1.090   -2.492  1.00 34.78 ? 96  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 62  ? 31.428  1.671   -3.689  1.00 34.02 ? 96  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 62  ? 31.344  2.988   -3.784  1.00 33.11 ? 96  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 62  ? 31.458  0.935   -4.792  1.00 40.02 ? 96  ARG   A NH2 1 
ATOM   497  N  N   . PHE   A 1 63  ? 28.429  1.837   3.957   1.00 27.12 ? 97  PHE   A N   1 
ATOM   498  C  CA  . PHE   A 1 63  ? 27.974  2.750   4.998   1.00 22.31 ? 97  PHE   A CA  1 
ATOM   499  C  C   . PHE   A 1 63  ? 29.186  3.462   5.581   1.00 21.34 ? 97  PHE   A C   1 
ATOM   500  O  O   . PHE   A 1 63  ? 30.135  2.816   6.032   1.00 24.04 ? 97  PHE   A O   1 
ATOM   501  C  CB  . PHE   A 1 63  ? 27.201  2.008   6.085   1.00 21.40 ? 97  PHE   A CB  1 
ATOM   502  C  CG  . PHE   A 1 63  ? 25.757  1.788   5.756   1.00 23.22 ? 97  PHE   A CG  1 
ATOM   503  C  CD1 . PHE   A 1 63  ? 25.207  2.314   4.597   1.00 22.49 ? 97  PHE   A CD1 1 
ATOM   504  C  CD2 . PHE   A 1 63  ? 24.940  1.061   6.615   1.00 21.49 ? 97  PHE   A CD2 1 
ATOM   505  C  CE1 . PHE   A 1 63  ? 23.866  2.114   4.295   1.00 23.18 ? 97  PHE   A CE1 1 
ATOM   506  C  CE2 . PHE   A 1 63  ? 23.602  0.861   6.326   1.00 17.41 ? 97  PHE   A CE2 1 
ATOM   507  C  CZ  . PHE   A 1 63  ? 23.068  1.380   5.160   1.00 21.01 ? 97  PHE   A CZ  1 
ATOM   508  N  N   . LEU   A 1 64  ? 29.162  4.787   5.544   1.00 24.13 ? 98  LEU   A N   1 
ATOM   509  C  CA  . LEU   A 1 64  ? 30.177  5.617   6.178   1.00 20.58 ? 98  LEU   A CA  1 
ATOM   510  C  C   . LEU   A 1 64  ? 29.600  6.197   7.460   1.00 24.81 ? 98  LEU   A C   1 
ATOM   511  O  O   . LEU   A 1 64  ? 28.428  6.594   7.502   1.00 24.14 ? 98  LEU   A O   1 
ATOM   512  C  CB  . LEU   A 1 64  ? 30.630  6.743   5.251   1.00 19.19 ? 98  LEU   A CB  1 
ATOM   513  C  CG  . LEU   A 1 64  ? 31.779  7.617   5.758   1.00 26.03 ? 98  LEU   A CG  1 
ATOM   514  C  CD1 . LEU   A 1 64  ? 33.020  6.773   5.996   1.00 23.51 ? 98  LEU   A CD1 1 
ATOM   515  C  CD2 . LEU   A 1 64  ? 32.062  8.796   4.800   1.00 25.33 ? 98  LEU   A CD2 1 
ATOM   516  N  N   . PHE   A 1 65  ? 30.420  6.226   8.510   1.00 21.06 ? 99  PHE   A N   1 
ATOM   517  C  CA  . PHE   A 1 65  ? 30.010  6.759   9.804   1.00 21.06 ? 99  PHE   A CA  1 
ATOM   518  C  C   . PHE   A 1 65  ? 31.039  7.799   10.208  1.00 22.93 ? 99  PHE   A C   1 
ATOM   519  O  O   . PHE   A 1 65  ? 32.240  7.503   10.219  1.00 28.33 ? 99  PHE   A O   1 
ATOM   520  C  CB  . PHE   A 1 65  ? 29.874  5.629   10.836  1.00 20.21 ? 99  PHE   A CB  1 
ATOM   521  C  CG  . PHE   A 1 65  ? 28.838  4.622   10.452  1.00 18.86 ? 99  PHE   A CG  1 
ATOM   522  C  CD1 . PHE   A 1 65  ? 29.148  3.598   9.574   1.00 19.59 ? 99  PHE   A CD1 1 
ATOM   523  C  CD2 . PHE   A 1 65  ? 27.531  4.748   10.892  1.00 18.86 ? 99  PHE   A CD2 1 
ATOM   524  C  CE1 . PHE   A 1 65  ? 28.195  2.716   9.179   1.00 17.89 ? 99  PHE   A CE1 1 
ATOM   525  C  CE2 . PHE   A 1 65  ? 26.564  3.847   10.500  1.00 16.58 ? 99  PHE   A CE2 1 
ATOM   526  C  CZ  . PHE   A 1 65  ? 26.897  2.834   9.648   1.00 18.24 ? 99  PHE   A CZ  1 
ATOM   527  N  N   . THR   A 1 66  ? 30.582  9.021   10.491  1.00 17.37 ? 100 THR   A N   1 
ATOM   528  C  CA  . THR   A 1 66  ? 31.488  10.142  10.684  1.00 16.38 ? 100 THR   A CA  1 
ATOM   529  C  C   . THR   A 1 66  ? 31.068  10.975  11.897  1.00 20.98 ? 100 THR   A C   1 
ATOM   530  O  O   . THR   A 1 66  ? 29.874  11.208  12.130  1.00 19.22 ? 100 THR   A O   1 
ATOM   531  C  CB  . THR   A 1 66  ? 31.557  10.983  9.397   1.00 20.11 ? 100 THR   A CB  1 
ATOM   532  O  OG1 . THR   A 1 66  ? 32.145  10.213  8.328   1.00 17.77 ? 100 THR   A OG1 1 
ATOM   533  C  CG2 . THR   A 1 66  ? 32.349  12.286  9.620   1.00 24.23 ? 100 THR   A CG2 1 
ATOM   534  N  N   . ALA   A 1 67  ? 32.057  11.379  12.692  1.00 22.30 ? 101 ALA   A N   1 
ATOM   535  C  CA  . ALA   A 1 67  ? 31.874  12.176  13.899  1.00 24.89 ? 101 ALA   A CA  1 
ATOM   536  C  C   . ALA   A 1 67  ? 32.995  13.205  14.006  1.00 24.69 ? 101 ALA   A C   1 
ATOM   537  O  O   . ALA   A 1 67  ? 34.076  13.009  13.445  1.00 26.05 ? 101 ALA   A O   1 
ATOM   538  C  CB  . ALA   A 1 67  ? 31.856  11.301  15.159  1.00 20.34 ? 101 ALA   A CB  1 
ATOM   539  N  N   . PRO   A 1 68  ? 32.758  14.324  14.727  1.00 26.35 ? 102 PRO   A N   1 
ATOM   540  C  CA  . PRO   A 1 68  ? 33.798  15.361  14.851  1.00 28.34 ? 102 PRO   A CA  1 
ATOM   541  C  C   . PRO   A 1 68  ? 34.661  15.252  16.099  1.00 24.89 ? 102 PRO   A C   1 
ATOM   542  O  O   . PRO   A 1 68  ? 34.137  14.951  17.175  1.00 23.71 ? 102 PRO   A O   1 
ATOM   543  C  CB  . PRO   A 1 68  ? 32.971  16.650  14.893  1.00 31.59 ? 102 PRO   A CB  1 
ATOM   544  C  CG  . PRO   A 1 68  ? 31.731  16.247  15.631  1.00 26.46 ? 102 PRO   A CG  1 
ATOM   545  C  CD  . PRO   A 1 68  ? 31.454  14.813  15.210  1.00 30.42 ? 102 PRO   A CD  1 
ATOM   546  N  N   . TYR   A 1 69  ? 35.966  15.523  15.971  1.00 23.46 ? 103 TYR   A N   1 
ATOM   547  C  CA  . TYR   A 1 69  ? 36.869  15.702  17.108  1.00 23.44 ? 103 TYR   A CA  1 
ATOM   548  C  C   . TYR   A 1 69  ? 36.653  17.067  17.764  1.00 32.72 ? 103 TYR   A C   1 
ATOM   549  O  O   . TYR   A 1 69  ? 35.843  17.891  17.313  1.00 31.70 ? 103 TYR   A O   1 
ATOM   550  C  CB  . TYR   A 1 69  ? 38.327  15.581  16.668  1.00 21.65 ? 103 TYR   A CB  1 
ATOM   551  C  CG  . TYR   A 1 69  ? 38.715  14.203  16.184  1.00 24.54 ? 103 TYR   A CG  1 
ATOM   552  C  CD1 . TYR   A 1 69  ? 38.416  13.066  16.944  1.00 25.60 ? 103 TYR   A CD1 1 
ATOM   553  C  CD2 . TYR   A 1 69  ? 39.391  14.030  14.979  1.00 24.02 ? 103 TYR   A CD2 1 
ATOM   554  C  CE1 . TYR   A 1 69  ? 38.778  11.792  16.502  1.00 28.53 ? 103 TYR   A CE1 1 
ATOM   555  C  CE2 . TYR   A 1 69  ? 39.753  12.766  14.527  1.00 25.53 ? 103 TYR   A CE2 1 
ATOM   556  C  CZ  . TYR   A 1 69  ? 39.447  11.644  15.294  1.00 26.28 ? 103 TYR   A CZ  1 
ATOM   557  O  OH  . TYR   A 1 69  ? 39.810  10.383  14.858  1.00 24.51 ? 103 TYR   A OH  1 
ATOM   558  N  N   . SER   A 1 70  ? 37.395  17.318  18.844  1.00 30.68 ? 104 SER   A N   1 
ATOM   559  C  CA  . SER   A 1 70  ? 37.443  18.665  19.405  1.00 28.91 ? 104 SER   A CA  1 
ATOM   560  C  C   . SER   A 1 70  ? 38.078  19.598  18.382  1.00 29.97 ? 104 SER   A C   1 
ATOM   561  O  O   . SER   A 1 70  ? 39.120  19.255  17.800  1.00 32.23 ? 104 SER   A O   1 
ATOM   562  C  CB  . SER   A 1 70  ? 38.245  18.686  20.713  1.00 31.82 ? 104 SER   A CB  1 
ATOM   563  O  OG  . SER   A 1 70  ? 38.747  19.986  21.020  1.00 28.68 ? 104 SER   A OG  1 
ATOM   564  N  N   . PRO   A 1 71  ? 37.488  20.761  18.108  1.00 33.46 ? 105 PRO   A N   1 
ATOM   565  C  CA  . PRO   A 1 71  ? 38.109  21.645  17.113  1.00 28.54 ? 105 PRO   A CA  1 
ATOM   566  C  C   . PRO   A 1 71  ? 39.509  22.063  17.508  1.00 25.07 ? 105 PRO   A C   1 
ATOM   567  O  O   . PRO   A 1 71  ? 40.354  22.258  16.631  1.00 29.88 ? 105 PRO   A O   1 
ATOM   568  C  CB  . PRO   A 1 71  ? 37.131  22.822  17.042  1.00 18.61 ? 105 PRO   A CB  1 
ATOM   569  C  CG  . PRO   A 1 71  ? 35.820  22.217  17.375  1.00 20.22 ? 105 PRO   A CG  1 
ATOM   570  C  CD  . PRO   A 1 71  ? 36.150  21.244  18.491  1.00 31.16 ? 105 PRO   A CD  1 
ATOM   571  N  N   . SER   A 1 72  ? 39.802  22.128  18.807  1.00 25.45 ? 106 SER   A N   1 
ATOM   572  C  CA  . SER   A 1 72  ? 41.152  22.455  19.256  1.00 27.26 ? 106 SER   A CA  1 
ATOM   573  C  C   . SER   A 1 72  ? 42.215  21.664  18.501  1.00 31.37 ? 106 SER   A C   1 
ATOM   574  O  O   . SER   A 1 72  ? 43.330  22.154  18.314  1.00 35.77 ? 106 SER   A O   1 
ATOM   575  C  CB  . SER   A 1 72  ? 41.286  22.205  20.766  1.00 27.23 ? 106 SER   A CB  1 
ATOM   576  O  OG  . SER   A 1 72  ? 40.815  20.906  21.150  1.00 31.07 ? 106 SER   A OG  1 
ATOM   577  N  N   . LEU   A 1 73  ? 41.891  20.450  18.049  1.00 27.61 ? 107 LEU   A N   1 
ATOM   578  C  CA  . LEU   A 1 73  ? 42.900  19.613  17.417  1.00 26.05 ? 107 LEU   A CA  1 
ATOM   579  C  C   . LEU   A 1 73  ? 43.365  20.163  16.072  1.00 29.39 ? 107 LEU   A C   1 
ATOM   580  O  O   . LEU   A 1 73  ? 44.478  19.860  15.632  1.00 31.89 ? 107 LEU   A O   1 
ATOM   581  C  CB  . LEU   A 1 73  ? 42.351  18.212  17.211  1.00 28.99 ? 107 LEU   A CB  1 
ATOM   582  C  CG  . LEU   A 1 73  ? 41.942  17.351  18.388  1.00 27.13 ? 107 LEU   A CG  1 
ATOM   583  C  CD1 . LEU   A 1 73  ? 41.692  15.957  17.876  1.00 24.84 ? 107 LEU   A CD1 1 
ATOM   584  C  CD2 . LEU   A 1 73  ? 43.063  17.355  19.378  1.00 33.76 ? 107 LEU   A CD2 1 
ATOM   585  N  N   . SER   A 1 74  ? 42.529  20.929  15.383  1.00 27.07 ? 108 SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 42.849  21.350  14.026  1.00 32.59 ? 108 SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 42.710  22.861  13.874  1.00 38.40 ? 108 SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 42.342  23.362  12.806  1.00 41.26 ? 108 SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 41.973  20.606  13.016  1.00 33.82 ? 108 SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 40.597  20.721  13.344  1.00 29.71 ? 108 SER   A OG  1 
ATOM   591  N  N   . ALA   A 1 75  ? 43.030  23.600  14.939  1.00 44.37 ? 109 ALA   A N   1 
ATOM   592  C  CA  . ALA   A 1 75  ? 42.739  25.032  14.993  1.00 45.86 ? 109 ALA   A CA  1 
ATOM   593  C  C   . ALA   A 1 75  ? 43.591  25.843  14.019  1.00 51.28 ? 109 ALA   A C   1 
ATOM   594  O  O   . ALA   A 1 75  ? 43.114  26.841  13.468  1.00 56.38 ? 109 ALA   A O   1 
ATOM   595  C  CB  . ALA   A 1 75  ? 42.934  25.545  16.419  1.00 40.91 ? 109 ALA   A CB  1 
ATOM   596  N  N   . GLY   A 1 76  ? 44.843  25.452  13.801  1.00 51.23 ? 110 GLY   A N   1 
ATOM   597  C  CA  . GLY   A 1 76  ? 45.671  26.132  12.825  1.00 44.14 ? 110 GLY   A CA  1 
ATOM   598  C  C   . GLY   A 1 76  ? 45.597  25.521  11.438  1.00 47.27 ? 110 GLY   A C   1 
ATOM   599  O  O   . GLY   A 1 76  ? 46.501  25.710  10.619  1.00 52.66 ? 110 GLY   A O   1 
ATOM   600  N  N   . GLU   A 1 77  ? 44.542  24.773  11.150  1.00 46.76 ? 111 GLU   A N   1 
ATOM   601  C  CA  . GLU   A 1 77  ? 44.348  24.226  9.817   1.00 46.49 ? 111 GLU   A CA  1 
ATOM   602  C  C   . GLU   A 1 77  ? 43.361  25.105  9.069   1.00 40.43 ? 111 GLU   A C   1 
ATOM   603  O  O   . GLU   A 1 77  ? 42.281  25.412  9.582   1.00 44.70 ? 111 GLU   A O   1 
ATOM   604  C  CB  . GLU   A 1 77  ? 43.860  22.775  9.862   1.00 38.49 ? 111 GLU   A CB  1 
ATOM   605  C  CG  . GLU   A 1 77  ? 44.929  21.797  10.316  1.00 38.03 ? 111 GLU   A CG  1 
ATOM   606  C  CD  . GLU   A 1 77  ? 44.422  20.362  10.438  1.00 35.92 ? 111 GLU   A CD  1 
ATOM   607  O  OE1 . GLU   A 1 77  ? 43.581  19.929  9.619   1.00 31.14 ? 111 GLU   A OE1 1 
ATOM   608  O  OE2 . GLU   A 1 77  ? 44.863  19.673  11.381  1.00 34.20 ? 111 GLU   A OE2 1 
ATOM   609  N  N   . ILE   A 1 78  ? 43.767  25.551  7.889   1.00 40.68 ? 112 ILE   A N   1 
ATOM   610  C  CA  . ILE   A 1 78  ? 42.882  26.194  6.942   1.00 39.60 ? 112 ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 78  ? 42.486  25.144  5.915   1.00 36.12 ? 112 ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 78  ? 43.050  24.056  5.867   1.00 39.41 ? 112 ILE   A O   1 
ATOM   613  C  CB  . ILE   A 1 78  ? 43.552  27.413  6.265   1.00 35.35 ? 112 ILE   A CB  1 
ATOM   614  C  CG1 . ILE   A 1 78  ? 44.893  26.976  5.662   1.00 31.48 ? 112 ILE   A CG1 1 
ATOM   615  C  CG2 . ILE   A 1 78  ? 43.700  28.561  7.261   1.00 28.30 ? 112 ILE   A CG2 1 
ATOM   616  C  CD1 . ILE   A 1 78  ? 45.464  27.909  4.676   1.00 33.83 ? 112 ILE   A CD1 1 
ATOM   617  N  N   . LYS   A 1 79  ? 41.510  25.468  5.068   1.00 35.86 ? 113 LYS   A N   1 
ATOM   618  C  CA  . LYS   A 1 79  ? 41.041  24.465  4.112   1.00 40.55 ? 113 LYS   A CA  1 
ATOM   619  C  C   . LYS   A 1 79  ? 42.148  23.963  3.182   1.00 39.17 ? 113 LYS   A C   1 
ATOM   620  O  O   . LYS   A 1 79  ? 42.161  22.753  2.889   1.00 36.80 ? 113 LYS   A O   1 
ATOM   621  C  CB  . LYS   A 1 79  ? 39.851  25.019  3.310   1.00 41.70 ? 113 LYS   A CB  1 
ATOM   622  C  CG  . LYS   A 1 79  ? 38.496  24.822  4.014   1.00 38.42 ? 113 LYS   A CG  1 
ATOM   623  C  CD  A LYS   A 1 79  ? 37.379  25.532  3.257   0.36 39.48 ? 113 LYS   A CD  1 
ATOM   624  C  CD  B LYS   A 1 79  ? 37.329  25.416  3.241   0.64 42.46 ? 113 LYS   A CD  1 
ATOM   625  C  CE  A LYS   A 1 79  ? 36.000  25.030  3.663   0.36 38.23 ? 113 LYS   A CE  1 
ATOM   626  C  CE  B LYS   A 1 79  ? 36.026  25.218  4.001   0.64 38.18 ? 113 LYS   A CE  1 
ATOM   627  N  NZ  A LYS   A 1 79  ? 35.727  23.651  3.155   0.36 39.47 ? 113 LYS   A NZ  1 
ATOM   628  N  NZ  B LYS   A 1 79  ? 34.847  25.797  3.311   0.64 33.99 ? 113 LYS   A NZ  1 
ATOM   629  N  N   . PRO   A 1 80  ? 43.099  24.784  2.713   1.00 41.22 ? 114 PRO   A N   1 
ATOM   630  C  CA  . PRO   A 1 80  ? 44.231  24.212  1.948   1.00 38.92 ? 114 PRO   A CA  1 
ATOM   631  C  C   . PRO   A 1 80  ? 45.155  23.263  2.728   1.00 40.34 ? 114 PRO   A C   1 
ATOM   632  O  O   . PRO   A 1 80  ? 45.740  22.365  2.104   1.00 40.52 ? 114 PRO   A O   1 
ATOM   633  C  CB  . PRO   A 1 80  ? 44.983  25.459  1.465   1.00 32.03 ? 114 PRO   A CB  1 
ATOM   634  C  CG  . PRO   A 1 80  ? 43.912  26.471  1.311   1.00 35.49 ? 114 PRO   A CG  1 
ATOM   635  C  CD  . PRO   A 1 80  ? 42.966  26.234  2.465   1.00 35.10 ? 114 PRO   A CD  1 
ATOM   636  N  N   . THR   A 1 81  ? 45.333  23.422  4.046   1.00 38.67 ? 115 THR   A N   1 
ATOM   637  C  CA  . THR   A 1 81  ? 46.206  22.524  4.807   1.00 40.20 ? 115 THR   A CA  1 
ATOM   638  C  C   . THR   A 1 81  ? 45.439  21.497  5.639   1.00 40.58 ? 115 THR   A C   1 
ATOM   639  O  O   . THR   A 1 81  ? 45.971  21.015  6.646   1.00 42.38 ? 115 THR   A O   1 
ATOM   640  C  CB  . THR   A 1 81  ? 47.148  23.298  5.734   1.00 36.44 ? 115 THR   A CB  1 
ATOM   641  O  OG1 . THR   A 1 81  ? 46.396  24.142  6.622   1.00 33.61 ? 115 THR   A OG1 1 
ATOM   642  C  CG2 . THR   A 1 81  ? 48.157  24.100  4.939   1.00 37.96 ? 115 THR   A CG2 1 
ATOM   643  N  N   . THR   A 1 82  ? 44.212  21.142  5.255   1.00 34.00 ? 116 THR   A N   1 
ATOM   644  C  CA  . THR   A 1 82  ? 43.385  20.324  6.129   1.00 35.63 ? 116 THR   A CA  1 
ATOM   645  C  C   . THR   A 1 82  ? 43.843  18.863  6.126   1.00 32.87 ? 116 THR   A C   1 
ATOM   646  O  O   . THR   A 1 82  ? 44.221  18.314  5.084   1.00 36.47 ? 116 THR   A O   1 
ATOM   647  C  CB  . THR   A 1 82  ? 41.909  20.431  5.733   1.00 34.15 ? 116 THR   A CB  1 
ATOM   648  O  OG1 . THR   A 1 82  ? 41.100  19.912  6.798   1.00 38.70 ? 116 THR   A OG1 1 
ATOM   649  C  CG2 . THR   A 1 82  ? 41.609  19.655  4.454   1.00 32.23 ? 116 THR   A CG2 1 
ATOM   650  N  N   . THR   A 1 83  ? 43.867  18.256  7.317   1.00 29.76 ? 117 THR   A N   1 
ATOM   651  C  CA  . THR   A 1 83  ? 44.070  16.814  7.452   1.00 35.18 ? 117 THR   A CA  1 
ATOM   652  C  C   . THR   A 1 83  ? 42.766  16.046  7.330   1.00 31.81 ? 117 THR   A C   1 
ATOM   653  O  O   . THR   A 1 83  ? 42.776  14.812  7.404   1.00 31.00 ? 117 THR   A O   1 
ATOM   654  C  CB  . THR   A 1 83  ? 44.741  16.448  8.789   1.00 25.36 ? 117 THR   A CB  1 
ATOM   655  O  OG1 . THR   A 1 83  ? 43.840  16.689  9.871   1.00 25.56 ? 117 THR   A OG1 1 
ATOM   656  C  CG2 . THR   A 1 83  ? 46.013  17.241  9.002   1.00 27.21 ? 117 THR   A CG2 1 
ATOM   657  N  N   . ALA   A 1 84  ? 41.653  16.754  7.148   1.00 27.16 ? 118 ALA   A N   1 
ATOM   658  C  CA  . ALA   A 1 84  ? 40.380  16.104  6.901   1.00 25.83 ? 118 ALA   A CA  1 
ATOM   659  C  C   . ALA   A 1 84  ? 40.423  15.384  5.560   1.00 32.60 ? 118 ALA   A C   1 
ATOM   660  O  O   . ALA   A 1 84  ? 40.871  15.949  4.557   1.00 34.89 ? 118 ALA   A O   1 
ATOM   661  C  CB  . ALA   A 1 84  ? 39.253  17.130  6.922   1.00 24.50 ? 118 ALA   A CB  1 
ATOM   662  N  N   . SER   A 1 85  ? 39.960  14.129  5.545   1.00 31.07 ? 119 SER   A N   1 
ATOM   663  C  CA  . SER   A 1 85  ? 39.856  13.370  4.307   1.00 26.35 ? 119 SER   A CA  1 
ATOM   664  C  C   . SER   A 1 85  ? 38.592  13.684  3.521   1.00 32.76 ? 119 SER   A C   1 
ATOM   665  O  O   . SER   A 1 85  ? 38.542  13.400  2.319   1.00 33.31 ? 119 SER   A O   1 
ATOM   666  C  CB  . SER   A 1 85  ? 39.876  11.884  4.605   1.00 31.17 ? 119 SER   A CB  1 
ATOM   667  O  OG  . SER   A 1 85  ? 38.803  11.554  5.474   1.00 34.39 ? 119 SER   A OG  1 
ATOM   668  N  N   . ILE   A 1 86  ? 37.563  14.224  4.161   1.00 30.81 ? 120 ILE   A N   1 
ATOM   669  C  CA  . ILE   A 1 86  ? 36.339  14.621  3.481   1.00 32.74 ? 120 ILE   A CA  1 
ATOM   670  C  C   . ILE   A 1 86  ? 36.190  16.124  3.628   1.00 36.68 ? 120 ILE   A C   1 
ATOM   671  O  O   . ILE   A 1 86  ? 35.630  16.606  4.611   1.00 36.71 ? 120 ILE   A O   1 
ATOM   672  C  CB  . ILE   A 1 86  ? 35.105  13.892  4.039   1.00 30.41 ? 120 ILE   A CB  1 
ATOM   673  C  CG1 . ILE   A 1 86  ? 35.259  12.378  3.850   1.00 30.68 ? 120 ILE   A CG1 1 
ATOM   674  C  CG2 . ILE   A 1 86  ? 33.826  14.455  3.391   1.00 22.27 ? 120 ILE   A CG2 1 
ATOM   675  C  CD1 . ILE   A 1 86  ? 34.412  11.555  4.772   1.00 24.85 ? 120 ILE   A CD1 1 
ATOM   676  N  N   . PRO   A 1 87  ? 36.647  16.901  2.634   1.00 45.70 ? 121 PRO   A N   1 
ATOM   677  C  CA  . PRO   A 1 87  ? 36.804  18.355  2.833   1.00 35.79 ? 121 PRO   A CA  1 
ATOM   678  C  C   . PRO   A 1 87  ? 35.503  19.110  2.972   1.00 34.20 ? 121 PRO   A C   1 
ATOM   679  O  O   . PRO   A 1 87  ? 35.536  20.259  3.417   1.00 39.52 ? 121 PRO   A O   1 
ATOM   680  C  CB  . PRO   A 1 87  ? 37.554  18.795  1.575   1.00 36.94 ? 121 PRO   A CB  1 
ATOM   681  C  CG  . PRO   A 1 87  ? 37.064  17.821  0.532   1.00 45.57 ? 121 PRO   A CG  1 
ATOM   682  C  CD  . PRO   A 1 87  ? 36.991  16.493  1.256   1.00 36.48 ? 121 PRO   A CD  1 
ATOM   683  N  N   . SER   A 1 88  ? 34.373  18.510  2.703   1.00 36.53 ? 122 SER   A N   1 
ATOM   684  C  CA  . SER   A 1 88  ? 33.136  19.233  2.880   1.00 34.25 ? 122 SER   A CA  1 
ATOM   685  C  C   . SER   A 1 88  ? 32.701  19.244  4.324   1.00 37.49 ? 122 SER   A C   1 
ATOM   686  O  O   . SER   A 1 88  ? 31.744  19.855  4.685   1.00 34.48 ? 122 SER   A O   1 
ATOM   687  C  CB  . SER   A 1 88  ? 32.033  18.690  1.996   1.00 30.30 ? 122 SER   A CB  1 
ATOM   688  O  OG  . SER   A 1 88  ? 31.886  17.313  2.066   1.00 32.12 ? 122 SER   A OG  1 
ATOM   689  N  N   . PHE   A 1 89  ? 33.445  18.557  5.157   1.00 40.55 ? 123 PHE   A N   1 
ATOM   690  C  CA  . PHE   A 1 89  ? 33.115  18.468  6.568   1.00 35.11 ? 123 PHE   A CA  1 
ATOM   691  C  C   . PHE   A 1 89  ? 33.337  19.822  7.245   1.00 36.80 ? 123 PHE   A C   1 
ATOM   692  O  O   . PHE   A 1 89  ? 34.007  20.712  6.719   1.00 37.51 ? 123 PHE   A O   1 
ATOM   693  C  CB  . PHE   A 1 89  ? 33.941  17.357  7.236   1.00 38.02 ? 123 PHE   A CB  1 
ATOM   694  C  CG  . PHE   A 1 89  ? 33.483  17.003  8.629   1.00 32.10 ? 123 PHE   A CG  1 
ATOM   695  C  CD1 . PHE   A 1 89  ? 32.374  16.211  8.825   1.00 30.25 ? 123 PHE   A CD1 1 
ATOM   696  C  CD2 . PHE   A 1 89  ? 34.171  17.477  9.744   1.00 32.50 ? 123 PHE   A CD2 1 
ATOM   697  C  CE1 . PHE   A 1 89  ? 31.954  15.898  10.107  1.00 34.62 ? 123 PHE   A CE1 1 
ATOM   698  C  CE2 . PHE   A 1 89  ? 33.759  17.180  11.024  1.00 30.21 ? 123 PHE   A CE2 1 
ATOM   699  C  CZ  . PHE   A 1 89  ? 32.654  16.391  11.215  1.00 32.33 ? 123 PHE   A CZ  1 
ATOM   700  N  N   . ASP   A 1 90  ? 32.742  19.970  8.429   1.00 40.06 ? 124 ASP   A N   1 
ATOM   701  C  CA  . ASP   A 1 90  ? 32.655  21.252  9.116   1.00 38.87 ? 124 ASP   A CA  1 
ATOM   702  C  C   . ASP   A 1 90  ? 32.106  21.063  10.527  1.00 37.75 ? 124 ASP   A C   1 
ATOM   703  O  O   . ASP   A 1 90  ? 30.919  20.743  10.690  1.00 35.74 ? 124 ASP   A O   1 
ATOM   704  C  CB  . ASP   A 1 90  ? 31.769  22.211  8.322   1.00 35.59 ? 124 ASP   A CB  1 
ATOM   705  C  CG  . ASP   A 1 90  ? 31.406  23.434  9.106   1.00 39.91 ? 124 ASP   A CG  1 
ATOM   706  O  OD1 . ASP   A 1 90  ? 32.106  24.452  8.953   1.00 52.26 ? 124 ASP   A OD1 1 
ATOM   707  O  OD2 . ASP   A 1 90  ? 30.420  23.385  9.868   1.00 39.34 ? 124 ASP   A OD2 1 
ATOM   708  N  N   . HIS   A 1 91  ? 32.954  21.273  11.546  1.00 34.46 ? 125 HIS   A N   1 
ATOM   709  C  CA  . HIS   A 1 91  ? 32.576  20.956  12.925  1.00 34.59 ? 125 HIS   A CA  1 
ATOM   710  C  C   . HIS   A 1 91  ? 31.202  21.519  13.271  1.00 37.21 ? 125 HIS   A C   1 
ATOM   711  O  O   . HIS   A 1 91  ? 30.350  20.812  13.823  1.00 42.74 ? 125 HIS   A O   1 
ATOM   712  C  CB  . HIS   A 1 91  ? 33.616  21.492  13.912  1.00 33.69 ? 125 HIS   A CB  1 
ATOM   713  C  CG  . HIS   A 1 91  ? 34.909  20.737  13.928  1.00 33.68 ? 125 HIS   A CG  1 
ATOM   714  N  ND1 . HIS   A 1 91  ? 35.125  19.647  14.748  1.00 34.81 ? 125 HIS   A ND1 1 
ATOM   715  C  CD2 . HIS   A 1 91  ? 36.074  20.948  13.269  1.00 30.80 ? 125 HIS   A CD2 1 
ATOM   716  C  CE1 . HIS   A 1 91  ? 36.358  19.204  14.574  1.00 30.19 ? 125 HIS   A CE1 1 
ATOM   717  N  NE2 . HIS   A 1 91  ? 36.954  19.976  13.680  1.00 31.97 ? 125 HIS   A NE2 1 
ATOM   718  N  N   . GLY   A 1 92  ? 30.966  22.791  12.941  1.00 30.08 ? 126 GLY   A N   1 
ATOM   719  C  CA  . GLY   A 1 92  ? 29.698  23.402  13.292  1.00 27.35 ? 126 GLY   A CA  1 
ATOM   720  C  C   . GLY   A 1 92  ? 28.523  22.712  12.631  1.00 28.31 ? 126 GLY   A C   1 
ATOM   721  O  O   . GLY   A 1 92  ? 27.512  22.424  13.272  1.00 26.93 ? 126 GLY   A O   1 
ATOM   722  N  N   . SER   A 1 93  ? 28.647  22.427  11.337  1.00 32.32 ? 127 SER   A N   1 
ATOM   723  C  CA  . SER   A 1 93  ? 27.532  21.831  10.613  1.00 31.28 ? 127 SER   A CA  1 
ATOM   724  C  C   . SER   A 1 93  ? 27.195  20.457  11.166  1.00 32.56 ? 127 SER   A C   1 
ATOM   725  O  O   . SER   A 1 93  ? 26.017  20.102  11.285  1.00 30.22 ? 127 SER   A O   1 
ATOM   726  C  CB  . SER   A 1 93  ? 27.862  21.753  9.133   1.00 22.58 ? 127 SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 93  ? 27.836  23.057  8.602   1.00 29.19 ? 127 SER   A OG  1 
ATOM   728  N  N   . CYS   A 1 94  ? 28.218  19.686  11.540  1.00 30.95 ? 128 CYS   A N   1 
ATOM   729  C  CA  . CYS   A 1 94  ? 27.979  18.372  12.116  1.00 30.64 ? 128 CYS   A CA  1 
ATOM   730  C  C   . CYS   A 1 94  ? 27.274  18.496  13.458  1.00 30.77 ? 128 CYS   A C   1 
ATOM   731  O  O   . CYS   A 1 94  ? 26.148  18.009  13.619  1.00 29.22 ? 128 CYS   A O   1 
ATOM   732  C  CB  . CYS   A 1 94  ? 29.294  17.610  12.261  1.00 32.30 ? 128 CYS   A CB  1 
ATOM   733  S  SG  . CYS   A 1 94  ? 29.074  15.816  12.381  1.00 30.45 ? 128 CYS   A SG  1 
ATOM   734  N  N   . ARG   A 1 95  ? 27.920  19.166  14.429  1.00 31.11 ? 129 ARG   A N   1 
ATOM   735  C  CA  . ARG   A 1 95  ? 27.329  19.317  15.759  1.00 31.83 ? 129 ARG   A CA  1 
ATOM   736  C  C   . ARG   A 1 95  ? 25.934  19.919  15.669  1.00 30.53 ? 129 ARG   A C   1 
ATOM   737  O  O   . ARG   A 1 95  ? 25.031  19.525  16.417  1.00 31.63 ? 129 ARG   A O   1 
ATOM   738  C  CB  . ARG   A 1 95  ? 28.235  20.159  16.671  1.00 28.97 ? 129 ARG   A CB  1 
ATOM   739  C  CG  . ARG   A 1 95  ? 29.646  19.558  16.882  1.00 34.95 ? 129 ARG   A CG  1 
ATOM   740  C  CD  . ARG   A 1 95  ? 30.464  20.265  17.983  1.00 38.38 ? 129 ARG   A CD  1 
ATOM   741  N  NE  . ARG   A 1 95  ? 31.919  20.078  17.847  1.00 42.77 ? 129 ARG   A NE  1 
ATOM   742  C  CZ  . ARG   A 1 95  ? 32.617  19.042  18.322  1.00 41.70 ? 129 ARG   A CZ  1 
ATOM   743  N  NH1 . ARG   A 1 95  ? 32.001  18.076  18.985  1.00 37.58 ? 129 ARG   A NH1 1 
ATOM   744  N  NH2 . ARG   A 1 95  ? 33.939  18.975  18.144  1.00 38.71 ? 129 ARG   A NH2 1 
ATOM   745  N  N   . SER   A 1 96  ? 25.734  20.849  14.733  1.00 27.38 ? 130 SER   A N   1 
ATOM   746  C  CA  . SER   A 1 96  ? 24.417  21.443  14.530  1.00 32.69 ? 130 SER   A CA  1 
ATOM   747  C  C   . SER   A 1 96  ? 23.433  20.413  13.972  1.00 32.94 ? 130 SER   A C   1 
ATOM   748  O  O   . SER   A 1 96  ? 22.354  20.197  14.540  1.00 34.32 ? 130 SER   A O   1 
ATOM   749  C  CB  . SER   A 1 96  ? 24.542  22.665  13.611  1.00 28.45 ? 130 SER   A CB  1 
ATOM   750  O  OG  . SER   A 1 96  ? 23.297  23.262  13.314  1.00 25.29 ? 130 SER   A OG  1 
ATOM   751  N  N   . PHE   A 1 97  ? 23.792  19.769  12.855  1.00 31.34 ? 131 PHE   A N   1 
ATOM   752  C  CA  . PHE   A 1 97  ? 22.975  18.695  12.299  1.00 26.89 ? 131 PHE   A CA  1 
ATOM   753  C  C   . PHE   A 1 97  ? 22.555  17.730  13.387  1.00 28.73 ? 131 PHE   A C   1 
ATOM   754  O  O   . PHE   A 1 97  ? 21.379  17.360  13.495  1.00 31.88 ? 131 PHE   A O   1 
ATOM   755  C  CB  . PHE   A 1 97  ? 23.761  17.957  11.202  1.00 30.51 ? 131 PHE   A CB  1 
ATOM   756  C  CG  . PHE   A 1 97  ? 23.000  16.821  10.521  1.00 28.82 ? 131 PHE   A CG  1 
ATOM   757  C  CD1 . PHE   A 1 97  ? 22.938  15.557  11.100  1.00 22.91 ? 131 PHE   A CD1 1 
ATOM   758  C  CD2 . PHE   A 1 97  ? 22.408  17.011  9.278   1.00 28.01 ? 131 PHE   A CD2 1 
ATOM   759  C  CE1 . PHE   A 1 97  ? 22.277  14.526  10.485  1.00 26.59 ? 131 PHE   A CE1 1 
ATOM   760  C  CE2 . PHE   A 1 97  ? 21.734  15.982  8.649   1.00 29.46 ? 131 PHE   A CE2 1 
ATOM   761  C  CZ  . PHE   A 1 97  ? 21.670  14.730  9.259   1.00 30.20 ? 131 PHE   A CZ  1 
ATOM   762  N  N   . PHE   A 1 98  ? 23.503  17.331  14.224  1.00 25.73 ? 132 PHE   A N   1 
ATOM   763  C  CA  . PHE   A 1 98  ? 23.222  16.228  15.124  1.00 28.19 ? 132 PHE   A CA  1 
ATOM   764  C  C   . PHE   A 1 98  ? 22.321  16.628  16.284  1.00 32.78 ? 132 PHE   A C   1 
ATOM   765  O  O   . PHE   A 1 98  ? 21.552  15.789  16.766  1.00 37.26 ? 132 PHE   A O   1 
ATOM   766  C  CB  . PHE   A 1 98  ? 24.516  15.619  15.663  1.00 26.63 ? 132 PHE   A CB  1 
ATOM   767  C  CG  . PHE   A 1 98  ? 24.298  14.341  16.401  1.00 27.06 ? 132 PHE   A CG  1 
ATOM   768  C  CD1 . PHE   A 1 98  ? 24.218  13.139  15.710  1.00 29.81 ? 132 PHE   A CD1 1 
ATOM   769  C  CD2 . PHE   A 1 98  ? 24.135  14.335  17.776  1.00 27.91 ? 132 PHE   A CD2 1 
ATOM   770  C  CE1 . PHE   A 1 98  ? 24.006  11.943  16.376  1.00 28.40 ? 132 PHE   A CE1 1 
ATOM   771  C  CE2 . PHE   A 1 98  ? 23.916  13.138  18.458  1.00 34.36 ? 132 PHE   A CE2 1 
ATOM   772  C  CZ  . PHE   A 1 98  ? 23.854  11.934  17.752  1.00 28.31 ? 132 PHE   A CZ  1 
ATOM   773  N  N   . SER   A 1 99  ? 22.407  17.867  16.776  1.00 29.92 ? 133 SER   A N   1 
ATOM   774  C  CA  . SER   A 1 99  ? 21.518  18.232  17.866  1.00 30.92 ? 133 SER   A CA  1 
ATOM   775  C  C   . SER   A 1 99  ? 20.125  18.537  17.364  1.00 30.81 ? 133 SER   A C   1 
ATOM   776  O  O   . SER   A 1 99  ? 19.166  18.494  18.139  1.00 34.12 ? 133 SER   A O   1 
ATOM   777  C  CB  . SER   A 1 99  ? 22.064  19.426  18.630  1.00 33.51 ? 133 SER   A CB  1 
ATOM   778  O  OG  . SER   A 1 99  ? 21.788  20.600  17.915  1.00 47.35 ? 133 SER   A OG  1 
ATOM   779  N  N   . SER   A 1 100 ? 19.994  18.817  16.077  1.00 33.00 ? 134 SER   A N   1 
ATOM   780  C  CA  . SER   A 1 100 ? 18.683  19.102  15.522  1.00 31.94 ? 134 SER   A CA  1 
ATOM   781  C  C   . SER   A 1 100 ? 17.941  17.823  15.156  1.00 31.76 ? 134 SER   A C   1 
ATOM   782  O  O   . SER   A 1 100 ? 16.717  17.759  15.297  1.00 34.84 ? 134 SER   A O   1 
ATOM   783  C  CB  . SER   A 1 100 ? 18.833  20.011  14.308  1.00 26.32 ? 134 SER   A CB  1 
ATOM   784  O  OG  . SER   A 1 100 ? 17.598  20.607  14.006  1.00 32.60 ? 134 SER   A OG  1 
ATOM   785  N  N   . HIS   A 1 101 ? 18.666  16.792  14.699  1.00 31.77 ? 135 HIS   A N   1 
ATOM   786  C  CA  . HIS   A 1 101 ? 18.070  15.569  14.163  1.00 29.09 ? 135 HIS   A CA  1 
ATOM   787  C  C   . HIS   A 1 101 ? 18.522  14.286  14.868  1.00 29.92 ? 135 HIS   A C   1 
ATOM   788  O  O   . HIS   A 1 101 ? 17.892  13.238  14.684  1.00 25.47 ? 135 HIS   A O   1 
ATOM   789  C  CB  . HIS   A 1 101 ? 18.389  15.428  12.661  1.00 24.37 ? 135 HIS   A CB  1 
ATOM   790  C  CG  . HIS   A 1 101 ? 18.132  16.662  11.841  1.00 28.45 ? 135 HIS   A CG  1 
ATOM   791  N  ND1 . HIS   A 1 101 ? 16.864  17.125  11.554  1.00 29.14 ? 135 HIS   A ND1 1 
ATOM   792  C  CD2 . HIS   A 1 101 ? 18.985  17.491  11.193  1.00 28.94 ? 135 HIS   A CD2 1 
ATOM   793  C  CE1 . HIS   A 1 101 ? 16.948  18.199  10.791  1.00 28.05 ? 135 HIS   A CE1 1 
ATOM   794  N  NE2 . HIS   A 1 101 ? 18.224  18.441  10.555  1.00 27.02 ? 135 HIS   A NE2 1 
ATOM   795  N  N   . GLY   A 1 102 ? 19.585  14.329  15.664  1.00 33.19 ? 136 GLY   A N   1 
ATOM   796  C  CA  . GLY   A 1 102 ? 20.136  13.097  16.171  1.00 25.62 ? 136 GLY   A CA  1 
ATOM   797  C  C   . GLY   A 1 102 ? 20.789  12.284  15.057  1.00 28.53 ? 136 GLY   A C   1 
ATOM   798  O  O   . GLY   A 1 102 ? 21.185  12.803  14.005  1.00 24.93 ? 136 GLY   A O   1 
ATOM   799  N  N   . LEU   A 1 103 ? 20.892  10.973  15.314  1.00 28.42 ? 137 LEU   A N   1 
ATOM   800  C  CA  . LEU   A 1 103 ? 21.535  10.047  14.390  1.00 21.87 ? 137 LEU   A CA  1 
ATOM   801  C  C   . LEU   A 1 103 ? 20.705  9.903   13.123  1.00 20.68 ? 137 LEU   A C   1 
ATOM   802  O  O   . LEU   A 1 103 ? 19.494  9.655   13.187  1.00 24.29 ? 137 LEU   A O   1 
ATOM   803  C  CB  . LEU   A 1 103 ? 21.734  8.688   15.060  1.00 27.80 ? 137 LEU   A CB  1 
ATOM   804  C  CG  . LEU   A 1 103 ? 22.272  7.566   14.166  1.00 21.22 ? 137 LEU   A CG  1 
ATOM   805  C  CD1 . LEU   A 1 103 ? 23.618  7.940   13.567  1.00 19.19 ? 137 LEU   A CD1 1 
ATOM   806  C  CD2 . LEU   A 1 103 ? 22.345  6.264   14.927  1.00 20.55 ? 137 LEU   A CD2 1 
ATOM   807  N  N   . GLY   A 1 104 ? 21.361  10.055  11.976  1.00 17.12 ? 138 GLY   A N   1 
ATOM   808  C  CA  . GLY   A 1 104 ? 20.649  10.206  10.720  1.00 18.95 ? 138 GLY   A CA  1 
ATOM   809  C  C   . GLY   A 1 104 ? 21.615  10.289  9.557   1.00 23.27 ? 138 GLY   A C   1 
ATOM   810  O  O   . GLY   A 1 104 ? 22.844  10.314  9.728   1.00 22.07 ? 138 GLY   A O   1 
ATOM   811  N  N   . VAL   A 1 105 ? 21.042  10.317  8.358   1.00 18.27 ? 139 VAL   A N   1 
ATOM   812  C  CA  . VAL   A 1 105 ? 21.823  10.345  7.128   1.00 20.37 ? 139 VAL   A CA  1 
ATOM   813  C  C   . VAL   A 1 105 ? 21.966  11.783  6.665   1.00 23.78 ? 139 VAL   A C   1 
ATOM   814  O  O   . VAL   A 1 105 ? 20.964  12.490  6.468   1.00 21.37 ? 139 VAL   A O   1 
ATOM   815  C  CB  . VAL   A 1 105 ? 21.184  9.496   6.019   1.00 20.64 ? 139 VAL   A CB  1 
ATOM   816  C  CG1 . VAL   A 1 105 ? 21.967  9.700   4.738   1.00 19.52 ? 139 VAL   A CG1 1 
ATOM   817  C  CG2 . VAL   A 1 105 ? 21.110  8.027   6.433   1.00 16.14 ? 139 VAL   A CG2 1 
ATOM   818  N  N   . ARG   A 1 106 ? 23.216  12.200  6.470   1.00 28.08 ? 140 ARG   A N   1 
ATOM   819  C  CA  . ARG   A 1 106 ? 23.596  13.511  5.970   1.00 24.73 ? 140 ARG   A CA  1 
ATOM   820  C  C   . ARG   A 1 106 ? 23.803  13.527  4.461   1.00 22.94 ? 140 ARG   A C   1 
ATOM   821  O  O   . ARG   A 1 106 ? 23.471  14.515  3.805   1.00 21.30 ? 140 ARG   A O   1 
ATOM   822  C  CB  . ARG   A 1 106 ? 24.881  13.967  6.670   1.00 19.96 ? 140 ARG   A CB  1 
ATOM   823  C  CG  . ARG   A 1 106 ? 25.667  15.030  5.908   1.00 21.64 ? 140 ARG   A CG  1 
ATOM   824  C  CD  . ARG   A 1 106 ? 25.111  16.417  6.164   1.00 20.15 ? 140 ARG   A CD  1 
ATOM   825  N  NE  . ARG   A 1 106 ? 25.829  17.444  5.420   1.00 24.40 ? 140 ARG   A NE  1 
ATOM   826  C  CZ  . ARG   A 1 106 ? 25.394  18.694  5.271   1.00 29.14 ? 140 ARG   A CZ  1 
ATOM   827  N  NH1 . ARG   A 1 106 ? 24.239  19.069  5.810   1.00 25.10 ? 140 ARG   A NH1 1 
ATOM   828  N  NH2 . ARG   A 1 106 ? 26.103  19.566  4.574   1.00 27.42 ? 140 ARG   A NH2 1 
ATOM   829  N  N   . ALA   A 1 107 ? 24.337  12.451  3.895   1.00 21.98 ? 141 ALA   A N   1 
ATOM   830  C  CA  . ALA   A 1 107 ? 24.789  12.455  2.513   1.00 20.93 ? 141 ALA   A CA  1 
ATOM   831  C  C   . ALA   A 1 107 ? 24.308  11.180  1.856   1.00 23.69 ? 141 ALA   A C   1 
ATOM   832  O  O   . ALA   A 1 107 ? 24.777  10.092  2.200   1.00 24.70 ? 141 ALA   A O   1 
ATOM   833  C  CB  . ALA   A 1 107 ? 26.311  12.556  2.421   1.00 23.10 ? 141 ALA   A CB  1 
ATOM   834  N  N   . VAL   A 1 108 ? 23.357  11.316  0.944   1.00 22.85 ? 142 VAL   A N   1 
ATOM   835  C  CA  . VAL   A 1 108 ? 23.093  10.305  -0.070  1.00 25.61 ? 142 VAL   A CA  1 
ATOM   836  C  C   . VAL   A 1 108 ? 24.050  10.593  -1.222  1.00 28.59 ? 142 VAL   A C   1 
ATOM   837  O  O   . VAL   A 1 108 ? 24.055  11.705  -1.769  1.00 27.64 ? 142 VAL   A O   1 
ATOM   838  C  CB  . VAL   A 1 108 ? 21.627  10.350  -0.531  1.00 31.28 ? 142 VAL   A CB  1 
ATOM   839  C  CG1 . VAL   A 1 108 ? 21.354  9.309   -1.633  1.00 23.61 ? 142 VAL   A CG1 1 
ATOM   840  C  CG2 . VAL   A 1 108 ? 20.694  10.183  0.669   1.00 25.51 ? 142 VAL   A CG2 1 
ATOM   841  N  N   . ALA   A 1 109 ? 24.883  9.616   -1.571  1.00 23.23 ? 143 ALA   A N   1 
ATOM   842  C  CA  . ALA   A 1 109 ? 26.012  9.856   -2.461  1.00 25.42 ? 143 ALA   A CA  1 
ATOM   843  C  C   . ALA   A 1 109 ? 25.909  8.928   -3.665  1.00 24.38 ? 143 ALA   A C   1 
ATOM   844  O  O   . ALA   A 1 109 ? 26.003  7.704   -3.529  1.00 26.53 ? 143 ALA   A O   1 
ATOM   845  C  CB  . ALA   A 1 109 ? 27.336  9.677   -1.715  1.00 26.15 ? 143 ALA   A CB  1 
ATOM   846  N  N   . ILE   A 1 110 ? 25.716  9.512   -4.835  1.00 27.77 ? 144 ILE   A N   1 
ATOM   847  C  CA  . ILE   A 1 110 ? 25.679  8.782   -6.095  1.00 31.91 ? 144 ILE   A CA  1 
ATOM   848  C  C   . ILE   A 1 110 ? 26.981  9.037   -6.832  1.00 28.80 ? 144 ILE   A C   1 
ATOM   849  O  O   . ILE   A 1 110 ? 27.612  10.086  -6.680  1.00 31.13 ? 144 ILE   A O   1 
ATOM   850  C  CB  . ILE   A 1 110 ? 24.457  9.195   -6.937  1.00 32.24 ? 144 ILE   A CB  1 
ATOM   851  C  CG1 . ILE   A 1 110 ? 24.649  10.598  -7.516  1.00 31.81 ? 144 ILE   A CG1 1 
ATOM   852  C  CG2 . ILE   A 1 110 ? 23.229  9.194   -6.061  1.00 28.13 ? 144 ILE   A CG2 1 
ATOM   853  C  CD1 . ILE   A 1 110 ? 23.405  11.180  -8.128  1.00 29.48 ? 144 ILE   A CD1 1 
ATOM   854  N  N   . GLU   A 1 111 ? 27.411  8.049   -7.605  1.00 30.12 ? 145 GLU   A N   1 
ATOM   855  C  CA  . GLU   A 1 111 ? 28.636  8.166   -8.379  1.00 37.34 ? 145 GLU   A CA  1 
ATOM   856  C  C   . GLU   A 1 111 ? 28.289  8.620   -9.792  1.00 34.29 ? 145 GLU   A C   1 
ATOM   857  O  O   . GLU   A 1 111 ? 27.372  8.092   -10.420 1.00 34.77 ? 145 GLU   A O   1 
ATOM   858  C  CB  . GLU   A 1 111 ? 29.407  6.844   -8.405  1.00 41.53 ? 145 GLU   A CB  1 
ATOM   859  C  CG  . GLU   A 1 111 ? 30.842  6.941   -8.944  1.00 46.93 ? 145 GLU   A CG  1 
ATOM   860  C  CD  . GLU   A 1 111 ? 31.501  5.575   -9.126  1.00 46.83 ? 145 GLU   A CD  1 
ATOM   861  O  OE1 . GLU   A 1 111 ? 31.316  4.689   -8.262  1.00 53.77 ? 145 GLU   A OE1 1 
ATOM   862  O  OE2 . GLU   A 1 111 ? 32.166  5.365   -10.162 1.00 50.69 ? 145 GLU   A OE2 1 
ATOM   863  N  N   . VAL   A 1 112 ? 29.002  9.626   -10.268 1.00 39.34 ? 146 VAL   A N   1 
ATOM   864  C  CA  . VAL   A 1 112 ? 28.720  10.241  -11.558 1.00 43.42 ? 146 VAL   A CA  1 
ATOM   865  C  C   . VAL   A 1 112 ? 29.950  10.054  -12.434 1.00 40.97 ? 146 VAL   A C   1 
ATOM   866  O  O   . VAL   A 1 112 ? 30.957  9.494   -11.988 1.00 42.07 ? 146 VAL   A O   1 
ATOM   867  C  CB  . VAL   A 1 112 ? 28.357  11.730  -11.390 1.00 38.47 ? 146 VAL   A CB  1 
ATOM   868  C  CG1 . VAL   A 1 112 ? 27.100  11.899  -10.533 1.00 28.49 ? 146 VAL   A CG1 1 
ATOM   869  C  CG2 . VAL   A 1 112 ? 29.523  12.481  -10.786 1.00 35.14 ? 146 VAL   A CG2 1 
ATOM   870  N  N   . GLU   A 1 113 ? 29.891  10.507  -13.685 1.00 45.43 ? 147 GLU   A N   1 
ATOM   871  C  CA  . GLU   A 1 113 ? 31.119  10.404  -14.463 1.00 43.95 ? 147 GLU   A CA  1 
ATOM   872  C  C   . GLU   A 1 113 ? 31.949  11.677  -14.396 1.00 41.55 ? 147 GLU   A C   1 
ATOM   873  O  O   . GLU   A 1 113 ? 33.180  11.603  -14.390 1.00 44.06 ? 147 GLU   A O   1 
ATOM   874  C  CB  . GLU   A 1 113 ? 30.823  10.015  -15.910 1.00 44.72 ? 147 GLU   A CB  1 
ATOM   875  C  CG  . GLU   A 1 113 ? 30.776  8.508   -16.031 1.00 50.27 ? 147 GLU   A CG  1 
ATOM   876  C  CD  . GLU   A 1 113 ? 32.174  7.902   -15.972 1.00 50.40 ? 147 GLU   A CD  1 
ATOM   877  O  OE1 . GLU   A 1 113 ? 33.130  8.554   -16.454 1.00 53.93 ? 147 GLU   A OE1 1 
ATOM   878  O  OE2 . GLU   A 1 113 ? 32.322  6.806   -15.391 1.00 47.48 ? 147 GLU   A OE2 1 
ATOM   879  N  N   . ASP   A 1 114 ? 31.320  12.846  -14.298 1.00 39.86 ? 148 ASP   A N   1 
ATOM   880  C  CA  . ASP   A 1 114 ? 32.037  14.061  -13.926 1.00 41.07 ? 148 ASP   A CA  1 
ATOM   881  C  C   . ASP   A 1 114 ? 31.252  14.836  -12.881 1.00 41.02 ? 148 ASP   A C   1 
ATOM   882  O  O   . ASP   A 1 114 ? 30.133  15.289  -13.145 1.00 43.19 ? 148 ASP   A O   1 
ATOM   883  C  CB  . ASP   A 1 114 ? 32.313  14.971  -15.115 1.00 41.33 ? 148 ASP   A CB  1 
ATOM   884  C  CG  . ASP   A 1 114 ? 33.161  16.143  -14.721 1.00 46.93 ? 148 ASP   A CG  1 
ATOM   885  O  OD1 . ASP   A 1 114 ? 34.337  15.904  -14.366 1.00 45.13 ? 148 ASP   A OD1 1 
ATOM   886  O  OD2 . ASP   A 1 114 ? 32.654  17.284  -14.720 1.00 47.79 ? 148 ASP   A OD2 1 
ATOM   887  N  N   . ALA   A 1 115 ? 31.866  15.031  -11.713 1.00 43.27 ? 149 ALA   A N   1 
ATOM   888  C  CA  . ALA   A 1 115 ? 31.211  15.724  -10.609 1.00 43.97 ? 149 ALA   A CA  1 
ATOM   889  C  C   . ALA   A 1 115 ? 31.224  17.245  -10.773 1.00 39.43 ? 149 ALA   A C   1 
ATOM   890  O  O   . ALA   A 1 115 ? 30.264  17.906  -10.358 1.00 35.01 ? 149 ALA   A O   1 
ATOM   891  C  CB  . ALA   A 1 115 ? 31.862  15.318  -9.283  1.00 38.71 ? 149 ALA   A CB  1 
ATOM   892  N  N   . GLU   A 1 116 ? 32.282  17.820  -11.365 1.00 40.85 ? 150 GLU   A N   1 
ATOM   893  C  CA  . GLU   A 1 116 ? 32.272  19.256  -11.646 1.00 38.54 ? 150 GLU   A CA  1 
ATOM   894  C  C   . GLU   A 1 116 ? 31.115  19.632  -12.564 1.00 38.02 ? 150 GLU   A C   1 
ATOM   895  O  O   . GLU   A 1 116 ? 30.433  20.639  -12.335 1.00 35.58 ? 150 GLU   A O   1 
ATOM   896  C  CB  . GLU   A 1 116 ? 33.601  19.692  -12.257 1.00 38.06 ? 150 GLU   A CB  1 
ATOM   897  C  CG  . GLU   A 1 116 ? 34.771  19.571  -11.304 1.00 45.05 ? 150 GLU   A CG  1 
ATOM   898  C  CD  . GLU   A 1 116 ? 36.022  20.254  -11.817 1.00 52.83 ? 150 GLU   A CD  1 
ATOM   899  O  OE1 . GLU   A 1 116 ? 37.120  19.694  -11.622 1.00 58.00 ? 150 GLU   A OE1 1 
ATOM   900  O  OE2 . GLU   A 1 116 ? 35.907  21.343  -12.422 1.00 60.50 ? 150 GLU   A OE2 1 
ATOM   901  N  N   . SER   A 1 117 ? 30.868  18.829  -13.604 1.00 36.50 ? 151 SER   A N   1 
ATOM   902  C  CA  . SER   A 1 117 ? 29.782  19.158  -14.525 1.00 41.27 ? 151 SER   A CA  1 
ATOM   903  C  C   . SER   A 1 117 ? 28.435  18.776  -13.937 1.00 41.77 ? 151 SER   A C   1 
ATOM   904  O  O   . SER   A 1 117 ? 27.438  19.473  -14.156 1.00 39.77 ? 151 SER   A O   1 
ATOM   905  C  CB  . SER   A 1 117 ? 29.985  18.477  -15.885 1.00 41.72 ? 151 SER   A CB  1 
ATOM   906  O  OG  . SER   A 1 117 ? 30.129  17.069  -15.759 1.00 42.94 ? 151 SER   A OG  1 
ATOM   907  N  N   . ALA   A 1 118 ? 28.386  17.669  -13.193 1.00 42.62 ? 152 ALA   A N   1 
ATOM   908  C  CA  . ALA   A 1 118 ? 27.172  17.344  -12.459 1.00 36.85 ? 152 ALA   A CA  1 
ATOM   909  C  C   . ALA   A 1 118 ? 26.782  18.484  -11.521 1.00 37.27 ? 152 ALA   A C   1 
ATOM   910  O  O   . ALA   A 1 118 ? 25.613  18.889  -11.484 1.00 39.07 ? 152 ALA   A O   1 
ATOM   911  C  CB  . ALA   A 1 118 ? 27.360  16.033  -11.694 1.00 33.25 ? 152 ALA   A CB  1 
ATOM   912  N  N   . PHE   A 1 119 ? 27.753  19.030  -10.771 1.00 33.17 ? 153 PHE   A N   1 
ATOM   913  C  CA  . PHE   A 1 119 ? 27.469  20.133  -9.851  1.00 32.32 ? 153 PHE   A CA  1 
ATOM   914  C  C   . PHE   A 1 119 ? 27.007  21.368  -10.611 1.00 38.26 ? 153 PHE   A C   1 
ATOM   915  O  O   . PHE   A 1 119 ? 25.995  21.987  -10.255 1.00 37.16 ? 153 PHE   A O   1 
ATOM   916  C  CB  . PHE   A 1 119 ? 28.712  20.443  -9.003  1.00 32.75 ? 153 PHE   A CB  1 
ATOM   917  C  CG  . PHE   A 1 119 ? 28.564  21.652  -8.106  1.00 35.80 ? 153 PHE   A CG  1 
ATOM   918  C  CD1 . PHE   A 1 119 ? 28.910  22.929  -8.558  1.00 38.78 ? 153 PHE   A CD1 1 
ATOM   919  C  CD2 . PHE   A 1 119 ? 28.107  21.518  -6.806  1.00 36.48 ? 153 PHE   A CD2 1 
ATOM   920  C  CE1 . PHE   A 1 119 ? 28.781  24.037  -7.736  1.00 30.55 ? 153 PHE   A CE1 1 
ATOM   921  C  CE2 . PHE   A 1 119 ? 27.966  22.641  -5.976  1.00 35.81 ? 153 PHE   A CE2 1 
ATOM   922  C  CZ  . PHE   A 1 119 ? 28.306  23.889  -6.448  1.00 34.62 ? 153 PHE   A CZ  1 
ATOM   923  N  N   . SER   A 1 120 ? 27.738  21.725  -11.678 1.00 39.88 ? 154 SER   A N   1 
ATOM   924  C  CA  . SER   A 1 120 ? 27.432  22.909  -12.480 1.00 37.60 ? 154 SER   A CA  1 
ATOM   925  C  C   . SER   A 1 120 ? 26.031  22.830  -13.078 1.00 35.98 ? 154 SER   A C   1 
ATOM   926  O  O   . SER   A 1 120 ? 25.210  23.737  -12.894 1.00 36.57 ? 154 SER   A O   1 
ATOM   927  C  CB  . SER   A 1 120 ? 28.473  23.064  -13.594 1.00 35.70 ? 154 SER   A CB  1 
ATOM   928  O  OG  . SER   A 1 120 ? 29.794  23.020  -13.082 1.00 45.47 ? 154 SER   A OG  1 
ATOM   929  N  N   . ILE   A 1 121 ? 25.761  21.763  -13.833 1.00 32.21 ? 155 ILE   A N   1 
ATOM   930  C  CA  . ILE   A 1 121 ? 24.442  21.558  -14.437 1.00 34.68 ? 155 ILE   A CA  1 
ATOM   931  C  C   . ILE   A 1 121 ? 23.349  21.624  -13.378 1.00 35.80 ? 155 ILE   A C   1 
ATOM   932  O  O   . ILE   A 1 121 ? 22.347  22.336  -13.533 1.00 32.21 ? 155 ILE   A O   1 
ATOM   933  C  CB  . ILE   A 1 121 ? 24.406  20.211  -15.184 1.00 36.85 ? 155 ILE   A CB  1 
ATOM   934  C  CG1 . ILE   A 1 121 ? 25.391  20.213  -16.357 1.00 35.90 ? 155 ILE   A CG1 1 
ATOM   935  C  CG2 . ILE   A 1 121 ? 22.987  19.880  -15.621 1.00 34.91 ? 155 ILE   A CG2 1 
ATOM   936  C  CD1 . ILE   A 1 121 ? 25.874  18.838  -16.752 1.00 32.75 ? 155 ILE   A CD1 1 
ATOM   937  N  N   . SER   A 1 122 ? 23.521  20.862  -12.293 1.00 33.42 ? 156 SER   A N   1 
ATOM   938  C  CA  . SER   A 1 122 ? 22.566  20.889  -11.192 1.00 36.56 ? 156 SER   A CA  1 
ATOM   939  C  C   . SER   A 1 122 ? 22.310  22.311  -10.716 1.00 40.02 ? 156 SER   A C   1 
ATOM   940  O  O   . SER   A 1 122 ? 21.164  22.781  -10.711 1.00 36.09 ? 156 SER   A O   1 
ATOM   941  C  CB  . SER   A 1 122 ? 23.067  20.033  -10.035 1.00 34.62 ? 156 SER   A CB  1 
ATOM   942  O  OG  . SER   A 1 122 ? 22.907  18.668  -10.329 1.00 36.19 ? 156 SER   A OG  1 
ATOM   943  N  N   . VAL   A 1 123 ? 23.378  23.008  -10.303 1.00 37.55 ? 157 VAL   A N   1 
ATOM   944  C  CA  . VAL   A 1 123 ? 23.241  24.390  -9.842  1.00 38.33 ? 157 VAL   A CA  1 
ATOM   945  C  C   . VAL   A 1 123 ? 22.703  25.285  -10.957 1.00 38.32 ? 157 VAL   A C   1 
ATOM   946  O  O   . VAL   A 1 123 ? 21.947  26.228  -10.691 1.00 41.19 ? 157 VAL   A O   1 
ATOM   947  C  CB  . VAL   A 1 123 ? 24.583  24.909  -9.273  1.00 39.48 ? 157 VAL   A CB  1 
ATOM   948  C  CG1 . VAL   A 1 123 ? 24.603  26.401  -9.273  1.00 36.28 ? 157 VAL   A CG1 1 
ATOM   949  C  CG2 . VAL   A 1 123 ? 24.813  24.403  -7.825  1.00 36.85 ? 157 VAL   A CG2 1 
ATOM   950  N  N   . ALA   A 1 124 ? 23.040  24.994  -12.218 1.00 37.90 ? 158 ALA   A N   1 
ATOM   951  C  CA  . ALA   A 1 124 ? 22.449  25.717  -13.345 1.00 39.88 ? 158 ALA   A CA  1 
ATOM   952  C  C   . ALA   A 1 124 ? 21.006  25.317  -13.612 1.00 42.71 ? 158 ALA   A C   1 
ATOM   953  O  O   . ALA   A 1 124 ? 20.398  25.829  -14.560 1.00 38.91 ? 158 ALA   A O   1 
ATOM   954  C  CB  . ALA   A 1 124 ? 23.269  25.507  -14.624 1.00 35.53 ? 158 ALA   A CB  1 
ATOM   955  N  N   . ASN   A 1 125 ? 20.447  24.409  -12.810 1.00 45.64 ? 159 ASN   A N   1 
ATOM   956  C  CA  . ASN   A 1 125 ? 19.073  23.959  -12.995 1.00 40.26 ? 159 ASN   A CA  1 
ATOM   957  C  C   . ASN   A 1 125 ? 18.275  23.980  -11.693 1.00 39.78 ? 159 ASN   A C   1 
ATOM   958  O  O   . ASN   A 1 125 ? 17.292  23.240  -11.566 1.00 36.24 ? 159 ASN   A O   1 
ATOM   959  C  CB  . ASN   A 1 125 ? 19.059  22.564  -13.608 1.00 35.60 ? 159 ASN   A CB  1 
ATOM   960  C  CG  . ASN   A 1 125 ? 19.474  22.573  -15.056 1.00 39.14 ? 159 ASN   A CG  1 
ATOM   961  O  OD1 . ASN   A 1 125 ? 18.631  22.609  -15.953 1.00 42.76 ? 159 ASN   A OD1 1 
ATOM   962  N  ND2 . ASN   A 1 125 ? 20.779  22.547  -15.296 1.00 36.24 ? 159 ASN   A ND2 1 
ATOM   963  N  N   . GLY   A 1 126 ? 18.666  24.813  -10.726 1.00 32.62 ? 160 GLY   A N   1 
ATOM   964  C  CA  . GLY   A 1 126 ? 17.869  25.035  -9.540  1.00 30.38 ? 160 GLY   A CA  1 
ATOM   965  C  C   . GLY   A 1 126 ? 18.449  24.463  -8.267  1.00 32.41 ? 160 GLY   A C   1 
ATOM   966  O  O   . GLY   A 1 126 ? 17.953  24.798  -7.181  1.00 30.46 ? 160 GLY   A O   1 
ATOM   967  N  N   . ALA   A 1 127 ? 19.480  23.623  -8.359  1.00 35.93 ? 161 ALA   A N   1 
ATOM   968  C  CA  . ALA   A 1 127 ? 20.109  23.059  -7.170  1.00 33.29 ? 161 ALA   A CA  1 
ATOM   969  C  C   . ALA   A 1 127 ? 20.771  24.167  -6.357  1.00 30.74 ? 161 ALA   A C   1 
ATOM   970  O  O   . ALA   A 1 127 ? 21.607  24.914  -6.875  1.00 30.09 ? 161 ALA   A O   1 
ATOM   971  C  CB  . ALA   A 1 127 ? 21.128  21.984  -7.555  1.00 24.92 ? 161 ALA   A CB  1 
ATOM   972  N  N   . ILE   A 1 128 ? 20.389  24.277  -5.085  1.00 31.88 ? 162 ILE   A N   1 
ATOM   973  C  CA  . ILE   A 1 128 ? 21.107  25.113  -4.125  1.00 31.62 ? 162 ILE   A CA  1 
ATOM   974  C  C   . ILE   A 1 128 ? 22.407  24.396  -3.785  1.00 31.87 ? 162 ILE   A C   1 
ATOM   975  O  O   . ILE   A 1 128 ? 22.375  23.245  -3.324  1.00 30.50 ? 162 ILE   A O   1 
ATOM   976  C  CB  . ILE   A 1 128 ? 20.273  25.377  -2.860  1.00 30.27 ? 162 ILE   A CB  1 
ATOM   977  C  CG1 . ILE   A 1 128 ? 19.010  26.173  -3.195  1.00 24.14 ? 162 ILE   A CG1 1 
ATOM   978  C  CG2 . ILE   A 1 128 ? 21.101  26.103  -1.815  1.00 23.40 ? 162 ILE   A CG2 1 
ATOM   979  C  CD1 . ILE   A 1 128 ? 17.774  25.623  -2.536  1.00 26.81 ? 162 ILE   A CD1 1 
ATOM   980  N  N   . PRO   A 1 129 ? 23.562  25.013  -4.014  1.00 32.91 ? 163 PRO   A N   1 
ATOM   981  C  CA  . PRO   A 1 129 ? 24.830  24.347  -3.692  1.00 31.87 ? 163 PRO   A CA  1 
ATOM   982  C  C   . PRO   A 1 129 ? 25.029  24.200  -2.197  1.00 30.74 ? 163 PRO   A C   1 
ATOM   983  O  O   . PRO   A 1 129 ? 24.591  25.035  -1.402  1.00 35.86 ? 163 PRO   A O   1 
ATOM   984  C  CB  . PRO   A 1 129 ? 25.879  25.289  -4.288  1.00 30.75 ? 163 PRO   A CB  1 
ATOM   985  C  CG  . PRO   A 1 129 ? 25.214  26.597  -4.294  1.00 32.37 ? 163 PRO   A CG  1 
ATOM   986  C  CD  . PRO   A 1 129 ? 23.783  26.309  -4.658  1.00 28.32 ? 163 PRO   A CD  1 
ATOM   987  N  N   . SER   A 1 130 ? 25.704  23.126  -1.817  1.00 30.81 ? 164 SER   A N   1 
ATOM   988  C  CA  . SER   A 1 130 ? 26.195  22.970  -0.453  1.00 28.16 ? 164 SER   A CA  1 
ATOM   989  C  C   . SER   A 1 130 ? 27.713  22.951  -0.385  1.00 29.96 ? 164 SER   A C   1 
ATOM   990  O  O   . SER   A 1 130 ? 28.300  23.619  0.464   1.00 30.53 ? 164 SER   A O   1 
ATOM   991  C  CB  . SER   A 1 130 ? 25.622  21.686  0.178   1.00 30.57 ? 164 SER   A CB  1 
ATOM   992  O  OG  . SER   A 1 130 ? 26.168  21.464  1.468   1.00 30.90 ? 164 SER   A OG  1 
ATOM   993  N  N   . SER   A 1 131 ? 28.365  22.213  -1.261  1.00 35.78 ? 165 SER   A N   1 
ATOM   994  C  CA  . SER   A 1 131 ? 29.815  22.297  -1.378  1.00 38.46 ? 165 SER   A CA  1 
ATOM   995  C  C   . SER   A 1 131 ? 30.185  22.224  -2.860  1.00 38.48 ? 165 SER   A C   1 
ATOM   996  O  O   . SER   A 1 131 ? 29.910  21.214  -3.521  1.00 35.63 ? 165 SER   A O   1 
ATOM   997  C  CB  . SER   A 1 131 ? 30.486  21.184  -0.571  1.00 32.83 ? 165 SER   A CB  1 
ATOM   998  O  OG  . SER   A 1 131 ? 31.832  21.502  -0.279  1.00 38.05 ? 165 SER   A OG  1 
ATOM   999  N  N   . PRO   A 1 132 ? 30.759  23.280  -3.430  1.00 41.60 ? 166 PRO   A N   1 
ATOM   1000 C  CA  . PRO   A 1 132 ? 31.207  23.211  -4.818  1.00 40.49 ? 166 PRO   A CA  1 
ATOM   1001 C  C   . PRO   A 1 132 ? 32.372  22.248  -4.953  1.00 38.41 ? 166 PRO   A C   1 
ATOM   1002 O  O   . PRO   A 1 132 ? 32.951  21.808  -3.946  1.00 35.19 ? 166 PRO   A O   1 
ATOM   1003 C  CB  . PRO   A 1 132 ? 31.608  24.665  -5.137  1.00 38.20 ? 166 PRO   A CB  1 
ATOM   1004 C  CG  . PRO   A 1 132 ? 31.842  25.301  -3.856  1.00 38.29 ? 166 PRO   A CG  1 
ATOM   1005 C  CD  . PRO   A 1 132 ? 30.949  24.625  -2.859  1.00 41.99 ? 166 PRO   A CD  1 
ATOM   1006 N  N   . PRO   A 1 133 ? 32.734  21.882  -6.179  1.00 37.63 ? 167 PRO   A N   1 
ATOM   1007 C  CA  . PRO   A 1 133 ? 33.650  20.749  -6.379  1.00 34.62 ? 167 PRO   A CA  1 
ATOM   1008 C  C   . PRO   A 1 133 ? 35.027  20.956  -5.765  1.00 37.93 ? 167 PRO   A C   1 
ATOM   1009 O  O   . PRO   A 1 133 ? 35.700  21.965  -6.002  1.00 39.93 ? 167 PRO   A O   1 
ATOM   1010 C  CB  . PRO   A 1 133 ? 33.734  20.643  -7.902  1.00 32.30 ? 167 PRO   A CB  1 
ATOM   1011 C  CG  . PRO   A 1 133 ? 32.422  21.181  -8.359  1.00 34.25 ? 167 PRO   A CG  1 
ATOM   1012 C  CD  . PRO   A 1 133 ? 32.157  22.343  -7.448  1.00 30.13 ? 167 PRO   A CD  1 
ATOM   1013 N  N   . ILE   A 1 134 ? 35.450  19.961  -4.990  1.00 39.86 ? 168 ILE   A N   1 
ATOM   1014 C  CA  . ILE   A 1 134 ? 36.803  19.850  -4.461  1.00 38.87 ? 168 ILE   A CA  1 
ATOM   1015 C  C   . ILE   A 1 134 ? 37.470  18.629  -5.081  1.00 43.55 ? 168 ILE   A C   1 
ATOM   1016 O  O   . ILE   A 1 134 ? 36.854  17.561  -5.195  1.00 43.02 ? 168 ILE   A O   1 
ATOM   1017 C  CB  . ILE   A 1 134 ? 36.780  19.746  -2.927  1.00 39.02 ? 168 ILE   A CB  1 
ATOM   1018 C  CG1 . ILE   A 1 134 ? 36.372  21.099  -2.345  1.00 43.63 ? 168 ILE   A CG1 1 
ATOM   1019 C  CG2 . ILE   A 1 134 ? 38.124  19.280  -2.409  1.00 37.87 ? 168 ILE   A CG2 1 
ATOM   1020 C  CD1 . ILE   A 1 134 ? 35.088  21.048  -1.560  1.00 48.43 ? 168 ILE   A CD1 1 
ATOM   1021 N  N   . VAL   A 1 135 ? 38.723  18.787  -5.493  1.00 43.76 ? 169 VAL   A N   1 
ATOM   1022 C  CA  . VAL   A 1 135 ? 39.471  17.709  -6.128  1.00 43.92 ? 169 VAL   A CA  1 
ATOM   1023 C  C   . VAL   A 1 135 ? 40.447  17.137  -5.108  1.00 46.58 ? 169 VAL   A C   1 
ATOM   1024 O  O   . VAL   A 1 135 ? 41.288  17.867  -4.569  1.00 47.97 ? 169 VAL   A O   1 
ATOM   1025 C  CB  . VAL   A 1 135 ? 40.199  18.194  -7.392  1.00 44.36 ? 169 VAL   A CB  1 
ATOM   1026 C  CG1 . VAL   A 1 135 ? 40.666  17.008  -8.209  1.00 51.24 ? 169 VAL   A CG1 1 
ATOM   1027 C  CG2 . VAL   A 1 135 ? 39.277  19.058  -8.225  1.00 47.02 ? 169 VAL   A CG2 1 
ATOM   1028 N  N   . LEU   A 1 136 ? 40.335  15.831  -4.851  1.00 43.61 ? 170 LEU   A N   1 
ATOM   1029 C  CA  . LEU   A 1 136 ? 41.144  15.121  -3.865  1.00 42.68 ? 170 LEU   A CA  1 
ATOM   1030 C  C   . LEU   A 1 136 ? 42.252  14.342  -4.569  1.00 51.37 ? 170 LEU   A C   1 
ATOM   1031 O  O   . LEU   A 1 136 ? 41.980  13.592  -5.515  1.00 52.02 ? 170 LEU   A O   1 
ATOM   1032 C  CB  . LEU   A 1 136 ? 40.277  14.158  -3.053  1.00 45.50 ? 170 LEU   A CB  1 
ATOM   1033 C  CG  . LEU   A 1 136 ? 39.014  14.637  -2.341  1.00 39.41 ? 170 LEU   A CG  1 
ATOM   1034 C  CD1 . LEU   A 1 136 ? 38.392  13.480  -1.614  1.00 30.41 ? 170 LEU   A CD1 1 
ATOM   1035 C  CD2 . LEU   A 1 136 ? 39.329  15.760  -1.377  1.00 34.88 ? 170 LEU   A CD2 1 
ATOM   1036 N  N   . ASN   A 1 137 ? 43.488  14.473  -4.072  1.00 55.27 ? 171 ASN   A N   1 
ATOM   1037 C  CA  . ASN   A 1 137 ? 44.657  14.001  -4.813  1.00 58.42 ? 171 ASN   A CA  1 
ATOM   1038 C  C   . ASN   A 1 137 ? 44.564  14.587  -6.213  1.00 60.94 ? 171 ASN   A C   1 
ATOM   1039 O  O   . ASN   A 1 137 ? 44.498  15.810  -6.377  1.00 70.54 ? 171 ASN   A O   1 
ATOM   1040 C  CB  . ASN   A 1 137 ? 44.732  12.468  -4.855  1.00 55.13 ? 171 ASN   A CB  1 
ATOM   1041 N  N   . GLU   A 1 138 ? 44.542  13.739  -7.225  1.00 49.65 ? 172 GLU   A N   1 
ATOM   1042 C  CA  . GLU   A 1 138 ? 43.961  14.167  -8.486  1.00 52.57 ? 172 GLU   A CA  1 
ATOM   1043 C  C   . GLU   A 1 138 ? 43.190  13.014  -9.105  1.00 56.84 ? 172 GLU   A C   1 
ATOM   1044 O  O   . GLU   A 1 138 ? 43.078  12.928  -10.331 1.00 50.87 ? 172 GLU   A O   1 
ATOM   1045 C  CB  . GLU   A 1 138 ? 45.017  14.727  -9.456  1.00 54.34 ? 172 GLU   A CB  1 
ATOM   1046 C  CG  . GLU   A 1 138 ? 45.109  16.280  -9.444  1.00 72.46 ? 172 GLU   A CG  1 
ATOM   1047 C  CD  . GLU   A 1 138 ? 44.321  16.981  -10.598 1.00 73.10 ? 172 GLU   A CD  1 
ATOM   1048 O  OE1 . GLU   A 1 138 ? 44.302  18.232  -10.640 1.00 61.02 ? 172 GLU   A OE1 1 
ATOM   1049 O  OE2 . GLU   A 1 138 ? 43.734  16.294  -11.467 1.00 72.47 ? 172 GLU   A OE2 1 
ATOM   1050 N  N   . ALA   A 1 139 ? 42.630  12.136  -8.266  1.00 53.17 ? 173 ALA   A N   1 
ATOM   1051 C  CA  . ALA   A 1 139 ? 41.877  10.968  -8.713  1.00 50.63 ? 173 ALA   A CA  1 
ATOM   1052 C  C   . ALA   A 1 139 ? 40.364  11.139  -8.617  1.00 47.27 ? 173 ALA   A C   1 
ATOM   1053 O  O   . ALA   A 1 139 ? 39.633  10.682  -9.504  1.00 47.55 ? 173 ALA   A O   1 
ATOM   1054 C  CB  . ALA   A 1 139 ? 42.298  9.733   -7.903  1.00 49.33 ? 173 ALA   A CB  1 
ATOM   1055 N  N   . VAL   A 1 140 ? 39.876  11.779  -7.559  1.00 40.01 ? 174 VAL   A N   1 
ATOM   1056 C  CA  . VAL   A 1 140 ? 38.461  11.780  -7.204  1.00 44.89 ? 174 VAL   A CA  1 
ATOM   1057 C  C   . VAL   A 1 140 ? 38.013  13.222  -7.027  1.00 36.65 ? 174 VAL   A C   1 
ATOM   1058 O  O   . VAL   A 1 140 ? 38.764  14.043  -6.492  1.00 44.31 ? 174 VAL   A O   1 
ATOM   1059 C  CB  . VAL   A 1 140 ? 38.220  10.960  -5.908  1.00 44.85 ? 174 VAL   A CB  1 
ATOM   1060 C  CG1 . VAL   A 1 140 ? 36.726  10.779  -5.604  1.00 29.96 ? 174 VAL   A CG1 1 
ATOM   1061 C  CG2 . VAL   A 1 140 ? 38.938  9.612   -5.990  1.00 36.28 ? 174 VAL   A CG2 1 
ATOM   1062 N  N   . THR   A 1 141 ? 36.796  13.537  -7.477  1.00 35.20 ? 175 THR   A N   1 
ATOM   1063 C  CA  . THR   A 1 141 ? 36.192  14.847  -7.239  1.00 46.48 ? 175 THR   A CA  1 
ATOM   1064 C  C   . THR   A 1 141 ? 34.863  14.690  -6.501  1.00 42.02 ? 175 THR   A C   1 
ATOM   1065 O  O   . THR   A 1 141 ? 34.099  13.750  -6.756  1.00 33.07 ? 175 THR   A O   1 
ATOM   1066 C  CB  . THR   A 1 141 ? 36.002  15.653  -8.558  1.00 39.00 ? 175 THR   A CB  1 
ATOM   1067 O  OG1 . THR   A 1 141 ? 37.244  16.255  -8.927  1.00 45.94 ? 175 THR   A OG1 1 
ATOM   1068 C  CG2 . THR   A 1 141 ? 34.992  16.772  -8.391  1.00 38.53 ? 175 THR   A CG2 1 
ATOM   1069 N  N   . ILE   A 1 142 ? 34.600  15.619  -5.579  1.00 39.34 ? 176 ILE   A N   1 
ATOM   1070 C  CA  . ILE   A 1 142 ? 33.441  15.563  -4.704  1.00 36.86 ? 176 ILE   A CA  1 
ATOM   1071 C  C   . ILE   A 1 142 ? 32.739  16.911  -4.754  1.00 35.63 ? 176 ILE   A C   1 
ATOM   1072 O  O   . ILE   A 1 142 ? 33.390  17.954  -4.871  1.00 42.03 ? 176 ILE   A O   1 
ATOM   1073 C  CB  . ILE   A 1 142 ? 33.863  15.183  -3.264  1.00 47.56 ? 176 ILE   A CB  1 
ATOM   1074 C  CG1 . ILE   A 1 142 ? 32.699  14.567  -2.520  1.00 36.18 ? 176 ILE   A CG1 1 
ATOM   1075 C  CG2 . ILE   A 1 142 ? 34.423  16.378  -2.487  1.00 50.15 ? 176 ILE   A CG2 1 
ATOM   1076 C  CD1 . ILE   A 1 142 ? 32.329  13.304  -3.107  1.00 40.46 ? 176 ILE   A CD1 1 
ATOM   1077 N  N   . ALA   A 1 143 ? 31.410  16.887  -4.707  1.00 34.37 ? 177 ALA   A N   1 
ATOM   1078 C  CA  . ALA   A 1 143 ? 30.607  18.104  -4.733  1.00 31.71 ? 177 ALA   A CA  1 
ATOM   1079 C  C   . ALA   A 1 143 ? 29.247  17.792  -4.123  1.00 30.34 ? 177 ALA   A C   1 
ATOM   1080 O  O   . ALA   A 1 143 ? 28.767  16.662  -4.208  1.00 28.79 ? 177 ALA   A O   1 
ATOM   1081 C  CB  . ALA   A 1 143 ? 30.451  18.649  -6.155  1.00 34.31 ? 177 ALA   A CB  1 
ATOM   1082 N  N   . GLU   A 1 144 ? 28.686  18.770  -3.449  1.00 33.32 ? 178 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 144 ? 27.459  18.601  -2.732  1.00 36.32 ? 178 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 144 ? 26.389  19.660  -2.963  1.00 32.67 ? 178 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 144 ? 26.615  20.815  -2.831  1.00 36.65 ? 178 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 144 ? 27.775  18.512  -1.225  1.00 29.86 ? 178 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 144 ? 28.341  17.187  -0.732  1.00 29.87 ? 178 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 144 ? 29.064  17.252  0.598   1.00 27.70 ? 178 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 144 ? 28.527  17.698  1.575   1.00 28.93 ? 178 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 144 ? 30.192  16.846  0.691   1.00 28.27 ? 178 GLU   A OE2 1 
ATOM   1091 N  N   . VAL   A 1 145 ? 25.213  19.238  -3.346  1.00 29.94 ? 179 VAL   A N   1 
ATOM   1092 C  CA  . VAL   A 1 145 ? 24.083  20.141  -3.475  1.00 28.80 ? 179 VAL   A CA  1 
ATOM   1093 C  C   . VAL   A 1 145 ? 23.065  19.758  -2.415  1.00 26.82 ? 179 VAL   A C   1 
ATOM   1094 O  O   . VAL   A 1 145 ? 23.158  18.714  -1.783  1.00 29.90 ? 179 VAL   A O   1 
ATOM   1095 C  CB  . VAL   A 1 145 ? 23.460  20.118  -4.889  1.00 29.31 ? 179 VAL   A CB  1 
ATOM   1096 C  CG1 . VAL   A 1 145 ? 24.453  20.673  -5.929  1.00 27.58 ? 179 VAL   A CG1 1 
ATOM   1097 C  CG2 . VAL   A 1 145 ? 22.992  18.701  -5.258  1.00 26.82 ? 179 VAL   A CG2 1 
ATOM   1098 N  N   . LYS   A 1 146 ? 22.091  20.621  -2.216  1.00 30.46 ? 180 LYS   A N   1 
ATOM   1099 C  CA  . LYS   A 1 146 ? 21.067  20.366  -1.222  1.00 32.08 ? 180 LYS   A CA  1 
ATOM   1100 C  C   . LYS   A 1 146 ? 20.033  19.397  -1.785  1.00 32.74 ? 180 LYS   A C   1 
ATOM   1101 O  O   . LYS   A 1 146 ? 19.654  19.497  -2.955  1.00 31.67 ? 180 LYS   A O   1 
ATOM   1102 C  CB  . LYS   A 1 146 ? 20.403  21.681  -0.806  1.00 32.18 ? 180 LYS   A CB  1 
ATOM   1103 C  CG  . LYS   A 1 146 ? 21.286  22.592  0.043   1.00 31.69 ? 180 LYS   A CG  1 
ATOM   1104 C  CD  . LYS   A 1 146 ? 20.415  23.538  0.861   1.00 34.19 ? 180 LYS   A CD  1 
ATOM   1105 C  CE  . LYS   A 1 146 ? 21.139  24.083  2.086   1.00 38.18 ? 180 LYS   A CE  1 
ATOM   1106 N  NZ  . LYS   A 1 146 ? 20.186  24.841  2.968   1.00 36.47 ? 180 LYS   A NZ  1 
ATOM   1107 N  N   . LEU   A 1 147 ? 19.574  18.459  -0.947  1.00 28.65 ? 181 LEU   A N   1 
ATOM   1108 C  CA  . LEU   A 1 147 ? 18.577  17.472  -1.356  1.00 28.85 ? 181 LEU   A CA  1 
ATOM   1109 C  C   . LEU   A 1 147 ? 17.222  17.760  -0.721  1.00 27.22 ? 181 LEU   A C   1 
ATOM   1110 O  O   . LEU   A 1 147 ? 16.281  18.126  -1.420  1.00 30.72 ? 181 LEU   A O   1 
ATOM   1111 C  CB  . LEU   A 1 147 ? 19.045  16.052  -1.022  1.00 27.86 ? 181 LEU   A CB  1 
ATOM   1112 C  CG  . LEU   A 1 147 ? 18.086  14.968  -1.531  1.00 28.16 ? 181 LEU   A CG  1 
ATOM   1113 C  CD1 . LEU   A 1 147 ? 17.773  15.187  -3.013  1.00 25.65 ? 181 LEU   A CD1 1 
ATOM   1114 C  CD2 . LEU   A 1 147 ? 18.619  13.556  -1.287  1.00 27.82 ? 181 LEU   A CD2 1 
ATOM   1115 N  N   . TYR   A 1 148 ? 17.085  17.543  0.582   1.00 29.64 ? 182 TYR   A N   1 
ATOM   1116 C  CA  . TYR   A 1 148 ? 15.940  17.972  1.372   1.00 27.10 ? 182 TYR   A CA  1 
ATOM   1117 C  C   . TYR   A 1 148 ? 16.422  18.007  2.807   1.00 26.33 ? 182 TYR   A C   1 
ATOM   1118 O  O   . TYR   A 1 148 ? 17.280  17.213  3.189   1.00 24.79 ? 182 TYR   A O   1 
ATOM   1119 C  CB  . TYR   A 1 148 ? 14.716  17.049  1.231   1.00 23.82 ? 182 TYR   A CB  1 
ATOM   1120 C  CG  . TYR   A 1 148 ? 15.032  15.567  1.007   1.00 31.20 ? 182 TYR   A CG  1 
ATOM   1121 C  CD1 . TYR   A 1 148 ? 15.737  14.808  1.961   1.00 28.06 ? 182 TYR   A CD1 1 
ATOM   1122 C  CD2 . TYR   A 1 148 ? 14.605  14.919  -0.152  1.00 24.99 ? 182 TYR   A CD2 1 
ATOM   1123 C  CE1 . TYR   A 1 148 ? 16.018  13.446  1.741   1.00 26.16 ? 182 TYR   A CE1 1 
ATOM   1124 C  CE2 . TYR   A 1 148 ? 14.876  13.580  -0.369  1.00 29.69 ? 182 TYR   A CE2 1 
ATOM   1125 C  CZ  . TYR   A 1 148 ? 15.585  12.846  0.572   1.00 26.65 ? 182 TYR   A CZ  1 
ATOM   1126 O  OH  . TYR   A 1 148 ? 15.829  11.516  0.312   1.00 26.12 ? 182 TYR   A OH  1 
ATOM   1127 N  N   . GLY   A 1 149 ? 15.870  18.935  3.588   1.00 27.69 ? 183 GLY   A N   1 
ATOM   1128 C  CA  . GLY   A 1 149 ? 16.314  19.131  4.958   1.00 25.74 ? 183 GLY   A CA  1 
ATOM   1129 C  C   . GLY   A 1 149 ? 17.770  19.536  4.991   1.00 24.72 ? 183 GLY   A C   1 
ATOM   1130 O  O   . GLY   A 1 149 ? 18.243  20.320  4.167   1.00 26.62 ? 183 GLY   A O   1 
ATOM   1131 N  N   . ASP   A 1 150 ? 18.508  18.982  5.938   1.00 22.50 ? 184 ASP   A N   1 
ATOM   1132 C  CA  . ASP   A 1 150 ? 19.951  19.150  5.937   1.00 24.40 ? 184 ASP   A CA  1 
ATOM   1133 C  C   . ASP   A 1 150 ? 20.658  18.021  5.245   1.00 23.67 ? 184 ASP   A C   1 
ATOM   1134 O  O   . ASP   A 1 150 ? 21.855  17.827  5.481   1.00 26.41 ? 184 ASP   A O   1 
ATOM   1135 C  CB  . ASP   A 1 150 ? 20.477  19.278  7.358   1.00 27.32 ? 184 ASP   A CB  1 
ATOM   1136 C  CG  . ASP   A 1 150 ? 19.862  20.431  8.069   1.00 27.14 ? 184 ASP   A CG  1 
ATOM   1137 O  OD1 . ASP   A 1 150 ? 19.784  21.489  7.426   1.00 23.86 ? 184 ASP   A OD1 1 
ATOM   1138 O  OD2 . ASP   A 1 150 ? 19.447  20.277  9.239   1.00 29.88 ? 184 ASP   A OD2 1 
ATOM   1139 N  N   . VAL   A 1 151 ? 19.944  17.262  4.422   1.00 21.47 ? 185 VAL   A N   1 
ATOM   1140 C  CA  . VAL   A 1 151 ? 20.531  16.172  3.651   1.00 23.78 ? 185 VAL   A CA  1 
ATOM   1141 C  C   . VAL   A 1 151 ? 20.982  16.722  2.307   1.00 23.27 ? 185 VAL   A C   1 
ATOM   1142 O  O   . VAL   A 1 151 ? 20.258  17.469  1.637   1.00 24.83 ? 185 VAL   A O   1 
ATOM   1143 C  CB  . VAL   A 1 151 ? 19.547  14.995  3.467   1.00 22.09 ? 185 VAL   A CB  1 
ATOM   1144 C  CG1 . VAL   A 1 151 ? 20.261  13.814  2.872   1.00 19.61 ? 185 VAL   A CG1 1 
ATOM   1145 C  CG2 . VAL   A 1 151 ? 18.923  14.583  4.771   1.00 22.27 ? 185 VAL   A CG2 1 
ATOM   1146 N  N   . VAL   A 1 152 ? 22.184  16.355  1.922   1.00 24.57 ? 186 VAL   A N   1 
ATOM   1147 C  CA  . VAL   A 1 152 ? 22.770  16.770  0.665   1.00 25.61 ? 186 VAL   A CA  1 
ATOM   1148 C  C   . VAL   A 1 152 ? 22.825  15.540  -0.247  1.00 24.55 ? 186 VAL   A C   1 
ATOM   1149 O  O   . VAL   A 1 152 ? 22.883  14.397  0.215   1.00 20.18 ? 186 VAL   A O   1 
ATOM   1150 C  CB  . VAL   A 1 152 ? 24.159  17.426  0.909   1.00 22.28 ? 186 VAL   A CB  1 
ATOM   1151 C  CG1 . VAL   A 1 152 ? 24.049  18.550  1.916   1.00 20.12 ? 186 VAL   A CG1 1 
ATOM   1152 C  CG2 . VAL   A 1 152 ? 25.174  16.420  1.416   1.00 22.92 ? 186 VAL   A CG2 1 
ATOM   1153 N  N   . LEU   A 1 153 ? 22.734  15.780  -1.553  1.00 26.89 ? 187 LEU   A N   1 
ATOM   1154 C  CA  . LEU   A 1 153 ? 23.041  14.771  -2.558  1.00 26.93 ? 187 LEU   A CA  1 
ATOM   1155 C  C   . LEU   A 1 153 ? 24.491  14.964  -2.978  1.00 27.70 ? 187 LEU   A C   1 
ATOM   1156 O  O   . LEU   A 1 153 ? 24.851  16.034  -3.498  1.00 28.64 ? 187 LEU   A O   1 
ATOM   1157 C  CB  . LEU   A 1 153 ? 22.117  14.900  -3.769  1.00 26.44 ? 187 LEU   A CB  1 
ATOM   1158 C  CG  . LEU   A 1 153 ? 22.294  13.847  -4.856  1.00 21.66 ? 187 LEU   A CG  1 
ATOM   1159 C  CD1 . LEU   A 1 153 ? 21.710  12.529  -4.401  1.00 23.05 ? 187 LEU   A CD1 1 
ATOM   1160 C  CD2 . LEU   A 1 153 ? 21.620  14.309  -6.128  1.00 29.07 ? 187 LEU   A CD2 1 
ATOM   1161 N  N   . ARG   A 1 154 ? 25.317  13.946  -2.748  1.00 22.29 ? 188 ARG   A N   1 
ATOM   1162 C  CA  . ARG   A 1 154 ? 26.758  14.054  -2.948  1.00 25.46 ? 188 ARG   A CA  1 
ATOM   1163 C  C   . ARG   A 1 154 ? 27.185  13.368  -4.239  1.00 30.81 ? 188 ARG   A C   1 
ATOM   1164 O  O   . ARG   A 1 154 ? 26.796  12.225  -4.502  1.00 28.83 ? 188 ARG   A O   1 
ATOM   1165 C  CB  . ARG   A 1 154 ? 27.525  13.453  -1.778  1.00 27.88 ? 188 ARG   A CB  1 
ATOM   1166 C  CG  . ARG   A 1 154 ? 29.014  13.388  -2.016  1.00 26.45 ? 188 ARG   A CG  1 
ATOM   1167 C  CD  . ARG   A 1 154 ? 29.707  12.799  -0.801  1.00 27.25 ? 188 ARG   A CD  1 
ATOM   1168 N  NE  . ARG   A 1 154 ? 29.736  13.713  0.336   1.00 26.74 ? 188 ARG   A NE  1 
ATOM   1169 C  CZ  . ARG   A 1 154 ? 29.772  13.310  1.602   1.00 30.39 ? 188 ARG   A CZ  1 
ATOM   1170 N  NH1 . ARG   A 1 154 ? 29.760  12.015  1.859   1.00 24.77 ? 188 ARG   A NH1 1 
ATOM   1171 N  NH2 . ARG   A 1 154 ? 29.816  14.188  2.605   1.00 28.89 ? 188 ARG   A NH2 1 
ATOM   1172 N  N   . TYR   A 1 155 ? 28.002  14.067  -5.025  1.00 34.17 ? 189 TYR   A N   1 
ATOM   1173 C  CA  . TYR   A 1 155 ? 28.506  13.585  -6.305  1.00 32.68 ? 189 TYR   A CA  1 
ATOM   1174 C  C   . TYR   A 1 155 ? 29.947  13.118  -6.137  1.00 36.40 ? 189 TYR   A C   1 
ATOM   1175 O  O   . TYR   A 1 155 ? 30.821  13.919  -5.777  1.00 36.92 ? 189 TYR   A O   1 
ATOM   1176 C  CB  . TYR   A 1 155 ? 28.442  14.695  -7.352  1.00 31.46 ? 189 TYR   A CB  1 
ATOM   1177 C  CG  . TYR   A 1 155 ? 27.047  15.139  -7.667  1.00 29.81 ? 189 TYR   A CG  1 
ATOM   1178 C  CD1 . TYR   A 1 155 ? 26.037  14.209  -7.789  1.00 31.18 ? 189 TYR   A CD1 1 
ATOM   1179 C  CD2 . TYR   A 1 155 ? 26.739  16.483  -7.854  1.00 27.99 ? 189 TYR   A CD2 1 
ATOM   1180 C  CE1 . TYR   A 1 155 ? 24.755  14.590  -8.091  1.00 33.94 ? 189 TYR   A CE1 1 
ATOM   1181 C  CE2 . TYR   A 1 155 ? 25.450  16.879  -8.148  1.00 30.79 ? 189 TYR   A CE2 1 
ATOM   1182 C  CZ  . TYR   A 1 155 ? 24.459  15.919  -8.270  1.00 32.27 ? 189 TYR   A CZ  1 
ATOM   1183 O  OH  . TYR   A 1 155 ? 23.157  16.256  -8.556  1.00 30.43 ? 189 TYR   A OH  1 
ATOM   1184 N  N   . VAL   A 1 156 ? 30.201  11.838  -6.414  1.00 33.76 ? 190 VAL   A N   1 
ATOM   1185 C  CA  . VAL   A 1 156 ? 31.556  11.302  -6.468  1.00 36.43 ? 190 VAL   A CA  1 
ATOM   1186 C  C   . VAL   A 1 156 ? 31.856  10.899  -7.907  1.00 34.85 ? 190 VAL   A C   1 
ATOM   1187 O  O   . VAL   A 1 156 ? 31.000  10.322  -8.581  1.00 33.67 ? 190 VAL   A O   1 
ATOM   1188 C  CB  . VAL   A 1 156 ? 31.741  10.089  -5.537  1.00 31.86 ? 190 VAL   A CB  1 
ATOM   1189 C  CG1 . VAL   A 1 156 ? 33.203  9.836   -5.322  1.00 33.57 ? 190 VAL   A CG1 1 
ATOM   1190 C  CG2 . VAL   A 1 156 ? 31.020  10.298  -4.243  1.00 36.96 ? 190 VAL   A CG2 1 
ATOM   1191 N  N   . SER   A 1 157 ? 33.074  11.171  -8.371  1.00 35.01 ? 191 SER   A N   1 
ATOM   1192 C  CA  . SER   A 1 157 ? 33.472  10.695  -9.688  1.00 36.04 ? 191 SER   A CA  1 
ATOM   1193 C  C   . SER   A 1 157 ? 34.945  10.334  -9.664  1.00 35.58 ? 191 SER   A C   1 
ATOM   1194 O  O   . SER   A 1 157 ? 35.718  10.794  -8.816  1.00 30.11 ? 191 SER   A O   1 
ATOM   1195 C  CB  . SER   A 1 157 ? 33.184  11.708  -10.813 1.00 34.86 ? 191 SER   A CB  1 
ATOM   1196 O  OG  . SER   A 1 157 ? 33.924  12.909  -10.674 1.00 28.69 ? 191 SER   A OG  1 
ATOM   1197 N  N   . TYR   A 1 158 ? 35.306  9.494   -10.625 1.00 42.17 ? 192 TYR   A N   1 
ATOM   1198 C  CA  . TYR   A 1 158 ? 36.625  8.901   -10.740 1.00 45.67 ? 192 TYR   A CA  1 
ATOM   1199 C  C   . TYR   A 1 158 ? 37.172  9.181   -12.130 1.00 50.37 ? 192 TYR   A C   1 
ATOM   1200 O  O   . TYR   A 1 158 ? 36.420  9.191   -13.112 1.00 61.48 ? 192 TYR   A O   1 
ATOM   1201 C  CB  . TYR   A 1 158 ? 36.566  7.373   -10.476 1.00 50.26 ? 192 TYR   A CB  1 
ATOM   1202 C  CG  . TYR   A 1 158 ? 36.184  7.034   -9.047  1.00 46.23 ? 192 TYR   A CG  1 
ATOM   1203 C  CD1 . TYR   A 1 158 ? 34.858  6.795   -8.687  1.00 44.50 ? 192 TYR   A CD1 1 
ATOM   1204 C  CD2 . TYR   A 1 158 ? 37.151  7.007   -8.044  1.00 44.88 ? 192 TYR   A CD2 1 
ATOM   1205 C  CE1 . TYR   A 1 158 ? 34.514  6.512   -7.360  1.00 44.51 ? 192 TYR   A CE1 1 
ATOM   1206 C  CE2 . TYR   A 1 158 ? 36.821  6.730   -6.726  1.00 43.44 ? 192 TYR   A CE2 1 
ATOM   1207 C  CZ  . TYR   A 1 158 ? 35.506  6.484   -6.384  1.00 46.90 ? 192 TYR   A CZ  1 
ATOM   1208 O  OH  . TYR   A 1 158 ? 35.202  6.218   -5.061  1.00 46.50 ? 192 TYR   A OH  1 
ATOM   1209 N  N   . LYS   A 1 159 ? 38.480  9.436   -12.206 1.00 54.45 ? 193 LYS   A N   1 
ATOM   1210 C  CA  . LYS   A 1 159 ? 39.158  9.436   -13.498 1.00 57.38 ? 193 LYS   A CA  1 
ATOM   1211 C  C   . LYS   A 1 159 ? 39.442  8.004   -13.962 1.00 59.02 ? 193 LYS   A C   1 
ATOM   1212 O  O   . LYS   A 1 159 ? 39.205  7.666   -15.131 1.00 56.30 ? 193 LYS   A O   1 
ATOM   1213 C  CB  . LYS   A 1 159 ? 40.442  10.265  -13.409 1.00 48.76 ? 193 LYS   A CB  1 
ATOM   1214 N  N   . ALA   A 1 160 ? 39.925  7.153   -13.050 1.00 57.04 ? 194 ALA   A N   1 
ATOM   1215 C  CA  . ALA   A 1 160 ? 40.123  5.715   -13.278 1.00 60.99 ? 194 ALA   A CA  1 
ATOM   1216 C  C   . ALA   A 1 160 ? 39.261  4.892   -12.326 1.00 50.47 ? 194 ALA   A C   1 
ATOM   1217 O  O   . ALA   A 1 160 ? 38.077  4.690   -12.572 1.00 53.98 ? 194 ALA   A O   1 
ATOM   1218 C  CB  . ALA   A 1 160 ? 41.590  5.339   -13.106 1.00 60.35 ? 194 ALA   A CB  1 
ATOM   1219 N  N   . PHE   A 1 168 ? 38.353  3.438   -1.113  1.00 42.46 ? 202 PHE   A N   1 
ATOM   1220 C  CA  . PHE   A 1 168 ? 37.190  4.308   -0.955  1.00 36.59 ? 202 PHE   A CA  1 
ATOM   1221 C  C   . PHE   A 1 168 ? 37.480  5.685   -1.515  1.00 38.31 ? 202 PHE   A C   1 
ATOM   1222 O  O   . PHE   A 1 168 ? 37.105  5.973   -2.641  1.00 48.40 ? 202 PHE   A O   1 
ATOM   1223 C  CB  . PHE   A 1 168 ? 36.771  4.425   0.511   1.00 29.03 ? 202 PHE   A CB  1 
ATOM   1224 C  CG  . PHE   A 1 168 ? 35.538  5.274   0.724   1.00 36.04 ? 202 PHE   A CG  1 
ATOM   1225 C  CD1 . PHE   A 1 168 ? 34.377  5.054   -0.018  1.00 32.33 ? 202 PHE   A CD1 1 
ATOM   1226 C  CD2 . PHE   A 1 168 ? 35.540  6.308   1.671   1.00 36.77 ? 202 PHE   A CD2 1 
ATOM   1227 C  CE1 . PHE   A 1 168 ? 33.235  5.840   0.179   1.00 33.48 ? 202 PHE   A CE1 1 
ATOM   1228 C  CE2 . PHE   A 1 168 ? 34.409  7.107   1.873   1.00 32.22 ? 202 PHE   A CE2 1 
ATOM   1229 C  CZ  . PHE   A 1 168 ? 33.252  6.874   1.125   1.00 33.00 ? 202 PHE   A CZ  1 
ATOM   1230 N  N   . LEU   A 1 169 ? 38.133  6.529   -0.719  1.00 36.40 ? 203 LEU   A N   1 
ATOM   1231 C  CA  . LEU   A 1 169 ? 38.529  7.886   -1.084  1.00 42.27 ? 203 LEU   A CA  1 
ATOM   1232 C  C   . LEU   A 1 169 ? 39.962  8.132   -0.630  1.00 44.58 ? 203 LEU   A C   1 
ATOM   1233 O  O   . LEU   A 1 169 ? 40.432  7.495   0.322   1.00 42.57 ? 203 LEU   A O   1 
ATOM   1234 C  CB  . LEU   A 1 169 ? 37.628  8.961   -0.453  1.00 37.64 ? 203 LEU   A CB  1 
ATOM   1235 C  CG  . LEU   A 1 169 ? 36.137  9.005   -0.771  1.00 34.69 ? 203 LEU   A CG  1 
ATOM   1236 C  CD1 . LEU   A 1 169 ? 35.479  10.040  0.102   1.00 29.59 ? 203 LEU   A CD1 1 
ATOM   1237 C  CD2 . LEU   A 1 169 ? 35.882  9.300   -2.230  1.00 40.83 ? 203 LEU   A CD2 1 
ATOM   1238 N  N   . PRO   A 1 170 ? 40.682  9.033   -1.298  1.00 43.88 ? 204 PRO   A N   1 
ATOM   1239 C  CA  . PRO   A 1 170 ? 42.066  9.305   -0.887  1.00 38.32 ? 204 PRO   A CA  1 
ATOM   1240 C  C   . PRO   A 1 170 ? 42.101  9.782   0.552   1.00 39.64 ? 204 PRO   A C   1 
ATOM   1241 O  O   . PRO   A 1 170 ? 41.270  10.588  0.977   1.00 43.91 ? 204 PRO   A O   1 
ATOM   1242 C  CB  . PRO   A 1 170 ? 42.530  10.398  -1.859  1.00 47.29 ? 204 PRO   A CB  1 
ATOM   1243 C  CG  . PRO   A 1 170 ? 41.436  10.551  -2.899  1.00 47.09 ? 204 PRO   A CG  1 
ATOM   1244 C  CD  . PRO   A 1 170 ? 40.381  9.528   -2.657  1.00 42.16 ? 204 PRO   A CD  1 
ATOM   1245 N  N   . GLY   A 1 171 ? 43.055  9.259   1.311   1.00 35.68 ? 205 GLY   A N   1 
ATOM   1246 C  CA  . GLY   A 1 171 ? 43.230  9.638   2.688   1.00 31.59 ? 205 GLY   A CA  1 
ATOM   1247 C  C   . GLY   A 1 171 ? 42.612  8.684   3.685   1.00 32.26 ? 205 GLY   A C   1 
ATOM   1248 O  O   . GLY   A 1 171 ? 42.896  8.791   4.883   1.00 34.81 ? 205 GLY   A O   1 
ATOM   1249 N  N   . PHE   A 1 172 ? 41.765  7.773   3.229   1.00 38.82 ? 206 PHE   A N   1 
ATOM   1250 C  CA  . PHE   A 1 172 ? 41.401  6.618   4.037   1.00 32.53 ? 206 PHE   A CA  1 
ATOM   1251 C  C   . PHE   A 1 172 ? 42.472  5.551   3.890   1.00 32.43 ? 206 PHE   A C   1 
ATOM   1252 O  O   . PHE   A 1 172 ? 43.177  5.487   2.881   1.00 33.64 ? 206 PHE   A O   1 
ATOM   1253 C  CB  . PHE   A 1 172 ? 40.043  6.048   3.610   1.00 29.05 ? 206 PHE   A CB  1 
ATOM   1254 C  CG  . PHE   A 1 172 ? 38.858  6.872   4.047   1.00 29.00 ? 206 PHE   A CG  1 
ATOM   1255 C  CD1 . PHE   A 1 172 ? 38.656  8.147   3.546   1.00 34.67 ? 206 PHE   A CD1 1 
ATOM   1256 C  CD2 . PHE   A 1 172 ? 37.931  6.359   4.929   1.00 27.70 ? 206 PHE   A CD2 1 
ATOM   1257 C  CE1 . PHE   A 1 172 ? 37.570  8.898   3.943   1.00 33.26 ? 206 PHE   A CE1 1 
ATOM   1258 C  CE2 . PHE   A 1 172 ? 36.839  7.101   5.322   1.00 28.67 ? 206 PHE   A CE2 1 
ATOM   1259 C  CZ  . PHE   A 1 172 ? 36.660  8.371   4.829   1.00 32.49 ? 206 PHE   A CZ  1 
ATOM   1260 N  N   . GLU   A 1 173 ? 42.594  4.711   4.910   1.00 40.52 ? 207 GLU   A N   1 
ATOM   1261 C  CA  . GLU   A 1 173 ? 43.405  3.504   4.850   1.00 35.58 ? 207 GLU   A CA  1 
ATOM   1262 C  C   . GLU   A 1 173 ? 42.501  2.283   4.864   1.00 33.39 ? 207 GLU   A C   1 
ATOM   1263 O  O   . GLU   A 1 173 ? 41.391  2.330   5.403   1.00 30.95 ? 207 GLU   A O   1 
ATOM   1264 C  CB  . GLU   A 1 173 ? 44.374  3.430   6.033   1.00 34.50 ? 207 GLU   A CB  1 
ATOM   1265 C  CG  . GLU   A 1 173 ? 45.351  4.587   6.085   1.00 38.54 ? 207 GLU   A CG  1 
ATOM   1266 C  CD  . GLU   A 1 173 ? 46.387  4.447   7.187   1.00 49.69 ? 207 GLU   A CD  1 
ATOM   1267 O  OE1 . GLU   A 1 173 ? 46.223  3.580   8.083   1.00 48.97 ? 207 GLU   A OE1 1 
ATOM   1268 O  OE2 . GLU   A 1 173 ? 47.365  5.225   7.158   1.00 51.87 ? 207 GLU   A OE2 1 
ATOM   1269 N  N   . ARG   A 1 174 ? 42.988  1.197   4.252   1.00 44.45 ? 208 ARG   A N   1 
ATOM   1270 C  CA  . ARG   A 1 174 ? 42.396  -0.126  4.437   1.00 37.18 ? 208 ARG   A CA  1 
ATOM   1271 C  C   . ARG   A 1 174 ? 42.458  -0.512  5.905   1.00 40.13 ? 208 ARG   A C   1 
ATOM   1272 O  O   . ARG   A 1 174 ? 43.464  -0.276  6.581   1.00 39.97 ? 208 ARG   A O   1 
ATOM   1273 C  CB  . ARG   A 1 174 ? 43.152  -1.178  3.618   1.00 39.52 ? 208 ARG   A CB  1 
ATOM   1274 C  CG  . ARG   A 1 174 ? 42.833  -1.246  2.122   1.00 49.22 ? 208 ARG   A CG  1 
ATOM   1275 C  CD  . ARG   A 1 174 ? 42.369  0.078   1.563   1.00 62.25 ? 208 ARG   A CD  1 
ATOM   1276 N  NE  . ARG   A 1 174 ? 42.264  0.165   0.102   1.00 64.35 ? 208 ARG   A NE  1 
ATOM   1277 C  CZ  . ARG   A 1 174 ? 41.798  1.208   -0.563  1.00 52.50 ? 208 ARG   A CZ  1 
ATOM   1278 N  NH1 . ARG   A 1 174 ? 41.395  2.268   0.108   1.00 61.71 ? 208 ARG   A NH1 1 
ATOM   1279 N  NH2 . ARG   A 1 174 ? 41.750  1.173   -1.890  1.00 55.45 ? 208 ARG   A NH2 1 
ATOM   1280 N  N   . VAL   A 1 175 ? 41.397  -1.151  6.394   1.00 43.07 ? 209 VAL   A N   1 
ATOM   1281 C  CA  . VAL   A 1 175 ? 41.453  -1.712  7.737   1.00 42.35 ? 209 VAL   A CA  1 
ATOM   1282 C  C   . VAL   A 1 175 ? 42.404  -2.901  7.762   1.00 47.92 ? 209 VAL   A C   1 
ATOM   1283 O  O   . VAL   A 1 175 ? 42.401  -3.745  6.851   1.00 48.15 ? 209 VAL   A O   1 
ATOM   1284 C  CB  . VAL   A 1 175 ? 40.053  -2.110  8.213   1.00 40.73 ? 209 VAL   A CB  1 
ATOM   1285 C  CG1 . VAL   A 1 175 ? 40.154  -2.757  9.569   1.00 47.56 ? 209 VAL   A CG1 1 
ATOM   1286 C  CG2 . VAL   A 1 175 ? 39.184  -0.878  8.295   1.00 40.85 ? 209 VAL   A CG2 1 
ATOM   1287 N  N   . GLU   A 1 176 ? 43.242  -2.955  8.806   1.00 48.97 ? 210 GLU   A N   1 
ATOM   1288 C  CA  . GLU   A 1 176 ? 44.184  -4.054  9.012   1.00 50.52 ? 210 GLU   A CA  1 
ATOM   1289 C  C   . GLU   A 1 176 ? 43.430  -5.345  9.321   1.00 55.45 ? 210 GLU   A C   1 
ATOM   1290 O  O   . GLU   A 1 176 ? 42.697  -5.414  10.315  1.00 55.46 ? 210 GLU   A O   1 
ATOM   1291 C  CB  . GLU   A 1 176 ? 45.144  -3.719  10.153  1.00 45.80 ? 210 GLU   A CB  1 
ATOM   1292 N  N   . ASP   A 1 177 ? 43.647  -6.370  8.487   1.00 51.79 ? 211 ASP   A N   1 
ATOM   1293 C  CA  . ASP   A 1 177 ? 42.926  -7.641  8.507   1.00 55.74 ? 211 ASP   A CA  1 
ATOM   1294 C  C   . ASP   A 1 177 ? 42.469  -8.094  9.892   1.00 53.45 ? 211 ASP   A C   1 
ATOM   1295 O  O   . ASP   A 1 177 ? 41.307  -8.484  10.061  1.00 52.11 ? 211 ASP   A O   1 
ATOM   1296 C  CB  . ASP   A 1 177 ? 43.791  -8.729  7.861   1.00 56.95 ? 211 ASP   A CB  1 
ATOM   1297 C  CG  . ASP   A 1 177 ? 43.458  -8.942  6.385   1.00 68.79 ? 211 ASP   A CG  1 
ATOM   1298 O  OD1 . ASP   A 1 177 ? 42.254  -9.014  6.047   1.00 64.09 ? 211 ASP   A OD1 1 
ATOM   1299 O  OD2 . ASP   A 1 177 ? 44.394  -9.040  5.561   1.00 69.86 ? 211 ASP   A OD2 1 
ATOM   1300 N  N   . ALA   A 1 178 ? 43.366  -8.038  10.886  1.00 49.70 ? 212 ALA   A N   1 
ATOM   1301 C  CA  . ALA   A 1 178 ? 43.022  -8.487  12.236  1.00 51.33 ? 212 ALA   A CA  1 
ATOM   1302 C  C   . ALA   A 1 178 ? 41.754  -7.814  12.750  1.00 46.57 ? 212 ALA   A C   1 
ATOM   1303 O  O   . ALA   A 1 178 ? 40.880  -8.468  13.329  1.00 45.29 ? 212 ALA   A O   1 
ATOM   1304 C  CB  . ALA   A 1 178 ? 44.189  -8.227  13.195  1.00 45.85 ? 212 ALA   A CB  1 
ATOM   1305 N  N   . SER   A 1 179 ? 41.628  -6.511  12.539  1.00 49.10 ? 213 SER   A N   1 
ATOM   1306 C  CA  . SER   A 1 179 ? 40.402  -5.823  12.910  1.00 51.08 ? 213 SER   A CA  1 
ATOM   1307 C  C   . SER   A 1 179 ? 39.261  -6.068  11.924  1.00 46.29 ? 213 SER   A C   1 
ATOM   1308 O  O   . SER   A 1 179 ? 38.138  -5.632  12.189  1.00 47.46 ? 213 SER   A O   1 
ATOM   1309 C  CB  . SER   A 1 179 ? 40.673  -4.313  13.042  1.00 51.85 ? 213 SER   A CB  1 
ATOM   1310 O  OG  . SER   A 1 179 ? 41.673  -4.030  14.023  1.00 43.25 ? 213 SER   A OG  1 
ATOM   1311 N  N   . SER   A 1 180 ? 39.509  -6.757  10.807  1.00 41.96 ? 214 SER   A N   1 
ATOM   1312 C  CA  . SER   A 1 180 ? 38.556  -6.834  9.702   1.00 41.49 ? 214 SER   A CA  1 
ATOM   1313 C  C   . SER   A 1 180 ? 37.964  -8.234  9.624   1.00 40.82 ? 214 SER   A C   1 
ATOM   1314 O  O   . SER   A 1 180 ? 38.572  -9.143  9.060   1.00 43.78 ? 214 SER   A O   1 
ATOM   1315 C  CB  . SER   A 1 180 ? 39.223  -6.462  8.386   1.00 44.18 ? 214 SER   A CB  1 
ATOM   1316 O  OG  . SER   A 1 180 ? 38.256  -6.375  7.355   1.00 39.00 ? 214 SER   A OG  1 
ATOM   1317 N  N   . PHE   A 1 181 ? 36.759  -8.393  10.156  1.00 38.60 ? 215 PHE   A N   1 
ATOM   1318 C  CA  . PHE   A 1 181 ? 36.108  -9.690  10.183  1.00 37.50 ? 215 PHE   A CA  1 
ATOM   1319 C  C   . PHE   A 1 181 ? 35.195  -9.821  8.973   1.00 35.96 ? 215 PHE   A C   1 
ATOM   1320 O  O   . PHE   A 1 181 ? 34.292  -8.991  8.805   1.00 34.97 ? 215 PHE   A O   1 
ATOM   1321 C  CB  . PHE   A 1 181 ? 35.311  -9.846  11.474  1.00 32.66 ? 215 PHE   A CB  1 
ATOM   1322 C  CG  . PHE   A 1 181 ? 34.888  -11.259 11.766  1.00 37.10 ? 215 PHE   A CG  1 
ATOM   1323 C  CD1 . PHE   A 1 181 ? 33.832  -11.839 11.083  1.00 34.00 ? 215 PHE   A CD1 1 
ATOM   1324 C  CD2 . PHE   A 1 181 ? 35.541  -12.004 12.740  1.00 39.47 ? 215 PHE   A CD2 1 
ATOM   1325 C  CE1 . PHE   A 1 181 ? 33.433  -13.127 11.358  1.00 34.14 ? 215 PHE   A CE1 1 
ATOM   1326 C  CE2 . PHE   A 1 181 ? 35.155  -13.305 13.013  1.00 33.84 ? 215 PHE   A CE2 1 
ATOM   1327 C  CZ  . PHE   A 1 181 ? 34.097  -13.867 12.324  1.00 36.25 ? 215 PHE   A CZ  1 
ATOM   1328 N  N   . PRO   A 1 182 ? 35.360  -10.831 8.124   1.00 34.43 ? 216 PRO   A N   1 
ATOM   1329 C  CA  . PRO   A 1 182 ? 34.554  -10.903 6.897   1.00 36.97 ? 216 PRO   A CA  1 
ATOM   1330 C  C   . PRO   A 1 182 ? 33.092  -11.284 7.131   1.00 36.52 ? 216 PRO   A C   1 
ATOM   1331 O  O   . PRO   A 1 182 ? 32.594  -12.259 6.552   1.00 32.97 ? 216 PRO   A O   1 
ATOM   1332 C  CB  . PRO   A 1 182 ? 35.286  -11.969 6.072   1.00 34.34 ? 216 PRO   A CB  1 
ATOM   1333 C  CG  . PRO   A 1 182 ? 35.945  -12.816 7.077   1.00 36.12 ? 216 PRO   A CG  1 
ATOM   1334 C  CD  . PRO   A 1 182 ? 36.372  -11.895 8.179   1.00 39.81 ? 216 PRO   A CD  1 
ATOM   1335 N  N   . LEU   A 1 183 ? 32.396  -10.506 7.959   1.00 31.08 ? 217 LEU   A N   1 
ATOM   1336 C  CA  . LEU   A 1 183 ? 30.980  -10.737 8.208   1.00 29.83 ? 217 LEU   A CA  1 
ATOM   1337 C  C   . LEU   A 1 183 ? 30.186  -10.620 6.917   1.00 30.90 ? 217 LEU   A C   1 
ATOM   1338 O  O   . LEU   A 1 183 ? 30.560  -9.887  6.004   1.00 42.22 ? 217 LEU   A O   1 
ATOM   1339 C  CB  . LEU   A 1 183 ? 30.439  -9.742  9.238   1.00 28.24 ? 217 LEU   A CB  1 
ATOM   1340 C  CG  . LEU   A 1 183 ? 30.906  -10.040 10.644  1.00 28.74 ? 217 LEU   A CG  1 
ATOM   1341 C  CD1 . LEU   A 1 183 ? 30.472  -8.954  11.586  1.00 28.87 ? 217 LEU   A CD1 1 
ATOM   1342 C  CD2 . LEU   A 1 183 ? 30.315  -11.391 11.077  1.00 28.25 ? 217 LEU   A CD2 1 
ATOM   1343 N  N   . ASP   A 1 184 ? 29.070  -11.341 6.847   1.00 27.35 ? 218 ASP   A N   1 
ATOM   1344 C  CA  . ASP   A 1 184 ? 28.249  -11.311 5.646   1.00 25.54 ? 218 ASP   A CA  1 
ATOM   1345 C  C   . ASP   A 1 184 ? 26.935  -12.050 5.858   1.00 27.05 ? 218 ASP   A C   1 
ATOM   1346 O  O   . ASP   A 1 184 ? 26.903  -13.285 5.914   1.00 34.01 ? 218 ASP   A O   1 
ATOM   1347 C  CB  . ASP   A 1 184 ? 29.013  -11.899 4.466   1.00 24.79 ? 218 ASP   A CB  1 
ATOM   1348 C  CG  . ASP   A 1 184 ? 28.199  -11.904 3.195   1.00 37.70 ? 218 ASP   A CG  1 
ATOM   1349 O  OD1 . ASP   A 1 184 ? 27.142  -11.222 3.152   1.00 30.60 ? 218 ASP   A OD1 1 
ATOM   1350 O  OD2 . ASP   A 1 184 ? 28.611  -12.604 2.236   1.00 42.73 ? 218 ASP   A OD2 1 
ATOM   1351 N  N   . TYR   A 1 185 ? 25.849  -11.293 5.979   1.00 21.67 ? 219 TYR   A N   1 
ATOM   1352 C  CA  . TYR   A 1 185 ? 24.505  -11.836 6.090   1.00 23.29 ? 219 TYR   A CA  1 
ATOM   1353 C  C   . TYR   A 1 185 ? 23.744  -11.750 4.765   1.00 26.94 ? 219 TYR   A C   1 
ATOM   1354 O  O   . TYR   A 1 185 ? 22.533  -11.978 4.749   1.00 24.19 ? 219 TYR   A O   1 
ATOM   1355 C  CB  . TYR   A 1 185 ? 23.705  -11.127 7.199   1.00 21.25 ? 219 TYR   A CB  1 
ATOM   1356 C  CG  . TYR   A 1 185 ? 24.428  -10.901 8.536   1.00 26.76 ? 219 TYR   A CG  1 
ATOM   1357 C  CD1 . TYR   A 1 185 ? 25.602  -11.580 8.858   1.00 29.29 ? 219 TYR   A CD1 1 
ATOM   1358 C  CD2 . TYR   A 1 185 ? 23.913  -10.025 9.489   1.00 24.03 ? 219 TYR   A CD2 1 
ATOM   1359 C  CE1 . TYR   A 1 185 ? 26.252  -11.377 10.072  1.00 25.42 ? 219 TYR   A CE1 1 
ATOM   1360 C  CE2 . TYR   A 1 185 ? 24.561  -9.820  10.716  1.00 24.34 ? 219 TYR   A CE2 1 
ATOM   1361 C  CZ  . TYR   A 1 185 ? 25.736  -10.499 10.990  1.00 25.12 ? 219 TYR   A CZ  1 
ATOM   1362 O  OH  . TYR   A 1 185 ? 26.402  -10.318 12.182  1.00 21.91 ? 219 TYR   A OH  1 
ATOM   1363 N  N   . GLY   A 1 186 ? 24.421  -11.402 3.662   1.00 20.60 ? 220 GLY   A N   1 
ATOM   1364 C  CA  . GLY   A 1 186 ? 23.847  -11.509 2.337   1.00 25.74 ? 220 GLY   A CA  1 
ATOM   1365 C  C   . GLY   A 1 186 ? 23.520  -10.213 1.625   1.00 27.09 ? 220 GLY   A C   1 
ATOM   1366 O  O   . GLY   A 1 186 ? 23.235  -10.261 0.418   1.00 27.57 ? 220 GLY   A O   1 
ATOM   1367 N  N   . ILE   A 1 187 ? 23.549  -9.063  2.312   1.00 26.64 ? 221 ILE   A N   1 
ATOM   1368 C  CA  . ILE   A 1 187 ? 23.146  -7.790  1.709   1.00 26.99 ? 221 ILE   A CA  1 
ATOM   1369 C  C   . ILE   A 1 187 ? 24.173  -7.361  0.662   1.00 27.94 ? 221 ILE   A C   1 
ATOM   1370 O  O   . ILE   A 1 187 ? 25.384  -7.581  0.828   1.00 27.50 ? 221 ILE   A O   1 
ATOM   1371 C  CB  . ILE   A 1 187 ? 22.969  -6.733  2.814   1.00 24.95 ? 221 ILE   A CB  1 
ATOM   1372 C  CG1 . ILE   A 1 187 ? 21.667  -6.966  3.595   1.00 21.21 ? 221 ILE   A CG1 1 
ATOM   1373 C  CG2 . ILE   A 1 187 ? 23.041  -5.310  2.254   1.00 21.30 ? 221 ILE   A CG2 1 
ATOM   1374 C  CD1 . ILE   A 1 187 ? 21.561  -6.138  4.908   1.00 13.25 ? 221 ILE   A CD1 1 
ATOM   1375 N  N   . ARG   A 1 188 ? 23.700  -6.764  -0.440  1.00 21.23 ? 222 ARG   A N   1 
ATOM   1376 C  CA  . ARG   A 1 188 ? 24.597  -6.585  -1.580  1.00 25.11 ? 222 ARG   A CA  1 
ATOM   1377 C  C   . ARG   A 1 188 ? 24.664  -5.170  -2.153  1.00 28.74 ? 222 ARG   A C   1 
ATOM   1378 O  O   . ARG   A 1 188 ? 25.735  -4.768  -2.611  1.00 30.73 ? 222 ARG   A O   1 
ATOM   1379 C  CB  . ARG   A 1 188 ? 24.242  -7.568  -2.706  1.00 28.68 ? 222 ARG   A CB  1 
ATOM   1380 C  CG  . ARG   A 1 188 ? 24.706  -9.018  -2.451  1.00 28.69 ? 222 ARG   A CG  1 
ATOM   1381 C  CD  . ARG   A 1 188 ? 26.134  -9.079  -1.906  1.00 26.73 ? 222 ARG   A CD  1 
ATOM   1382 N  NE  . ARG   A 1 188 ? 26.674  -10.440 -1.815  1.00 30.26 ? 222 ARG   A NE  1 
ATOM   1383 C  CZ  . ARG   A 1 188 ? 26.972  -11.068 -0.676  1.00 34.00 ? 222 ARG   A CZ  1 
ATOM   1384 N  NH1 . ARG   A 1 188 ? 26.773  -10.476 0.493   1.00 36.04 ? 222 ARG   A NH1 1 
ATOM   1385 N  NH2 . ARG   A 1 188 ? 27.468  -12.300 -0.700  1.00 41.07 ? 222 ARG   A NH2 1 
ATOM   1386 N  N   . ARG   A 1 189 ? 23.574  -4.396  -2.147  1.00 31.23 ? 223 ARG   A N   1 
ATOM   1387 C  CA  . ARG   A 1 189 ? 23.651  -3.014  -2.624  1.00 24.82 ? 223 ARG   A CA  1 
ATOM   1388 C  C   . ARG   A 1 189 ? 22.546  -2.179  -1.977  1.00 28.97 ? 223 ARG   A C   1 
ATOM   1389 O  O   . ARG   A 1 189 ? 21.667  -2.711  -1.293  1.00 28.82 ? 223 ARG   A O   1 
ATOM   1390 C  CB  . ARG   A 1 189 ? 23.570  -2.962  -4.153  1.00 27.09 ? 223 ARG   A CB  1 
ATOM   1391 C  CG  . ARG   A 1 189 ? 22.217  -3.323  -4.722  1.00 29.45 ? 223 ARG   A CG  1 
ATOM   1392 C  CD  . ARG   A 1 189 ? 22.261  -3.367  -6.241  1.00 35.24 ? 223 ARG   A CD  1 
ATOM   1393 N  NE  . ARG   A 1 189 ? 20.956  -3.695  -6.825  1.00 40.10 ? 223 ARG   A NE  1 
ATOM   1394 C  CZ  . ARG   A 1 189 ? 20.063  -2.788  -7.232  1.00 43.31 ? 223 ARG   A CZ  1 
ATOM   1395 N  NH1 . ARG   A 1 189 ? 20.326  -1.480  -7.135  1.00 36.38 ? 223 ARG   A NH1 1 
ATOM   1396 N  NH2 . ARG   A 1 189 ? 18.901  -3.188  -7.743  1.00 39.54 ? 223 ARG   A NH2 1 
ATOM   1397 N  N   . LEU   A 1 190 ? 22.615  -0.849  -2.176  1.00 21.86 ? 224 LEU   A N   1 
ATOM   1398 C  CA  . LEU   A 1 190 ? 21.515  0.034   -1.797  1.00 21.02 ? 224 LEU   A CA  1 
ATOM   1399 C  C   . LEU   A 1 190 ? 20.519  0.102   -2.953  1.00 26.64 ? 224 LEU   A C   1 
ATOM   1400 O  O   . LEU   A 1 190 ? 20.910  0.327   -4.104  1.00 29.04 ? 224 LEU   A O   1 
ATOM   1401 C  CB  . LEU   A 1 190 ? 22.006  1.443   -1.430  1.00 22.66 ? 224 LEU   A CB  1 
ATOM   1402 C  CG  . LEU   A 1 190 ? 20.942  2.517   -1.081  1.00 20.65 ? 224 LEU   A CG  1 
ATOM   1403 C  CD1 . LEU   A 1 190 ? 20.241  2.264   0.274   1.00 17.86 ? 224 LEU   A CD1 1 
ATOM   1404 C  CD2 . LEU   A 1 190 ? 21.494  3.922   -1.129  1.00 18.72 ? 224 LEU   A CD2 1 
ATOM   1405 N  N   . ASP   A 1 191 ? 19.235  -0.096  -2.649  1.00 27.87 ? 225 ASP   A N   1 
ATOM   1406 C  CA  . ASP   A 1 191 ? 18.217  -0.163  -3.692  1.00 26.19 ? 225 ASP   A CA  1 
ATOM   1407 C  C   . ASP   A 1 191 ? 17.420  1.117   -3.821  1.00 27.26 ? 225 ASP   A C   1 
ATOM   1408 O  O   . ASP   A 1 191 ? 17.240  1.614   -4.937  1.00 33.46 ? 225 ASP   A O   1 
ATOM   1409 C  CB  . ASP   A 1 191 ? 17.252  -1.311  -3.446  1.00 27.19 ? 225 ASP   A CB  1 
ATOM   1410 C  CG  . ASP   A 1 191 ? 16.151  -1.358  -4.460  1.00 27.37 ? 225 ASP   A CG  1 
ATOM   1411 O  OD1 . ASP   A 1 191 ? 16.240  -2.184  -5.399  1.00 27.51 ? 225 ASP   A OD1 1 
ATOM   1412 O  OD2 . ASP   A 1 191 ? 15.186  -0.582  -4.305  1.00 29.99 ? 225 ASP   A OD2 1 
ATOM   1413 N  N   . HIS   A 1 192 ? 16.900  1.647   -2.721  1.00 26.29 ? 226 HIS   A N   1 
ATOM   1414 C  CA  . HIS   A 1 192 ? 16.391  3.001   -2.792  1.00 26.25 ? 226 HIS   A CA  1 
ATOM   1415 C  C   . HIS   A 1 192 ? 16.720  3.762   -1.513  1.00 28.76 ? 226 HIS   A C   1 
ATOM   1416 O  O   . HIS   A 1 192 ? 17.131  3.187   -0.499  1.00 29.74 ? 226 HIS   A O   1 
ATOM   1417 C  CB  . HIS   A 1 192 ? 14.889  3.035   -3.139  1.00 25.88 ? 226 HIS   A CB  1 
ATOM   1418 C  CG  . HIS   A 1 192 ? 14.016  2.123   -2.335  1.00 24.48 ? 226 HIS   A CG  1 
ATOM   1419 N  ND1 . HIS   A 1 192 ? 13.731  0.834   -2.723  1.00 26.75 ? 226 HIS   A ND1 1 
ATOM   1420 C  CD2 . HIS   A 1 192 ? 13.272  2.354   -1.228  1.00 27.81 ? 226 HIS   A CD2 1 
ATOM   1421 C  CE1 . HIS   A 1 192 ? 12.890  0.293   -1.860  1.00 28.71 ? 226 HIS   A CE1 1 
ATOM   1422 N  NE2 . HIS   A 1 192 ? 12.600  1.195   -0.940  1.00 27.18 ? 226 HIS   A NE2 1 
ATOM   1423 N  N   . ALA   A 1 193 ? 16.589  5.090   -1.606  1.00 29.36 ? 227 ALA   A N   1 
ATOM   1424 C  CA  . ALA   A 1 193 ? 16.808  6.011   -0.502  1.00 25.29 ? 227 ALA   A CA  1 
ATOM   1425 C  C   . ALA   A 1 193 ? 15.636  6.976   -0.459  1.00 24.89 ? 227 ALA   A C   1 
ATOM   1426 O  O   . ALA   A 1 193 ? 15.332  7.618   -1.465  1.00 35.14 ? 227 ALA   A O   1 
ATOM   1427 C  CB  . ALA   A 1 193 ? 18.128  6.764   -0.676  1.00 25.35 ? 227 ALA   A CB  1 
ATOM   1428 N  N   . VAL   A 1 194 ? 14.977  7.079   0.688   1.00 22.32 ? 228 VAL   A N   1 
ATOM   1429 C  CA  . VAL   A 1 194 ? 13.673  7.725   0.779   1.00 27.98 ? 228 VAL   A CA  1 
ATOM   1430 C  C   . VAL   A 1 194 ? 13.740  8.888   1.768   1.00 35.00 ? 228 VAL   A C   1 
ATOM   1431 O  O   . VAL   A 1 194 ? 14.307  8.759   2.862   1.00 32.11 ? 228 VAL   A O   1 
ATOM   1432 C  CB  . VAL   A 1 194 ? 12.583  6.706   1.182   1.00 26.70 ? 228 VAL   A CB  1 
ATOM   1433 C  CG1 . VAL   A 1 194 ? 11.233  7.373   1.311   1.00 23.73 ? 228 VAL   A CG1 1 
ATOM   1434 C  CG2 . VAL   A 1 194 ? 12.527  5.573   0.160   1.00 26.64 ? 228 VAL   A CG2 1 
ATOM   1435 N  N   . GLY   A 1 195 ? 13.166  10.032  1.375   1.00 27.49 ? 229 GLY   A N   1 
ATOM   1436 C  CA  . GLY   A 1 195 ? 13.061  11.189  2.240   1.00 27.15 ? 229 GLY   A CA  1 
ATOM   1437 C  C   . GLY   A 1 195 ? 11.628  11.416  2.685   1.00 30.60 ? 229 GLY   A C   1 
ATOM   1438 O  O   . GLY   A 1 195 ? 10.681  10.996  2.016   1.00 29.93 ? 229 GLY   A O   1 
ATOM   1439 N  N   . ASN   A 1 196 ? 11.472  12.053  3.840   1.00 25.54 ? 230 ASN   A N   1 
ATOM   1440 C  CA  . ASN   A 1 196 ? 10.196  12.603  4.268   1.00 26.58 ? 230 ASN   A CA  1 
ATOM   1441 C  C   . ASN   A 1 196 ? 10.280  14.122  4.165   1.00 31.75 ? 230 ASN   A C   1 
ATOM   1442 O  O   . ASN   A 1 196 ? 11.250  14.725  4.643   1.00 26.65 ? 230 ASN   A O   1 
ATOM   1443 C  CB  . ASN   A 1 196 ? 9.859   12.214  5.709   1.00 25.34 ? 230 ASN   A CB  1 
ATOM   1444 C  CG  . ASN   A 1 196 ? 9.332   10.807  5.854   1.00 26.52 ? 230 ASN   A CG  1 
ATOM   1445 O  OD1 . ASN   A 1 196 ? 8.997   10.122  4.882   1.00 28.27 ? 230 ASN   A OD1 1 
ATOM   1446 N  ND2 . ASN   A 1 196 ? 9.221   10.376  7.098   1.00 27.35 ? 230 ASN   A ND2 1 
ATOM   1447 N  N   . VAL   A 1 197 ? 9.278   14.733  3.539   1.00 30.26 ? 231 VAL   A N   1 
ATOM   1448 C  CA  . VAL   A 1 197 ? 9.187   16.192  3.489   1.00 30.70 ? 231 VAL   A CA  1 
ATOM   1449 C  C   . VAL   A 1 197 ? 7.757   16.583  3.830   1.00 34.99 ? 231 VAL   A C   1 
ATOM   1450 O  O   . VAL   A 1 197 ? 6.834   15.752  3.748   1.00 32.30 ? 231 VAL   A O   1 
ATOM   1451 C  CB  . VAL   A 1 197 ? 9.618   16.756  2.109   1.00 30.25 ? 231 VAL   A CB  1 
ATOM   1452 C  CG1 . VAL   A 1 197 ? 11.070  16.370  1.766   1.00 20.94 ? 231 VAL   A CG1 1 
ATOM   1453 C  CG2 . VAL   A 1 197 ? 8.637   16.353  1.002   1.00 28.47 ? 231 VAL   A CG2 1 
ATOM   1454 N  N   . PRO   A 1 198 ? 7.542   17.833  4.271   1.00 34.68 ? 232 PRO   A N   1 
ATOM   1455 C  CA  . PRO   A 1 198 ? 6.170   18.268  4.585   1.00 29.91 ? 232 PRO   A CA  1 
ATOM   1456 C  C   . PRO   A 1 198 ? 5.351   18.633  3.365   1.00 31.53 ? 232 PRO   A C   1 
ATOM   1457 O  O   . PRO   A 1 198 ? 4.114   18.578  3.429   1.00 27.84 ? 232 PRO   A O   1 
ATOM   1458 C  CB  . PRO   A 1 198 ? 6.380   19.483  5.499   1.00 29.28 ? 232 PRO   A CB  1 
ATOM   1459 C  CG  . PRO   A 1 198 ? 7.773   19.925  5.256   1.00 30.58 ? 232 PRO   A CG  1 
ATOM   1460 C  CD  . PRO   A 1 198 ? 8.564   18.737  4.833   1.00 29.08 ? 232 PRO   A CD  1 
ATOM   1461 N  N   . GLU   A 1 199 ? 5.989   19.004  2.259   1.00 35.82 ? 233 GLU   A N   1 
ATOM   1462 C  CA  . GLU   A 1 199 ? 5.289   19.231  1.000   1.00 33.98 ? 233 GLU   A CA  1 
ATOM   1463 C  C   . GLU   A 1 199 ? 6.004   18.475  -0.110  1.00 30.19 ? 233 GLU   A C   1 
ATOM   1464 O  O   . GLU   A 1 199 ? 7.146   18.798  -0.455  1.00 29.55 ? 233 GLU   A O   1 
ATOM   1465 C  CB  . GLU   A 1 199 ? 5.190   20.714  0.672   1.00 28.43 ? 233 GLU   A CB  1 
ATOM   1466 C  CG  . GLU   A 1 199 ? 4.551   21.516  1.738   1.00 29.82 ? 233 GLU   A CG  1 
ATOM   1467 C  CD  . GLU   A 1 199 ? 5.591   22.140  2.635   1.00 40.29 ? 233 GLU   A CD  1 
ATOM   1468 O  OE1 . GLU   A 1 199 ? 6.744   22.298  2.158   1.00 32.29 ? 233 GLU   A OE1 1 
ATOM   1469 O  OE2 . GLU   A 1 199 ? 5.257   22.469  3.805   1.00 41.45 ? 233 GLU   A OE2 1 
ATOM   1470 N  N   . LEU   A 1 200 ? 5.312   17.492  -0.684  1.00 33.83 ? 234 LEU   A N   1 
ATOM   1471 C  CA  . LEU   A 1 200 ? 5.893   16.701  -1.767  1.00 37.88 ? 234 LEU   A CA  1 
ATOM   1472 C  C   . LEU   A 1 200 ? 6.160   17.565  -2.990  1.00 31.67 ? 234 LEU   A C   1 
ATOM   1473 O  O   . LEU   A 1 200 ? 7.272   17.557  -3.532  1.00 29.56 ? 234 LEU   A O   1 
ATOM   1474 C  CB  . LEU   A 1 200 ? 4.969   15.533  -2.121  1.00 34.53 ? 234 LEU   A CB  1 
ATOM   1475 C  CG  . LEU   A 1 200 ? 5.423   14.618  -3.255  1.00 42.71 ? 234 LEU   A CG  1 
ATOM   1476 C  CD1 . LEU   A 1 200 ? 6.777   13.955  -2.934  1.00 34.53 ? 234 LEU   A CD1 1 
ATOM   1477 C  CD2 . LEU   A 1 200 ? 4.341   13.578  -3.557  1.00 37.98 ? 234 LEU   A CD2 1 
ATOM   1478 N  N   . GLY   A 1 201 ? 5.150   18.336  -3.415  1.00 33.50 ? 235 GLY   A N   1 
ATOM   1479 C  CA  . GLY   A 1 201 ? 5.172   19.139  -4.624  1.00 30.51 ? 235 GLY   A CA  1 
ATOM   1480 C  C   . GLY   A 1 201 ? 6.408   19.993  -4.856  1.00 29.23 ? 235 GLY   A C   1 
ATOM   1481 O  O   . GLY   A 1 201 ? 7.105   19.837  -5.858  1.00 30.36 ? 235 GLY   A O   1 
ATOM   1482 N  N   . PRO   A 1 202 ? 6.701   20.928  -3.953  1.00 29.17 ? 236 PRO   A N   1 
ATOM   1483 C  CA  . PRO   A 1 202 ? 7.958   21.681  -4.105  1.00 29.38 ? 236 PRO   A CA  1 
ATOM   1484 C  C   . PRO   A 1 202 ? 9.186   20.785  -4.151  1.00 29.15 ? 236 PRO   A C   1 
ATOM   1485 O  O   . PRO   A 1 202 ? 10.115  21.046  -4.919  1.00 29.09 ? 236 PRO   A O   1 
ATOM   1486 C  CB  . PRO   A 1 202 ? 7.971   22.602  -2.873  1.00 30.35 ? 236 PRO   A CB  1 
ATOM   1487 C  CG  . PRO   A 1 202 ? 6.561   22.658  -2.407  1.00 33.12 ? 236 PRO   A CG  1 
ATOM   1488 C  CD  . PRO   A 1 202 ? 5.943   21.339  -2.759  1.00 32.47 ? 236 PRO   A CD  1 
ATOM   1489 N  N   . ALA   A 1 203 ? 9.209   19.721  -3.345  1.00 32.16 ? 237 ALA   A N   1 
ATOM   1490 C  CA  . ALA   A 1 203 ? 10.397  18.884  -3.257  1.00 27.81 ? 237 ALA   A CA  1 
ATOM   1491 C  C   . ALA   A 1 203 ? 10.582  18.058  -4.524  1.00 33.51 ? 237 ALA   A C   1 
ATOM   1492 O  O   . ALA   A 1 203 ? 11.703  17.917  -5.029  1.00 31.54 ? 237 ALA   A O   1 
ATOM   1493 C  CB  . ALA   A 1 203 ? 10.307  17.989  -2.022  1.00 31.72 ? 237 ALA   A CB  1 
ATOM   1494 N  N   . LEU   A 1 204 ? 9.493   17.519  -5.068  1.00 34.14 ? 238 LEU   A N   1 
ATOM   1495 C  CA  . LEU   A 1 204 ? 9.613   16.737  -6.289  1.00 33.77 ? 238 LEU   A CA  1 
ATOM   1496 C  C   . LEU   A 1 204 ? 9.964   17.626  -7.483  1.00 33.30 ? 238 LEU   A C   1 
ATOM   1497 O  O   . LEU   A 1 204 ? 10.667  17.188  -8.404  1.00 33.03 ? 238 LEU   A O   1 
ATOM   1498 C  CB  . LEU   A 1 204 ? 8.315   15.958  -6.523  1.00 33.07 ? 238 LEU   A CB  1 
ATOM   1499 C  CG  . LEU   A 1 204 ? 8.391   14.628  -7.291  1.00 40.05 ? 238 LEU   A CG  1 
ATOM   1500 C  CD1 . LEU   A 1 204 ? 9.270   13.586  -6.592  1.00 28.39 ? 238 LEU   A CD1 1 
ATOM   1501 C  CD2 . LEU   A 1 204 ? 6.980   14.085  -7.511  1.00 49.46 ? 238 LEU   A CD2 1 
ATOM   1502 N  N   . THR   A 1 205 ? 9.508   18.879  -7.475  1.00 31.18 ? 239 THR   A N   1 
ATOM   1503 C  CA  . THR   A 1 205 ? 9.853   19.798  -8.554  1.00 32.35 ? 239 THR   A CA  1 
ATOM   1504 C  C   . THR   A 1 205 ? 11.317  20.211  -8.470  1.00 29.14 ? 239 THR   A C   1 
ATOM   1505 O  O   . THR   A 1 205 ? 12.047  20.151  -9.463  1.00 31.23 ? 239 THR   A O   1 
ATOM   1506 C  CB  . THR   A 1 205 ? 8.944   21.028  -8.502  1.00 33.70 ? 239 THR   A CB  1 
ATOM   1507 O  OG1 . THR   A 1 205 ? 7.576   20.608  -8.512  1.00 37.05 ? 239 THR   A OG1 1 
ATOM   1508 C  CG2 . THR   A 1 205 ? 9.194   21.930  -9.700  1.00 30.75 ? 239 THR   A CG2 1 
ATOM   1509 N  N   . TYR   A 1 206 ? 11.759  20.628  -7.283  1.00 27.02 ? 240 TYR   A N   1 
ATOM   1510 C  CA  . TYR   A 1 206 ? 13.152  21.008  -7.056  1.00 26.35 ? 240 TYR   A CA  1 
ATOM   1511 C  C   . TYR   A 1 206 ? 14.120  19.921  -7.524  1.00 30.37 ? 240 TYR   A C   1 
ATOM   1512 O  O   . TYR   A 1 206 ? 15.030  20.181  -8.323  1.00 27.02 ? 240 TYR   A O   1 
ATOM   1513 C  CB  . TYR   A 1 206 ? 13.345  21.316  -5.560  1.00 22.38 ? 240 TYR   A CB  1 
ATOM   1514 C  CG  . TYR   A 1 206 ? 14.777  21.508  -5.122  1.00 26.30 ? 240 TYR   A CG  1 
ATOM   1515 C  CD1 . TYR   A 1 206 ? 15.518  22.588  -5.568  1.00 28.86 ? 240 TYR   A CD1 1 
ATOM   1516 C  CD2 . TYR   A 1 206 ? 15.392  20.614  -4.250  1.00 31.26 ? 240 TYR   A CD2 1 
ATOM   1517 C  CE1 . TYR   A 1 206 ? 16.836  22.780  -5.170  1.00 30.42 ? 240 TYR   A CE1 1 
ATOM   1518 C  CE2 . TYR   A 1 206 ? 16.724  20.795  -3.844  1.00 32.49 ? 240 TYR   A CE2 1 
ATOM   1519 C  CZ  . TYR   A 1 206 ? 17.444  21.884  -4.315  1.00 33.84 ? 240 TYR   A CZ  1 
ATOM   1520 O  OH  . TYR   A 1 206 ? 18.762  22.094  -3.928  1.00 30.67 ? 240 TYR   A OH  1 
ATOM   1521 N  N   . VAL   A 1 207 ? 13.918  18.685  -7.043  1.00 30.90 ? 241 VAL   A N   1 
ATOM   1522 C  CA  . VAL   A 1 207 ? 14.881  17.603  -7.238  1.00 26.70 ? 241 VAL   A CA  1 
ATOM   1523 C  C   . VAL   A 1 207 ? 14.832  17.068  -8.670  1.00 26.98 ? 241 VAL   A C   1 
ATOM   1524 O  O   . VAL   A 1 207 ? 15.875  16.805  -9.279  1.00 25.39 ? 241 VAL   A O   1 
ATOM   1525 C  CB  . VAL   A 1 207 ? 14.635  16.488  -6.201  1.00 26.57 ? 241 VAL   A CB  1 
ATOM   1526 C  CG1 . VAL   A 1 207 ? 15.530  15.291  -6.480  1.00 26.09 ? 241 VAL   A CG1 1 
ATOM   1527 C  CG2 . VAL   A 1 207 ? 14.840  16.998  -4.780  1.00 26.37 ? 241 VAL   A CG2 1 
ATOM   1528 N  N   . ALA   A 1 208 ? 13.628  16.873  -9.223  1.00 26.70 ? 242 ALA   A N   1 
ATOM   1529 C  CA  . ALA   A 1 208 ? 13.521  16.472  -10.624 1.00 28.35 ? 242 ALA   A CA  1 
ATOM   1530 C  C   . ALA   A 1 208 ? 14.030  17.569  -11.543 1.00 32.66 ? 242 ALA   A C   1 
ATOM   1531 O  O   . ALA   A 1 208 ? 14.570  17.282  -12.622 1.00 30.41 ? 242 ALA   A O   1 
ATOM   1532 C  CB  . ALA   A 1 208 ? 12.076  16.124  -10.971 1.00 24.53 ? 242 ALA   A CB  1 
ATOM   1533 N  N   . GLY   A 1 209 ? 13.881  18.823  -11.108 1.00 31.94 ? 243 GLY   A N   1 
ATOM   1534 C  CA  . GLY   A 1 209 ? 14.342  19.951  -11.898 1.00 30.03 ? 243 GLY   A CA  1 
ATOM   1535 C  C   . GLY   A 1 209 ? 15.840  19.940  -12.136 1.00 35.19 ? 243 GLY   A C   1 
ATOM   1536 O  O   . GLY   A 1 209 ? 16.293  20.111  -13.269 1.00 38.64 ? 243 GLY   A O   1 
ATOM   1537 N  N   . PHE   A 1 210 ? 16.635  19.741  -11.081 1.00 32.74 ? 244 PHE   A N   1 
ATOM   1538 C  CA  . PHE   A 1 210 ? 18.081  19.814  -11.278 1.00 34.39 ? 244 PHE   A CA  1 
ATOM   1539 C  C   . PHE   A 1 210 ? 18.723  18.472  -11.612 1.00 36.06 ? 244 PHE   A C   1 
ATOM   1540 O  O   . PHE   A 1 210 ? 19.930  18.431  -11.873 1.00 41.54 ? 244 PHE   A O   1 
ATOM   1541 C  CB  . PHE   A 1 210 ? 18.786  20.462  -10.067 1.00 33.20 ? 244 PHE   A CB  1 
ATOM   1542 C  CG  . PHE   A 1 210 ? 18.863  19.601  -8.835  1.00 30.69 ? 244 PHE   A CG  1 
ATOM   1543 C  CD1 . PHE   A 1 210 ? 17.991  19.813  -7.771  1.00 33.47 ? 244 PHE   A CD1 1 
ATOM   1544 C  CD2 . PHE   A 1 210 ? 19.845  18.635  -8.701  1.00 32.11 ? 244 PHE   A CD2 1 
ATOM   1545 C  CE1 . PHE   A 1 210 ? 18.070  19.042  -6.616  1.00 31.00 ? 244 PHE   A CE1 1 
ATOM   1546 C  CE2 . PHE   A 1 210 ? 19.935  17.860  -7.551  1.00 32.42 ? 244 PHE   A CE2 1 
ATOM   1547 C  CZ  . PHE   A 1 210 ? 19.050  18.062  -6.505  1.00 28.38 ? 244 PHE   A CZ  1 
ATOM   1548 N  N   . THR   A 1 211 ? 17.971  17.382  -11.648 1.00 28.20 ? 245 THR   A N   1 
ATOM   1549 C  CA  . THR   A 1 211 ? 18.556  16.126  -12.099 1.00 33.96 ? 245 THR   A CA  1 
ATOM   1550 C  C   . THR   A 1 211 ? 18.056  15.693  -13.460 1.00 33.19 ? 245 THR   A C   1 
ATOM   1551 O  O   . THR   A 1 211 ? 18.816  15.123  -14.242 1.00 35.18 ? 245 THR   A O   1 
ATOM   1552 C  CB  . THR   A 1 211 ? 18.278  14.992  -11.093 1.00 35.45 ? 245 THR   A CB  1 
ATOM   1553 O  OG1 . THR   A 1 211 ? 16.859  14.775  -10.976 1.00 33.71 ? 245 THR   A OG1 1 
ATOM   1554 C  CG2 . THR   A 1 211 ? 18.874  15.321  -9.729  1.00 29.43 ? 245 THR   A CG2 1 
ATOM   1555 N  N   . GLY   A 1 212 ? 16.792  15.949  -13.758 1.00 33.79 ? 246 GLY   A N   1 
ATOM   1556 C  CA  . GLY   A 1 212 ? 16.175  15.279  -14.870 1.00 36.10 ? 246 GLY   A CA  1 
ATOM   1557 C  C   . GLY   A 1 212 ? 15.729  13.867  -14.581 1.00 30.60 ? 246 GLY   A C   1 
ATOM   1558 O  O   . GLY   A 1 212 ? 15.361  13.155  -15.515 1.00 34.37 ? 246 GLY   A O   1 
ATOM   1559 N  N   . PHE   A 1 213 ? 15.759  13.433  -13.324 1.00 35.00 ? 247 PHE   A N   1 
ATOM   1560 C  CA  . PHE   A 1 213 ? 15.204  12.131  -12.980 1.00 33.73 ? 247 PHE   A CA  1 
ATOM   1561 C  C   . PHE   A 1 213 ? 13.720  12.104  -13.321 1.00 36.37 ? 247 PHE   A C   1 
ATOM   1562 O  O   . PHE   A 1 213 ? 13.023  13.117  -13.230 1.00 36.64 ? 247 PHE   A O   1 
ATOM   1563 C  CB  . PHE   A 1 213 ? 15.403  11.824  -11.494 1.00 30.82 ? 247 PHE   A CB  1 
ATOM   1564 C  CG  . PHE   A 1 213 ? 16.818  11.468  -11.122 1.00 30.48 ? 247 PHE   A CG  1 
ATOM   1565 C  CD1 . PHE   A 1 213 ? 17.821  11.448  -12.074 1.00 29.55 ? 247 PHE   A CD1 1 
ATOM   1566 C  CD2 . PHE   A 1 213 ? 17.139  11.130  -9.816  1.00 28.95 ? 247 PHE   A CD2 1 
ATOM   1567 C  CE1 . PHE   A 1 213 ? 19.119  11.106  -11.729 1.00 31.81 ? 247 PHE   A CE1 1 
ATOM   1568 C  CE2 . PHE   A 1 213 ? 18.437  10.801  -9.468  1.00 28.66 ? 247 PHE   A CE2 1 
ATOM   1569 C  CZ  . PHE   A 1 213 ? 19.430  10.780  -10.430 1.00 25.81 ? 247 PHE   A CZ  1 
ATOM   1570 N  N   . HIS   A 1 214 ? 13.231  10.945  -13.731 1.00 36.01 ? 248 HIS   A N   1 
ATOM   1571 C  CA  . HIS   A 1 214 ? 11.840  10.865  -14.142 1.00 38.44 ? 248 HIS   A CA  1 
ATOM   1572 C  C   . HIS   A 1 214 ? 11.000  10.185  -13.072 1.00 37.84 ? 248 HIS   A C   1 
ATOM   1573 O  O   . HIS   A 1 214 ? 11.514  9.464   -12.214 1.00 39.41 ? 248 HIS   A O   1 
ATOM   1574 C  CB  . HIS   A 1 214 ? 11.710  10.116  -15.466 1.00 43.03 ? 248 HIS   A CB  1 
ATOM   1575 C  CG  . HIS   A 1 214 ? 12.274  8.735   -15.422 1.00 45.13 ? 248 HIS   A CG  1 
ATOM   1576 N  ND1 . HIS   A 1 214 ? 13.630  8.491   -15.375 1.00 39.18 ? 248 HIS   A ND1 1 
ATOM   1577 C  CD2 . HIS   A 1 214 ? 11.669  7.524   -15.403 1.00 43.44 ? 248 HIS   A CD2 1 
ATOM   1578 C  CE1 . HIS   A 1 214 ? 13.834  7.188   -15.331 1.00 35.04 ? 248 HIS   A CE1 1 
ATOM   1579 N  NE2 . HIS   A 1 214 ? 12.663  6.579   -15.353 1.00 40.96 ? 248 HIS   A NE2 1 
ATOM   1580 N  N   . GLN   A 1 215 ? 9.693   10.460  -13.119 1.00 39.62 ? 249 GLN   A N   1 
ATOM   1581 C  CA  . GLN   A 1 215 ? 8.725   9.706   -12.333 1.00 40.87 ? 249 GLN   A CA  1 
ATOM   1582 C  C   . GLN   A 1 215 ? 8.678   8.259   -12.810 1.00 47.86 ? 249 GLN   A C   1 
ATOM   1583 O  O   . GLN   A 1 215 ? 8.829   7.966   -14.003 1.00 47.61 ? 249 GLN   A O   1 
ATOM   1584 C  CB  . GLN   A 1 215 ? 7.334   10.335  -12.430 1.00 41.44 ? 249 GLN   A CB  1 
ATOM   1585 C  CG  . GLN   A 1 215 ? 7.011   11.288  -11.286 1.00 57.93 ? 249 GLN   A CG  1 
ATOM   1586 C  CD  . GLN   A 1 215 ? 5.606   11.881  -11.347 1.00 58.97 ? 249 GLN   A CD  1 
ATOM   1587 O  OE1 . GLN   A 1 215 ? 4.644   11.291  -10.836 1.00 54.74 ? 249 GLN   A OE1 1 
ATOM   1588 N  NE2 . GLN   A 1 215 ? 5.490   13.069  -11.942 1.00 56.44 ? 249 GLN   A NE2 1 
ATOM   1589 N  N   . PHE   A 1 216 ? 8.467   7.346   -11.862 1.00 45.35 ? 250 PHE   A N   1 
ATOM   1590 C  CA  . PHE   A 1 216 ? 8.620   5.918   -12.106 1.00 42.95 ? 250 PHE   A CA  1 
ATOM   1591 C  C   . PHE   A 1 216 ? 7.294   5.192   -12.285 1.00 44.28 ? 250 PHE   A C   1 
ATOM   1592 O  O   . PHE   A 1 216 ? 7.201   4.303   -13.137 1.00 46.46 ? 250 PHE   A O   1 
ATOM   1593 C  CB  . PHE   A 1 216 ? 9.419   5.302   -10.958 1.00 42.98 ? 250 PHE   A CB  1 
ATOM   1594 C  CG  . PHE   A 1 216 ? 9.595   3.817   -11.050 1.00 43.16 ? 250 PHE   A CG  1 
ATOM   1595 C  CD1 . PHE   A 1 216 ? 8.767   2.962   -10.329 1.00 46.06 ? 250 PHE   A CD1 1 
ATOM   1596 C  CD2 . PHE   A 1 216 ? 10.607  3.272   -11.823 1.00 43.45 ? 250 PHE   A CD2 1 
ATOM   1597 C  CE1 . PHE   A 1 216 ? 8.931   1.584   -10.387 1.00 43.47 ? 250 PHE   A CE1 1 
ATOM   1598 C  CE2 . PHE   A 1 216 ? 10.785  1.891   -11.889 1.00 48.82 ? 250 PHE   A CE2 1 
ATOM   1599 C  CZ  . PHE   A 1 216 ? 9.945   1.044   -11.169 1.00 46.12 ? 250 PHE   A CZ  1 
ATOM   1600 N  N   . ALA   A 1 217 ? 6.271   5.559   -11.514 1.00 44.95 ? 251 ALA   A N   1 
ATOM   1601 C  CA  . ALA   A 1 217 ? 4.921   4.986   -11.635 1.00 53.18 ? 251 ALA   A CA  1 
ATOM   1602 C  C   . ALA   A 1 217 ? 4.864   3.517   -11.214 1.00 45.77 ? 251 ALA   A C   1 
ATOM   1603 O  O   . ALA   A 1 217 ? 5.643   2.689   -11.685 1.00 43.35 ? 251 ALA   A O   1 
ATOM   1604 C  CB  . ALA   A 1 217 ? 4.394   5.143   -13.066 1.00 51.48 ? 251 ALA   A CB  1 
ATOM   1605 N  N   . GLU   A 1 228 ? -6.882  6.277   2.808   1.00 42.92 ? 262 GLU   A N   1 
ATOM   1606 C  CA  . GLU   A 1 228 ? -5.432  6.480   2.838   1.00 53.02 ? 262 GLU   A CA  1 
ATOM   1607 C  C   . GLU   A 1 228 ? -4.818  6.055   4.176   1.00 52.94 ? 262 GLU   A C   1 
ATOM   1608 O  O   . GLU   A 1 228 ? -5.482  6.067   5.219   1.00 44.84 ? 262 GLU   A O   1 
ATOM   1609 C  CB  . GLU   A 1 228 ? -5.080  7.947   2.563   1.00 44.81 ? 262 GLU   A CB  1 
ATOM   1610 C  CG  . GLU   A 1 228 ? -3.585  8.216   2.369   1.00 42.75 ? 262 GLU   A CG  1 
ATOM   1611 C  CD  . GLU   A 1 228 ? -2.956  7.314   1.317   1.00 49.38 ? 262 GLU   A CD  1 
ATOM   1612 O  OE1 . GLU   A 1 228 ? -2.066  6.502   1.669   1.00 45.29 ? 262 GLU   A OE1 1 
ATOM   1613 O  OE2 . GLU   A 1 228 ? -3.369  7.412   0.137   1.00 48.84 ? 262 GLU   A OE2 1 
ATOM   1614 N  N   . SER   A 1 229 ? -3.539  5.680   4.132   1.00 48.77 ? 263 SER   A N   1 
ATOM   1615 C  CA  . SER   A 1 229 ? -2.780  5.349   5.324   1.00 45.78 ? 263 SER   A CA  1 
ATOM   1616 C  C   . SER   A 1 229 ? -1.927  6.515   5.818   1.00 46.72 ? 263 SER   A C   1 
ATOM   1617 O  O   . SER   A 1 229 ? -1.055  6.318   6.669   1.00 44.32 ? 263 SER   A O   1 
ATOM   1618 C  CB  . SER   A 1 229 ? -1.914  4.114   5.067   1.00 57.23 ? 263 SER   A CB  1 
ATOM   1619 O  OG  . SER   A 1 229 ? -2.676  3.059   4.504   1.00 57.50 ? 263 SER   A OG  1 
ATOM   1620 N  N   . GLY   A 1 230 ? -2.162  7.724   5.310   1.00 52.85 ? 264 GLY   A N   1 
ATOM   1621 C  CA  . GLY   A 1 230 ? -1.568  8.929   5.860   1.00 40.01 ? 264 GLY   A CA  1 
ATOM   1622 C  C   . GLY   A 1 230 ? -0.372  9.479   5.118   1.00 36.39 ? 264 GLY   A C   1 
ATOM   1623 O  O   . GLY   A 1 230 ? 0.343   10.314  5.675   1.00 34.68 ? 264 GLY   A O   1 
ATOM   1624 N  N   . LEU   A 1 231 ? -0.115  9.037   3.894   1.00 32.07 ? 265 LEU   A N   1 
ATOM   1625 C  CA  . LEU   A 1 231 ? 1.054   9.544   3.208   1.00 34.05 ? 265 LEU   A CA  1 
ATOM   1626 C  C   . LEU   A 1 231 ? 0.804   9.546   1.715   1.00 37.83 ? 265 LEU   A C   1 
ATOM   1627 O  O   . LEU   A 1 231 ? -0.032  8.800   1.193   1.00 39.03 ? 265 LEU   A O   1 
ATOM   1628 C  CB  . LEU   A 1 231 ? 2.313   8.724   3.495   1.00 36.35 ? 265 LEU   A CB  1 
ATOM   1629 C  CG  . LEU   A 1 231 ? 2.559   7.589   2.511   1.00 36.66 ? 265 LEU   A CG  1 
ATOM   1630 C  CD1 . LEU   A 1 231 ? 3.876   7.037   2.726   1.00 40.84 ? 265 LEU   A CD1 1 
ATOM   1631 C  CD2 . LEU   A 1 231 ? 1.538   6.517   2.582   1.00 38.46 ? 265 LEU   A CD2 1 
ATOM   1632 N  N   . ASN   A 1 232 ? 1.581   10.385  1.040   1.00 33.47 ? 266 ASN   A N   1 
ATOM   1633 C  CA  . ASN   A 1 232 ? 1.571   10.539  -0.400  1.00 33.86 ? 266 ASN   A CA  1 
ATOM   1634 C  C   . ASN   A 1 232 ? 3.023   10.537  -0.854  1.00 35.45 ? 266 ASN   A C   1 
ATOM   1635 O  O   . ASN   A 1 232 ? 3.876   11.167  -0.216  1.00 34.80 ? 266 ASN   A O   1 
ATOM   1636 C  CB  . ASN   A 1 232 ? 0.859   11.843  -0.791  1.00 34.58 ? 266 ASN   A CB  1 
ATOM   1637 C  CG  . ASN   A 1 232 ? 0.564   11.928  -2.264  1.00 43.48 ? 266 ASN   A CG  1 
ATOM   1638 O  OD1 . ASN   A 1 232 ? 0.123   10.951  -2.868  1.00 46.91 ? 266 ASN   A OD1 1 
ATOM   1639 N  ND2 . ASN   A 1 232 ? 0.805   13.103  -2.861  1.00 46.06 ? 266 ASN   A ND2 1 
ATOM   1640 N  N   . SER   A 1 233 ? 3.320   9.817   -1.931  1.00 30.36 ? 267 SER   A N   1 
ATOM   1641 C  CA  . SER   A 1 233 ? 4.707   9.772   -2.367  1.00 35.54 ? 267 SER   A CA  1 
ATOM   1642 C  C   . SER   A 1 233 ? 4.812   9.565   -3.866  1.00 30.54 ? 267 SER   A C   1 
ATOM   1643 O  O   . SER   A 1 233 ? 3.883   9.107   -4.528  1.00 29.14 ? 267 SER   A O   1 
ATOM   1644 C  CB  . SER   A 1 233 ? 5.501   8.680   -1.630  1.00 36.92 ? 267 SER   A CB  1 
ATOM   1645 O  OG  . SER   A 1 233 ? 4.776   7.483   -1.523  1.00 36.03 ? 267 SER   A OG  1 
ATOM   1646 N  N   . ALA   A 1 234 ? 5.971   9.924   -4.392  1.00 33.43 ? 268 ALA   A N   1 
ATOM   1647 C  CA  . ALA   A 1 234 ? 6.308   9.638   -5.772  1.00 28.93 ? 268 ALA   A CA  1 
ATOM   1648 C  C   . ALA   A 1 234 ? 7.794   9.331   -5.827  1.00 31.22 ? 268 ALA   A C   1 
ATOM   1649 O  O   . ALA   A 1 234 ? 8.539   9.589   -4.873  1.00 28.02 ? 268 ALA   A O   1 
ATOM   1650 C  CB  . ALA   A 1 234 ? 5.940   10.795  -6.705  1.00 33.64 ? 268 ALA   A CB  1 
ATOM   1651 N  N   . VAL   A 1 235 ? 8.216   8.775   -6.961  1.00 35.08 ? 269 VAL   A N   1 
ATOM   1652 C  CA  . VAL   A 1 235 ? 9.515   8.122   -7.094  1.00 37.08 ? 269 VAL   A CA  1 
ATOM   1653 C  C   . VAL   A 1 235 ? 10.255  8.708   -8.291  1.00 38.36 ? 269 VAL   A C   1 
ATOM   1654 O  O   . VAL   A 1 235 ? 9.757   8.657   -9.424  1.00 39.11 ? 269 VAL   A O   1 
ATOM   1655 C  CB  . VAL   A 1 235 ? 9.367   6.597   -7.247  1.00 35.07 ? 269 VAL   A CB  1 
ATOM   1656 C  CG1 . VAL   A 1 235 ? 10.711  5.971   -7.555  1.00 37.33 ? 269 VAL   A CG1 1 
ATOM   1657 C  CG2 . VAL   A 1 235 ? 8.740   5.974   -5.977  1.00 23.33 ? 269 VAL   A CG2 1 
ATOM   1658 N  N   . LEU   A 1 236 ? 11.454  9.232   -8.047  1.00 34.82 ? 270 LEU   A N   1 
ATOM   1659 C  CA  . LEU   A 1 236 ? 12.317  9.744   -9.100  1.00 34.69 ? 270 LEU   A CA  1 
ATOM   1660 C  C   . LEU   A 1 236 ? 13.384  8.709   -9.427  1.00 33.55 ? 270 LEU   A C   1 
ATOM   1661 O  O   . LEU   A 1 236 ? 13.794  7.931   -8.565  1.00 35.41 ? 270 LEU   A O   1 
ATOM   1662 C  CB  . LEU   A 1 236 ? 12.962  11.067  -8.680  1.00 30.45 ? 270 LEU   A CB  1 
ATOM   1663 C  CG  . LEU   A 1 236 ? 11.994  12.253  -8.550  1.00 32.49 ? 270 LEU   A CG  1 
ATOM   1664 C  CD1 . LEU   A 1 236 ? 12.678  13.486  -7.959  1.00 27.29 ? 270 LEU   A CD1 1 
ATOM   1665 C  CD2 . LEU   A 1 236 ? 11.356  12.585  -9.898  1.00 32.20 ? 270 LEU   A CD2 1 
ATOM   1666 N  N   . ALA   A 1 237 ? 13.824  8.686   -10.683 1.00 33.01 ? 271 ALA   A N   1 
ATOM   1667 C  CA  . ALA   A 1 237 ? 14.796  7.674   -11.065 1.00 32.68 ? 271 ALA   A CA  1 
ATOM   1668 C  C   . ALA   A 1 237 ? 15.687  8.187   -12.182 1.00 30.87 ? 271 ALA   A C   1 
ATOM   1669 O  O   . ALA   A 1 237 ? 15.256  8.965   -13.037 1.00 34.52 ? 271 ALA   A O   1 
ATOM   1670 C  CB  . ALA   A 1 237 ? 14.109  6.375   -11.490 1.00 32.10 ? 271 ALA   A CB  1 
ATOM   1671 N  N   . SER   A 1 238 ? 16.941  7.741   -12.152 1.00 30.24 ? 272 SER   A N   1 
ATOM   1672 C  CA  . SER   A 1 238 ? 17.895  7.973   -13.225 1.00 32.91 ? 272 SER   A CA  1 
ATOM   1673 C  C   . SER   A 1 238 ? 17.476  7.206   -14.486 1.00 37.93 ? 272 SER   A C   1 
ATOM   1674 O  O   . SER   A 1 238 ? 16.496  6.457   -14.495 1.00 32.71 ? 272 SER   A O   1 
ATOM   1675 C  CB  . SER   A 1 238 ? 19.292  7.552   -12.777 1.00 34.80 ? 272 SER   A CB  1 
ATOM   1676 O  OG  . SER   A 1 238 ? 19.336  6.160   -12.494 1.00 30.59 ? 272 SER   A OG  1 
ATOM   1677 N  N   . ASN   A 1 239 ? 18.271  7.364   -15.555 1.00 36.99 ? 273 ASN   A N   1 
ATOM   1678 C  CA  . ASN   A 1 239 ? 17.893  6.863   -16.877 1.00 35.74 ? 273 ASN   A CA  1 
ATOM   1679 C  C   . ASN   A 1 239 ? 17.710  5.346   -16.893 1.00 41.45 ? 273 ASN   A C   1 
ATOM   1680 O  O   . ASN   A 1 239 ? 16.748  4.832   -17.482 1.00 41.66 ? 273 ASN   A O   1 
ATOM   1681 C  CB  . ASN   A 1 239 ? 18.939  7.266   -17.909 1.00 39.93 ? 273 ASN   A CB  1 
ATOM   1682 C  CG  . ASN   A 1 239 ? 18.831  8.695   -18.312 1.00 41.36 ? 273 ASN   A CG  1 
ATOM   1683 O  OD1 . ASN   A 1 239 ? 17.824  9.349   -18.055 1.00 38.53 ? 273 ASN   A OD1 1 
ATOM   1684 N  ND2 . ASN   A 1 239 ? 19.878  9.207   -18.947 1.00 40.66 ? 273 ASN   A ND2 1 
ATOM   1685 N  N   . ASP   A 1 240 ? 18.643  4.603   -16.300 1.00 34.17 ? 274 ASP   A N   1 
ATOM   1686 C  CA  . ASP   A 1 240 ? 18.412  3.171   -16.219 1.00 33.12 ? 274 ASP   A CA  1 
ATOM   1687 C  C   . ASP   A 1 240 ? 17.575  2.792   -15.012 1.00 34.36 ? 274 ASP   A C   1 
ATOM   1688 O  O   . ASP   A 1 240 ? 17.293  1.607   -14.835 1.00 42.03 ? 274 ASP   A O   1 
ATOM   1689 C  CB  . ASP   A 1 240 ? 19.743  2.392   -16.232 1.00 33.21 ? 274 ASP   A CB  1 
ATOM   1690 C  CG  . ASP   A 1 240 ? 20.623  2.663   -15.017 1.00 39.17 ? 274 ASP   A CG  1 
ATOM   1691 O  OD1 . ASP   A 1 240 ? 20.155  3.300   -14.053 1.00 43.25 ? 274 ASP   A OD1 1 
ATOM   1692 O  OD2 . ASP   A 1 240 ? 21.804  2.237   -15.026 1.00 34.31 ? 274 ASP   A OD2 1 
ATOM   1693 N  N   . GLU   A 1 241 ? 17.184  3.760   -14.180 1.00 33.68 ? 275 GLU   A N   1 
ATOM   1694 C  CA  . GLU   A 1 241 ? 16.340  3.512   -13.005 1.00 39.16 ? 275 GLU   A CA  1 
ATOM   1695 C  C   . GLU   A 1 241 ? 17.050  2.647   -11.951 1.00 38.33 ? 275 GLU   A C   1 
ATOM   1696 O  O   . GLU   A 1 241 ? 16.426  1.834   -11.264 1.00 29.89 ? 275 GLU   A O   1 
ATOM   1697 C  CB  . GLU   A 1 241 ? 14.994  2.892   -13.409 1.00 35.79 ? 275 GLU   A CB  1 
ATOM   1698 C  CG  . GLU   A 1 241 ? 14.274  3.663   -14.510 1.00 40.15 ? 275 GLU   A CG  1 
ATOM   1699 C  CD  . GLU   A 1 241 ? 12.826  3.238   -14.711 1.00 44.12 ? 275 GLU   A CD  1 
ATOM   1700 O  OE1 . GLU   A 1 241 ? 11.949  4.122   -14.810 1.00 42.92 ? 275 GLU   A OE1 1 
ATOM   1701 O  OE2 . GLU   A 1 241 ? 12.559  2.021   -14.795 1.00 47.60 ? 275 GLU   A OE2 1 
ATOM   1702 N  N   . MET   A 1 242 ? 18.363  2.841   -11.801 1.00 36.76 ? 276 MET   A N   1 
ATOM   1703 C  CA  . MET   A 1 242 ? 19.139  2.175   -10.760 1.00 33.35 ? 276 MET   A CA  1 
ATOM   1704 C  C   . MET   A 1 242 ? 19.350  3.040   -9.524  1.00 32.33 ? 276 MET   A C   1 
ATOM   1705 O  O   . MET   A 1 242 ? 19.485  2.499   -8.428  1.00 39.99 ? 276 MET   A O   1 
ATOM   1706 C  CB  . MET   A 1 242 ? 20.501  1.723   -11.309 1.00 32.37 ? 276 MET   A CB  1 
ATOM   1707 C  CG  . MET   A 1 242 ? 20.431  0.462   -12.151 1.00 38.57 ? 276 MET   A CG  1 
ATOM   1708 S  SD  . MET   A 1 242 ? 19.840  -1.005  -11.255 1.00 48.24 ? 276 MET   A SD  1 
ATOM   1709 C  CE  . MET   A 1 242 ? 18.850  -1.790  -12.495 1.00 41.45 ? 276 MET   A CE  1 
ATOM   1710 N  N   . VAL   A 1 243 ? 19.394  4.360   -9.673  1.00 33.12 ? 277 VAL   A N   1 
ATOM   1711 C  CA  . VAL   A 1 243 ? 19.211  5.291   -8.563  1.00 29.59 ? 277 VAL   A CA  1 
ATOM   1712 C  C   . VAL   A 1 243 ? 17.720  5.607   -8.445  1.00 32.58 ? 277 VAL   A C   1 
ATOM   1713 O  O   . VAL   A 1 243 ? 17.102  6.122   -9.388  1.00 29.39 ? 277 VAL   A O   1 
ATOM   1714 C  CB  . VAL   A 1 243 ? 20.031  6.574   -8.769  1.00 31.23 ? 277 VAL   A CB  1 
ATOM   1715 C  CG1 . VAL   A 1 243 ? 19.701  7.600   -7.693  1.00 22.90 ? 277 VAL   A CG1 1 
ATOM   1716 C  CG2 . VAL   A 1 243 ? 21.506  6.251   -8.757  1.00 33.91 ? 277 VAL   A CG2 1 
ATOM   1717 N  N   . LEU   A 1 244 ? 17.143  5.284   -7.288  1.00 34.36 ? 278 LEU   A N   1 
ATOM   1718 C  CA  . LEU   A 1 244 ? 15.733  5.510   -6.996  1.00 28.92 ? 278 LEU   A CA  1 
ATOM   1719 C  C   . LEU   A 1 244 ? 15.617  6.412   -5.775  1.00 28.56 ? 278 LEU   A C   1 
ATOM   1720 O  O   . LEU   A 1 244 ? 16.278  6.181   -4.753  1.00 27.73 ? 278 LEU   A O   1 
ATOM   1721 C  CB  . LEU   A 1 244 ? 15.014  4.183   -6.761  1.00 27.31 ? 278 LEU   A CB  1 
ATOM   1722 C  CG  . LEU   A 1 244 ? 15.221  3.185   -7.894  1.00 27.68 ? 278 LEU   A CG  1 
ATOM   1723 C  CD1 . LEU   A 1 244 ? 14.733  1.800   -7.535  1.00 27.50 ? 278 LEU   A CD1 1 
ATOM   1724 C  CD2 . LEU   A 1 244 ? 14.498  3.693   -9.114  1.00 36.15 ? 278 LEU   A CD2 1 
ATOM   1725 N  N   . LEU   A 1 245 ? 14.781  7.436   -5.887  1.00 31.13 ? 279 LEU   A N   1 
ATOM   1726 C  CA  . LEU   A 1 245 ? 14.609  8.450   -4.844  1.00 30.20 ? 279 LEU   A CA  1 
ATOM   1727 C  C   . LEU   A 1 245 ? 13.123  8.712   -4.606  1.00 29.73 ? 279 LEU   A C   1 
ATOM   1728 O  O   . LEU   A 1 245 ? 12.557  9.696   -5.103  1.00 29.20 ? 279 LEU   A O   1 
ATOM   1729 C  CB  . LEU   A 1 245 ? 15.352  9.731   -5.220  1.00 25.14 ? 279 LEU   A CB  1 
ATOM   1730 C  CG  . LEU   A 1 245 ? 16.871  9.539   -5.167  1.00 27.41 ? 279 LEU   A CG  1 
ATOM   1731 C  CD1 . LEU   A 1 245 ? 17.607  10.818  -5.504  1.00 22.92 ? 279 LEU   A CD1 1 
ATOM   1732 C  CD2 . LEU   A 1 245 ? 17.320  9.016   -3.800  1.00 28.02 ? 279 LEU   A CD2 1 
ATOM   1733 N  N   . PRO   A 1 246 ? 12.457  7.842   -3.851  1.00 30.98 ? 280 PRO   A N   1 
ATOM   1734 C  CA  . PRO   A 1 246 ? 11.090  8.151   -3.402  1.00 31.61 ? 280 PRO   A CA  1 
ATOM   1735 C  C   . PRO   A 1 246 ? 11.074  9.303   -2.403  1.00 29.29 ? 280 PRO   A C   1 
ATOM   1736 O  O   . PRO   A 1 246 ? 12.035  9.532   -1.666  1.00 30.28 ? 280 PRO   A O   1 
ATOM   1737 C  CB  . PRO   A 1 246 ? 10.627  6.843   -2.745  1.00 29.33 ? 280 PRO   A CB  1 
ATOM   1738 C  CG  . PRO   A 1 246 ? 11.593  5.757   -3.292  1.00 28.46 ? 280 PRO   A CG  1 
ATOM   1739 C  CD  . PRO   A 1 246 ? 12.886  6.471   -3.500  1.00 27.66 ? 280 PRO   A CD  1 
ATOM   1740 N  N   . ILE   A 1 247 ? 9.971   10.050  -2.389  1.00 29.19 ? 281 ILE   A N   1 
ATOM   1741 C  CA  . ILE   A 1 247 ? 9.768   11.093  -1.384  1.00 29.43 ? 281 ILE   A CA  1 
ATOM   1742 C  C   . ILE   A 1 247 ? 8.348   11.015  -0.848  1.00 31.32 ? 281 ILE   A C   1 
ATOM   1743 O  O   . ILE   A 1 247 ? 7.386   10.993  -1.620  1.00 34.15 ? 281 ILE   A O   1 
ATOM   1744 C  CB  . ILE   A 1 247 ? 10.022  12.511  -1.919  1.00 26.41 ? 281 ILE   A CB  1 
ATOM   1745 C  CG1 . ILE   A 1 247 ? 11.425  12.623  -2.494  1.00 27.41 ? 281 ILE   A CG1 1 
ATOM   1746 C  CG2 . ILE   A 1 247 ? 9.868   13.475  -0.795  1.00 26.81 ? 281 ILE   A CG2 1 
ATOM   1747 C  CD1 . ILE   A 1 247 ? 11.504  13.553  -3.677  1.00 32.18 ? 281 ILE   A CD1 1 
ATOM   1748 N  N   . ASN   A 1 248 ? 8.219   11.011  0.470   1.00 30.49 ? 282 ASN   A N   1 
ATOM   1749 C  CA  . ASN   A 1 248 ? 6.931   10.998  1.142   1.00 32.57 ? 282 ASN   A CA  1 
ATOM   1750 C  C   . ASN   A 1 248 ? 6.630   12.395  1.657   1.00 35.32 ? 282 ASN   A C   1 
ATOM   1751 O  O   . ASN   A 1 248 ? 7.532   13.105  2.113   1.00 33.58 ? 282 ASN   A O   1 
ATOM   1752 C  CB  . ASN   A 1 248 ? 6.921   10.042  2.344   1.00 38.81 ? 282 ASN   A CB  1 
ATOM   1753 C  CG  . ASN   A 1 248 ? 7.514   8.682   2.049   1.00 30.38 ? 282 ASN   A CG  1 
ATOM   1754 O  OD1 . ASN   A 1 248 ? 8.290   8.185   2.854   1.00 32.35 ? 282 ASN   A OD1 1 
ATOM   1755 N  ND2 . ASN   A 1 248 ? 7.121   8.053   0.945   1.00 29.28 ? 282 ASN   A ND2 1 
ATOM   1756 N  N   . GLU   A 1 249 ? 5.363   12.777  1.588   1.00 36.29 ? 283 GLU   A N   1 
ATOM   1757 C  CA  . GLU   A 1 249 ? 4.801   13.906  2.309   1.00 31.28 ? 283 GLU   A CA  1 
ATOM   1758 C  C   . GLU   A 1 249 ? 3.687   13.386  3.199   1.00 34.46 ? 283 GLU   A C   1 
ATOM   1759 O  O   . GLU   A 1 249 ? 3.178   12.281  2.983   1.00 33.59 ? 283 GLU   A O   1 
ATOM   1760 C  CB  . GLU   A 1 249 ? 4.208   14.950  1.363   1.00 34.66 ? 283 GLU   A CB  1 
ATOM   1761 C  CG  . GLU   A 1 249 ? 2.756   14.642  1.078   1.00 35.45 ? 283 GLU   A CG  1 
ATOM   1762 C  CD  . GLU   A 1 249 ? 2.145   15.580  0.095   1.00 42.13 ? 283 GLU   A CD  1 
ATOM   1763 O  OE1 . GLU   A 1 249 ? 1.601   15.082  -0.922  1.00 45.34 ? 283 GLU   A OE1 1 
ATOM   1764 O  OE2 . GLU   A 1 249 ? 2.225   16.812  0.336   1.00 41.76 ? 283 GLU   A OE2 1 
ATOM   1765 N  N   . PRO   A 1 250 ? 3.259   14.157  4.191   1.00 33.80 ? 284 PRO   A N   1 
ATOM   1766 C  CA  . PRO   A 1 250 ? 2.099   13.731  4.972   1.00 32.98 ? 284 PRO   A CA  1 
ATOM   1767 C  C   . PRO   A 1 250 ? 0.806   14.169  4.312   1.00 33.94 ? 284 PRO   A C   1 
ATOM   1768 O  O   . PRO   A 1 250 ? 0.711   15.225  3.683   1.00 36.97 ? 284 PRO   A O   1 
ATOM   1769 C  CB  . PRO   A 1 250 ? 2.296   14.443  6.315   1.00 30.57 ? 284 PRO   A CB  1 
ATOM   1770 C  CG  . PRO   A 1 250 ? 3.430   15.422  6.094   1.00 32.86 ? 284 PRO   A CG  1 
ATOM   1771 C  CD  . PRO   A 1 250 ? 3.755   15.455  4.650   1.00 33.77 ? 284 PRO   A CD  1 
ATOM   1772 N  N   . VAL   A 1 251 ? -0.183  13.303  4.425   1.00 28.24 ? 285 VAL   A N   1 
ATOM   1773 C  CA  . VAL   A 1 251 ? -1.562  13.634  4.131   1.00 37.62 ? 285 VAL   A CA  1 
ATOM   1774 C  C   . VAL   A 1 251 ? -2.189  13.907  5.492   1.00 37.19 ? 285 VAL   A C   1 
ATOM   1775 O  O   . VAL   A 1 251 ? -2.526  12.986  6.239   1.00 38.70 ? 285 VAL   A O   1 
ATOM   1776 C  CB  . VAL   A 1 251 ? -2.275  12.512  3.365   1.00 40.81 ? 285 VAL   A CB  1 
ATOM   1777 C  CG1 . VAL   A 1 251 ? -3.769  12.777  3.291   1.00 40.63 ? 285 VAL   A CG1 1 
ATOM   1778 C  CG2 . VAL   A 1 251 ? -1.699  12.371  1.958   1.00 32.89 ? 285 VAL   A CG2 1 
ATOM   1779 N  N   . HIS   A 1 252 ? -2.282  15.173  5.854   1.00 38.63 ? 286 HIS   A N   1 
ATOM   1780 C  CA  . HIS   A 1 252 ? -2.924  15.514  7.109   1.00 38.51 ? 286 HIS   A CA  1 
ATOM   1781 C  C   . HIS   A 1 252 ? -4.425  15.385  6.943   1.00 44.02 ? 286 HIS   A C   1 
ATOM   1782 O  O   . HIS   A 1 252 ? -4.997  15.821  5.938   1.00 39.31 ? 286 HIS   A O   1 
ATOM   1783 C  CB  . HIS   A 1 252 ? -2.549  16.925  7.558   1.00 30.40 ? 286 HIS   A CB  1 
ATOM   1784 C  CG  . HIS   A 1 252 ? -1.083  17.101  7.776   1.00 33.66 ? 286 HIS   A CG  1 
ATOM   1785 N  ND1 . HIS   A 1 252 ? -0.231  17.543  6.788   1.00 33.91 ? 286 HIS   A ND1 1 
ATOM   1786 C  CD2 . HIS   A 1 252 ? -0.307  16.844  8.854   1.00 35.66 ? 286 HIS   A CD2 1 
ATOM   1787 C  CE1 . HIS   A 1 252 ? 1.003   17.579  7.256   1.00 31.13 ? 286 HIS   A CE1 1 
ATOM   1788 N  NE2 . HIS   A 1 252 ? 0.984   17.157  8.508   1.00 31.93 ? 286 HIS   A NE2 1 
ATOM   1789 N  N   . GLY   A 1 253 ? -5.058  14.776  7.913   1.00 42.96 ? 287 GLY   A N   1 
ATOM   1790 C  CA  . GLY   A 1 253 ? -6.503  14.743  7.951   1.00 41.69 ? 287 GLY   A CA  1 
ATOM   1791 C  C   . GLY   A 1 253 ? -7.047  14.724  9.343   1.00 47.30 ? 287 GLY   A C   1 
ATOM   1792 O  O   . GLY   A 1 253 ? -6.501  15.321  10.276  1.00 46.11 ? 287 GLY   A O   1 
ATOM   1793 N  N   . THR   A 1 254 ? -8.117  13.999  9.490   1.00 53.86 ? 288 THR   A N   1 
ATOM   1794 C  CA  . THR   A 1 254 ? -9.003  14.183  10.621  1.00 51.67 ? 288 THR   A CA  1 
ATOM   1795 C  C   . THR   A 1 254 ? -9.253  12.860  11.340  1.00 54.79 ? 288 THR   A C   1 
ATOM   1796 O  O   . THR   A 1 254 ? -9.814  12.864  12.438  1.00 53.74 ? 288 THR   A O   1 
ATOM   1797 C  CB  . THR   A 1 254 ? -10.271 14.856  10.058  1.00 49.93 ? 288 THR   A CB  1 
ATOM   1798 O  OG1 . THR   A 1 254 ? -10.004 16.243  9.837   1.00 60.03 ? 288 THR   A OG1 1 
ATOM   1799 C  CG2 . THR   A 1 254 ? -11.474 14.728  10.934  1.00 42.82 ? 288 THR   A CG2 1 
ATOM   1800 N  N   . LYS   A 1 255 ? -8.791  11.739  10.779  1.00 52.53 ? 289 LYS   A N   1 
ATOM   1801 C  CA  . LYS   A 1 255 ? -9.008  10.400  11.319  1.00 48.28 ? 289 LYS   A CA  1 
ATOM   1802 C  C   . LYS   A 1 255 ? -7.829  9.910   12.155  1.00 46.68 ? 289 LYS   A C   1 
ATOM   1803 O  O   . LYS   A 1 255 ? -7.991  9.591   13.335  1.00 50.98 ? 289 LYS   A O   1 
ATOM   1804 C  CB  . LYS   A 1 255 ? -9.282  9.431   10.163  1.00 42.70 ? 289 LYS   A CB  1 
ATOM   1805 C  CG  . LYS   A 1 255 ? -9.381  7.995   10.558  1.00 40.99 ? 289 LYS   A CG  1 
ATOM   1806 C  CD  . LYS   A 1 255 ? -9.481  7.130   9.313   1.00 42.25 ? 289 LYS   A CD  1 
ATOM   1807 C  CE  . LYS   A 1 255 ? -9.646  5.661   9.685   1.00 47.86 ? 289 LYS   A CE  1 
ATOM   1808 N  NZ  . LYS   A 1 255 ? -9.270  4.705   8.601   1.00 44.94 ? 289 LYS   A NZ  1 
ATOM   1809 N  N   . ARG   A 1 256 ? -6.646  9.830   11.560  1.00 46.54 ? 290 ARG   A N   1 
ATOM   1810 C  CA  . ARG   A 1 256 ? -5.431  9.470   12.271  1.00 47.48 ? 290 ARG   A CA  1 
ATOM   1811 C  C   . ARG   A 1 256 ? -4.363  10.512  11.979  1.00 48.61 ? 290 ARG   A C   1 
ATOM   1812 O  O   . ARG   A 1 256 ? -4.345  11.113  10.901  1.00 50.86 ? 290 ARG   A O   1 
ATOM   1813 C  CB  . ARG   A 1 256 ? -4.922  8.076   11.861  1.00 46.10 ? 290 ARG   A CB  1 
ATOM   1814 N  N   . LYS   A 1 257 ? -3.478  10.733  12.954  1.00 46.26 ? 291 LYS   A N   1 
ATOM   1815 C  CA  . LYS   A 1 257 ? -2.288  11.541  12.715  1.00 37.83 ? 291 LYS   A CA  1 
ATOM   1816 C  C   . LYS   A 1 257 ? -1.318  10.784  11.823  1.00 35.70 ? 291 LYS   A C   1 
ATOM   1817 O  O   . LYS   A 1 257 ? -0.957  9.649   12.125  1.00 44.50 ? 291 LYS   A O   1 
ATOM   1818 C  CB  . LYS   A 1 257 ? -1.595  11.892  14.024  1.00 34.27 ? 291 LYS   A CB  1 
ATOM   1819 C  CG  . LYS   A 1 257 ? -0.347  12.762  13.842  1.00 36.73 ? 291 LYS   A CG  1 
ATOM   1820 C  CD  . LYS   A 1 257 ? 0.762   12.379  14.821  1.00 39.30 ? 291 LYS   A CD  1 
ATOM   1821 C  CE  . LYS   A 1 257 ? 1.634   13.584  15.210  1.00 51.58 ? 291 LYS   A CE  1 
ATOM   1822 N  NZ  . LYS   A 1 257 ? 2.502   13.327  16.406  1.00 49.15 ? 291 LYS   A NZ  1 
ATOM   1823 N  N   . SER   A 1 258 ? -0.873  11.427  10.746  1.00 28.68 ? 292 SER   A N   1 
ATOM   1824 C  CA  . SER   A 1 258 ? 0.053   10.804  9.817   1.00 30.11 ? 292 SER   A CA  1 
ATOM   1825 C  C   . SER   A 1 258 ? 1.379   10.420  10.479  1.00 29.58 ? 292 SER   A C   1 
ATOM   1826 O  O   . SER   A 1 258 ? 1.944   11.170  11.273  1.00 30.35 ? 292 SER   A O   1 
ATOM   1827 C  CB  . SER   A 1 258 ? 0.326   11.741  8.653   1.00 29.04 ? 292 SER   A CB  1 
ATOM   1828 O  OG  . SER   A 1 258 ? 1.541   11.368  8.038   1.00 34.29 ? 292 SER   A OG  1 
ATOM   1829 N  N   . GLN   A 1 259 ? 1.883   9.240   10.115  1.00 31.91 ? 293 GLN   A N   1 
ATOM   1830 C  CA  . GLN   A 1 259 ? 3.202   8.800   10.556  1.00 34.51 ? 293 GLN   A CA  1 
ATOM   1831 C  C   . GLN   A 1 259 ? 4.304   9.690   9.997   1.00 34.40 ? 293 GLN   A C   1 
ATOM   1832 O  O   . GLN   A 1 259 ? 5.343   9.866   10.647  1.00 33.56 ? 293 GLN   A O   1 
ATOM   1833 C  CB  . GLN   A 1 259 ? 3.452   7.337   10.137  1.00 33.90 ? 293 GLN   A CB  1 
ATOM   1834 C  CG  . GLN   A 1 259 ? 2.515   6.276   10.769  1.00 36.30 ? 293 GLN   A CG  1 
ATOM   1835 C  CD  . GLN   A 1 259 ? 3.079   4.829   10.731  1.00 47.78 ? 293 GLN   A CD  1 
ATOM   1836 O  OE1 . GLN   A 1 259 ? 3.505   4.339   9.681   1.00 50.63 ? 293 GLN   A OE1 1 
ATOM   1837 N  NE2 . GLN   A 1 259 ? 3.051   4.145   11.879  1.00 48.12 ? 293 GLN   A NE2 1 
ATOM   1838 N  N   . ILE   A 1 260 ? 4.114   10.239  8.792   1.00 27.69 ? 294 ILE   A N   1 
ATOM   1839 C  CA  . ILE   A 1 260 ? 5.129   11.124  8.234   1.00 28.94 ? 294 ILE   A CA  1 
ATOM   1840 C  C   . ILE   A 1 260 ? 5.259   12.379  9.079   1.00 33.74 ? 294 ILE   A C   1 
ATOM   1841 O  O   . ILE   A 1 260 ? 6.356   12.945  9.211   1.00 33.45 ? 294 ILE   A O   1 
ATOM   1842 C  CB  . ILE   A 1 260 ? 4.801   11.470  6.774   1.00 33.54 ? 294 ILE   A CB  1 
ATOM   1843 C  CG1 . ILE   A 1 260 ? 4.480   10.187  5.980   1.00 38.96 ? 294 ILE   A CG1 1 
ATOM   1844 C  CG2 . ILE   A 1 260 ? 5.946   12.281  6.135   1.00 27.85 ? 294 ILE   A CG2 1 
ATOM   1845 C  CD1 . ILE   A 1 260 ? 5.597   9.151   5.930   1.00 24.50 ? 294 ILE   A CD1 1 
ATOM   1846 N  N   . GLN   A 1 261 ? 4.154   12.827  9.678   1.00 33.20 ? 295 GLN   A N   1 
ATOM   1847 C  CA  . GLN   A 1 261 ? 4.206   14.025  10.507  1.00 34.27 ? 295 GLN   A CA  1 
ATOM   1848 C  C   . GLN   A 1 261 ? 4.970   13.759  11.792  1.00 33.02 ? 295 GLN   A C   1 
ATOM   1849 O  O   . GLN   A 1 261 ? 5.725   14.619  12.269  1.00 29.81 ? 295 GLN   A O   1 
ATOM   1850 C  CB  . GLN   A 1 261 ? 2.794   14.519  10.811  1.00 32.19 ? 295 GLN   A CB  1 
ATOM   1851 C  CG  . GLN   A 1 261 ? 2.742   15.741  11.707  1.00 34.13 ? 295 GLN   A CG  1 
ATOM   1852 C  CD  . GLN   A 1 261 ? 3.316   16.997  11.055  1.00 37.94 ? 295 GLN   A CD  1 
ATOM   1853 O  OE1 . GLN   A 1 261 ? 3.533   17.041  9.829   1.00 32.21 ? 295 GLN   A OE1 1 
ATOM   1854 N  NE2 . GLN   A 1 261 ? 3.561   18.032  11.877  1.00 28.39 ? 295 GLN   A NE2 1 
ATOM   1855 N  N   . THR   A 1 262 ? 4.786   12.569  12.361  1.00 29.69 ? 296 THR   A N   1 
ATOM   1856 C  CA  . THR   A 1 262 ? 5.551   12.196  13.538  1.00 29.40 ? 296 THR   A CA  1 
ATOM   1857 C  C   . THR   A 1 262 ? 7.041   12.201  13.240  1.00 26.93 ? 296 THR   A C   1 
ATOM   1858 O  O   . THR   A 1 262 ? 7.838   12.712  14.033  1.00 24.03 ? 296 THR   A O   1 
ATOM   1859 C  CB  . THR   A 1 262 ? 5.091   10.827  14.024  1.00 36.43 ? 296 THR   A CB  1 
ATOM   1860 O  OG1 . THR   A 1 262 ? 3.683   10.882  14.288  1.00 41.58 ? 296 THR   A OG1 1 
ATOM   1861 C  CG2 . THR   A 1 262 ? 5.835   10.423  15.289  1.00 36.22 ? 296 THR   A CG2 1 
ATOM   1862 N  N   . TYR   A 1 263 ? 7.435   11.655  12.086  1.00 33.47 ? 297 TYR   A N   1 
ATOM   1863 C  CA  . TYR   A 1 263 ? 8.835   11.746  11.679  1.00 33.39 ? 297 TYR   A CA  1 
ATOM   1864 C  C   . TYR   A 1 263 ? 9.310   13.209  11.687  1.00 28.19 ? 297 TYR   A C   1 
ATOM   1865 O  O   . TYR   A 1 263 ? 10.340  13.537  12.293  1.00 26.60 ? 297 TYR   A O   1 
ATOM   1866 C  CB  . TYR   A 1 263 ? 9.039   11.090  10.301  1.00 20.78 ? 297 TYR   A CB  1 
ATOM   1867 C  CG  . TYR   A 1 263 ? 10.442  11.299  9.764   1.00 22.41 ? 297 TYR   A CG  1 
ATOM   1868 C  CD1 . TYR   A 1 263 ? 10.779  12.470  9.084   1.00 25.87 ? 297 TYR   A CD1 1 
ATOM   1869 C  CD2 . TYR   A 1 263 ? 11.437  10.353  9.959   1.00 23.40 ? 297 TYR   A CD2 1 
ATOM   1870 C  CE1 . TYR   A 1 263 ? 12.061  12.692  8.611   1.00 24.42 ? 297 TYR   A CE1 1 
ATOM   1871 C  CE2 . TYR   A 1 263 ? 12.730  10.560  9.491   1.00 26.54 ? 297 TYR   A CE2 1 
ATOM   1872 C  CZ  . TYR   A 1 263 ? 13.035  11.745  8.813   1.00 29.26 ? 297 TYR   A CZ  1 
ATOM   1873 O  OH  . TYR   A 1 263 ? 14.310  11.984  8.337   1.00 24.52 ? 297 TYR   A OH  1 
ATOM   1874 N  N   . LEU   A 1 264 ? 8.555   14.103  11.041  1.00 23.79 ? 298 LEU   A N   1 
ATOM   1875 C  CA  . LEU   A 1 264 ? 9.007   15.489  10.892  1.00 30.98 ? 298 LEU   A CA  1 
ATOM   1876 C  C   . LEU   A 1 264 ? 9.193   16.163  12.243  1.00 27.60 ? 298 LEU   A C   1 
ATOM   1877 O  O   . LEU   A 1 264 ? 10.143  16.935  12.436  1.00 25.37 ? 298 LEU   A O   1 
ATOM   1878 C  CB  . LEU   A 1 264 ? 8.019   16.283  10.028  1.00 27.96 ? 298 LEU   A CB  1 
ATOM   1879 C  CG  . LEU   A 1 264 ? 7.949   15.832  8.566   1.00 28.05 ? 298 LEU   A CG  1 
ATOM   1880 C  CD1 . LEU   A 1 264 ? 6.587   16.113  7.974   1.00 30.21 ? 298 LEU   A CD1 1 
ATOM   1881 C  CD2 . LEU   A 1 264 ? 9.072   16.475  7.719   1.00 23.22 ? 298 LEU   A CD2 1 
ATOM   1882 N  N   . GLU   A 1 265 ? 8.312   15.857  13.197  1.00 28.25 ? 299 GLU   A N   1 
ATOM   1883 C  CA  . GLU   A 1 265 ? 8.397   16.470  14.517  1.00 28.88 ? 299 GLU   A CA  1 
ATOM   1884 C  C   . GLU   A 1 265 ? 9.646   16.015  15.266  1.00 29.89 ? 299 GLU   A C   1 
ATOM   1885 O  O   . GLU   A 1 265 ? 10.466  16.841  15.678  1.00 30.72 ? 299 GLU   A O   1 
ATOM   1886 C  CB  . GLU   A 1 265 ? 7.126   16.162  15.304  1.00 25.48 ? 299 GLU   A CB  1 
ATOM   1887 C  CG  . GLU   A 1 265 ? 5.918   16.839  14.693  1.00 24.84 ? 299 GLU   A CG  1 
ATOM   1888 C  CD  . GLU   A 1 265 ? 4.616   16.382  15.294  1.00 35.40 ? 299 GLU   A CD  1 
ATOM   1889 O  OE1 . GLU   A 1 265 ? 4.657   15.559  16.227  1.00 42.90 ? 299 GLU   A OE1 1 
ATOM   1890 O  OE2 . GLU   A 1 265 ? 3.549   16.835  14.830  1.00 35.24 ? 299 GLU   A OE2 1 
ATOM   1891 N  N   . HIS   A 1 266 ? 9.829   14.705  15.436  1.00 28.94 ? 300 HIS   A N   1 
ATOM   1892 C  CA  . HIS   A 1 266 ? 11.008  14.241  16.159  1.00 27.95 ? 300 HIS   A CA  1 
ATOM   1893 C  C   . HIS   A 1 266 ? 12.306  14.457  15.385  1.00 27.25 ? 300 HIS   A C   1 
ATOM   1894 O  O   . HIS   A 1 266 ? 13.373  14.540  16.006  1.00 26.77 ? 300 HIS   A O   1 
ATOM   1895 C  CB  . HIS   A 1 266 ? 10.850  12.766  16.534  1.00 26.31 ? 300 HIS   A CB  1 
ATOM   1896 C  CG  . HIS   A 1 266 ? 9.794   12.521  17.570  1.00 29.48 ? 300 HIS   A CG  1 
ATOM   1897 N  ND1 . HIS   A 1 266 ? 10.083  12.397  18.914  1.00 24.54 ? 300 HIS   A ND1 1 
ATOM   1898 C  CD2 . HIS   A 1 266 ? 8.451   12.370  17.458  1.00 30.76 ? 300 HIS   A CD2 1 
ATOM   1899 C  CE1 . HIS   A 1 266 ? 8.962   12.188  19.585  1.00 27.07 ? 300 HIS   A CE1 1 
ATOM   1900 N  NE2 . HIS   A 1 266 ? 7.957   12.173  18.726  1.00 29.02 ? 300 HIS   A NE2 1 
ATOM   1901 N  N   . ASN   A 1 267 ? 12.256  14.550  14.057  1.00 22.33 ? 301 ASN   A N   1 
ATOM   1902 C  CA  . ASN   A 1 267 ? 13.462  14.884  13.317  1.00 22.87 ? 301 ASN   A CA  1 
ATOM   1903 C  C   . ASN   A 1 267 ? 13.683  16.385  13.196  1.00 29.46 ? 301 ASN   A C   1 
ATOM   1904 O  O   . ASN   A 1 267 ? 14.742  16.798  12.713  1.00 30.05 ? 301 ASN   A O   1 
ATOM   1905 C  CB  . ASN   A 1 267 ? 13.434  14.268  11.910  1.00 25.74 ? 301 ASN   A CB  1 
ATOM   1906 C  CG  . ASN   A 1 267 ? 14.749  14.476  11.160  1.00 24.14 ? 301 ASN   A CG  1 
ATOM   1907 O  OD1 . ASN   A 1 267 ? 15.793  14.083  11.637  1.00 22.42 ? 301 ASN   A OD1 1 
ATOM   1908 N  ND2 . ASN   A 1 267 ? 14.695  15.114  10.006  1.00 23.21 ? 301 ASN   A ND2 1 
ATOM   1909 N  N   . GLU   A 1 268 ? 12.675  17.163  13.465  1.00 28.85 ? 302 GLU   A N   1 
ATOM   1910 C  CA  . GLU   A 1 268 ? 12.807  18.580  13.359  1.00 27.71 ? 302 GLU   A CA  1 
ATOM   1911 C  C   . GLU   A 1 268 ? 12.852  18.938  11.914  1.00 28.52 ? 302 GLU   A C   1 
ATOM   1912 O  O   . GLU   A 1 268 ? 13.684  19.664  11.466  1.00 32.24 ? 302 GLU   A O   1 
ATOM   1913 C  CB  . GLU   A 1 268 ? 14.016  19.111  14.118  1.00 28.78 ? 302 GLU   A CB  1 
ATOM   1914 C  CG  . GLU   A 1 268 ? 13.771  19.377  15.585  1.00 35.49 ? 302 GLU   A CG  1 
ATOM   1915 C  CD  . GLU   A 1 268 ? 14.767  20.320  16.223  1.00 40.13 ? 302 GLU   A CD  1 
ATOM   1916 O  OE1 . GLU   A 1 268 ? 15.354  21.127  15.523  1.00 31.51 ? 302 GLU   A OE1 1 
ATOM   1917 O  OE2 . GLU   A 1 268 ? 14.944  20.274  17.441  1.00 37.62 ? 302 GLU   A OE2 1 
ATOM   1918 N  N   . GLY   A 1 269 ? 11.964  18.348  11.168  1.00 25.08 ? 303 GLY   A N   1 
ATOM   1919 C  CA  . GLY   A 1 269 ? 11.810  18.672  9.772   1.00 27.15 ? 303 GLY   A CA  1 
ATOM   1920 C  C   . GLY   A 1 269 ? 12.202  17.541  8.838   1.00 27.37 ? 303 GLY   A C   1 
ATOM   1921 O  O   . GLY   A 1 269 ? 12.303  16.373  9.217   1.00 22.36 ? 303 GLY   A O   1 
ATOM   1922 N  N   . ALA   A 1 270 ? 12.433  17.918  7.588   1.00 27.77 ? 304 ALA   A N   1 
ATOM   1923 C  CA  . ALA   A 1 270 ? 12.648  16.953  6.532   1.00 25.05 ? 304 ALA   A CA  1 
ATOM   1924 C  C   . ALA   A 1 270 ? 13.969  16.232  6.721   1.00 27.98 ? 304 ALA   A C   1 
ATOM   1925 O  O   . ALA   A 1 270 ? 14.963  16.800  7.177   1.00 30.32 ? 304 ALA   A O   1 
ATOM   1926 C  CB  . ALA   A 1 270 ? 12.622  17.632  5.162   1.00 19.68 ? 304 ALA   A CB  1 
ATOM   1927 N  N   . GLY   A 1 271 ? 13.963  14.957  6.364   1.00 33.88 ? 305 GLY   A N   1 
ATOM   1928 C  CA  . GLY   A 1 271 ? 15.188  14.200  6.290   1.00 28.60 ? 305 GLY   A CA  1 
ATOM   1929 C  C   . GLY   A 1 271 ? 14.938  12.854  5.658   1.00 23.59 ? 305 GLY   A C   1 
ATOM   1930 O  O   . GLY   A 1 271 ? 13.856  12.568  5.144   1.00 23.44 ? 305 GLY   A O   1 
ATOM   1931 N  N   . LEU   A 1 272 ? 15.950  12.019  5.742   1.00 23.81 ? 306 LEU   A N   1 
ATOM   1932 C  CA  . LEU   A 1 272 ? 15.904  10.727  5.089   1.00 29.60 ? 306 LEU   A CA  1 
ATOM   1933 C  C   . LEU   A 1 272 ? 15.136  9.713   5.947   1.00 30.57 ? 306 LEU   A C   1 
ATOM   1934 O  O   . LEU   A 1 272 ? 15.515  9.430   7.090   1.00 27.82 ? 306 LEU   A O   1 
ATOM   1935 C  CB  . LEU   A 1 272 ? 17.330  10.276  4.813   1.00 28.91 ? 306 LEU   A CB  1 
ATOM   1936 C  CG  . LEU   A 1 272 ? 17.404  8.995   4.022   1.00 27.96 ? 306 LEU   A CG  1 
ATOM   1937 C  CD1 . LEU   A 1 272 ? 18.436  9.168   2.954   1.00 21.23 ? 306 LEU   A CD1 1 
ATOM   1938 C  CD2 . LEU   A 1 272 ? 17.750  7.894   4.990   1.00 29.10 ? 306 LEU   A CD2 1 
ATOM   1939 N  N   . GLN   A 1 273 ? 14.054  9.163   5.388   1.00 28.96 ? 307 GLN   A N   1 
ATOM   1940 C  CA  . GLN   A 1 273 ? 13.196  8.258   6.144   1.00 27.96 ? 307 GLN   A CA  1 
ATOM   1941 C  C   . GLN   A 1 273 ? 13.836  6.883   6.285   1.00 29.36 ? 307 GLN   A C   1 
ATOM   1942 O  O   . GLN   A 1 273 ? 14.129  6.436   7.400   1.00 30.46 ? 307 GLN   A O   1 
ATOM   1943 C  CB  . GLN   A 1 273 ? 11.819  8.130   5.475   1.00 27.29 ? 307 GLN   A CB  1 
ATOM   1944 C  CG  . GLN   A 1 273 ? 10.724  7.552   6.387   1.00 22.05 ? 307 GLN   A CG  1 
ATOM   1945 C  CD  . GLN   A 1 273 ? 9.673   6.774   5.606   1.00 25.64 ? 307 GLN   A CD  1 
ATOM   1946 O  OE1 . GLN   A 1 273 ? 9.972   6.207   4.556   1.00 22.50 ? 307 GLN   A OE1 1 
ATOM   1947 N  NE2 . GLN   A 1 273 ? 8.440   6.749   6.109   1.00 20.27 ? 307 GLN   A NE2 1 
ATOM   1948 N  N   . HIS   A 1 274 ? 14.032  6.178   5.169   1.00 27.09 ? 308 HIS   A N   1 
ATOM   1949 C  CA  . HIS   A 1 274 ? 14.583  4.839   5.250   1.00 22.71 ? 308 HIS   A CA  1 
ATOM   1950 C  C   . HIS   A 1 274 ? 15.502  4.522   4.076   1.00 28.20 ? 308 HIS   A C   1 
ATOM   1951 O  O   . HIS   A 1 274 ? 15.398  5.086   2.977   1.00 25.67 ? 308 HIS   A O   1 
ATOM   1952 C  CB  . HIS   A 1 274 ? 13.480  3.784   5.374   1.00 26.85 ? 308 HIS   A CB  1 
ATOM   1953 C  CG  . HIS   A 1 274 ? 12.684  3.545   4.123   1.00 31.10 ? 308 HIS   A CG  1 
ATOM   1954 N  ND1 . HIS   A 1 274 ? 11.635  4.351   3.737   1.00 27.92 ? 308 HIS   A ND1 1 
ATOM   1955 C  CD2 . HIS   A 1 274 ? 12.746  2.547   3.208   1.00 26.82 ? 308 HIS   A CD2 1 
ATOM   1956 C  CE1 . HIS   A 1 274 ? 11.096  3.868   2.633   1.00 27.73 ? 308 HIS   A CE1 1 
ATOM   1957 N  NE2 . HIS   A 1 274 ? 11.750  2.773   2.293   1.00 26.01 ? 308 HIS   A NE2 1 
ATOM   1958 N  N   . LEU   A 1 275 ? 16.436  3.630   4.366   1.00 25.00 ? 309 LEU   A N   1 
ATOM   1959 C  CA  . LEU   A 1 275 ? 17.319  3.029   3.389   1.00 26.64 ? 309 LEU   A CA  1 
ATOM   1960 C  C   . LEU   A 1 275 ? 16.797  1.642   3.060   1.00 25.18 ? 309 LEU   A C   1 
ATOM   1961 O  O   . LEU   A 1 275 ? 16.505  0.867   3.970   1.00 28.11 ? 309 LEU   A O   1 
ATOM   1962 C  CB  . LEU   A 1 275 ? 18.725  2.922   3.960   1.00 25.45 ? 309 LEU   A CB  1 
ATOM   1963 C  CG  . LEU   A 1 275 ? 19.297  4.251   4.387   1.00 21.41 ? 309 LEU   A CG  1 
ATOM   1964 C  CD1 . LEU   A 1 275 ? 20.627  3.983   5.069   1.00 23.68 ? 309 LEU   A CD1 1 
ATOM   1965 C  CD2 . LEU   A 1 275 ? 19.469  5.083   3.143   1.00 22.96 ? 309 LEU   A CD2 1 
ATOM   1966 N  N   . ALA   A 1 276 ? 16.677  1.324   1.777   1.00 28.75 ? 310 ALA   A N   1 
ATOM   1967 C  CA  . ALA   A 1 276 ? 16.259  -0.012  1.350   1.00 27.92 ? 310 ALA   A CA  1 
ATOM   1968 C  C   . ALA   A 1 276 ? 17.480  -0.785  0.879   1.00 27.47 ? 310 ALA   A C   1 
ATOM   1969 O  O   . ALA   A 1 276 ? 18.088  -0.441  -0.149  1.00 22.42 ? 310 ALA   A O   1 
ATOM   1970 C  CB  . ALA   A 1 276 ? 15.218  0.063   0.244   1.00 28.57 ? 310 ALA   A CB  1 
ATOM   1971 N  N   . LEU   A 1 277 ? 17.822  -1.836  1.622   1.00 23.47 ? 311 LEU   A N   1 
ATOM   1972 C  CA  . LEU   A 1 277 ? 19.031  -2.606  1.370   1.00 22.86 ? 311 LEU   A CA  1 
ATOM   1973 C  C   . LEU   A 1 277 ? 18.664  -3.929  0.696   1.00 33.41 ? 311 LEU   A C   1 
ATOM   1974 O  O   . LEU   A 1 277 ? 17.909  -4.738  1.261   1.00 33.99 ? 311 LEU   A O   1 
ATOM   1975 C  CB  . LEU   A 1 277 ? 19.790  -2.839  2.674   1.00 20.28 ? 311 LEU   A CB  1 
ATOM   1976 C  CG  . LEU   A 1 277 ? 19.892  -1.599  3.556   1.00 20.02 ? 311 LEU   A CG  1 
ATOM   1977 C  CD1 . LEU   A 1 277 ? 20.710  -1.847  4.806   1.00 15.96 ? 311 LEU   A CD1 1 
ATOM   1978 C  CD2 . LEU   A 1 277 ? 20.477  -0.459  2.759   1.00 23.89 ? 311 LEU   A CD2 1 
ATOM   1979 N  N   . MET   A 1 278 ? 19.195  -4.142  -0.511  1.00 31.55 ? 312 MET   A N   1 
ATOM   1980 C  CA  . MET   A 1 278 ? 18.928  -5.359  -1.264  1.00 28.67 ? 312 MET   A CA  1 
ATOM   1981 C  C   . MET   A 1 278 ? 19.816  -6.508  -0.787  1.00 30.65 ? 312 MET   A C   1 
ATOM   1982 O  O   . MET   A 1 278 ? 21.046  -6.378  -0.717  1.00 26.29 ? 312 MET   A O   1 
ATOM   1983 C  CB  . MET   A 1 278 ? 19.143  -5.101  -2.753  1.00 30.75 ? 312 MET   A CB  1 
ATOM   1984 C  CG  . MET   A 1 278 ? 18.818  -6.284  -3.684  1.00 34.52 ? 312 MET   A CG  1 
ATOM   1985 S  SD  . MET   A 1 278 ? 20.251  -7.323  -4.035  1.00 52.98 ? 312 MET   A SD  1 
ATOM   1986 C  CE  . MET   A 1 278 ? 19.569  -8.571  -5.143  1.00 41.72 ? 312 MET   A CE  1 
ATOM   1987 N  N   . SER   A 1 279 ? 19.185  -7.641  -0.482  1.00 28.59 ? 313 SER   A N   1 
ATOM   1988 C  CA  . SER   A 1 279 ? 19.883  -8.879  -0.164  1.00 27.62 ? 313 SER   A CA  1 
ATOM   1989 C  C   . SER   A 1 279 ? 19.874  -9.825  -1.361  1.00 31.88 ? 313 SER   A C   1 
ATOM   1990 O  O   . SER   A 1 279 ? 18.877  -9.916  -2.084  1.00 32.02 ? 313 SER   A O   1 
ATOM   1991 C  CB  . SER   A 1 279 ? 19.230  -9.580  1.027   1.00 26.73 ? 313 SER   A CB  1 
ATOM   1992 O  OG  . SER   A 1 279 ? 19.900  -10.792 1.305   1.00 27.67 ? 313 SER   A OG  1 
ATOM   1993 N  N   . GLU   A 1 280 ? 20.987  -10.540 -1.560  1.00 34.77 ? 314 GLU   A N   1 
ATOM   1994 C  CA  . GLU   A 1 280 ? 21.027  -11.653 -2.513  1.00 36.89 ? 314 GLU   A CA  1 
ATOM   1995 C  C   . GLU   A 1 280 ? 20.228  -12.860 -2.035  1.00 36.60 ? 314 GLU   A C   1 
ATOM   1996 O  O   . GLU   A 1 280 ? 20.013  -13.789 -2.819  1.00 37.06 ? 314 GLU   A O   1 
ATOM   1997 C  CB  . GLU   A 1 280 ? 22.471  -12.109 -2.763  1.00 32.55 ? 314 GLU   A CB  1 
ATOM   1998 C  CG  . GLU   A 1 280 ? 22.951  -13.140 -1.740  1.00 31.72 ? 314 GLU   A CG  1 
ATOM   1999 C  CD  . GLU   A 1 280 ? 24.437  -13.432 -1.848  1.00 43.98 ? 314 GLU   A CD  1 
ATOM   2000 O  OE1 . GLU   A 1 280 ? 25.048  -13.045 -2.882  1.00 38.83 ? 314 GLU   A OE1 1 
ATOM   2001 O  OE2 . GLU   A 1 280 ? 24.988  -14.046 -0.890  1.00 44.90 ? 314 GLU   A OE2 1 
ATOM   2002 N  N   . ASP   A 1 281 ? 19.811  -12.876 -0.767  1.00 32.17 ? 315 ASP   A N   1 
ATOM   2003 C  CA  . ASP   A 1 281 ? 19.080  -14.012 -0.204  1.00 34.03 ? 315 ASP   A CA  1 
ATOM   2004 C  C   . ASP   A 1 281 ? 18.418  -13.530 1.095   1.00 33.66 ? 315 ASP   A C   1 
ATOM   2005 O  O   . ASP   A 1 281 ? 18.981  -13.675 2.183   1.00 33.08 ? 315 ASP   A O   1 
ATOM   2006 C  CB  . ASP   A 1 281 ? 19.991  -15.190 0.031   1.00 34.78 ? 315 ASP   A CB  1 
ATOM   2007 C  CG  . ASP   A 1 281 ? 19.291  -16.330 0.701   1.00 32.93 ? 315 ASP   A CG  1 
ATOM   2008 O  OD1 . ASP   A 1 281 ? 18.039  -16.337 0.705   1.00 28.45 ? 315 ASP   A OD1 1 
ATOM   2009 O  OD2 . ASP   A 1 281 ? 20.008  -17.197 1.243   1.00 28.53 ? 315 ASP   A OD2 1 
ATOM   2010 N  N   . ILE   A 1 282 ? 17.211  -12.973 0.954   1.00 32.62 ? 316 ILE   A N   1 
ATOM   2011 C  CA  . ILE   A 1 282 ? 16.570  -12.267 2.059   1.00 32.50 ? 316 ILE   A CA  1 
ATOM   2012 C  C   . ILE   A 1 282 ? 16.258  -13.216 3.211   1.00 30.68 ? 316 ILE   A C   1 
ATOM   2013 O  O   . ILE   A 1 282 ? 16.345  -12.828 4.377   1.00 29.24 ? 316 ILE   A O   1 
ATOM   2014 C  CB  . ILE   A 1 282 ? 15.314  -11.529 1.551   1.00 29.58 ? 316 ILE   A CB  1 
ATOM   2015 C  CG1 . ILE   A 1 282 ? 14.770  -10.582 2.620   1.00 31.68 ? 316 ILE   A CG1 1 
ATOM   2016 C  CG2 . ILE   A 1 282 ? 14.246  -12.507 1.108   1.00 30.20 ? 316 ILE   A CG2 1 
ATOM   2017 C  CD1 . ILE   A 1 282 ? 13.856  -9.476  2.056   1.00 31.67 ? 316 ILE   A CD1 1 
ATOM   2018 N  N   . PHE   A 1 283 ? 15.931  -14.477 2.915   1.00 35.11 ? 317 PHE   A N   1 
ATOM   2019 C  CA  . PHE   A 1 283 ? 15.679  -15.440 3.980   1.00 27.83 ? 317 PHE   A CA  1 
ATOM   2020 C  C   . PHE   A 1 283 ? 16.898  -15.595 4.870   1.00 28.38 ? 317 PHE   A C   1 
ATOM   2021 O  O   . PHE   A 1 283 ? 16.786  -15.571 6.102   1.00 28.45 ? 317 PHE   A O   1 
ATOM   2022 C  CB  . PHE   A 1 283 ? 15.271  -16.785 3.388   1.00 33.01 ? 317 PHE   A CB  1 
ATOM   2023 C  CG  . PHE   A 1 283 ? 13.914  -16.777 2.758   1.00 31.46 ? 317 PHE   A CG  1 
ATOM   2024 C  CD1 . PHE   A 1 283 ? 13.021  -15.737 3.008   1.00 37.20 ? 317 PHE   A CD1 1 
ATOM   2025 C  CD2 . PHE   A 1 283 ? 13.536  -17.791 1.901   1.00 29.30 ? 317 PHE   A CD2 1 
ATOM   2026 C  CE1 . PHE   A 1 283 ? 11.766  -15.715 2.414   1.00 36.20 ? 317 PHE   A CE1 1 
ATOM   2027 C  CE2 . PHE   A 1 283 ? 12.286  -17.787 1.306   1.00 33.52 ? 317 PHE   A CE2 1 
ATOM   2028 C  CZ  . PHE   A 1 283 ? 11.397  -16.753 1.560   1.00 38.54 ? 317 PHE   A CZ  1 
ATOM   2029 N  N   . ARG   A 1 284 ? 18.079  -15.742 4.259   1.00 29.55 ? 318 ARG   A N   1 
ATOM   2030 C  CA  . ARG   A 1 284 ? 19.308  -15.901 5.038   1.00 32.42 ? 318 ARG   A CA  1 
ATOM   2031 C  C   . ARG   A 1 284 ? 19.626  -14.652 5.845   1.00 32.66 ? 318 ARG   A C   1 
ATOM   2032 O  O   . ARG   A 1 284 ? 20.006  -14.733 7.022   1.00 28.11 ? 318 ARG   A O   1 
ATOM   2033 C  CB  . ARG   A 1 284 ? 20.477  -16.220 4.116   1.00 31.84 ? 318 ARG   A CB  1 
ATOM   2034 C  CG  . ARG   A 1 284 ? 21.813  -16.188 4.804   1.00 32.71 ? 318 ARG   A CG  1 
ATOM   2035 C  CD  . ARG   A 1 284 ? 22.895  -16.692 3.872   1.00 41.95 ? 318 ARG   A CD  1 
ATOM   2036 N  NE  . ARG   A 1 284 ? 24.049  -15.798 3.872   1.00 42.81 ? 318 ARG   A NE  1 
ATOM   2037 C  CZ  . ARG   A 1 284 ? 24.585  -15.305 2.765   1.00 43.39 ? 318 ARG   A CZ  1 
ATOM   2038 N  NH1 . ARG   A 1 284 ? 24.063  -15.631 1.583   1.00 42.47 ? 318 ARG   A NH1 1 
ATOM   2039 N  NH2 . ARG   A 1 284 ? 25.633  -14.490 2.837   1.00 43.93 ? 318 ARG   A NH2 1 
ATOM   2040 N  N   . THR   A 1 285 ? 19.494  -13.487 5.214   1.00 29.22 ? 319 THR   A N   1 
ATOM   2041 C  CA  . THR   A 1 285 ? 19.770  -12.233 5.893   1.00 25.03 ? 319 THR   A CA  1 
ATOM   2042 C  C   . THR   A 1 285 ? 18.857  -12.039 7.091   1.00 23.01 ? 319 THR   A C   1 
ATOM   2043 O  O   . THR   A 1 285 ? 19.319  -11.729 8.191   1.00 23.56 ? 319 THR   A O   1 
ATOM   2044 C  CB  . THR   A 1 285 ? 19.613  -11.090 4.900   1.00 30.54 ? 319 THR   A CB  1 
ATOM   2045 O  OG1 . THR   A 1 285 ? 20.506  -11.300 3.793   1.00 28.10 ? 319 THR   A OG1 1 
ATOM   2046 C  CG2 . THR   A 1 285 ? 19.901  -9.754  5.578   1.00 25.57 ? 319 THR   A CG2 1 
ATOM   2047 N  N   . LEU   A 1 286 ? 17.555  -12.202 6.888   1.00 21.53 ? 320 LEU   A N   1 
ATOM   2048 C  CA  . LEU   A 1 286 ? 16.613  -12.059 7.987   1.00 22.76 ? 320 LEU   A CA  1 
ATOM   2049 C  C   . LEU   A 1 286 ? 16.921  -13.037 9.111   1.00 29.38 ? 320 LEU   A C   1 
ATOM   2050 O  O   . LEU   A 1 286 ? 16.836  -12.673 10.295  1.00 28.30 ? 320 LEU   A O   1 
ATOM   2051 C  CB  . LEU   A 1 286 ? 15.187  -12.256 7.483   1.00 22.64 ? 320 LEU   A CB  1 
ATOM   2052 C  CG  . LEU   A 1 286 ? 14.475  -10.914 7.357   1.00 30.16 ? 320 LEU   A CG  1 
ATOM   2053 C  CD1 . LEU   A 1 286 ? 14.278  -10.326 8.766   1.00 27.47 ? 320 LEU   A CD1 1 
ATOM   2054 C  CD2 . LEU   A 1 286 ? 15.276  -9.943  6.458   1.00 23.40 ? 320 LEU   A CD2 1 
ATOM   2055 N  N   . ARG   A 1 287 ? 17.268  -14.284 8.757   1.00 26.55 ? 321 ARG   A N   1 
ATOM   2056 C  CA  . ARG   A 1 287 ? 17.658  -15.271 9.754   1.00 25.79 ? 321 ARG   A CA  1 
ATOM   2057 C  C   . ARG   A 1 287 ? 18.776  -14.732 10.625  1.00 26.49 ? 321 ARG   A C   1 
ATOM   2058 O  O   . ARG   A 1 287 ? 18.694  -14.761 11.856  1.00 26.18 ? 321 ARG   A O   1 
ATOM   2059 C  CB  . ARG   A 1 287 ? 18.113  -16.572 9.074   1.00 35.97 ? 321 ARG   A CB  1 
ATOM   2060 C  CG  . ARG   A 1 287 ? 17.140  -17.729 9.125   1.00 37.76 ? 321 ARG   A CG  1 
ATOM   2061 C  CD  . ARG   A 1 287 ? 17.812  -19.085 8.839   1.00 40.47 ? 321 ARG   A CD  1 
ATOM   2062 N  NE  . ARG   A 1 287 ? 18.271  -19.232 7.460   1.00 50.34 ? 321 ARG   A NE  1 
ATOM   2063 C  CZ  . ARG   A 1 287 ? 17.469  -19.525 6.437   1.00 53.32 ? 321 ARG   A CZ  1 
ATOM   2064 N  NH1 . ARG   A 1 287 ? 16.165  -19.673 6.648   1.00 49.11 ? 321 ARG   A NH1 1 
ATOM   2065 N  NH2 . ARG   A 1 287 ? 17.964  -19.651 5.203   1.00 42.65 ? 321 ARG   A NH2 1 
ATOM   2066 N  N   . GLU   A 1 288 ? 19.839  -14.231 9.998   1.00 22.95 ? 322 GLU   A N   1 
ATOM   2067 C  CA  . GLU   A 1 288 ? 21.004  -13.836 10.776  1.00 28.29 ? 322 GLU   A CA  1 
ATOM   2068 C  C   . GLU   A 1 288 ? 20.752  -12.543 11.546  1.00 26.48 ? 322 GLU   A C   1 
ATOM   2069 O  O   . GLU   A 1 288 ? 21.275  -12.370 12.656  1.00 25.84 ? 322 GLU   A O   1 
ATOM   2070 C  CB  . GLU   A 1 288 ? 22.231  -13.697 9.863   1.00 33.43 ? 322 GLU   A CB  1 
ATOM   2071 C  CG  . GLU   A 1 288 ? 22.646  -14.961 9.084   1.00 26.65 ? 322 GLU   A CG  1 
ATOM   2072 C  CD  . GLU   A 1 288 ? 23.086  -16.132 9.984   1.00 34.73 ? 322 GLU   A CD  1 
ATOM   2073 O  OE1 . GLU   A 1 288 ? 22.768  -17.297 9.637   1.00 41.61 ? 322 GLU   A OE1 1 
ATOM   2074 O  OE2 . GLU   A 1 288 ? 23.740  -15.896 11.030  1.00 30.59 ? 322 GLU   A OE2 1 
ATOM   2075 N  N   . MET   A 1 289 ? 19.957  -11.630 10.980  1.00 26.39 ? 323 MET   A N   1 
ATOM   2076 C  CA  . MET   A 1 289 ? 19.665  -10.382 11.672  1.00 23.53 ? 323 MET   A CA  1 
ATOM   2077 C  C   . MET   A 1 289 ? 18.769  -10.626 12.874  1.00 25.18 ? 323 MET   A C   1 
ATOM   2078 O  O   . MET   A 1 289 ? 19.002  -10.066 13.957  1.00 25.47 ? 323 MET   A O   1 
ATOM   2079 C  CB  . MET   A 1 289 ? 19.016  -9.372  10.721  1.00 23.49 ? 323 MET   A CB  1 
ATOM   2080 C  CG  . MET   A 1 289 ? 19.965  -8.662  9.780   1.00 21.85 ? 323 MET   A CG  1 
ATOM   2081 S  SD  . MET   A 1 289 ? 19.123  -7.338  8.894   1.00 26.33 ? 323 MET   A SD  1 
ATOM   2082 C  CE  . MET   A 1 289 ? 18.950  -6.136  10.227  1.00 18.35 ? 323 MET   A CE  1 
ATOM   2083 N  N   . ARG   A 1 290 ? 17.731  -11.451 12.706  1.00 23.36 ? 324 ARG   A N   1 
ATOM   2084 C  CA  . ARG   A 1 290 ? 16.840  -11.696 13.835  1.00 26.64 ? 324 ARG   A CA  1 
ATOM   2085 C  C   . ARG   A 1 290 ? 17.528  -12.485 14.953  1.00 23.85 ? 324 ARG   A C   1 
ATOM   2086 O  O   . ARG   A 1 290 ? 17.118  -12.388 16.115  1.00 23.70 ? 324 ARG   A O   1 
ATOM   2087 C  CB  . ARG   A 1 290 ? 15.569  -12.407 13.367  1.00 22.45 ? 324 ARG   A CB  1 
ATOM   2088 C  CG  . ARG   A 1 290 ? 14.640  -11.572 12.520  1.00 18.59 ? 324 ARG   A CG  1 
ATOM   2089 C  CD  . ARG   A 1 290 ? 13.373  -12.363 12.226  1.00 20.61 ? 324 ARG   A CD  1 
ATOM   2090 N  NE  . ARG   A 1 290 ? 12.242  -11.534 11.816  1.00 25.72 ? 324 ARG   A NE  1 
ATOM   2091 C  CZ  . ARG   A 1 290 ? 11.450  -10.878 12.663  1.00 27.85 ? 324 ARG   A CZ  1 
ATOM   2092 N  NH1 . ARG   A 1 290 ? 11.675  -10.955 13.970  1.00 19.04 ? 324 ARG   A NH1 1 
ATOM   2093 N  NH2 . ARG   A 1 290 ? 10.430  -10.143 12.208  1.00 28.53 ? 324 ARG   A NH2 1 
ATOM   2094 N  N   . LYS   A 1 291 ? 18.582  -13.237 14.639  1.00 23.01 ? 325 LYS   A N   1 
ATOM   2095 C  CA  . LYS   A 1 291 ? 19.347  -13.886 15.696  1.00 26.84 ? 325 LYS   A CA  1 
ATOM   2096 C  C   . LYS   A 1 291 ? 20.030  -12.849 16.580  1.00 24.53 ? 325 LYS   A C   1 
ATOM   2097 O  O   . LYS   A 1 291 ? 20.131  -13.020 17.801  1.00 20.99 ? 325 LYS   A O   1 
ATOM   2098 C  CB  . LYS   A 1 291 ? 20.381  -14.853 15.094  1.00 30.39 ? 325 LYS   A CB  1 
ATOM   2099 C  CG  . LYS   A 1 291 ? 19.815  -16.189 14.608  1.00 25.73 ? 325 LYS   A CG  1 
ATOM   2100 C  CD  . LYS   A 1 291 ? 20.896  -17.261 14.523  1.00 36.67 ? 325 LYS   A CD  1 
ATOM   2101 C  CE  . LYS   A 1 291 ? 21.676  -17.226 13.210  1.00 37.64 ? 325 LYS   A CE  1 
ATOM   2102 N  NZ  . LYS   A 1 291 ? 22.703  -18.328 13.143  1.00 38.59 ? 325 LYS   A NZ  1 
ATOM   2103 N  N   . ARG   A 1 292 ? 20.482  -11.756 15.987  1.00 24.35 ? 326 ARG   A N   1 
ATOM   2104 C  CA  . ARG   A 1 292 ? 21.258  -10.780 16.729  1.00 23.75 ? 326 ARG   A CA  1 
ATOM   2105 C  C   . ARG   A 1 292 ? 20.422  -9.650  17.309  1.00 22.37 ? 326 ARG   A C   1 
ATOM   2106 O  O   . ARG   A 1 292 ? 20.985  -8.812  18.016  1.00 24.20 ? 326 ARG   A O   1 
ATOM   2107 C  CB  . ARG   A 1 292 ? 22.359  -10.228 15.832  1.00 21.21 ? 326 ARG   A CB  1 
ATOM   2108 C  CG  . ARG   A 1 292 ? 23.468  -11.239 15.587  1.00 22.20 ? 326 ARG   A CG  1 
ATOM   2109 C  CD  . ARG   A 1 292 ? 24.212  -10.938 14.333  1.00 20.27 ? 326 ARG   A CD  1 
ATOM   2110 N  NE  . ARG   A 1 292 ? 25.213  -11.941 13.986  1.00 22.55 ? 326 ARG   A NE  1 
ATOM   2111 C  CZ  . ARG   A 1 292 ? 25.003  -13.029 13.234  1.00 26.28 ? 326 ARG   A CZ  1 
ATOM   2112 N  NH1 . ARG   A 1 292 ? 23.802  -13.307 12.721  1.00 22.32 ? 326 ARG   A NH1 1 
ATOM   2113 N  NH2 . ARG   A 1 292 ? 26.019  -13.845 12.986  1.00 27.01 ? 326 ARG   A NH2 1 
ATOM   2114 N  N   . SER   A 1 293 ? 19.105  -9.641  17.065  1.00 19.39 ? 327 SER   A N   1 
ATOM   2115 C  CA  . SER   A 1 293 ? 18.254  -8.503  17.411  1.00 23.25 ? 327 SER   A CA  1 
ATOM   2116 C  C   . SER   A 1 293 ? 18.456  -8.057  18.850  1.00 27.85 ? 327 SER   A C   1 
ATOM   2117 O  O   . SER   A 1 293 ? 18.752  -6.886  19.124  1.00 30.46 ? 327 SER   A O   1 
ATOM   2118 C  CB  . SER   A 1 293 ? 16.782  -8.844  17.196  1.00 21.45 ? 327 SER   A CB  1 
ATOM   2119 O  OG  . SER   A 1 293 ? 16.568  -9.263  15.882  1.00 21.74 ? 327 SER   A OG  1 
ATOM   2120 N  N   . SER   A 1 294 ? 18.283  -8.977  19.786  1.00 26.44 ? 328 SER   A N   1 
ATOM   2121 C  CA  . SER   A 1 294 ? 18.370  -8.643  21.193  1.00 27.46 ? 328 SER   A CA  1 
ATOM   2122 C  C   . SER   A 1 294 ? 19.761  -8.861  21.796  1.00 25.78 ? 328 SER   A C   1 
ATOM   2123 O  O   . SER   A 1 294 ? 19.872  -8.934  23.025  1.00 24.99 ? 328 SER   A O   1 
ATOM   2124 C  CB  . SER   A 1 294 ? 17.311  -9.428  21.949  1.00 37.30 ? 328 SER   A CB  1 
ATOM   2125 O  OG  . SER   A 1 294 ? 16.030  -9.028  21.489  1.00 50.65 ? 328 SER   A OG  1 
ATOM   2126 N  N   . ILE   A 1 295 ? 20.820  -8.943  20.972  1.00 22.79 ? 329 ILE   A N   1 
ATOM   2127 C  CA  . ILE   A 1 295 ? 22.199  -8.994  21.469  1.00 20.15 ? 329 ILE   A CA  1 
ATOM   2128 C  C   . ILE   A 1 295 ? 23.065  -8.033  20.683  1.00 24.45 ? 329 ILE   A C   1 
ATOM   2129 O  O   . ILE   A 1 295 ? 24.207  -8.356  20.324  1.00 21.81 ? 329 ILE   A O   1 
ATOM   2130 C  CB  . ILE   A 1 295 ? 22.824  -10.397 21.401  1.00 26.46 ? 329 ILE   A CB  1 
ATOM   2131 C  CG1 . ILE   A 1 295 ? 22.715  -10.992 20.000  1.00 28.74 ? 329 ILE   A CG1 1 
ATOM   2132 C  CG2 . ILE   A 1 295 ? 22.232  -11.332 22.428  1.00 26.04 ? 329 ILE   A CG2 1 
ATOM   2133 C  CD1 . ILE   A 1 295 ? 23.636  -12.177 19.804  1.00 23.16 ? 329 ILE   A CD1 1 
ATOM   2134 N  N   . GLY   A 1 296 ? 22.525  -6.847  20.408  1.00 28.02 ? 330 GLY   A N   1 
ATOM   2135 C  CA  . GLY   A 1 296 ? 23.282  -5.732  19.870  1.00 22.03 ? 330 GLY   A CA  1 
ATOM   2136 C  C   . GLY   A 1 296 ? 22.779  -5.204  18.544  1.00 23.94 ? 330 GLY   A C   1 
ATOM   2137 O  O   . GLY   A 1 296 ? 23.092  -4.059  18.190  1.00 25.36 ? 330 GLY   A O   1 
ATOM   2138 N  N   . GLY   A 1 297 ? 22.015  -5.993  17.794  1.00 24.27 ? 331 GLY   A N   1 
ATOM   2139 C  CA  . GLY   A 1 297 ? 21.575  -5.584  16.477  1.00 22.38 ? 331 GLY   A CA  1 
ATOM   2140 C  C   . GLY   A 1 297 ? 20.271  -4.810  16.429  1.00 25.76 ? 331 GLY   A C   1 
ATOM   2141 O  O   . GLY   A 1 297 ? 20.009  -3.948  17.280  1.00 23.68 ? 331 GLY   A O   1 
ATOM   2142 N  N   . PHE   A 1 298 ? 19.441  -5.121  15.431  1.00 23.99 ? 332 PHE   A N   1 
ATOM   2143 C  CA  . PHE   A 1 298 ? 18.270  -4.328  15.084  1.00 17.79 ? 332 PHE   A CA  1 
ATOM   2144 C  C   . PHE   A 1 298 ? 17.008  -5.135  15.333  1.00 18.35 ? 332 PHE   A C   1 
ATOM   2145 O  O   . PHE   A 1 298 ? 16.938  -6.305  14.960  1.00 22.23 ? 332 PHE   A O   1 
ATOM   2146 C  CB  . PHE   A 1 298 ? 18.364  -3.882  13.620  1.00 21.61 ? 332 PHE   A CB  1 
ATOM   2147 C  CG  . PHE   A 1 298 ? 19.557  -2.982  13.333  1.00 22.40 ? 332 PHE   A CG  1 
ATOM   2148 C  CD1 . PHE   A 1 298 ? 19.526  -1.624  13.664  1.00 19.72 ? 332 PHE   A CD1 1 
ATOM   2149 C  CD2 . PHE   A 1 298 ? 20.717  -3.496  12.760  1.00 19.76 ? 332 PHE   A CD2 1 
ATOM   2150 C  CE1 . PHE   A 1 298 ? 20.633  -0.795  13.415  1.00 20.03 ? 332 PHE   A CE1 1 
ATOM   2151 C  CE2 . PHE   A 1 298 ? 21.822  -2.674  12.506  1.00 19.89 ? 332 PHE   A CE2 1 
ATOM   2152 C  CZ  . PHE   A 1 298 ? 21.779  -1.320  12.835  1.00 17.76 ? 332 PHE   A CZ  1 
ATOM   2153 N  N   . ASP   A 1 299 ? 16.033  -4.533  16.007  1.00 26.20 ? 333 ASP   A N   1 
ATOM   2154 C  CA  . ASP   A 1 299 ? 14.701  -5.123  16.097  1.00 25.00 ? 333 ASP   A CA  1 
ATOM   2155 C  C   . ASP   A 1 299 ? 13.952  -4.939  14.786  1.00 24.30 ? 333 ASP   A C   1 
ATOM   2156 O  O   . ASP   A 1 299 ? 14.357  -4.186  13.896  1.00 25.75 ? 333 ASP   A O   1 
ATOM   2157 C  CB  . ASP   A 1 299 ? 13.857  -4.485  17.199  1.00 26.32 ? 333 ASP   A CB  1 
ATOM   2158 C  CG  . ASP   A 1 299 ? 14.602  -4.310  18.488  1.00 29.12 ? 333 ASP   A CG  1 
ATOM   2159 O  OD1 . ASP   A 1 299 ? 14.889  -5.326  19.153  1.00 26.90 ? 333 ASP   A OD1 1 
ATOM   2160 O  OD2 . ASP   A 1 299 ? 14.889  -3.139  18.828  1.00 33.53 ? 333 ASP   A OD2 1 
ATOM   2161 N  N   . PHE   A 1 300 ? 12.821  -5.603  14.682  1.00 24.23 ? 334 PHE   A N   1 
ATOM   2162 C  CA  . PHE   A 1 300 ? 11.978  -5.421  13.518  1.00 25.43 ? 334 PHE   A CA  1 
ATOM   2163 C  C   . PHE   A 1 300 ? 10.579  -5.074  13.976  1.00 25.05 ? 334 PHE   A C   1 
ATOM   2164 O  O   . PHE   A 1 300 ? 10.163  -5.430  15.082  1.00 21.81 ? 334 PHE   A O   1 
ATOM   2165 C  CB  . PHE   A 1 300 ? 11.961  -6.661  12.624  1.00 23.19 ? 334 PHE   A CB  1 
ATOM   2166 C  CG  . PHE   A 1 300 ? 13.248  -6.884  11.922  1.00 22.77 ? 334 PHE   A CG  1 
ATOM   2167 C  CD1 . PHE   A 1 300 ? 13.426  -6.444  10.626  1.00 21.16 ? 334 PHE   A CD1 1 
ATOM   2168 C  CD2 . PHE   A 1 300 ? 14.299  -7.502  12.568  1.00 21.56 ? 334 PHE   A CD2 1 
ATOM   2169 C  CE1 . PHE   A 1 300 ? 14.621  -6.638  9.968   1.00 18.52 ? 334 PHE   A CE1 1 
ATOM   2170 C  CE2 . PHE   A 1 300 ? 15.501  -7.697  11.915  1.00 25.01 ? 334 PHE   A CE2 1 
ATOM   2171 C  CZ  . PHE   A 1 300 ? 15.662  -7.258  10.609  1.00 20.79 ? 334 PHE   A CZ  1 
ATOM   2172 N  N   . MET   A 1 301 ? 9.890   -4.335  13.116  1.00 25.91 ? 335 MET   A N   1 
ATOM   2173 C  CA  . MET   A 1 301 ? 8.498   -4.012  13.332  1.00 22.79 ? 335 MET   A CA  1 
ATOM   2174 C  C   . MET   A 1 301 ? 7.743   -5.290  13.651  1.00 27.74 ? 335 MET   A C   1 
ATOM   2175 O  O   . MET   A 1 301 ? 8.111   -6.357  13.148  1.00 32.80 ? 335 MET   A O   1 
ATOM   2176 C  CB  . MET   A 1 301 ? 7.917   -3.343  12.090  1.00 22.87 ? 335 MET   A CB  1 
ATOM   2177 C  CG  . MET   A 1 301 ? 8.368   -1.883  11.935  1.00 26.55 ? 335 MET   A CG  1 
ATOM   2178 S  SD  . MET   A 1 301 ? 7.810   -0.778  13.272  1.00 32.42 ? 335 MET   A SD  1 
ATOM   2179 C  CE  . MET   A 1 301 ? 6.041   -0.703  12.911  1.00 20.94 ? 335 MET   A CE  1 
ATOM   2180 N  N   . PRO   A 1 302 ? 6.738   -5.238  14.521  1.00 28.19 ? 336 PRO   A N   1 
ATOM   2181 C  CA  . PRO   A 1 302 ? 5.941   -6.437  14.791  1.00 33.47 ? 336 PRO   A CA  1 
ATOM   2182 C  C   . PRO   A 1 302 ? 5.353   -6.989  13.503  1.00 30.03 ? 336 PRO   A C   1 
ATOM   2183 O  O   . PRO   A 1 302 ? 5.042   -6.246  12.571  1.00 29.94 ? 336 PRO   A O   1 
ATOM   2184 C  CB  . PRO   A 1 302 ? 4.854   -5.936  15.749  1.00 32.46 ? 336 PRO   A CB  1 
ATOM   2185 C  CG  . PRO   A 1 302 ? 4.841   -4.472  15.584  1.00 30.01 ? 336 PRO   A CG  1 
ATOM   2186 C  CD  . PRO   A 1 302 ? 6.242   -4.073  15.256  1.00 26.02 ? 336 PRO   A CD  1 
ATOM   2187 N  N   . SER   A 1 303 ? 5.237   -8.313  13.452  1.00 32.48 ? 337 SER   A N   1 
ATOM   2188 C  CA  . SER   A 1 303 ? 4.942   -9.010  12.210  1.00 34.95 ? 337 SER   A CA  1 
ATOM   2189 C  C   . SER   A 1 303 ? 3.437   -9.035  11.922  1.00 38.08 ? 337 SER   A C   1 
ATOM   2190 O  O   . SER   A 1 303 ? 2.617   -8.904  12.836  1.00 39.58 ? 337 SER   A O   1 
ATOM   2191 C  CB  . SER   A 1 303 ? 5.495   -10.424 12.278  1.00 32.20 ? 337 SER   A CB  1 
ATOM   2192 O  OG  . SER   A 1 303 ? 6.900   -10.353 12.458  1.00 42.65 ? 337 SER   A OG  1 
ATOM   2193 N  N   . PRO   A 1 304 ? 3.055   -9.169  10.654  1.00 31.34 ? 338 PRO   A N   1 
ATOM   2194 C  CA  . PRO   A 1 304 ? 1.633   -9.203  10.302  1.00 32.55 ? 338 PRO   A CA  1 
ATOM   2195 C  C   . PRO   A 1 304 ? 0.937   -10.412 10.900  1.00 34.21 ? 338 PRO   A C   1 
ATOM   2196 O  O   . PRO   A 1 304 ? 1.604   -11.378 11.304  1.00 35.39 ? 338 PRO   A O   1 
ATOM   2197 C  CB  . PRO   A 1 304 ? 1.651   -9.263  8.766   1.00 33.34 ? 338 PRO   A CB  1 
ATOM   2198 C  CG  . PRO   A 1 304 ? 3.055   -9.516  8.382   1.00 32.36 ? 338 PRO   A CG  1 
ATOM   2199 C  CD  . PRO   A 1 304 ? 3.905   -8.986  9.472   1.00 28.90 ? 338 PRO   A CD  1 
ATOM   2200 N  N   . PRO   A 1 305 ? -0.398  -10.394 10.980  1.00 35.30 ? 339 PRO   A N   1 
ATOM   2201 C  CA  . PRO   A 1 305 ? -1.130  -11.514 11.564  1.00 40.78 ? 339 PRO   A CA  1 
ATOM   2202 C  C   . PRO   A 1 305 ? -1.216  -12.668 10.588  1.00 36.98 ? 339 PRO   A C   1 
ATOM   2203 O  O   . PRO   A 1 305 ? -1.132  -12.463 9.367   1.00 34.62 ? 339 PRO   A O   1 
ATOM   2204 C  CB  . PRO   A 1 305 ? -2.518  -10.918 11.835  1.00 36.59 ? 339 PRO   A CB  1 
ATOM   2205 C  CG  . PRO   A 1 305 ? -2.685  -9.977  10.775  1.00 35.23 ? 339 PRO   A CG  1 
ATOM   2206 C  CD  . PRO   A 1 305 ? -1.330  -9.347  10.545  1.00 41.02 ? 339 PRO   A CD  1 
ATOM   2207 N  N   . PRO   A 1 306 ? -1.418  -13.887 11.093  1.00 40.70 ? 340 PRO   A N   1 
ATOM   2208 C  CA  . PRO   A 1 306 ? -1.372  -15.073 10.215  1.00 40.97 ? 340 PRO   A CA  1 
ATOM   2209 C  C   . PRO   A 1 306 ? -2.314  -14.977 9.040   1.00 40.55 ? 340 PRO   A C   1 
ATOM   2210 O  O   . PRO   A 1 306 ? -1.994  -15.457 7.949   1.00 39.06 ? 340 PRO   A O   1 
ATOM   2211 C  CB  . PRO   A 1 306 ? -1.758  -16.225 11.155  1.00 37.50 ? 340 PRO   A CB  1 
ATOM   2212 C  CG  . PRO   A 1 306 ? -2.489  -15.572 12.284  1.00 42.17 ? 340 PRO   A CG  1 
ATOM   2213 C  CD  . PRO   A 1 306 ? -1.865  -14.217 12.458  1.00 39.85 ? 340 PRO   A CD  1 
ATOM   2214 N  N   . THR   A 1 307 ? -3.467  -14.343 9.229   1.00 42.17 ? 341 THR   A N   1 
ATOM   2215 C  CA  . THR   A 1 307 ? -4.355  -14.077 8.113   1.00 43.33 ? 341 THR   A CA  1 
ATOM   2216 C  C   . THR   A 1 307 ? -3.609  -13.424 6.952   1.00 47.16 ? 341 THR   A C   1 
ATOM   2217 O  O   . THR   A 1 307 ? -3.911  -13.703 5.785   1.00 51.76 ? 341 THR   A O   1 
ATOM   2218 C  CB  . THR   A 1 307 ? -5.501  -13.197 8.602   1.00 48.57 ? 341 THR   A CB  1 
ATOM   2219 O  OG1 . THR   A 1 307 ? -6.281  -12.728 7.496   1.00 48.82 ? 341 THR   A OG1 1 
ATOM   2220 C  CG2 . THR   A 1 307 ? -4.927  -12.042 9.319   1.00 41.41 ? 341 THR   A CG2 1 
ATOM   2221 N  N   . TYR   A 1 308 ? -2.614  -12.578 7.239   1.00 39.95 ? 342 TYR   A N   1 
ATOM   2222 C  CA  . TYR   A 1 308 ? -1.832  -12.016 6.141   1.00 40.81 ? 342 TYR   A CA  1 
ATOM   2223 C  C   . TYR   A 1 308 ? -1.110  -13.103 5.356   1.00 38.85 ? 342 TYR   A C   1 
ATOM   2224 O  O   . TYR   A 1 308 ? -0.952  -12.994 4.135   1.00 40.21 ? 342 TYR   A O   1 
ATOM   2225 C  CB  . TYR   A 1 308 ? -0.820  -10.990 6.658   1.00 42.82 ? 342 TYR   A CB  1 
ATOM   2226 C  CG  . TYR   A 1 308 ? 0.065   -10.410 5.563   1.00 38.89 ? 342 TYR   A CG  1 
ATOM   2227 C  CD1 . TYR   A 1 308 ? -0.343  -9.296  4.825   1.00 37.12 ? 342 TYR   A CD1 1 
ATOM   2228 C  CD2 . TYR   A 1 308 ? 1.309   -10.976 5.268   1.00 33.15 ? 342 TYR   A CD2 1 
ATOM   2229 C  CE1 . TYR   A 1 308 ? 0.462   -8.761  3.820   1.00 39.76 ? 342 TYR   A CE1 1 
ATOM   2230 C  CE2 . TYR   A 1 308 ? 2.119   -10.449 4.259   1.00 33.43 ? 342 TYR   A CE2 1 
ATOM   2231 C  CZ  . TYR   A 1 308 ? 1.689   -9.342  3.537   1.00 33.73 ? 342 TYR   A CZ  1 
ATOM   2232 O  OH  . TYR   A 1 308 ? 2.480   -8.821  2.544   1.00 26.30 ? 342 TYR   A OH  1 
ATOM   2233 N  N   . TYR   A 1 309 ? -0.653  -14.143 6.030   1.00 36.26 ? 343 TYR   A N   1 
ATOM   2234 C  CA  . TYR   A 1 309 ? 0.089   -15.172 5.324   1.00 40.04 ? 343 TYR   A CA  1 
ATOM   2235 C  C   . TYR   A 1 309 ? -0.805  -16.263 4.756   1.00 38.20 ? 343 TYR   A C   1 
ATOM   2236 O  O   . TYR   A 1 309 ? -0.440  -16.875 3.749   1.00 35.84 ? 343 TYR   A O   1 
ATOM   2237 C  CB  . TYR   A 1 309 ? 1.146   -15.767 6.249   1.00 38.16 ? 343 TYR   A CB  1 
ATOM   2238 C  CG  . TYR   A 1 309 ? 2.202   -14.760 6.600   1.00 37.22 ? 343 TYR   A CG  1 
ATOM   2239 C  CD1 . TYR   A 1 309 ? 2.121   -14.016 7.770   1.00 36.73 ? 343 TYR   A CD1 1 
ATOM   2240 C  CD2 . TYR   A 1 309 ? 3.267   -14.526 5.743   1.00 34.17 ? 343 TYR   A CD2 1 
ATOM   2241 C  CE1 . TYR   A 1 309 ? 3.092   -13.084 8.088   1.00 36.80 ? 343 TYR   A CE1 1 
ATOM   2242 C  CE2 . TYR   A 1 309 ? 4.236   -13.603 6.045   1.00 35.25 ? 343 TYR   A CE2 1 
ATOM   2243 C  CZ  . TYR   A 1 309 ? 4.150   -12.885 7.218   1.00 34.64 ? 343 TYR   A CZ  1 
ATOM   2244 O  OH  . TYR   A 1 309 ? 5.121   -11.969 7.512   1.00 29.79 ? 343 TYR   A OH  1 
ATOM   2245 N  N   . GLN   A 1 310 ? -1.966  -16.515 5.371   1.00 36.82 ? 344 GLN   A N   1 
ATOM   2246 C  CA  . GLN   A 1 310 ? -2.948  -17.397 4.753   1.00 42.03 ? 344 GLN   A CA  1 
ATOM   2247 C  C   . GLN   A 1 310 ? -3.358  -16.881 3.379   1.00 41.71 ? 344 GLN   A C   1 
ATOM   2248 O  O   . GLN   A 1 310 ? -3.649  -17.679 2.475   1.00 40.75 ? 344 GLN   A O   1 
ATOM   2249 C  CB  . GLN   A 1 310 ? -4.170  -17.554 5.662   1.00 43.81 ? 344 GLN   A CB  1 
ATOM   2250 N  N   . ASN   A 1 311 ? -3.344  -15.560 3.193   1.00 37.66 ? 345 ASN   A N   1 
ATOM   2251 C  CA  . ASN   A 1 311 ? -3.701  -14.937 1.927   1.00 41.70 ? 345 ASN   A CA  1 
ATOM   2252 C  C   . ASN   A 1 311 ? -2.533  -14.880 0.936   1.00 39.66 ? 345 ASN   A C   1 
ATOM   2253 O  O   . ASN   A 1 311 ? -2.726  -14.471 -0.219  1.00 34.80 ? 345 ASN   A O   1 
ATOM   2254 C  CB  . ASN   A 1 311 ? -4.257  -13.535 2.190   1.00 40.92 ? 345 ASN   A CB  1 
ATOM   2255 C  CG  . ASN   A 1 311 ? -4.497  -12.755 0.902   1.00 57.40 ? 345 ASN   A CG  1 
ATOM   2256 O  OD1 . ASN   A 1 311 ? -5.070  -13.284 -0.062  1.00 58.00 ? 345 ASN   A OD1 1 
ATOM   2257 N  ND2 . ASN   A 1 311 ? -4.041  -11.496 0.870   1.00 59.07 ? 345 ASN   A ND2 1 
ATOM   2258 N  N   . LEU   A 1 312 ? -1.340  -15.328 1.333   1.00 31.85 ? 346 LEU   A N   1 
ATOM   2259 C  CA  . LEU   A 1 312 ? -0.173  -15.174 0.470   1.00 33.03 ? 346 LEU   A CA  1 
ATOM   2260 C  C   . LEU   A 1 312 ? -0.274  -16.046 -0.783  1.00 37.09 ? 346 LEU   A C   1 
ATOM   2261 O  O   . LEU   A 1 312 ? -0.081  -15.562 -1.906  1.00 38.14 ? 346 LEU   A O   1 
ATOM   2262 C  CB  . LEU   A 1 312 ? 1.092   -15.480 1.274   1.00 33.03 ? 346 LEU   A CB  1 
ATOM   2263 C  CG  . LEU   A 1 312 ? 2.354   -14.728 0.893   1.00 35.59 ? 346 LEU   A CG  1 
ATOM   2264 C  CD1 . LEU   A 1 312 ? 2.002   -13.270 0.734   1.00 35.44 ? 346 LEU   A CD1 1 
ATOM   2265 C  CD2 . LEU   A 1 312 ? 3.434   -14.908 1.963   1.00 35.01 ? 346 LEU   A CD2 1 
ATOM   2266 N  N   . LYS   A 1 313 ? -0.605  -17.331 -0.616  1.00 35.49 ? 347 LYS   A N   1 
ATOM   2267 C  CA  . LYS   A 1 313 ? -0.653  -18.240 -1.756  1.00 34.55 ? 347 LYS   A CA  1 
ATOM   2268 C  C   . LYS   A 1 313 ? -1.643  -17.777 -2.824  1.00 39.79 ? 347 LYS   A C   1 
ATOM   2269 O  O   . LYS   A 1 313 ? -1.434  -18.045 -4.015  1.00 38.59 ? 347 LYS   A O   1 
ATOM   2270 C  CB  . LYS   A 1 313 ? -0.990  -19.660 -1.283  1.00 35.18 ? 347 LYS   A CB  1 
ATOM   2271 C  CG  . LYS   A 1 313 ? -0.800  -20.727 -2.362  1.00 31.54 ? 347 LYS   A CG  1 
ATOM   2272 C  CD  . LYS   A 1 313 ? -0.821  -22.142 -1.816  1.00 35.24 ? 347 LYS   A CD  1 
ATOM   2273 C  CE  . LYS   A 1 313 ? -0.742  -23.162 -2.957  1.00 39.94 ? 347 LYS   A CE  1 
ATOM   2274 N  NZ  . LYS   A 1 313 ? -0.770  -24.588 -2.476  1.00 39.97 ? 347 LYS   A NZ  1 
ATOM   2275 N  N   . LYS   A 1 314 ? -2.717  -17.076 -2.429  1.00 40.83 ? 348 LYS   A N   1 
ATOM   2276 C  CA  . LYS   A 1 314 ? -3.669  -16.586 -3.423  1.00 37.77 ? 348 LYS   A CA  1 
ATOM   2277 C  C   . LYS   A 1 314 ? -3.050  -15.533 -4.326  1.00 40.03 ? 348 LYS   A C   1 
ATOM   2278 O  O   . LYS   A 1 314 ? -3.503  -15.357 -5.465  1.00 41.35 ? 348 LYS   A O   1 
ATOM   2279 C  CB  . LYS   A 1 314 ? -4.924  -16.008 -2.758  1.00 38.40 ? 348 LYS   A CB  1 
ATOM   2280 N  N   . ARG   A 1 315 ? -2.035  -14.810 -3.853  1.00 42.01 ? 349 ARG   A N   1 
ATOM   2281 C  CA  . ARG   A 1 315 ? -1.535  -13.701 -4.653  1.00 37.74 ? 349 ARG   A CA  1 
ATOM   2282 C  C   . ARG   A 1 315 ? -0.179  -13.948 -5.274  1.00 34.23 ? 349 ARG   A C   1 
ATOM   2283 O  O   . ARG   A 1 315 ? 0.100   -13.381 -6.327  1.00 43.35 ? 349 ARG   A O   1 
ATOM   2284 C  CB  . ARG   A 1 315 ? -1.508  -12.394 -3.839  1.00 41.19 ? 349 ARG   A CB  1 
ATOM   2285 C  CG  . ARG   A 1 315 ? -1.223  -12.507 -2.349  1.00 46.13 ? 349 ARG   A CG  1 
ATOM   2286 C  CD  . ARG   A 1 315 ? -1.683  -11.263 -1.610  1.00 39.75 ? 349 ARG   A CD  1 
ATOM   2287 N  NE  . ARG   A 1 315 ? -0.723  -10.200 -1.582  1.00 43.93 ? 349 ARG   A NE  1 
ATOM   2288 C  CZ  . ARG   A 1 315 ? 0.131   -9.971  -0.622  1.00 41.91 ? 349 ARG   A CZ  1 
ATOM   2289 N  NH1 . ARG   A 1 315 ? 0.151   -10.709 0.453   1.00 36.85 ? 349 ARG   A NH1 1 
ATOM   2290 N  NH2 . ARG   A 1 315 ? 0.933   -8.958  -0.734  1.00 39.10 ? 349 ARG   A NH2 1 
ATOM   2291 N  N   . VAL   A 1 316 ? 0.660   -14.794 -4.693  1.00 34.65 ? 350 VAL   A N   1 
ATOM   2292 C  CA  . VAL   A 1 316 ? 1.953   -15.074 -5.311  1.00 37.67 ? 350 VAL   A CA  1 
ATOM   2293 C  C   . VAL   A 1 316 ? 2.193   -16.580 -5.355  1.00 36.77 ? 350 VAL   A C   1 
ATOM   2294 O  O   . VAL   A 1 316 ? 3.343   -17.035 -5.369  1.00 33.02 ? 350 VAL   A O   1 
ATOM   2295 C  CB  . VAL   A 1 316 ? 3.099   -14.346 -4.576  1.00 32.39 ? 350 VAL   A CB  1 
ATOM   2296 C  CG1 . VAL   A 1 316 ? 3.011   -12.858 -4.804  1.00 32.96 ? 350 VAL   A CG1 1 
ATOM   2297 C  CG2 . VAL   A 1 316 ? 3.075   -14.656 -3.088  1.00 31.94 ? 350 VAL   A CG2 1 
ATOM   2298 N  N   . GLY   A 1 317 ? 1.111   -17.360 -5.387  1.00 32.10 ? 351 GLY   A N   1 
ATOM   2299 C  CA  . GLY   A 1 317 ? 1.234   -18.805 -5.437  1.00 35.12 ? 351 GLY   A CA  1 
ATOM   2300 C  C   . GLY   A 1 317 ? 1.924   -19.339 -6.680  1.00 39.16 ? 351 GLY   A C   1 
ATOM   2301 O  O   . GLY   A 1 317 ? 2.224   -20.540 -6.730  1.00 34.99 ? 351 GLY   A O   1 
ATOM   2302 N  N   . ASP   A 1 318 ? 2.169   -18.484 -7.679  1.00 36.44 ? 352 ASP   A N   1 
ATOM   2303 C  CA  . ASP   A 1 318 ? 2.885   -18.841 -8.898  1.00 38.06 ? 352 ASP   A CA  1 
ATOM   2304 C  C   . ASP   A 1 318 ? 4.350   -18.420 -8.879  1.00 37.98 ? 352 ASP   A C   1 
ATOM   2305 O  O   . ASP   A 1 318 ? 5.102   -18.810 -9.777  1.00 33.68 ? 352 ASP   A O   1 
ATOM   2306 C  CB  . ASP   A 1 318 ? 2.201   -18.203 -10.110 1.00 33.51 ? 352 ASP   A CB  1 
ATOM   2307 C  CG  . ASP   A 1 318 ? 2.273   -16.679 -10.084 1.00 43.60 ? 352 ASP   A CG  1 
ATOM   2308 O  OD1 . ASP   A 1 318 ? 2.340   -16.071 -11.170 1.00 47.90 ? 352 ASP   A OD1 1 
ATOM   2309 O  OD2 . ASP   A 1 318 ? 2.277   -16.085 -8.979  1.00 38.18 ? 352 ASP   A OD2 1 
ATOM   2310 N  N   . VAL   A 1 319 ? 4.763   -17.632 -7.890  1.00 39.75 ? 353 VAL   A N   1 
ATOM   2311 C  CA  . VAL   A 1 319 ? 6.139   -17.188 -7.750  1.00 35.98 ? 353 VAL   A CA  1 
ATOM   2312 C  C   . VAL   A 1 319 ? 6.848   -17.898 -6.600  1.00 37.97 ? 353 VAL   A C   1 
ATOM   2313 O  O   . VAL   A 1 319 ? 8.003   -18.309 -6.741  1.00 38.59 ? 353 VAL   A O   1 
ATOM   2314 C  CB  . VAL   A 1 319 ? 6.180   -15.658 -7.567  1.00 36.05 ? 353 VAL   A CB  1 
ATOM   2315 C  CG1 . VAL   A 1 319 ? 7.601   -15.181 -7.387  1.00 34.13 ? 353 VAL   A CG1 1 
ATOM   2316 C  CG2 . VAL   A 1 319 ? 5.514   -14.975 -8.756  1.00 37.36 ? 353 VAL   A CG2 1 
ATOM   2317 N  N   . LEU   A 1 320 ? 6.165   -18.070 -5.463  1.00 34.42 ? 354 LEU   A N   1 
ATOM   2318 C  CA  . LEU   A 1 320 ? 6.743   -18.651 -4.256  1.00 36.70 ? 354 LEU   A CA  1 
ATOM   2319 C  C   . LEU   A 1 320 ? 6.150   -20.027 -3.975  1.00 36.93 ? 354 LEU   A C   1 
ATOM   2320 O  O   . LEU   A 1 320 ? 4.938   -20.230 -4.098  1.00 41.64 ? 354 LEU   A O   1 
ATOM   2321 C  CB  . LEU   A 1 320 ? 6.507   -17.745 -3.034  1.00 39.71 ? 354 LEU   A CB  1 
ATOM   2322 C  CG  . LEU   A 1 320 ? 7.126   -16.343 -2.975  1.00 38.79 ? 354 LEU   A CG  1 
ATOM   2323 C  CD1 . LEU   A 1 320 ? 6.720   -15.630 -1.685  1.00 38.52 ? 354 LEU   A CD1 1 
ATOM   2324 C  CD2 . LEU   A 1 320 ? 8.644   -16.411 -3.098  1.00 31.74 ? 354 LEU   A CD2 1 
ATOM   2325 N  N   . SER   A 1 321 ? 6.997   -20.968 -3.570  1.00 31.04 ? 355 SER   A N   1 
ATOM   2326 C  CA  . SER   A 1 321 ? 6.483   -22.281 -3.228  1.00 32.28 ? 355 SER   A CA  1 
ATOM   2327 C  C   . SER   A 1 321 ? 5.751   -22.229 -1.882  1.00 39.91 ? 355 SER   A C   1 
ATOM   2328 O  O   . SER   A 1 321 ? 5.810   -21.237 -1.146  1.00 36.42 ? 355 SER   A O   1 
ATOM   2329 C  CB  . SER   A 1 321 ? 7.616   -23.302 -3.192  1.00 30.19 ? 355 SER   A CB  1 
ATOM   2330 O  OG  . SER   A 1 321 ? 8.365   -23.213 -1.991  1.00 37.63 ? 355 SER   A OG  1 
ATOM   2331 N  N   . ASP   A 1 322 ? 5.038   -23.315 -1.564  1.00 38.93 ? 356 ASP   A N   1 
ATOM   2332 C  CA  . ASP   A 1 322 ? 4.356   -23.376 -0.278  1.00 34.08 ? 356 ASP   A CA  1 
ATOM   2333 C  C   . ASP   A 1 322 ? 5.363   -23.326 0.855   1.00 35.77 ? 356 ASP   A C   1 
ATOM   2334 O  O   . ASP   A 1 322 ? 5.114   -22.707 1.895   1.00 36.17 ? 356 ASP   A O   1 
ATOM   2335 C  CB  . ASP   A 1 322 ? 3.502   -24.640 -0.174  1.00 30.59 ? 356 ASP   A CB  1 
ATOM   2336 C  CG  . ASP   A 1 322 ? 2.577   -24.846 -1.387  1.00 50.51 ? 356 ASP   A CG  1 
ATOM   2337 O  OD1 . ASP   A 1 322 ? 1.349   -24.835 -1.177  1.00 48.91 ? 356 ASP   A OD1 1 
ATOM   2338 O  OD2 . ASP   A 1 322 ? 3.049   -25.028 -2.541  1.00 53.42 ? 356 ASP   A OD2 1 
ATOM   2339 N  N   . ASP   A 1 323 ? 6.522   -23.948 0.658   1.00 36.34 ? 357 ASP   A N   1 
ATOM   2340 C  CA  . ASP   A 1 323 ? 7.582   -23.878 1.656   1.00 43.68 ? 357 ASP   A CA  1 
ATOM   2341 C  C   . ASP   A 1 323 ? 8.134   -22.465 1.797   1.00 40.33 ? 357 ASP   A C   1 
ATOM   2342 O  O   . ASP   A 1 323 ? 8.457   -22.029 2.903   1.00 39.71 ? 357 ASP   A O   1 
ATOM   2343 C  CB  . ASP   A 1 323 ? 8.701   -24.850 1.289   1.00 48.18 ? 357 ASP   A CB  1 
ATOM   2344 C  CG  . ASP   A 1 323 ? 10.032  -24.459 1.896   1.00 59.50 ? 357 ASP   A CG  1 
ATOM   2345 O  OD1 . ASP   A 1 323 ? 10.890  -23.928 1.142   1.00 57.90 ? 357 ASP   A OD1 1 
ATOM   2346 O  OD2 . ASP   A 1 323 ? 10.216  -24.676 3.119   1.00 62.97 ? 357 ASP   A OD2 1 
ATOM   2347 N  N   . GLN   A 1 324 ? 8.281   -21.745 0.688   1.00 41.29 ? 358 GLN   A N   1 
ATOM   2348 C  CA  . GLN   A 1 324 ? 8.861   -20.405 0.760   1.00 42.46 ? 358 GLN   A CA  1 
ATOM   2349 C  C   . GLN   A 1 324 ? 7.891   -19.385 1.356   1.00 37.38 ? 358 GLN   A C   1 
ATOM   2350 O  O   . GLN   A 1 324 ? 8.317   -18.444 2.039   1.00 28.93 ? 358 GLN   A O   1 
ATOM   2351 C  CB  . GLN   A 1 324 ? 9.326   -19.991 -0.630  1.00 38.05 ? 358 GLN   A CB  1 
ATOM   2352 C  CG  . GLN   A 1 324 ? 10.464  -20.850 -1.118  1.00 37.11 ? 358 GLN   A CG  1 
ATOM   2353 C  CD  . GLN   A 1 324 ? 10.427  -21.064 -2.603  1.00 37.84 ? 358 GLN   A CD  1 
ATOM   2354 O  OE1 . GLN   A 1 324 ? 9.614   -20.469 -3.324  1.00 37.67 ? 358 GLN   A OE1 1 
ATOM   2355 N  NE2 . GLN   A 1 324 ? 11.300  -21.938 -3.079  1.00 40.34 ? 358 GLN   A NE2 1 
ATOM   2356 N  N   . ILE   A 1 325 ? 6.592   -19.543 1.098   1.00 42.15 ? 359 ILE   A N   1 
ATOM   2357 C  CA  . ILE   A 1 325 ? 5.594   -18.795 1.854   1.00 38.28 ? 359 ILE   A CA  1 
ATOM   2358 C  C   . ILE   A 1 325 ? 5.723   -19.102 3.338   1.00 33.67 ? 359 ILE   A C   1 
ATOM   2359 O  O   . ILE   A 1 325 ? 5.659   -18.205 4.180   1.00 33.86 ? 359 ILE   A O   1 
ATOM   2360 C  CB  . ILE   A 1 325 ? 4.189   -19.116 1.322   1.00 35.38 ? 359 ILE   A CB  1 
ATOM   2361 C  CG1 . ILE   A 1 325 ? 4.026   -18.509 -0.070  1.00 35.14 ? 359 ILE   A CG1 1 
ATOM   2362 C  CG2 . ILE   A 1 325 ? 3.113   -18.666 2.313   1.00 30.68 ? 359 ILE   A CG2 1 
ATOM   2363 C  CD1 . ILE   A 1 325 ? 2.729   -18.857 -0.724  1.00 34.41 ? 359 ILE   A CD1 1 
ATOM   2364 N  N   . LYS   A 1 326 ? 5.930   -20.369 3.680   1.00 37.99 ? 360 LYS   A N   1 
ATOM   2365 C  CA  . LYS   A 1 326 ? 6.087   -20.722 5.083   1.00 39.36 ? 360 LYS   A CA  1 
ATOM   2366 C  C   . LYS   A 1 326 ? 7.218   -19.922 5.722   1.00 38.67 ? 360 LYS   A C   1 
ATOM   2367 O  O   . LYS   A 1 326 ? 7.063   -19.400 6.829   1.00 41.27 ? 360 LYS   A O   1 
ATOM   2368 C  CB  . LYS   A 1 326 ? 6.326   -22.227 5.210   1.00 34.47 ? 360 LYS   A CB  1 
ATOM   2369 C  CG  . LYS   A 1 326 ? 5.864   -22.840 6.508   1.00 45.43 ? 360 LYS   A CG  1 
ATOM   2370 C  CD  . LYS   A 1 326 ? 5.788   -24.355 6.379   1.00 55.24 ? 360 LYS   A CD  1 
ATOM   2371 C  CE  . LYS   A 1 326 ? 5.252   -24.994 7.644   1.00 62.04 ? 360 LYS   A CE  1 
ATOM   2372 N  NZ  . LYS   A 1 326 ? 5.246   -26.479 7.534   1.00 60.97 ? 360 LYS   A NZ  1 
ATOM   2373 N  N   . GLU   A 1 327 ? 8.343   -19.768 5.011   1.00 37.80 ? 361 GLU   A N   1 
ATOM   2374 C  CA  . GLU   A 1 327 ? 9.517   -19.087 5.560   1.00 33.80 ? 361 GLU   A CA  1 
ATOM   2375 C  C   . GLU   A 1 327 ? 9.322   -17.572 5.657   1.00 36.05 ? 361 GLU   A C   1 
ATOM   2376 O  O   . GLU   A 1 327 ? 9.842   -16.946 6.586   1.00 35.71 ? 361 GLU   A O   1 
ATOM   2377 C  CB  . GLU   A 1 327 ? 10.749  -19.433 4.717   1.00 35.80 ? 361 GLU   A CB  1 
ATOM   2378 C  CG  . GLU   A 1 327 ? 12.096  -18.962 5.292   1.00 41.95 ? 361 GLU   A CG  1 
ATOM   2379 C  CD  . GLU   A 1 327 ? 13.247  -19.934 5.029   1.00 49.95 ? 361 GLU   A CD  1 
ATOM   2380 O  OE1 . GLU   A 1 327 ? 14.051  -20.121 5.964   1.00 57.93 ? 361 GLU   A OE1 1 
ATOM   2381 O  OE2 . GLU   A 1 327 ? 13.344  -20.524 3.921   1.00 49.12 ? 361 GLU   A OE2 1 
ATOM   2382 N  N   . CYS   A 1 328 ? 8.590   -16.963 4.717   1.00 35.18 ? 362 CYS   A N   1 
ATOM   2383 C  CA  . CYS   A 1 328 ? 8.157   -15.585 4.903   1.00 31.26 ? 362 CYS   A CA  1 
ATOM   2384 C  C   . CYS   A 1 328 ? 7.499   -15.400 6.268   1.00 38.18 ? 362 CYS   A C   1 
ATOM   2385 O  O   . CYS   A 1 328 ? 7.895   -14.529 7.056   1.00 39.27 ? 362 CYS   A O   1 
ATOM   2386 C  CB  . CYS   A 1 328 ? 7.196   -15.188 3.785   1.00 29.69 ? 362 CYS   A CB  1 
ATOM   2387 S  SG  . CYS   A 1 328 ? 8.011   -14.916 2.230   1.00 33.77 ? 362 CYS   A SG  1 
ATOM   2388 N  N   . GLU   A 1 329 ? 6.502   -16.234 6.577   1.00 36.42 ? 363 GLU   A N   1 
ATOM   2389 C  CA  . GLU   A 1 329 ? 5.750   -16.053 7.812   1.00 38.16 ? 363 GLU   A CA  1 
ATOM   2390 C  C   . GLU   A 1 329 ? 6.625   -16.247 9.038   1.00 36.49 ? 363 GLU   A C   1 
ATOM   2391 O  O   . GLU   A 1 329 ? 6.444   -15.554 10.045  1.00 42.94 ? 363 GLU   A O   1 
ATOM   2392 C  CB  . GLU   A 1 329 ? 4.562   -17.003 7.864   1.00 41.22 ? 363 GLU   A CB  1 
ATOM   2393 C  CG  . GLU   A 1 329 ? 3.923   -17.081 9.238   1.00 40.66 ? 363 GLU   A CG  1 
ATOM   2394 C  CD  . GLU   A 1 329 ? 2.748   -18.016 9.259   1.00 49.97 ? 363 GLU   A CD  1 
ATOM   2395 O  OE1 . GLU   A 1 329 ? 1.652   -17.594 9.691   1.00 51.28 ? 363 GLU   A OE1 1 
ATOM   2396 O  OE2 . GLU   A 1 329 ? 2.922   -19.174 8.811   1.00 61.13 ? 363 GLU   A OE2 1 
ATOM   2397 N  N   . GLU   A 1 330 ? 7.574   -17.182 8.985   1.00 34.95 ? 364 GLU   A N   1 
ATOM   2398 C  CA  . GLU   A 1 330 ? 8.430   -17.369 10.155  1.00 45.09 ? 364 GLU   A CA  1 
ATOM   2399 C  C   . GLU   A 1 330 ? 9.316   -16.156 10.373  1.00 36.37 ? 364 GLU   A C   1 
ATOM   2400 O  O   . GLU   A 1 330 ? 9.678   -15.849 11.514  1.00 32.90 ? 364 GLU   A O   1 
ATOM   2401 C  CB  . GLU   A 1 330 ? 9.288   -18.639 10.032  1.00 39.20 ? 364 GLU   A CB  1 
ATOM   2402 C  CG  . GLU   A 1 330 ? 8.562   -19.822 9.437   1.00 43.32 ? 364 GLU   A CG  1 
ATOM   2403 C  CD  . GLU   A 1 330 ? 9.045   -21.146 9.971   1.00 60.09 ? 364 GLU   A CD  1 
ATOM   2404 O  OE1 . GLU   A 1 330 ? 9.146   -21.283 11.214  1.00 63.16 ? 364 GLU   A OE1 1 
ATOM   2405 O  OE2 . GLU   A 1 330 ? 9.316   -22.049 9.145   1.00 56.13 ? 364 GLU   A OE2 1 
ATOM   2406 N  N   . LEU   A 1 331 ? 9.643   -15.442 9.300   1.00 31.89 ? 365 LEU   A N   1 
ATOM   2407 C  CA  . LEU   A 1 331 ? 10.513  -14.282 9.385   1.00 35.60 ? 365 LEU   A CA  1 
ATOM   2408 C  C   . LEU   A 1 331 ? 9.740   -12.964 9.397   1.00 36.65 ? 365 LEU   A C   1 
ATOM   2409 O  O   . LEU   A 1 331 ? 10.345  -11.910 9.628   1.00 34.99 ? 365 LEU   A O   1 
ATOM   2410 C  CB  . LEU   A 1 331 ? 11.531  -14.314 8.224   1.00 32.59 ? 365 LEU   A CB  1 
ATOM   2411 C  CG  . LEU   A 1 331 ? 12.460  -15.553 8.138   1.00 29.86 ? 365 LEU   A CG  1 
ATOM   2412 C  CD1 . LEU   A 1 331 ? 13.212  -15.618 6.813   1.00 24.54 ? 365 LEU   A CD1 1 
ATOM   2413 C  CD2 . LEU   A 1 331 ? 13.449  -15.645 9.322   1.00 25.63 ? 365 LEU   A CD2 1 
ATOM   2414 N  N   . GLY   A 1 332 ? 8.426   -13.001 9.186   1.00 33.66 ? 366 GLY   A N   1 
ATOM   2415 C  CA  . GLY   A 1 332 ? 7.621   -11.795 9.197   1.00 24.79 ? 366 GLY   A CA  1 
ATOM   2416 C  C   . GLY   A 1 332 ? 7.853   -10.909 7.997   1.00 30.58 ? 366 GLY   A C   1 
ATOM   2417 O  O   . GLY   A 1 332 ? 7.816   -9.680  8.124   1.00 30.27 ? 366 GLY   A O   1 
ATOM   2418 N  N   . ILE   A 1 333 ? 8.075   -11.507 6.824   1.00 32.47 ? 367 ILE   A N   1 
ATOM   2419 C  CA  . ILE   A 1 333 ? 8.348   -10.794 5.581   1.00 31.68 ? 367 ILE   A CA  1 
ATOM   2420 C  C   . ILE   A 1 333 ? 7.032   -10.397 4.915   1.00 30.30 ? 367 ILE   A C   1 
ATOM   2421 O  O   . ILE   A 1 333 ? 6.015   -11.080 5.064   1.00 28.35 ? 367 ILE   A O   1 
ATOM   2422 C  CB  . ILE   A 1 333 ? 9.233   -11.676 4.668   1.00 30.32 ? 367 ILE   A CB  1 
ATOM   2423 C  CG1 . ILE   A 1 333 ? 10.597  -11.888 5.331   1.00 29.96 ? 367 ILE   A CG1 1 
ATOM   2424 C  CG2 . ILE   A 1 333 ? 9.384   -11.092 3.264   1.00 23.04 ? 367 ILE   A CG2 1 
ATOM   2425 C  CD1 . ILE   A 1 333 ? 11.649  -12.530 4.432   1.00 30.47 ? 367 ILE   A CD1 1 
ATOM   2426 N  N   . LEU   A 1 334 ? 7.047   -9.267  4.191   1.00 30.32 ? 368 LEU   A N   1 
ATOM   2427 C  CA  . LEU   A 1 334 ? 5.908   -8.769  3.421   1.00 25.77 ? 368 LEU   A CA  1 
ATOM   2428 C  C   . LEU   A 1 334 ? 6.154   -8.954  1.928   1.00 27.45 ? 368 LEU   A C   1 
ATOM   2429 O  O   . LEU   A 1 334 ? 7.282   -8.800  1.458   1.00 25.93 ? 368 LEU   A O   1 
ATOM   2430 C  CB  . LEU   A 1 334 ? 5.655   -7.287  3.689   1.00 25.17 ? 368 LEU   A CB  1 
ATOM   2431 C  CG  . LEU   A 1 334 ? 5.654   -6.684  5.095   1.00 27.34 ? 368 LEU   A CG  1 
ATOM   2432 C  CD1 . LEU   A 1 334 ? 5.456   -5.191  4.949   1.00 37.44 ? 368 LEU   A CD1 1 
ATOM   2433 C  CD2 . LEU   A 1 334 ? 4.554   -7.250  5.935   1.00 23.45 ? 368 LEU   A CD2 1 
ATOM   2434 N  N   . VAL   A 1 335 ? 5.095   -9.268  1.178   1.00 27.19 ? 369 VAL   A N   1 
ATOM   2435 C  CA  . VAL   A 1 335 ? 5.192   -9.510  -0.259  1.00 30.46 ? 369 VAL   A CA  1 
ATOM   2436 C  C   . VAL   A 1 335 ? 4.244   -8.556  -0.971  1.00 32.53 ? 369 VAL   A C   1 
ATOM   2437 O  O   . VAL   A 1 335 ? 3.119   -8.342  -0.514  1.00 34.36 ? 369 VAL   A O   1 
ATOM   2438 C  CB  . VAL   A 1 335 ? 4.857   -10.974 -0.644  1.00 25.75 ? 369 VAL   A CB  1 
ATOM   2439 C  CG1 . VAL   A 1 335 ? 5.139   -11.220 -2.111  1.00 20.42 ? 369 VAL   A CG1 1 
ATOM   2440 C  CG2 . VAL   A 1 335 ? 5.624   -11.959 0.204   1.00 26.96 ? 369 VAL   A CG2 1 
ATOM   2441 N  N   . ASP   A 1 336 ? 4.698   -7.986  -2.088  1.00 33.67 ? 370 ASP   A N   1 
ATOM   2442 C  CA  . ASP   A 1 336 ? 3.852   -7.206  -2.983  1.00 33.71 ? 370 ASP   A CA  1 
ATOM   2443 C  C   . ASP   A 1 336 ? 4.179   -7.579  -4.421  1.00 36.40 ? 370 ASP   A C   1 
ATOM   2444 O  O   . ASP   A 1 336 ? 5.272   -8.066  -4.724  1.00 36.98 ? 370 ASP   A O   1 
ATOM   2445 C  CB  . ASP   A 1 336 ? 4.027   -5.696  -2.790  1.00 30.93 ? 370 ASP   A CB  1 
ATOM   2446 C  CG  . ASP   A 1 336 ? 2.811   -4.912  -3.257  1.00 42.04 ? 370 ASP   A CG  1 
ATOM   2447 O  OD1 . ASP   A 1 336 ? 1.724   -5.535  -3.394  1.00 45.70 ? 370 ASP   A OD1 1 
ATOM   2448 O  OD2 . ASP   A 1 336 ? 2.933   -3.683  -3.492  1.00 43.12 ? 370 ASP   A OD2 1 
ATOM   2449 N  N   . ARG   A 1 337 ? 3.226   -7.334  -5.318  1.00 37.70 ? 371 ARG   A N   1 
ATOM   2450 C  CA  . ARG   A 1 337 ? 3.369   -7.755  -6.702  1.00 37.67 ? 371 ARG   A CA  1 
ATOM   2451 C  C   . ARG   A 1 337 ? 3.085   -6.600  -7.652  1.00 43.27 ? 371 ARG   A C   1 
ATOM   2452 O  O   . ARG   A 1 337 ? 2.158   -5.814  -7.434  1.00 44.51 ? 371 ARG   A O   1 
ATOM   2453 C  CB  . ARG   A 1 337 ? 2.447   -8.932  -7.004  1.00 37.67 ? 371 ARG   A CB  1 
ATOM   2454 C  CG  . ARG   A 1 337 ? 2.778   -9.620  -8.285  1.00 39.79 ? 371 ARG   A CG  1 
ATOM   2455 C  CD  . ARG   A 1 337 ? 2.334   -11.051 -8.281  1.00 40.22 ? 371 ARG   A CD  1 
ATOM   2456 N  NE  . ARG   A 1 337 ? 2.803   -11.714 -9.487  1.00 41.92 ? 371 ARG   A NE  1 
ATOM   2457 C  CZ  . ARG   A 1 337 ? 2.564   -12.980 -9.782  1.00 38.13 ? 371 ARG   A CZ  1 
ATOM   2458 N  NH1 . ARG   A 1 337 ? 1.864   -13.728 -8.946  1.00 40.37 ? 371 ARG   A NH1 1 
ATOM   2459 N  NH2 . ARG   A 1 337 ? 3.038   -13.495 -10.905 1.00 38.16 ? 371 ARG   A NH2 1 
ATOM   2460 N  N   . ASP   A 1 338 ? 3.884   -6.524  -8.716  1.00 46.85 ? 372 ASP   A N   1 
ATOM   2461 C  CA  . ASP   A 1 338 ? 3.847   -5.455  -9.705  1.00 52.45 ? 372 ASP   A CA  1 
ATOM   2462 C  C   . ASP   A 1 338 ? 2.895   -5.819  -10.843 1.00 52.17 ? 372 ASP   A C   1 
ATOM   2463 O  O   . ASP   A 1 338 ? 2.173   -6.815  -10.793 1.00 50.05 ? 372 ASP   A O   1 
ATOM   2464 C  CB  . ASP   A 1 338 ? 5.255   -5.211  -10.264 1.00 47.84 ? 372 ASP   A CB  1 
ATOM   2465 C  CG  . ASP   A 1 338 ? 5.578   -3.744  -10.450 1.00 51.28 ? 372 ASP   A CG  1 
ATOM   2466 O  OD1 . ASP   A 1 338 ? 4.662   -2.904  -10.307 1.00 56.67 ? 372 ASP   A OD1 1 
ATOM   2467 O  OD2 . ASP   A 1 338 ? 6.757   -3.436  -10.753 1.00 50.92 ? 372 ASP   A OD2 1 
ATOM   2468 N  N   . ASP   A 1 339 ? 2.883   -4.989  -11.884 1.00 60.95 ? 373 ASP   A N   1 
ATOM   2469 C  CA  . ASP   A 1 339 ? 2.516   -5.430  -13.223 1.00 54.42 ? 373 ASP   A CA  1 
ATOM   2470 C  C   . ASP   A 1 339 ? 3.582   -6.321  -13.828 1.00 52.24 ? 373 ASP   A C   1 
ATOM   2471 O  O   . ASP   A 1 339 ? 3.336   -6.934  -14.867 1.00 60.10 ? 373 ASP   A O   1 
ATOM   2472 C  CB  . ASP   A 1 339 ? 2.323   -4.220  -14.141 1.00 59.90 ? 373 ASP   A CB  1 
ATOM   2473 C  CG  . ASP   A 1 339 ? 3.423   -3.166  -13.952 1.00 66.40 ? 373 ASP   A CG  1 
ATOM   2474 O  OD1 . ASP   A 1 339 ? 4.159   -2.866  -14.923 1.00 60.86 ? 373 ASP   A OD1 1 
ATOM   2475 O  OD2 . ASP   A 1 339 ? 3.547   -2.636  -12.821 1.00 67.70 ? 373 ASP   A OD2 1 
ATOM   2476 N  N   . GLN   A 1 340 ? 4.753   -6.399  -13.201 1.00 55.73 ? 374 GLN   A N   1 
ATOM   2477 C  CA  . GLN   A 1 340 ? 5.956   -6.933  -13.829 1.00 55.60 ? 374 GLN   A CA  1 
ATOM   2478 C  C   . GLN   A 1 340 ? 6.808   -7.804  -12.917 1.00 51.58 ? 374 GLN   A C   1 
ATOM   2479 O  O   . GLN   A 1 340 ? 7.613   -8.580  -13.438 1.00 59.26 ? 374 GLN   A O   1 
ATOM   2480 C  CB  . GLN   A 1 340 ? 6.812   -5.773  -14.356 1.00 62.39 ? 374 GLN   A CB  1 
ATOM   2481 C  CG  . GLN   A 1 340 ? 8.071   -6.144  -15.133 1.00 69.10 ? 374 GLN   A CG  1 
ATOM   2482 C  CD  . GLN   A 1 340 ? 9.040   -4.963  -15.257 1.00 75.14 ? 374 GLN   A CD  1 
ATOM   2483 O  OE1 . GLN   A 1 340 ? 8.786   -3.866  -14.739 1.00 68.77 ? 374 GLN   A OE1 1 
ATOM   2484 N  NE2 . GLN   A 1 340 ? 10.159  -5.190  -15.942 1.00 79.27 ? 374 GLN   A NE2 1 
ATOM   2485 N  N   . GLY   A 1 341 ? 6.668   -7.733  -11.595 1.00 45.02 ? 375 GLY   A N   1 
ATOM   2486 C  CA  . GLY   A 1 341 ? 7.486   -8.547  -10.721 1.00 46.57 ? 375 GLY   A CA  1 
ATOM   2487 C  C   . GLY   A 1 341 ? 6.950   -8.617  -9.304  1.00 45.07 ? 375 GLY   A C   1 
ATOM   2488 O  O   . GLY   A 1 341 ? 5.842   -8.156  -9.015  1.00 43.55 ? 375 GLY   A O   1 
ATOM   2489 N  N   . THR   A 1 342 ? 7.774   -9.197  -8.415  1.00 39.51 ? 376 THR   A N   1 
ATOM   2490 C  CA  . THR   A 1 342 ? 7.405   -9.504  -7.036  1.00 38.77 ? 376 THR   A CA  1 
ATOM   2491 C  C   . THR   A 1 342 ? 8.484   -9.018  -6.070  1.00 35.67 ? 376 THR   A C   1 
ATOM   2492 O  O   . THR   A 1 342 ? 9.684   -9.127  -6.342  1.00 33.96 ? 376 THR   A O   1 
ATOM   2493 C  CB  . THR   A 1 342 ? 7.165   -11.019 -6.861  1.00 34.76 ? 376 THR   A CB  1 
ATOM   2494 O  OG1 . THR   A 1 342 ? 6.004   -11.390 -7.613  1.00 45.08 ? 376 THR   A OG1 1 
ATOM   2495 C  CG2 . THR   A 1 342 ? 6.963   -11.394 -5.389  1.00 25.07 ? 376 THR   A CG2 1 
ATOM   2496 N  N   . LEU   A 1 343 ? 8.049   -8.513  -4.922  1.00 32.71 ? 377 LEU   A N   1 
ATOM   2497 C  CA  . LEU   A 1 343 ? 8.921   -7.853  -3.966  1.00 30.47 ? 377 LEU   A CA  1 
ATOM   2498 C  C   . LEU   A 1 343 ? 8.814   -8.502  -2.586  1.00 28.10 ? 377 LEU   A C   1 
ATOM   2499 O  O   . LEU   A 1 343 ? 7.719   -8.628  -2.028  1.00 26.07 ? 377 LEU   A O   1 
ATOM   2500 C  CB  . LEU   A 1 343 ? 8.547   -6.371  -3.930  1.00 30.92 ? 377 LEU   A CB  1 
ATOM   2501 C  CG  . LEU   A 1 343 ? 9.069   -5.377  -2.918  1.00 40.09 ? 377 LEU   A CG  1 
ATOM   2502 C  CD1 . LEU   A 1 343 ? 8.861   -3.974  -3.433  1.00 37.84 ? 377 LEU   A CD1 1 
ATOM   2503 C  CD2 . LEU   A 1 343 ? 8.261   -5.512  -1.672  1.00 42.72 ? 377 LEU   A CD2 1 
ATOM   2504 N  N   . LEU   A 1 344 ? 9.948   -8.893  -2.027  1.00 25.14 ? 378 LEU   A N   1 
ATOM   2505 C  CA  . LEU   A 1 344 ? 10.024  -9.307  -0.635  1.00 25.33 ? 378 LEU   A CA  1 
ATOM   2506 C  C   . LEU   A 1 344 ? 10.679  -8.183  0.152   1.00 29.98 ? 378 LEU   A C   1 
ATOM   2507 O  O   . LEU   A 1 344 ? 11.680  -7.614  -0.298  1.00 33.26 ? 378 LEU   A O   1 
ATOM   2508 C  CB  . LEU   A 1 344 ? 10.821  -10.603 -0.496  1.00 31.91 ? 378 LEU   A CB  1 
ATOM   2509 C  CG  . LEU   A 1 344 ? 10.414  -11.766 -1.409  1.00 28.13 ? 378 LEU   A CG  1 
ATOM   2510 C  CD1 . LEU   A 1 344 ? 11.217  -12.965 -1.033  1.00 31.49 ? 378 LEU   A CD1 1 
ATOM   2511 C  CD2 . LEU   A 1 344 ? 8.940   -12.088 -1.295  1.00 28.16 ? 378 LEU   A CD2 1 
ATOM   2512 N  N   . GLN   A 1 345 ? 10.110  -7.851  1.310   1.00 28.07 ? 379 GLN   A N   1 
ATOM   2513 C  CA  . GLN   A 1 345 ? 10.511  -6.648  2.026   1.00 26.68 ? 379 GLN   A CA  1 
ATOM   2514 C  C   . GLN   A 1 345 ? 10.208  -6.792  3.506   1.00 24.73 ? 379 GLN   A C   1 
ATOM   2515 O  O   . GLN   A 1 345 ? 9.220   -7.417  3.896   1.00 27.34 ? 379 GLN   A O   1 
ATOM   2516 C  CB  . GLN   A 1 345 ? 9.792   -5.416  1.489   1.00 27.50 ? 379 GLN   A CB  1 
ATOM   2517 C  CG  . GLN   A 1 345 ? 8.292   -5.390  1.768   1.00 26.82 ? 379 GLN   A CG  1 
ATOM   2518 C  CD  . GLN   A 1 345 ? 7.611   -4.152  1.181   1.00 33.74 ? 379 GLN   A CD  1 
ATOM   2519 O  OE1 . GLN   A 1 345 ? 6.386   -4.093  1.061   1.00 38.68 ? 379 GLN   A OE1 1 
ATOM   2520 N  NE2 . GLN   A 1 345 ? 8.413   -3.169  0.787   1.00 32.04 ? 379 GLN   A NE2 1 
ATOM   2521 N  N   . ILE   A 1 346 ? 11.056  -6.197  4.340   1.00 23.99 ? 380 ILE   A N   1 
ATOM   2522 C  CA  . ILE   A 1 346 ? 10.768  -6.144  5.769   1.00 25.99 ? 380 ILE   A CA  1 
ATOM   2523 C  C   . ILE   A 1 346 ? 11.374  -4.859  6.335   1.00 22.64 ? 380 ILE   A C   1 
ATOM   2524 O  O   . ILE   A 1 346 ? 12.268  -4.257  5.740   1.00 22.21 ? 380 ILE   A O   1 
ATOM   2525 C  CB  . ILE   A 1 346 ? 11.256  -7.432  6.497   1.00 18.56 ? 380 ILE   A CB  1 
ATOM   2526 C  CG1 . ILE   A 1 346 ? 10.466  -7.646  7.779   1.00 19.86 ? 380 ILE   A CG1 1 
ATOM   2527 C  CG2 . ILE   A 1 346 ? 12.748  -7.401  6.780   1.00 20.41 ? 380 ILE   A CG2 1 
ATOM   2528 C  CD1 . ILE   A 1 346 ? 10.869  -8.853  8.561   1.00 24.38 ? 380 ILE   A CD1 1 
ATOM   2529 N  N   . PHE   A 1 347 ? 10.858  -4.420  7.485   1.00 23.50 ? 381 PHE   A N   1 
ATOM   2530 C  CA  . PHE   A 1 347 ? 11.223  -3.119  8.049   1.00 27.31 ? 381 PHE   A CA  1 
ATOM   2531 C  C   . PHE   A 1 347 ? 11.626  -3.260  9.503   1.00 21.56 ? 381 PHE   A C   1 
ATOM   2532 O  O   . PHE   A 1 347 ? 10.855  -3.778  10.311  1.00 23.95 ? 381 PHE   A O   1 
ATOM   2533 C  CB  . PHE   A 1 347 ? 10.074  -2.102  7.955   1.00 21.11 ? 381 PHE   A CB  1 
ATOM   2534 C  CG  . PHE   A 1 347 ? 9.614   -1.848  6.564   1.00 27.43 ? 381 PHE   A CG  1 
ATOM   2535 C  CD1 . PHE   A 1 347 ? 8.615   -2.638  5.997   1.00 25.87 ? 381 PHE   A CD1 1 
ATOM   2536 C  CD2 . PHE   A 1 347 ? 10.183  -0.835  5.808   1.00 25.33 ? 381 PHE   A CD2 1 
ATOM   2537 C  CE1 . PHE   A 1 347 ? 8.182   -2.414  4.713   1.00 28.85 ? 381 PHE   A CE1 1 
ATOM   2538 C  CE2 . PHE   A 1 347 ? 9.754   -0.604  4.511   1.00 31.28 ? 381 PHE   A CE2 1 
ATOM   2539 C  CZ  . PHE   A 1 347 ? 8.753   -1.393  3.961   1.00 31.38 ? 381 PHE   A CZ  1 
ATOM   2540 N  N   . THR   A 1 348 ? 12.808  -2.744  9.830   1.00 21.59 ? 382 THR   A N   1 
ATOM   2541 C  CA  . THR   A 1 348 ? 13.274  -2.615  11.206  1.00 26.84 ? 382 THR   A CA  1 
ATOM   2542 C  C   . THR   A 1 348 ? 12.535  -1.507  11.960  1.00 23.51 ? 382 THR   A C   1 
ATOM   2543 O  O   . THR   A 1 348 ? 11.801  -0.692  11.394  1.00 19.65 ? 382 THR   A O   1 
ATOM   2544 C  CB  . THR   A 1 348 ? 14.757  -2.266  11.255  1.00 22.76 ? 382 THR   A CB  1 
ATOM   2545 O  OG1 . THR   A 1 348 ? 14.892  -0.839  11.142  1.00 17.92 ? 382 THR   A OG1 1 
ATOM   2546 C  CG2 . THR   A 1 348 ? 15.494  -2.958  10.118  1.00 20.42 ? 382 THR   A CG2 1 
ATOM   2547 N  N   . LYS   A 1 349 ? 12.762  -1.494  13.266  1.00 23.99 ? 383 LYS   A N   1 
ATOM   2548 C  CA  . LYS   A 1 349 ? 12.376  -0.397  14.132  1.00 20.62 ? 383 LYS   A CA  1 
ATOM   2549 C  C   . LYS   A 1 349 ? 13.433  0.697   13.951  1.00 22.05 ? 383 LYS   A C   1 
ATOM   2550 O  O   . LYS   A 1 349 ? 14.378  0.532   13.181  1.00 26.73 ? 383 LYS   A O   1 
ATOM   2551 C  CB  . LYS   A 1 349 ? 12.209  -0.934  15.553  1.00 20.22 ? 383 LYS   A CB  1 
ATOM   2552 C  CG  . LYS   A 1 349 ? 10.779  -1.334  15.858  1.00 22.42 ? 383 LYS   A CG  1 
ATOM   2553 C  CD  . LYS   A 1 349 ? 10.501  -1.449  17.359  1.00 27.37 ? 383 LYS   A CD  1 
ATOM   2554 C  CE  . LYS   A 1 349 ? 10.784  -2.864  17.878  1.00 37.25 ? 383 LYS   A CE  1 
ATOM   2555 N  NZ  . LYS   A 1 349 ? 10.272  -3.116  19.269  1.00 44.65 ? 383 LYS   A NZ  1 
ATOM   2556 N  N   . PRO   A 1 350 ? 13.306  1.848   14.622  1.00 19.29 ? 384 PRO   A N   1 
ATOM   2557 C  CA  . PRO   A 1 350 ? 14.305  2.912   14.422  1.00 19.65 ? 384 PRO   A CA  1 
ATOM   2558 C  C   . PRO   A 1 350 ? 15.723  2.543   14.871  1.00 15.80 ? 384 PRO   A C   1 
ATOM   2559 O  O   . PRO   A 1 350 ? 15.938  1.990   15.946  1.00 16.35 ? 384 PRO   A O   1 
ATOM   2560 C  CB  . PRO   A 1 350 ? 13.745  4.074   15.255  1.00 19.82 ? 384 PRO   A CB  1 
ATOM   2561 C  CG  . PRO   A 1 350 ? 12.284  3.783   15.375  1.00 18.47 ? 384 PRO   A CG  1 
ATOM   2562 C  CD  . PRO   A 1 350 ? 12.193  2.316   15.471  1.00 18.35 ? 384 PRO   A CD  1 
ATOM   2563 N  N   . LEU   A 1 351 ? 16.701  2.936   14.050  1.00 15.64 ? 385 LEU   A N   1 
ATOM   2564 C  CA  . LEU   A 1 351 ? 18.122  2.655   14.249  1.00 16.91 ? 385 LEU   A CA  1 
ATOM   2565 C  C   . LEU   A 1 351 ? 18.734  3.380   15.444  1.00 18.01 ? 385 LEU   A C   1 
ATOM   2566 O  O   . LEU   A 1 351 ? 19.870  3.070   15.822  1.00 21.93 ? 385 LEU   A O   1 
ATOM   2567 C  CB  . LEU   A 1 351 ? 18.918  3.034   12.982  1.00 18.82 ? 385 LEU   A CB  1 
ATOM   2568 C  CG  . LEU   A 1 351 ? 18.188  2.858   11.635  1.00 19.79 ? 385 LEU   A CG  1 
ATOM   2569 C  CD1 . LEU   A 1 351 ? 18.999  3.338   10.451  1.00 17.11 ? 385 LEU   A CD1 1 
ATOM   2570 C  CD2 . LEU   A 1 351 ? 17.795  1.412   11.431  1.00 18.43 ? 385 LEU   A CD2 1 
ATOM   2571 N  N   . GLY   A 1 352 ? 18.048  4.360   16.016  1.00 18.96 ? 386 GLY   A N   1 
ATOM   2572 C  CA  . GLY   A 1 352 ? 18.620  5.175   17.068  1.00 15.58 ? 386 GLY   A CA  1 
ATOM   2573 C  C   . GLY   A 1 352 ? 17.545  5.628   18.023  1.00 17.62 ? 386 GLY   A C   1 
ATOM   2574 O  O   . GLY   A 1 352 ? 16.442  5.084   18.025  1.00 18.52 ? 386 GLY   A O   1 
ATOM   2575 N  N   . ASP   A 1 353 ? 17.842  6.642   18.826  1.00 22.22 ? 387 ASP   A N   1 
ATOM   2576 C  CA  . ASP   A 1 353 ? 16.917  7.039   19.879  1.00 21.13 ? 387 ASP   A CA  1 
ATOM   2577 C  C   . ASP   A 1 353 ? 15.624  7.608   19.321  1.00 26.59 ? 387 ASP   A C   1 
ATOM   2578 O  O   . ASP   A 1 353 ? 14.575  7.498   19.968  1.00 27.76 ? 387 ASP   A O   1 
ATOM   2579 C  CB  . ASP   A 1 353 ? 17.586  8.061   20.783  1.00 21.49 ? 387 ASP   A CB  1 
ATOM   2580 C  CG  . ASP   A 1 353 ? 18.676  7.456   21.611  1.00 23.58 ? 387 ASP   A CG  1 
ATOM   2581 O  OD1 . ASP   A 1 353 ? 18.505  6.307   22.047  1.00 28.31 ? 387 ASP   A OD1 1 
ATOM   2582 O  OD2 . ASP   A 1 353 ? 19.698  8.111   21.829  1.00 25.64 ? 387 ASP   A OD2 1 
ATOM   2583 N  N   . ARG   A 1 354 ? 15.674  8.224   18.083  1.00 22.24 ? 388 ARG   A N   1 
ATOM   2584 C  CA  . ARG   A 1 354 ? 14.431  8.912   17.810  1.00 18.78 ? 388 ARG   A CA  1 
ATOM   2585 C  C   . ARG   A 1 354 ? 13.563  8.119   16.852  1.00 19.38 ? 388 ARG   A C   1 
ATOM   2586 O  O   . ARG   A 1 354 ? 14.066  7.390   15.997  1.00 21.22 ? 388 ARG   A O   1 
ATOM   2587 C  CB  . ARG   A 1 354 ? 14.699  10.286  17.207  1.00 23.29 ? 388 ARG   A CB  1 
ATOM   2588 C  CG  . ARG   A 1 354 ? 15.646  11.171  17.999  1.00 21.03 ? 388 ARG   A CG  1 
ATOM   2589 C  CD  . ARG   A 1 354 ? 15.694  12.512  17.342  1.00 20.70 ? 388 ARG   A CD  1 
ATOM   2590 N  NE  . ARG   A 1 354 ? 16.659  13.397  17.958  1.00 25.74 ? 388 ARG   A NE  1 
ATOM   2591 C  CZ  . ARG   A 1 354 ? 16.733  14.699  17.697  1.00 29.68 ? 388 ARG   A CZ  1 
ATOM   2592 N  NH1 . ARG   A 1 354 ? 17.653  15.433  18.308  1.00 33.04 ? 388 ARG   A NH1 1 
ATOM   2593 N  NH2 . ARG   A 1 354 ? 15.887  15.267  16.835  1.00 25.88 ? 388 ARG   A NH2 1 
ATOM   2594 N  N   . PRO   A 1 355 ? 12.270  8.242   16.956  1.00 17.17 ? 389 PRO   A N   1 
ATOM   2595 C  CA  . PRO   A 1 355 ? 11.410  7.577   15.977  1.00 14.35 ? 389 PRO   A CA  1 
ATOM   2596 C  C   . PRO   A 1 355 ? 11.494  8.254   14.618  1.00 18.24 ? 389 PRO   A C   1 
ATOM   2597 O  O   . PRO   A 1 355 ? 10.542  8.899   14.178  1.00 22.75 ? 389 PRO   A O   1 
ATOM   2598 C  CB  . PRO   A 1 355 ? 10.018  7.695   16.604  1.00 13.92 ? 389 PRO   A CB  1 
ATOM   2599 C  CG  . PRO   A 1 355 ? 10.098  8.884   17.490  1.00 16.58 ? 389 PRO   A CG  1 
ATOM   2600 C  CD  . PRO   A 1 355 ? 11.503  8.960   17.984  1.00 16.40 ? 389 PRO   A CD  1 
ATOM   2601 N  N   . THR   A 1 356 ? 12.630  8.114   13.932  1.00 19.92 ? 390 THR   A N   1 
ATOM   2602 C  CA  . THR   A 1 356 ? 12.840  8.780   12.654  1.00 21.33 ? 390 THR   A CA  1 
ATOM   2603 C  C   . THR   A 1 356 ? 13.265  7.772   11.621  1.00 21.98 ? 390 THR   A C   1 
ATOM   2604 O  O   . THR   A 1 356 ? 12.417  7.100   11.015  1.00 18.14 ? 390 THR   A O   1 
ATOM   2605 C  CB  . THR   A 1 356 ? 13.844  9.907   12.826  1.00 21.42 ? 390 THR   A CB  1 
ATOM   2606 O  OG1 . THR   A 1 356 ? 14.922  9.417   13.639  1.00 23.45 ? 390 THR   A OG1 1 
ATOM   2607 C  CG2 . THR   A 1 356 ? 13.183  11.076  13.512  1.00 20.91 ? 390 THR   A CG2 1 
ATOM   2608 N  N   . ILE   A 1 357 ? 14.576  7.596   11.370  1.00 19.64 ? 391 ILE   A N   1 
ATOM   2609 C  CA  . ILE   A 1 357 ? 15.083  6.765   10.278  1.00 21.72 ? 391 ILE   A CA  1 
ATOM   2610 C  C   . ILE   A 1 357 ? 15.035  5.277   10.640  1.00 28.64 ? 391 ILE   A C   1 
ATOM   2611 O  O   . ILE   A 1 357 ? 15.295  4.873   11.789  1.00 24.33 ? 391 ILE   A O   1 
ATOM   2612 C  CB  . ILE   A 1 357 ? 16.513  7.203   9.912   1.00 21.08 ? 391 ILE   A CB  1 
ATOM   2613 C  CG1 . ILE   A 1 357 ? 17.107  6.336   8.803   1.00 21.92 ? 391 ILE   A CG1 1 
ATOM   2614 C  CG2 . ILE   A 1 357 ? 17.409  7.158   11.118  1.00 16.26 ? 391 ILE   A CG2 1 
ATOM   2615 C  CD1 . ILE   A 1 357 ? 18.528  6.739   8.435   1.00 19.96 ? 391 ILE   A CD1 1 
ATOM   2616 N  N   . PHE   A 1 358 ? 14.723  4.441   9.641   1.00 24.99 ? 392 PHE   A N   1 
ATOM   2617 C  CA  . PHE   A 1 358 ? 14.723  3.003   9.826   1.00 20.21 ? 392 PHE   A CA  1 
ATOM   2618 C  C   . PHE   A 1 358 ? 15.275  2.345   8.567   1.00 23.71 ? 392 PHE   A C   1 
ATOM   2619 O  O   . PHE   A 1 358 ? 15.561  3.006   7.569   1.00 22.39 ? 392 PHE   A O   1 
ATOM   2620 C  CB  . PHE   A 1 358 ? 13.324  2.483   10.190  1.00 22.05 ? 392 PHE   A CB  1 
ATOM   2621 C  CG  . PHE   A 1 358 ? 12.244  2.845   9.206   1.00 21.75 ? 392 PHE   A CG  1 
ATOM   2622 C  CD1 . PHE   A 1 358 ? 11.421  3.950   9.436   1.00 19.05 ? 392 PHE   A CD1 1 
ATOM   2623 C  CD2 . PHE   A 1 358 ? 12.019  2.053   8.075   1.00 18.79 ? 392 PHE   A CD2 1 
ATOM   2624 C  CE1 . PHE   A 1 358 ? 10.402  4.276   8.541   1.00 19.73 ? 392 PHE   A CE1 1 
ATOM   2625 C  CE2 . PHE   A 1 358 ? 11.014  2.355   7.175   1.00 21.72 ? 392 PHE   A CE2 1 
ATOM   2626 C  CZ  . PHE   A 1 358 ? 10.191  3.479   7.400   1.00 26.20 ? 392 PHE   A CZ  1 
ATOM   2627 N  N   . ILE   A 1 359 ? 15.468  1.029   8.634   1.00 20.86 ? 393 ILE   A N   1 
ATOM   2628 C  CA  . ILE   A 1 359 ? 16.022  0.294   7.509   1.00 22.20 ? 393 ILE   A CA  1 
ATOM   2629 C  C   . ILE   A 1 359 ? 14.977  -0.694  7.007   1.00 24.75 ? 393 ILE   A C   1 
ATOM   2630 O  O   . ILE   A 1 359 ? 14.083  -1.120  7.744   1.00 23.16 ? 393 ILE   A O   1 
ATOM   2631 C  CB  . ILE   A 1 359 ? 17.355  -0.402  7.864   1.00 20.01 ? 393 ILE   A CB  1 
ATOM   2632 C  CG1 . ILE   A 1 359 ? 18.503  0.595   7.682   1.00 18.31 ? 393 ILE   A CG1 1 
ATOM   2633 C  CG2 . ILE   A 1 359 ? 17.603  -1.658  7.004   1.00 17.11 ? 393 ILE   A CG2 1 
ATOM   2634 C  CD1 . ILE   A 1 359 ? 19.836  0.115   8.217   1.00 15.67 ? 393 ILE   A CD1 1 
ATOM   2635 N  N   . GLU   A 1 360 ? 15.049  -0.981  5.711   1.00 20.93 ? 394 GLU   A N   1 
ATOM   2636 C  CA  . GLU   A 1 360 ? 14.204  -1.954  5.057   1.00 22.50 ? 394 GLU   A CA  1 
ATOM   2637 C  C   . GLU   A 1 360 ? 15.112  -2.857  4.252   1.00 26.00 ? 394 GLU   A C   1 
ATOM   2638 O  O   . GLU   A 1 360 ? 15.981  -2.371  3.514   1.00 23.61 ? 394 GLU   A O   1 
ATOM   2639 C  CB  . GLU   A 1 360 ? 13.167  -1.285  4.151   1.00 24.31 ? 394 GLU   A CB  1 
ATOM   2640 C  CG  . GLU   A 1 360 ? 12.661  -2.157  3.047   1.00 22.55 ? 394 GLU   A CG  1 
ATOM   2641 C  CD  . GLU   A 1 360 ? 11.926  -1.387  1.995   1.00 27.69 ? 394 GLU   A CD  1 
ATOM   2642 O  OE1 . GLU   A 1 360 ? 11.994  -0.148  2.022   1.00 36.80 ? 394 GLU   A OE1 1 
ATOM   2643 O  OE2 . GLU   A 1 360 ? 11.266  -1.998  1.134   1.00 27.30 ? 394 GLU   A OE2 1 
ATOM   2644 N  N   . ILE   A 1 361 ? 14.936  -4.166  4.435   1.00 25.65 ? 395 ILE   A N   1 
ATOM   2645 C  CA  . ILE   A 1 361 ? 15.606  -5.172  3.622   1.00 26.36 ? 395 ILE   A CA  1 
ATOM   2646 C  C   . ILE   A 1 361 ? 14.645  -5.673  2.560   1.00 28.48 ? 395 ILE   A C   1 
ATOM   2647 O  O   . ILE   A 1 361 ? 13.473  -5.977  2.844   1.00 24.72 ? 395 ILE   A O   1 
ATOM   2648 C  CB  . ILE   A 1 361 ? 16.120  -6.334  4.476   1.00 21.27 ? 395 ILE   A CB  1 
ATOM   2649 C  CG1 . ILE   A 1 361 ? 16.666  -5.784  5.797   1.00 17.68 ? 395 ILE   A CG1 1 
ATOM   2650 C  CG2 . ILE   A 1 361 ? 17.177  -7.088  3.678   1.00 19.83 ? 395 ILE   A CG2 1 
ATOM   2651 C  CD1 . ILE   A 1 361 ? 18.015  -5.143  5.648   1.00 16.45 ? 395 ILE   A CD1 1 
ATOM   2652 N  N   . ILE   A 1 362 ? 15.147  -5.764  1.330   1.00 25.90 ? 396 ILE   A N   1 
ATOM   2653 C  CA  . ILE   A 1 362 ? 14.347  -6.147  0.179   1.00 29.48 ? 396 ILE   A CA  1 
ATOM   2654 C  C   . ILE   A 1 362 ? 15.070  -7.185  -0.661  1.00 31.28 ? 396 ILE   A C   1 
ATOM   2655 O  O   . ILE   A 1 362 ? 16.291  -7.343  -0.598  1.00 33.29 ? 396 ILE   A O   1 
ATOM   2656 C  CB  . ILE   A 1 362 ? 14.052  -4.952  -0.726  1.00 30.66 ? 396 ILE   A CB  1 
ATOM   2657 C  CG1 . ILE   A 1 362 ? 15.379  -4.301  -1.078  1.00 27.81 ? 396 ILE   A CG1 1 
ATOM   2658 C  CG2 . ILE   A 1 362 ? 13.154  -3.985  -0.044  1.00 32.94 ? 396 ILE   A CG2 1 
ATOM   2659 C  CD1 . ILE   A 1 362 ? 15.500  -4.026  -2.518  1.00 30.73 ? 396 ILE   A CD1 1 
ATOM   2660 N  N   . GLN   A 1 363 ? 14.293  -7.851  -1.502  1.00 31.90 ? 397 GLN   A N   1 
ATOM   2661 C  CA  . GLN   A 1 363 ? 14.821  -8.598  -2.633  1.00 31.08 ? 397 GLN   A CA  1 
ATOM   2662 C  C   . GLN   A 1 363 ? 13.738  -8.617  -3.702  1.00 35.45 ? 397 GLN   A C   1 
ATOM   2663 O  O   . GLN   A 1 363 ? 12.555  -8.830  -3.399  1.00 29.24 ? 397 GLN   A O   1 
ATOM   2664 C  CB  . GLN   A 1 363 ? 15.236  -10.015 -2.238  1.00 23.55 ? 397 GLN   A CB  1 
ATOM   2665 C  CG  . GLN   A 1 363 ? 15.933  -10.782 -3.348  1.00 30.56 ? 397 GLN   A CG  1 
ATOM   2666 C  CD  . GLN   A 1 363 ? 16.666  -12.042 -2.858  1.00 31.09 ? 397 GLN   A CD  1 
ATOM   2667 O  OE1 . GLN   A 1 363 ? 16.407  -12.541 -1.772  1.00 28.81 ? 397 GLN   A OE1 1 
ATOM   2668 N  NE2 . GLN   A 1 363 ? 17.577  -12.552 -3.674  1.00 31.02 ? 397 GLN   A NE2 1 
ATOM   2669 N  N   . ARG   A 1 364 ? 14.139  -8.361  -4.937  1.00 27.58 ? 398 ARG   A N   1 
ATOM   2670 C  CA  . ARG   A 1 364 ? 13.209  -8.331  -6.047  1.00 30.27 ? 398 ARG   A CA  1 
ATOM   2671 C  C   . ARG   A 1 364 ? 13.347  -9.585  -6.910  1.00 35.86 ? 398 ARG   A C   1 
ATOM   2672 O  O   . ARG   A 1 364 ? 14.455  -10.076 -7.142  1.00 32.51 ? 398 ARG   A O   1 
ATOM   2673 C  CB  . ARG   A 1 364 ? 13.451  -7.082  -6.883  1.00 34.78 ? 398 ARG   A CB  1 
ATOM   2674 C  CG  . ARG   A 1 364 ? 13.505  -5.830  -6.059  1.00 31.92 ? 398 ARG   A CG  1 
ATOM   2675 C  CD  . ARG   A 1 364 ? 13.626  -4.627  -6.947  1.00 28.99 ? 398 ARG   A CD  1 
ATOM   2676 N  NE  . ARG   A 1 364 ? 13.574  -3.376  -6.205  1.00 28.38 ? 398 ARG   A NE  1 
ATOM   2677 C  CZ  . ARG   A 1 364 ? 12.445  -2.734  -5.923  1.00 33.00 ? 398 ARG   A CZ  1 
ATOM   2678 N  NH1 . ARG   A 1 364 ? 11.277  -3.254  -6.305  1.00 27.52 ? 398 ARG   A NH1 1 
ATOM   2679 N  NH2 . ARG   A 1 364 ? 12.484  -1.576  -5.262  1.00 28.67 ? 398 ARG   A NH2 1 
ATOM   2680 N  N   . VAL   A 1 365 ? 12.213  -10.099 -7.388  1.00 39.36 ? 399 VAL   A N   1 
ATOM   2681 C  CA  . VAL   A 1 365 ? 12.184  -11.226 -8.315  1.00 42.07 ? 399 VAL   A CA  1 
ATOM   2682 C  C   . VAL   A 1 365 ? 11.289  -10.882 -9.509  1.00 42.56 ? 399 VAL   A C   1 
ATOM   2683 O  O   . VAL   A 1 365 ? 10.125  -10.500 -9.336  1.00 35.32 ? 399 VAL   A O   1 
ATOM   2684 C  CB  . VAL   A 1 365 ? 11.728  -12.530 -7.627  1.00 36.72 ? 399 VAL   A CB  1 
ATOM   2685 C  CG1 . VAL   A 1 365 ? 10.479  -12.313 -6.796  1.00 33.57 ? 399 VAL   A CG1 1 
ATOM   2686 C  CG2 . VAL   A 1 365 ? 11.498  -13.604 -8.669  1.00 41.24 ? 399 VAL   A CG2 1 
ATOM   2687 N  N   . GLY   A 1 366 ? 11.839  -11.021 -10.719 1.00 42.07 ? 400 GLY   A N   1 
ATOM   2688 C  CA  . GLY   A 1 366 ? 11.156  -10.725 -11.958 1.00 38.40 ? 400 GLY   A CA  1 
ATOM   2689 C  C   . GLY   A 1 366 ? 12.085  -9.985  -12.887 1.00 46.08 ? 400 GLY   A C   1 
ATOM   2690 O  O   . GLY   A 1 366 ? 13.296  -9.972  -12.679 1.00 56.41 ? 400 GLY   A O   1 
ATOM   2691 N  N   . CYS   A 1 367 ? 11.498  -9.387  -13.922 1.00 41.14 ? 401 CYS   A N   1 
ATOM   2692 C  CA  . CYS   A 1 367 ? 12.149  -8.367  -14.762 1.00 54.24 ? 401 CYS   A CA  1 
ATOM   2693 C  C   . CYS   A 1 367 ? 13.572  -8.755  -15.179 1.00 61.57 ? 401 CYS   A C   1 
ATOM   2694 O  O   . CYS   A 1 367 ? 14.535  -8.005  -14.978 1.00 58.72 ? 401 CYS   A O   1 
ATOM   2695 C  CB  . CYS   A 1 367 ? 12.154  -6.999  -14.070 1.00 54.99 ? 401 CYS   A CB  1 
ATOM   2696 S  SG  . CYS   A 1 367 ? 10.724  -6.604  -13.010 1.00 56.65 ? 401 CYS   A SG  1 
ATOM   2697 N  N   . MET   A 1 368 ? 13.690  -9.926  -15.806 1.00 66.91 ? 402 MET   A N   1 
ATOM   2698 C  CA  . MET   A 1 368 ? 14.975  -10.434 -16.293 1.00 58.50 ? 402 MET   A CA  1 
ATOM   2699 C  C   . MET   A 1 368 ? 15.329  -9.977  -17.708 1.00 54.96 ? 402 MET   A C   1 
ATOM   2700 O  O   . MET   A 1 368 ? 14.455  -9.603  -18.491 1.00 55.29 ? 402 MET   A O   1 
ATOM   2701 C  CB  . MET   A 1 368 ? 14.972  -11.959 -16.228 1.00 61.27 ? 402 MET   A CB  1 
ATOM   2702 C  CG  . MET   A 1 368 ? 15.302  -12.438 -14.848 1.00 64.10 ? 402 MET   A CG  1 
ATOM   2703 S  SD  . MET   A 1 368 ? 16.703  -11.456 -14.280 1.00 76.98 ? 402 MET   A SD  1 
ATOM   2704 C  CE  . MET   A 1 368 ? 18.001  -12.124 -15.331 1.00 56.92 ? 402 MET   A CE  1 
ATOM   2705 N  N   . TYR   A 1 377 ? 20.285  -9.899  -16.317 1.00 59.95 ? 411 TYR   A N   1 
ATOM   2706 C  CA  . TYR   A 1 377 ? 20.284  -8.743  -15.432 1.00 60.76 ? 411 TYR   A CA  1 
ATOM   2707 C  C   . TYR   A 1 377 ? 18.869  -8.336  -15.028 1.00 62.94 ? 411 TYR   A C   1 
ATOM   2708 O  O   . TYR   A 1 377 ? 17.944  -8.327  -15.846 1.00 57.06 ? 411 TYR   A O   1 
ATOM   2709 C  CB  . TYR   A 1 377 ? 20.993  -7.559  -16.099 1.00 69.74 ? 411 TYR   A CB  1 
ATOM   2710 N  N   . GLN   A 1 378 ? 18.712  -7.993  -13.754 1.00 62.35 ? 412 GLN   A N   1 
ATOM   2711 C  CA  . GLN   A 1 378 ? 17.456  -7.446  -13.270 1.00 58.67 ? 412 GLN   A CA  1 
ATOM   2712 C  C   . GLN   A 1 378 ? 17.376  -5.950  -13.564 1.00 58.48 ? 412 GLN   A C   1 
ATOM   2713 O  O   . GLN   A 1 378 ? 18.389  -5.242  -13.572 1.00 56.73 ? 412 GLN   A O   1 
ATOM   2714 C  CB  . GLN   A 1 378 ? 17.324  -7.689  -11.771 1.00 50.06 ? 412 GLN   A CB  1 
ATOM   2715 C  CG  . GLN   A 1 378 ? 15.893  -7.729  -11.274 1.00 50.05 ? 412 GLN   A CG  1 
ATOM   2716 C  CD  . GLN   A 1 378 ? 15.732  -8.684  -10.107 1.00 48.51 ? 412 GLN   A CD  1 
ATOM   2717 O  OE1 . GLN   A 1 378 ? 16.169  -8.393  -8.995  1.00 51.54 ? 412 GLN   A OE1 1 
ATOM   2718 N  NE2 . GLN   A 1 378 ? 15.113  -9.833  -10.356 1.00 41.67 ? 412 GLN   A NE2 1 
ATOM   2719 N  N   . SER   A 1 379 ? 16.162  -5.468  -13.815 1.00 53.06 ? 413 SER   A N   1 
ATOM   2720 C  CA  . SER   A 1 379 ? 15.941  -4.040  -14.003 1.00 51.92 ? 413 SER   A CA  1 
ATOM   2721 C  C   . SER   A 1 379 ? 15.370  -3.430  -12.726 1.00 44.94 ? 413 SER   A C   1 
ATOM   2722 O  O   . SER   A 1 379 ? 14.610  -4.068  -11.993 1.00 45.31 ? 413 SER   A O   1 
ATOM   2723 C  CB  . SER   A 1 379 ? 15.018  -3.762  -15.197 1.00 46.71 ? 413 SER   A CB  1 
ATOM   2724 O  OG  . SER   A 1 379 ? 13.690  -4.161  -14.928 1.00 49.47 ? 413 SER   A OG  1 
ATOM   2725 N  N   . GLY   A 1 380 ? 15.757  -2.187  -12.463 1.00 37.92 ? 414 GLY   A N   1 
ATOM   2726 C  CA  . GLY   A 1 380 ? 15.502  -1.599  -11.165 1.00 38.37 ? 414 GLY   A CA  1 
ATOM   2727 C  C   . GLY   A 1 380 ? 14.022  -1.475  -10.860 1.00 41.31 ? 414 GLY   A C   1 
ATOM   2728 O  O   . GLY   A 1 380 ? 13.163  -1.505  -11.746 1.00 43.58 ? 414 GLY   A O   1 
ATOM   2729 N  N   . GLY   A 1 381 ? 13.732  -1.339  -9.564  1.00 38.08 ? 415 GLY   A N   1 
ATOM   2730 C  CA  . GLY   A 1 381 ? 12.372  -1.131  -9.109  1.00 34.46 ? 415 GLY   A CA  1 
ATOM   2731 C  C   . GLY   A 1 381 ? 11.457  -2.278  -9.432  1.00 36.29 ? 415 GLY   A C   1 
ATOM   2732 O  O   . GLY   A 1 381 ? 10.229  -2.127  -9.394  1.00 34.02 ? 415 GLY   A O   1 
ATOM   2733 N  N   . CYS   A 1 382 ? 12.033  -3.426  -9.765  1.00 33.13 ? 416 CYS   A N   1 
ATOM   2734 C  CA  . CYS   A 1 382 ? 11.260  -4.585  -10.153 1.00 36.08 ? 416 CYS   A CA  1 
ATOM   2735 C  C   . CYS   A 1 382 ? 10.312  -4.978  -9.033  1.00 37.64 ? 416 CYS   A C   1 
ATOM   2736 O  O   . CYS   A 1 382 ? 10.750  -5.374  -7.946  1.00 37.70 ? 416 CYS   A O   1 
ATOM   2737 C  CB  . CYS   A 1 382 ? 12.194  -5.738  -10.504 1.00 42.25 ? 416 CYS   A CB  1 
ATOM   2738 S  SG  . CYS   A 1 382 ? 11.325  -7.169  -11.147 1.00 47.63 ? 416 CYS   A SG  1 
ATOM   2739 N  N   . GLY   A 1 383 ? 9.015   -4.862  -9.275  1.00 34.41 ? 417 GLY   A N   1 
ATOM   2740 C  CA  . GLY   A 1 383 ? 8.042   -5.196  -8.263  1.00 32.63 ? 417 GLY   A CA  1 
ATOM   2741 C  C   . GLY   A 1 383 ? 7.482   -4.019  -7.504  1.00 36.39 ? 417 GLY   A C   1 
ATOM   2742 O  O   . GLY   A 1 383 ? 6.571   -4.215  -6.692  1.00 35.39 ? 417 GLY   A O   1 
ATOM   2743 N  N   . GLY   A 1 384 ? 7.995   -2.806  -7.737  1.00 32.55 ? 418 GLY   A N   1 
ATOM   2744 C  CA  . GLY   A 1 384 ? 7.502   -1.645  -7.025  1.00 30.30 ? 418 GLY   A CA  1 
ATOM   2745 C  C   . GLY   A 1 384 ? 8.198   -1.423  -5.691  1.00 30.59 ? 418 GLY   A C   1 
ATOM   2746 O  O   . GLY   A 1 384 ? 9.350   -1.809  -5.482  1.00 28.95 ? 418 GLY   A O   1 
ATOM   2747 N  N   . PHE   A 1 385 ? 7.467   -0.783  -4.772  1.00 31.21 ? 419 PHE   A N   1 
ATOM   2748 C  CA  . PHE   A 1 385 ? 8.022   -0.332  -3.503  1.00 25.87 ? 419 PHE   A CA  1 
ATOM   2749 C  C   . PHE   A 1 385 ? 7.156   -0.726  -2.312  1.00 35.24 ? 419 PHE   A C   1 
ATOM   2750 O  O   . PHE   A 1 385 ? 7.465   -0.330  -1.177  1.00 33.83 ? 419 PHE   A O   1 
ATOM   2751 C  CB  . PHE   A 1 385 ? 8.241   1.184   -3.525  1.00 26.87 ? 419 PHE   A CB  1 
ATOM   2752 C  CG  . PHE   A 1 385 ? 9.335   1.616   -4.473  1.00 32.95 ? 419 PHE   A CG  1 
ATOM   2753 C  CD1 . PHE   A 1 385 ? 9.031   2.010   -5.775  1.00 31.03 ? 419 PHE   A CD1 1 
ATOM   2754 C  CD2 . PHE   A 1 385 ? 10.673  1.604   -4.070  1.00 29.47 ? 419 PHE   A CD2 1 
ATOM   2755 C  CE1 . PHE   A 1 385 ? 10.032  2.396   -6.652  1.00 33.19 ? 419 PHE   A CE1 1 
ATOM   2756 C  CE2 . PHE   A 1 385 ? 11.682  1.979   -4.947  1.00 30.60 ? 419 PHE   A CE2 1 
ATOM   2757 C  CZ  . PHE   A 1 385 ? 11.361  2.383   -6.240  1.00 32.88 ? 419 PHE   A CZ  1 
ATOM   2758 N  N   . GLY   A 1 386 ? 6.100   -1.508  -2.532  1.00 34.61 ? 420 GLY   A N   1 
ATOM   2759 C  CA  . GLY   A 1 386 ? 5.322   -2.073  -1.454  1.00 29.19 ? 420 GLY   A CA  1 
ATOM   2760 C  C   . GLY   A 1 386 ? 4.003   -1.405  -1.168  1.00 28.97 ? 420 GLY   A C   1 
ATOM   2761 O  O   . GLY   A 1 386 ? 3.338   -1.793  -0.206  1.00 32.76 ? 420 GLY   A O   1 
ATOM   2762 N  N   . LYS   A 1 387 ? 3.603   -0.414  -1.968  1.00 34.01 ? 421 LYS   A N   1 
ATOM   2763 C  CA  . LYS   A 1 387 ? 2.380   0.330   -1.683  1.00 34.76 ? 421 LYS   A CA  1 
ATOM   2764 C  C   . LYS   A 1 387 ? 1.168   -0.591  -1.610  1.00 32.75 ? 421 LYS   A C   1 
ATOM   2765 O  O   . LYS   A 1 387 ? 0.198   -0.287  -0.909  1.00 32.84 ? 421 LYS   A O   1 
ATOM   2766 C  CB  . LYS   A 1 387 ? 2.178   1.429   -2.734  1.00 36.24 ? 421 LYS   A CB  1 
ATOM   2767 C  CG  . LYS   A 1 387 ? 3.099   2.649   -2.574  1.00 35.73 ? 421 LYS   A CG  1 
ATOM   2768 C  CD  . LYS   A 1 387 ? 2.950   3.634   -3.735  1.00 33.43 ? 421 LYS   A CD  1 
ATOM   2769 C  CE  . LYS   A 1 387 ? 3.513   5.028   -3.415  1.00 34.64 ? 421 LYS   A CE  1 
ATOM   2770 N  NZ  . LYS   A 1 387 ? 3.315   5.989   -4.561  1.00 32.27 ? 421 LYS   A NZ  1 
ATOM   2771 N  N   . GLY   A 1 388 ? 1.216   -1.735  -2.289  1.00 33.79 ? 422 GLY   A N   1 
ATOM   2772 C  CA  . GLY   A 1 388 ? 0.120   -2.681  -2.183  1.00 36.81 ? 422 GLY   A CA  1 
ATOM   2773 C  C   . GLY   A 1 388 ? -0.110  -3.176  -0.766  1.00 42.05 ? 422 GLY   A C   1 
ATOM   2774 O  O   . GLY   A 1 388 ? -1.242  -3.491  -0.390  1.00 43.59 ? 422 GLY   A O   1 
ATOM   2775 N  N   . ASN   A 1 389 ? 0.947   -3.237  0.042   1.00 40.34 ? 423 ASN   A N   1 
ATOM   2776 C  CA  . ASN   A 1 389 ? 0.856   -3.756  1.401   1.00 42.56 ? 423 ASN   A CA  1 
ATOM   2777 C  C   . ASN   A 1 389 ? 0.208   -2.791  2.390   1.00 44.38 ? 423 ASN   A C   1 
ATOM   2778 O  O   . ASN   A 1 389 ? 0.004   -3.180  3.546   1.00 45.79 ? 423 ASN   A O   1 
ATOM   2779 C  CB  . ASN   A 1 389 ? 2.247   -4.143  1.909   1.00 40.39 ? 423 ASN   A CB  1 
ATOM   2780 C  CG  . ASN   A 1 389 ? 2.697   -5.495  1.405   1.00 37.35 ? 423 ASN   A CG  1 
ATOM   2781 O  OD1 . ASN   A 1 389 ? 1.959   -6.475  1.495   1.00 36.76 ? 423 ASN   A OD1 1 
ATOM   2782 N  ND2 . ASN   A 1 389 ? 3.916   -5.558  0.874   1.00 32.72 ? 423 ASN   A ND2 1 
ATOM   2783 N  N   . PHE   A 1 390 ? -0.114  -1.555  1.990   1.00 41.83 ? 424 PHE   A N   1 
ATOM   2784 C  CA  . PHE   A 1 390 ? -0.873  -0.682  2.884   1.00 43.32 ? 424 PHE   A CA  1 
ATOM   2785 C  C   . PHE   A 1 390 ? -2.299  -1.192  3.053   1.00 45.44 ? 424 PHE   A C   1 
ATOM   2786 O  O   . PHE   A 1 390 ? -2.776  -1.367  4.180   1.00 47.92 ? 424 PHE   A O   1 
ATOM   2787 C  CB  . PHE   A 1 390 ? -0.868  0.767   2.374   1.00 41.90 ? 424 PHE   A CB  1 
ATOM   2788 C  CG  . PHE   A 1 390 ? 0.409   1.514   2.673   1.00 32.68 ? 424 PHE   A CG  1 
ATOM   2789 C  CD1 . PHE   A 1 390 ? 1.314   1.802   1.669   1.00 36.42 ? 424 PHE   A CD1 1 
ATOM   2790 C  CD2 . PHE   A 1 390 ? 0.708   1.908   3.958   1.00 34.98 ? 424 PHE   A CD2 1 
ATOM   2791 C  CE1 . PHE   A 1 390 ? 2.495   2.478   1.935   1.00 35.48 ? 424 PHE   A CE1 1 
ATOM   2792 C  CE2 . PHE   A 1 390 ? 1.881   2.581   4.234   1.00 40.50 ? 424 PHE   A CE2 1 
ATOM   2793 C  CZ  . PHE   A 1 390 ? 2.779   2.865   3.217   1.00 37.18 ? 424 PHE   A CZ  1 
ATOM   2794 N  N   . SER   A 1 391 ? -2.991  -1.457  1.946   1.00 46.43 ? 425 SER   A N   1 
ATOM   2795 C  CA  . SER   A 1 391 ? -4.307  -2.074  2.057   1.00 51.84 ? 425 SER   A CA  1 
ATOM   2796 C  C   . SER   A 1 391 ? -4.234  -3.587  2.274   1.00 53.05 ? 425 SER   A C   1 
ATOM   2797 O  O   . SER   A 1 391 ? -5.192  -4.167  2.791   1.00 57.11 ? 425 SER   A O   1 
ATOM   2798 C  CB  . SER   A 1 391 ? -5.152  -1.744  0.822   1.00 48.00 ? 425 SER   A CB  1 
ATOM   2799 O  OG  . SER   A 1 391 ? -4.351  -1.734  -0.343  1.00 50.61 ? 425 SER   A OG  1 
ATOM   2800 N  N   . GLU   A 1 392 ? -3.127  -4.244  1.911   1.00 52.27 ? 426 GLU   A N   1 
ATOM   2801 C  CA  . GLU   A 1 392 ? -3.014  -5.675  2.191   1.00 50.92 ? 426 GLU   A CA  1 
ATOM   2802 C  C   . GLU   A 1 392 ? -2.960  -5.946  3.685   1.00 54.76 ? 426 GLU   A C   1 
ATOM   2803 O  O   . GLU   A 1 392 ? -3.341  -7.039  4.129   1.00 53.44 ? 426 GLU   A O   1 
ATOM   2804 C  CB  . GLU   A 1 392 ? -1.771  -6.278  1.530   1.00 44.70 ? 426 GLU   A CB  1 
ATOM   2805 C  CG  . GLU   A 1 392 ? -2.016  -6.963  0.199   1.00 45.05 ? 426 GLU   A CG  1 
ATOM   2806 C  CD  . GLU   A 1 392 ? -3.321  -7.738  0.160   1.00 51.11 ? 426 GLU   A CD  1 
ATOM   2807 O  OE1 . GLU   A 1 392 ? -3.528  -8.638  1.010   1.00 54.13 ? 426 GLU   A OE1 1 
ATOM   2808 O  OE2 . GLU   A 1 392 ? -4.149  -7.436  -0.727  1.00 51.83 ? 426 GLU   A OE2 1 
ATOM   2809 N  N   . LEU   A 1 393 ? -2.478  -4.976  4.466   1.00 54.20 ? 427 LEU   A N   1 
ATOM   2810 C  CA  . LEU   A 1 393 ? -2.251  -5.175  5.890   1.00 51.02 ? 427 LEU   A CA  1 
ATOM   2811 C  C   . LEU   A 1 393 ? -3.514  -4.908  6.693   1.00 53.98 ? 427 LEU   A C   1 
ATOM   2812 O  O   . LEU   A 1 393 ? -3.880  -5.702  7.566   1.00 52.77 ? 427 LEU   A O   1 
ATOM   2813 C  CB  . LEU   A 1 393 ? -1.107  -4.283  6.370   1.00 48.20 ? 427 LEU   A CB  1 
ATOM   2814 C  CG  . LEU   A 1 393 ? -0.218  -4.909  7.441   1.00 51.34 ? 427 LEU   A CG  1 
ATOM   2815 C  CD1 . LEU   A 1 393 ? 0.248   -6.269  6.987   1.00 48.91 ? 427 LEU   A CD1 1 
ATOM   2816 C  CD2 . LEU   A 1 393 ? 0.982   -4.029  7.742   1.00 58.06 ? 427 LEU   A CD2 1 
ATOM   2817 N  N   . PHE   A 1 394 ? -4.198  -3.803  6.401   1.00 52.88 ? 428 PHE   A N   1 
ATOM   2818 C  CA  . PHE   A 1 394 ? -5.467  -3.553  7.067   1.00 56.01 ? 428 PHE   A CA  1 
ATOM   2819 C  C   . PHE   A 1 394 ? -6.489  -4.618  6.696   1.00 55.62 ? 428 PHE   A C   1 
ATOM   2820 O  O   . PHE   A 1 394 ? -7.262  -5.071  7.549   1.00 52.63 ? 428 PHE   A O   1 
ATOM   2821 C  CB  . PHE   A 1 394 ? -5.948  -2.147  6.730   1.00 56.10 ? 428 PHE   A CB  1 
ATOM   2822 C  CG  . PHE   A 1 394 ? -5.043  -1.082  7.275   1.00 64.21 ? 428 PHE   A CG  1 
ATOM   2823 C  CD1 . PHE   A 1 394 ? -4.339  -1.306  8.452   1.00 66.81 ? 428 PHE   A CD1 1 
ATOM   2824 C  CD2 . PHE   A 1 394 ? -4.860  0.118   6.609   1.00 66.49 ? 428 PHE   A CD2 1 
ATOM   2825 C  CE1 . PHE   A 1 394 ? -3.486  -0.342  8.968   1.00 67.65 ? 428 PHE   A CE1 1 
ATOM   2826 C  CE2 . PHE   A 1 394 ? -4.002  1.089   7.119   1.00 67.08 ? 428 PHE   A CE2 1 
ATOM   2827 C  CZ  . PHE   A 1 394 ? -3.314  0.855   8.299   1.00 65.30 ? 428 PHE   A CZ  1 
ATOM   2828 N  N   . LYS   A 1 395 ? -6.470  -5.071  5.441   1.00 54.31 ? 429 LYS   A N   1 
ATOM   2829 C  CA  . LYS   A 1 395 ? -7.359  -6.156  5.043   1.00 50.65 ? 429 LYS   A CA  1 
ATOM   2830 C  C   . LYS   A 1 395 ? -7.123  -7.399  5.891   1.00 51.24 ? 429 LYS   A C   1 
ATOM   2831 O  O   . LYS   A 1 395 ? -8.076  -8.090  6.263   1.00 54.33 ? 429 LYS   A O   1 
ATOM   2832 C  CB  . LYS   A 1 395 ? -7.177  -6.476  3.560   1.00 52.34 ? 429 LYS   A CB  1 
ATOM   2833 N  N   . SER   A 1 396 ? -5.863  -7.694  6.225   1.00 50.70 ? 430 SER   A N   1 
ATOM   2834 C  CA  . SER   A 1 396 ? -5.610  -8.857  7.067   1.00 52.14 ? 430 SER   A CA  1 
ATOM   2835 C  C   . SER   A 1 396 ? -5.889  -8.566  8.544   1.00 53.45 ? 430 SER   A C   1 
ATOM   2836 O  O   . SER   A 1 396 ? -6.287  -9.474  9.283   1.00 52.71 ? 430 SER   A O   1 
ATOM   2837 C  CB  . SER   A 1 396 ? -4.178  -9.377  6.860   1.00 46.59 ? 430 SER   A CB  1 
ATOM   2838 O  OG  . SER   A 1 396 ? -3.188  -8.564  7.457   1.00 49.75 ? 430 SER   A OG  1 
ATOM   2839 N  N   . ILE   A 1 397 ? -5.738  -7.313  8.987   1.00 51.90 ? 431 ILE   A N   1 
ATOM   2840 C  CA  . ILE   A 1 397 ? -6.059  -6.988  10.376  1.00 53.16 ? 431 ILE   A CA  1 
ATOM   2841 C  C   . ILE   A 1 397 ? -7.555  -7.151  10.641  1.00 55.93 ? 431 ILE   A C   1 
ATOM   2842 O  O   . ILE   A 1 397 ? -7.961  -7.580  11.733  1.00 59.65 ? 431 ILE   A O   1 
ATOM   2843 C  CB  . ILE   A 1 397 ? -5.564  -5.568  10.709  1.00 53.11 ? 431 ILE   A CB  1 
ATOM   2844 C  CG1 . ILE   A 1 397 ? -4.036  -5.535  10.726  1.00 47.05 ? 431 ILE   A CG1 1 
ATOM   2845 C  CG2 . ILE   A 1 397 ? -6.134  -5.084  12.038  1.00 47.52 ? 431 ILE   A CG2 1 
ATOM   2846 C  CD1 . ILE   A 1 397 ? -3.467  -4.146  10.671  1.00 53.03 ? 431 ILE   A CD1 1 
ATOM   2847 N  N   . GLU   A 1 398 ? -8.397  -6.834  9.653   1.00 52.92 ? 432 GLU   A N   1 
ATOM   2848 C  CA  . GLU   A 1 398 ? -9.836  -7.017  9.814   1.00 52.63 ? 432 GLU   A CA  1 
ATOM   2849 C  C   . GLU   A 1 398 ? -10.191 -8.490  9.924   1.00 55.89 ? 432 GLU   A C   1 
ATOM   2850 O  O   . GLU   A 1 398 ? -11.044 -8.868  10.733  1.00 59.93 ? 432 GLU   A O   1 
ATOM   2851 C  CB  . GLU   A 1 398 ? -10.584 -6.382  8.644   1.00 49.74 ? 432 GLU   A CB  1 
ATOM   2852 N  N   . GLU   A 1 399 ? -9.530  -9.336  9.126   1.00 61.52 ? 433 GLU   A N   1 
ATOM   2853 C  CA  . GLU   A 1 399 ? -9.867  -10.757 9.068   1.00 58.71 ? 433 GLU   A CA  1 
ATOM   2854 C  C   . GLU   A 1 399 ? -9.394  -11.500 10.314  1.00 59.58 ? 433 GLU   A C   1 
ATOM   2855 O  O   . GLU   A 1 399 ? -10.101 -12.377 10.827  1.00 62.38 ? 433 GLU   A O   1 
ATOM   2856 C  CB  . GLU   A 1 399 ? -9.265  -11.377 7.803   1.00 54.87 ? 433 GLU   A CB  1 
ATOM   2857 N  N   . TYR   A 1 400 ? -8.203  -11.163 10.814  1.00 63.50 ? 434 TYR   A N   1 
ATOM   2858 C  CA  . TYR   A 1 400 ? -7.689  -11.805 12.020  1.00 63.51 ? 434 TYR   A CA  1 
ATOM   2859 C  C   . TYR   A 1 400 ? -8.636  -11.617 13.205  1.00 65.38 ? 434 TYR   A C   1 
ATOM   2860 O  O   . TYR   A 1 400 ? -8.765  -12.510 14.056  1.00 65.46 ? 434 TYR   A O   1 
ATOM   2861 C  CB  . TYR   A 1 400 ? -6.305  -11.249 12.344  1.00 54.97 ? 434 TYR   A CB  1 
ATOM   2862 C  CG  . TYR   A 1 400 ? -5.653  -11.951 13.497  1.00 57.58 ? 434 TYR   A CG  1 
ATOM   2863 C  CD1 . TYR   A 1 400 ? -5.472  -13.327 13.478  1.00 52.09 ? 434 TYR   A CD1 1 
ATOM   2864 C  CD2 . TYR   A 1 400 ? -5.216  -11.242 14.607  1.00 56.42 ? 434 TYR   A CD2 1 
ATOM   2865 C  CE1 . TYR   A 1 400 ? -4.880  -13.975 14.532  1.00 52.67 ? 434 TYR   A CE1 1 
ATOM   2866 C  CE2 . TYR   A 1 400 ? -4.622  -11.882 15.663  1.00 56.96 ? 434 TYR   A CE2 1 
ATOM   2867 C  CZ  . TYR   A 1 400 ? -4.456  -13.247 15.621  1.00 55.54 ? 434 TYR   A CZ  1 
ATOM   2868 O  OH  . TYR   A 1 400 ? -3.858  -13.891 16.674  1.00 61.95 ? 434 TYR   A OH  1 
ATOM   2869 N  N   . GLU   A 1 401 ? -9.302  -10.460 13.278  1.00 66.35 ? 435 GLU   A N   1 
ATOM   2870 C  CA  . GLU   A 1 401 ? -10.238 -10.199 14.369  1.00 67.50 ? 435 GLU   A CA  1 
ATOM   2871 C  C   . GLU   A 1 401 ? -11.338 -11.260 14.418  1.00 68.95 ? 435 GLU   A C   1 
ATOM   2872 O  O   . GLU   A 1 401 ? -11.631 -11.824 15.481  1.00 70.41 ? 435 GLU   A O   1 
ATOM   2873 C  CB  . GLU   A 1 401 ? -10.829 -8.794  14.217  1.00 69.87 ? 435 GLU   A CB  1 
ATOM   2874 N  N   . LYS   A 1 402 ? -11.937 -11.564 13.270  1.00 63.67 ? 436 LYS   A N   1 
ATOM   2875 C  CA  . LYS   A 1 402 ? -13.031 -12.533 13.204  1.00 65.23 ? 436 LYS   A CA  1 
ATOM   2876 C  C   . LYS   A 1 402 ? -12.580 -13.938 13.592  1.00 58.95 ? 436 LYS   A C   1 
ATOM   2877 O  O   . LYS   A 1 402 ? -11.451 -14.339 13.316  1.00 55.97 ? 436 LYS   A O   1 
ATOM   2878 C  CB  . LYS   A 1 402 ? -13.639 -12.547 11.800  1.00 64.84 ? 436 LYS   A CB  1 
ATOM   2879 N  N   . ASN   B 1 2   ? 44.187  3.416   57.244  1.00 57.54 ? 36  ASN   B N   1 
ATOM   2880 C  CA  . ASN   B 1 2   ? 42.722  3.368   57.198  1.00 60.81 ? 36  ASN   B CA  1 
ATOM   2881 C  C   . ASN   B 1 2   ? 42.112  4.064   58.422  1.00 58.40 ? 36  ASN   B C   1 
ATOM   2882 O  O   . ASN   B 1 2   ? 41.536  3.410   59.300  1.00 57.42 ? 36  ASN   B O   1 
ATOM   2883 C  CB  . ASN   B 1 2   ? 42.232  1.906   57.107  1.00 56.49 ? 36  ASN   B CB  1 
ATOM   2884 C  CG  . ASN   B 1 2   ? 40.736  1.793   56.775  1.00 54.39 ? 36  ASN   B CG  1 
ATOM   2885 O  OD1 . ASN   B 1 2   ? 40.001  2.785   56.793  1.00 53.21 ? 36  ASN   B OD1 1 
ATOM   2886 N  ND2 . ASN   B 1 2   ? 40.283  0.569   56.490  1.00 52.64 ? 36  ASN   B ND2 1 
ATOM   2887 N  N   . PRO   B 1 3   ? 42.229  5.394   58.486  1.00 57.87 ? 37  PRO   B N   1 
ATOM   2888 C  CA  . PRO   B 1 3   ? 41.657  6.121   59.635  1.00 55.88 ? 37  PRO   B CA  1 
ATOM   2889 C  C   . PRO   B 1 3   ? 40.139  6.045   59.718  1.00 56.25 ? 37  PRO   B C   1 
ATOM   2890 O  O   . PRO   B 1 3   ? 39.580  6.488   60.731  1.00 56.52 ? 37  PRO   B O   1 
ATOM   2891 C  CB  . PRO   B 1 3   ? 42.132  7.567   59.421  1.00 49.43 ? 37  PRO   B CB  1 
ATOM   2892 C  CG  . PRO   B 1 3   ? 42.524  7.649   57.979  1.00 52.71 ? 37  PRO   B CG  1 
ATOM   2893 C  CD  . PRO   B 1 3   ? 42.971  6.277   57.570  1.00 48.31 ? 37  PRO   B CD  1 
ATOM   2894 N  N   . LYS   B 1 4   ? 39.463  5.488   58.707  1.00 55.10 ? 38  LYS   B N   1 
ATOM   2895 C  CA  . LYS   B 1 4   ? 38.000  5.418   58.676  1.00 51.60 ? 38  LYS   B CA  1 
ATOM   2896 C  C   . LYS   B 1 4   ? 37.393  6.792   58.946  1.00 49.65 ? 38  LYS   B C   1 
ATOM   2897 O  O   . LYS   B 1 4   ? 36.555  6.964   59.837  1.00 49.55 ? 38  LYS   B O   1 
ATOM   2898 C  CB  . LYS   B 1 4   ? 37.461  4.381   59.673  1.00 48.72 ? 38  LYS   B CB  1 
ATOM   2899 C  CG  . LYS   B 1 4   ? 37.581  2.925   59.235  1.00 49.37 ? 38  LYS   B CG  1 
ATOM   2900 C  CD  . LYS   B 1 4   ? 36.373  2.102   59.699  1.00 53.37 ? 38  LYS   B CD  1 
ATOM   2901 C  CE  . LYS   B 1 4   ? 36.163  0.826   58.867  1.00 52.03 ? 38  LYS   B CE  1 
ATOM   2902 N  NZ  . LYS   B 1 4   ? 34.710  0.573   58.534  1.00 48.34 ? 38  LYS   B NZ  1 
ATOM   2903 N  N   . SER   B 1 5   ? 37.824  7.780   58.152  1.00 48.50 ? 39  SER   B N   1 
ATOM   2904 C  CA  . SER   B 1 5   ? 37.535  9.190   58.399  1.00 40.31 ? 39  SER   B CA  1 
ATOM   2905 C  C   . SER   B 1 5   ? 36.439  9.758   57.496  1.00 37.16 ? 39  SER   B C   1 
ATOM   2906 O  O   . SER   B 1 5   ? 36.419  10.963  57.258  1.00 36.98 ? 39  SER   B O   1 
ATOM   2907 C  CB  . SER   B 1 5   ? 38.807  10.022  58.247  1.00 38.20 ? 39  SER   B CB  1 
ATOM   2908 O  OG  . SER   B 1 5   ? 39.292  10.002  56.923  1.00 31.70 ? 39  SER   B OG  1 
ATOM   2909 N  N   . ASP   B 1 6   ? 35.506  8.931   57.020  1.00 42.76 ? 40  ASP   B N   1 
ATOM   2910 C  CA  . ASP   B 1 6   ? 34.477  9.411   56.099  1.00 44.84 ? 40  ASP   B CA  1 
ATOM   2911 C  C   . ASP   B 1 6   ? 33.467  10.319  56.804  1.00 46.48 ? 40  ASP   B C   1 
ATOM   2912 O  O   . ASP   B 1 6   ? 32.888  9.954   57.833  1.00 47.26 ? 40  ASP   B O   1 
ATOM   2913 C  CB  . ASP   B 1 6   ? 33.752  8.237   55.441  1.00 43.05 ? 40  ASP   B CB  1 
ATOM   2914 C  CG  . ASP   B 1 6   ? 34.650  7.454   54.476  1.00 53.56 ? 40  ASP   B CG  1 
ATOM   2915 O  OD1 . ASP   B 1 6   ? 35.903  7.542   54.596  1.00 51.43 ? 40  ASP   B OD1 1 
ATOM   2916 O  OD2 . ASP   B 1 6   ? 34.097  6.737   53.606  1.00 52.27 ? 40  ASP   B OD2 1 
ATOM   2917 N  N   . LYS   B 1 7   ? 33.232  11.494  56.216  1.00 45.19 ? 41  LYS   B N   1 
ATOM   2918 C  CA  . LYS   B 1 7   ? 32.305  12.487  56.750  1.00 47.65 ? 41  LYS   B CA  1 
ATOM   2919 C  C   . LYS   B 1 7   ? 30.835  12.079  56.622  1.00 47.26 ? 41  LYS   B C   1 
ATOM   2920 O  O   . LYS   B 1 7   ? 29.974  12.754  57.204  1.00 51.73 ? 41  LYS   B O   1 
ATOM   2921 C  CB  . LYS   B 1 7   ? 32.539  13.840  56.056  1.00 46.08 ? 41  LYS   B CB  1 
ATOM   2922 C  CG  . LYS   B 1 7   ? 34.011  14.272  55.975  1.00 42.17 ? 41  LYS   B CG  1 
ATOM   2923 C  CD  . LYS   B 1 7   ? 34.162  15.791  55.963  1.00 45.04 ? 41  LYS   B CD  1 
ATOM   2924 C  CE  . LYS   B 1 7   ? 33.813  16.397  57.338  1.00 53.00 ? 41  LYS   B CE  1 
ATOM   2925 N  NZ  . LYS   B 1 7   ? 35.004  16.768  58.164  1.00 53.34 ? 41  LYS   B NZ  1 
ATOM   2926 N  N   . PHE   B 1 8   ? 30.524  11.018  55.878  1.00 41.93 ? 42  PHE   B N   1 
ATOM   2927 C  CA  . PHE   B 1 8   ? 29.184  10.441  55.858  1.00 43.13 ? 42  PHE   B CA  1 
ATOM   2928 C  C   . PHE   B 1 8   ? 29.319  8.956   55.540  1.00 44.42 ? 42  PHE   B C   1 
ATOM   2929 O  O   . PHE   B 1 8   ? 30.426  8.439   55.366  1.00 50.66 ? 42  PHE   B O   1 
ATOM   2930 C  CB  . PHE   B 1 8   ? 28.256  11.178  54.874  1.00 45.29 ? 42  PHE   B CB  1 
ATOM   2931 C  CG  . PHE   B 1 8   ? 28.865  11.426  53.525  1.00 46.74 ? 42  PHE   B CG  1 
ATOM   2932 C  CD1 . PHE   B 1 8   ? 28.785  10.470  52.526  1.00 38.68 ? 42  PHE   B CD1 1 
ATOM   2933 C  CD2 . PHE   B 1 8   ? 29.517  12.620  53.257  1.00 48.50 ? 42  PHE   B CD2 1 
ATOM   2934 C  CE1 . PHE   B 1 8   ? 29.348  10.692  51.298  1.00 38.57 ? 42  PHE   B CE1 1 
ATOM   2935 C  CE2 . PHE   B 1 8   ? 30.088  12.849  52.015  1.00 46.67 ? 42  PHE   B CE2 1 
ATOM   2936 C  CZ  . PHE   B 1 8   ? 30.002  11.879  51.036  1.00 40.28 ? 42  PHE   B CZ  1 
ATOM   2937 N  N   . LYS   B 1 9   ? 28.186  8.262   55.479  1.00 38.40 ? 43  LYS   B N   1 
ATOM   2938 C  CA  . LYS   B 1 9   ? 28.174  6.811   55.339  1.00 42.39 ? 43  LYS   B CA  1 
ATOM   2939 C  C   . LYS   B 1 9   ? 27.950  6.429   53.878  1.00 41.32 ? 43  LYS   B C   1 
ATOM   2940 O  O   . LYS   B 1 9   ? 26.895  6.733   53.311  1.00 44.56 ? 43  LYS   B O   1 
ATOM   2941 C  CB  . LYS   B 1 9   ? 27.098  6.190   56.233  1.00 33.30 ? 43  LYS   B CB  1 
ATOM   2942 N  N   . VAL   B 1 10  ? 28.928  5.730   53.292  1.00 40.29 ? 44  VAL   B N   1 
ATOM   2943 C  CA  . VAL   B 1 10  ? 28.898  5.270   51.901  1.00 43.71 ? 44  VAL   B CA  1 
ATOM   2944 C  C   . VAL   B 1 10  ? 28.841  3.743   51.870  1.00 44.97 ? 44  VAL   B C   1 
ATOM   2945 O  O   . VAL   B 1 10  ? 29.581  3.073   52.602  1.00 48.86 ? 44  VAL   B O   1 
ATOM   2946 C  CB  . VAL   B 1 10  ? 30.135  5.782   51.129  1.00 43.30 ? 44  VAL   B CB  1 
ATOM   2947 C  CG1 . VAL   B 1 10  ? 30.196  5.176   49.713  1.00 43.83 ? 44  VAL   B CG1 1 
ATOM   2948 C  CG2 . VAL   B 1 10  ? 30.149  7.297   51.075  1.00 38.82 ? 44  VAL   B CG2 1 
ATOM   2949 N  N   . LYS   B 1 11  ? 27.978  3.182   51.000  1.00 44.63 ? 45  LYS   B N   1 
ATOM   2950 C  CA  . LYS   B 1 11  ? 27.834  1.725   50.852  1.00 46.09 ? 45  LYS   B CA  1 
ATOM   2951 C  C   . LYS   B 1 11  ? 27.938  1.324   49.364  1.00 50.63 ? 45  LYS   B C   1 
ATOM   2952 O  O   . LYS   B 1 11  ? 26.938  1.013   48.706  1.00 58.98 ? 45  LYS   B O   1 
ATOM   2953 C  CB  . LYS   B 1 11  ? 26.520  1.249   51.487  1.00 45.75 ? 45  LYS   B CB  1 
ATOM   2954 C  CG  . LYS   B 1 11  ? 25.278  2.020   51.039  1.00 45.39 ? 45  LYS   B CG  1 
ATOM   2955 C  CD  . LYS   B 1 11  ? 24.167  2.015   52.092  1.00 48.50 ? 45  LYS   B CD  1 
ATOM   2956 C  CE  . LYS   B 1 11  ? 23.064  1.013   51.771  1.00 53.66 ? 45  LYS   B CE  1 
ATOM   2957 N  NZ  . LYS   B 1 11  ? 22.224  0.722   52.967  1.00 55.26 ? 45  LYS   B NZ  1 
ATOM   2958 N  N   . ARG   B 1 12  ? 29.166  1.332   48.836  1.00 42.77 ? 46  ARG   B N   1 
ATOM   2959 C  CA  . ARG   B 1 12  ? 29.486  0.862   47.482  1.00 49.64 ? 46  ARG   B CA  1 
ATOM   2960 C  C   . ARG   B 1 12  ? 28.964  1.708   46.327  1.00 43.12 ? 46  ARG   B C   1 
ATOM   2961 O  O   . ARG   B 1 12  ? 27.949  2.408   46.441  1.00 40.95 ? 46  ARG   B O   1 
ATOM   2962 C  CB  . ARG   B 1 12  ? 28.982  -0.571  47.243  1.00 50.12 ? 46  ARG   B CB  1 
ATOM   2963 C  CG  . ARG   B 1 12  ? 29.979  -1.660  47.580  1.00 50.57 ? 46  ARG   B CG  1 
ATOM   2964 C  CD  . ARG   B 1 12  ? 29.314  -2.707  48.444  1.00 58.51 ? 46  ARG   B CD  1 
ATOM   2965 N  NE  . ARG   B 1 12  ? 28.898  -2.107  49.713  1.00 64.22 ? 46  ARG   B NE  1 
ATOM   2966 C  CZ  . ARG   B 1 12  ? 29.731  -1.755  50.690  1.00 62.81 ? 46  ARG   B CZ  1 
ATOM   2967 N  NH1 . ARG   B 1 12  ? 31.026  -1.963  50.567  1.00 55.83 ? 46  ARG   B NH1 1 
ATOM   2968 N  NH2 . ARG   B 1 12  ? 29.267  -1.200  51.802  1.00 67.35 ? 46  ARG   B NH2 1 
ATOM   2969 N  N   . PHE   B 1 13  ? 29.662  1.582   45.192  1.00 39.67 ? 47  PHE   B N   1 
ATOM   2970 C  CA  . PHE   B 1 13  ? 29.236  2.140   43.913  1.00 36.57 ? 47  PHE   B CA  1 
ATOM   2971 C  C   . PHE   B 1 13  ? 27.815  1.722   43.565  1.00 31.18 ? 47  PHE   B C   1 
ATOM   2972 O  O   . PHE   B 1 13  ? 27.390  0.597   43.837  1.00 36.91 ? 47  PHE   B O   1 
ATOM   2973 C  CB  . PHE   B 1 13  ? 30.183  1.679   42.807  1.00 27.68 ? 47  PHE   B CB  1 
ATOM   2974 C  CG  . PHE   B 1 13  ? 31.536  2.285   42.892  1.00 28.02 ? 47  PHE   B CG  1 
ATOM   2975 C  CD1 . PHE   B 1 13  ? 31.710  3.647   42.669  1.00 27.38 ? 47  PHE   B CD1 1 
ATOM   2976 C  CD2 . PHE   B 1 13  ? 32.640  1.506   43.191  1.00 27.40 ? 47  PHE   B CD2 1 
ATOM   2977 C  CE1 . PHE   B 1 13  ? 32.967  4.224   42.754  1.00 28.71 ? 47  PHE   B CE1 1 
ATOM   2978 C  CE2 . PHE   B 1 13  ? 33.895  2.071   43.280  1.00 30.14 ? 47  PHE   B CE2 1 
ATOM   2979 C  CZ  . PHE   B 1 13  ? 34.062  3.442   43.060  1.00 27.52 ? 47  PHE   B CZ  1 
ATOM   2980 N  N   . HIS   B 1 14  ? 27.093  2.621   42.914  1.00 26.85 ? 48  HIS   B N   1 
ATOM   2981 C  CA  . HIS   B 1 14  ? 25.718  2.358   42.529  1.00 31.63 ? 48  HIS   B CA  1 
ATOM   2982 C  C   . HIS   B 1 14  ? 25.507  2.296   41.022  1.00 35.14 ? 48  HIS   B C   1 
ATOM   2983 O  O   . HIS   B 1 14  ? 24.767  1.426   40.551  1.00 35.66 ? 48  HIS   B O   1 
ATOM   2984 C  CB  . HIS   B 1 14  ? 24.797  3.416   43.134  1.00 36.54 ? 48  HIS   B CB  1 
ATOM   2985 C  CG  . HIS   B 1 14  ? 23.352  3.041   43.110  1.00 37.60 ? 48  HIS   B CG  1 
ATOM   2986 N  ND1 . HIS   B 1 14  ? 22.495  3.450   42.112  1.00 36.88 ? 48  HIS   B ND1 1 
ATOM   2987 C  CD2 . HIS   B 1 14  ? 22.612  2.294   43.960  1.00 43.40 ? 48  HIS   B CD2 1 
ATOM   2988 C  CE1 . HIS   B 1 14  ? 21.287  2.968   42.345  1.00 39.49 ? 48  HIS   B CE1 1 
ATOM   2989 N  NE2 . HIS   B 1 14  ? 21.332  2.263   43.461  1.00 50.32 ? 48  HIS   B NE2 1 
ATOM   2990 N  N   . HIS   B 1 15  ? 26.123  3.190   40.246  1.00 32.13 ? 49  HIS   B N   1 
ATOM   2991 C  CA  . HIS   B 1 15  ? 26.082  3.107   38.785  1.00 31.62 ? 49  HIS   B CA  1 
ATOM   2992 C  C   . HIS   B 1 15  ? 27.044  4.123   38.192  1.00 29.91 ? 49  HIS   B C   1 
ATOM   2993 O  O   . HIS   B 1 15  ? 27.395  5.127   38.820  1.00 27.05 ? 49  HIS   B O   1 
ATOM   2994 C  CB  . HIS   B 1 15  ? 24.668  3.339   38.205  1.00 30.37 ? 49  HIS   B CB  1 
ATOM   2995 C  CG  . HIS   B 1 15  ? 24.119  4.715   38.445  1.00 29.94 ? 49  HIS   B CG  1 
ATOM   2996 N  ND1 . HIS   B 1 15  ? 23.271  5.007   39.492  1.00 32.00 ? 49  HIS   B ND1 1 
ATOM   2997 C  CD2 . HIS   B 1 15  ? 24.287  5.876   37.766  1.00 33.46 ? 49  HIS   B CD2 1 
ATOM   2998 C  CE1 . HIS   B 1 15  ? 22.934  6.283   39.446  1.00 29.96 ? 49  HIS   B CE1 1 
ATOM   2999 N  NE2 . HIS   B 1 15  ? 23.539  6.835   38.410  1.00 31.35 ? 49  HIS   B NE2 1 
ATOM   3000 N  N   . ILE   B 1 16  ? 27.441  3.849   36.956  1.00 24.93 ? 50  ILE   B N   1 
ATOM   3001 C  CA  . ILE   B 1 16  ? 28.239  4.750   36.131  1.00 26.78 ? 50  ILE   B CA  1 
ATOM   3002 C  C   . ILE   B 1 16  ? 27.328  5.268   35.023  1.00 30.31 ? 50  ILE   B C   1 
ATOM   3003 O  O   . ILE   B 1 16  ? 26.664  4.461   34.351  1.00 23.97 ? 50  ILE   B O   1 
ATOM   3004 C  CB  . ILE   B 1 16  ? 29.461  4.007   35.562  1.00 19.53 ? 50  ILE   B CB  1 
ATOM   3005 C  CG1 . ILE   B 1 16  ? 30.425  3.620   36.688  1.00 26.62 ? 50  ILE   B CG1 1 
ATOM   3006 C  CG2 . ILE   B 1 16  ? 30.163  4.795   34.516  1.00 23.07 ? 50  ILE   B CG2 1 
ATOM   3007 C  CD1 . ILE   B 1 16  ? 31.065  4.786   37.410  1.00 29.31 ? 50  ILE   B CD1 1 
ATOM   3008 N  N   . GLU   B 1 17  ? 27.258  6.604   34.841  1.00 23.25 ? 51  GLU   B N   1 
ATOM   3009 C  CA  . GLU   B 1 17  ? 26.420  7.180   33.783  1.00 25.49 ? 51  GLU   B CA  1 
ATOM   3010 C  C   . GLU   B 1 17  ? 27.274  7.825   32.695  1.00 28.99 ? 51  GLU   B C   1 
ATOM   3011 O  O   . GLU   B 1 17  ? 28.047  8.747   32.973  1.00 30.23 ? 51  GLU   B O   1 
ATOM   3012 C  CB  . GLU   B 1 17  ? 25.412  8.203   34.311  1.00 27.37 ? 51  GLU   B CB  1 
ATOM   3013 C  CG  . GLU   B 1 17  ? 24.617  8.885   33.160  1.00 32.75 ? 51  GLU   B CG  1 
ATOM   3014 C  CD  . GLU   B 1 17  ? 23.431  9.774   33.599  1.00 33.17 ? 51  GLU   B CD  1 
ATOM   3015 O  OE1 . GLU   B 1 17  ? 23.525  10.461  34.643  1.00 29.58 ? 51  GLU   B OE1 1 
ATOM   3016 O  OE2 . GLU   B 1 17  ? 22.401  9.789   32.873  1.00 30.72 ? 51  GLU   B OE2 1 
ATOM   3017 N  N   . PHE   B 1 18  ? 27.103  7.344   31.453  1.00 30.36 ? 52  PHE   B N   1 
ATOM   3018 C  CA  . PHE   B 1 18  ? 27.681  7.934   30.247  1.00 26.18 ? 52  PHE   B CA  1 
ATOM   3019 C  C   . PHE   B 1 18  ? 26.688  8.891   29.619  1.00 24.63 ? 52  PHE   B C   1 
ATOM   3020 O  O   . PHE   B 1 18  ? 25.496  8.582   29.507  1.00 25.76 ? 52  PHE   B O   1 
ATOM   3021 C  CB  . PHE   B 1 18  ? 28.024  6.870   29.192  1.00 21.71 ? 52  PHE   B CB  1 
ATOM   3022 C  CG  . PHE   B 1 18  ? 29.147  5.961   29.569  1.00 22.38 ? 52  PHE   B CG  1 
ATOM   3023 C  CD1 . PHE   B 1 18  ? 28.917  4.824   30.364  1.00 23.13 ? 52  PHE   B CD1 1 
ATOM   3024 C  CD2 . PHE   B 1 18  ? 30.436  6.217   29.120  1.00 17.33 ? 52  PHE   B CD2 1 
ATOM   3025 C  CE1 . PHE   B 1 18  ? 29.971  3.969   30.715  1.00 19.26 ? 52  PHE   B CE1 1 
ATOM   3026 C  CE2 . PHE   B 1 18  ? 31.492  5.368   29.466  1.00 17.73 ? 52  PHE   B CE2 1 
ATOM   3027 C  CZ  . PHE   B 1 18  ? 31.261  4.250   30.263  1.00 16.18 ? 52  PHE   B CZ  1 
ATOM   3028 N  N   . TRP   B 1 19  ? 27.186  10.033  29.169  1.00 27.60 ? 53  TRP   B N   1 
ATOM   3029 C  CA  . TRP   B 1 19  ? 26.394  10.948  28.355  1.00 29.56 ? 53  TRP   B CA  1 
ATOM   3030 C  C   . TRP   B 1 19  ? 26.803  10.754  26.904  1.00 25.47 ? 53  TRP   B C   1 
ATOM   3031 O  O   . TRP   B 1 19  ? 27.996  10.725  26.584  1.00 23.79 ? 53  TRP   B O   1 
ATOM   3032 C  CB  . TRP   B 1 19  ? 26.563  12.411  28.796  1.00 30.79 ? 53  TRP   B CB  1 
ATOM   3033 C  CG  . TRP   B 1 19  ? 25.576  12.846  29.910  1.00 32.86 ? 53  TRP   B CG  1 
ATOM   3034 C  CD1 . TRP   B 1 19  ? 24.639  12.064  30.519  1.00 31.39 ? 53  TRP   B CD1 1 
ATOM   3035 C  CD2 . TRP   B 1 19  ? 25.444  14.154  30.509  1.00 36.08 ? 53  TRP   B CD2 1 
ATOM   3036 N  NE1 . TRP   B 1 19  ? 23.946  12.787  31.458  1.00 33.88 ? 53  TRP   B NE1 1 
ATOM   3037 C  CE2 . TRP   B 1 19  ? 24.415  14.071  31.470  1.00 33.69 ? 53  TRP   B CE2 1 
ATOM   3038 C  CE3 . TRP   B 1 19  ? 26.096  15.380  30.325  1.00 35.73 ? 53  TRP   B CE3 1 
ATOM   3039 C  CZ2 . TRP   B 1 19  ? 24.019  15.163  32.240  1.00 35.68 ? 53  TRP   B CZ2 1 
ATOM   3040 C  CZ3 . TRP   B 1 19  ? 25.710  16.461  31.106  1.00 36.02 ? 53  TRP   B CZ3 1 
ATOM   3041 C  CH2 . TRP   B 1 19  ? 24.680  16.344  32.049  1.00 36.42 ? 53  TRP   B CH2 1 
ATOM   3042 N  N   . CYS   B 1 20  ? 25.818  10.565  26.040  1.00 26.12 ? 54  CYS   B N   1 
ATOM   3043 C  CA  . CYS   B 1 20  ? 26.096  10.162  24.677  1.00 21.61 ? 54  CYS   B CA  1 
ATOM   3044 C  C   . CYS   B 1 20  ? 25.255  11.001  23.754  1.00 22.52 ? 54  CYS   B C   1 
ATOM   3045 O  O   . CYS   B 1 20  ? 24.294  11.644  24.176  1.00 23.32 ? 54  CYS   B O   1 
ATOM   3046 C  CB  . CYS   B 1 20  ? 25.791  8.678   24.432  1.00 25.86 ? 54  CYS   B CB  1 
ATOM   3047 S  SG  . CYS   B 1 20  ? 25.969  7.573   25.862  1.00 38.47 ? 54  CYS   B SG  1 
ATOM   3048 N  N   . GLY   B 1 21  ? 25.630  10.973  22.482  1.00 22.85 ? 55  GLY   B N   1 
ATOM   3049 C  CA  . GLY   B 1 21  ? 24.837  11.578  21.443  1.00 25.04 ? 55  GLY   B CA  1 
ATOM   3050 C  C   . GLY   B 1 21  ? 23.621  10.745  21.132  1.00 24.09 ? 55  GLY   B C   1 
ATOM   3051 O  O   . GLY   B 1 21  ? 22.500  11.265  21.126  1.00 29.79 ? 55  GLY   B O   1 
ATOM   3052 N  N   . ASP   B 1 22  ? 23.825  9.452   20.874  1.00 23.21 ? 56  ASP   B N   1 
ATOM   3053 C  CA  . ASP   B 1 22  ? 22.723  8.513   20.673  1.00 24.16 ? 56  ASP   B CA  1 
ATOM   3054 C  C   . ASP   B 1 22  ? 22.888  7.318   21.603  1.00 23.01 ? 56  ASP   B C   1 
ATOM   3055 O  O   . ASP   B 1 22  ? 23.797  6.502   21.420  1.00 21.91 ? 56  ASP   B O   1 
ATOM   3056 C  CB  . ASP   B 1 22  ? 22.617  8.043   19.226  1.00 24.22 ? 56  ASP   B CB  1 
ATOM   3057 C  CG  . ASP   B 1 22  ? 21.359  7.256   18.993  1.00 23.65 ? 56  ASP   B CG  1 
ATOM   3058 O  OD1 . ASP   B 1 22  ? 20.318  7.873   18.714  1.00 26.10 ? 56  ASP   B OD1 1 
ATOM   3059 O  OD2 . ASP   B 1 22  ? 21.394  6.022   19.146  1.00 27.37 ? 56  ASP   B OD2 1 
ATOM   3060 N  N   . ALA   B 1 23  ? 21.959  7.189   22.553  1.00 22.26 ? 57  ALA   B N   1 
ATOM   3061 C  CA  . ALA   B 1 23  ? 22.080  6.237   23.645  1.00 24.42 ? 57  ALA   B CA  1 
ATOM   3062 C  C   . ALA   B 1 23  ? 21.745  4.797   23.226  1.00 24.55 ? 57  ALA   B C   1 
ATOM   3063 O  O   . ALA   B 1 23  ? 22.343  3.849   23.743  1.00 21.36 ? 57  ALA   B O   1 
ATOM   3064 C  CB  . ALA   B 1 23  ? 21.195  6.715   24.798  1.00 23.35 ? 57  ALA   B CB  1 
ATOM   3065 N  N   . THR   B 1 24  ? 20.794  4.614   22.309  1.00 23.93 ? 58  THR   B N   1 
ATOM   3066 C  CA  . THR   B 1 24  ? 20.523  3.293   21.754  1.00 22.61 ? 58  THR   B CA  1 
ATOM   3067 C  C   . THR   B 1 24  ? 21.803  2.615   21.280  1.00 22.12 ? 58  THR   B C   1 
ATOM   3068 O  O   . THR   B 1 24  ? 22.117  1.493   21.691  1.00 26.16 ? 58  THR   B O   1 
ATOM   3069 C  CB  . THR   B 1 24  ? 19.518  3.428   20.607  1.00 21.76 ? 58  THR   B CB  1 
ATOM   3070 O  OG1 . THR   B 1 24  ? 18.200  3.543   21.151  1.00 24.12 ? 58  THR   B OG1 1 
ATOM   3071 C  CG2 . THR   B 1 24  ? 19.578  2.262   19.681  1.00 18.01 ? 58  THR   B CG2 1 
ATOM   3072 N  N   . ASN   B 1 25  ? 22.584  3.305   20.455  1.00 22.20 ? 59  ASN   B N   1 
ATOM   3073 C  CA  . ASN   B 1 25  ? 23.707  2.653   19.791  1.00 23.19 ? 59  ASN   B CA  1 
ATOM   3074 C  C   . ASN   B 1 25  ? 24.908  2.439   20.694  1.00 20.93 ? 59  ASN   B C   1 
ATOM   3075 O  O   . ASN   B 1 25  ? 25.663  1.488   20.494  1.00 25.86 ? 59  ASN   B O   1 
ATOM   3076 C  CB  . ASN   B 1 25  ? 24.126  3.457   18.566  1.00 22.09 ? 59  ASN   B CB  1 
ATOM   3077 C  CG  . ASN   B 1 25  ? 23.377  3.039   17.347  1.00 22.30 ? 59  ASN   B CG  1 
ATOM   3078 O  OD1 . ASN   B 1 25  ? 23.877  2.261   16.544  1.00 21.81 ? 59  ASN   B OD1 1 
ATOM   3079 N  ND2 . ASN   B 1 25  ? 22.144  3.516   17.214  1.00 24.82 ? 59  ASN   B ND2 1 
ATOM   3080 N  N   . VAL   B 1 26  ? 25.153  3.318   21.650  1.00 21.45 ? 60  VAL   B N   1 
ATOM   3081 C  CA  . VAL   B 1 26  ? 26.247  3.042   22.568  1.00 22.70 ? 60  VAL   B CA  1 
ATOM   3082 C  C   . VAL   B 1 26  ? 25.888  1.860   23.452  1.00 19.00 ? 60  VAL   B C   1 
ATOM   3083 O  O   . VAL   B 1 26  ? 26.703  0.961   23.671  1.00 20.99 ? 60  VAL   B O   1 
ATOM   3084 C  CB  . VAL   B 1 26  ? 26.581  4.293   23.402  1.00 19.58 ? 60  VAL   B CB  1 
ATOM   3085 C  CG1 . VAL   B 1 26  ? 27.695  3.983   24.417  1.00 17.27 ? 60  VAL   B CG1 1 
ATOM   3086 C  CG2 . VAL   B 1 26  ? 26.970  5.416   22.501  1.00 16.81 ? 60  VAL   B CG2 1 
ATOM   3087 N  N   . ALA   B 1 27  ? 24.658  1.841   23.960  1.00 17.83 ? 61  ALA   B N   1 
ATOM   3088 C  CA  . ALA   B 1 27  ? 24.260  0.825   24.922  1.00 24.91 ? 61  ALA   B CA  1 
ATOM   3089 C  C   . ALA   B 1 27  ? 24.266  -0.564  24.288  1.00 26.86 ? 61  ALA   B C   1 
ATOM   3090 O  O   . ALA   B 1 27  ? 24.683  -1.548  24.927  1.00 19.60 ? 61  ALA   B O   1 
ATOM   3091 C  CB  . ALA   B 1 27  ? 22.882  1.171   25.486  1.00 21.69 ? 61  ALA   B CB  1 
ATOM   3092 N  N   . ARG   B 1 28  ? 23.823  -0.652  23.020  1.00 28.03 ? 62  ARG   B N   1 
ATOM   3093 C  CA  . ARG   B 1 28  ? 23.856  -1.925  22.296  1.00 24.39 ? 62  ARG   B CA  1 
ATOM   3094 C  C   . ARG   B 1 28  ? 25.283  -2.360  22.007  1.00 20.05 ? 62  ARG   B C   1 
ATOM   3095 O  O   . ARG   B 1 28  ? 25.593  -3.550  22.083  1.00 23.44 ? 62  ARG   B O   1 
ATOM   3096 C  CB  . ARG   B 1 28  ? 23.050  -1.855  20.992  1.00 19.58 ? 62  ARG   B CB  1 
ATOM   3097 C  CG  . ARG   B 1 28  ? 21.608  -1.467  21.194  1.00 20.92 ? 62  ARG   B CG  1 
ATOM   3098 C  CD  . ARG   B 1 28  ? 20.679  -2.333  20.494  1.00 22.40 ? 62  ARG   B CD  1 
ATOM   3099 N  NE  . ARG   B 1 28  ? 19.302  -2.137  20.937  1.00 24.65 ? 62  ARG   B NE  1 
ATOM   3100 C  CZ  . ARG   B 1 28  ? 18.218  -2.642  20.377  1.00 28.31 ? 62  ARG   B CZ  1 
ATOM   3101 N  NH1 . ARG   B 1 28  ? 17.041  -2.345  20.907  1.00 25.57 ? 62  ARG   B NH1 1 
ATOM   3102 N  NH2 . ARG   B 1 28  ? 18.323  -3.437  19.327  1.00 30.41 ? 62  ARG   B NH2 1 
ATOM   3103 N  N   . ARG   B 1 29  ? 26.172  -1.430  21.674  1.00 18.11 ? 63  ARG   B N   1 
ATOM   3104 C  CA  . ARG   B 1 29  ? 27.559  -1.840  21.510  1.00 18.56 ? 63  ARG   B CA  1 
ATOM   3105 C  C   . ARG   B 1 29  ? 28.117  -2.367  22.834  1.00 22.35 ? 63  ARG   B C   1 
ATOM   3106 O  O   . ARG   B 1 29  ? 28.638  -3.492  22.894  1.00 26.51 ? 63  ARG   B O   1 
ATOM   3107 C  CB  . ARG   B 1 29  ? 28.389  -0.691  20.946  1.00 16.79 ? 63  ARG   B CB  1 
ATOM   3108 C  CG  . ARG   B 1 29  ? 29.787  -1.065  20.508  1.00 16.48 ? 63  ARG   B CG  1 
ATOM   3109 C  CD  . ARG   B 1 29  ? 30.796  -1.103  21.675  1.00 17.07 ? 63  ARG   B CD  1 
ATOM   3110 N  NE  . ARG   B 1 29  ? 32.149  -1.388  21.211  1.00 17.94 ? 63  ARG   B NE  1 
ATOM   3111 C  CZ  . ARG   B 1 29  ? 33.081  -0.461  21.041  1.00 17.32 ? 63  ARG   B CZ  1 
ATOM   3112 N  NH1 . ARG   B 1 29  ? 34.294  -0.791  20.605  1.00 15.61 ? 63  ARG   B NH1 1 
ATOM   3113 N  NH2 . ARG   B 1 29  ? 32.791  0.798   21.325  1.00 14.76 ? 63  ARG   B NH2 1 
ATOM   3114 N  N   . PHE   B 1 30  ? 27.949  -1.601  23.920  1.00 17.57 ? 64  PHE   B N   1 
ATOM   3115 C  CA  . PHE   B 1 30  ? 28.487  -2.007  25.218  1.00 17.03 ? 64  PHE   B CA  1 
ATOM   3116 C  C   . PHE   B 1 30  ? 27.876  -3.313  25.705  1.00 21.79 ? 64  PHE   B C   1 
ATOM   3117 O  O   . PHE   B 1 30  ? 28.570  -4.159  26.282  1.00 25.61 ? 64  PHE   B O   1 
ATOM   3118 C  CB  . PHE   B 1 30  ? 28.239  -0.918  26.250  1.00 18.04 ? 64  PHE   B CB  1 
ATOM   3119 C  CG  . PHE   B 1 30  ? 29.314  0.122   26.308  1.00 19.74 ? 64  PHE   B CG  1 
ATOM   3120 C  CD1 . PHE   B 1 30  ? 29.515  0.990   25.241  1.00 16.58 ? 64  PHE   B CD1 1 
ATOM   3121 C  CD2 . PHE   B 1 30  ? 30.116  0.247   27.445  1.00 19.42 ? 64  PHE   B CD2 1 
ATOM   3122 C  CE1 . PHE   B 1 30  ? 30.495  1.957   25.301  1.00 21.63 ? 64  PHE   B CE1 1 
ATOM   3123 C  CE2 . PHE   B 1 30  ? 31.108  1.228   27.521  1.00 20.73 ? 64  PHE   B CE2 1 
ATOM   3124 C  CZ  . PHE   B 1 30  ? 31.303  2.087   26.450  1.00 20.83 ? 64  PHE   B CZ  1 
ATOM   3125 N  N   . SER   B 1 31  ? 26.570  -3.484  25.508  1.00 24.38 ? 65  SER   B N   1 
ATOM   3126 C  CA  . SER   B 1 31  ? 25.905  -4.724  25.891  1.00 26.73 ? 65  SER   B CA  1 
ATOM   3127 C  C   . SER   B 1 31  ? 26.623  -5.939  25.312  1.00 28.67 ? 65  SER   B C   1 
ATOM   3128 O  O   . SER   B 1 31  ? 27.063  -6.838  26.042  1.00 27.61 ? 65  SER   B O   1 
ATOM   3129 C  CB  . SER   B 1 31  ? 24.457  -4.680  25.407  1.00 24.81 ? 65  SER   B CB  1 
ATOM   3130 O  OG  . SER   B 1 31  ? 23.785  -5.878  25.724  1.00 31.94 ? 65  SER   B OG  1 
ATOM   3131 N  N   . TRP   B 1 32  ? 26.771  -5.952  23.992  1.00 27.29 ? 66  TRP   B N   1 
ATOM   3132 C  CA  . TRP   B 1 32  ? 27.399  -7.060  23.291  1.00 26.00 ? 66  TRP   B CA  1 
ATOM   3133 C  C   . TRP   B 1 32  ? 28.886  -7.151  23.616  1.00 28.45 ? 66  TRP   B C   1 
ATOM   3134 O  O   . TRP   B 1 32  ? 29.443  -8.252  23.709  1.00 27.60 ? 66  TRP   B O   1 
ATOM   3135 C  CB  . TRP   B 1 32  ? 27.152  -6.882  21.783  1.00 26.52 ? 66  TRP   B CB  1 
ATOM   3136 C  CG  . TRP   B 1 32  ? 27.835  -7.852  20.871  1.00 24.32 ? 66  TRP   B CG  1 
ATOM   3137 C  CD1 . TRP   B 1 32  ? 28.702  -7.557  19.859  1.00 19.49 ? 66  TRP   B CD1 1 
ATOM   3138 C  CD2 . TRP   B 1 32  ? 27.703  -9.280  20.890  1.00 26.11 ? 66  TRP   B CD2 1 
ATOM   3139 N  NE1 . TRP   B 1 32  ? 29.106  -8.712  19.235  1.00 22.16 ? 66  TRP   B NE1 1 
ATOM   3140 C  CE2 . TRP   B 1 32  ? 28.515  -9.784  19.859  1.00 24.04 ? 66  TRP   B CE2 1 
ATOM   3141 C  CE3 . TRP   B 1 32  ? 26.981  -10.182 21.690  1.00 24.46 ? 66  TRP   B CE3 1 
ATOM   3142 C  CZ2 . TRP   B 1 32  ? 28.633  -11.146 19.612  1.00 21.45 ? 66  TRP   B CZ2 1 
ATOM   3143 C  CZ3 . TRP   B 1 32  ? 27.083  -11.520 21.433  1.00 25.04 ? 66  TRP   B CZ3 1 
ATOM   3144 C  CH2 . TRP   B 1 32  ? 27.892  -11.994 20.393  1.00 26.38 ? 66  TRP   B CH2 1 
ATOM   3145 N  N   . GLY   B 1 33  ? 29.552  -6.015  23.796  1.00 25.26 ? 67  GLY   B N   1 
ATOM   3146 C  CA  . GLY   B 1 33  ? 30.990  -6.070  23.989  1.00 24.48 ? 67  GLY   B CA  1 
ATOM   3147 C  C   . GLY   B 1 33  ? 31.401  -6.570  25.358  1.00 22.47 ? 67  GLY   B C   1 
ATOM   3148 O  O   . GLY   B 1 33  ? 32.518  -7.055  25.526  1.00 21.66 ? 67  GLY   B O   1 
ATOM   3149 N  N   . LEU   B 1 34  ? 30.530  -6.432  26.361  1.00 24.70 ? 68  LEU   B N   1 
ATOM   3150 C  CA  . LEU   B 1 34  ? 30.890  -6.744  27.740  1.00 25.73 ? 68  LEU   B CA  1 
ATOM   3151 C  C   . LEU   B 1 34  ? 30.002  -7.799  28.400  1.00 26.77 ? 68  LEU   B C   1 
ATOM   3152 O  O   . LEU   B 1 34  ? 30.318  -8.253  29.503  1.00 21.38 ? 68  LEU   B O   1 
ATOM   3153 C  CB  . LEU   B 1 34  ? 30.839  -5.479  28.605  1.00 26.17 ? 68  LEU   B CB  1 
ATOM   3154 C  CG  . LEU   B 1 34  ? 31.699  -4.242  28.408  1.00 26.74 ? 68  LEU   B CG  1 
ATOM   3155 C  CD1 . LEU   B 1 34  ? 30.845  -3.047  28.824  1.00 21.03 ? 68  LEU   B CD1 1 
ATOM   3156 C  CD2 . LEU   B 1 34  ? 32.977  -4.323  29.259  1.00 21.48 ? 68  LEU   B CD2 1 
ATOM   3157 N  N   . GLY   B 1 35  ? 28.896  -8.178  27.787  1.00 24.08 ? 69  GLY   B N   1 
ATOM   3158 C  CA  . GLY   B 1 35  ? 28.065  -9.174  28.406  1.00 25.30 ? 69  GLY   B CA  1 
ATOM   3159 C  C   . GLY   B 1 35  ? 27.202  -8.555  29.470  1.00 26.46 ? 69  GLY   B C   1 
ATOM   3160 O  O   . GLY   B 1 35  ? 27.148  -9.036  30.603  1.00 28.98 ? 69  GLY   B O   1 
ATOM   3161 N  N   . MET   B 1 36  ? 26.529  -7.473  29.117  1.00 27.14 ? 70  MET   B N   1 
ATOM   3162 C  CA  . MET   B 1 36  ? 25.670  -6.766  30.045  1.00 27.35 ? 70  MET   B CA  1 
ATOM   3163 C  C   . MET   B 1 36  ? 24.257  -6.798  29.490  1.00 29.01 ? 70  MET   B C   1 
ATOM   3164 O  O   . MET   B 1 36  ? 24.051  -6.783  28.274  1.00 27.50 ? 70  MET   B O   1 
ATOM   3165 C  CB  . MET   B 1 36  ? 26.156  -5.321  30.262  1.00 30.12 ? 70  MET   B CB  1 
ATOM   3166 C  CG  . MET   B 1 36  ? 27.655  -5.238  30.532  1.00 25.35 ? 70  MET   B CG  1 
ATOM   3167 S  SD  . MET   B 1 36  ? 28.184  -3.643  31.153  1.00 27.62 ? 70  MET   B SD  1 
ATOM   3168 C  CE  . MET   B 1 36  ? 27.095  -3.433  32.557  1.00 23.47 ? 70  MET   B CE  1 
ATOM   3169 N  N   . ARG   B 1 37  ? 23.291  -6.870  30.391  1.00 28.68 ? 71  ARG   B N   1 
ATOM   3170 C  CA  . ARG   B 1 37  ? 21.901  -7.090  30.037  1.00 28.37 ? 71  ARG   B CA  1 
ATOM   3171 C  C   . ARG   B 1 37  ? 21.137  -5.783  30.141  1.00 25.64 ? 71  ARG   B C   1 
ATOM   3172 O  O   . ARG   B 1 37  ? 21.285  -5.059  31.124  1.00 30.52 ? 71  ARG   B O   1 
ATOM   3173 C  CB  . ARG   B 1 37  ? 21.279  -8.142  30.958  1.00 35.85 ? 71  ARG   B CB  1 
ATOM   3174 N  N   . PHE   B 1 38  ? 20.330  -5.480  29.130  1.00 31.66 ? 72  PHE   B N   1 
ATOM   3175 C  CA  . PHE   B 1 38  ? 19.348  -4.406  29.250  1.00 36.72 ? 72  PHE   B CA  1 
ATOM   3176 C  C   . PHE   B 1 38  ? 18.342  -4.731  30.352  1.00 39.94 ? 72  PHE   B C   1 
ATOM   3177 O  O   . PHE   B 1 38  ? 17.549  -5.672  30.219  1.00 39.25 ? 72  PHE   B O   1 
ATOM   3178 C  CB  . PHE   B 1 38  ? 18.583  -4.204  27.947  1.00 31.74 ? 72  PHE   B CB  1 
ATOM   3179 C  CG  . PHE   B 1 38  ? 19.279  -3.364  26.934  1.00 34.07 ? 72  PHE   B CG  1 
ATOM   3180 C  CD1 . PHE   B 1 38  ? 20.131  -3.942  25.998  1.00 36.27 ? 72  PHE   B CD1 1 
ATOM   3181 C  CD2 . PHE   B 1 38  ? 19.019  -2.003  26.850  1.00 38.62 ? 72  PHE   B CD2 1 
ATOM   3182 C  CE1 . PHE   B 1 38  ? 20.745  -3.173  24.997  1.00 32.62 ? 72  PHE   B CE1 1 
ATOM   3183 C  CE2 . PHE   B 1 38  ? 19.633  -1.219  25.857  1.00 34.37 ? 72  PHE   B CE2 1 
ATOM   3184 C  CZ  . PHE   B 1 38  ? 20.496  -1.814  24.930  1.00 31.16 ? 72  PHE   B CZ  1 
ATOM   3185 N  N   . SER   B 1 39  ? 18.337  -3.959  31.435  1.00 35.66 ? 73  SER   B N   1 
ATOM   3186 C  CA  . SER   B 1 39  ? 17.415  -4.244  32.520  1.00 30.89 ? 73  SER   B CA  1 
ATOM   3187 C  C   . SER   B 1 39  ? 16.344  -3.189  32.711  1.00 29.90 ? 73  SER   B C   1 
ATOM   3188 O  O   . SER   B 1 39  ? 15.228  -3.545  33.086  1.00 33.27 ? 73  SER   B O   1 
ATOM   3189 C  CB  . SER   B 1 39  ? 18.173  -4.446  33.842  1.00 35.67 ? 73  SER   B CB  1 
ATOM   3190 O  OG  . SER   B 1 39  ? 19.078  -3.389  34.101  1.00 36.87 ? 73  SER   B OG  1 
ATOM   3191 N  N   . ALA   B 1 40  ? 16.633  -1.914  32.453  1.00 31.69 ? 74  ALA   B N   1 
ATOM   3192 C  CA  . ALA   B 1 40  ? 15.631  -0.873  32.660  1.00 30.06 ? 74  ALA   B CA  1 
ATOM   3193 C  C   . ALA   B 1 40  ? 15.793  0.211   31.606  1.00 29.78 ? 74  ALA   B C   1 
ATOM   3194 O  O   . ALA   B 1 40  ? 16.900  0.482   31.136  1.00 25.46 ? 74  ALA   B O   1 
ATOM   3195 C  CB  . ALA   B 1 40  ? 15.716  -0.255  34.062  1.00 24.70 ? 74  ALA   B CB  1 
ATOM   3196 N  N   . LYS   B 1 41  ? 14.673  0.836   31.252  1.00 31.51 ? 75  LYS   B N   1 
ATOM   3197 C  CA  . LYS   B 1 41  ? 14.644  1.907   30.273  1.00 28.99 ? 75  LYS   B CA  1 
ATOM   3198 C  C   . LYS   B 1 41  ? 13.878  3.116   30.816  1.00 29.83 ? 75  LYS   B C   1 
ATOM   3199 O  O   . LYS   B 1 41  ? 13.045  2.999   31.719  1.00 31.02 ? 75  LYS   B O   1 
ATOM   3200 C  CB  . LYS   B 1 41  ? 14.006  1.418   28.969  1.00 25.86 ? 75  LYS   B CB  1 
ATOM   3201 C  CG  . LYS   B 1 41  ? 12.535  1.084   29.097  1.00 28.85 ? 75  LYS   B CG  1 
ATOM   3202 C  CD  . LYS   B 1 41  ? 11.910  0.837   27.724  1.00 27.71 ? 75  LYS   B CD  1 
ATOM   3203 C  CE  . LYS   B 1 41  ? 10.455  0.399   27.836  1.00 26.69 ? 75  LYS   B CE  1 
ATOM   3204 N  NZ  . LYS   B 1 41  ? 9.844   0.202   26.487  1.00 29.49 ? 75  LYS   B NZ  1 
ATOM   3205 N  N   . SER   B 1 42  ? 14.170  4.288   30.244  1.00 24.69 ? 76  SER   B N   1 
ATOM   3206 C  CA  . SER   B 1 42  ? 13.389  5.503   30.484  1.00 24.46 ? 76  SER   B CA  1 
ATOM   3207 C  C   . SER   B 1 42  ? 13.481  6.361   29.228  1.00 28.75 ? 76  SER   B C   1 
ATOM   3208 O  O   . SER   B 1 42  ? 14.536  6.956   28.954  1.00 28.04 ? 76  SER   B O   1 
ATOM   3209 C  CB  . SER   B 1 42  ? 13.890  6.261   31.713  1.00 26.68 ? 76  SER   B CB  1 
ATOM   3210 O  OG  . SER   B 1 42  ? 13.227  7.501   31.875  1.00 27.31 ? 76  SER   B OG  1 
ATOM   3211 N  N   . ASP   B 1 43  ? 12.397  6.410   28.454  1.00 24.46 ? 77  ASP   B N   1 
ATOM   3212 C  CA  . ASP   B 1 43  ? 12.404  7.128   27.180  1.00 28.44 ? 77  ASP   B CA  1 
ATOM   3213 C  C   . ASP   B 1 43  ? 10.967  7.481   26.811  1.00 32.27 ? 77  ASP   B C   1 
ATOM   3214 O  O   . ASP   B 1 43  ? 10.059  7.388   27.643  1.00 33.36 ? 77  ASP   B O   1 
ATOM   3215 C  CB  . ASP   B 1 43  ? 13.100  6.317   26.078  1.00 26.79 ? 77  ASP   B CB  1 
ATOM   3216 C  CG  . ASP   B 1 43  ? 12.420  4.968   25.778  1.00 29.14 ? 77  ASP   B CG  1 
ATOM   3217 O  OD1 . ASP   B 1 43  ? 11.255  4.734   26.180  1.00 26.46 ? 77  ASP   B OD1 1 
ATOM   3218 O  OD2 . ASP   B 1 43  ? 13.073  4.142   25.099  1.00 26.96 ? 77  ASP   B OD2 1 
ATOM   3219 N  N   . LEU   B 1 44  ? 10.766  7.888   25.549  1.00 31.13 ? 78  LEU   B N   1 
ATOM   3220 C  CA  . LEU   B 1 44  ? 9.430   8.223   25.054  1.00 31.02 ? 78  LEU   B CA  1 
ATOM   3221 C  C   . LEU   B 1 44  ? 8.416   7.128   25.361  1.00 31.78 ? 78  LEU   B C   1 
ATOM   3222 O  O   . LEU   B 1 44  ? 7.255   7.423   25.665  1.00 31.51 ? 78  LEU   B O   1 
ATOM   3223 C  CB  . LEU   B 1 44  ? 9.470   8.476   23.544  1.00 23.65 ? 78  LEU   B CB  1 
ATOM   3224 C  CG  . LEU   B 1 44  ? 10.395  9.566   23.013  1.00 26.28 ? 78  LEU   B CG  1 
ATOM   3225 C  CD1 . LEU   B 1 44  ? 10.690  9.297   21.559  1.00 30.33 ? 78  LEU   B CD1 1 
ATOM   3226 C  CD2 . LEU   B 1 44  ? 9.793   10.941  23.183  1.00 24.94 ? 78  LEU   B CD2 1 
ATOM   3227 N  N   . SER   B 1 45  ? 8.832   5.855   25.285  1.00 29.73 ? 79  SER   B N   1 
ATOM   3228 C  CA  . SER   B 1 45  ? 7.902   4.759   25.539  1.00 31.33 ? 79  SER   B CA  1 
ATOM   3229 C  C   . SER   B 1 45  ? 7.439   4.717   26.988  1.00 31.24 ? 79  SER   B C   1 
ATOM   3230 O  O   . SER   B 1 45  ? 6.347   4.217   27.258  1.00 30.86 ? 79  SER   B O   1 
ATOM   3231 C  CB  . SER   B 1 45  ? 8.523   3.414   25.152  1.00 29.78 ? 79  SER   B CB  1 
ATOM   3232 O  OG  . SER   B 1 45  ? 9.401   2.935   26.157  1.00 34.37 ? 79  SER   B OG  1 
ATOM   3233 N  N   . THR   B 1 46  ? 8.233   5.240   27.922  1.00 32.57 ? 80  THR   B N   1 
ATOM   3234 C  CA  . THR   B 1 46  ? 7.827   5.369   29.313  1.00 30.25 ? 80  THR   B CA  1 
ATOM   3235 C  C   . THR   B 1 46  ? 7.376   6.797   29.664  1.00 36.32 ? 80  THR   B C   1 
ATOM   3236 O  O   . THR   B 1 46  ? 7.273   7.136   30.850  1.00 39.58 ? 80  THR   B O   1 
ATOM   3237 C  CB  . THR   B 1 46  ? 8.968   4.919   30.227  1.00 29.62 ? 80  THR   B CB  1 
ATOM   3238 O  OG1 . THR   B 1 46  ? 10.112  5.760   30.011  1.00 32.15 ? 80  THR   B OG1 1 
ATOM   3239 C  CG2 . THR   B 1 46  ? 9.345   3.476   29.937  1.00 24.48 ? 80  THR   B CG2 1 
ATOM   3240 N  N   . GLY   B 1 47  ? 7.103   7.636   28.657  1.00 33.88 ? 81  GLY   B N   1 
ATOM   3241 C  CA  . GLY   B 1 47  ? 6.638   8.995   28.893  1.00 32.86 ? 81  GLY   B CA  1 
ATOM   3242 C  C   . GLY   B 1 47  ? 7.717   10.013  29.185  1.00 32.95 ? 81  GLY   B C   1 
ATOM   3243 O  O   . GLY   B 1 47  ? 7.436   11.045  29.798  1.00 40.32 ? 81  GLY   B O   1 
ATOM   3244 N  N   . ASN   B 1 48  ? 8.942   9.755   28.766  1.00 33.34 ? 82  ASN   B N   1 
ATOM   3245 C  CA  . ASN   B 1 48  ? 10.053  10.679  28.933  1.00 34.09 ? 82  ASN   B CA  1 
ATOM   3246 C  C   . ASN   B 1 48  ? 10.212  11.457  27.623  1.00 39.27 ? 82  ASN   B C   1 
ATOM   3247 O  O   . ASN   B 1 48  ? 10.567  10.881  26.587  1.00 32.34 ? 82  ASN   B O   1 
ATOM   3248 C  CB  . ASN   B 1 48  ? 11.316  9.903   29.308  1.00 31.80 ? 82  ASN   B CB  1 
ATOM   3249 C  CG  . ASN   B 1 48  ? 12.370  10.764  29.936  1.00 31.64 ? 82  ASN   B CG  1 
ATOM   3250 O  OD1 . ASN   B 1 48  ? 12.416  11.963  29.700  1.00 33.19 ? 82  ASN   B OD1 1 
ATOM   3251 N  ND2 . ASN   B 1 48  ? 13.246  10.154  30.732  1.00 31.86 ? 82  ASN   B ND2 1 
ATOM   3252 N  N   . MET   B 1 49  ? 9.907   12.758  27.667  1.00 41.13 ? 83  MET   B N   1 
ATOM   3253 C  CA  . MET   B 1 49  ? 10.054  13.668  26.541  1.00 35.06 ? 83  MET   B CA  1 
ATOM   3254 C  C   . MET   B 1 49  ? 11.408  14.338  26.518  1.00 35.26 ? 83  MET   B C   1 
ATOM   3255 O  O   . MET   B 1 49  ? 11.685  15.108  25.593  1.00 39.26 ? 83  MET   B O   1 
ATOM   3256 C  CB  . MET   B 1 49  ? 8.978   14.756  26.591  1.00 40.78 ? 83  MET   B CB  1 
ATOM   3257 C  CG  . MET   B 1 49  ? 7.611   14.260  26.976  1.00 43.56 ? 83  MET   B CG  1 
ATOM   3258 S  SD  . MET   B 1 49  ? 7.060   13.136  25.699  1.00 59.22 ? 83  MET   B SD  1 
ATOM   3259 C  CE  . MET   B 1 49  ? 7.275   14.184  24.265  1.00 49.05 ? 83  MET   B CE  1 
ATOM   3260 N  N   . VAL   B 1 50  ? 12.241  14.082  27.518  1.00 30.40 ? 84  VAL   B N   1 
ATOM   3261 C  CA  . VAL   B 1 50  ? 13.438  14.868  27.761  1.00 32.27 ? 84  VAL   B CA  1 
ATOM   3262 C  C   . VAL   B 1 50  ? 14.691  14.115  27.326  1.00 30.85 ? 84  VAL   B C   1 
ATOM   3263 O  O   . VAL   B 1 50  ? 15.406  14.556  26.425  1.00 35.84 ? 84  VAL   B O   1 
ATOM   3264 C  CB  . VAL   B 1 50  ? 13.521  15.307  29.241  1.00 31.58 ? 84  VAL   B CB  1 
ATOM   3265 C  CG1 . VAL   B 1 50  ? 14.602  16.357  29.437  1.00 25.87 ? 84  VAL   B CG1 1 
ATOM   3266 C  CG2 . VAL   B 1 50  ? 12.184  15.830  29.707  1.00 32.17 ? 84  VAL   B CG2 1 
ATOM   3267 N  N   . HIS   B 1 51  ? 14.975  12.974  27.953  1.00 28.58 ? 85  HIS   B N   1 
ATOM   3268 C  CA  . HIS   B 1 51  ? 16.133  12.164  27.587  1.00 32.45 ? 85  HIS   B CA  1 
ATOM   3269 C  C   . HIS   B 1 51  ? 15.737  10.699  27.385  1.00 32.78 ? 85  HIS   B C   1 
ATOM   3270 O  O   . HIS   B 1 51  ? 14.681  10.249  27.839  1.00 31.58 ? 85  HIS   B O   1 
ATOM   3271 C  CB  . HIS   B 1 51  ? 17.260  12.271  28.642  1.00 31.72 ? 85  HIS   B CB  1 
ATOM   3272 C  CG  . HIS   B 1 51  ? 16.827  11.933  30.038  1.00 34.79 ? 85  HIS   B CG  1 
ATOM   3273 N  ND1 . HIS   B 1 51  ? 16.655  10.636  30.473  1.00 31.13 ? 85  HIS   B ND1 1 
ATOM   3274 C  CD2 . HIS   B 1 51  ? 16.529  12.728  31.096  1.00 31.23 ? 85  HIS   B CD2 1 
ATOM   3275 C  CE1 . HIS   B 1 51  ? 16.263  10.649  31.736  1.00 32.95 ? 85  HIS   B CE1 1 
ATOM   3276 N  NE2 . HIS   B 1 51  ? 16.183  11.904  32.137  1.00 31.96 ? 85  HIS   B NE2 1 
ATOM   3277 N  N   . ALA   B 1 52  ? 16.600  9.961   26.676  1.00 29.16 ? 86  ALA   B N   1 
ATOM   3278 C  CA  . ALA   B 1 52  ? 16.505  8.511   26.541  1.00 23.48 ? 86  ALA   B CA  1 
ATOM   3279 C  C   . ALA   B 1 52  ? 17.622  7.864   27.352  1.00 28.78 ? 86  ALA   B C   1 
ATOM   3280 O  O   . ALA   B 1 52  ? 18.789  8.252   27.220  1.00 25.31 ? 86  ALA   B O   1 
ATOM   3281 C  CB  . ALA   B 1 52  ? 16.614  8.088   25.079  1.00 22.02 ? 86  ALA   B CB  1 
ATOM   3282 N  N   . SER   B 1 53  ? 17.271  6.876   28.181  1.00 27.29 ? 87  SER   B N   1 
ATOM   3283 C  CA  . SER   B 1 53  ? 18.214  6.272   29.121  1.00 25.39 ? 87  SER   B CA  1 
ATOM   3284 C  C   . SER   B 1 53  ? 18.029  4.762   29.181  1.00 24.81 ? 87  SER   B C   1 
ATOM   3285 O  O   . SER   B 1 53  ? 16.902  4.270   29.270  1.00 26.13 ? 87  SER   B O   1 
ATOM   3286 C  CB  . SER   B 1 53  ? 18.055  6.843   30.545  1.00 25.66 ? 87  SER   B CB  1 
ATOM   3287 O  OG  . SER   B 1 53  ? 18.538  8.171   30.657  1.00 30.62 ? 87  SER   B OG  1 
ATOM   3288 N  N   . TYR   B 1 54  ? 19.140  4.028   29.172  1.00 24.68 ? 88  TYR   B N   1 
ATOM   3289 C  CA  . TYR   B 1 54  ? 19.107  2.570   29.149  1.00 20.78 ? 88  TYR   B CA  1 
ATOM   3290 C  C   . TYR   B 1 54  ? 20.140  2.055   30.139  1.00 26.75 ? 88  TYR   B C   1 
ATOM   3291 O  O   . TYR   B 1 54  ? 21.307  2.463   30.102  1.00 24.97 ? 88  TYR   B O   1 
ATOM   3292 C  CB  . TYR   B 1 54  ? 19.356  2.029   27.728  1.00 18.55 ? 88  TYR   B CB  1 
ATOM   3293 C  CG  . TYR   B 1 54  ? 18.394  2.646   26.736  1.00 24.22 ? 88  TYR   B CG  1 
ATOM   3294 C  CD1 . TYR   B 1 54  ? 17.038  2.295   26.751  1.00 23.08 ? 88  TYR   B CD1 1 
ATOM   3295 C  CD2 . TYR   B 1 54  ? 18.815  3.624   25.821  1.00 19.99 ? 88  TYR   B CD2 1 
ATOM   3296 C  CE1 . TYR   B 1 54  ? 16.131  2.880   25.878  1.00 20.05 ? 88  TYR   B CE1 1 
ATOM   3297 C  CE2 . TYR   B 1 54  ? 17.909  4.213   24.945  1.00 21.38 ? 88  TYR   B CE2 1 
ATOM   3298 C  CZ  . TYR   B 1 54  ? 16.564  3.844   24.987  1.00 23.25 ? 88  TYR   B CZ  1 
ATOM   3299 O  OH  . TYR   B 1 54  ? 15.642  4.421   24.141  1.00 23.51 ? 88  TYR   B OH  1 
ATOM   3300 N  N   . LEU   B 1 55  ? 19.698  1.164   31.026  1.00 28.25 ? 89  LEU   B N   1 
ATOM   3301 C  CA  . LEU   B 1 55  ? 20.531  0.592   32.070  1.00 23.79 ? 89  LEU   B CA  1 
ATOM   3302 C  C   . LEU   B 1 55  ? 21.031  -0.784  31.632  1.00 32.55 ? 89  LEU   B C   1 
ATOM   3303 O  O   . LEU   B 1 55  ? 20.231  -1.671  31.312  1.00 29.99 ? 89  LEU   B O   1 
ATOM   3304 C  CB  . LEU   B 1 55  ? 19.744  0.497   33.375  1.00 24.43 ? 89  LEU   B CB  1 
ATOM   3305 C  CG  . LEU   B 1 55  ? 20.587  0.207   34.617  1.00 31.89 ? 89  LEU   B CG  1 
ATOM   3306 C  CD1 . LEU   B 1 55  ? 20.999  1.490   35.280  1.00 32.12 ? 89  LEU   B CD1 1 
ATOM   3307 C  CD2 . LEU   B 1 55  ? 19.833  -0.648  35.613  1.00 38.18 ? 89  LEU   B CD2 1 
ATOM   3308 N  N   . LEU   B 1 56  ? 22.352  -0.955  31.612  1.00 32.64 ? 90  LEU   B N   1 
ATOM   3309 C  CA  . LEU   B 1 56  ? 22.974  -2.265  31.508  1.00 27.57 ? 90  LEU   B CA  1 
ATOM   3310 C  C   . LEU   B 1 56  ? 23.380  -2.725  32.900  1.00 27.49 ? 90  LEU   B C   1 
ATOM   3311 O  O   . LEU   B 1 56  ? 23.788  -1.906  33.723  1.00 28.41 ? 90  LEU   B O   1 
ATOM   3312 C  CB  . LEU   B 1 56  ? 24.205  -2.227  30.598  1.00 25.58 ? 90  LEU   B CB  1 
ATOM   3313 C  CG  . LEU   B 1 56  ? 24.080  -1.647  29.191  1.00 25.42 ? 90  LEU   B CG  1 
ATOM   3314 C  CD1 . LEU   B 1 56  ? 25.380  -1.854  28.388  1.00 20.92 ? 90  LEU   B CD1 1 
ATOM   3315 C  CD2 . LEU   B 1 56  ? 22.856  -2.201  28.448  1.00 24.66 ? 90  LEU   B CD2 1 
ATOM   3316 N  N   . THR   B 1 57  ? 23.277  -4.036  33.156  1.00 28.57 ? 91  THR   B N   1 
ATOM   3317 C  CA  . THR   B 1 57  ? 23.704  -4.644  34.417  1.00 31.40 ? 91  THR   B CA  1 
ATOM   3318 C  C   . THR   B 1 57  ? 24.415  -5.967  34.154  1.00 35.14 ? 91  THR   B C   1 
ATOM   3319 O  O   . THR   B 1 57  ? 23.916  -6.803  33.391  1.00 31.83 ? 91  THR   B O   1 
ATOM   3320 C  CB  . THR   B 1 57  ? 22.526  -4.926  35.373  1.00 28.02 ? 91  THR   B CB  1 
ATOM   3321 O  OG1 . THR   B 1 57  ? 21.609  -5.827  34.745  1.00 31.74 ? 91  THR   B OG1 1 
ATOM   3322 C  CG2 . THR   B 1 57  ? 21.796  -3.668  35.778  1.00 25.61 ? 91  THR   B CG2 1 
ATOM   3323 N  N   . SER   B 1 58  ? 25.556  -6.170  34.817  1.00 32.06 ? 92  SER   B N   1 
ATOM   3324 C  CA  . SER   B 1 58  ? 26.203  -7.481  34.899  1.00 27.46 ? 92  SER   B CA  1 
ATOM   3325 C  C   . SER   B 1 58  ? 26.595  -7.707  36.354  1.00 29.67 ? 92  SER   B C   1 
ATOM   3326 O  O   . SER   B 1 58  ? 27.608  -7.176  36.815  1.00 31.59 ? 92  SER   B O   1 
ATOM   3327 C  CB  . SER   B 1 58  ? 27.419  -7.575  33.985  1.00 29.85 ? 92  SER   B CB  1 
ATOM   3328 O  OG  . SER   B 1 58  ? 27.771  -8.942  33.767  1.00 29.62 ? 92  SER   B OG  1 
ATOM   3329 N  N   . GLY   B 1 59  ? 25.808  -8.501  37.073  1.00 29.17 ? 93  GLY   B N   1 
ATOM   3330 C  CA  . GLY   B 1 59  ? 26.023  -8.666  38.497  1.00 26.21 ? 93  GLY   B CA  1 
ATOM   3331 C  C   . GLY   B 1 59  ? 25.537  -7.467  39.283  1.00 30.69 ? 93  GLY   B C   1 
ATOM   3332 O  O   . GLY   B 1 59  ? 24.330  -7.220  39.370  1.00 33.65 ? 93  GLY   B O   1 
ATOM   3333 N  N   . ASP   B 1 60  ? 26.479  -6.714  39.858  1.00 33.48 ? 94  ASP   B N   1 
ATOM   3334 C  CA  . ASP   B 1 60  ? 26.215  -5.452  40.544  1.00 34.30 ? 94  ASP   B CA  1 
ATOM   3335 C  C   . ASP   B 1 60  ? 26.597  -4.242  39.703  1.00 36.31 ? 94  ASP   B C   1 
ATOM   3336 O  O   . ASP   B 1 60  ? 26.329  -3.103  40.114  1.00 35.60 ? 94  ASP   B O   1 
ATOM   3337 C  CB  . ASP   B 1 60  ? 26.983  -5.384  41.879  1.00 29.78 ? 94  ASP   B CB  1 
ATOM   3338 C  CG  . ASP   B 1 60  ? 26.381  -6.284  42.953  1.00 46.83 ? 94  ASP   B CG  1 
ATOM   3339 O  OD1 . ASP   B 1 60  ? 25.140  -6.476  42.942  1.00 47.07 ? 94  ASP   B OD1 1 
ATOM   3340 O  OD2 . ASP   B 1 60  ? 27.147  -6.798  43.809  1.00 50.95 ? 94  ASP   B OD2 1 
ATOM   3341 N  N   . LEU   B 1 61  ? 27.250  -4.463  38.563  1.00 30.90 ? 95  LEU   B N   1 
ATOM   3342 C  CA  . LEU   B 1 61  ? 27.643  -3.358  37.714  1.00 27.05 ? 95  LEU   B CA  1 
ATOM   3343 C  C   . LEU   B 1 61  ? 26.401  -2.803  37.036  1.00 34.52 ? 95  LEU   B C   1 
ATOM   3344 O  O   . LEU   B 1 61  ? 25.582  -3.560  36.493  1.00 27.52 ? 95  LEU   B O   1 
ATOM   3345 C  CB  . LEU   B 1 61  ? 28.670  -3.812  36.683  1.00 26.67 ? 95  LEU   B CB  1 
ATOM   3346 C  CG  . LEU   B 1 61  ? 29.319  -2.674  35.893  1.00 26.59 ? 95  LEU   B CG  1 
ATOM   3347 C  CD1 . LEU   B 1 61  ? 30.119  -1.787  36.818  1.00 23.05 ? 95  LEU   B CD1 1 
ATOM   3348 C  CD2 . LEU   B 1 61  ? 30.178  -3.211  34.764  1.00 22.68 ? 95  LEU   B CD2 1 
ATOM   3349 N  N   . ARG   B 1 62  ? 26.245  -1.477  37.105  1.00 34.57 ? 96  ARG   B N   1 
ATOM   3350 C  CA  . ARG   B 1 62  ? 25.128  -0.779  36.477  1.00 27.31 ? 96  ARG   B CA  1 
ATOM   3351 C  C   . ARG   B 1 62  ? 25.701  0.303   35.587  1.00 21.99 ? 96  ARG   B C   1 
ATOM   3352 O  O   . ARG   B 1 62  ? 26.195  1.308   36.093  1.00 29.56 ? 96  ARG   B O   1 
ATOM   3353 C  CB  . ARG   B 1 62  ? 24.183  -0.171  37.510  1.00 32.34 ? 96  ARG   B CB  1 
ATOM   3354 C  CG  . ARG   B 1 62  ? 23.438  -1.157  38.414  1.00 35.65 ? 96  ARG   B CG  1 
ATOM   3355 C  CD  . ARG   B 1 62  ? 22.575  -0.345  39.373  1.00 43.97 ? 96  ARG   B CD  1 
ATOM   3356 N  NE  . ARG   B 1 62  ? 22.068  -1.057  40.553  1.00 50.73 ? 96  ARG   B NE  1 
ATOM   3357 C  CZ  . ARG   B 1 62  ? 22.776  -1.333  41.651  1.00 48.79 ? 96  ARG   B CZ  1 
ATOM   3358 N  NH1 . ARG   B 1 62  ? 24.067  -1.013  41.744  1.00 42.70 ? 96  ARG   B NH1 1 
ATOM   3359 N  NH2 . ARG   B 1 62  ? 22.188  -1.953  42.664  1.00 55.89 ? 96  ARG   B NH2 1 
ATOM   3360 N  N   . PHE   B 1 63  ? 25.643  0.095   34.273  1.00 26.60 ? 97  PHE   B N   1 
ATOM   3361 C  CA  . PHE   B 1 63  ? 25.966  1.121   33.288  1.00 19.01 ? 97  PHE   B CA  1 
ATOM   3362 C  C   . PHE   B 1 63  ? 24.685  1.757   32.776  1.00 21.37 ? 97  PHE   B C   1 
ATOM   3363 O  O   . PHE   B 1 63  ? 23.751  1.057   32.365  1.00 24.95 ? 97  PHE   B O   1 
ATOM   3364 C  CB  . PHE   B 1 63  ? 26.751  0.548   32.113  1.00 16.67 ? 97  PHE   B CB  1 
ATOM   3365 C  CG  . PHE   B 1 63  ? 28.192  0.353   32.400  1.00 17.59 ? 97  PHE   B CG  1 
ATOM   3366 C  CD1 . PHE   B 1 63  ? 28.693  0.584   33.679  1.00 19.02 ? 97  PHE   B CD1 1 
ATOM   3367 C  CD2 . PHE   B 1 63  ? 29.057  -0.072  31.405  1.00 15.93 ? 97  PHE   B CD2 1 
ATOM   3368 C  CE1 . PHE   B 1 63  ? 30.042  0.383   33.966  1.00 18.33 ? 97  PHE   B CE1 1 
ATOM   3369 C  CE2 . PHE   B 1 63  ? 30.410  -0.247  31.678  1.00 16.55 ? 97  PHE   B CE2 1 
ATOM   3370 C  CZ  . PHE   B 1 63  ? 30.902  -0.025  32.968  1.00 15.78 ? 97  PHE   B CZ  1 
ATOM   3371 N  N   . LEU   B 1 64  ? 24.649  3.081   32.790  1.00 21.25 ? 98  LEU   B N   1 
ATOM   3372 C  CA  . LEU   B 1 64  ? 23.511  3.843   32.302  1.00 22.40 ? 98  LEU   B CA  1 
ATOM   3373 C  C   . LEU   B 1 64  ? 23.965  4.778   31.184  1.00 24.84 ? 98  LEU   B C   1 
ATOM   3374 O  O   . LEU   B 1 64  ? 25.067  5.343   31.233  1.00 22.63 ? 98  LEU   B O   1 
ATOM   3375 C  CB  . LEU   B 1 64  ? 22.864  4.618   33.452  1.00 20.55 ? 98  LEU   B CB  1 
ATOM   3376 C  CG  . LEU   B 1 64  ? 21.587  5.418   33.209  1.00 28.10 ? 98  LEU   B CG  1 
ATOM   3377 C  CD1 . LEU   B 1 64  ? 20.339  4.535   33.044  1.00 20.30 ? 98  LEU   B CD1 1 
ATOM   3378 C  CD2 . LEU   B 1 64  ? 21.431  6.424   34.350  1.00 26.80 ? 98  LEU   B CD2 1 
ATOM   3379 N  N   . PHE   B 1 65  ? 23.113  4.929   30.170  1.00 21.82 ? 99  PHE   B N   1 
ATOM   3380 C  CA  . PHE   B 1 65  ? 23.466  5.632   28.944  1.00 21.90 ? 99  PHE   B CA  1 
ATOM   3381 C  C   . PHE   B 1 65  ? 22.339  6.598   28.633  1.00 30.84 ? 99  PHE   B C   1 
ATOM   3382 O  O   . PHE   B 1 65  ? 21.191  6.162   28.466  1.00 29.87 ? 99  PHE   B O   1 
ATOM   3383 C  CB  . PHE   B 1 65  ? 23.679  4.654   27.779  1.00 22.40 ? 99  PHE   B CB  1 
ATOM   3384 C  CG  . PHE   B 1 65  ? 24.785  3.664   28.016  1.00 21.81 ? 99  PHE   B CG  1 
ATOM   3385 C  CD1 . PHE   B 1 65  ? 24.533  2.467   28.671  1.00 19.16 ? 99  PHE   B CD1 1 
ATOM   3386 C  CD2 . PHE   B 1 65  ? 26.079  3.936   27.602  1.00 20.10 ? 99  PHE   B CD2 1 
ATOM   3387 C  CE1 . PHE   B 1 65  ? 25.540  1.586   28.912  1.00 18.61 ? 99  PHE   B CE1 1 
ATOM   3388 C  CE2 . PHE   B 1 65  ? 27.099  3.027   27.830  1.00 16.54 ? 99  PHE   B CE2 1 
ATOM   3389 C  CZ  . PHE   B 1 65  ? 26.831  1.866   28.492  1.00 16.58 ? 99  PHE   B CZ  1 
ATOM   3390 N  N   . THR   B 1 66  ? 22.669  7.901   28.547  1.00 24.62 ? 100 THR   B N   1 
ATOM   3391 C  CA  . THR   B 1 66  ? 21.692  8.977   28.396  1.00 24.43 ? 100 THR   B CA  1 
ATOM   3392 C  C   . THR   B 1 66  ? 22.077  9.890   27.240  1.00 26.07 ? 100 THR   B C   1 
ATOM   3393 O  O   . THR   B 1 66  ? 23.224  10.354  27.159  1.00 26.18 ? 100 THR   B O   1 
ATOM   3394 C  CB  . THR   B 1 66  ? 21.568  9.817   29.689  1.00 26.34 ? 100 THR   B CB  1 
ATOM   3395 O  OG1 . THR   B 1 66  ? 21.181  8.985   30.796  1.00 24.60 ? 100 THR   B OG1 1 
ATOM   3396 C  CG2 . THR   B 1 66  ? 20.545  10.943  29.509  1.00 23.51 ? 100 THR   B CG2 1 
ATOM   3397 N  N   . ALA   B 1 67  ? 21.116  10.156  26.362  1.00 24.16 ? 101 ALA   B N   1 
ATOM   3398 C  CA  . ALA   B 1 67  ? 21.203  11.170  25.323  1.00 22.96 ? 101 ALA   B CA  1 
ATOM   3399 C  C   . ALA   B 1 67  ? 19.937  12.010  25.355  1.00 29.78 ? 101 ALA   B C   1 
ATOM   3400 O  O   . ALA   B 1 67  ? 18.892  11.555  25.835  1.00 30.74 ? 101 ALA   B O   1 
ATOM   3401 C  CB  . ALA   B 1 67  ? 21.379  10.557  23.928  1.00 18.11 ? 101 ALA   B CB  1 
ATOM   3402 N  N   . PRO   B 1 68  ? 19.991  13.242  24.854  1.00 31.10 ? 102 PRO   B N   1 
ATOM   3403 C  CA  . PRO   B 1 68  ? 18.806  14.103  24.878  1.00 30.47 ? 102 PRO   B CA  1 
ATOM   3404 C  C   . PRO   B 1 68  ? 17.944  13.966  23.638  1.00 26.96 ? 102 PRO   B C   1 
ATOM   3405 O  O   . PRO   B 1 68  ? 18.429  13.693  22.545  1.00 26.11 ? 102 PRO   B O   1 
ATOM   3406 C  CB  . PRO   B 1 68  ? 19.421  15.507  24.933  1.00 32.39 ? 102 PRO   B CB  1 
ATOM   3407 C  CG  . PRO   B 1 68  ? 20.683  15.352  24.138  1.00 33.59 ? 102 PRO   B CG  1 
ATOM   3408 C  CD  . PRO   B 1 68  ? 21.194  13.970  24.399  1.00 26.76 ? 102 PRO   B CD  1 
ATOM   3409 N  N   . TYR   B 1 69  ? 16.645  14.202  23.819  1.00 30.98 ? 103 TYR   B N   1 
ATOM   3410 C  CA  . TYR   B 1 69  ? 15.735  14.393  22.692  1.00 30.48 ? 103 TYR   B CA  1 
ATOM   3411 C  C   . TYR   B 1 69  ? 15.863  15.815  22.124  1.00 33.95 ? 103 TYR   B C   1 
ATOM   3412 O  O   . TYR   B 1 69  ? 16.680  16.627  22.569  1.00 33.54 ? 103 TYR   B O   1 
ATOM   3413 C  CB  . TYR   B 1 69  ? 14.303  14.091  23.123  1.00 24.68 ? 103 TYR   B CB  1 
ATOM   3414 C  CG  . TYR   B 1 69  ? 14.081  12.624  23.346  1.00 28.84 ? 103 TYR   B CG  1 
ATOM   3415 C  CD1 . TYR   B 1 69  ? 14.212  11.714  22.294  1.00 27.22 ? 103 TYR   B CD1 1 
ATOM   3416 C  CD2 . TYR   B 1 69  ? 13.765  12.129  24.603  1.00 32.41 ? 103 TYR   B CD2 1 
ATOM   3417 C  CE1 . TYR   B 1 69  ? 14.027  10.355  22.489  1.00 25.06 ? 103 TYR   B CE1 1 
ATOM   3418 C  CE2 . TYR   B 1 69  ? 13.566  10.763  24.810  1.00 30.77 ? 103 TYR   B CE2 1 
ATOM   3419 C  CZ  . TYR   B 1 69  ? 13.704  9.880   23.750  1.00 29.66 ? 103 TYR   B CZ  1 
ATOM   3420 O  OH  . TYR   B 1 69  ? 13.510  8.527   23.959  1.00 27.06 ? 103 TYR   B OH  1 
ATOM   3421 N  N   . SER   B 1 70  ? 15.069  16.126  21.106  1.00 36.69 ? 104 SER   B N   1 
ATOM   3422 C  CA  . SER   B 1 70  ? 14.990  17.511  20.674  1.00 37.29 ? 104 SER   B CA  1 
ATOM   3423 C  C   . SER   B 1 70  ? 14.362  18.332  21.794  1.00 41.52 ? 104 SER   B C   1 
ATOM   3424 O  O   . SER   B 1 70  ? 13.448  17.850  22.481  1.00 44.87 ? 104 SER   B O   1 
ATOM   3425 C  CB  . SER   B 1 70  ? 14.168  17.645  19.389  1.00 43.99 ? 104 SER   B CB  1 
ATOM   3426 O  OG  . SER   B 1 70  ? 13.961  19.009  19.023  1.00 45.08 ? 104 SER   B OG  1 
ATOM   3427 N  N   . PRO   B 1 71  ? 14.843  19.549  22.044  1.00 41.10 ? 105 PRO   B N   1 
ATOM   3428 C  CA  . PRO   B 1 71  ? 14.240  20.344  23.118  1.00 42.13 ? 105 PRO   B CA  1 
ATOM   3429 C  C   . PRO   B 1 71  ? 12.824  20.754  22.791  1.00 43.51 ? 105 PRO   B C   1 
ATOM   3430 O  O   . PRO   B 1 71  ? 12.046  21.034  23.711  1.00 47.17 ? 105 PRO   B O   1 
ATOM   3431 C  CB  . PRO   B 1 71  ? 15.175  21.554  23.238  1.00 41.71 ? 105 PRO   B CB  1 
ATOM   3432 C  CG  . PRO   B 1 71  ? 16.401  21.185  22.446  1.00 45.11 ? 105 PRO   B CG  1 
ATOM   3433 C  CD  . PRO   B 1 71  ? 15.922  20.277  21.364  1.00 43.47 ? 105 PRO   B CD  1 
ATOM   3434 N  N   . SER   B 1 72  ? 12.464  20.776  21.506  1.00 38.55 ? 106 SER   B N   1 
ATOM   3435 C  CA  . SER   B 1 72  ? 11.086  21.041  21.121  1.00 36.44 ? 106 SER   B CA  1 
ATOM   3436 C  C   . SER   B 1 72  ? 10.137  20.053  21.775  1.00 45.96 ? 106 SER   B C   1 
ATOM   3437 O  O   . SER   B 1 72  ? 9.082   20.442  22.286  1.00 53.35 ? 106 SER   B O   1 
ATOM   3438 C  CB  . SER   B 1 72  ? 10.951  20.970  19.607  1.00 40.49 ? 106 SER   B CB  1 
ATOM   3439 O  OG  . SER   B 1 72  ? 11.262  19.662  19.145  1.00 47.85 ? 106 SER   B OG  1 
ATOM   3440 N  N   . LEU   B 1 73  ? 10.494  18.764  21.762  1.00 49.64 ? 107 LEU   B N   1 
ATOM   3441 C  CA  . LEU   B 1 73  ? 9.665   17.743  22.396  1.00 46.16 ? 107 LEU   B CA  1 
ATOM   3442 C  C   . LEU   B 1 73  ? 9.218   18.159  23.791  1.00 52.73 ? 107 LEU   B C   1 
ATOM   3443 O  O   . LEU   B 1 73  ? 8.074   17.900  24.184  1.00 55.96 ? 107 LEU   B O   1 
ATOM   3444 C  CB  . LEU   B 1 73  ? 10.423  16.422  22.493  1.00 50.98 ? 107 LEU   B CB  1 
ATOM   3445 C  CG  . LEU   B 1 73  ? 10.751  15.572  21.277  1.00 41.78 ? 107 LEU   B CG  1 
ATOM   3446 C  CD1 . LEU   B 1 73  ? 10.774  14.131  21.750  1.00 32.54 ? 107 LEU   B CD1 1 
ATOM   3447 C  CD2 . LEU   B 1 73  ? 9.741   15.762  20.165  1.00 36.79 ? 107 LEU   B CD2 1 
ATOM   3448 N  N   . SER   B 1 74  ? 10.113  18.785  24.562  1.00 53.04 ? 108 SER   B N   1 
ATOM   3449 C  CA  . SER   B 1 74  ? 9.831   19.199  25.933  1.00 55.47 ? 108 SER   B CA  1 
ATOM   3450 C  C   . SER   B 1 74  ? 9.733   20.716  26.058  1.00 59.26 ? 108 SER   B C   1 
ATOM   3451 O  O   . SER   B 1 74  ? 10.136  21.289  27.075  1.00 65.09 ? 108 SER   B O   1 
ATOM   3452 C  CB  . SER   B 1 74  ? 10.891  18.653  26.896  1.00 51.83 ? 108 SER   B CB  1 
ATOM   3453 O  OG  . SER   B 1 74  ? 12.212  18.899  26.428  1.00 51.34 ? 108 SER   B OG  1 
ATOM   3454 N  N   . ALA   B 1 75  ? 9.187   21.380  25.032  1.00 59.53 ? 109 ALA   B N   1 
ATOM   3455 C  CA  . ALA   B 1 75  ? 9.187   22.841  25.012  1.00 58.78 ? 109 ALA   B CA  1 
ATOM   3456 C  C   . ALA   B 1 75  ? 8.170   23.436  25.983  1.00 64.62 ? 109 ALA   B C   1 
ATOM   3457 O  O   . ALA   B 1 75  ? 8.357   24.565  26.453  1.00 64.22 ? 109 ALA   B O   1 
ATOM   3458 C  CB  . ALA   B 1 75  ? 8.926   23.341  23.593  1.00 56.32 ? 109 ALA   B CB  1 
ATOM   3459 N  N   . GLY   B 1 76  ? 7.097   22.703  26.295  1.00 69.04 ? 110 GLY   B N   1 
ATOM   3460 C  CA  . GLY   B 1 76  ? 6.072   23.188  27.206  1.00 64.47 ? 110 GLY   B CA  1 
ATOM   3461 C  C   . GLY   B 1 76  ? 6.294   22.770  28.645  1.00 58.22 ? 110 GLY   B C   1 
ATOM   3462 O  O   . GLY   B 1 76  ? 5.371   22.787  29.465  1.00 54.31 ? 110 GLY   B O   1 
ATOM   3463 N  N   . GLU   B 1 77  ? 7.520   22.382  28.966  1.00 64.64 ? 111 GLU   B N   1 
ATOM   3464 C  CA  . GLU   B 1 77  ? 7.881   22.018  30.323  1.00 71.41 ? 111 GLU   B CA  1 
ATOM   3465 C  C   . GLU   B 1 77  ? 8.977   22.949  30.821  1.00 72.89 ? 111 GLU   B C   1 
ATOM   3466 O  O   . GLU   B 1 77  ? 9.791   23.456  30.040  1.00 69.25 ? 111 GLU   B O   1 
ATOM   3467 C  CB  . GLU   B 1 77  ? 8.348   20.554  30.407  1.00 67.06 ? 111 GLU   B CB  1 
ATOM   3468 N  N   . ILE   B 1 78  ? 8.959   23.198  32.131  1.00 74.96 ? 112 ILE   B N   1 
ATOM   3469 C  CA  . ILE   B 1 78  ? 10.090  23.797  32.833  1.00 72.86 ? 112 ILE   B CA  1 
ATOM   3470 C  C   . ILE   B 1 78  ? 10.711  22.715  33.717  1.00 73.85 ? 112 ILE   B C   1 
ATOM   3471 O  O   . ILE   B 1 78  ? 10.410  21.524  33.559  1.00 72.21 ? 112 ILE   B O   1 
ATOM   3472 C  CB  . ILE   B 1 78  ? 9.670   25.040  33.646  1.00 68.15 ? 112 ILE   B CB  1 
ATOM   3473 C  CG1 . ILE   B 1 78  ? 8.364   24.785  34.415  1.00 68.17 ? 112 ILE   B CG1 1 
ATOM   3474 C  CG2 . ILE   B 1 78  ? 9.532   26.230  32.736  1.00 57.64 ? 112 ILE   B CG2 1 
ATOM   3475 C  CD1 . ILE   B 1 78  ? 8.070   25.806  35.500  1.00 64.24 ? 112 ILE   B CD1 1 
ATOM   3476 N  N   . LYS   B 1 79  ? 11.595  23.111  34.643  1.00 71.02 ? 113 LYS   B N   1 
ATOM   3477 C  CA  . LYS   B 1 79  ? 12.353  22.146  35.449  1.00 70.68 ? 113 LYS   B CA  1 
ATOM   3478 C  C   . LYS   B 1 79  ? 11.532  21.397  36.506  1.00 72.48 ? 113 LYS   B C   1 
ATOM   3479 O  O   . LYS   B 1 79  ? 11.868  20.248  36.838  1.00 71.82 ? 113 LYS   B O   1 
ATOM   3480 C  CB  . LYS   B 1 79  ? 13.528  22.845  36.135  1.00 59.84 ? 113 LYS   B CB  1 
ATOM   3481 C  CG  . LYS   B 1 79  ? 14.599  21.900  36.656  1.00 56.13 ? 113 LYS   B CG  1 
ATOM   3482 C  CD  . LYS   B 1 79  ? 15.877  22.087  35.863  1.00 63.09 ? 113 LYS   B CD  1 
ATOM   3483 C  CE  . LYS   B 1 79  ? 16.659  20.791  35.727  1.00 52.36 ? 113 LYS   B CE  1 
ATOM   3484 N  NZ  . LYS   B 1 79  ? 18.025  21.092  35.244  1.00 45.83 ? 113 LYS   B NZ  1 
ATOM   3485 N  N   . PRO   B 1 80  ? 10.484  22.000  37.100  1.00 75.23 ? 114 PRO   B N   1 
ATOM   3486 C  CA  . PRO   B 1 80  ? 9.658   21.230  38.048  1.00 77.17 ? 114 PRO   B CA  1 
ATOM   3487 C  C   . PRO   B 1 80  ? 8.539   20.452  37.367  1.00 80.30 ? 114 PRO   B C   1 
ATOM   3488 O  O   . PRO   B 1 80  ? 8.013   19.492  37.951  1.00 82.13 ? 114 PRO   B O   1 
ATOM   3489 C  CB  . PRO   B 1 80  ? 9.100   22.313  38.973  1.00 76.04 ? 114 PRO   B CB  1 
ATOM   3490 C  CG  . PRO   B 1 80  ? 8.984   23.497  38.039  1.00 71.12 ? 114 PRO   B CG  1 
ATOM   3491 C  CD  . PRO   B 1 80  ? 10.200  23.448  37.193  1.00 67.34 ? 114 PRO   B CD  1 
ATOM   3492 N  N   . THR   B 1 81  ? 8.167   20.858  36.140  1.00 75.09 ? 115 THR   B N   1 
ATOM   3493 C  CA  . THR   B 1 81  ? 7.127   20.190  35.356  1.00 76.52 ? 115 THR   B CA  1 
ATOM   3494 C  C   . THR   B 1 81  ? 7.689   19.144  34.388  1.00 72.31 ? 115 THR   B C   1 
ATOM   3495 O  O   . THR   B 1 81  ? 6.928   18.585  33.585  1.00 68.38 ? 115 THR   B O   1 
ATOM   3496 C  CB  . THR   B 1 81  ? 6.274   21.219  34.577  1.00 74.06 ? 115 THR   B CB  1 
ATOM   3497 O  OG1 . THR   B 1 81  ? 6.985   21.713  33.430  1.00 69.22 ? 115 THR   B OG1 1 
ATOM   3498 C  CG2 . THR   B 1 81  ? 5.875   22.389  35.467  1.00 67.43 ? 115 THR   B CG2 1 
ATOM   3499 N  N   . THR   B 1 82  ? 8.986   18.846  34.470  1.00 72.07 ? 116 THR   B N   1 
ATOM   3500 C  CA  . THR   B 1 82  ? 9.643   18.022  33.464  1.00 60.42 ? 116 THR   B CA  1 
ATOM   3501 C  C   . THR   B 1 82  ? 9.147   16.586  33.515  1.00 57.75 ? 116 THR   B C   1 
ATOM   3502 O  O   . THR   B 1 82  ? 8.781   16.059  34.573  1.00 57.53 ? 116 THR   B O   1 
ATOM   3503 C  CB  . THR   B 1 82  ? 11.162  18.038  33.646  1.00 54.56 ? 116 THR   B CB  1 
ATOM   3504 O  OG1 . THR   B 1 82  ? 11.778  17.423  32.511  1.00 49.18 ? 116 THR   B OG1 1 
ATOM   3505 C  CG2 . THR   B 1 82  ? 11.583  17.290  34.915  1.00 44.26 ? 116 THR   B CG2 1 
ATOM   3506 N  N   . THR   B 1 83  ? 9.132   15.957  32.343  1.00 55.59 ? 117 THR   B N   1 
ATOM   3507 C  CA  . THR   B 1 83  ? 8.860   14.531  32.233  1.00 47.98 ? 117 THR   B CA  1 
ATOM   3508 C  C   . THR   B 1 83  ? 10.104  13.680  32.454  1.00 38.91 ? 117 THR   B C   1 
ATOM   3509 O  O   . THR   B 1 83  ? 10.011  12.453  32.393  1.00 39.98 ? 117 THR   B O   1 
ATOM   3510 C  CB  . THR   B 1 83  ? 8.249   14.218  30.861  1.00 47.23 ? 117 THR   B CB  1 
ATOM   3511 O  OG1 . THR   B 1 83  ? 9.074   14.782  29.826  1.00 43.43 ? 117 THR   B OG1 1 
ATOM   3512 C  CG2 . THR   B 1 83  ? 6.821   14.798  30.770  1.00 40.38 ? 117 THR   B CG2 1 
ATOM   3513 N  N   . ALA   B 1 84  ? 11.252  14.299  32.729  1.00 34.65 ? 118 ALA   B N   1 
ATOM   3514 C  CA  . ALA   B 1 84  ? 12.506  13.567  32.832  1.00 35.66 ? 118 ALA   B CA  1 
ATOM   3515 C  C   . ALA   B 1 84  ? 12.570  12.747  34.112  1.00 40.03 ? 118 ALA   B C   1 
ATOM   3516 O  O   . ALA   B 1 84  ? 12.232  13.226  35.199  1.00 42.99 ? 118 ALA   B O   1 
ATOM   3517 C  CB  . ALA   B 1 84  ? 13.692  14.524  32.786  1.00 36.94 ? 118 ALA   B CB  1 
ATOM   3518 N  N   . SER   B 1 85  ? 13.028  11.504  33.980  1.00 35.32 ? 119 SER   B N   1 
ATOM   3519 C  CA  . SER   B 1 85  ? 13.116  10.638  35.143  1.00 38.51 ? 119 SER   B CA  1 
ATOM   3520 C  C   . SER   B 1 85  ? 14.366  10.899  35.962  1.00 38.57 ? 119 SER   B C   1 
ATOM   3521 O  O   . SER   B 1 85  ? 14.413  10.513  37.135  1.00 39.17 ? 119 SER   B O   1 
ATOM   3522 C  CB  . SER   B 1 85  ? 13.075  9.171   34.716  1.00 39.47 ? 119 SER   B CB  1 
ATOM   3523 O  OG  . SER   B 1 85  ? 13.857  8.964   33.557  1.00 40.25 ? 119 SER   B OG  1 
ATOM   3524 N  N   . ILE   B 1 86  ? 15.378  11.526  35.374  1.00 33.49 ? 120 ILE   B N   1 
ATOM   3525 C  CA  . ILE   B 1 86  ? 16.570  11.894  36.126  1.00 35.42 ? 120 ILE   B CA  1 
ATOM   3526 C  C   . ILE   B 1 86  ? 16.659  13.409  36.132  1.00 38.73 ? 120 ILE   B C   1 
ATOM   3527 O  O   . ILE   B 1 86  ? 17.275  13.997  35.229  1.00 37.48 ? 120 ILE   B O   1 
ATOM   3528 C  CB  . ILE   B 1 86  ? 17.844  11.291  35.535  1.00 35.11 ? 120 ILE   B CB  1 
ATOM   3529 C  CG1 . ILE   B 1 86  ? 17.708  9.782   35.398  1.00 28.78 ? 120 ILE   B CG1 1 
ATOM   3530 C  CG2 . ILE   B 1 86  ? 19.046  11.675  36.415  1.00 31.64 ? 120 ILE   B CG2 1 
ATOM   3531 C  CD1 . ILE   B 1 86  ? 18.883  9.158   34.695  1.00 26.90 ? 120 ILE   B CD1 1 
ATOM   3532 N  N   . PRO   B 1 87  ? 16.091  14.074  37.140  1.00 40.24 ? 121 PRO   B N   1 
ATOM   3533 C  CA  . PRO   B 1 87  ? 15.806  15.506  37.010  1.00 34.78 ? 121 PRO   B CA  1 
ATOM   3534 C  C   . PRO   B 1 87  ? 17.027  16.412  37.105  1.00 37.19 ? 121 PRO   B C   1 
ATOM   3535 O  O   . PRO   B 1 87  ? 16.892  17.614  36.829  1.00 41.97 ? 121 PRO   B O   1 
ATOM   3536 C  CB  . PRO   B 1 87  ? 14.814  15.754  38.151  1.00 34.32 ? 121 PRO   B CB  1 
ATOM   3537 C  CG  . PRO   B 1 87  ? 15.172  14.751  39.164  1.00 34.03 ? 121 PRO   B CG  1 
ATOM   3538 C  CD  . PRO   B 1 87  ? 15.611  13.527  38.418  1.00 35.52 ? 121 PRO   B CD  1 
ATOM   3539 N  N   . SER   B 1 88  ? 18.216  15.900  37.447  1.00 35.58 ? 122 SER   B N   1 
ATOM   3540 C  CA  . SER   B 1 88  ? 19.405  16.746  37.307  1.00 34.02 ? 122 SER   B CA  1 
ATOM   3541 C  C   . SER   B 1 88  ? 19.836  16.919  35.855  1.00 38.15 ? 122 SER   B C   1 
ATOM   3542 O  O   . SER   B 1 88  ? 20.797  17.650  35.580  1.00 32.15 ? 122 SER   B O   1 
ATOM   3543 C  CB  . SER   B 1 88  ? 20.570  16.180  38.111  1.00 30.29 ? 122 SER   B CB  1 
ATOM   3544 O  OG  . SER   B 1 88  ? 21.274  15.231  37.354  1.00 34.17 ? 122 SER   B OG  1 
ATOM   3545 N  N   . PHE   B 1 89  ? 19.161  16.258  34.921  1.00 40.60 ? 123 PHE   B N   1 
ATOM   3546 C  CA  . PHE   B 1 89  ? 19.526  16.376  33.523  1.00 41.14 ? 123 PHE   B CA  1 
ATOM   3547 C  C   . PHE   B 1 89  ? 19.247  17.804  33.021  1.00 45.27 ? 123 PHE   B C   1 
ATOM   3548 O  O   . PHE   B 1 89  ? 18.516  18.581  33.647  1.00 40.64 ? 123 PHE   B O   1 
ATOM   3549 C  CB  . PHE   B 1 89  ? 18.786  15.311  32.700  1.00 32.81 ? 123 PHE   B CB  1 
ATOM   3550 C  CG  . PHE   B 1 89  ? 19.235  15.241  31.280  1.00 30.55 ? 123 PHE   B CG  1 
ATOM   3551 C  CD1 . PHE   B 1 89  ? 20.526  14.847  30.977  1.00 28.89 ? 123 PHE   B CD1 1 
ATOM   3552 C  CD2 . PHE   B 1 89  ? 18.375  15.601  30.243  1.00 33.16 ? 123 PHE   B CD2 1 
ATOM   3553 C  CE1 . PHE   B 1 89  ? 20.960  14.809  29.661  1.00 35.94 ? 123 PHE   B CE1 1 
ATOM   3554 C  CE2 . PHE   B 1 89  ? 18.798  15.562  28.921  1.00 30.15 ? 123 PHE   B CE2 1 
ATOM   3555 C  CZ  . PHE   B 1 89  ? 20.095  15.172  28.626  1.00 29.44 ? 123 PHE   B CZ  1 
ATOM   3556 N  N   . ASP   B 1 90  ? 19.879  18.151  31.889  1.00 37.74 ? 124 ASP   B N   1 
ATOM   3557 C  CA  . ASP   B 1 90  ? 19.782  19.467  31.266  1.00 36.33 ? 124 ASP   B CA  1 
ATOM   3558 C  C   . ASP   B 1 90  ? 20.323  19.419  29.833  1.00 35.72 ? 124 ASP   B C   1 
ATOM   3559 O  O   . ASP   B 1 90  ? 21.505  19.105  29.639  1.00 31.17 ? 124 ASP   B O   1 
ATOM   3560 C  CB  . ASP   B 1 90  ? 20.553  20.508  32.098  1.00 38.35 ? 124 ASP   B CB  1 
ATOM   3561 C  CG  . ASP   B 1 90  ? 20.430  21.930  31.536  1.00 40.75 ? 124 ASP   B CG  1 
ATOM   3562 O  OD1 . ASP   B 1 90  ? 21.264  22.342  30.695  1.00 37.04 ? 124 ASP   B OD1 1 
ATOM   3563 O  OD2 . ASP   B 1 90  ? 19.491  22.644  31.940  1.00 48.28 ? 124 ASP   B OD2 1 
ATOM   3564 N  N   . HIS   B 1 91  ? 19.477  19.743  28.835  1.00 33.83 ? 125 HIS   B N   1 
ATOM   3565 C  CA  . HIS   B 1 91  ? 19.890  19.713  27.425  1.00 33.40 ? 125 HIS   B CA  1 
ATOM   3566 C  C   . HIS   B 1 91  ? 21.230  20.425  27.204  1.00 39.29 ? 125 HIS   B C   1 
ATOM   3567 O  O   . HIS   B 1 91  ? 22.173  19.835  26.657  1.00 36.24 ? 125 HIS   B O   1 
ATOM   3568 C  CB  . HIS   B 1 91  ? 18.811  20.343  26.531  1.00 34.36 ? 125 HIS   B CB  1 
ATOM   3569 C  CG  . HIS   B 1 91  ? 17.579  19.505  26.342  1.00 39.77 ? 125 HIS   B CG  1 
ATOM   3570 N  ND1 . HIS   B 1 91  ? 17.457  18.572  25.331  1.00 43.65 ? 125 HIS   B ND1 1 
ATOM   3571 C  CD2 . HIS   B 1 91  ? 16.392  19.499  26.997  1.00 41.61 ? 125 HIS   B CD2 1 
ATOM   3572 C  CE1 . HIS   B 1 91  ? 16.267  17.998  25.397  1.00 41.01 ? 125 HIS   B CE1 1 
ATOM   3573 N  NE2 . HIS   B 1 91  ? 15.598  18.547  26.397  1.00 45.38 ? 125 HIS   B NE2 1 
ATOM   3574 N  N   . GLY   B 1 92  ? 21.336  21.693  27.634  1.00 29.57 ? 126 GLY   B N   1 
ATOM   3575 C  CA  . GLY   B 1 92  ? 22.523  22.481  27.324  1.00 26.75 ? 126 GLY   B CA  1 
ATOM   3576 C  C   . GLY   B 1 92  ? 23.795  21.956  27.970  1.00 32.30 ? 126 GLY   B C   1 
ATOM   3577 O  O   . GLY   B 1 92  ? 24.862  21.945  27.348  1.00 30.13 ? 126 GLY   B O   1 
ATOM   3578 N  N   . SER   B 1 93  ? 23.707  21.530  29.232  1.00 35.31 ? 127 SER   B N   1 
ATOM   3579 C  CA  . SER   B 1 93  ? 24.844  20.870  29.870  1.00 39.42 ? 127 SER   B CA  1 
ATOM   3580 C  C   . SER   B 1 93  ? 25.273  19.645  29.071  1.00 42.95 ? 127 SER   B C   1 
ATOM   3581 O  O   . SER   B 1 93  ? 26.456  19.479  28.736  1.00 40.21 ? 127 SER   B O   1 
ATOM   3582 C  CB  . SER   B 1 93  ? 24.486  20.455  31.299  1.00 33.12 ? 127 SER   B CB  1 
ATOM   3583 O  OG  . SER   B 1 93  ? 23.921  21.523  32.027  1.00 41.75 ? 127 SER   B OG  1 
ATOM   3584 N  N   . CYS   B 1 94  ? 24.307  18.779  28.748  1.00 38.25 ? 128 CYS   B N   1 
ATOM   3585 C  CA  . CYS   B 1 94  ? 24.607  17.513  28.092  1.00 38.28 ? 128 CYS   B CA  1 
ATOM   3586 C  C   . CYS   B 1 94  ? 25.264  17.734  26.732  1.00 36.13 ? 128 CYS   B C   1 
ATOM   3587 O  O   . CYS   B 1 94  ? 26.322  17.162  26.446  1.00 37.62 ? 128 CYS   B O   1 
ATOM   3588 C  CB  . CYS   B 1 94  ? 23.324  16.688  27.973  1.00 36.96 ? 128 CYS   B CB  1 
ATOM   3589 S  SG  . CYS   B 1 94  ? 23.530  15.071  27.248  1.00 32.85 ? 128 CYS   B SG  1 
ATOM   3590 N  N   . ARG   B 1 95  ? 24.666  18.581  25.888  1.00 37.92 ? 129 ARG   B N   1 
ATOM   3591 C  CA  . ARG   B 1 95  ? 25.273  18.869  24.592  1.00 30.28 ? 129 ARG   B CA  1 
ATOM   3592 C  C   . ARG   B 1 95  ? 26.632  19.543  24.757  1.00 31.70 ? 129 ARG   B C   1 
ATOM   3593 O  O   . ARG   B 1 95  ? 27.571  19.260  24.003  1.00 26.61 ? 129 ARG   B O   1 
ATOM   3594 C  CB  . ARG   B 1 95  ? 24.323  19.726  23.768  1.00 29.10 ? 129 ARG   B CB  1 
ATOM   3595 C  CG  . ARG   B 1 95  ? 22.977  19.076  23.552  1.00 35.22 ? 129 ARG   B CG  1 
ATOM   3596 C  CD  . ARG   B 1 95  ? 22.092  19.876  22.602  1.00 44.90 ? 129 ARG   B CD  1 
ATOM   3597 N  NE  . ARG   B 1 95  ? 21.299  18.996  21.740  1.00 52.93 ? 129 ARG   B NE  1 
ATOM   3598 C  CZ  . ARG   B 1 95  ? 20.010  18.720  21.922  1.00 50.61 ? 129 ARG   B CZ  1 
ATOM   3599 N  NH1 . ARG   B 1 95  ? 19.347  19.269  22.938  1.00 48.88 ? 129 ARG   B NH1 1 
ATOM   3600 N  NH2 . ARG   B 1 95  ? 19.386  17.900  21.079  1.00 43.67 ? 129 ARG   B NH2 1 
ATOM   3601 N  N   . SER   B 1 96  ? 26.756  20.432  25.748  1.00 34.12 ? 130 SER   B N   1 
ATOM   3602 C  CA  . SER   B 1 96  ? 28.042  21.055  26.051  1.00 34.79 ? 130 SER   B CA  1 
ATOM   3603 C  C   . SER   B 1 96  ? 29.085  20.008  26.434  1.00 34.47 ? 130 SER   B C   1 
ATOM   3604 O  O   . SER   B 1 96  ? 30.183  19.960  25.860  1.00 33.61 ? 130 SER   B O   1 
ATOM   3605 C  CB  . SER   B 1 96  ? 27.859  22.072  27.181  1.00 37.02 ? 130 SER   B CB  1 
ATOM   3606 O  OG  . SER   B 1 96  ? 29.067  22.744  27.507  1.00 51.98 ? 130 SER   B OG  1 
ATOM   3607 N  N   . PHE   B 1 97  ? 28.749  19.166  27.417  1.00 37.49 ? 131 PHE   B N   1 
ATOM   3608 C  CA  . PHE   B 1 97  ? 29.616  18.075  27.854  1.00 33.80 ? 131 PHE   B CA  1 
ATOM   3609 C  C   . PHE   B 1 97  ? 30.093  17.250  26.672  1.00 30.07 ? 131 PHE   B C   1 
ATOM   3610 O  O   . PHE   B 1 97  ? 31.297  17.027  26.498  1.00 28.77 ? 131 PHE   B O   1 
ATOM   3611 C  CB  . PHE   B 1 97  ? 28.851  17.201  28.853  1.00 32.72 ? 131 PHE   B CB  1 
ATOM   3612 C  CG  . PHE   B 1 97  ? 29.642  16.047  29.418  1.00 33.34 ? 131 PHE   B CG  1 
ATOM   3613 C  CD1 . PHE   B 1 97  ? 29.704  14.821  28.744  1.00 30.66 ? 131 PHE   B CD1 1 
ATOM   3614 C  CD2 . PHE   B 1 97  ? 30.279  16.166  30.654  1.00 27.23 ? 131 PHE   B CD2 1 
ATOM   3615 C  CE1 . PHE   B 1 97  ? 30.425  13.742  29.274  1.00 27.74 ? 131 PHE   B CE1 1 
ATOM   3616 C  CE2 . PHE   B 1 97  ? 30.993  15.096  31.200  1.00 31.08 ? 131 PHE   B CE2 1 
ATOM   3617 C  CZ  . PHE   B 1 97  ? 31.068  13.870  30.505  1.00 27.99 ? 131 PHE   B CZ  1 
ATOM   3618 N  N   . PHE   B 1 98  ? 29.152  16.814  25.829  1.00 30.98 ? 132 PHE   B N   1 
ATOM   3619 C  CA  . PHE   B 1 98  ? 29.506  15.941  24.718  1.00 26.64 ? 132 PHE   B CA  1 
ATOM   3620 C  C   . PHE   B 1 98  ? 30.319  16.663  23.657  1.00 28.83 ? 132 PHE   B C   1 
ATOM   3621 O  O   . PHE   B 1 98  ? 31.283  16.099  23.127  1.00 31.88 ? 132 PHE   B O   1 
ATOM   3622 C  CB  . PHE   B 1 98  ? 28.266  15.337  24.087  1.00 23.97 ? 132 PHE   B CB  1 
ATOM   3623 C  CG  . PHE   B 1 98  ? 28.559  14.070  23.324  1.00 29.31 ? 132 PHE   B CG  1 
ATOM   3624 C  CD1 . PHE   B 1 98  ? 28.733  12.873  24.002  1.00 20.56 ? 132 PHE   B CD1 1 
ATOM   3625 C  CD2 . PHE   B 1 98  ? 28.706  14.087  21.938  1.00 25.02 ? 132 PHE   B CD2 1 
ATOM   3626 C  CE1 . PHE   B 1 98  ? 29.008  11.701  23.320  1.00 25.51 ? 132 PHE   B CE1 1 
ATOM   3627 C  CE2 . PHE   B 1 98  ? 28.989  12.930  21.248  1.00 32.01 ? 132 PHE   B CE2 1 
ATOM   3628 C  CZ  . PHE   B 1 98  ? 29.139  11.720  21.939  1.00 30.14 ? 132 PHE   B CZ  1 
ATOM   3629 N  N   . SER   B 1 99  ? 29.940  17.899  23.318  1.00 28.95 ? 133 SER   B N   1 
ATOM   3630 C  CA  . SER   B 1 99  ? 30.696  18.645  22.320  1.00 30.07 ? 133 SER   B CA  1 
ATOM   3631 C  C   . SER   B 1 99  ? 32.113  18.932  22.785  1.00 28.97 ? 133 SER   B C   1 
ATOM   3632 O  O   . SER   B 1 99  ? 33.038  18.963  21.967  1.00 27.44 ? 133 SER   B O   1 
ATOM   3633 C  CB  . SER   B 1 99  ? 29.968  19.931  21.980  1.00 28.69 ? 133 SER   B CB  1 
ATOM   3634 O  OG  . SER   B 1 99  ? 28.645  19.618  21.597  1.00 32.89 ? 133 SER   B OG  1 
ATOM   3635 N  N   . SER   B 1 100 ? 32.304  19.113  24.088  1.00 29.90 ? 134 SER   B N   1 
ATOM   3636 C  CA  . SER   B 1 100 ? 33.639  19.368  24.609  1.00 33.39 ? 134 SER   B CA  1 
ATOM   3637 C  C   . SER   B 1 100 ? 34.466  18.080  24.741  1.00 32.48 ? 134 SER   B C   1 
ATOM   3638 O  O   . SER   B 1 100 ? 35.612  18.027  24.275  1.00 33.64 ? 134 SER   B O   1 
ATOM   3639 C  CB  . SER   B 1 100 ? 33.532  20.099  25.953  1.00 33.06 ? 134 SER   B CB  1 
ATOM   3640 O  OG  . SER   B 1 100 ? 34.807  20.289  26.556  1.00 33.58 ? 134 SER   B OG  1 
ATOM   3641 N  N   . HIS   B 1 101 ? 33.907  17.027  25.362  1.00 30.02 ? 135 HIS   B N   1 
ATOM   3642 C  CA  . HIS   B 1 101 ? 34.703  15.875  25.790  1.00 27.33 ? 135 HIS   B CA  1 
ATOM   3643 C  C   . HIS   B 1 101 ? 34.529  14.615  24.949  1.00 30.48 ? 135 HIS   B C   1 
ATOM   3644 O  O   . HIS   B 1 101 ? 35.384  13.727  25.028  1.00 31.02 ? 135 HIS   B O   1 
ATOM   3645 C  CB  . HIS   B 1 101 ? 34.390  15.508  27.250  1.00 23.77 ? 135 HIS   B CB  1 
ATOM   3646 C  CG  . HIS   B 1 101 ? 34.422  16.668  28.196  1.00 27.19 ? 135 HIS   B CG  1 
ATOM   3647 N  ND1 . HIS   B 1 101 ? 35.580  17.359  28.494  1.00 27.09 ? 135 HIS   B ND1 1 
ATOM   3648 C  CD2 . HIS   B 1 101 ? 33.440  17.251  28.924  1.00 25.74 ? 135 HIS   B CD2 1 
ATOM   3649 C  CE1 . HIS   B 1 101 ? 35.308  18.322  29.357  1.00 27.98 ? 135 HIS   B CE1 1 
ATOM   3650 N  NE2 . HIS   B 1 101 ? 34.016  18.280  29.631  1.00 30.77 ? 135 HIS   B NE2 1 
ATOM   3651 N  N   . GLY   B 1 102 ? 33.463  14.501  24.158  1.00 34.14 ? 136 GLY   B N   1 
ATOM   3652 C  CA  . GLY   B 1 102 ? 33.168  13.255  23.453  1.00 27.30 ? 136 GLY   B CA  1 
ATOM   3653 C  C   . GLY   B 1 102 ? 32.330  12.327  24.316  1.00 29.00 ? 136 GLY   B C   1 
ATOM   3654 O  O   . GLY   B 1 102 ? 31.676  12.751  25.270  1.00 33.35 ? 136 GLY   B O   1 
ATOM   3655 N  N   . LEU   B 1 103 ? 32.353  11.040  23.982  1.00 29.75 ? 137 LEU   B N   1 
ATOM   3656 C  CA  . LEU   B 1 103 ? 31.647  10.056  24.802  1.00 23.68 ? 137 LEU   B CA  1 
ATOM   3657 C  C   . LEU   B 1 103 ? 32.438  9.777   26.074  1.00 22.62 ? 137 LEU   B C   1 
ATOM   3658 O  O   . LEU   B 1 103 ? 33.658  9.589   26.032  1.00 22.88 ? 137 LEU   B O   1 
ATOM   3659 C  CB  . LEU   B 1 103 ? 31.428  8.773   24.009  1.00 22.99 ? 137 LEU   B CB  1 
ATOM   3660 C  CG  . LEU   B 1 103 ? 31.150  7.498   24.784  1.00 26.29 ? 137 LEU   B CG  1 
ATOM   3661 C  CD1 . LEU   B 1 103 ? 29.657  7.356   25.141  1.00 23.53 ? 137 LEU   B CD1 1 
ATOM   3662 C  CD2 . LEU   B 1 103 ? 31.650  6.357   23.947  1.00 25.78 ? 137 LEU   B CD2 1 
ATOM   3663 N  N   . GLY   B 1 104 ? 31.751  9.771   27.211  1.00 22.17 ? 138 GLY   B N   1 
ATOM   3664 C  CA  . GLY   B 1 104 ? 32.454  9.596   28.468  1.00 20.67 ? 138 GLY   B CA  1 
ATOM   3665 C  C   . GLY   B 1 104 ? 31.506  9.613   29.650  1.00 24.74 ? 138 GLY   B C   1 
ATOM   3666 O  O   . GLY   B 1 104 ? 30.276  9.706   29.508  1.00 21.68 ? 138 GLY   B O   1 
ATOM   3667 N  N   . VAL   B 1 105 ? 32.110  9.521   30.828  1.00 20.70 ? 139 VAL   B N   1 
ATOM   3668 C  CA  . VAL   B 1 105 ? 31.373  9.421   32.076  1.00 24.01 ? 139 VAL   B CA  1 
ATOM   3669 C  C   . VAL   B 1 105 ? 31.058  10.808  32.624  1.00 29.86 ? 139 VAL   B C   1 
ATOM   3670 O  O   . VAL   B 1 105 ? 31.955  11.641  32.834  1.00 24.45 ? 139 VAL   B O   1 
ATOM   3671 C  CB  . VAL   B 1 105 ? 32.156  8.595   33.099  1.00 27.15 ? 139 VAL   B CB  1 
ATOM   3672 C  CG1 . VAL   B 1 105 ? 31.538  8.740   34.484  1.00 22.04 ? 139 VAL   B CG1 1 
ATOM   3673 C  CG2 . VAL   B 1 105 ? 32.163  7.150   32.637  1.00 27.57 ? 139 VAL   B CG2 1 
ATOM   3674 N  N   . ARG   B 1 106 ? 29.770  11.046  32.856  1.00 28.95 ? 140 ARG   B N   1 
ATOM   3675 C  CA  . ARG   B 1 106 ? 29.277  12.239  33.519  1.00 29.30 ? 140 ARG   B CA  1 
ATOM   3676 C  C   . ARG   B 1 106 ? 29.092  12.042  35.018  1.00 33.23 ? 140 ARG   B C   1 
ATOM   3677 O  O   . ARG   B 1 106 ? 29.291  12.992  35.785  1.00 32.96 ? 140 ARG   B O   1 
ATOM   3678 C  CB  . ARG   B 1 106 ? 27.949  12.675  32.875  1.00 29.27 ? 140 ARG   B CB  1 
ATOM   3679 C  CG  . ARG   B 1 106 ? 27.096  13.675  33.662  1.00 30.98 ? 140 ARG   B CG  1 
ATOM   3680 C  CD  . ARG   B 1 106 ? 27.750  15.043  33.832  1.00 28.98 ? 140 ARG   B CD  1 
ATOM   3681 N  NE  . ARG   B 1 106 ? 26.819  15.967  34.474  1.00 35.94 ? 140 ARG   B NE  1 
ATOM   3682 C  CZ  . ARG   B 1 106 ? 27.076  17.244  34.761  1.00 37.74 ? 140 ARG   B CZ  1 
ATOM   3683 N  NH1 . ARG   B 1 106 ? 28.255  17.790  34.478  1.00 29.21 ? 140 ARG   B NH1 1 
ATOM   3684 N  NH2 . ARG   B 1 106 ? 26.137  17.981  35.335  1.00 35.42 ? 140 ARG   B NH2 1 
ATOM   3685 N  N   . ALA   B 1 107 ? 28.762  10.834  35.467  1.00 25.28 ? 141 ALA   B N   1 
ATOM   3686 C  CA  . ALA   B 1 107 ? 28.350  10.655  36.846  1.00 22.90 ? 141 ALA   B CA  1 
ATOM   3687 C  C   . ALA   B 1 107 ? 28.971  9.397   37.426  1.00 26.99 ? 141 ALA   B C   1 
ATOM   3688 O  O   . ALA   B 1 107 ? 28.695  8.293   36.949  1.00 33.69 ? 141 ALA   B O   1 
ATOM   3689 C  CB  . ALA   B 1 107 ? 26.832  10.592  36.928  1.00 18.67 ? 141 ALA   B CB  1 
ATOM   3690 N  N   . VAL   B 1 108 ? 29.797  9.551   38.454  1.00 24.07 ? 142 VAL   B N   1 
ATOM   3691 C  CA  . VAL   B 1 108 ? 30.159  8.432   39.321  1.00 28.09 ? 142 VAL   B CA  1 
ATOM   3692 C  C   . VAL   B 1 108 ? 29.194  8.442   40.507  1.00 24.63 ? 142 VAL   B C   1 
ATOM   3693 O  O   . VAL   B 1 108 ? 29.193  9.374   41.309  1.00 31.75 ? 142 VAL   B O   1 
ATOM   3694 C  CB  . VAL   B 1 108 ? 31.619  8.520   39.777  1.00 33.42 ? 142 VAL   B CB  1 
ATOM   3695 C  CG1 . VAL   B 1 108 ? 31.991  7.305   40.646  1.00 24.94 ? 142 VAL   B CG1 1 
ATOM   3696 C  CG2 . VAL   B 1 108 ? 32.566  8.692   38.564  1.00 21.71 ? 142 VAL   B CG2 1 
ATOM   3697 N  N   . ALA   B 1 109 ? 28.355  7.422   40.609  1.00 29.13 ? 143 ALA   B N   1 
ATOM   3698 C  CA  . ALA   B 1 109 ? 27.228  7.404   41.545  1.00 35.63 ? 143 ALA   B CA  1 
ATOM   3699 C  C   . ALA   B 1 109 ? 27.494  6.413   42.671  1.00 33.14 ? 143 ALA   B C   1 
ATOM   3700 O  O   . ALA   B 1 109 ? 27.688  5.216   42.423  1.00 31.93 ? 143 ALA   B O   1 
ATOM   3701 C  CB  . ALA   B 1 109 ? 25.914  7.042   40.845  1.00 30.22 ? 143 ALA   B CB  1 
ATOM   3702 N  N   . ILE   B 1 110 ? 27.456  6.902   43.906  1.00 36.00 ? 144 ILE   B N   1 
ATOM   3703 C  CA  . ILE   B 1 110 ? 27.659  6.067   45.080  1.00 38.70 ? 144 ILE   B CA  1 
ATOM   3704 C  C   . ILE   B 1 110 ? 26.378  6.033   45.901  1.00 39.13 ? 144 ILE   B C   1 
ATOM   3705 O  O   . ILE   B 1 110 ? 25.658  7.034   46.009  1.00 32.75 ? 144 ILE   B O   1 
ATOM   3706 C  CB  . ILE   B 1 110 ? 28.845  6.566   45.927  1.00 43.66 ? 144 ILE   B CB  1 
ATOM   3707 C  CG1 . ILE   B 1 110 ? 28.644  8.030   46.307  1.00 36.70 ? 144 ILE   B CG1 1 
ATOM   3708 C  CG2 . ILE   B 1 110 ? 30.163  6.381   45.163  1.00 36.59 ? 144 ILE   B CG2 1 
ATOM   3709 C  CD1 . ILE   B 1 110 ? 29.553  8.457   47.415  1.00 40.32 ? 144 ILE   B CD1 1 
ATOM   3710 N  N   . GLU   B 1 111 ? 26.096  4.859   46.463  1.00 47.80 ? 145 GLU   B N   1 
ATOM   3711 C  CA  . GLU   B 1 111 ? 24.993  4.681   47.398  1.00 46.06 ? 145 GLU   B CA  1 
ATOM   3712 C  C   . GLU   B 1 111 ? 25.427  5.132   48.790  1.00 39.73 ? 145 GLU   B C   1 
ATOM   3713 O  O   . GLU   B 1 111 ? 26.514  4.791   49.265  1.00 36.84 ? 145 GLU   B O   1 
ATOM   3714 C  CB  . GLU   B 1 111 ? 24.542  3.218   47.413  1.00 45.64 ? 145 GLU   B CB  1 
ATOM   3715 C  CG  . GLU   B 1 111 ? 23.182  2.978   48.057  1.00 46.12 ? 145 GLU   B CG  1 
ATOM   3716 C  CD  . GLU   B 1 111 ? 22.861  1.494   48.211  1.00 61.69 ? 145 GLU   B CD  1 
ATOM   3717 O  OE1 . GLU   B 1 111 ? 23.706  0.645   47.834  1.00 64.42 ? 145 GLU   B OE1 1 
ATOM   3718 O  OE2 . GLU   B 1 111 ? 21.760  1.175   48.715  1.00 65.13 ? 145 GLU   B OE2 1 
ATOM   3719 N  N   . VAL   B 1 112 ? 24.584  5.930   49.428  1.00 42.22 ? 146 VAL   B N   1 
ATOM   3720 C  CA  . VAL   B 1 112 ? 24.878  6.511   50.727  1.00 43.17 ? 146 VAL   B CA  1 
ATOM   3721 C  C   . VAL   B 1 112 ? 23.641  6.315   51.591  1.00 48.41 ? 146 VAL   B C   1 
ATOM   3722 O  O   . VAL   B 1 112 ? 22.545  6.037   51.093  1.00 45.40 ? 146 VAL   B O   1 
ATOM   3723 C  CB  . VAL   B 1 112 ? 25.263  8.010   50.630  1.00 35.18 ? 146 VAL   B CB  1 
ATOM   3724 C  CG1 . VAL   B 1 112 ? 26.497  8.186   49.752  1.00 36.33 ? 146 VAL   B CG1 1 
ATOM   3725 C  CG2 . VAL   B 1 112 ? 24.099  8.831   50.100  1.00 33.71 ? 146 VAL   B CG2 1 
ATOM   3726 N  N   . GLU   B 1 113 ? 23.826  6.452   52.905  1.00 40.77 ? 147 GLU   B N   1 
ATOM   3727 C  CA  . GLU   B 1 113 ? 22.685  6.275   53.788  1.00 43.14 ? 147 GLU   B CA  1 
ATOM   3728 C  C   . GLU   B 1 113 ? 21.662  7.390   53.595  1.00 43.56 ? 147 GLU   B C   1 
ATOM   3729 O  O   . GLU   B 1 113 ? 20.453  7.129   53.583  1.00 47.35 ? 147 GLU   B O   1 
ATOM   3730 C  CB  . GLU   B 1 113 ? 23.149  6.179   55.244  1.00 51.04 ? 147 GLU   B CB  1 
ATOM   3731 C  CG  . GLU   B 1 113 ? 22.027  5.842   56.236  1.00 54.62 ? 147 GLU   B CG  1 
ATOM   3732 C  CD  . GLU   B 1 113 ? 21.276  4.541   55.933  1.00 56.92 ? 147 GLU   B CD  1 
ATOM   3733 O  OE1 . GLU   B 1 113 ? 21.824  3.630   55.261  1.00 52.83 ? 147 GLU   B OE1 1 
ATOM   3734 O  OE2 . GLU   B 1 113 ? 20.110  4.443   56.372  1.00 58.43 ? 147 GLU   B OE2 1 
ATOM   3735 N  N   . ASP   B 1 114 ? 22.119  8.632   53.418  1.00 48.01 ? 148 ASP   B N   1 
ATOM   3736 C  CA  . ASP   B 1 114 ? 21.216  9.757   53.167  1.00 55.09 ? 148 ASP   B CA  1 
ATOM   3737 C  C   . ASP   B 1 114 ? 21.850  10.726  52.176  1.00 50.73 ? 148 ASP   B C   1 
ATOM   3738 O  O   . ASP   B 1 114 ? 22.918  11.285  52.448  1.00 49.05 ? 148 ASP   B O   1 
ATOM   3739 C  CB  . ASP   B 1 114 ? 20.847  10.494  54.465  1.00 49.74 ? 148 ASP   B CB  1 
ATOM   3740 C  CG  . ASP   B 1 114 ? 19.753  11.540  54.254  1.00 50.57 ? 148 ASP   B CG  1 
ATOM   3741 O  OD1 . ASP   B 1 114 ? 19.799  12.602  54.923  1.00 49.01 ? 148 ASP   B OD1 1 
ATOM   3742 O  OD2 . ASP   B 1 114 ? 18.842  11.292  53.424  1.00 50.36 ? 148 ASP   B OD2 1 
ATOM   3743 N  N   . ALA   B 1 115 ? 21.159  10.953  51.049  1.00 47.30 ? 149 ALA   B N   1 
ATOM   3744 C  CA  . ALA   B 1 115 ? 21.671  11.835  50.002  1.00 49.43 ? 149 ALA   B CA  1 
ATOM   3745 C  C   . ALA   B 1 115 ? 21.566  13.303  50.401  1.00 46.26 ? 149 ALA   B C   1 
ATOM   3746 O  O   . ALA   B 1 115 ? 22.510  14.074  50.199  1.00 45.67 ? 149 ALA   B O   1 
ATOM   3747 C  CB  . ALA   B 1 115 ? 20.919  11.581  48.693  1.00 45.89 ? 149 ALA   B CB  1 
ATOM   3748 N  N   . GLU   B 1 116 ? 20.419  13.709  50.950  1.00 52.52 ? 150 GLU   B N   1 
ATOM   3749 C  CA  . GLU   B 1 116 ? 20.240  15.070  51.450  1.00 49.55 ? 150 GLU   B CA  1 
ATOM   3750 C  C   . GLU   B 1 116 ? 21.369  15.465  52.396  1.00 47.36 ? 150 GLU   B C   1 
ATOM   3751 O  O   . GLU   B 1 116 ? 22.115  16.419  52.140  1.00 45.56 ? 150 GLU   B O   1 
ATOM   3752 C  CB  . GLU   B 1 116 ? 18.886  15.174  52.150  1.00 46.52 ? 150 GLU   B CB  1 
ATOM   3753 C  CG  . GLU   B 1 116 ? 18.712  16.446  52.912  1.00 55.33 ? 150 GLU   B CG  1 
ATOM   3754 C  CD  . GLU   B 1 116 ? 18.878  17.657  52.028  1.00 61.00 ? 150 GLU   B CD  1 
ATOM   3755 O  OE1 . GLU   B 1 116 ? 17.902  18.006  51.327  1.00 68.68 ? 150 GLU   B OE1 1 
ATOM   3756 O  OE2 . GLU   B 1 116 ? 19.985  18.245  52.023  1.00 57.55 ? 150 GLU   B OE2 1 
ATOM   3757 N  N   . SER   B 1 117 ? 21.484  14.740  53.511  1.00 48.31 ? 151 SER   B N   1 
ATOM   3758 C  CA  . SER   B 1 117 ? 22.617  14.830  54.426  1.00 49.45 ? 151 SER   B CA  1 
ATOM   3759 C  C   . SER   B 1 117 ? 23.953  14.928  53.689  1.00 47.66 ? 151 SER   B C   1 
ATOM   3760 O  O   . SER   B 1 117 ? 24.676  15.924  53.816  1.00 40.84 ? 151 SER   B O   1 
ATOM   3761 C  CB  . SER   B 1 117 ? 22.602  13.592  55.338  1.00 49.21 ? 151 SER   B CB  1 
ATOM   3762 O  OG  . SER   B 1 117 ? 23.182  13.832  56.601  1.00 46.61 ? 151 SER   B OG  1 
ATOM   3763 N  N   . ALA   B 1 118 ? 24.277  13.882  52.912  1.00 44.15 ? 152 ALA   B N   1 
ATOM   3764 C  CA  . ALA   B 1 118 ? 25.570  13.787  52.233  1.00 44.75 ? 152 ALA   B CA  1 
ATOM   3765 C  C   . ALA   B 1 118 ? 25.868  15.030  51.412  1.00 43.18 ? 152 ALA   B C   1 
ATOM   3766 O  O   . ALA   B 1 118 ? 27.009  15.502  51.373  1.00 42.79 ? 152 ALA   B O   1 
ATOM   3767 C  CB  . ALA   B 1 118 ? 25.602  12.549  51.332  1.00 40.07 ? 152 ALA   B CB  1 
ATOM   3768 N  N   . PHE   B 1 119 ? 24.849  15.559  50.738  1.00 40.92 ? 153 PHE   B N   1 
ATOM   3769 C  CA  . PHE   B 1 119 ? 24.997  16.794  49.984  1.00 42.92 ? 153 PHE   B CA  1 
ATOM   3770 C  C   . PHE   B 1 119 ? 25.322  17.963  50.912  1.00 44.14 ? 153 PHE   B C   1 
ATOM   3771 O  O   . PHE   B 1 119 ? 26.266  18.725  50.667  1.00 39.29 ? 153 PHE   B O   1 
ATOM   3772 C  CB  . PHE   B 1 119 ? 23.710  17.035  49.191  1.00 41.99 ? 153 PHE   B CB  1 
ATOM   3773 C  CG  . PHE   B 1 119 ? 23.726  18.271  48.361  1.00 43.52 ? 153 PHE   B CG  1 
ATOM   3774 C  CD1 . PHE   B 1 119 ? 23.229  19.462  48.866  1.00 44.60 ? 153 PHE   B CD1 1 
ATOM   3775 C  CD2 . PHE   B 1 119 ? 24.235  18.246  47.074  1.00 39.44 ? 153 PHE   B CD2 1 
ATOM   3776 C  CE1 . PHE   B 1 119 ? 23.238  20.597  48.099  1.00 44.75 ? 153 PHE   B CE1 1 
ATOM   3777 C  CE2 . PHE   B 1 119 ? 24.251  19.377  46.302  1.00 37.47 ? 153 PHE   B CE2 1 
ATOM   3778 C  CZ  . PHE   B 1 119 ? 23.750  20.554  46.809  1.00 43.01 ? 153 PHE   B CZ  1 
ATOM   3779 N  N   . SER   B 1 120 ? 24.559  18.101  52.000  1.00 48.27 ? 154 SER   B N   1 
ATOM   3780 C  CA  . SER   B 1 120 ? 24.795  19.181  52.953  1.00 42.83 ? 154 SER   B CA  1 
ATOM   3781 C  C   . SER   B 1 120 ? 26.181  19.083  53.567  1.00 48.13 ? 154 SER   B C   1 
ATOM   3782 O  O   . SER   B 1 120 ? 26.869  20.099  53.728  1.00 53.36 ? 154 SER   B O   1 
ATOM   3783 C  CB  . SER   B 1 120 ? 23.738  19.157  54.057  1.00 45.32 ? 154 SER   B CB  1 
ATOM   3784 O  OG  . SER   B 1 120 ? 22.429  19.133  53.519  1.00 57.55 ? 154 SER   B OG  1 
ATOM   3785 N  N   . ILE   B 1 121 ? 26.611  17.872  53.924  1.00 44.78 ? 155 ILE   B N   1 
ATOM   3786 C  CA  . ILE   B 1 121 ? 27.919  17.730  54.552  1.00 46.71 ? 155 ILE   B CA  1 
ATOM   3787 C  C   . ILE   B 1 121 ? 29.038  17.966  53.545  1.00 45.57 ? 155 ILE   B C   1 
ATOM   3788 O  O   . ILE   B 1 121 ? 30.118  18.448  53.908  1.00 46.98 ? 155 ILE   B O   1 
ATOM   3789 C  CB  . ILE   B 1 121 ? 28.031  16.353  55.225  1.00 43.18 ? 155 ILE   B CB  1 
ATOM   3790 C  CG1 . ILE   B 1 121 ? 27.016  16.253  56.359  1.00 42.77 ? 155 ILE   B CG1 1 
ATOM   3791 C  CG2 . ILE   B 1 121 ? 29.420  16.135  55.767  1.00 42.67 ? 155 ILE   B CG2 1 
ATOM   3792 C  CD1 . ILE   B 1 121 ? 26.988  14.908  57.029  1.00 48.38 ? 155 ILE   B CD1 1 
ATOM   3793 N  N   . SER   B 1 122 ? 28.800  17.668  52.268  1.00 44.47 ? 156 SER   B N   1 
ATOM   3794 C  CA  . SER   B 1 122 ? 29.850  17.855  51.270  1.00 48.58 ? 156 SER   B CA  1 
ATOM   3795 C  C   . SER   B 1 122 ? 30.091  19.336  50.981  1.00 50.43 ? 156 SER   B C   1 
ATOM   3796 O  O   . SER   B 1 122 ? 31.240  19.794  50.996  1.00 48.98 ? 156 SER   B O   1 
ATOM   3797 C  CB  . SER   B 1 122 ? 29.512  17.090  49.984  1.00 42.66 ? 156 SER   B CB  1 
ATOM   3798 O  OG  . SER   B 1 122 ? 29.656  15.697  50.188  1.00 40.06 ? 156 SER   B OG  1 
ATOM   3799 N  N   . VAL   B 1 123 ? 29.023  20.104  50.710  1.00 46.89 ? 157 VAL   B N   1 
ATOM   3800 C  CA  . VAL   B 1 123 ? 29.206  21.520  50.390  1.00 48.33 ? 157 VAL   B CA  1 
ATOM   3801 C  C   . VAL   B 1 123 ? 29.779  22.270  51.585  1.00 52.36 ? 157 VAL   B C   1 
ATOM   3802 O  O   . VAL   B 1 123 ? 30.590  23.195  51.420  1.00 50.72 ? 157 VAL   B O   1 
ATOM   3803 C  CB  . VAL   B 1 123 ? 27.887  22.161  49.895  1.00 43.77 ? 157 VAL   B CB  1 
ATOM   3804 C  CG1 . VAL   B 1 123 ? 27.278  21.348  48.773  1.00 41.66 ? 157 VAL   B CG1 1 
ATOM   3805 C  CG2 . VAL   B 1 123 ? 26.899  22.325  51.019  1.00 47.74 ? 157 VAL   B CG2 1 
ATOM   3806 N  N   . ALA   B 1 124 ? 29.394  21.868  52.803  1.00 55.86 ? 158 ALA   B N   1 
ATOM   3807 C  CA  . ALA   B 1 124 ? 29.889  22.505  54.018  1.00 61.24 ? 158 ALA   B CA  1 
ATOM   3808 C  C   . ALA   B 1 124 ? 31.353  22.191  54.277  1.00 55.64 ? 158 ALA   B C   1 
ATOM   3809 O  O   . ALA   B 1 124 ? 31.994  22.880  55.077  1.00 55.59 ? 158 ALA   B O   1 
ATOM   3810 C  CB  . ALA   B 1 124 ? 29.049  22.074  55.219  1.00 56.35 ? 158 ALA   B CB  1 
ATOM   3811 N  N   . ASN   B 1 125 ? 31.894  21.168  53.622  1.00 50.10 ? 159 ASN   B N   1 
ATOM   3812 C  CA  . ASN   B 1 125 ? 33.322  20.898  53.667  1.00 52.81 ? 159 ASN   B CA  1 
ATOM   3813 C  C   . ASN   B 1 125 ? 34.019  21.206  52.338  1.00 50.75 ? 159 ASN   B C   1 
ATOM   3814 O  O   . ASN   B 1 125 ? 35.116  20.698  52.093  1.00 49.53 ? 159 ASN   B O   1 
ATOM   3815 C  CB  . ASN   B 1 125 ? 33.573  19.452  54.104  1.00 46.24 ? 159 ASN   B CB  1 
ATOM   3816 C  CG  . ASN   B 1 125 ? 33.333  19.247  55.595  1.00 49.80 ? 159 ASN   B CG  1 
ATOM   3817 O  OD1 . ASN   B 1 125 ? 34.268  19.269  56.405  1.00 44.53 ? 159 ASN   B OD1 1 
ATOM   3818 N  ND2 . ASN   B 1 125 ? 32.077  19.051  55.964  1.00 54.62 ? 159 ASN   B ND2 1 
ATOM   3819 N  N   . GLY   B 1 126 ? 33.404  22.027  51.477  1.00 45.75 ? 160 GLY   B N   1 
ATOM   3820 C  CA  . GLY   B 1 126 ? 34.079  22.592  50.320  1.00 45.08 ? 160 GLY   B CA  1 
ATOM   3821 C  C   . GLY   B 1 126 ? 33.616  22.115  48.950  1.00 47.88 ? 160 GLY   B C   1 
ATOM   3822 O  O   . GLY   B 1 126 ? 34.142  22.598  47.936  1.00 45.66 ? 160 GLY   B O   1 
ATOM   3823 N  N   . ALA   B 1 127 ? 32.658  21.202  48.867  1.00 44.01 ? 161 ALA   B N   1 
ATOM   3824 C  CA  . ALA   B 1 127 ? 32.253  20.685  47.568  1.00 43.47 ? 161 ALA   B CA  1 
ATOM   3825 C  C   . ALA   B 1 127 ? 31.455  21.717  46.777  1.00 42.89 ? 161 ALA   B C   1 
ATOM   3826 O  O   . ALA   B 1 127 ? 30.544  22.363  47.306  1.00 44.85 ? 161 ALA   B O   1 
ATOM   3827 C  CB  . ALA   B 1 127 ? 31.424  19.413  47.743  1.00 43.04 ? 161 ALA   B CB  1 
ATOM   3828 N  N   . ILE   B 1 128 ? 31.792  21.857  45.496  1.00 37.84 ? 162 ILE   B N   1 
ATOM   3829 C  CA  . ILE   B 1 128 ? 30.989  22.662  44.578  1.00 40.88 ? 162 ILE   B CA  1 
ATOM   3830 C  C   . ILE   B 1 128 ? 29.679  21.937  44.291  1.00 41.14 ? 162 ILE   B C   1 
ATOM   3831 O  O   . ILE   B 1 128 ? 29.694  20.808  43.783  1.00 39.93 ? 162 ILE   B O   1 
ATOM   3832 C  CB  . ILE   B 1 128 ? 31.729  22.945  43.264  1.00 42.18 ? 162 ILE   B CB  1 
ATOM   3833 C  CG1 . ILE   B 1 128 ? 33.073  23.617  43.527  1.00 40.63 ? 162 ILE   B CG1 1 
ATOM   3834 C  CG2 . ILE   B 1 128 ? 30.853  23.800  42.340  1.00 48.12 ? 162 ILE   B CG2 1 
ATOM   3835 C  CD1 . ILE   B 1 128 ? 33.638  24.320  42.302  1.00 44.38 ? 162 ILE   B CD1 1 
ATOM   3836 N  N   . PRO   B 1 129 ? 28.529  22.531  44.594  1.00 45.90 ? 163 PRO   B N   1 
ATOM   3837 C  CA  . PRO   B 1 129 ? 27.264  21.870  44.263  1.00 43.09 ? 163 PRO   B CA  1 
ATOM   3838 C  C   . PRO   B 1 129 ? 27.027  21.853  42.762  1.00 44.56 ? 163 PRO   B C   1 
ATOM   3839 O  O   . PRO   B 1 129 ? 27.275  22.838  42.057  1.00 45.27 ? 163 PRO   B O   1 
ATOM   3840 C  CB  . PRO   B 1 129 ? 26.220  22.724  44.990  1.00 35.26 ? 163 PRO   B CB  1 
ATOM   3841 C  CG  . PRO   B 1 129 ? 26.844  24.063  45.071  1.00 43.73 ? 163 PRO   B CG  1 
ATOM   3842 C  CD  . PRO   B 1 129 ? 28.316  23.822  45.269  1.00 44.14 ? 163 PRO   B CD  1 
ATOM   3843 N  N   . SER   B 1 130 ? 26.559  20.707  42.272  1.00 42.64 ? 164 SER   B N   1 
ATOM   3844 C  CA  . SER   B 1 130 ? 26.086  20.611  40.899  1.00 44.11 ? 164 SER   B CA  1 
ATOM   3845 C  C   . SER   B 1 130 ? 24.570  20.492  40.812  1.00 40.35 ? 164 SER   B C   1 
ATOM   3846 O  O   . SER   B 1 130 ? 23.940  21.241  40.066  1.00 35.67 ? 164 SER   B O   1 
ATOM   3847 C  CB  . SER   B 1 130 ? 26.779  19.436  40.190  1.00 47.28 ? 164 SER   B CB  1 
ATOM   3848 O  OG  . SER   B 1 130 ? 26.506  19.432  38.798  1.00 43.78 ? 164 SER   B OG  1 
ATOM   3849 N  N   . SER   B 1 131 ? 23.957  19.605  41.597  1.00 39.21 ? 165 SER   B N   1 
ATOM   3850 C  CA  . SER   B 1 131 ? 22.528  19.478  41.587  1.00 42.28 ? 165 SER   B CA  1 
ATOM   3851 C  C   . SER   B 1 131 ? 22.048  19.339  43.022  1.00 46.64 ? 165 SER   B C   1 
ATOM   3852 O  O   . SER   B 1 131 ? 22.601  18.512  43.777  1.00 46.80 ? 165 SER   B O   1 
ATOM   3853 C  CB  . SER   B 1 131 ? 22.048  18.284  40.767  1.00 47.79 ? 165 SER   B CB  1 
ATOM   3854 O  OG  . SER   B 1 131 ? 20.632  18.253  40.722  1.00 41.03 ? 165 SER   B OG  1 
ATOM   3855 N  N   . PRO   B 1 132 ? 21.020  20.097  43.416  1.00 44.44 ? 166 PRO   B N   1 
ATOM   3856 C  CA  . PRO   B 1 132 ? 20.506  20.017  44.797  1.00 47.37 ? 166 PRO   B CA  1 
ATOM   3857 C  C   . PRO   B 1 132 ? 19.834  18.675  45.027  1.00 46.25 ? 166 PRO   B C   1 
ATOM   3858 O  O   . PRO   B 1 132 ? 19.612  17.912  44.071  1.00 41.36 ? 166 PRO   B O   1 
ATOM   3859 C  CB  . PRO   B 1 132 ? 19.480  21.152  44.866  1.00 47.60 ? 166 PRO   B CB  1 
ATOM   3860 C  CG  . PRO   B 1 132 ? 19.065  21.311  43.446  1.00 53.62 ? 166 PRO   B CG  1 
ATOM   3861 C  CD  . PRO   B 1 132 ? 20.220  21.009  42.591  1.00 48.84 ? 166 PRO   B CD  1 
ATOM   3862 N  N   . PRO   B 1 133 ? 19.499  18.342  46.279  1.00 48.81 ? 167 PRO   B N   1 
ATOM   3863 C  CA  . PRO   B 1 133 ? 18.758  17.094  46.538  1.00 44.33 ? 167 PRO   B CA  1 
ATOM   3864 C  C   . PRO   B 1 133 ? 17.341  17.133  45.973  1.00 46.53 ? 167 PRO   B C   1 
ATOM   3865 O  O   . PRO   B 1 133 ? 16.598  18.092  46.197  1.00 46.70 ? 167 PRO   B O   1 
ATOM   3866 C  CB  . PRO   B 1 133 ? 18.753  16.998  48.067  1.00 46.23 ? 167 PRO   B CB  1 
ATOM   3867 C  CG  . PRO   B 1 133 ? 19.946  17.800  48.487  1.00 45.62 ? 167 PRO   B CG  1 
ATOM   3868 C  CD  . PRO   B 1 133 ? 20.011  18.936  47.524  1.00 45.59 ? 167 PRO   B CD  1 
ATOM   3869 N  N   . ILE   B 1 134 ? 16.979  16.064  45.241  1.00 47.04 ? 168 ILE   B N   1 
ATOM   3870 C  CA  . ILE   B 1 134 ? 15.671  15.862  44.614  1.00 42.47 ? 168 ILE   B CA  1 
ATOM   3871 C  C   . ILE   B 1 134 ? 15.210  14.435  44.901  1.00 46.55 ? 168 ILE   B C   1 
ATOM   3872 O  O   . ILE   B 1 134 ? 16.008  13.494  44.824  1.00 50.30 ? 168 ILE   B O   1 
ATOM   3873 C  CB  . ILE   B 1 134 ? 15.736  16.096  43.093  1.00 39.71 ? 168 ILE   B CB  1 
ATOM   3874 C  CG1 . ILE   B 1 134 ? 16.231  17.512  42.791  1.00 43.38 ? 168 ILE   B CG1 1 
ATOM   3875 C  CG2 . ILE   B 1 134 ? 14.389  15.815  42.467  1.00 41.90 ? 168 ILE   B CG2 1 
ATOM   3876 C  CD1 . ILE   B 1 134 ? 17.249  17.569  41.682  1.00 41.72 ? 168 ILE   B CD1 1 
ATOM   3877 N  N   . VAL   B 1 135 ? 13.927  14.264  45.228  1.00 50.43 ? 169 VAL   B N   1 
ATOM   3878 C  CA  . VAL   B 1 135 ? 13.377  12.966  45.625  1.00 53.17 ? 169 VAL   B CA  1 
ATOM   3879 C  C   . VAL   B 1 135 ? 12.351  12.524  44.590  1.00 51.98 ? 169 VAL   B C   1 
ATOM   3880 O  O   . VAL   B 1 135 ? 11.564  13.340  44.089  1.00 48.12 ? 169 VAL   B O   1 
ATOM   3881 C  CB  . VAL   B 1 135 ? 12.756  13.009  47.040  1.00 52.04 ? 169 VAL   B CB  1 
ATOM   3882 C  CG1 . VAL   B 1 135 ? 11.775  14.158  47.167  1.00 56.89 ? 169 VAL   B CG1 1 
ATOM   3883 C  CG2 . VAL   B 1 135 ? 12.071  11.699  47.367  1.00 51.83 ? 169 VAL   B CG2 1 
ATOM   3884 N  N   . LEU   B 1 136 ? 12.375  11.229  44.269  1.00 54.64 ? 170 LEU   B N   1 
ATOM   3885 C  CA  . LEU   B 1 136 ? 11.574  10.614  43.215  1.00 54.82 ? 170 LEU   B CA  1 
ATOM   3886 C  C   . LEU   B 1 136 ? 10.465  9.811   43.880  1.00 58.26 ? 170 LEU   B C   1 
ATOM   3887 O  O   . LEU   B 1 136 ? 10.758  8.896   44.656  1.00 54.61 ? 170 LEU   B O   1 
ATOM   3888 C  CB  . LEU   B 1 136 ? 12.423  9.672   42.357  1.00 52.36 ? 170 LEU   B CB  1 
ATOM   3889 C  CG  . LEU   B 1 136 ? 13.832  10.046  41.915  1.00 47.76 ? 170 LEU   B CG  1 
ATOM   3890 C  CD1 . LEU   B 1 136 ? 14.298  9.099   40.809  1.00 49.98 ? 170 LEU   B CD1 1 
ATOM   3891 C  CD2 . LEU   B 1 136 ? 13.927  11.478  41.426  1.00 42.38 ? 170 LEU   B CD2 1 
ATOM   3892 N  N   . ASN   B 1 137 ? 9.204   10.140  43.575  1.00 58.31 ? 171 ASN   B N   1 
ATOM   3893 C  CA  . ASN   B 1 137 ? 8.036   9.334   43.960  1.00 60.48 ? 171 ASN   B CA  1 
ATOM   3894 C  C   . ASN   B 1 137 ? 8.202   8.869   45.410  1.00 67.79 ? 171 ASN   B C   1 
ATOM   3895 O  O   . ASN   B 1 137 ? 8.000   7.697   45.739  1.00 66.74 ? 171 ASN   B O   1 
ATOM   3896 C  CB  . ASN   B 1 137 ? 7.852   8.199   42.909  1.00 68.54 ? 171 ASN   B CB  1 
ATOM   3897 C  CG  . ASN   B 1 137 ? 6.714   7.161   43.217  1.00 84.82 ? 171 ASN   B CG  1 
ATOM   3898 O  OD1 . ASN   B 1 137 ? 6.769   6.361   44.150  1.00 89.02 ? 171 ASN   B OD1 1 
ATOM   3899 N  ND2 . ASN   B 1 137 ? 5.676   7.196   42.388  1.00 83.01 ? 171 ASN   B ND2 1 
ATOM   3900 N  N   . GLU   B 1 138 ? 8.650   9.788   46.274  1.00 65.06 ? 172 GLU   B N   1 
ATOM   3901 C  CA  . GLU   B 1 138 ? 8.747   9.536   47.718  1.00 57.76 ? 172 GLU   B CA  1 
ATOM   3902 C  C   . GLU   B 1 138 ? 9.465   8.214   48.040  1.00 64.16 ? 172 GLU   B C   1 
ATOM   3903 O  O   . GLU   B 1 138 ? 9.098   7.490   48.976  1.00 66.03 ? 172 GLU   B O   1 
ATOM   3904 C  CB  . GLU   B 1 138 ? 7.358   9.571   48.363  1.00 57.87 ? 172 GLU   B CB  1 
ATOM   3905 N  N   . ALA   B 1 139 ? 10.505  7.887   47.260  1.00 61.16 ? 173 ALA   B N   1 
ATOM   3906 C  CA  . ALA   B 1 139 ? 11.287  6.676   47.514  1.00 57.15 ? 173 ALA   B CA  1 
ATOM   3907 C  C   . ALA   B 1 139 ? 12.792  6.913   47.431  1.00 52.67 ? 173 ALA   B C   1 
ATOM   3908 O  O   . ALA   B 1 139 ? 13.520  6.622   48.387  1.00 54.03 ? 173 ALA   B O   1 
ATOM   3909 C  CB  . ALA   B 1 139 ? 10.897  5.555   46.551  1.00 42.50 ? 173 ALA   B CB  1 
ATOM   3910 N  N   . VAL   B 1 140 ? 13.282  7.423   46.305  1.00 46.47 ? 174 VAL   B N   1 
ATOM   3911 C  CA  . VAL   B 1 140 ? 14.717  7.553   46.080  1.00 52.28 ? 174 VAL   B CA  1 
ATOM   3912 C  C   . VAL   B 1 140 ? 15.079  9.031   46.025  1.00 49.27 ? 174 VAL   B C   1 
ATOM   3913 O  O   . VAL   B 1 140 ? 14.349  9.837   45.440  1.00 50.42 ? 174 VAL   B O   1 
ATOM   3914 C  CB  . VAL   B 1 140 ? 15.172  6.820   44.798  1.00 47.14 ? 174 VAL   B CB  1 
ATOM   3915 C  CG1 . VAL   B 1 140 ? 16.675  6.621   44.813  1.00 39.97 ? 174 VAL   B CG1 1 
ATOM   3916 C  CG2 . VAL   B 1 140 ? 14.475  5.474   44.674  1.00 46.73 ? 174 VAL   B CG2 1 
ATOM   3917 N  N   . THR   B 1 141 ? 16.205  9.381   46.654  1.00 49.09 ? 175 THR   B N   1 
ATOM   3918 C  CA  . THR   B 1 141 ? 16.744  10.735  46.679  1.00 47.92 ? 175 THR   B CA  1 
ATOM   3919 C  C   . THR   B 1 141 ? 18.054  10.779  45.904  1.00 44.70 ? 175 THR   B C   1 
ATOM   3920 O  O   . THR   B 1 141 ? 18.898  9.887   46.042  1.00 45.78 ? 175 THR   B O   1 
ATOM   3921 C  CB  . THR   B 1 141 ? 16.999  11.217  48.118  1.00 53.64 ? 175 THR   B CB  1 
ATOM   3922 O  OG1 . THR   B 1 141 ? 15.832  11.005  48.926  1.00 51.60 ? 175 THR   B OG1 1 
ATOM   3923 C  CG2 . THR   B 1 141 ? 17.376  12.703  48.134  1.00 43.22 ? 175 THR   B CG2 1 
ATOM   3924 N  N   . ILE   B 1 142 ? 18.237  11.831  45.109  1.00 44.97 ? 176 ILE   B N   1 
ATOM   3925 C  CA  . ILE   B 1 142 ? 19.426  11.963  44.278  1.00 45.11 ? 176 ILE   B CA  1 
ATOM   3926 C  C   . ILE   B 1 142 ? 20.045  13.346  44.467  1.00 44.35 ? 176 ILE   B C   1 
ATOM   3927 O  O   . ILE   B 1 142 ? 19.344  14.341  44.676  1.00 39.72 ? 176 ILE   B O   1 
ATOM   3928 C  CB  . ILE   B 1 142 ? 19.099  11.699  42.787  1.00 40.78 ? 176 ILE   B CB  1 
ATOM   3929 C  CG1 . ILE   B 1 142 ? 20.350  11.269  42.046  1.00 46.83 ? 176 ILE   B CG1 1 
ATOM   3930 C  CG2 . ILE   B 1 142 ? 18.444  12.908  42.115  1.00 42.99 ? 176 ILE   B CG2 1 
ATOM   3931 C  CD1 . ILE   B 1 142 ? 20.980  10.048  42.656  1.00 49.17 ? 176 ILE   B CD1 1 
ATOM   3932 N  N   . ALA   B 1 143 ? 21.375  13.403  44.395  1.00 42.81 ? 177 ALA   B N   1 
ATOM   3933 C  CA  . ALA   B 1 143 ? 22.086  14.671  44.493  1.00 43.14 ? 177 ALA   B CA  1 
ATOM   3934 C  C   . ALA   B 1 143 ? 23.428  14.572  43.779  1.00 42.18 ? 177 ALA   B C   1 
ATOM   3935 O  O   . ALA   B 1 143 ? 24.024  13.494  43.691  1.00 38.54 ? 177 ALA   B O   1 
ATOM   3936 C  CB  . ALA   B 1 143 ? 22.302  15.090  45.951  1.00 39.00 ? 177 ALA   B CB  1 
ATOM   3937 N  N   . GLU   B 1 144 ? 23.912  15.717  43.289  1.00 45.54 ? 178 GLU   B N   1 
ATOM   3938 C  CA  . GLU   B 1 144 ? 25.169  15.769  42.551  1.00 44.01 ? 178 GLU   B CA  1 
ATOM   3939 C  C   . GLU   B 1 144 ? 26.050  16.902  43.065  1.00 43.70 ? 178 GLU   B C   1 
ATOM   3940 O  O   . GLU   B 1 144 ? 25.606  18.054  43.172  1.00 46.22 ? 178 GLU   B O   1 
ATOM   3941 C  CB  . GLU   B 1 144 ? 24.906  15.904  41.037  1.00 42.67 ? 178 GLU   B CB  1 
ATOM   3942 C  CG  . GLU   B 1 144 ? 24.588  14.550  40.369  1.00 40.12 ? 178 GLU   B CG  1 
ATOM   3943 C  CD  . GLU   B 1 144 ? 23.674  14.654  39.153  1.00 36.64 ? 178 GLU   B CD  1 
ATOM   3944 O  OE1 . GLU   B 1 144 ? 23.925  15.492  38.251  1.00 36.21 ? 178 GLU   B OE1 1 
ATOM   3945 O  OE2 . GLU   B 1 144 ? 22.695  13.880  39.116  1.00 31.28 ? 178 GLU   B OE2 1 
ATOM   3946 N  N   . VAL   B 1 145 ? 27.288  16.552  43.415  1.00 39.14 ? 179 VAL   B N   1 
ATOM   3947 C  CA  . VAL   B 1 145 ? 28.353  17.509  43.676  1.00 42.16 ? 179 VAL   B CA  1 
ATOM   3948 C  C   . VAL   B 1 145 ? 29.395  17.329  42.587  1.00 39.24 ? 179 VAL   B C   1 
ATOM   3949 O  O   . VAL   B 1 145 ? 29.443  16.305  41.908  1.00 38.57 ? 179 VAL   B O   1 
ATOM   3950 C  CB  . VAL   B 1 145 ? 28.992  17.340  45.073  1.00 37.80 ? 179 VAL   B CB  1 
ATOM   3951 C  CG1 . VAL   B 1 145 ? 27.921  17.252  46.153  1.00 43.87 ? 179 VAL   B CG1 1 
ATOM   3952 C  CG2 . VAL   B 1 145 ? 29.901  16.124  45.117  1.00 33.93 ? 179 VAL   B CG2 1 
ATOM   3953 N  N   . LYS   B 1 146 ? 30.244  18.339  42.421  1.00 43.63 ? 180 LYS   B N   1 
ATOM   3954 C  CA  . LYS   B 1 146 ? 31.281  18.278  41.399  1.00 41.86 ? 180 LYS   B CA  1 
ATOM   3955 C  C   . LYS   B 1 146 ? 32.451  17.413  41.871  1.00 39.25 ? 180 LYS   B C   1 
ATOM   3956 O  O   . LYS   B 1 146 ? 32.868  17.483  43.031  1.00 40.13 ? 180 LYS   B O   1 
ATOM   3957 C  CB  . LYS   B 1 146 ? 31.761  19.683  41.036  1.00 34.38 ? 180 LYS   B CB  1 
ATOM   3958 C  CG  . LYS   B 1 146 ? 30.833  20.459  40.130  1.00 38.19 ? 180 LYS   B CG  1 
ATOM   3959 C  CD  . LYS   B 1 146 ? 31.533  21.744  39.681  1.00 48.66 ? 180 LYS   B CD  1 
ATOM   3960 C  CE  . LYS   B 1 146 ? 30.742  22.568  38.668  1.00 44.75 ? 180 LYS   B CE  1 
ATOM   3961 N  NZ  . LYS   B 1 146 ? 31.609  23.661  38.129  1.00 43.03 ? 180 LYS   B NZ  1 
ATOM   3962 N  N   . LEU   B 1 147 ? 32.974  16.588  40.961  1.00 38.19 ? 181 LEU   B N   1 
ATOM   3963 C  CA  . LEU   B 1 147 ? 34.071  15.671  41.269  1.00 38.24 ? 181 LEU   B CA  1 
ATOM   3964 C  C   . LEU   B 1 147 ? 35.378  16.136  40.646  1.00 37.83 ? 181 LEU   B C   1 
ATOM   3965 O  O   . LEU   B 1 147 ? 36.295  16.547  41.370  1.00 32.44 ? 181 LEU   B O   1 
ATOM   3966 C  CB  . LEU   B 1 147 ? 33.699  14.254  40.818  1.00 29.90 ? 181 LEU   B CB  1 
ATOM   3967 C  CG  . LEU   B 1 147 ? 34.738  13.183  41.107  1.00 28.69 ? 181 LEU   B CG  1 
ATOM   3968 C  CD1 . LEU   B 1 147 ? 34.871  13.043  42.604  1.00 26.23 ? 181 LEU   B CD1 1 
ATOM   3969 C  CD2 . LEU   B 1 147 ? 34.334  11.884  40.470  1.00 30.46 ? 181 LEU   B CD2 1 
ATOM   3970 N  N   . TYR   B 1 148 ? 35.523  16.036  39.317  1.00 34.16 ? 182 TYR   B N   1 
ATOM   3971 C  CA  . TYR   B 1 148 ? 36.591  16.688  38.562  1.00 30.48 ? 182 TYR   B CA  1 
ATOM   3972 C  C   . TYR   B 1 148 ? 36.099  16.901  37.139  1.00 30.06 ? 182 TYR   B C   1 
ATOM   3973 O  O   . TYR   B 1 148 ? 35.175  16.226  36.678  1.00 32.55 ? 182 TYR   B O   1 
ATOM   3974 C  CB  . TYR   B 1 148 ? 37.903  15.885  38.566  1.00 32.94 ? 182 TYR   B CB  1 
ATOM   3975 C  CG  . TYR   B 1 148 ? 37.709  14.384  38.572  1.00 35.20 ? 182 TYR   B CG  1 
ATOM   3976 C  CD1 . TYR   B 1 148 ? 37.251  13.712  37.444  1.00 27.60 ? 182 TYR   B CD1 1 
ATOM   3977 C  CD2 . TYR   B 1 148 ? 37.989  13.640  39.713  1.00 31.36 ? 182 TYR   B CD2 1 
ATOM   3978 C  CE1 . TYR   B 1 148 ? 37.069  12.337  37.463  1.00 28.23 ? 182 TYR   B CE1 1 
ATOM   3979 C  CE2 . TYR   B 1 148 ? 37.814  12.288  39.737  1.00 31.98 ? 182 TYR   B CE2 1 
ATOM   3980 C  CZ  . TYR   B 1 148 ? 37.354  11.637  38.613  1.00 30.16 ? 182 TYR   B CZ  1 
ATOM   3981 O  OH  . TYR   B 1 148 ? 37.181  10.279  38.668  1.00 32.64 ? 182 TYR   B OH  1 
ATOM   3982 N  N   . GLY   B 1 149 ? 36.724  17.850  36.444  1.00 28.28 ? 183 GLY   B N   1 
ATOM   3983 C  CA  . GLY   B 1 149 ? 36.266  18.229  35.119  1.00 27.06 ? 183 GLY   B CA  1 
ATOM   3984 C  C   . GLY   B 1 149 ? 34.787  18.555  35.071  1.00 29.50 ? 183 GLY   B C   1 
ATOM   3985 O  O   . GLY   B 1 149 ? 34.322  19.450  35.780  1.00 33.52 ? 183 GLY   B O   1 
ATOM   3986 N  N   . ASP   B 1 150 ? 34.022  17.847  34.247  1.00 29.23 ? 184 ASP   B N   1 
ATOM   3987 C  CA  . ASP   B 1 150 ? 32.570  17.967  34.287  1.00 29.35 ? 184 ASP   B CA  1 
ATOM   3988 C  C   . ASP   B 1 150 ? 31.927  16.665  34.763  1.00 31.35 ? 184 ASP   B C   1 
ATOM   3989 O  O   . ASP   B 1 150 ? 30.792  16.346  34.397  1.00 31.79 ? 184 ASP   B O   1 
ATOM   3990 C  CB  . ASP   B 1 150 ? 32.019  18.411  32.932  1.00 28.86 ? 184 ASP   B CB  1 
ATOM   3991 C  CG  . ASP   B 1 150 ? 32.459  19.840  32.547  1.00 34.45 ? 184 ASP   B CG  1 
ATOM   3992 O  OD1 . ASP   B 1 150 ? 32.027  20.808  33.214  1.00 40.47 ? 184 ASP   B OD1 1 
ATOM   3993 O  OD2 . ASP   B 1 150 ? 33.217  20.003  31.562  1.00 31.83 ? 184 ASP   B OD2 1 
ATOM   3994 N  N   . VAL   B 1 151 ? 32.647  15.923  35.607  1.00 29.25 ? 185 VAL   B N   1 
ATOM   3995 C  CA  . VAL   B 1 151 ? 32.201  14.641  36.140  1.00 28.15 ? 185 VAL   B CA  1 
ATOM   3996 C  C   . VAL   B 1 151 ? 31.715  14.846  37.563  1.00 29.21 ? 185 VAL   B C   1 
ATOM   3997 O  O   . VAL   B 1 151 ? 32.485  15.258  38.433  1.00 31.69 ? 185 VAL   B O   1 
ATOM   3998 C  CB  . VAL   B 1 151 ? 33.324  13.597  36.099  1.00 31.11 ? 185 VAL   B CB  1 
ATOM   3999 C  CG1 . VAL   B 1 151 ? 32.812  12.235  36.614  1.00 23.61 ? 185 VAL   B CG1 1 
ATOM   4000 C  CG2 . VAL   B 1 151 ? 33.911  13.514  34.680  1.00 28.07 ? 185 VAL   B CG2 1 
ATOM   4001 N  N   . VAL   B 1 152 ? 30.454  14.539  37.805  1.00 32.27 ? 186 VAL   B N   1 
ATOM   4002 C  CA  . VAL   B 1 152 ? 29.838  14.706  39.114  1.00 31.05 ? 186 VAL   B CA  1 
ATOM   4003 C  C   . VAL   B 1 152 ? 29.949  13.398  39.886  1.00 33.61 ? 186 VAL   B C   1 
ATOM   4004 O  O   . VAL   B 1 152 ? 30.002  12.297  39.318  1.00 30.85 ? 186 VAL   B O   1 
ATOM   4005 C  CB  . VAL   B 1 152 ? 28.362  15.165  38.986  1.00 35.24 ? 186 VAL   B CB  1 
ATOM   4006 C  CG1 . VAL   B 1 152 ? 28.243  16.371  38.070  1.00 35.92 ? 186 VAL   B CG1 1 
ATOM   4007 C  CG2 . VAL   B 1 152 ? 27.460  14.043  38.468  1.00 31.65 ? 186 VAL   B CG2 1 
ATOM   4008 N  N   . LEU   B 1 153 ? 30.006  13.527  41.205  1.00 36.50 ? 187 LEU   B N   1 
ATOM   4009 C  CA  . LEU   B 1 153 ? 29.804  12.418  42.121  1.00 33.44 ? 187 LEU   B CA  1 
ATOM   4010 C  C   . LEU   B 1 153 ? 28.342  12.441  42.551  1.00 36.71 ? 187 LEU   B C   1 
ATOM   4011 O  O   . LEU   B 1 153 ? 27.815  13.499  42.913  1.00 38.02 ? 187 LEU   B O   1 
ATOM   4012 C  CB  . LEU   B 1 153 ? 30.736  12.530  43.330  1.00 26.17 ? 187 LEU   B CB  1 
ATOM   4013 C  CG  . LEU   B 1 153 ? 30.641  11.370  44.320  1.00 35.52 ? 187 LEU   B CG  1 
ATOM   4014 C  CD1 . LEU   B 1 153 ? 31.153  10.020  43.727  1.00 26.88 ? 187 LEU   B CD1 1 
ATOM   4015 C  CD2 . LEU   B 1 153 ? 31.377  11.726  45.599  1.00 34.22 ? 187 LEU   B CD2 1 
ATOM   4016 N  N   . ARG   B 1 154 ? 27.684  11.287  42.499  1.00 33.25 ? 188 ARG   B N   1 
ATOM   4017 C  CA  . ARG   B 1 154 ? 26.235  11.230  42.644  1.00 34.94 ? 188 ARG   B CA  1 
ATOM   4018 C  C   . ARG   B 1 154 ? 25.861  10.407  43.866  1.00 36.13 ? 188 ARG   B C   1 
ATOM   4019 O  O   . ARG   B 1 154 ? 26.492  9.382   44.151  1.00 36.80 ? 188 ARG   B O   1 
ATOM   4020 C  CB  . ARG   B 1 154 ? 25.585  10.652  41.378  1.00 37.24 ? 188 ARG   B CB  1 
ATOM   4021 C  CG  . ARG   B 1 154 ? 24.072  10.657  41.379  1.00 34.53 ? 188 ARG   B CG  1 
ATOM   4022 C  CD  . ARG   B 1 154 ? 23.501  10.124  40.059  1.00 31.37 ? 188 ARG   B CD  1 
ATOM   4023 N  NE  . ARG   B 1 154 ? 23.282  11.186  39.076  1.00 35.29 ? 188 ARG   B NE  1 
ATOM   4024 C  CZ  . ARG   B 1 154 ? 23.399  11.028  37.758  1.00 31.56 ? 188 ARG   B CZ  1 
ATOM   4025 N  NH1 . ARG   B 1 154 ? 23.741  9.853   37.249  1.00 30.83 ? 188 ARG   B NH1 1 
ATOM   4026 N  NH2 . ARG   B 1 154 ? 23.180  12.045  36.946  1.00 29.22 ? 188 ARG   B NH2 1 
ATOM   4027 N  N   . TYR   B 1 155 ? 24.838  10.874  44.593  1.00 42.78 ? 189 TYR   B N   1 
ATOM   4028 C  CA  . TYR   B 1 155 ? 24.380  10.255  45.840  1.00 39.38 ? 189 TYR   B CA  1 
ATOM   4029 C  C   . TYR   B 1 155 ? 22.965  9.714   45.641  1.00 38.99 ? 189 TYR   B C   1 
ATOM   4030 O  O   . TYR   B 1 155 ? 22.019  10.482  45.446  1.00 34.26 ? 189 TYR   B O   1 
ATOM   4031 C  CB  . TYR   B 1 155 ? 24.410  11.244  47.006  1.00 32.73 ? 189 TYR   B CB  1 
ATOM   4032 C  CG  . TYR   B 1 155 ? 25.752  11.885  47.289  1.00 39.14 ? 189 TYR   B CG  1 
ATOM   4033 C  CD1 . TYR   B 1 155 ? 26.943  11.163  47.187  1.00 36.36 ? 189 TYR   B CD1 1 
ATOM   4034 C  CD2 . TYR   B 1 155 ? 25.827  13.229  47.655  1.00 38.67 ? 189 TYR   B CD2 1 
ATOM   4035 C  CE1 . TYR   B 1 155 ? 28.169  11.774  47.454  1.00 39.43 ? 189 TYR   B CE1 1 
ATOM   4036 C  CE2 . TYR   B 1 155 ? 27.040  13.846  47.918  1.00 35.90 ? 189 TYR   B CE2 1 
ATOM   4037 C  CZ  . TYR   B 1 155 ? 28.207  13.124  47.821  1.00 37.25 ? 189 TYR   B CZ  1 
ATOM   4038 O  OH  . TYR   B 1 155 ? 29.402  13.761  48.089  1.00 28.03 ? 189 TYR   B OH  1 
ATOM   4039 N  N   . VAL   B 1 156 ? 22.831  8.393   45.702  1.00 39.10 ? 190 VAL   B N   1 
ATOM   4040 C  CA  . VAL   B 1 156 ? 21.551  7.705   45.686  1.00 39.77 ? 190 VAL   B CA  1 
ATOM   4041 C  C   . VAL   B 1 156 ? 21.280  7.230   47.106  1.00 39.08 ? 190 VAL   B C   1 
ATOM   4042 O  O   . VAL   B 1 156 ? 22.150  6.611   47.731  1.00 39.60 ? 190 VAL   B O   1 
ATOM   4043 C  CB  . VAL   B 1 156 ? 21.563  6.513   44.706  1.00 42.30 ? 190 VAL   B CB  1 
ATOM   4044 C  CG1 . VAL   B 1 156 ? 20.173  6.004   44.425  1.00 36.39 ? 190 VAL   B CG1 1 
ATOM   4045 C  CG2 . VAL   B 1 156 ? 22.273  6.865   43.438  1.00 39.25 ? 190 VAL   B CG2 1 
ATOM   4046 N  N   . SER   B 1 157 ? 20.085  7.520   47.616  1.00 38.39 ? 191 SER   B N   1 
ATOM   4047 C  CA  . SER   B 1 157 ? 19.652  7.007   48.906  1.00 41.20 ? 191 SER   B CA  1 
ATOM   4048 C  C   . SER   B 1 157 ? 18.226  6.498   48.788  1.00 43.48 ? 191 SER   B C   1 
ATOM   4049 O  O   . SER   B 1 157 ? 17.434  6.989   47.980  1.00 43.09 ? 191 SER   B O   1 
ATOM   4050 C  CB  . SER   B 1 157 ? 19.745  8.070   50.034  1.00 43.32 ? 191 SER   B CB  1 
ATOM   4051 O  OG  . SER   B 1 157 ? 18.909  9.197   49.803  1.00 43.61 ? 191 SER   B OG  1 
ATOM   4052 N  N   . TYR   B 1 158 ? 17.909  5.506   49.609  1.00 45.41 ? 192 TYR   B N   1 
ATOM   4053 C  CA  . TYR   B 1 158 ? 16.602  4.874   49.610  1.00 51.16 ? 192 TYR   B CA  1 
ATOM   4054 C  C   . TYR   B 1 158 ? 15.863  5.182   50.908  1.00 56.09 ? 192 TYR   B C   1 
ATOM   4055 O  O   . TYR   B 1 158 ? 16.470  5.317   51.976  1.00 60.08 ? 192 TYR   B O   1 
ATOM   4056 C  CB  . TYR   B 1 158 ? 16.737  3.358   49.419  1.00 50.47 ? 192 TYR   B CB  1 
ATOM   4057 C  CG  . TYR   B 1 158 ? 17.245  2.983   48.048  1.00 46.56 ? 192 TYR   B CG  1 
ATOM   4058 C  CD1 . TYR   B 1 158 ? 18.565  2.595   47.848  1.00 47.24 ? 192 TYR   B CD1 1 
ATOM   4059 C  CD2 . TYR   B 1 158 ? 16.409  3.047   46.946  1.00 47.78 ? 192 TYR   B CD2 1 
ATOM   4060 C  CE1 . TYR   B 1 158 ? 19.033  2.260   46.580  1.00 51.59 ? 192 TYR   B CE1 1 
ATOM   4061 C  CE2 . TYR   B 1 158 ? 16.859  2.721   45.679  1.00 49.91 ? 192 TYR   B CE2 1 
ATOM   4062 C  CZ  . TYR   B 1 158 ? 18.169  2.327   45.491  1.00 54.89 ? 192 TYR   B CZ  1 
ATOM   4063 O  OH  . TYR   B 1 158 ? 18.596  1.999   44.209  1.00 51.71 ? 192 TYR   B OH  1 
ATOM   4064 N  N   . LYS   B 1 159 ? 14.539  5.305   50.798  1.00 57.96 ? 193 LYS   B N   1 
ATOM   4065 C  CA  . LYS   B 1 159 ? 13.682  5.458   51.968  1.00 65.89 ? 193 LYS   B CA  1 
ATOM   4066 C  C   . LYS   B 1 159 ? 13.376  4.087   52.565  1.00 73.83 ? 193 LYS   B C   1 
ATOM   4067 O  O   . LYS   B 1 159 ? 14.014  3.672   53.539  1.00 82.52 ? 193 LYS   B O   1 
ATOM   4068 C  CB  . LYS   B 1 159 ? 12.392  6.200   51.596  1.00 68.04 ? 193 LYS   B CB  1 
ATOM   4069 N  N   . ALA   B 1 160 ? 12.425  3.363   51.982  1.00 68.43 ? 194 ALA   B N   1 
ATOM   4070 C  CA  . ALA   B 1 160 ? 12.107  2.019   52.455  1.00 71.95 ? 194 ALA   B CA  1 
ATOM   4071 C  C   . ALA   B 1 160 ? 13.130  0.992   51.947  1.00 76.67 ? 194 ALA   B C   1 
ATOM   4072 O  O   . ALA   B 1 160 ? 13.858  0.368   52.727  1.00 69.68 ? 194 ALA   B O   1 
ATOM   4073 C  CB  . ALA   B 1 160 ? 10.694  1.629   52.027  1.00 68.61 ? 194 ALA   B CB  1 
ATOM   4074 N  N   . GLU   B 1 167 ? 13.915  -1.975  38.017  1.00 58.99 ? 201 GLU   B N   1 
ATOM   4075 C  CA  . GLU   B 1 167 ? 13.641  -1.256  39.262  1.00 64.65 ? 201 GLU   B CA  1 
ATOM   4076 C  C   . GLU   B 1 167 ? 14.867  -0.442  39.689  1.00 65.38 ? 201 GLU   B C   1 
ATOM   4077 O  O   . GLU   B 1 167 ? 15.407  -0.621  40.784  1.00 73.02 ? 201 GLU   B O   1 
ATOM   4078 C  CB  . GLU   B 1 167 ? 13.232  -2.229  40.373  1.00 63.93 ? 201 GLU   B CB  1 
ATOM   4079 N  N   . PHE   B 1 168 ? 15.294  0.456   38.807  1.00 52.98 ? 202 PHE   B N   1 
ATOM   4080 C  CA  . PHE   B 1 168 ? 16.485  1.269   39.007  1.00 50.49 ? 202 PHE   B CA  1 
ATOM   4081 C  C   . PHE   B 1 168 ? 16.123  2.518   39.796  1.00 52.25 ? 202 PHE   B C   1 
ATOM   4082 O  O   . PHE   B 1 168 ? 16.398  2.614   40.998  1.00 53.98 ? 202 PHE   B O   1 
ATOM   4083 C  CB  . PHE   B 1 168 ? 17.084  1.630   37.642  1.00 49.43 ? 202 PHE   B CB  1 
ATOM   4084 C  CG  . PHE   B 1 168 ? 18.342  2.452   37.706  1.00 42.43 ? 202 PHE   B CG  1 
ATOM   4085 C  CD1 . PHE   B 1 168 ? 19.405  2.060   38.504  1.00 38.40 ? 202 PHE   B CD1 1 
ATOM   4086 C  CD2 . PHE   B 1 168 ? 18.481  3.592   36.912  1.00 38.06 ? 202 PHE   B CD2 1 
ATOM   4087 C  CE1 . PHE   B 1 168 ? 20.574  2.809   38.543  1.00 38.91 ? 202 PHE   B CE1 1 
ATOM   4088 C  CE2 . PHE   B 1 168 ? 19.654  4.355   36.948  1.00 35.18 ? 202 PHE   B CE2 1 
ATOM   4089 C  CZ  . PHE   B 1 168 ? 20.695  3.968   37.764  1.00 34.40 ? 202 PHE   B CZ  1 
ATOM   4090 N  N   . LEU   B 1 169 ? 15.504  3.474   39.118  1.00 46.36 ? 203 LEU   B N   1 
ATOM   4091 C  CA  . LEU   B 1 169 ? 14.924  4.664   39.711  1.00 44.18 ? 203 LEU   B CA  1 
ATOM   4092 C  C   . LEU   B 1 169 ? 13.437  4.710   39.372  1.00 42.99 ? 203 LEU   B C   1 
ATOM   4093 O  O   . LEU   B 1 169 ? 12.983  4.049   38.431  1.00 42.68 ? 203 LEU   B O   1 
ATOM   4094 C  CB  . LEU   B 1 169 ? 15.642  5.923   39.202  1.00 37.04 ? 203 LEU   B CB  1 
ATOM   4095 C  CG  . LEU   B 1 169 ? 17.145  5.856   39.484  1.00 34.69 ? 203 LEU   B CG  1 
ATOM   4096 C  CD1 . LEU   B 1 169 ? 17.944  6.804   38.617  1.00 28.71 ? 203 LEU   B CD1 1 
ATOM   4097 C  CD2 . LEU   B 1 169 ? 17.398  6.135   40.951  1.00 40.28 ? 203 LEU   B CD2 1 
ATOM   4098 N  N   . PRO   B 1 170 ? 12.640  5.424   40.156  1.00 38.99 ? 204 PRO   B N   1 
ATOM   4099 C  CA  . PRO   B 1 170 ? 11.243  5.644   39.768  1.00 45.10 ? 204 PRO   B CA  1 
ATOM   4100 C  C   . PRO   B 1 170 ? 11.150  6.251   38.375  1.00 46.93 ? 204 PRO   B C   1 
ATOM   4101 O  O   . PRO   B 1 170 ? 11.993  7.059   37.973  1.00 44.00 ? 204 PRO   B O   1 
ATOM   4102 C  CB  . PRO   B 1 170 ? 10.732  6.604   40.844  1.00 45.37 ? 204 PRO   B CB  1 
ATOM   4103 C  CG  . PRO   B 1 170 ? 11.525  6.195   42.065  1.00 48.41 ? 204 PRO   B CG  1 
ATOM   4104 C  CD  . PRO   B 1 170 ? 12.903  5.842   41.542  1.00 41.68 ? 204 PRO   B CD  1 
ATOM   4105 N  N   . GLY   B 1 171 ? 10.121  5.844   37.630  1.00 45.04 ? 205 GLY   B N   1 
ATOM   4106 C  CA  . GLY   B 1 171 ? 9.954   6.319   36.271  1.00 42.49 ? 205 GLY   B CA  1 
ATOM   4107 C  C   . GLY   B 1 171 ? 10.829  5.631   35.246  1.00 41.21 ? 205 GLY   B C   1 
ATOM   4108 O  O   . GLY   B 1 171 ? 10.790  5.999   34.066  1.00 42.79 ? 205 GLY   B O   1 
ATOM   4109 N  N   . PHE   B 1 172 ? 11.658  4.695   35.663  1.00 39.29 ? 206 PHE   B N   1 
ATOM   4110 C  CA  . PHE   B 1 172 ? 12.208  3.710   34.757  1.00 39.06 ? 206 PHE   B CA  1 
ATOM   4111 C  C   . PHE   B 1 172 ? 11.278  2.506   34.748  1.00 41.95 ? 206 PHE   B C   1 
ATOM   4112 O  O   . PHE   B 1 172 ? 10.643  2.186   35.756  1.00 45.87 ? 206 PHE   B O   1 
ATOM   4113 C  CB  . PHE   B 1 172 ? 13.613  3.287   35.195  1.00 39.31 ? 206 PHE   B CB  1 
ATOM   4114 C  CG  . PHE   B 1 172 ? 14.697  4.211   34.736  1.00 37.63 ? 206 PHE   B CG  1 
ATOM   4115 C  CD1 . PHE   B 1 172 ? 14.768  5.515   35.216  1.00 36.06 ? 206 PHE   B CD1 1 
ATOM   4116 C  CD2 . PHE   B 1 172 ? 15.663  3.772   33.828  1.00 31.90 ? 206 PHE   B CD2 1 
ATOM   4117 C  CE1 . PHE   B 1 172 ? 15.778  6.377   34.793  1.00 30.87 ? 206 PHE   B CE1 1 
ATOM   4118 C  CE2 . PHE   B 1 172 ? 16.670  4.626   33.395  1.00 29.44 ? 206 PHE   B CE2 1 
ATOM   4119 C  CZ  . PHE   B 1 172 ? 16.725  5.935   33.880  1.00 29.95 ? 206 PHE   B CZ  1 
ATOM   4120 N  N   . GLU   B 1 173 ? 11.191  1.843   33.604  1.00 37.45 ? 207 GLU   B N   1 
ATOM   4121 C  CA  . GLU   B 1 173 ? 10.490  0.573   33.506  1.00 37.20 ? 207 GLU   B CA  1 
ATOM   4122 C  C   . GLU   B 1 173 ? 11.490  -0.570  33.378  1.00 30.95 ? 207 GLU   B C   1 
ATOM   4123 O  O   . GLU   B 1 173 ? 12.511  -0.441  32.701  1.00 32.43 ? 207 GLU   B O   1 
ATOM   4124 C  CB  . GLU   B 1 173 ? 9.525   0.576   32.317  1.00 43.11 ? 207 GLU   B CB  1 
ATOM   4125 C  CG  . GLU   B 1 173 ? 8.270   1.409   32.541  1.00 46.27 ? 207 GLU   B CG  1 
ATOM   4126 C  CD  . GLU   B 1 173 ? 7.195   0.652   33.305  1.00 62.69 ? 207 GLU   B CD  1 
ATOM   4127 O  OE1 . GLU   B 1 173 ? 6.675   1.189   34.314  1.00 60.19 ? 207 GLU   B OE1 1 
ATOM   4128 O  OE2 . GLU   B 1 173 ? 6.866   -0.484  32.889  1.00 67.04 ? 207 GLU   B OE2 1 
ATOM   4129 N  N   . ARG   B 1 174 ? 11.139  -1.714  33.924  1.00 34.12 ? 208 ARG   B N   1 
ATOM   4130 C  CA  . ARG   B 1 174 ? 11.912  -2.921  33.798  1.00 38.18 ? 208 ARG   B CA  1 
ATOM   4131 C  C   . ARG   B 1 174 ? 11.792  -3.343  32.357  1.00 37.26 ? 208 ARG   B C   1 
ATOM   4132 O  O   . ARG   B 1 174 ? 10.783  -3.165  31.732  1.00 39.17 ? 208 ARG   B O   1 
ATOM   4133 C  CB  . ARG   B 1 174 ? 11.419  -3.995  34.735  1.00 44.64 ? 208 ARG   B CB  1 
ATOM   4134 N  N   . VAL   B 1 175 ? 12.830  -3.936  31.829  1.00 33.56 ? 209 VAL   B N   1 
ATOM   4135 C  CA  . VAL   B 1 175 ? 12.868  -4.168  30.390  1.00 43.85 ? 209 VAL   B CA  1 
ATOM   4136 C  C   . VAL   B 1 175 ? 12.268  -5.534  30.063  1.00 58.44 ? 209 VAL   B C   1 
ATOM   4137 O  O   . VAL   B 1 175 ? 12.652  -6.554  30.656  1.00 58.27 ? 209 VAL   B O   1 
ATOM   4138 C  CB  . VAL   B 1 175 ? 14.307  -4.033  29.860  1.00 42.86 ? 209 VAL   B CB  1 
ATOM   4139 C  CG1 . VAL   B 1 175 ? 14.529  -4.833  28.648  1.00 46.26 ? 209 VAL   B CG1 1 
ATOM   4140 C  CG2 . VAL   B 1 175 ? 14.622  -2.607  29.582  1.00 31.76 ? 209 VAL   B CG2 1 
ATOM   4141 N  N   . GLU   B 1 176 ? 11.316  -5.547  29.116  1.00 60.03 ? 210 GLU   B N   1 
ATOM   4142 C  CA  . GLU   B 1 176 ? 10.636  -6.775  28.708  1.00 65.01 ? 210 GLU   B CA  1 
ATOM   4143 C  C   . GLU   B 1 176 ? 11.651  -7.812  28.245  1.00 65.21 ? 210 GLU   B C   1 
ATOM   4144 O  O   . GLU   B 1 176 ? 12.403  -7.581  27.290  1.00 65.24 ? 210 GLU   B O   1 
ATOM   4145 C  CB  . GLU   B 1 176 ? 9.627   -6.476  27.599  1.00 60.06 ? 210 GLU   B CB  1 
ATOM   4146 N  N   . ASP   B 1 177 ? 11.659  -8.960  28.919  1.00 64.25 ? 211 ASP   B N   1 
ATOM   4147 C  CA  . ASP   B 1 177 ? 12.757  -9.915  28.820  1.00 71.30 ? 211 ASP   B CA  1 
ATOM   4148 C  C   . ASP   B 1 177 ? 12.918  -10.524 27.429  1.00 65.04 ? 211 ASP   B C   1 
ATOM   4149 O  O   . ASP   B 1 177 ? 13.895  -11.248 27.216  1.00 65.10 ? 211 ASP   B O   1 
ATOM   4150 C  CB  . ASP   B 1 177 ? 12.567  -11.013 29.876  1.00 70.34 ? 211 ASP   B CB  1 
ATOM   4151 C  CG  . ASP   B 1 177 ? 12.391  -10.447 31.289  1.00 71.28 ? 211 ASP   B CG  1 
ATOM   4152 O  OD1 . ASP   B 1 177 ? 12.789  -11.130 32.260  1.00 76.10 ? 211 ASP   B OD1 1 
ATOM   4153 O  OD2 . ASP   B 1 177 ? 11.854  -9.323  31.430  1.00 68.67 ? 211 ASP   B OD2 1 
ATOM   4154 N  N   . ALA   B 1 178 ? 12.050  -10.160 26.507  1.00 64.59 ? 212 ALA   B N   1 
ATOM   4155 C  CA  . ALA   B 1 178 ? 12.040  -10.653 25.129  1.00 69.21 ? 212 ALA   B CA  1 
ATOM   4156 C  C   . ALA   B 1 178 ? 12.829  -9.797  24.185  1.00 69.92 ? 212 ALA   B C   1 
ATOM   4157 O  O   . ALA   B 1 178 ? 12.725  -9.940  22.983  1.00 66.94 ? 212 ALA   B O   1 
ATOM   4158 C  CB  . ALA   B 1 178 ? 10.608  -10.699 24.619  1.00 71.58 ? 212 ALA   B CB  1 
ATOM   4159 N  N   . SER   B 1 179 ? 13.606  -8.903  24.756  1.00 68.78 ? 213 SER   B N   1 
ATOM   4160 C  CA  . SER   B 1 179 ? 14.430  -7.942  24.033  1.00 61.57 ? 213 SER   B CA  1 
ATOM   4161 C  C   . SER   B 1 179 ? 15.772  -7.760  24.687  1.00 57.85 ? 213 SER   B C   1 
ATOM   4162 O  O   . SER   B 1 179 ? 16.634  -7.098  24.178  1.00 53.22 ? 213 SER   B O   1 
ATOM   4163 C  CB  . SER   B 1 179 ? 13.715  -6.590  24.000  1.00 62.70 ? 213 SER   B CB  1 
ATOM   4164 O  OG  . SER   B 1 179 ? 12.769  -6.434  25.051  1.00 62.33 ? 213 SER   B OG  1 
ATOM   4165 N  N   . SER   B 1 180 ? 15.913  -8.347  25.854  1.00 65.63 ? 214 SER   B N   1 
ATOM   4166 C  CA  . SER   B 1 180 ? 17.100  -8.317  26.658  1.00 61.38 ? 214 SER   B CA  1 
ATOM   4167 C  C   . SER   B 1 180 ? 17.394  -9.776  26.872  1.00 60.63 ? 214 SER   B C   1 
ATOM   4168 O  O   . SER   B 1 180 ? 16.705  -10.437 27.627  1.00 60.43 ? 214 SER   B O   1 
ATOM   4169 C  CB  . SER   B 1 180 ? 16.725  -7.742  27.983  1.00 59.08 ? 214 SER   B CB  1 
ATOM   4170 O  OG  . SER   B 1 180 ? 15.702  -8.541  28.477  1.00 60.23 ? 214 SER   B OG  1 
ATOM   4171 N  N   . PHE   B 1 181 ? 18.412  -10.248 26.178  1.00 56.10 ? 215 PHE   B N   1 
ATOM   4172 C  CA  . PHE   B 1 181 ? 18.878  -11.605 26.172  1.00 52.42 ? 215 PHE   B CA  1 
ATOM   4173 C  C   . PHE   B 1 181 ? 19.889  -11.780 27.268  1.00 55.52 ? 215 PHE   B C   1 
ATOM   4174 O  O   . PHE   B 1 181 ? 20.781  -10.995 27.389  1.00 53.95 ? 215 PHE   B O   1 
ATOM   4175 C  CB  . PHE   B 1 181 ? 19.525  -11.798 24.823  1.00 52.06 ? 215 PHE   B CB  1 
ATOM   4176 C  CG  . PHE   B 1 181 ? 20.197  -13.124 24.619  1.00 63.59 ? 215 PHE   B CG  1 
ATOM   4177 C  CD1 . PHE   B 1 181 ? 21.310  -13.482 25.338  1.00 57.84 ? 215 PHE   B CD1 1 
ATOM   4178 C  CD2 . PHE   B 1 181 ? 19.764  -13.959 23.625  1.00 53.39 ? 215 PHE   B CD2 1 
ATOM   4179 C  CE1 . PHE   B 1 181 ? 21.921  -14.675 25.120  1.00 55.13 ? 215 PHE   B CE1 1 
ATOM   4180 C  CE2 . PHE   B 1 181 ? 20.385  -15.134 23.391  1.00 51.27 ? 215 PHE   B CE2 1 
ATOM   4181 C  CZ  . PHE   B 1 181 ? 21.458  -15.494 24.141  1.00 57.85 ? 215 PHE   B CZ  1 
ATOM   4182 N  N   . PRO   B 1 182 ? 19.738  -12.816 28.079  1.00 54.46 ? 216 PRO   B N   1 
ATOM   4183 C  CA  . PRO   B 1 182 ? 20.600  -13.152 29.214  1.00 53.79 ? 216 PRO   B CA  1 
ATOM   4184 C  C   . PRO   B 1 182 ? 22.063  -13.239 28.830  1.00 49.93 ? 216 PRO   B C   1 
ATOM   4185 O  O   . PRO   B 1 182 ? 22.528  -14.274 28.465  1.00 55.88 ? 216 PRO   B O   1 
ATOM   4186 C  CB  . PRO   B 1 182 ? 20.099  -14.526 29.597  1.00 59.57 ? 216 PRO   B CB  1 
ATOM   4187 C  CG  . PRO   B 1 182 ? 19.618  -15.100 28.327  1.00 60.07 ? 216 PRO   B CG  1 
ATOM   4188 C  CD  . PRO   B 1 182 ? 18.947  -13.962 27.641  1.00 56.84 ? 216 PRO   B CD  1 
ATOM   4189 N  N   . LEU   B 1 183 ? 22.782  -12.146 28.912  1.00 45.36 ? 217 LEU   B N   1 
ATOM   4190 C  CA  . LEU   B 1 183 ? 24.167  -12.136 28.513  1.00 42.20 ? 217 LEU   B CA  1 
ATOM   4191 C  C   . LEU   B 1 183 ? 24.984  -12.030 29.713  1.00 35.27 ? 217 LEU   B C   1 
ATOM   4192 O  O   . LEU   B 1 183 ? 24.630  -11.290 30.581  1.00 39.31 ? 217 LEU   B O   1 
ATOM   4193 C  CB  . LEU   B 1 183 ? 24.466  -10.931 27.641  1.00 40.17 ? 217 LEU   B CB  1 
ATOM   4194 C  CG  . LEU   B 1 183 ? 24.297  -11.197 26.178  1.00 40.39 ? 217 LEU   B CG  1 
ATOM   4195 C  CD1 . LEU   B 1 183 ? 24.715  -10.044 25.322  1.00 29.12 ? 217 LEU   B CD1 1 
ATOM   4196 C  CD2 . LEU   B 1 183 ? 25.055  -12.437 25.838  1.00 41.44 ? 217 LEU   B CD2 1 
ATOM   4197 N  N   . ASP   B 1 184 ? 26.099  -12.734 29.720  1.00 33.17 ? 218 ASP   B N   1 
ATOM   4198 C  CA  . ASP   B 1 184 ? 26.997  -12.732 30.827  1.00 27.09 ? 218 ASP   B CA  1 
ATOM   4199 C  C   . ASP   B 1 184 ? 28.349  -13.302 30.541  1.00 28.06 ? 218 ASP   B C   1 
ATOM   4200 O  O   . ASP   B 1 184 ? 28.485  -14.454 30.251  1.00 34.97 ? 218 ASP   B O   1 
ATOM   4201 C  CB  . ASP   B 1 184 ? 26.410  -13.548 31.957  1.00 27.63 ? 218 ASP   B CB  1 
ATOM   4202 C  CG  . ASP   B 1 184 ? 27.180  -13.458 33.158  1.00 31.79 ? 218 ASP   B CG  1 
ATOM   4203 O  OD1 . ASP   B 1 184 ? 28.057  -12.652 33.222  1.00 27.28 ? 218 ASP   B OD1 1 
ATOM   4204 O  OD2 . ASP   B 1 184 ? 26.933  -14.230 34.045  1.00 38.95 ? 218 ASP   B OD2 1 
ATOM   4205 N  N   . TYR   B 1 185 ? 29.366  -12.483 30.649  1.00 24.77 ? 219 TYR   B N   1 
ATOM   4206 C  CA  . TYR   B 1 185 ? 30.719  -12.935 30.477  1.00 24.26 ? 219 TYR   B CA  1 
ATOM   4207 C  C   . TYR   B 1 185 ? 31.508  -12.902 31.794  1.00 26.67 ? 219 TYR   B C   1 
ATOM   4208 O  O   . TYR   B 1 185 ? 32.686  -12.949 31.763  1.00 24.41 ? 219 TYR   B O   1 
ATOM   4209 C  CB  . TYR   B 1 185 ? 31.468  -12.239 29.341  1.00 24.69 ? 219 TYR   B CB  1 
ATOM   4210 C  CG  . TYR   B 1 185 ? 30.707  -11.843 28.075  1.00 28.01 ? 219 TYR   B CG  1 
ATOM   4211 C  CD1 . TYR   B 1 185 ? 29.632  -12.548 27.584  1.00 24.37 ? 219 TYR   B CD1 1 
ATOM   4212 C  CD2 . TYR   B 1 185 ? 31.114  -10.765 27.363  1.00 31.54 ? 219 TYR   B CD2 1 
ATOM   4213 C  CE1 . TYR   B 1 185 ? 28.960  -12.145 26.471  1.00 26.93 ? 219 TYR   B CE1 1 
ATOM   4214 C  CE2 . TYR   B 1 185 ? 30.459  -10.364 26.245  1.00 28.11 ? 219 TYR   B CE2 1 
ATOM   4215 C  CZ  . TYR   B 1 185 ? 29.388  -11.048 25.815  1.00 30.81 ? 219 TYR   B CZ  1 
ATOM   4216 O  OH  . TYR   B 1 185 ? 28.794  -10.573 24.717  1.00 31.00 ? 219 TYR   B OH  1 
ATOM   4217 N  N   . GLY   B 1 186 ? 30.835  -12.754 32.932  1.00 23.79 ? 220 GLY   B N   1 
ATOM   4218 C  CA  . GLY   B 1 186 ? 31.425  -12.860 34.252  1.00 29.46 ? 220 GLY   B CA  1 
ATOM   4219 C  C   . GLY   B 1 186 ? 31.716  -11.563 34.998  1.00 34.98 ? 220 GLY   B C   1 
ATOM   4220 O  O   . GLY   B 1 186 ? 32.255  -11.622 36.121  1.00 35.22 ? 220 GLY   B O   1 
ATOM   4221 N  N   . ILE   B 1 187 ? 31.399  -10.398 34.429  1.00 28.18 ? 221 ILE   B N   1 
ATOM   4222 C  CA  . ILE   B 1 187 ? 31.676  -9.149  35.133  1.00 31.66 ? 221 ILE   B CA  1 
ATOM   4223 C  C   . ILE   B 1 187 ? 30.623  -8.953  36.211  1.00 30.62 ? 221 ILE   B C   1 
ATOM   4224 O  O   . ILE   B 1 187 ? 29.445  -9.285  36.027  1.00 30.26 ? 221 ILE   B O   1 
ATOM   4225 C  CB  . ILE   B 1 187 ? 31.737  -7.955  34.165  1.00 26.85 ? 221 ILE   B CB  1 
ATOM   4226 C  CG1 . ILE   B 1 187 ? 32.934  -8.115  33.217  1.00 22.22 ? 221 ILE   B CG1 1 
ATOM   4227 C  CG2 . ILE   B 1 187 ? 31.824  -6.660  34.951  1.00 21.71 ? 221 ILE   B CG2 1 
ATOM   4228 C  CD1 . ILE   B 1 187 ? 33.221  -6.891  32.389  1.00 20.47 ? 221 ILE   B CD1 1 
ATOM   4229 N  N   . ARG   B 1 188 ? 31.057  -8.447  37.356  1.00 26.62 ? 222 ARG   B N   1 
ATOM   4230 C  CA  . ARG   B 1 188 ? 30.210  -8.449  38.538  1.00 27.97 ? 222 ARG   B CA  1 
ATOM   4231 C  C   . ARG   B 1 188 ? 30.224  -7.147  39.322  1.00 29.49 ? 222 ARG   B C   1 
ATOM   4232 O  O   . ARG   B 1 188 ? 29.209  -6.828  39.947  1.00 29.37 ? 222 ARG   B O   1 
ATOM   4233 C  CB  . ARG   B 1 188 ? 30.622  -9.604  39.467  1.00 33.94 ? 222 ARG   B CB  1 
ATOM   4234 C  CG  . ARG   B 1 188 ? 30.446  -10.998 38.872  1.00 27.56 ? 222 ARG   B CG  1 
ATOM   4235 C  CD  . ARG   B 1 188 ? 28.985  -11.392 38.864  1.00 26.33 ? 222 ARG   B CD  1 
ATOM   4236 N  NE  . ARG   B 1 188 ? 28.808  -12.687 38.224  1.00 37.35 ? 222 ARG   B NE  1 
ATOM   4237 C  CZ  . ARG   B 1 188 ? 28.364  -12.874 36.982  1.00 35.30 ? 222 ARG   B CZ  1 
ATOM   4238 N  NH1 . ARG   B 1 188 ? 28.020  -11.850 36.217  1.00 28.91 ? 222 ARG   B NH1 1 
ATOM   4239 N  NH2 . ARG   B 1 188 ? 28.257  -14.102 36.506  1.00 38.78 ? 222 ARG   B NH2 1 
ATOM   4240 N  N   . ARG   B 1 189 ? 31.302  -6.368  39.296  1.00 31.32 ? 223 ARG   B N   1 
ATOM   4241 C  CA  . ARG   B 1 189 ? 31.383  -5.181  40.131  1.00 33.76 ? 223 ARG   B CA  1 
ATOM   4242 C  C   . ARG   B 1 189 ? 32.204  -4.096  39.448  1.00 35.03 ? 223 ARG   B C   1 
ATOM   4243 O  O   . ARG   B 1 189 ? 33.147  -4.387  38.703  1.00 30.86 ? 223 ARG   B O   1 
ATOM   4244 C  CB  . ARG   B 1 189 ? 32.021  -5.494  41.493  1.00 34.62 ? 223 ARG   B CB  1 
ATOM   4245 C  CG  . ARG   B 1 189 ? 31.066  -6.016  42.554  1.00 43.30 ? 223 ARG   B CG  1 
ATOM   4246 C  CD  . ARG   B 1 189 ? 31.782  -6.175  43.889  1.00 43.07 ? 223 ARG   B CD  1 
ATOM   4247 N  NE  . ARG   B 1 189 ? 32.651  -5.031  44.124  1.00 42.18 ? 223 ARG   B NE  1 
ATOM   4248 C  CZ  . ARG   B 1 189 ? 33.925  -5.123  44.486  1.00 44.29 ? 223 ARG   B CZ  1 
ATOM   4249 N  NH1 . ARG   B 1 189 ? 34.468  -6.316  44.677  1.00 51.48 ? 223 ARG   B NH1 1 
ATOM   4250 N  NH2 . ARG   B 1 189 ? 34.649  -4.022  44.666  1.00 36.71 ? 223 ARG   B NH2 1 
ATOM   4251 N  N   . LEU   B 1 190 ? 31.829  -2.838  39.716  1.00 35.17 ? 224 LEU   B N   1 
ATOM   4252 C  CA  . LEU   B 1 190 ? 32.770  -1.732  39.598  1.00 31.09 ? 224 LEU   B CA  1 
ATOM   4253 C  C   . LEU   B 1 190 ? 33.769  -1.812  40.756  1.00 33.94 ? 224 LEU   B C   1 
ATOM   4254 O  O   . LEU   B 1 190 ? 33.381  -1.904  41.924  1.00 33.41 ? 224 LEU   B O   1 
ATOM   4255 C  CB  . LEU   B 1 190 ? 32.021  -0.394  39.592  1.00 31.74 ? 224 LEU   B CB  1 
ATOM   4256 C  CG  . LEU   B 1 190 ? 32.739  0.962   39.708  1.00 28.02 ? 224 LEU   B CG  1 
ATOM   4257 C  CD1 . LEU   B 1 190 ? 33.848  1.113   38.682  1.00 34.02 ? 224 LEU   B CD1 1 
ATOM   4258 C  CD2 . LEU   B 1 190 ? 31.738  2.077   39.547  1.00 29.23 ? 224 LEU   B CD2 1 
ATOM   4259 N  N   . ASP   B 1 191 ? 35.059  -1.827  40.431  1.00 37.35 ? 225 ASP   B N   1 
ATOM   4260 C  CA  . ASP   B 1 191 ? 36.122  -1.934  41.428  1.00 34.42 ? 225 ASP   B CA  1 
ATOM   4261 C  C   . ASP   B 1 191 ? 36.849  -0.626  41.688  1.00 35.22 ? 225 ASP   B C   1 
ATOM   4262 O  O   . ASP   B 1 191 ? 37.185  -0.339  42.837  1.00 31.89 ? 225 ASP   B O   1 
ATOM   4263 C  CB  . ASP   B 1 191 ? 37.149  -2.981  41.003  1.00 32.60 ? 225 ASP   B CB  1 
ATOM   4264 C  CG  . ASP   B 1 191 ? 38.224  -3.184  42.050  1.00 38.94 ? 225 ASP   B CG  1 
ATOM   4265 O  OD1 . ASP   B 1 191 ? 38.004  -4.045  42.929  1.00 37.26 ? 225 ASP   B OD1 1 
ATOM   4266 O  OD2 . ASP   B 1 191 ? 39.272  -2.491  42.005  1.00 39.65 ? 225 ASP   B OD2 1 
ATOM   4267 N  N   . HIS   B 1 192 ? 37.150  0.156   40.653  1.00 33.29 ? 226 HIS   B N   1 
ATOM   4268 C  CA  . HIS   B 1 192 ? 37.551  1.535   40.887  1.00 34.99 ? 226 HIS   B CA  1 
ATOM   4269 C  C   . HIS   B 1 192 ? 37.238  2.363   39.652  1.00 36.54 ? 226 HIS   B C   1 
ATOM   4270 O  O   . HIS   B 1 192 ? 37.153  1.842   38.535  1.00 36.01 ? 226 HIS   B O   1 
ATOM   4271 C  CB  . HIS   B 1 192 ? 39.035  1.687   41.293  1.00 33.27 ? 226 HIS   B CB  1 
ATOM   4272 C  CG  . HIS   B 1 192 ? 40.008  0.909   40.456  1.00 34.03 ? 226 HIS   B CG  1 
ATOM   4273 N  ND1 . HIS   B 1 192 ? 40.283  -0.424  40.679  1.00 38.46 ? 226 HIS   B ND1 1 
ATOM   4274 C  CD2 . HIS   B 1 192 ? 40.819  1.294   39.439  1.00 32.65 ? 226 HIS   B CD2 1 
ATOM   4275 C  CE1 . HIS   B 1 192 ? 41.191  -0.837  39.810  1.00 36.64 ? 226 HIS   B CE1 1 
ATOM   4276 N  NE2 . HIS   B 1 192 ? 41.535  0.187   39.048  1.00 34.54 ? 226 HIS   B NE2 1 
ATOM   4277 N  N   . ALA   B 1 193 ? 37.011  3.655   39.890  1.00 34.77 ? 227 ALA   B N   1 
ATOM   4278 C  CA  . ALA   B 1 193 ? 36.874  4.665   38.853  1.00 29.15 ? 227 ALA   B CA  1 
ATOM   4279 C  C   . ALA   B 1 193 ? 38.015  5.658   39.019  1.00 30.99 ? 227 ALA   B C   1 
ATOM   4280 O  O   . ALA   B 1 193 ? 38.246  6.156   40.127  1.00 33.11 ? 227 ALA   B O   1 
ATOM   4281 C  CB  . ALA   B 1 193 ? 35.521  5.371   38.952  1.00 23.79 ? 227 ALA   B CB  1 
ATOM   4282 N  N   . VAL   B 1 194 ? 38.730  5.944   37.929  1.00 30.54 ? 228 VAL   B N   1 
ATOM   4283 C  CA  . VAL   B 1 194 ? 39.938  6.763   37.969  1.00 29.31 ? 228 VAL   B CA  1 
ATOM   4284 C  C   . VAL   B 1 194 ? 39.750  8.014   37.124  1.00 26.03 ? 228 VAL   B C   1 
ATOM   4285 O  O   . VAL   B 1 194 ? 39.161  7.957   36.039  1.00 25.50 ? 228 VAL   B O   1 
ATOM   4286 C  CB  . VAL   B 1 194 ? 41.156  5.956   37.489  1.00 29.64 ? 228 VAL   B CB  1 
ATOM   4287 C  CG1 . VAL   B 1 194 ? 42.448  6.740   37.704  1.00 27.26 ? 228 VAL   B CG1 1 
ATOM   4288 C  CG2 . VAL   B 1 194 ? 41.177  4.607   38.201  1.00 28.76 ? 228 VAL   B CG2 1 
ATOM   4289 N  N   . GLY   B 1 195 ? 40.264  9.139   37.625  1.00 31.79 ? 229 GLY   B N   1 
ATOM   4290 C  CA  . GLY   B 1 195 ? 40.195  10.420  36.925  1.00 29.02 ? 229 GLY   B CA  1 
ATOM   4291 C  C   . GLY   B 1 195 ? 41.571  10.978  36.609  1.00 28.13 ? 229 GLY   B C   1 
ATOM   4292 O  O   . GLY   B 1 195 ? 42.494  10.864  37.422  1.00 26.23 ? 229 GLY   B O   1 
ATOM   4293 N  N   . ASN   B 1 196 ? 41.702  11.568  35.412  1.00 25.57 ? 230 ASN   B N   1 
ATOM   4294 C  CA  . ASN   B 1 196 ? 42.902  12.272  34.964  1.00 26.68 ? 230 ASN   B CA  1 
ATOM   4295 C  C   . ASN   B 1 196 ? 42.747  13.777  35.194  1.00 27.69 ? 230 ASN   B C   1 
ATOM   4296 O  O   . ASN   B 1 196 ? 41.703  14.352  34.868  1.00 24.92 ? 230 ASN   B O   1 
ATOM   4297 C  CB  . ASN   B 1 196 ? 43.160  12.013  33.478  1.00 27.54 ? 230 ASN   B CB  1 
ATOM   4298 C  CG  . ASN   B 1 196 ? 43.985  10.768  33.218  1.00 31.48 ? 230 ASN   B CG  1 
ATOM   4299 O  OD1 . ASN   B 1 196 ? 44.176  9.915   34.099  1.00 32.91 ? 230 ASN   B OD1 1 
ATOM   4300 N  ND2 . ASN   B 1 196 ? 44.487  10.655  31.989  1.00 29.37 ? 230 ASN   B ND2 1 
ATOM   4301 N  N   . VAL   B 1 197 ? 43.780  14.409  35.747  1.00 27.70 ? 231 VAL   B N   1 
ATOM   4302 C  CA  . VAL   B 1 197 ? 43.726  15.831  36.096  1.00 36.29 ? 231 VAL   B CA  1 
ATOM   4303 C  C   . VAL   B 1 197 ? 45.076  16.474  35.807  1.00 38.18 ? 231 VAL   B C   1 
ATOM   4304 O  O   . VAL   B 1 197 ? 46.085  15.777  35.619  1.00 38.61 ? 231 VAL   B O   1 
ATOM   4305 C  CB  . VAL   B 1 197 ? 43.336  16.058  37.584  1.00 38.52 ? 231 VAL   B CB  1 
ATOM   4306 C  CG1 . VAL   B 1 197 ? 41.969  15.423  37.939  1.00 25.31 ? 231 VAL   B CG1 1 
ATOM   4307 C  CG2 . VAL   B 1 197 ? 44.464  15.618  38.557  1.00 35.25 ? 231 VAL   B CG2 1 
ATOM   4308 N  N   . PRO   B 1 198 ? 45.128  17.837  35.753  1.00 40.08 ? 232 PRO   B N   1 
ATOM   4309 C  CA  . PRO   B 1 198 ? 46.413  18.524  35.529  1.00 40.06 ? 232 PRO   B CA  1 
ATOM   4310 C  C   . PRO   B 1 198 ? 47.303  18.595  36.764  1.00 37.94 ? 232 PRO   B C   1 
ATOM   4311 O  O   . PRO   B 1 198 ? 48.530  18.463  36.657  1.00 33.78 ? 232 PRO   B O   1 
ATOM   4312 C  CB  . PRO   B 1 198 ? 45.986  19.926  35.068  1.00 35.06 ? 232 PRO   B CB  1 
ATOM   4313 C  CG  . PRO   B 1 198 ? 44.608  20.118  35.597  1.00 35.04 ? 232 PRO   B CG  1 
ATOM   4314 C  CD  . PRO   B 1 198 ? 43.979  18.758  35.627  1.00 39.32 ? 232 PRO   B CD  1 
ATOM   4315 N  N   . GLU   B 1 199 ? 46.697  18.794  37.936  1.00 36.47 ? 233 GLU   B N   1 
ATOM   4316 C  CA  . GLU   B 1 199 ? 47.425  18.888  39.198  1.00 34.95 ? 233 GLU   B CA  1 
ATOM   4317 C  C   . GLU   B 1 199 ? 46.754  17.988  40.225  1.00 34.97 ? 233 GLU   B C   1 
ATOM   4318 O  O   . GLU   B 1 199 ? 45.606  18.234  40.610  1.00 33.31 ? 233 GLU   B O   1 
ATOM   4319 C  CB  . GLU   B 1 199 ? 47.455  20.331  39.707  1.00 40.34 ? 233 GLU   B CB  1 
ATOM   4320 C  CG  . GLU   B 1 199 ? 48.017  21.353  38.738  1.00 43.58 ? 233 GLU   B CG  1 
ATOM   4321 C  CD  . GLU   B 1 199 ? 47.294  22.700  38.837  1.00 49.03 ? 233 GLU   B CD  1 
ATOM   4322 O  OE1 . GLU   B 1 199 ? 47.558  23.445  39.807  1.00 48.15 ? 233 GLU   B OE1 1 
ATOM   4323 O  OE2 . GLU   B 1 199 ? 46.454  23.001  37.959  1.00 43.88 ? 233 GLU   B OE2 1 
ATOM   4324 N  N   . LEU   B 1 200 ? 47.476  16.964  40.684  1.00 34.89 ? 234 LEU   B N   1 
ATOM   4325 C  CA  . LEU   B 1 200 ? 46.914  15.994  41.629  1.00 36.58 ? 234 LEU   B CA  1 
ATOM   4326 C  C   . LEU   B 1 200 ? 46.645  16.618  43.003  1.00 39.65 ? 234 LEU   B C   1 
ATOM   4327 O  O   . LEU   B 1 200 ? 45.533  16.508  43.543  1.00 36.85 ? 234 LEU   B O   1 
ATOM   4328 C  CB  . LEU   B 1 200 ? 47.871  14.809  41.752  1.00 39.19 ? 234 LEU   B CB  1 
ATOM   4329 C  CG  . LEU   B 1 200 ? 47.566  13.568  42.593  1.00 31.93 ? 234 LEU   B CG  1 
ATOM   4330 C  CD1 . LEU   B 1 200 ? 46.232  12.933  42.259  1.00 29.42 ? 234 LEU   B CD1 1 
ATOM   4331 C  CD2 . LEU   B 1 200 ? 48.674  12.595  42.359  1.00 33.96 ? 234 LEU   B CD2 1 
ATOM   4332 N  N   . GLY   B 1 201 ? 47.666  17.251  43.592  1.00 41.79 ? 235 GLY   B N   1 
ATOM   4333 C  CA  . GLY   B 1 201 ? 47.570  17.979  44.843  1.00 37.18 ? 235 GLY   B CA  1 
ATOM   4334 C  C   . GLY   B 1 201 ? 46.264  18.713  45.073  1.00 37.32 ? 235 GLY   B C   1 
ATOM   4335 O  O   . GLY   B 1 201 ? 45.559  18.474  46.056  1.00 41.49 ? 235 GLY   B O   1 
ATOM   4336 N  N   . PRO   B 1 202 ? 45.920  19.635  44.179  1.00 33.97 ? 236 PRO   B N   1 
ATOM   4337 C  CA  . PRO   B 1 202 ? 44.636  20.344  44.336  1.00 32.56 ? 236 PRO   B CA  1 
ATOM   4338 C  C   . PRO   B 1 202 ? 43.411  19.442  44.249  1.00 35.96 ? 236 PRO   B C   1 
ATOM   4339 O  O   . PRO   B 1 202 ? 42.458  19.630  45.015  1.00 35.89 ? 236 PRO   B O   1 
ATOM   4340 C  CB  . PRO   B 1 202 ? 44.666  21.372  43.196  1.00 31.41 ? 236 PRO   B CB  1 
ATOM   4341 C  CG  . PRO   B 1 202 ? 46.113  21.584  42.922  1.00 34.36 ? 236 PRO   B CG  1 
ATOM   4342 C  CD  . PRO   B 1 202 ? 46.800  20.269  43.187  1.00 29.57 ? 236 PRO   B CD  1 
ATOM   4343 N  N   . ALA   B 1 203 ? 43.399  18.465  43.336  1.00 39.98 ? 237 ALA   B N   1 
ATOM   4344 C  CA  . ALA   B 1 203 ? 42.221  17.609  43.214  1.00 36.37 ? 237 ALA   B CA  1 
ATOM   4345 C  C   . ALA   B 1 203 ? 42.074  16.703  44.430  1.00 35.62 ? 237 ALA   B C   1 
ATOM   4346 O  O   . ALA   B 1 203 ? 40.967  16.553  44.964  1.00 34.24 ? 237 ALA   B O   1 
ATOM   4347 C  CB  . ALA   B 1 203 ? 42.279  16.791  41.922  1.00 29.61 ? 237 ALA   B CB  1 
ATOM   4348 N  N   . LEU   B 1 204 ? 43.175  16.101  44.895  1.00 34.79 ? 238 LEU   B N   1 
ATOM   4349 C  CA  . LEU   B 1 204 ? 43.112  15.270  46.101  1.00 38.81 ? 238 LEU   B CA  1 
ATOM   4350 C  C   . LEU   B 1 204 ? 42.648  16.080  47.300  1.00 38.26 ? 238 LEU   B C   1 
ATOM   4351 O  O   . LEU   B 1 204 ? 41.772  15.649  48.055  1.00 37.43 ? 238 LEU   B O   1 
ATOM   4352 C  CB  . LEU   B 1 204 ? 44.477  14.653  46.407  1.00 39.76 ? 238 LEU   B CB  1 
ATOM   4353 C  CG  . LEU   B 1 204 ? 44.994  13.478  45.584  1.00 41.20 ? 238 LEU   B CG  1 
ATOM   4354 C  CD1 . LEU   B 1 204 ? 46.399  13.145  46.037  1.00 34.55 ? 238 LEU   B CD1 1 
ATOM   4355 C  CD2 . LEU   B 1 204 ? 44.072  12.271  45.686  1.00 37.62 ? 238 LEU   B CD2 1 
ATOM   4356 N  N   . THR   B 1 205 ? 43.256  17.252  47.499  1.00 38.41 ? 239 THR   B N   1 
ATOM   4357 C  CA  . THR   B 1 205 ? 42.905  18.105  48.626  1.00 42.85 ? 239 THR   B CA  1 
ATOM   4358 C  C   . THR   B 1 205 ? 41.421  18.454  48.618  1.00 41.61 ? 239 THR   B C   1 
ATOM   4359 O  O   . THR   B 1 205 ? 40.758  18.423  49.664  1.00 38.48 ? 239 THR   B O   1 
ATOM   4360 C  CB  . THR   B 1 205 ? 43.783  19.362  48.597  1.00 43.43 ? 239 THR   B CB  1 
ATOM   4361 O  OG1 . THR   B 1 205 ? 45.063  19.057  49.159  1.00 41.79 ? 239 THR   B OG1 1 
ATOM   4362 C  CG2 . THR   B 1 205 ? 43.163  20.510  49.375  1.00 44.14 ? 239 THR   B CG2 1 
ATOM   4363 N  N   . TYR   B 1 206 ? 40.878  18.776  47.449  1.00 41.25 ? 240 TYR   B N   1 
ATOM   4364 C  CA  . TYR   B 1 206 ? 39.471  19.154  47.386  1.00 41.44 ? 240 TYR   B CA  1 
ATOM   4365 C  C   . TYR   B 1 206 ? 38.556  17.952  47.629  1.00 41.21 ? 240 TYR   B C   1 
ATOM   4366 O  O   . TYR   B 1 206 ? 37.543  18.065  48.332  1.00 44.58 ? 240 TYR   B O   1 
ATOM   4367 C  CB  . TYR   B 1 206 ? 39.188  19.811  46.041  1.00 29.78 ? 240 TYR   B CB  1 
ATOM   4368 C  CG  . TYR   B 1 206 ? 37.750  19.796  45.623  1.00 35.01 ? 240 TYR   B CG  1 
ATOM   4369 C  CD1 . TYR   B 1 206 ? 36.878  20.773  46.046  1.00 35.93 ? 240 TYR   B CD1 1 
ATOM   4370 C  CD2 . TYR   B 1 206 ? 37.272  18.816  44.763  1.00 42.04 ? 240 TYR   B CD2 1 
ATOM   4371 C  CE1 . TYR   B 1 206 ? 35.562  20.776  45.640  1.00 38.01 ? 240 TYR   B CE1 1 
ATOM   4372 C  CE2 . TYR   B 1 206 ? 35.958  18.803  44.353  1.00 37.83 ? 240 TYR   B CE2 1 
ATOM   4373 C  CZ  . TYR   B 1 206 ? 35.106  19.789  44.797  1.00 39.44 ? 240 TYR   B CZ  1 
ATOM   4374 O  OH  . TYR   B 1 206 ? 33.790  19.793  44.394  1.00 39.10 ? 240 TYR   B OH  1 
ATOM   4375 N  N   . VAL   B 1 207 ? 38.914  16.790  47.097  1.00 35.11 ? 241 VAL   B N   1 
ATOM   4376 C  CA  . VAL   B 1 207 ? 38.002  15.651  47.098  1.00 40.29 ? 241 VAL   B CA  1 
ATOM   4377 C  C   . VAL   B 1 207 ? 38.076  14.846  48.396  1.00 37.15 ? 241 VAL   B C   1 
ATOM   4378 O  O   . VAL   B 1 207 ? 37.049  14.378  48.897  1.00 34.98 ? 241 VAL   B O   1 
ATOM   4379 C  CB  . VAL   B 1 207 ? 38.279  14.770  45.863  1.00 40.30 ? 241 VAL   B CB  1 
ATOM   4380 C  CG1 . VAL   B 1 207 ? 37.605  13.415  46.002  1.00 25.50 ? 241 VAL   B CG1 1 
ATOM   4381 C  CG2 . VAL   B 1 207 ? 37.804  15.487  44.600  1.00 40.79 ? 241 VAL   B CG2 1 
ATOM   4382 N  N   . ALA   B 1 208 ? 39.265  14.632  48.965  1.00 33.92 ? 242 ALA   B N   1 
ATOM   4383 C  CA  . ALA   B 1 208 ? 39.301  14.053  50.304  1.00 37.02 ? 242 ALA   B CA  1 
ATOM   4384 C  C   . ALA   B 1 208 ? 38.734  15.021  51.348  1.00 40.34 ? 242 ALA   B C   1 
ATOM   4385 O  O   . ALA   B 1 208 ? 38.279  14.578  52.407  1.00 34.92 ? 242 ALA   B O   1 
ATOM   4386 C  CB  . ALA   B 1 208 ? 40.726  13.628  50.669  1.00 29.63 ? 242 ALA   B CB  1 
ATOM   4387 N  N   . GLY   B 1 209 ? 38.712  16.323  51.047  1.00 34.76 ? 243 GLY   B N   1 
ATOM   4388 C  CA  . GLY   B 1 209 ? 38.122  17.285  51.962  1.00 38.60 ? 243 GLY   B CA  1 
ATOM   4389 C  C   . GLY   B 1 209 ? 36.631  17.086  52.186  1.00 44.48 ? 243 GLY   B C   1 
ATOM   4390 O  O   . GLY   B 1 209 ? 36.162  17.090  53.328  1.00 51.24 ? 243 GLY   B O   1 
ATOM   4391 N  N   . PHE   B 1 210 ? 35.853  16.941  51.109  1.00 41.04 ? 244 PHE   B N   1 
ATOM   4392 C  CA  . PHE   B 1 210 ? 34.409  16.892  51.302  1.00 41.71 ? 244 PHE   B CA  1 
ATOM   4393 C  C   . PHE   B 1 210 ? 33.870  15.476  51.480  1.00 44.59 ? 244 PHE   B C   1 
ATOM   4394 O  O   . PHE   B 1 210 ? 32.651  15.311  51.625  1.00 41.75 ? 244 PHE   B O   1 
ATOM   4395 C  CB  . PHE   B 1 210 ? 33.669  17.632  50.171  1.00 38.96 ? 244 PHE   B CB  1 
ATOM   4396 C  CG  . PHE   B 1 210 ? 33.603  16.908  48.842  1.00 41.23 ? 244 PHE   B CG  1 
ATOM   4397 C  CD1 . PHE   B 1 210 ? 34.386  17.331  47.766  1.00 43.64 ? 244 PHE   B CD1 1 
ATOM   4398 C  CD2 . PHE   B 1 210 ? 32.687  15.882  48.622  1.00 40.44 ? 244 PHE   B CD2 1 
ATOM   4399 C  CE1 . PHE   B 1 210 ? 34.302  16.704  46.509  1.00 34.31 ? 244 PHE   B CE1 1 
ATOM   4400 C  CE2 . PHE   B 1 210 ? 32.604  15.248  47.372  1.00 40.85 ? 244 PHE   B CE2 1 
ATOM   4401 C  CZ  . PHE   B 1 210 ? 33.411  15.667  46.315  1.00 33.97 ? 244 PHE   B CZ  1 
ATOM   4402 N  N   . THR   B 1 211 ? 34.748  14.461  51.506  1.00 38.95 ? 245 THR   B N   1 
ATOM   4403 C  CA  . THR   B 1 211 ? 34.354  13.079  51.755  1.00 43.57 ? 245 THR   B CA  1 
ATOM   4404 C  C   . THR   B 1 211 ? 35.024  12.470  52.970  1.00 42.59 ? 245 THR   B C   1 
ATOM   4405 O  O   . THR   B 1 211 ? 34.504  11.493  53.518  1.00 43.04 ? 245 THR   B O   1 
ATOM   4406 C  CB  . THR   B 1 211 ? 34.680  12.165  50.550  1.00 46.46 ? 245 THR   B CB  1 
ATOM   4407 O  OG1 . THR   B 1 211 ? 36.104  12.055  50.385  1.00 43.97 ? 245 THR   B OG1 1 
ATOM   4408 C  CG2 . THR   B 1 211 ? 34.043  12.671  49.259  1.00 38.64 ? 245 THR   B CG2 1 
ATOM   4409 N  N   . GLY   B 1 212 ? 36.164  12.995  53.391  1.00 41.20 ? 246 GLY   B N   1 
ATOM   4410 C  CA  . GLY   B 1 212 ? 36.921  12.314  54.406  1.00 39.54 ? 246 GLY   B CA  1 
ATOM   4411 C  C   . GLY   B 1 212 ? 37.489  10.999  53.956  1.00 37.92 ? 246 GLY   B C   1 
ATOM   4412 O  O   . GLY   B 1 212 ? 37.819  10.162  54.799  1.00 42.71 ? 246 GLY   B O   1 
ATOM   4413 N  N   . PHE   B 1 213 ? 37.598  10.774  52.650  1.00 38.64 ? 247 PHE   B N   1 
ATOM   4414 C  CA  . PHE   B 1 213 ? 38.278  9.574   52.175  1.00 43.51 ? 247 PHE   B CA  1 
ATOM   4415 C  C   . PHE   B 1 213 ? 39.766  9.663   52.499  1.00 42.39 ? 247 PHE   B C   1 
ATOM   4416 O  O   . PHE   B 1 213 ? 40.361  10.741  52.473  1.00 45.84 ? 247 PHE   B O   1 
ATOM   4417 C  CB  . PHE   B 1 213 ? 38.060  9.379   50.671  1.00 39.54 ? 247 PHE   B CB  1 
ATOM   4418 C  CG  . PHE   B 1 213 ? 36.651  8.972   50.307  1.00 43.16 ? 247 PHE   B CG  1 
ATOM   4419 C  CD1 . PHE   B 1 213 ? 35.694  8.746   51.290  1.00 46.75 ? 247 PHE   B CD1 1 
ATOM   4420 C  CD2 . PHE   B 1 213 ? 36.282  8.808   48.983  1.00 40.81 ? 247 PHE   B CD2 1 
ATOM   4421 C  CE1 . PHE   B 1 213 ? 34.388  8.368   50.951  1.00 45.68 ? 247 PHE   B CE1 1 
ATOM   4422 C  CE2 . PHE   B 1 213 ? 34.980  8.436   48.642  1.00 38.42 ? 247 PHE   B CE2 1 
ATOM   4423 C  CZ  . PHE   B 1 213 ? 34.036  8.218   49.623  1.00 38.62 ? 247 PHE   B CZ  1 
ATOM   4424 N  N   . HIS   B 1 214 ? 40.363  8.535   52.848  1.00 45.65 ? 248 HIS   B N   1 
ATOM   4425 C  CA  . HIS   B 1 214 ? 41.769  8.513   53.218  1.00 43.35 ? 248 HIS   B CA  1 
ATOM   4426 C  C   . HIS   B 1 214 ? 42.614  8.061   52.035  1.00 42.16 ? 248 HIS   B C   1 
ATOM   4427 O  O   . HIS   B 1 214 ? 42.113  7.464   51.082  1.00 41.99 ? 248 HIS   B O   1 
ATOM   4428 C  CB  . HIS   B 1 214 ? 41.999  7.593   54.417  1.00 43.78 ? 248 HIS   B CB  1 
ATOM   4429 C  CG  . HIS   B 1 214 ? 41.631  6.163   54.165  1.00 46.31 ? 248 HIS   B CG  1 
ATOM   4430 N  ND1 . HIS   B 1 214 ? 40.323  5.730   54.100  1.00 48.51 ? 248 HIS   B ND1 1 
ATOM   4431 C  CD2 . HIS   B 1 214 ? 42.400  5.067   53.965  1.00 50.45 ? 248 HIS   B CD2 1 
ATOM   4432 C  CE1 . HIS   B 1 214 ? 40.302  4.430   53.861  1.00 46.90 ? 248 HIS   B CE1 1 
ATOM   4433 N  NE2 . HIS   B 1 214 ? 41.549  4.003   53.774  1.00 49.15 ? 248 HIS   B NE2 1 
ATOM   4434 N  N   . GLN   B 1 215 ? 43.910  8.350   52.107  1.00 37.64 ? 249 GLN   B N   1 
ATOM   4435 C  CA  . GLN   B 1 215 ? 44.822  7.870   51.084  1.00 40.80 ? 249 GLN   B CA  1 
ATOM   4436 C  C   . GLN   B 1 215 ? 45.127  6.397   51.299  1.00 49.66 ? 249 GLN   B C   1 
ATOM   4437 O  O   . GLN   B 1 215 ? 45.395  5.956   52.421  1.00 58.51 ? 249 GLN   B O   1 
ATOM   4438 C  CB  . GLN   B 1 215 ? 46.114  8.671   51.067  1.00 44.67 ? 249 GLN   B CB  1 
ATOM   4439 C  CG  . GLN   B 1 215 ? 46.691  8.768   49.664  1.00 55.46 ? 249 GLN   B CG  1 
ATOM   4440 C  CD  . GLN   B 1 215 ? 47.925  9.654   49.575  1.00 67.24 ? 249 GLN   B CD  1 
ATOM   4441 O  OE1 . GLN   B 1 215 ? 47.939  10.790  50.078  1.00 65.93 ? 249 GLN   B OE1 1 
ATOM   4442 N  NE2 . GLN   B 1 215 ? 48.969  9.143   48.920  1.00 61.85 ? 249 GLN   B NE2 1 
ATOM   4443 N  N   . PHE   B 1 216 ? 45.085  5.640   50.218  1.00 53.52 ? 250 PHE   B N   1 
ATOM   4444 C  CA  . PHE   B 1 216 ? 45.267  4.205   50.267  1.00 50.93 ? 250 PHE   B CA  1 
ATOM   4445 C  C   . PHE   B 1 216 ? 46.755  3.882   50.199  1.00 50.91 ? 250 PHE   B C   1 
ATOM   4446 O  O   . PHE   B 1 216 ? 47.542  4.626   49.607  1.00 53.33 ? 250 PHE   B O   1 
ATOM   4447 C  CB  . PHE   B 1 216 ? 44.497  3.562   49.111  1.00 50.77 ? 250 PHE   B CB  1 
ATOM   4448 C  CG  . PHE   B 1 216 ? 44.411  2.062   49.174  1.00 52.89 ? 250 PHE   B CG  1 
ATOM   4449 C  CD1 . PHE   B 1 216 ? 45.390  1.273   48.590  1.00 54.81 ? 250 PHE   B CD1 1 
ATOM   4450 C  CD2 . PHE   B 1 216 ? 43.330  1.443   49.780  1.00 51.99 ? 250 PHE   B CD2 1 
ATOM   4451 C  CE1 . PHE   B 1 216 ? 45.308  -0.102  48.634  1.00 60.26 ? 250 PHE   B CE1 1 
ATOM   4452 C  CE2 . PHE   B 1 216 ? 43.239  0.066   49.824  1.00 55.14 ? 250 PHE   B CE2 1 
ATOM   4453 C  CZ  . PHE   B 1 216 ? 44.229  -0.709  49.252  1.00 61.47 ? 250 PHE   B CZ  1 
ATOM   4454 N  N   . ALA   B 1 217 ? 47.132  2.767   50.827  1.00 59.41 ? 251 ALA   B N   1 
ATOM   4455 C  CA  . ALA   B 1 217 ? 48.526  2.312   50.909  1.00 62.60 ? 251 ALA   B CA  1 
ATOM   4456 C  C   . ALA   B 1 217 ? 49.052  1.725   49.594  1.00 59.74 ? 251 ALA   B C   1 
ATOM   4457 O  O   . ALA   B 1 217 ? 50.112  2.126   49.090  1.00 59.52 ? 251 ALA   B O   1 
ATOM   4458 C  CB  . ALA   B 1 217 ? 48.668  1.286   52.027  1.00 56.90 ? 251 ALA   B CB  1 
ATOM   4459 N  N   . GLU   B 1 228 ? 59.464  8.828   36.997  1.00 63.44 ? 262 GLU   B N   1 
ATOM   4460 C  CA  . GLU   B 1 228 ? 58.374  7.883   36.796  1.00 63.46 ? 262 GLU   B CA  1 
ATOM   4461 C  C   . GLU   B 1 228 ? 58.207  7.583   35.310  1.00 64.44 ? 262 GLU   B C   1 
ATOM   4462 O  O   . GLU   B 1 228 ? 59.117  7.832   34.510  1.00 62.99 ? 262 GLU   B O   1 
ATOM   4463 C  CB  . GLU   B 1 228 ? 57.066  8.421   37.394  1.00 56.58 ? 262 GLU   B CB  1 
ATOM   4464 N  N   . SER   B 1 229 ? 57.049  7.034   34.945  1.00 64.82 ? 263 SER   B N   1 
ATOM   4465 C  CA  . SER   B 1 229 ? 56.749  6.650   33.568  1.00 62.91 ? 263 SER   B CA  1 
ATOM   4466 C  C   . SER   B 1 229 ? 55.553  7.424   33.026  1.00 68.04 ? 263 SER   B C   1 
ATOM   4467 O  O   . SER   B 1 229 ? 54.702  6.876   32.318  1.00 60.86 ? 263 SER   B O   1 
ATOM   4468 C  CB  . SER   B 1 229 ? 56.493  5.153   33.457  1.00 52.05 ? 263 SER   B CB  1 
ATOM   4469 O  OG  . SER   B 1 229 ? 57.342  4.441   34.329  1.00 64.72 ? 263 SER   B OG  1 
ATOM   4470 N  N   . GLY   B 1 230 ? 55.466  8.710   33.368  1.00 63.47 ? 264 GLY   B N   1 
ATOM   4471 C  CA  . GLY   B 1 230 ? 54.476  9.598   32.795  1.00 55.81 ? 264 GLY   B CA  1 
ATOM   4472 C  C   . GLY   B 1 230 ? 53.366  10.031  33.726  1.00 46.61 ? 264 GLY   B C   1 
ATOM   4473 O  O   . GLY   B 1 230 ? 52.555  10.874  33.323  1.00 45.41 ? 264 GLY   B O   1 
ATOM   4474 N  N   . LEU   B 1 231 ? 53.285  9.496   34.943  1.00 41.59 ? 265 LEU   B N   1 
ATOM   4475 C  CA  . LEU   B 1 231 ? 52.190  9.886   35.817  1.00 40.54 ? 265 LEU   B CA  1 
ATOM   4476 C  C   . LEU   B 1 231 ? 52.590  9.790   37.278  1.00 39.88 ? 265 LEU   B C   1 
ATOM   4477 O  O   . LEU   B 1 231 ? 53.568  9.135   37.645  1.00 40.45 ? 265 LEU   B O   1 
ATOM   4478 C  CB  . LEU   B 1 231 ? 50.941  9.031   35.593  1.00 41.93 ? 265 LEU   B CB  1 
ATOM   4479 C  CG  . LEU   B 1 231 ? 50.920  7.616   36.177  1.00 41.08 ? 265 LEU   B CG  1 
ATOM   4480 C  CD1 . LEU   B 1 231 ? 49.489  7.219   36.431  1.00 35.01 ? 265 LEU   B CD1 1 
ATOM   4481 C  CD2 . LEU   B 1 231 ? 51.598  6.623   35.234  1.00 41.95 ? 265 LEU   B CD2 1 
ATOM   4482 N  N   . ASN   B 1 232 ? 51.812  10.487  38.098  1.00 41.05 ? 266 ASN   B N   1 
ATOM   4483 C  CA  . ASN   B 1 232 ? 51.777  10.327  39.542  1.00 42.82 ? 266 ASN   B CA  1 
ATOM   4484 C  C   . ASN   B 1 232 ? 50.338  10.080  39.950  1.00 40.11 ? 266 ASN   B C   1 
ATOM   4485 O  O   . ASN   B 1 232 ? 49.404  10.612  39.344  1.00 42.03 ? 266 ASN   B O   1 
ATOM   4486 C  CB  . ASN   B 1 232 ? 52.274  11.559  40.298  1.00 51.52 ? 266 ASN   B CB  1 
ATOM   4487 C  CG  . ASN   B 1 232 ? 53.627  12.028  39.827  1.00 54.46 ? 266 ASN   B CG  1 
ATOM   4488 O  OD1 . ASN   B 1 232 ? 54.433  11.235  39.325  1.00 55.21 ? 266 ASN   B OD1 1 
ATOM   4489 N  ND2 . ASN   B 1 232 ? 53.891  13.329  39.989  1.00 43.94 ? 266 ASN   B ND2 1 
ATOM   4490 N  N   . SER   B 1 233 ? 50.162  9.306   41.006  1.00 40.42 ? 267 SER   B N   1 
ATOM   4491 C  CA  . SER   B 1 233 ? 48.838  8.785   41.272  1.00 41.20 ? 267 SER   B CA  1 
ATOM   4492 C  C   . SER   B 1 233 ? 48.646  8.577   42.762  1.00 42.08 ? 267 SER   B C   1 
ATOM   4493 O  O   . SER   B 1 233 ? 49.571  8.164   43.468  1.00 47.65 ? 267 SER   B O   1 
ATOM   4494 C  CB  . SER   B 1 233 ? 48.635  7.467   40.520  1.00 39.09 ? 267 SER   B CB  1 
ATOM   4495 O  OG  . SER   B 1 233 ? 47.262  7.217   40.308  1.00 40.98 ? 267 SER   B OG  1 
ATOM   4496 N  N   . ALA   B 1 234 ? 47.432  8.852   43.224  1.00 36.48 ? 268 ALA   B N   1 
ATOM   4497 C  CA  . ALA   B 1 234 ? 47.014  8.482   44.565  1.00 40.54 ? 268 ALA   B CA  1 
ATOM   4498 C  C   . ALA   B 1 234 ? 45.558  8.050   44.532  1.00 36.72 ? 268 ALA   B C   1 
ATOM   4499 O  O   . ALA   B 1 234 ? 44.781  8.465   43.667  1.00 32.25 ? 268 ALA   B O   1 
ATOM   4500 C  CB  . ALA   B 1 234 ? 47.193  9.629   45.567  1.00 46.48 ? 268 ALA   B CB  1 
ATOM   4501 N  N   . VAL   B 1 235 ? 45.198  7.213   45.492  1.00 35.96 ? 269 VAL   B N   1 
ATOM   4502 C  CA  . VAL   B 1 235 ? 43.868  6.636   45.577  1.00 35.29 ? 269 VAL   B CA  1 
ATOM   4503 C  C   . VAL   B 1 235 ? 43.178  7.209   46.807  1.00 43.70 ? 269 VAL   B C   1 
ATOM   4504 O  O   . VAL   B 1 235 ? 43.807  7.378   47.860  1.00 43.15 ? 269 VAL   B O   1 
ATOM   4505 C  CB  . VAL   B 1 235 ? 43.942  5.095   45.634  1.00 37.14 ? 269 VAL   B CB  1 
ATOM   4506 C  CG1 . VAL   B 1 235 ? 42.570  4.469   45.392  1.00 37.41 ? 269 VAL   B CG1 1 
ATOM   4507 C  CG2 . VAL   B 1 235 ? 44.947  4.573   44.612  1.00 32.24 ? 269 VAL   B CG2 1 
ATOM   4508 N  N   . LEU   B 1 236 ? 41.897  7.542   46.662  1.00 34.63 ? 270 LEU   B N   1 
ATOM   4509 C  CA  . LEU   B 1 236 ? 41.049  7.903   47.782  1.00 32.05 ? 270 LEU   B CA  1 
ATOM   4510 C  C   . LEU   B 1 236 ? 40.042  6.791   48.017  1.00 40.06 ? 270 LEU   B C   1 
ATOM   4511 O  O   . LEU   B 1 236 ? 39.528  6.201   47.059  1.00 42.46 ? 270 LEU   B O   1 
ATOM   4512 C  CB  . LEU   B 1 236 ? 40.350  9.220   47.524  1.00 34.53 ? 270 LEU   B CB  1 
ATOM   4513 C  CG  . LEU   B 1 236 ? 41.387  10.337  47.510  1.00 32.17 ? 270 LEU   B CG  1 
ATOM   4514 C  CD1 . LEU   B 1 236 ? 40.728  11.653  47.176  1.00 31.17 ? 270 LEU   B CD1 1 
ATOM   4515 C  CD2 . LEU   B 1 236 ? 42.089  10.410  48.851  1.00 33.78 ? 270 LEU   B CD2 1 
ATOM   4516 N  N   . ALA   B 1 237 ? 39.781  6.490   49.296  1.00 43.97 ? 271 ALA   B N   1 
ATOM   4517 C  CA  . ALA   B 1 237 ? 39.059  5.285   49.684  1.00 41.26 ? 271 ALA   B CA  1 
ATOM   4518 C  C   . ALA   B 1 237 ? 38.045  5.580   50.784  1.00 42.47 ? 271 ALA   B C   1 
ATOM   4519 O  O   . ALA   B 1 237 ? 38.206  6.505   51.579  1.00 44.47 ? 271 ALA   B O   1 
ATOM   4520 C  CB  . ALA   B 1 237 ? 40.024  4.192   50.155  1.00 41.58 ? 271 ALA   B CB  1 
ATOM   4521 N  N   . SER   B 1 238 ? 37.001  4.764   50.826  1.00 45.53 ? 272 SER   B N   1 
ATOM   4522 C  CA  . SER   B 1 238 ? 35.998  4.834   51.873  1.00 43.78 ? 272 SER   B CA  1 
ATOM   4523 C  C   . SER   B 1 238 ? 36.464  4.038   53.093  1.00 44.19 ? 272 SER   B C   1 
ATOM   4524 O  O   . SER   B 1 238 ? 37.550  3.454   53.102  1.00 41.39 ? 272 SER   B O   1 
ATOM   4525 C  CB  . SER   B 1 238 ? 34.660  4.317   51.350  1.00 41.60 ? 272 SER   B CB  1 
ATOM   4526 O  OG  . SER   B 1 238 ? 34.729  2.931   51.071  1.00 40.25 ? 272 SER   B OG  1 
ATOM   4527 N  N   . ASN   B 1 239 ? 35.619  4.010   54.134  1.00 47.86 ? 273 ASN   B N   1 
ATOM   4528 C  CA  . ASN   B 1 239 ? 35.991  3.374   55.401  1.00 46.47 ? 273 ASN   B CA  1 
ATOM   4529 C  C   . ASN   B 1 239 ? 36.336  1.909   55.208  1.00 40.13 ? 273 ASN   B C   1 
ATOM   4530 O  O   . ASN   B 1 239 ? 37.358  1.429   55.712  1.00 38.13 ? 273 ASN   B O   1 
ATOM   4531 C  CB  . ASN   B 1 239 ? 34.857  3.506   56.414  1.00 49.27 ? 273 ASN   B CB  1 
ATOM   4532 C  CG  . ASN   B 1 239 ? 34.823  4.854   57.078  1.00 48.51 ? 273 ASN   B CG  1 
ATOM   4533 O  OD1 . ASN   B 1 239 ? 35.564  5.758   56.705  1.00 49.82 ? 273 ASN   B OD1 1 
ATOM   4534 N  ND2 . ASN   B 1 239 ? 33.951  5.002   58.070  1.00 49.60 ? 273 ASN   B ND2 1 
ATOM   4535 N  N   . ASP   B 1 240 ? 35.480  1.180   54.498  1.00 40.33 ? 274 ASP   B N   1 
ATOM   4536 C  CA  . ASP   B 1 240 ? 35.702  -0.226  54.181  1.00 44.80 ? 274 ASP   B CA  1 
ATOM   4537 C  C   . ASP   B 1 240 ? 36.509  -0.428  52.901  1.00 42.36 ? 274 ASP   B C   1 
ATOM   4538 O  O   . ASP   B 1 240 ? 36.762  -1.576  52.529  1.00 42.53 ? 274 ASP   B O   1 
ATOM   4539 C  CB  . ASP   B 1 240 ? 34.353  -0.977  54.085  1.00 39.06 ? 274 ASP   B CB  1 
ATOM   4540 C  CG  . ASP   B 1 240 ? 33.373  -0.345  53.084  1.00 49.12 ? 274 ASP   B CG  1 
ATOM   4541 O  OD1 . ASP   B 1 240 ? 33.597  0.802   52.627  1.00 54.68 ? 274 ASP   B OD1 1 
ATOM   4542 O  OD2 . ASP   B 1 240 ? 32.348  -0.991  52.772  1.00 47.06 ? 274 ASP   B OD2 1 
ATOM   4543 N  N   . GLU   B 1 241 ? 36.903  0.659   52.221  1.00 43.67 ? 275 GLU   B N   1 
ATOM   4544 C  CA  . GLU   B 1 241 ? 37.733  0.606   51.009  1.00 45.19 ? 275 GLU   B CA  1 
ATOM   4545 C  C   . GLU   B 1 241 ? 37.082  -0.232  49.900  1.00 47.13 ? 275 GLU   B C   1 
ATOM   4546 O  O   . GLU   B 1 241 ? 37.746  -0.979  49.176  1.00 41.07 ? 275 GLU   B O   1 
ATOM   4547 C  CB  . GLU   B 1 241 ? 39.144  0.115   51.340  1.00 41.04 ? 275 GLU   B CB  1 
ATOM   4548 C  CG  . GLU   B 1 241 ? 39.781  0.945   52.447  1.00 48.75 ? 275 GLU   B CG  1 
ATOM   4549 C  CD  . GLU   B 1 241 ? 41.173  0.490   52.835  1.00 51.83 ? 275 GLU   B CD  1 
ATOM   4550 O  OE1 . GLU   B 1 241 ? 41.988  1.364   53.228  1.00 50.92 ? 275 GLU   B OE1 1 
ATOM   4551 O  OE2 . GLU   B 1 241 ? 41.445  -0.731  52.751  1.00 51.45 ? 275 GLU   B OE2 1 
ATOM   4552 N  N   . MET   B 1 242 ? 35.763  -0.084  49.758  1.00 44.42 ? 276 MET   B N   1 
ATOM   4553 C  CA  . MET   B 1 242 ? 35.011  -0.656  48.654  1.00 39.34 ? 276 MET   B CA  1 
ATOM   4554 C  C   . MET   B 1 242 ? 34.697  0.361   47.568  1.00 42.19 ? 276 MET   B C   1 
ATOM   4555 O  O   . MET   B 1 242 ? 34.416  -0.029  46.425  1.00 35.65 ? 276 MET   B O   1 
ATOM   4556 C  CB  . MET   B 1 242 ? 33.714  -1.260  49.178  1.00 39.64 ? 276 MET   B CB  1 
ATOM   4557 C  CG  . MET   B 1 242 ? 33.968  -2.434  50.096  1.00 50.08 ? 276 MET   B CG  1 
ATOM   4558 S  SD  . MET   B 1 242 ? 34.696  -3.830  49.200  1.00 62.62 ? 276 MET   B SD  1 
ATOM   4559 C  CE  . MET   B 1 242 ? 36.161  -4.114  50.176  1.00 54.47 ? 276 MET   B CE  1 
ATOM   4560 N  N   . VAL   B 1 243 ? 34.721  1.647   47.909  1.00 39.19 ? 277 VAL   B N   1 
ATOM   4561 C  CA  . VAL   B 1 243 ? 34.753  2.725   46.940  1.00 28.25 ? 277 VAL   B CA  1 
ATOM   4562 C  C   . VAL   B 1 243 ? 36.203  3.189   46.846  1.00 35.12 ? 277 VAL   B C   1 
ATOM   4563 O  O   . VAL   B 1 243 ? 36.809  3.593   47.849  1.00 37.44 ? 277 VAL   B O   1 
ATOM   4564 C  CB  . VAL   B 1 243 ? 33.784  3.850   47.336  1.00 32.49 ? 277 VAL   B CB  1 
ATOM   4565 C  CG1 . VAL   B 1 243 ? 33.981  5.101   46.482  1.00 35.15 ? 277 VAL   B CG1 1 
ATOM   4566 C  CG2 . VAL   B 1 243 ? 32.344  3.343   47.211  1.00 32.66 ? 277 VAL   B CG2 1 
ATOM   4567 N  N   . LEU   B 1 244 ? 36.786  3.049   45.658  1.00 36.01 ? 278 LEU   B N   1 
ATOM   4568 C  CA  . LEU   B 1 244 ? 38.152  3.475   45.378  1.00 37.05 ? 278 LEU   B CA  1 
ATOM   4569 C  C   . LEU   B 1 244 ? 38.137  4.464   44.222  1.00 36.82 ? 278 LEU   B C   1 
ATOM   4570 O  O   . LEU   B 1 244 ? 37.561  4.175   43.169  1.00 36.16 ? 278 LEU   B O   1 
ATOM   4571 C  CB  . LEU   B 1 244 ? 39.037  2.283   45.025  1.00 33.94 ? 278 LEU   B CB  1 
ATOM   4572 C  CG  . LEU   B 1 244 ? 39.251  1.205   46.084  1.00 36.89 ? 278 LEU   B CG  1 
ATOM   4573 C  CD1 . LEU   B 1 244 ? 39.655  -0.076  45.411  1.00 28.16 ? 278 LEU   B CD1 1 
ATOM   4574 C  CD2 . LEU   B 1 244 ? 40.324  1.658   47.071  1.00 41.05 ? 278 LEU   B CD2 1 
ATOM   4575 N  N   . LEU   B 1 245 ? 38.781  5.620   44.411  1.00 33.96 ? 279 LEU   B N   1 
ATOM   4576 C  CA  . LEU   B 1 245 ? 38.822  6.681   43.404  1.00 28.01 ? 279 LEU   B CA  1 
ATOM   4577 C  C   . LEU   B 1 245 ? 40.241  7.180   43.198  1.00 29.48 ? 279 LEU   B C   1 
ATOM   4578 O  O   . LEU   B 1 245 ? 40.624  8.231   43.727  1.00 31.07 ? 279 LEU   B O   1 
ATOM   4579 C  CB  . LEU   B 1 245 ? 37.923  7.838   43.808  1.00 32.25 ? 279 LEU   B CB  1 
ATOM   4580 C  CG  . LEU   B 1 245 ? 36.503  7.382   44.072  1.00 34.15 ? 279 LEU   B CG  1 
ATOM   4581 C  CD1 . LEU   B 1 245 ? 35.732  8.554   44.629  1.00 28.55 ? 279 LEU   B CD1 1 
ATOM   4582 C  CD2 . LEU   B 1 245 ? 35.901  6.850   42.779  1.00 25.20 ? 279 LEU   B CD2 1 
ATOM   4583 N  N   . PRO   B 1 246 ? 41.036  6.475   42.400  1.00 30.67 ? 280 PRO   B N   1 
ATOM   4584 C  CA  . PRO   B 1 246 ? 42.384  6.958   42.085  1.00 32.95 ? 280 PRO   B CA  1 
ATOM   4585 C  C   . PRO   B 1 246 ? 42.334  8.200   41.211  1.00 33.81 ? 280 PRO   B C   1 
ATOM   4586 O  O   . PRO   B 1 246 ? 41.372  8.422   40.469  1.00 36.14 ? 280 PRO   B O   1 
ATOM   4587 C  CB  . PRO   B 1 246 ? 43.012  5.778   41.327  1.00 37.77 ? 280 PRO   B CB  1 
ATOM   4588 C  CG  . PRO   B 1 246 ? 42.141  4.591   41.654  1.00 30.33 ? 280 PRO   B CG  1 
ATOM   4589 C  CD  . PRO   B 1 246 ? 40.769  5.168   41.785  1.00 31.55 ? 280 PRO   B CD  1 
ATOM   4590 N  N   . ILE   B 1 247 ? 43.387  9.018   41.301  1.00 35.54 ? 281 ILE   B N   1 
ATOM   4591 C  CA  . ILE   B 1 247 ? 43.514  10.216  40.468  1.00 34.59 ? 281 ILE   B CA  1 
ATOM   4592 C  C   . ILE   B 1 247 ? 44.956  10.340  39.983  1.00 40.48 ? 281 ILE   B C   1 
ATOM   4593 O  O   . ILE   B 1 247 ? 45.900  10.148  40.760  1.00 41.14 ? 281 ILE   B O   1 
ATOM   4594 C  CB  . ILE   B 1 247 ? 43.069  11.485  41.218  1.00 26.32 ? 281 ILE   B CB  1 
ATOM   4595 C  CG1 . ILE   B 1 247 ? 41.631  11.315  41.720  1.00 28.58 ? 281 ILE   B CG1 1 
ATOM   4596 C  CG2 . ILE   B 1 247 ? 43.159  12.689  40.300  1.00 23.34 ? 281 ILE   B CG2 1 
ATOM   4597 C  CD1 . ILE   B 1 247 ? 41.205  12.323  42.785  1.00 34.02 ? 281 ILE   B CD1 1 
ATOM   4598 N  N   . ASN   B 1 248 ? 45.128  10.637  38.692  1.00 34.28 ? 282 ASN   B N   1 
ATOM   4599 C  CA  . ASN   B 1 248 ? 46.452  10.761  38.103  1.00 33.63 ? 282 ASN   B CA  1 
ATOM   4600 C  C   . ASN   B 1 248 ? 46.673  12.168  37.577  1.00 37.62 ? 282 ASN   B C   1 
ATOM   4601 O  O   . ASN   B 1 248 ? 45.732  12.890  37.223  1.00 30.06 ? 282 ASN   B O   1 
ATOM   4602 C  CB  . ASN   B 1 248 ? 46.679  9.789   36.938  1.00 35.64 ? 282 ASN   B CB  1 
ATOM   4603 C  CG  . ASN   B 1 248 ? 46.080  8.436   37.179  1.00 35.47 ? 282 ASN   B CG  1 
ATOM   4604 O  OD1 . ASN   B 1 248 ? 46.030  7.958   38.311  1.00 38.15 ? 282 ASN   B OD1 1 
ATOM   4605 N  ND2 . ASN   B 1 248 ? 45.609  7.802   36.111  1.00 31.68 ? 282 ASN   B ND2 1 
ATOM   4606 N  N   . GLU   B 1 249 ? 47.946  12.528  37.510  1.00 38.01 ? 283 GLU   B N   1 
ATOM   4607 C  CA  . GLU   B 1 249 ? 48.421  13.729  36.848  1.00 37.54 ? 283 GLU   B CA  1 
ATOM   4608 C  C   . GLU   B 1 249 ? 49.587  13.341  35.955  1.00 37.61 ? 283 GLU   B C   1 
ATOM   4609 O  O   . GLU   B 1 249 ? 50.152  12.253  36.102  1.00 39.21 ? 283 GLU   B O   1 
ATOM   4610 C  CB  . GLU   B 1 249 ? 48.843  14.804  37.866  1.00 38.98 ? 283 GLU   B CB  1 
ATOM   4611 C  CG  . GLU   B 1 249 ? 50.116  14.512  38.651  1.00 40.14 ? 283 GLU   B CG  1 
ATOM   4612 C  CD  . GLU   B 1 249 ? 50.574  15.702  39.494  1.00 44.16 ? 283 GLU   B CD  1 
ATOM   4613 O  OE1 . GLU   B 1 249 ? 51.683  15.620  40.061  1.00 52.81 ? 283 GLU   B OE1 1 
ATOM   4614 O  OE2 . GLU   B 1 249 ? 49.836  16.715  39.590  1.00 41.52 ? 283 GLU   B OE2 1 
ATOM   4615 N  N   . PRO   B 1 250 ? 49.961  14.196  35.010  1.00 34.10 ? 284 PRO   B N   1 
ATOM   4616 C  CA  . PRO   B 1 250 ? 51.071  13.873  34.116  1.00 36.63 ? 284 PRO   B CA  1 
ATOM   4617 C  C   . PRO   B 1 250 ? 52.428  14.207  34.721  1.00 38.39 ? 284 PRO   B C   1 
ATOM   4618 O  O   . PRO   B 1 250 ? 52.567  15.051  35.606  1.00 41.07 ? 284 PRO   B O   1 
ATOM   4619 C  CB  . PRO   B 1 250 ? 50.804  14.759  32.890  1.00 43.35 ? 284 PRO   B CB  1 
ATOM   4620 C  CG  . PRO   B 1 250 ? 49.491  15.446  33.136  1.00 33.68 ? 284 PRO   B CG  1 
ATOM   4621 C  CD  . PRO   B 1 250 ? 49.291  15.441  34.601  1.00 36.52 ? 284 PRO   B CD  1 
ATOM   4622 N  N   . VAL   B 1 251 ? 53.445  13.537  34.190  1.00 42.85 ? 285 VAL   B N   1 
ATOM   4623 C  CA  . VAL   B 1 251 ? 54.846  13.834  34.462  1.00 48.49 ? 285 VAL   B CA  1 
ATOM   4624 C  C   . VAL   B 1 251 ? 55.478  14.219  33.132  1.00 58.24 ? 285 VAL   B C   1 
ATOM   4625 O  O   . VAL   B 1 251 ? 55.636  13.369  32.245  1.00 63.20 ? 285 VAL   B O   1 
ATOM   4626 C  CB  . VAL   B 1 251 ? 55.577  12.643  35.093  1.00 50.67 ? 285 VAL   B CB  1 
ATOM   4627 C  CG1 . VAL   B 1 251 ? 57.081  12.873  35.066  1.00 49.09 ? 285 VAL   B CG1 1 
ATOM   4628 C  CG2 . VAL   B 1 251 ? 55.080  12.400  36.509  1.00 39.93 ? 285 VAL   B CG2 1 
ATOM   4629 N  N   . HIS   B 1 252 ? 55.853  15.487  32.992  1.00 65.99 ? 286 HIS   B N   1 
ATOM   4630 C  CA  . HIS   B 1 252 ? 56.258  16.049  31.711  1.00 66.35 ? 286 HIS   B CA  1 
ATOM   4631 C  C   . HIS   B 1 252 ? 57.771  16.027  31.532  1.00 68.80 ? 286 HIS   B C   1 
ATOM   4632 O  O   . HIS   B 1 252 ? 58.538  15.763  32.463  1.00 69.55 ? 286 HIS   B O   1 
ATOM   4633 C  CB  . HIS   B 1 252 ? 55.738  17.481  31.574  1.00 65.50 ? 286 HIS   B CB  1 
ATOM   4634 C  CG  . HIS   B 1 252 ? 54.275  17.557  31.290  1.00 63.55 ? 286 HIS   B CG  1 
ATOM   4635 N  ND1 . HIS   B 1 252 ? 53.368  18.091  32.182  1.00 59.71 ? 286 HIS   B ND1 1 
ATOM   4636 C  CD2 . HIS   B 1 252 ? 53.556  17.147  30.218  1.00 60.57 ? 286 HIS   B CD2 1 
ATOM   4637 C  CE1 . HIS   B 1 252 ? 52.154  18.022  31.662  1.00 59.21 ? 286 HIS   B CE1 1 
ATOM   4638 N  NE2 . HIS   B 1 252 ? 52.240  17.450  30.473  1.00 59.70 ? 286 HIS   B NE2 1 
ATOM   4639 N  N   . GLY   B 1 253 ? 58.192  16.336  30.302  1.00 75.67 ? 287 GLY   B N   1 
ATOM   4640 C  CA  . GLY   B 1 253 ? 59.591  16.347  29.918  1.00 81.56 ? 287 GLY   B CA  1 
ATOM   4641 C  C   . GLY   B 1 253 ? 60.201  14.985  29.675  1.00 84.82 ? 287 GLY   B C   1 
ATOM   4642 O  O   . GLY   B 1 253 ? 61.342  14.910  29.192  1.00 84.95 ? 287 GLY   B O   1 
ATOM   4643 N  N   . THR   B 1 254 ? 59.473  13.910  29.975  1.00 81.82 ? 288 THR   B N   1 
ATOM   4644 C  CA  . THR   B 1 254 ? 59.982  12.550  29.908  1.00 82.81 ? 288 THR   B CA  1 
ATOM   4645 C  C   . THR   B 1 254 ? 60.391  12.178  28.477  1.00 83.82 ? 288 THR   B C   1 
ATOM   4646 O  O   . THR   B 1 254 ? 60.108  12.894  27.508  1.00 83.94 ? 288 THR   B O   1 
ATOM   4647 C  CB  . THR   B 1 254 ? 58.927  11.580  30.444  1.00 84.07 ? 288 THR   B CB  1 
ATOM   4648 O  OG1 . THR   B 1 254 ? 57.623  11.994  29.999  1.00 77.61 ? 288 THR   B OG1 1 
ATOM   4649 C  CG2 . THR   B 1 254 ? 58.954  11.557  31.970  1.00 71.37 ? 288 THR   B CG2 1 
ATOM   4650 N  N   . LYS   B 1 255 ? 61.072  11.031  28.360  1.00 82.45 ? 289 LYS   B N   1 
ATOM   4651 C  CA  . LYS   B 1 255 ? 61.587  10.575  27.068  1.00 82.52 ? 289 LYS   B CA  1 
ATOM   4652 C  C   . LYS   B 1 255 ? 60.459  10.391  26.057  1.00 87.55 ? 289 LYS   B C   1 
ATOM   4653 O  O   . LYS   B 1 255 ? 60.490  10.962  24.961  1.00 89.69 ? 289 LYS   B O   1 
ATOM   4654 C  CB  . LYS   B 1 255 ? 62.375  9.276   27.246  1.00 70.67 ? 289 LYS   B CB  1 
ATOM   4655 N  N   . ARG   B 1 256 ? 59.465  9.578   26.401  1.00 87.80 ? 290 ARG   B N   1 
ATOM   4656 C  CA  . ARG   B 1 256 ? 58.183  9.601   25.712  1.00 82.87 ? 290 ARG   B CA  1 
ATOM   4657 C  C   . ARG   B 1 256 ? 57.265  10.627  26.379  1.00 80.90 ? 290 ARG   B C   1 
ATOM   4658 O  O   . ARG   B 1 256 ? 57.521  11.087  27.496  1.00 84.36 ? 290 ARG   B O   1 
ATOM   4659 C  CB  . ARG   B 1 256 ? 57.538  8.214   25.725  1.00 84.28 ? 290 ARG   B CB  1 
ATOM   4660 N  N   . LYS   B 1 257 ? 56.195  11.001  25.677  1.00 73.92 ? 291 LYS   B N   1 
ATOM   4661 C  CA  . LYS   B 1 257 ? 55.232  11.948  26.229  1.00 67.68 ? 291 LYS   B CA  1 
ATOM   4662 C  C   . LYS   B 1 257 ? 54.168  11.208  27.027  1.00 62.27 ? 291 LYS   B C   1 
ATOM   4663 O  O   . LYS   B 1 257 ? 53.797  10.076  26.704  1.00 61.94 ? 291 LYS   B O   1 
ATOM   4664 C  CB  . LYS   B 1 257 ? 54.569  12.783  25.132  1.00 57.78 ? 291 LYS   B CB  1 
ATOM   4665 N  N   . SER   B 1 258 ? 53.672  11.865  28.074  1.00 56.93 ? 292 SER   B N   1 
ATOM   4666 C  CA  . SER   B 1 258 ? 52.801  11.203  29.036  1.00 52.60 ? 292 SER   B CA  1 
ATOM   4667 C  C   . SER   B 1 258 ? 51.405  10.963  28.462  1.00 49.09 ? 292 SER   B C   1 
ATOM   4668 O  O   . SER   B 1 258 ? 50.735  11.886  27.975  1.00 42.99 ? 292 SER   B O   1 
ATOM   4669 C  CB  . SER   B 1 258 ? 52.712  12.008  30.333  1.00 50.75 ? 292 SER   B CB  1 
ATOM   4670 O  OG  . SER   B 1 258 ? 52.724  13.397  30.070  1.00 54.00 ? 292 SER   B OG  1 
ATOM   4671 N  N   . GLN   B 1 259 ? 50.991  9.696   28.521  1.00 44.00 ? 293 GLN   B N   1 
ATOM   4672 C  CA  . GLN   B 1 259 ? 49.635  9.287   28.197  1.00 38.13 ? 293 GLN   B CA  1 
ATOM   4673 C  C   . GLN   B 1 259 ? 48.609  10.103  28.968  1.00 39.40 ? 293 GLN   B C   1 
ATOM   4674 O  O   . GLN   B 1 259 ? 47.513  10.371  28.454  1.00 43.25 ? 293 GLN   B O   1 
ATOM   4675 C  CB  . GLN   B 1 259 ? 49.481  7.792   28.509  1.00 46.18 ? 293 GLN   B CB  1 
ATOM   4676 C  CG  . GLN   B 1 259 ? 49.823  7.456   29.982  1.00 52.69 ? 293 GLN   B CG  1 
ATOM   4677 C  CD  . GLN   B 1 259 ? 50.639  6.201   30.171  1.00 53.65 ? 293 GLN   B CD  1 
ATOM   4678 O  OE1 . GLN   B 1 259 ? 51.490  5.847   29.338  1.00 64.10 ? 293 GLN   B OE1 1 
ATOM   4679 N  NE2 . GLN   B 1 259 ? 50.429  5.545   31.305  1.00 49.40 ? 293 GLN   B NE2 1 
ATOM   4680 N  N   . ILE   B 1 260 ? 48.924  10.489  30.205  1.00 35.04 ? 294 ILE   B N   1 
ATOM   4681 C  CA  . ILE   B 1 260 ? 48.012  11.358  30.933  1.00 34.26 ? 294 ILE   B CA  1 
ATOM   4682 C  C   . ILE   B 1 260 ? 47.837  12.659  30.171  1.00 37.35 ? 294 ILE   B C   1 
ATOM   4683 O  O   . ILE   B 1 260 ? 46.711  13.142  29.978  1.00 38.39 ? 294 ILE   B O   1 
ATOM   4684 C  CB  . ILE   B 1 260 ? 48.517  11.599  32.367  1.00 38.51 ? 294 ILE   B CB  1 
ATOM   4685 C  CG1 . ILE   B 1 260 ? 48.803  10.264  33.056  1.00 39.32 ? 294 ILE   B CG1 1 
ATOM   4686 C  CG2 . ILE   B 1 260 ? 47.487  12.381  33.169  1.00 31.53 ? 294 ILE   B CG2 1 
ATOM   4687 C  CD1 . ILE   B 1 260 ? 47.598  9.371   33.189  1.00 28.95 ? 294 ILE   B CD1 1 
ATOM   4688 N  N   . GLN   B 1 261 ? 48.945  13.220  29.680  1.00 38.04 ? 295 GLN   B N   1 
ATOM   4689 C  CA  . GLN   B 1 261 ? 48.866  14.483  28.955  1.00 42.03 ? 295 GLN   B CA  1 
ATOM   4690 C  C   . GLN   B 1 261 ? 48.029  14.344  27.693  1.00 41.88 ? 295 GLN   B C   1 
ATOM   4691 O  O   . GLN   B 1 261 ? 47.219  15.223  27.377  1.00 38.15 ? 295 GLN   B O   1 
ATOM   4692 C  CB  . GLN   B 1 261 ? 50.267  14.983  28.616  1.00 43.47 ? 295 GLN   B CB  1 
ATOM   4693 C  CG  . GLN   B 1 261 ? 50.297  16.296  27.846  1.00 42.95 ? 295 GLN   B CG  1 
ATOM   4694 C  CD  . GLN   B 1 261 ? 49.631  17.441  28.585  1.00 44.32 ? 295 GLN   B CD  1 
ATOM   4695 O  OE1 . GLN   B 1 261 ? 49.275  17.321  29.757  1.00 42.31 ? 295 GLN   B OE1 1 
ATOM   4696 N  NE2 . GLN   B 1 261 ? 49.458  18.564  27.896  1.00 43.06 ? 295 GLN   B NE2 1 
ATOM   4697 N  N   . THR   B 1 262 ? 48.209  13.239  26.965  1.00 39.10 ? 296 THR   B N   1 
ATOM   4698 C  CA  . THR   B 1 262 ? 47.419  13.011  25.763  1.00 38.79 ? 296 THR   B CA  1 
ATOM   4699 C  C   . THR   B 1 262 ? 45.932  12.955  26.084  1.00 32.84 ? 296 THR   B C   1 
ATOM   4700 O  O   . THR   B 1 262 ? 45.100  13.460  25.318  1.00 28.33 ? 296 THR   B O   1 
ATOM   4701 C  CB  . THR   B 1 262 ? 47.881  11.723  25.086  1.00 37.65 ? 296 THR   B CB  1 
ATOM   4702 O  OG1 . THR   B 1 262 ? 49.258  11.856  24.725  1.00 35.92 ? 296 THR   B OG1 1 
ATOM   4703 C  CG2 . THR   B 1 262 ? 47.042  11.423  23.847  1.00 28.14 ? 296 THR   B CG2 1 
ATOM   4704 N  N   . TYR   B 1 263 ? 45.577  12.347  27.213  1.00 29.19 ? 297 TYR   B N   1 
ATOM   4705 C  CA  . TYR   B 1 263 ? 44.176  12.324  27.601  1.00 28.74 ? 297 TYR   B CA  1 
ATOM   4706 C  C   . TYR   B 1 263 ? 43.626  13.740  27.690  1.00 30.40 ? 297 TYR   B C   1 
ATOM   4707 O  O   . TYR   B 1 263 ? 42.600  14.057  27.082  1.00 29.43 ? 297 TYR   B O   1 
ATOM   4708 C  CB  . TYR   B 1 263 ? 44.001  11.589  28.934  1.00 26.22 ? 297 TYR   B CB  1 
ATOM   4709 C  CG  . TYR   B 1 263 ? 42.583  11.645  29.438  1.00 24.95 ? 297 TYR   B CG  1 
ATOM   4710 C  CD1 . TYR   B 1 263 ? 42.113  12.760  30.128  1.00 26.44 ? 297 TYR   B CD1 1 
ATOM   4711 C  CD2 . TYR   B 1 263 ? 41.710  10.589  29.230  1.00 26.16 ? 297 TYR   B CD2 1 
ATOM   4712 C  CE1 . TYR   B 1 263 ? 40.828  12.829  30.579  1.00 26.69 ? 297 TYR   B CE1 1 
ATOM   4713 C  CE2 . TYR   B 1 263 ? 40.403  10.644  29.687  1.00 26.06 ? 297 TYR   B CE2 1 
ATOM   4714 C  CZ  . TYR   B 1 263 ? 39.966  11.773  30.359  1.00 26.36 ? 297 TYR   B CZ  1 
ATOM   4715 O  OH  . TYR   B 1 263 ? 38.668  11.857  30.813  1.00 22.74 ? 297 TYR   B OH  1 
ATOM   4716 N  N   . LEU   B 1 264 ? 44.307  14.607  28.455  1.00 33.89 ? 298 LEU   B N   1 
ATOM   4717 C  CA  . LEU   B 1 264 ? 43.760  15.924  28.782  1.00 31.28 ? 298 LEU   B CA  1 
ATOM   4718 C  C   . LEU   B 1 264 ? 43.569  16.767  27.533  1.00 28.77 ? 298 LEU   B C   1 
ATOM   4719 O  O   . LEU   B 1 264 ? 42.590  17.515  27.416  1.00 28.04 ? 298 LEU   B O   1 
ATOM   4720 C  CB  . LEU   B 1 264 ? 44.685  16.633  29.774  1.00 33.94 ? 298 LEU   B CB  1 
ATOM   4721 C  CG  . LEU   B 1 264 ? 44.763  16.014  31.171  1.00 35.51 ? 298 LEU   B CG  1 
ATOM   4722 C  CD1 . LEU   B 1 264 ? 46.043  16.415  31.882  1.00 34.99 ? 298 LEU   B CD1 1 
ATOM   4723 C  CD2 . LEU   B 1 264 ? 43.531  16.417  31.982  1.00 30.12 ? 298 LEU   B CD2 1 
ATOM   4724 N  N   . GLU   B 1 265 ? 44.508  16.666  26.596  1.00 28.32 ? 299 GLU   B N   1 
ATOM   4725 C  CA  . GLU   B 1 265 ? 44.386  17.339  25.311  1.00 29.34 ? 299 GLU   B CA  1 
ATOM   4726 C  C   . GLU   B 1 265 ? 43.131  16.893  24.566  1.00 33.44 ? 299 GLU   B C   1 
ATOM   4727 O  O   . GLU   B 1 265 ? 42.254  17.712  24.246  1.00 29.94 ? 299 GLU   B O   1 
ATOM   4728 C  CB  . GLU   B 1 265 ? 45.645  17.071  24.486  1.00 34.78 ? 299 GLU   B CB  1 
ATOM   4729 C  CG  . GLU   B 1 265 ? 46.903  17.587  25.179  1.00 40.77 ? 299 GLU   B CG  1 
ATOM   4730 C  CD  . GLU   B 1 265 ? 48.197  17.193  24.492  1.00 46.41 ? 299 GLU   B CD  1 
ATOM   4731 O  OE1 . GLU   B 1 265 ? 48.158  16.580  23.396  1.00 46.11 ? 299 GLU   B OE1 1 
ATOM   4732 O  OE2 . GLU   B 1 265 ? 49.261  17.504  25.066  1.00 47.85 ? 299 GLU   B OE2 1 
ATOM   4733 N  N   . HIS   B 1 266 ? 43.021  15.586  24.282  1.00 30.94 ? 300 HIS   B N   1 
ATOM   4734 C  CA  . HIS   B 1 266 ? 41.885  15.108  23.506  1.00 25.68 ? 300 HIS   B CA  1 
ATOM   4735 C  C   . HIS   B 1 266 ? 40.576  15.107  24.292  1.00 28.83 ? 300 HIS   B C   1 
ATOM   4736 O  O   . HIS   B 1 266 ? 39.503  15.111  23.672  1.00 29.85 ? 300 HIS   B O   1 
ATOM   4737 C  CB  . HIS   B 1 266 ? 42.183  13.728  22.955  1.00 24.11 ? 300 HIS   B CB  1 
ATOM   4738 C  CG  . HIS   B 1 266 ? 43.294  13.725  21.951  1.00 33.78 ? 300 HIS   B CG  1 
ATOM   4739 N  ND1 . HIS   B 1 266 ? 43.075  13.619  20.592  1.00 30.80 ? 300 HIS   B ND1 1 
ATOM   4740 C  CD2 . HIS   B 1 266 ? 44.637  13.824  22.109  1.00 33.89 ? 300 HIS   B CD2 1 
ATOM   4741 C  CE1 . HIS   B 1 266 ? 44.235  13.654  19.959  1.00 31.32 ? 300 HIS   B CE1 1 
ATOM   4742 N  NE2 . HIS   B 1 266 ? 45.198  13.770  20.856  1.00 32.96 ? 300 HIS   B NE2 1 
ATOM   4743 N  N   . ASN   B 1 267 ? 40.621  15.133  25.627  1.00 24.03 ? 301 ASN   B N   1 
ATOM   4744 C  CA  . ASN   B 1 267 ? 39.391  15.300  26.387  1.00 24.79 ? 301 ASN   B CA  1 
ATOM   4745 C  C   . ASN   B 1 267 ? 39.022  16.767  26.652  1.00 27.42 ? 301 ASN   B C   1 
ATOM   4746 O  O   . ASN   B 1 267 ? 37.940  17.032  27.192  1.00 25.56 ? 301 ASN   B O   1 
ATOM   4747 C  CB  . ASN   B 1 267 ? 39.476  14.552  27.721  1.00 24.20 ? 301 ASN   B CB  1 
ATOM   4748 C  CG  . ASN   B 1 267 ? 38.118  14.422  28.375  1.00 24.51 ? 301 ASN   B CG  1 
ATOM   4749 O  OD1 . ASN   B 1 267 ? 37.144  14.154  27.687  1.00 25.34 ? 301 ASN   B OD1 1 
ATOM   4750 N  ND2 . ASN   B 1 267 ? 38.028  14.686  29.672  1.00 22.21 ? 301 ASN   B ND2 1 
ATOM   4751 N  N   . GLU   B 1 268 ? 39.859  17.724  26.268  1.00 27.78 ? 302 GLU   B N   1 
ATOM   4752 C  CA  . GLU   B 1 268 ? 39.689  19.111  26.689  1.00 28.40 ? 302 GLU   B CA  1 
ATOM   4753 C  C   . GLU   B 1 268 ? 39.518  19.189  28.208  1.00 27.88 ? 302 GLU   B C   1 
ATOM   4754 O  O   . GLU   B 1 268 ? 38.529  19.704  28.729  1.00 30.25 ? 302 GLU   B O   1 
ATOM   4755 C  CB  . GLU   B 1 268 ? 38.507  19.779  25.981  1.00 27.75 ? 302 GLU   B CB  1 
ATOM   4756 C  CG  . GLU   B 1 268 ? 38.718  20.128  24.519  1.00 34.05 ? 302 GLU   B CG  1 
ATOM   4757 C  CD  . GLU   B 1 268 ? 37.454  20.725  23.893  1.00 37.72 ? 302 GLU   B CD  1 
ATOM   4758 O  OE1 . GLU   B 1 268 ? 36.503  20.980  24.663  1.00 38.48 ? 302 GLU   B OE1 1 
ATOM   4759 O  OE2 . GLU   B 1 268 ? 37.394  20.921  22.652  1.00 32.74 ? 302 GLU   B OE2 1 
ATOM   4760 N  N   . GLY   B 1 269 ? 40.489  18.641  28.917  1.00 23.81 ? 303 GLY   B N   1 
ATOM   4761 C  CA  . GLY   B 1 269 ? 40.590  18.839  30.344  1.00 24.18 ? 303 GLY   B CA  1 
ATOM   4762 C  C   . GLY   B 1 269 ? 40.423  17.556  31.139  1.00 30.43 ? 303 GLY   B C   1 
ATOM   4763 O  O   . GLY   B 1 269 ? 40.234  16.463  30.604  1.00 28.46 ? 303 GLY   B O   1 
ATOM   4764 N  N   . ALA   B 1 270 ? 40.524  17.726  32.455  1.00 22.89 ? 304 ALA   B N   1 
ATOM   4765 C  CA  . ALA   B 1 270 ? 40.197  16.723  33.444  1.00 24.95 ? 304 ALA   B CA  1 
ATOM   4766 C  C   . ALA   B 1 270 ? 38.961  15.917  33.068  1.00 31.93 ? 304 ALA   B C   1 
ATOM   4767 O  O   . ALA   B 1 270 ? 37.999  16.452  32.504  1.00 30.41 ? 304 ALA   B O   1 
ATOM   4768 C  CB  . ALA   B 1 270 ? 39.983  17.388  34.800  1.00 23.39 ? 304 ALA   B CB  1 
ATOM   4769 N  N   . GLY   B 1 271 ? 38.989  14.628  33.390  1.00 30.07 ? 305 GLY   B N   1 
ATOM   4770 C  CA  . GLY   B 1 271 ? 37.856  13.755  33.158  1.00 25.17 ? 305 GLY   B CA  1 
ATOM   4771 C  C   . GLY   B 1 271 ? 38.162  12.368  33.678  1.00 28.20 ? 305 GLY   B C   1 
ATOM   4772 O  O   . GLY   B 1 271 ? 39.252  12.090  34.204  1.00 27.57 ? 305 GLY   B O   1 
ATOM   4773 N  N   . LEU   B 1 272 ? 37.182  11.488  33.507  1.00 23.49 ? 306 LEU   B N   1 
ATOM   4774 C  CA  . LEU   B 1 272 ? 37.311  10.115  33.984  1.00 25.63 ? 306 LEU   B CA  1 
ATOM   4775 C  C   . LEU   B 1 272 ? 38.173  9.292   33.016  1.00 25.92 ? 306 LEU   B C   1 
ATOM   4776 O  O   . LEU   B 1 272 ? 37.797  9.045   31.863  1.00 21.30 ? 306 LEU   B O   1 
ATOM   4777 C  CB  . LEU   B 1 272 ? 35.927  9.510   34.181  1.00 21.54 ? 306 LEU   B CB  1 
ATOM   4778 C  CG  . LEU   B 1 272 ? 35.953  8.152   34.849  1.00 24.90 ? 306 LEU   B CG  1 
ATOM   4779 C  CD1 . LEU   B 1 272 ? 34.892  8.074   35.920  1.00 22.75 ? 306 LEU   B CD1 1 
ATOM   4780 C  CD2 . LEU   B 1 272 ? 35.732  7.106   33.768  1.00 32.13 ? 306 LEU   B CD2 1 
ATOM   4781 N  N   . GLN   B 1 273 ? 39.336  8.857   33.491  1.00 24.88 ? 307 GLN   B N   1 
ATOM   4782 C  CA  . GLN   B 1 273 ? 40.235  8.099   32.636  1.00 27.22 ? 307 GLN   B CA  1 
ATOM   4783 C  C   . GLN   B 1 273 ? 39.690  6.698   32.371  1.00 31.59 ? 307 GLN   B C   1 
ATOM   4784 O  O   . GLN   B 1 273 ? 39.347  6.392   31.223  1.00 29.38 ? 307 GLN   B O   1 
ATOM   4785 C  CB  . GLN   B 1 273 ? 41.635  8.025   33.247  1.00 26.31 ? 307 GLN   B CB  1 
ATOM   4786 C  CG  . GLN   B 1 273 ? 42.628  7.233   32.409  1.00 24.63 ? 307 GLN   B CG  1 
ATOM   4787 C  CD  . GLN   B 1 273 ? 43.731  6.639   33.256  1.00 26.13 ? 307 GLN   B CD  1 
ATOM   4788 O  OE1 . GLN   B 1 273 ? 43.533  6.381   34.439  1.00 31.78 ? 307 GLN   B OE1 1 
ATOM   4789 N  NE2 . GLN   B 1 273 ? 44.909  6.461   32.673  1.00 22.95 ? 307 GLN   B NE2 1 
ATOM   4790 N  N   . HIS   B 1 274 ? 39.604  5.830   33.393  1.00 29.38 ? 308 HIS   B N   1 
ATOM   4791 C  CA  . HIS   B 1 274 ? 39.181  4.456   33.134  1.00 27.32 ? 308 HIS   B CA  1 
ATOM   4792 C  C   . HIS   B 1 274 ? 38.284  3.903   34.239  1.00 28.59 ? 308 HIS   B C   1 
ATOM   4793 O  O   . HIS   B 1 274 ? 38.282  4.370   35.379  1.00 31.16 ? 308 HIS   B O   1 
ATOM   4794 C  CB  . HIS   B 1 274 ? 40.378  3.532   32.898  1.00 23.93 ? 308 HIS   B CB  1 
ATOM   4795 C  CG  . HIS   B 1 274 ? 41.127  3.146   34.132  1.00 27.08 ? 308 HIS   B CG  1 
ATOM   4796 N  ND1 . HIS   B 1 274 ? 42.382  3.637   34.421  1.00 29.67 ? 308 HIS   B ND1 1 
ATOM   4797 C  CD2 . HIS   B 1 274 ? 40.830  2.270   35.122  1.00 27.92 ? 308 HIS   B CD2 1 
ATOM   4798 C  CE1 . HIS   B 1 274 ? 42.814  3.109   35.551  1.00 28.00 ? 308 HIS   B CE1 1 
ATOM   4799 N  NE2 . HIS   B 1 274 ? 41.892  2.273   35.996  1.00 33.82 ? 308 HIS   B NE2 1 
ATOM   4800 N  N   . LEU   B 1 275 ? 37.481  2.920   33.859  1.00 22.64 ? 309 LEU   B N   1 
ATOM   4801 C  CA  . LEU   B 1 275 ? 36.626  2.180   34.776  1.00 27.98 ? 309 LEU   B CA  1 
ATOM   4802 C  C   . LEU   B 1 275 ? 37.155  0.754   34.855  1.00 25.21 ? 309 LEU   B C   1 
ATOM   4803 O  O   . LEU   B 1 275 ? 37.506  0.167   33.829  1.00 27.13 ? 309 LEU   B O   1 
ATOM   4804 C  CB  . LEU   B 1 275 ? 35.170  2.184   34.294  1.00 27.35 ? 309 LEU   B CB  1 
ATOM   4805 C  CG  . LEU   B 1 275 ? 34.443  3.514   34.086  1.00 27.82 ? 309 LEU   B CG  1 
ATOM   4806 C  CD1 . LEU   B 1 275 ? 33.276  3.356   33.124  1.00 25.50 ? 309 LEU   B CD1 1 
ATOM   4807 C  CD2 . LEU   B 1 275 ? 33.936  4.040   35.418  1.00 30.23 ? 309 LEU   B CD2 1 
ATOM   4808 N  N   . ALA   B 1 276 ? 37.240  0.201   36.057  1.00 25.21 ? 310 ALA   B N   1 
ATOM   4809 C  CA  . ALA   B 1 276 ? 37.808  -1.125  36.244  1.00 22.60 ? 310 ALA   B CA  1 
ATOM   4810 C  C   . ALA   B 1 276 ? 36.691  -2.050  36.691  1.00 29.77 ? 310 ALA   B C   1 
ATOM   4811 O  O   . ALA   B 1 276 ? 36.043  -1.794  37.711  1.00 35.00 ? 310 ALA   B O   1 
ATOM   4812 C  CB  . ALA   B 1 276 ? 38.955  -1.111  37.254  1.00 26.68 ? 310 ALA   B CB  1 
ATOM   4813 N  N   . LEU   B 1 277 ? 36.459  -3.113  35.930  1.00 27.56 ? 311 LEU   B N   1 
ATOM   4814 C  CA  . LEU   B 1 277 ? 35.358  -4.029  36.193  1.00 29.20 ? 311 LEU   B CA  1 
ATOM   4815 C  C   . LEU   B 1 277 ? 35.901  -5.337  36.767  1.00 30.71 ? 311 LEU   B C   1 
ATOM   4816 O  O   . LEU   B 1 277 ? 36.816  -5.941  36.189  1.00 28.14 ? 311 LEU   B O   1 
ATOM   4817 C  CB  . LEU   B 1 277 ? 34.555  -4.258  34.908  1.00 27.10 ? 311 LEU   B CB  1 
ATOM   4818 C  CG  . LEU   B 1 277 ? 34.346  -2.930  34.144  1.00 26.44 ? 311 LEU   B CG  1 
ATOM   4819 C  CD1 . LEU   B 1 277 ? 33.523  -3.154  32.905  1.00 26.47 ? 311 LEU   B CD1 1 
ATOM   4820 C  CD2 . LEU   B 1 277 ? 33.680  -1.852  34.999  1.00 21.11 ? 311 LEU   B CD2 1 
ATOM   4821 N  N   . MET   B 1 278 ? 35.356  -5.748  37.923  1.00 30.98 ? 312 MET   B N   1 
ATOM   4822 C  CA  . MET   B 1 278 ? 35.771  -6.969  38.608  1.00 31.31 ? 312 MET   B CA  1 
ATOM   4823 C  C   . MET   B 1 278 ? 35.088  -8.186  38.010  1.00 27.83 ? 312 MET   B C   1 
ATOM   4824 O  O   . MET   B 1 278 ? 33.862  -8.220  37.881  1.00 26.68 ? 312 MET   B O   1 
ATOM   4825 C  CB  . MET   B 1 278 ? 35.455  -6.926  40.101  1.00 35.12 ? 312 MET   B CB  1 
ATOM   4826 C  CG  . MET   B 1 278 ? 35.713  -8.283  40.786  1.00 32.54 ? 312 MET   B CG  1 
ATOM   4827 S  SD  . MET   B 1 278 ? 36.613  -8.102  42.328  1.00 45.40 ? 312 MET   B SD  1 
ATOM   4828 C  CE  . MET   B 1 278 ? 38.214  -7.625  41.696  1.00 40.85 ? 312 MET   B CE  1 
ATOM   4829 N  N   . SER   B 1 279 ? 35.886  -9.195  37.688  1.00 28.03 ? 313 SER   B N   1 
ATOM   4830 C  CA  . SER   B 1 279 ? 35.405  -10.438 37.104  1.00 36.07 ? 313 SER   B CA  1 
ATOM   4831 C  C   . SER   B 1 279 ? 35.546  -11.576 38.105  1.00 41.21 ? 313 SER   B C   1 
ATOM   4832 O  O   . SER   B 1 279 ? 36.581  -11.701 38.773  1.00 38.45 ? 313 SER   B O   1 
ATOM   4833 C  CB  . SER   B 1 279 ? 36.185  -10.790 35.840  1.00 31.81 ? 313 SER   B CB  1 
ATOM   4834 O  OG  . SER   B 1 279 ? 35.876  -12.103 35.443  1.00 33.85 ? 313 SER   B OG  1 
ATOM   4835 N  N   . GLU   B 1 280 ? 34.503  -12.407 38.209  1.00 35.91 ? 314 GLU   B N   1 
ATOM   4836 C  CA  . GLU   B 1 280 ? 34.621  -13.608 39.022  1.00 36.53 ? 314 GLU   B CA  1 
ATOM   4837 C  C   . GLU   B 1 280 ? 35.421  -14.701 38.330  1.00 40.18 ? 314 GLU   B C   1 
ATOM   4838 O  O   . GLU   B 1 280 ? 35.642  -15.748 38.933  1.00 48.19 ? 314 GLU   B O   1 
ATOM   4839 C  CB  . GLU   B 1 280 ? 33.241  -14.142 39.415  1.00 38.90 ? 314 GLU   B CB  1 
ATOM   4840 C  CG  . GLU   B 1 280 ? 32.325  -14.463 38.247  1.00 48.09 ? 314 GLU   B CG  1 
ATOM   4841 C  CD  . GLU   B 1 280 ? 31.061  -15.215 38.666  1.00 56.01 ? 314 GLU   B CD  1 
ATOM   4842 O  OE1 . GLU   B 1 280 ? 30.503  -14.922 39.761  1.00 51.85 ? 314 GLU   B OE1 1 
ATOM   4843 O  OE2 . GLU   B 1 280 ? 30.629  -16.099 37.885  1.00 58.35 ? 314 GLU   B OE2 1 
ATOM   4844 N  N   . ASP   B 1 281 ? 35.855  -14.479 37.087  1.00 46.50 ? 315 ASP   B N   1 
ATOM   4845 C  CA  . ASP   B 1 281 ? 36.739  -15.377 36.343  1.00 47.02 ? 315 ASP   B CA  1 
ATOM   4846 C  C   . ASP   B 1 281 ? 37.296  -14.610 35.145  1.00 43.74 ? 315 ASP   B C   1 
ATOM   4847 O  O   . ASP   B 1 281 ? 36.695  -14.599 34.062  1.00 40.84 ? 315 ASP   B O   1 
ATOM   4848 C  CB  . ASP   B 1 281 ? 36.003  -16.652 35.901  1.00 39.49 ? 315 ASP   B CB  1 
ATOM   4849 C  CG  . ASP   B 1 281 ? 36.922  -17.667 35.226  1.00 45.96 ? 315 ASP   B CG  1 
ATOM   4850 O  OD1 . ASP   B 1 281 ? 38.143  -17.438 35.163  1.00 53.10 ? 315 ASP   B OD1 1 
ATOM   4851 O  OD2 . ASP   B 1 281 ? 36.426  -18.713 34.759  1.00 54.14 ? 315 ASP   B OD2 1 
ATOM   4852 N  N   . ILE   B 1 282 ? 38.445  -13.955 35.341  1.00 40.63 ? 316 ILE   B N   1 
ATOM   4853 C  CA  . ILE   B 1 282 ? 38.953  -13.017 34.344  1.00 40.35 ? 316 ILE   B CA  1 
ATOM   4854 C  C   . ILE   B 1 282 ? 39.282  -13.728 33.040  1.00 38.45 ? 316 ILE   B C   1 
ATOM   4855 O  O   . ILE   B 1 282 ? 39.274  -13.107 31.968  1.00 36.37 ? 316 ILE   B O   1 
ATOM   4856 C  CB  . ILE   B 1 282 ? 40.179  -12.264 34.891  1.00 36.89 ? 316 ILE   B CB  1 
ATOM   4857 C  CG1 . ILE   B 1 282 ? 40.430  -11.008 34.055  1.00 31.20 ? 316 ILE   B CG1 1 
ATOM   4858 C  CG2 . ILE   B 1 282 ? 41.410  -13.182 34.909  1.00 35.81 ? 316 ILE   B CG2 1 
ATOM   4859 C  CD1 . ILE   B 1 282 ? 41.774  -10.340 34.300  1.00 27.60 ? 316 ILE   B CD1 1 
ATOM   4860 N  N   . PHE   B 1 283 ? 39.568  -15.033 33.103  1.00 41.83 ? 317 PHE   B N   1 
ATOM   4861 C  CA  . PHE   B 1 283 ? 39.886  -15.789 31.895  1.00 38.06 ? 317 PHE   B CA  1 
ATOM   4862 C  C   . PHE   B 1 283 ? 38.630  -16.061 31.080  1.00 36.58 ? 317 PHE   B C   1 
ATOM   4863 O  O   . PHE   B 1 283 ? 38.660  -15.999 29.847  1.00 30.93 ? 317 PHE   B O   1 
ATOM   4864 C  CB  . PHE   B 1 283 ? 40.595  -17.093 32.261  1.00 40.83 ? 317 PHE   B CB  1 
ATOM   4865 C  CG  . PHE   B 1 283 ? 41.959  -16.898 32.856  1.00 43.98 ? 317 PHE   B CG  1 
ATOM   4866 C  CD1 . PHE   B 1 283 ? 43.096  -17.154 32.118  1.00 52.91 ? 317 PHE   B CD1 1 
ATOM   4867 C  CD2 . PHE   B 1 283 ? 42.106  -16.441 34.152  1.00 51.81 ? 317 PHE   B CD2 1 
ATOM   4868 C  CE1 . PHE   B 1 283 ? 44.363  -16.967 32.675  1.00 58.41 ? 317 PHE   B CE1 1 
ATOM   4869 C  CE2 . PHE   B 1 283 ? 43.364  -16.258 34.722  1.00 55.81 ? 317 PHE   B CE2 1 
ATOM   4870 C  CZ  . PHE   B 1 283 ? 44.492  -16.519 33.982  1.00 53.92 ? 317 PHE   B CZ  1 
ATOM   4871 N  N   . ARG   B 1 284 ? 37.514  -16.360 31.751  1.00 36.44 ? 318 ARG   B N   1 
ATOM   4872 C  CA  . ARG   B 1 284 ? 36.233  -16.458 31.058  1.00 37.59 ? 318 ARG   B CA  1 
ATOM   4873 C  C   . ARG   B 1 284 ? 35.865  -15.132 30.402  1.00 37.89 ? 318 ARG   B C   1 
ATOM   4874 O  O   . ARG   B 1 284 ? 35.422  -15.092 29.244  1.00 39.50 ? 318 ARG   B O   1 
ATOM   4875 C  CB  . ARG   B 1 284 ? 35.146  -16.881 32.047  1.00 42.97 ? 318 ARG   B CB  1 
ATOM   4876 C  CG  . ARG   B 1 284 ? 33.728  -16.988 31.483  1.00 38.30 ? 318 ARG   B CG  1 
ATOM   4877 C  CD  . ARG   B 1 284 ? 32.704  -16.968 32.634  1.00 44.85 ? 318 ARG   B CD  1 
ATOM   4878 N  NE  . ARG   B 1 284 ? 31.317  -17.007 32.165  1.00 48.59 ? 318 ARG   B NE  1 
ATOM   4879 C  CZ  . ARG   B 1 284 ? 30.250  -16.918 32.958  1.00 44.16 ? 318 ARG   B CZ  1 
ATOM   4880 N  NH1 . ARG   B 1 284 ? 30.403  -16.785 34.269  1.00 41.16 ? 318 ARG   B NH1 1 
ATOM   4881 N  NH2 . ARG   B 1 284 ? 29.024  -16.960 32.441  1.00 40.31 ? 318 ARG   B NH2 1 
ATOM   4882 N  N   . THR   B 1 285 ? 36.040  -14.034 31.130  1.00 31.95 ? 319 THR   B N   1 
ATOM   4883 C  CA  . THR   B 1 285 ? 35.645  -12.738 30.608  1.00 29.11 ? 319 THR   B CA  1 
ATOM   4884 C  C   . THR   B 1 285 ? 36.477  -12.361 29.398  1.00 27.02 ? 319 THR   B C   1 
ATOM   4885 O  O   . THR   B 1 285 ? 35.936  -11.943 28.370  1.00 24.11 ? 319 THR   B O   1 
ATOM   4886 C  CB  . THR   B 1 285 ? 35.782  -11.698 31.704  1.00 30.16 ? 319 THR   B CB  1 
ATOM   4887 O  OG1 . THR   B 1 285 ? 34.872  -12.023 32.762  1.00 25.70 ? 319 THR   B OG1 1 
ATOM   4888 C  CG2 . THR   B 1 285 ? 35.489  -10.322 31.146  1.00 24.68 ? 319 THR   B CG2 1 
ATOM   4889 N  N   . LEU   B 1 286 ? 37.794  -12.530 29.503  1.00 26.41 ? 320 LEU   B N   1 
ATOM   4890 C  CA  . LEU   B 1 286 ? 38.692  -12.185 28.411  1.00 24.79 ? 320 LEU   B CA  1 
ATOM   4891 C  C   . LEU   B 1 286 ? 38.416  -13.012 27.172  1.00 31.57 ? 320 LEU   B C   1 
ATOM   4892 O  O   . LEU   B 1 286 ? 38.435  -12.483 26.052  1.00 35.24 ? 320 LEU   B O   1 
ATOM   4893 C  CB  . LEU   B 1 286 ? 40.139  -12.373 28.841  1.00 26.83 ? 320 LEU   B CB  1 
ATOM   4894 C  CG  . LEU   B 1 286 ? 40.750  -11.015 29.149  1.00 38.23 ? 320 LEU   B CG  1 
ATOM   4895 C  CD1 . LEU   B 1 286 ? 40.953  -10.323 27.825  1.00 37.91 ? 320 LEU   B CD1 1 
ATOM   4896 C  CD2 . LEU   B 1 286 ? 39.841  -10.187 30.056  1.00 29.18 ? 320 LEU   B CD2 1 
ATOM   4897 N  N   . ARG   B 1 287 ? 38.193  -14.317 27.346  1.00 30.46 ? 321 ARG   B N   1 
ATOM   4898 C  CA  . ARG   B 1 287 ? 37.875  -15.166 26.206  1.00 30.06 ? 321 ARG   B CA  1 
ATOM   4899 C  C   . ARG   B 1 287 ? 36.645  -14.650 25.496  1.00 31.78 ? 321 ARG   B C   1 
ATOM   4900 O  O   . ARG   B 1 287 ? 36.680  -14.387 24.289  1.00 34.82 ? 321 ARG   B O   1 
ATOM   4901 C  CB  . ARG   B 1 287 ? 37.652  -16.620 26.639  1.00 37.48 ? 321 ARG   B CB  1 
ATOM   4902 C  CG  . ARG   B 1 287 ? 38.915  -17.429 26.862  1.00 35.92 ? 321 ARG   B CG  1 
ATOM   4903 C  CD  . ARG   B 1 287 ? 38.652  -18.917 26.757  1.00 39.35 ? 321 ARG   B CD  1 
ATOM   4904 N  NE  . ARG   B 1 287 ? 39.367  -19.652 27.792  1.00 44.90 ? 321 ARG   B NE  1 
ATOM   4905 C  CZ  . ARG   B 1 287 ? 38.846  -19.966 28.973  1.00 49.76 ? 321 ARG   B CZ  1 
ATOM   4906 N  NH1 . ARG   B 1 287 ? 37.596  -19.616 29.272  1.00 45.13 ? 321 ARG   B NH1 1 
ATOM   4907 N  NH2 . ARG   B 1 287 ? 39.575  -20.634 29.856  1.00 61.97 ? 321 ARG   B NH2 1 
ATOM   4908 N  N   . GLU   B 1 288 ? 35.545  -14.485 26.238  1.00 33.18 ? 322 GLU   B N   1 
ATOM   4909 C  CA  . GLU   B 1 288 ? 34.307  -14.019 25.622  1.00 31.33 ? 322 GLU   B CA  1 
ATOM   4910 C  C   . GLU   B 1 288 ? 34.515  -12.675 24.942  1.00 27.88 ? 322 GLU   B C   1 
ATOM   4911 O  O   . GLU   B 1 288 ? 34.101  -12.480 23.795  1.00 29.41 ? 322 GLU   B O   1 
ATOM   4912 C  CB  . GLU   B 1 288 ? 33.188  -13.942 26.663  1.00 29.94 ? 322 GLU   B CB  1 
ATOM   4913 C  CG  . GLU   B 1 288 ? 32.793  -15.296 27.247  1.00 31.49 ? 322 GLU   B CG  1 
ATOM   4914 C  CD  . GLU   B 1 288 ? 32.553  -16.365 26.170  1.00 37.71 ? 322 GLU   B CD  1 
ATOM   4915 O  OE1 . GLU   B 1 288 ? 31.860  -16.076 25.169  1.00 35.38 ? 322 GLU   B OE1 1 
ATOM   4916 O  OE2 . GLU   B 1 288 ? 33.062  -17.504 26.325  1.00 43.63 ? 322 GLU   B OE2 1 
ATOM   4917 N  N   . MET   B 1 289 ? 35.187  -11.744 25.627  1.00 26.98 ? 323 MET   B N   1 
ATOM   4918 C  CA  . MET   B 1 289 ? 35.413  -10.424 25.052  1.00 25.90 ? 323 MET   B CA  1 
ATOM   4919 C  C   . MET   B 1 289 ? 36.295  -10.505 23.811  1.00 26.73 ? 323 MET   B C   1 
ATOM   4920 O  O   . MET   B 1 289 ? 35.943  -9.969  22.753  1.00 25.15 ? 323 MET   B O   1 
ATOM   4921 C  CB  . MET   B 1 289 ? 36.019  -9.495  26.100  1.00 20.86 ? 323 MET   B CB  1 
ATOM   4922 C  CG  . MET   B 1 289 ? 35.027  -9.136  27.177  1.00 26.31 ? 323 MET   B CG  1 
ATOM   4923 S  SD  . MET   B 1 289 ? 35.516  -7.820  28.304  1.00 26.32 ? 323 MET   B SD  1 
ATOM   4924 C  CE  . MET   B 1 289 ? 35.571  -6.448  27.135  1.00 18.94 ? 323 MET   B CE  1 
ATOM   4925 N  N   . ARG   B 1 290 ? 37.440  -11.183 23.912  1.00 27.48 ? 324 ARG   B N   1 
ATOM   4926 C  CA  . ARG   B 1 290 ? 38.319  -11.269 22.755  1.00 27.21 ? 324 ARG   B CA  1 
ATOM   4927 C  C   . ARG   B 1 290 ? 37.607  -11.903 21.568  1.00 27.80 ? 324 ARG   B C   1 
ATOM   4928 O  O   . ARG   B 1 290 ? 37.818  -11.490 20.421  1.00 23.56 ? 324 ARG   B O   1 
ATOM   4929 C  CB  . ARG   B 1 290 ? 39.578  -12.042 23.107  1.00 23.51 ? 324 ARG   B CB  1 
ATOM   4930 C  CG  . ARG   B 1 290 ? 40.505  -11.313 24.010  1.00 23.51 ? 324 ARG   B CG  1 
ATOM   4931 C  CD  . ARG   B 1 290 ? 41.871  -11.904 23.857  1.00 25.68 ? 324 ARG   B CD  1 
ATOM   4932 N  NE  . ARG   B 1 290 ? 42.866  -11.125 24.558  1.00 29.17 ? 324 ARG   B NE  1 
ATOM   4933 C  CZ  . ARG   B 1 290 ? 43.657  -10.243 23.967  1.00 31.77 ? 324 ARG   B CZ  1 
ATOM   4934 N  NH1 . ARG   B 1 290 ? 43.559  -10.050 22.667  1.00 28.38 ? 324 ARG   B NH1 1 
ATOM   4935 N  NH2 . ARG   B 1 290 ? 44.552  -9.561  24.675  1.00 39.13 ? 324 ARG   B NH2 1 
ATOM   4936 N  N   . LYS   B 1 291 ? 36.734  -12.886 21.835  1.00 27.65 ? 325 LYS   B N   1 
ATOM   4937 C  CA  . LYS   B 1 291 ? 35.942  -13.518 20.782  1.00 24.18 ? 325 LYS   B CA  1 
ATOM   4938 C  C   . LYS   B 1 291 ? 35.115  -12.512 19.997  1.00 28.44 ? 325 LYS   B C   1 
ATOM   4939 O  O   . LYS   B 1 291 ? 34.808  -12.760 18.832  1.00 39.44 ? 325 LYS   B O   1 
ATOM   4940 C  CB  . LYS   B 1 291 ? 35.016  -14.590 21.371  1.00 26.58 ? 325 LYS   B CB  1 
ATOM   4941 C  CG  . LYS   B 1 291 ? 35.735  -15.897 21.683  1.00 35.99 ? 325 LYS   B CG  1 
ATOM   4942 C  CD  . LYS   B 1 291 ? 34.827  -17.098 21.683  1.00 35.73 ? 325 LYS   B CD  1 
ATOM   4943 C  CE  . LYS   B 1 291 ? 34.159  -17.292 23.020  1.00 38.20 ? 325 LYS   B CE  1 
ATOM   4944 N  NZ  . LYS   B 1 291 ? 33.641  -18.677 23.081  1.00 46.22 ? 325 LYS   B NZ  1 
ATOM   4945 N  N   . ARG   B 1 292 ? 34.737  -11.383 20.599  1.00 23.26 ? 326 ARG   B N   1 
ATOM   4946 C  CA  . ARG   B 1 292 ? 33.832  -10.451 19.946  1.00 24.30 ? 326 ARG   B CA  1 
ATOM   4947 C  C   . ARG   B 1 292 ? 34.486  -9.129  19.565  1.00 27.02 ? 326 ARG   B C   1 
ATOM   4948 O  O   . ARG   B 1 292 ? 33.781  -8.220  19.115  1.00 25.61 ? 326 ARG   B O   1 
ATOM   4949 C  CB  . ARG   B 1 292 ? 32.626  -10.184 20.832  1.00 23.42 ? 326 ARG   B CB  1 
ATOM   4950 C  CG  . ARG   B 1 292 ? 31.736  -11.363 21.041  1.00 18.86 ? 326 ARG   B CG  1 
ATOM   4951 C  CD  . ARG   B 1 292 ? 30.941  -11.164 22.301  1.00 21.81 ? 326 ARG   B CD  1 
ATOM   4952 N  NE  . ARG   B 1 292 ? 29.925  -12.183 22.486  1.00 28.45 ? 326 ARG   B NE  1 
ATOM   4953 C  CZ  . ARG   B 1 292 ? 30.129  -13.347 23.094  1.00 29.77 ? 326 ARG   B CZ  1 
ATOM   4954 N  NH1 . ARG   B 1 292 ? 31.321  -13.638 23.597  1.00 25.63 ? 326 ARG   B NH1 1 
ATOM   4955 N  NH2 . ARG   B 1 292 ? 29.135  -14.217 23.194  1.00 29.72 ? 326 ARG   B NH2 1 
ATOM   4956 N  N   . SER   B 1 293 ? 35.808  -9.010  19.711  1.00 25.24 ? 327 SER   B N   1 
ATOM   4957 C  CA  . SER   B 1 293 ? 36.502  -7.763  19.403  1.00 22.91 ? 327 SER   B CA  1 
ATOM   4958 C  C   . SER   B 1 293 ? 36.224  -7.297  17.980  1.00 26.55 ? 327 SER   B C   1 
ATOM   4959 O  O   . SER   B 1 293 ? 35.741  -6.175  17.757  1.00 27.07 ? 327 SER   B O   1 
ATOM   4960 C  CB  . SER   B 1 293 ? 37.999  -7.939  19.613  1.00 21.97 ? 327 SER   B CB  1 
ATOM   4961 O  OG  . SER   B 1 293 ? 38.227  -8.566  20.848  1.00 28.75 ? 327 SER   B OG  1 
ATOM   4962 N  N   . SER   B 1 294 ? 36.553  -8.125  16.996  1.00 26.10 ? 328 SER   B N   1 
ATOM   4963 C  CA  . SER   B 1 294 ? 36.379  -7.668  15.624  1.00 25.62 ? 328 SER   B CA  1 
ATOM   4964 C  C   . SER   B 1 294 ? 34.956  -7.831  15.104  1.00 22.97 ? 328 SER   B C   1 
ATOM   4965 O  O   . SER   B 1 294 ? 34.746  -7.627  13.908  1.00 26.21 ? 328 SER   B O   1 
ATOM   4966 C  CB  . SER   B 1 294 ? 37.363  -8.377  14.705  1.00 26.65 ? 328 SER   B CB  1 
ATOM   4967 O  OG  . SER   B 1 294 ? 38.683  -8.022  15.054  1.00 30.25 ? 328 SER   B OG  1 
ATOM   4968 N  N   . ILE   B 1 295 ? 33.977  -8.147  15.957  1.00 19.94 ? 329 ILE   B N   1 
ATOM   4969 C  CA  . ILE   B 1 295 ? 32.587  -8.241  15.515  1.00 20.96 ? 329 ILE   B CA  1 
ATOM   4970 C  C   . ILE   B 1 295 ? 31.684  -7.420  16.421  1.00 23.05 ? 329 ILE   B C   1 
ATOM   4971 O  O   . ILE   B 1 295 ? 30.562  -7.841  16.740  1.00 23.36 ? 329 ILE   B O   1 
ATOM   4972 C  CB  . ILE   B 1 295 ? 32.074  -9.697  15.439  1.00 20.69 ? 329 ILE   B CB  1 
ATOM   4973 C  CG1 . ILE   B 1 295 ? 32.261  -10.430 16.764  1.00 22.59 ? 329 ILE   B CG1 1 
ATOM   4974 C  CG2 . ILE   B 1 295 ? 32.751  -10.458 14.318  1.00 22.36 ? 329 ILE   B CG2 1 
ATOM   4975 C  CD1 . ILE   B 1 295 ? 31.660  -11.791 16.756  1.00 16.51 ? 329 ILE   B CD1 1 
ATOM   4976 N  N   . GLY   B 1 296 ? 32.165  -6.247  16.838  1.00 23.20 ? 330 GLY   B N   1 
ATOM   4977 C  CA  . GLY   B 1 296 ? 31.331  -5.225  17.450  1.00 19.94 ? 330 GLY   B CA  1 
ATOM   4978 C  C   . GLY   B 1 296 ? 31.717  -4.823  18.858  1.00 22.92 ? 330 GLY   B C   1 
ATOM   4979 O  O   . GLY   B 1 296 ? 31.207  -3.802  19.348  1.00 21.03 ? 330 GLY   B O   1 
ATOM   4980 N  N   . GLY   B 1 297 ? 32.596  -5.561  19.528  1.00 24.58 ? 331 GLY   B N   1 
ATOM   4981 C  CA  . GLY   B 1 297 ? 32.982  -5.313  20.908  1.00 21.50 ? 331 GLY   B CA  1 
ATOM   4982 C  C   . GLY   B 1 297 ? 34.245  -4.486  21.022  1.00 22.63 ? 331 GLY   B C   1 
ATOM   4983 O  O   . GLY   B 1 297 ? 34.577  -3.691  20.136  1.00 22.44 ? 331 GLY   B O   1 
ATOM   4984 N  N   . PHE   B 1 298 ? 34.971  -4.686  22.118  1.00 22.06 ? 332 PHE   B N   1 
ATOM   4985 C  CA  . PHE   B 1 298 ? 36.123  -3.866  22.462  1.00 19.28 ? 332 PHE   B CA  1 
ATOM   4986 C  C   . PHE   B 1 298 ? 37.424  -4.579  22.124  1.00 19.82 ? 332 PHE   B C   1 
ATOM   4987 O  O   . PHE   B 1 298 ? 37.635  -5.733  22.510  1.00 25.24 ? 332 PHE   B O   1 
ATOM   4988 C  CB  . PHE   B 1 298 ? 36.069  -3.488  23.947  1.00 19.54 ? 332 PHE   B CB  1 
ATOM   4989 C  CG  . PHE   B 1 298 ? 34.784  -2.800  24.327  1.00 20.97 ? 332 PHE   B CG  1 
ATOM   4990 C  CD1 . PHE   B 1 298 ? 34.614  -1.433  24.089  1.00 16.43 ? 332 PHE   B CD1 1 
ATOM   4991 C  CD2 . PHE   B 1 298 ? 33.717  -3.527  24.853  1.00 19.33 ? 332 PHE   B CD2 1 
ATOM   4992 C  CE1 . PHE   B 1 298 ? 33.432  -0.801  24.396  1.00 16.92 ? 332 PHE   B CE1 1 
ATOM   4993 C  CE2 . PHE   B 1 298 ? 32.524  -2.899  25.185  1.00 18.99 ? 332 PHE   B CE2 1 
ATOM   4994 C  CZ  . PHE   B 1 298 ? 32.380  -1.522  24.948  1.00 20.33 ? 332 PHE   B CZ  1 
ATOM   4995 N  N   . ASP   B 1 299 ? 38.285  -3.891  21.390  1.00 21.87 ? 333 ASP   B N   1 
ATOM   4996 C  CA  . ASP   B 1 299 ? 39.640  -4.359  21.185  1.00 24.24 ? 333 ASP   B CA  1 
ATOM   4997 C  C   . ASP   B 1 299 ? 40.429  -4.236  22.478  1.00 23.50 ? 333 ASP   B C   1 
ATOM   4998 O  O   . ASP   B 1 299 ? 39.981  -3.640  23.456  1.00 24.33 ? 333 ASP   B O   1 
ATOM   4999 C  CB  . ASP   B 1 299 ? 40.325  -3.564  20.084  1.00 23.55 ? 333 ASP   B CB  1 
ATOM   5000 C  CG  . ASP   B 1 299 ? 39.579  -3.632  18.775  1.00 26.58 ? 333 ASP   B CG  1 
ATOM   5001 O  OD1 . ASP   B 1 299 ? 39.268  -4.745  18.336  1.00 27.92 ? 333 ASP   B OD1 1 
ATOM   5002 O  OD2 . ASP   B 1 299 ? 39.300  -2.572  18.178  1.00 32.26 ? 333 ASP   B OD2 1 
ATOM   5003 N  N   . PHE   B 1 300 ? 41.627  -4.806  22.469  1.00 25.25 ? 334 PHE   B N   1 
ATOM   5004 C  CA  . PHE   B 1 300 ? 42.490  -4.807  23.635  1.00 23.96 ? 334 PHE   B CA  1 
ATOM   5005 C  C   . PHE   B 1 300 ? 43.861  -4.262  23.272  1.00 27.60 ? 334 PHE   B C   1 
ATOM   5006 O  O   . PHE   B 1 300 ? 44.287  -4.301  22.111  1.00 25.63 ? 334 PHE   B O   1 
ATOM   5007 C  CB  . PHE   B 1 300 ? 42.640  -6.201  24.230  1.00 23.05 ? 334 PHE   B CB  1 
ATOM   5008 C  CG  . PHE   B 1 300 ? 41.492  -6.606  25.088  1.00 25.58 ? 334 PHE   B CG  1 
ATOM   5009 C  CD1 . PHE   B 1 300 ? 41.478  -6.292  26.430  1.00 26.72 ? 334 PHE   B CD1 1 
ATOM   5010 C  CD2 . PHE   B 1 300 ? 40.421  -7.293  24.555  1.00 27.48 ? 334 PHE   B CD2 1 
ATOM   5011 C  CE1 . PHE   B 1 300 ? 40.430  -6.660  27.235  1.00 26.87 ? 334 PHE   B CE1 1 
ATOM   5012 C  CE2 . PHE   B 1 300 ? 39.364  -7.667  25.353  1.00 26.02 ? 334 PHE   B CE2 1 
ATOM   5013 C  CZ  . PHE   B 1 300 ? 39.367  -7.343  26.698  1.00 29.28 ? 334 PHE   B CZ  1 
ATOM   5014 N  N   . MET   B 1 301 ? 44.538  -3.732  24.295  1.00 29.94 ? 335 MET   B N   1 
ATOM   5015 C  CA  . MET   B 1 301 ? 45.908  -3.292  24.129  1.00 26.87 ? 335 MET   B CA  1 
ATOM   5016 C  C   . MET   B 1 301 ? 46.733  -4.461  23.603  1.00 28.94 ? 335 MET   B C   1 
ATOM   5017 O  O   . MET   B 1 301 ? 46.366  -5.625  23.805  1.00 29.16 ? 335 MET   B O   1 
ATOM   5018 C  CB  . MET   B 1 301 ? 46.493  -2.779  25.442  1.00 25.73 ? 335 MET   B CB  1 
ATOM   5019 C  CG  . MET   B 1 301 ? 45.903  -1.466  25.941  1.00 28.34 ? 335 MET   B CG  1 
ATOM   5020 S  SD  . MET   B 1 301 ? 45.962  -0.080  24.769  1.00 36.27 ? 335 MET   B SD  1 
ATOM   5021 C  CE  . MET   B 1 301 ? 47.713  0.258   24.631  1.00 29.44 ? 335 MET   B CE  1 
ATOM   5022 N  N   . PRO   B 1 302 ? 47.805  -4.183  22.869  1.00 28.79 ? 336 PRO   B N   1 
ATOM   5023 C  CA  . PRO   B 1 302 ? 48.626  -5.276  22.344  1.00 28.35 ? 336 PRO   B CA  1 
ATOM   5024 C  C   . PRO   B 1 302 ? 49.269  -6.023  23.502  1.00 33.57 ? 336 PRO   B C   1 
ATOM   5025 O  O   . PRO   B 1 302 ? 49.770  -5.410  24.444  1.00 31.91 ? 336 PRO   B O   1 
ATOM   5026 C  CB  . PRO   B 1 302 ? 49.657  -4.562  21.458  1.00 33.89 ? 336 PRO   B CB  1 
ATOM   5027 C  CG  . PRO   B 1 302 ? 49.609  -3.101  21.879  1.00 36.32 ? 336 PRO   B CG  1 
ATOM   5028 C  CD  . PRO   B 1 302 ? 48.229  -2.854  22.381  1.00 31.43 ? 336 PRO   B CD  1 
ATOM   5029 N  N   . SER   B 1 303 ? 49.212  -7.358  23.445  1.00 36.29 ? 337 SER   B N   1 
ATOM   5030 C  CA  . SER   B 1 303 ? 49.614  -8.158  24.591  1.00 36.75 ? 337 SER   B CA  1 
ATOM   5031 C  C   . SER   B 1 303 ? 51.125  -8.073  24.788  1.00 41.92 ? 337 SER   B C   1 
ATOM   5032 O  O   . SER   B 1 303 ? 51.863  -7.781  23.843  1.00 42.56 ? 337 SER   B O   1 
ATOM   5033 C  CB  . SER   B 1 303 ? 49.178  -9.607  24.419  1.00 38.32 ? 337 SER   B CB  1 
ATOM   5034 O  OG  . SER   B 1 303 ? 47.759  -9.683  24.465  1.00 48.62 ? 337 SER   B OG  1 
ATOM   5035 N  N   . PRO   B 1 304 ? 51.603  -8.269  26.014  1.00 43.50 ? 338 PRO   B N   1 
ATOM   5036 C  CA  . PRO   B 1 304 ? 53.030  -8.111  26.283  1.00 43.93 ? 338 PRO   B CA  1 
ATOM   5037 C  C   . PRO   B 1 304 ? 53.829  -9.222  25.631  1.00 42.39 ? 338 PRO   B C   1 
ATOM   5038 O  O   . PRO   B 1 304 ? 53.269  -10.278 25.295  1.00 47.18 ? 338 PRO   B O   1 
ATOM   5039 C  CB  . PRO   B 1 304 ? 53.112  -8.174  27.817  1.00 36.58 ? 338 PRO   B CB  1 
ATOM   5040 C  CG  . PRO   B 1 304 ? 51.899  -8.842  28.232  1.00 41.46 ? 338 PRO   B CG  1 
ATOM   5041 C  CD  . PRO   B 1 304 ? 50.840  -8.453  27.255  1.00 41.36 ? 338 PRO   B CD  1 
ATOM   5042 N  N   . PRO   B 1 305 ? 55.133  -9.025  25.440  1.00 42.13 ? 339 PRO   B N   1 
ATOM   5043 C  CA  . PRO   B 1 305 ? 55.957  -10.045 24.779  1.00 45.21 ? 339 PRO   B CA  1 
ATOM   5044 C  C   . PRO   B 1 305 ? 56.122  -11.265 25.664  1.00 45.30 ? 339 PRO   B C   1 
ATOM   5045 O  O   . PRO   B 1 305 ? 55.837  -11.209 26.872  1.00 41.24 ? 339 PRO   B O   1 
ATOM   5046 C  CB  . PRO   B 1 305 ? 57.297  -9.328  24.566  1.00 46.84 ? 339 PRO   B CB  1 
ATOM   5047 C  CG  . PRO   B 1 305 ? 57.361  -8.358  25.691  1.00 49.72 ? 339 PRO   B CG  1 
ATOM   5048 C  CD  . PRO   B 1 305 ? 55.944  -7.883  25.902  1.00 45.81 ? 339 PRO   B CD  1 
ATOM   5049 N  N   . PRO   B 1 306 ? 56.583  -12.384 25.097  1.00 46.97 ? 340 PRO   B N   1 
ATOM   5050 C  CA  . PRO   B 1 306 ? 56.738  -13.608 25.902  1.00 48.33 ? 340 PRO   B CA  1 
ATOM   5051 C  C   . PRO   B 1 306 ? 57.761  -13.487 27.014  1.00 41.25 ? 340 PRO   B C   1 
ATOM   5052 O  O   . PRO   B 1 306 ? 57.672  -14.226 28.001  1.00 41.23 ? 340 PRO   B O   1 
ATOM   5053 C  CB  . PRO   B 1 306 ? 57.159  -14.655 24.862  1.00 39.88 ? 340 PRO   B CB  1 
ATOM   5054 C  CG  . PRO   B 1 306 ? 57.739  -13.867 23.749  1.00 44.03 ? 340 PRO   B CG  1 
ATOM   5055 C  CD  . PRO   B 1 306 ? 56.919  -12.616 23.686  1.00 42.70 ? 340 PRO   B CD  1 
ATOM   5056 N  N   . THR   B 1 307 ? 58.724  -12.579 26.890  1.00 42.60 ? 341 THR   B N   1 
ATOM   5057 C  CA  . THR   B 1 307 ? 59.669  -12.357 27.977  1.00 46.41 ? 341 THR   B CA  1 
ATOM   5058 C  C   . THR   B 1 307 ? 58.965  -11.904 29.253  1.00 47.90 ? 341 THR   B C   1 
ATOM   5059 O  O   . THR   B 1 307 ? 59.441  -12.193 30.358  1.00 50.73 ? 341 THR   B O   1 
ATOM   5060 C  CB  . THR   B 1 307 ? 60.731  -11.336 27.546  1.00 54.95 ? 341 THR   B CB  1 
ATOM   5061 O  OG1 . THR   B 1 307 ? 60.094  -10.190 26.957  1.00 51.88 ? 341 THR   B OG1 1 
ATOM   5062 C  CG2 . THR   B 1 307 ? 61.714  -11.956 26.544  1.00 45.78 ? 341 THR   B CG2 1 
ATOM   5063 N  N   . TYR   B 1 308 ? 57.825  -11.211 29.131  1.00 48.65 ? 342 TYR   B N   1 
ATOM   5064 C  CA  . TYR   B 1 308 ? 57.064  -10.835 30.323  1.00 48.84 ? 342 TYR   B CA  1 
ATOM   5065 C  C   . TYR   B 1 308 ? 56.519  -12.057 31.046  1.00 46.59 ? 342 TYR   B C   1 
ATOM   5066 O  O   . TYR   B 1 308 ? 56.353  -12.037 32.271  1.00 46.61 ? 342 TYR   B O   1 
ATOM   5067 C  CB  . TYR   B 1 308 ? 55.911  -9.890  29.960  1.00 45.97 ? 342 TYR   B CB  1 
ATOM   5068 C  CG  . TYR   B 1 308 ? 54.995  -9.590  31.136  1.00 47.23 ? 342 TYR   B CG  1 
ATOM   5069 C  CD1 . TYR   B 1 308 ? 55.250  -8.528  31.985  1.00 45.45 ? 342 TYR   B CD1 1 
ATOM   5070 C  CD2 . TYR   B 1 308 ? 53.878  -10.383 31.406  1.00 47.97 ? 342 TYR   B CD2 1 
ATOM   5071 C  CE1 . TYR   B 1 308 ? 54.426  -8.262  33.071  1.00 41.50 ? 342 TYR   B CE1 1 
ATOM   5072 C  CE2 . TYR   B 1 308 ? 53.051  -10.118 32.489  1.00 41.68 ? 342 TYR   B CE2 1 
ATOM   5073 C  CZ  . TYR   B 1 308 ? 53.334  -9.055  33.316  1.00 36.78 ? 342 TYR   B CZ  1 
ATOM   5074 O  OH  . TYR   B 1 308 ? 52.523  -8.780  34.392  1.00 36.88 ? 342 TYR   B OH  1 
ATOM   5075 N  N   . TYR   B 1 309 ? 56.230  -13.122 30.316  1.00 44.33 ? 343 TYR   B N   1 
ATOM   5076 C  CA  . TYR   B 1 309 ? 55.622  -14.286 30.934  1.00 46.08 ? 343 TYR   B CA  1 
ATOM   5077 C  C   . TYR   B 1 309 ? 56.648  -15.284 31.465  1.00 48.26 ? 343 TYR   B C   1 
ATOM   5078 O  O   . TYR   B 1 309 ? 56.362  -15.993 32.436  1.00 46.94 ? 343 TYR   B O   1 
ATOM   5079 C  CB  . TYR   B 1 309 ? 54.652  -14.927 29.934  1.00 46.01 ? 343 TYR   B CB  1 
ATOM   5080 C  CG  . TYR   B 1 309 ? 53.461  -14.027 29.685  1.00 44.69 ? 343 TYR   B CG  1 
ATOM   5081 C  CD1 . TYR   B 1 309 ? 53.428  -13.152 28.600  1.00 47.88 ? 343 TYR   B CD1 1 
ATOM   5082 C  CD2 . TYR   B 1 309 ? 52.396  -14.002 30.575  1.00 45.92 ? 343 TYR   B CD2 1 
ATOM   5083 C  CE1 . TYR   B 1 309 ? 52.339  -12.306 28.391  1.00 43.55 ? 343 TYR   B CE1 1 
ATOM   5084 C  CE2 . TYR   B 1 309 ? 51.310  -13.157 30.384  1.00 45.79 ? 343 TYR   B CE2 1 
ATOM   5085 C  CZ  . TYR   B 1 309 ? 51.282  -12.315 29.289  1.00 42.17 ? 343 TYR   B CZ  1 
ATOM   5086 O  OH  . TYR   B 1 309 ? 50.198  -11.482 29.111  1.00 38.77 ? 343 TYR   B OH  1 
ATOM   5087 N  N   . GLN   B 1 310 ? 57.847  -15.350 30.880  1.00 47.40 ? 344 GLN   B N   1 
ATOM   5088 C  CA  . GLN   B 1 310 ? 58.920  -16.112 31.514  1.00 47.33 ? 344 GLN   B CA  1 
ATOM   5089 C  C   . GLN   B 1 310 ? 59.224  -15.552 32.896  1.00 50.26 ? 344 GLN   B C   1 
ATOM   5090 O  O   . GLN   B 1 310 ? 59.326  -16.295 33.879  1.00 52.09 ? 344 GLN   B O   1 
ATOM   5091 C  CB  . GLN   B 1 310 ? 60.173  -16.094 30.636  1.00 50.32 ? 344 GLN   B CB  1 
ATOM   5092 N  N   . ASN   B 1 311 ? 59.336  -14.225 32.988  1.00 56.02 ? 345 ASN   B N   1 
ATOM   5093 C  CA  . ASN   B 1 311 ? 59.549  -13.556 34.264  1.00 57.36 ? 345 ASN   B CA  1 
ATOM   5094 C  C   . ASN   B 1 311 ? 58.400  -13.785 35.240  1.00 56.82 ? 345 ASN   B C   1 
ATOM   5095 O  O   . ASN   B 1 311 ? 58.567  -13.541 36.442  1.00 54.27 ? 345 ASN   B O   1 
ATOM   5096 C  CB  . ASN   B 1 311 ? 59.746  -12.052 34.032  1.00 53.02 ? 345 ASN   B CB  1 
ATOM   5097 C  CG  . ASN   B 1 311 ? 60.904  -11.752 33.099  1.00 58.73 ? 345 ASN   B CG  1 
ATOM   5098 O  OD1 . ASN   B 1 311 ? 61.879  -12.507 33.041  1.00 65.01 ? 345 ASN   B OD1 1 
ATOM   5099 N  ND2 . ASN   B 1 311 ? 60.798  -10.647 32.350  1.00 59.99 ? 345 ASN   B ND2 1 
ATOM   5100 N  N   . LEU   B 1 312 ? 57.243  -14.249 34.759  1.00 55.19 ? 346 LEU   B N   1 
ATOM   5101 C  CA  . LEU   B 1 312 ? 56.109  -14.450 35.655  1.00 60.00 ? 346 LEU   B CA  1 
ATOM   5102 C  C   . LEU   B 1 312 ? 56.382  -15.558 36.667  1.00 58.28 ? 346 LEU   B C   1 
ATOM   5103 O  O   . LEU   B 1 312 ? 56.063  -15.406 37.852  1.00 54.85 ? 346 LEU   B O   1 
ATOM   5104 C  CB  . LEU   B 1 312 ? 54.838  -14.747 34.858  1.00 55.24 ? 346 LEU   B CB  1 
ATOM   5105 C  CG  . LEU   B 1 312 ? 54.014  -13.504 34.526  1.00 53.68 ? 346 LEU   B CG  1 
ATOM   5106 C  CD1 . LEU   B 1 312 ? 52.650  -13.896 33.963  1.00 51.77 ? 346 LEU   B CD1 1 
ATOM   5107 C  CD2 . LEU   B 1 312 ? 53.866  -12.641 35.774  1.00 48.82 ? 346 LEU   B CD2 1 
ATOM   5108 N  N   . LYS   B 1 313 ? 56.973  -16.676 36.230  1.00 60.06 ? 347 LYS   B N   1 
ATOM   5109 C  CA  . LYS   B 1 313 ? 57.250  -17.753 37.176  1.00 63.28 ? 347 LYS   B CA  1 
ATOM   5110 C  C   . LYS   B 1 313 ? 58.113  -17.263 38.338  1.00 64.33 ? 347 LYS   B C   1 
ATOM   5111 O  O   . LYS   B 1 313 ? 57.941  -17.720 39.476  1.00 61.14 ? 347 LYS   B O   1 
ATOM   5112 C  CB  . LYS   B 1 313 ? 57.909  -18.931 36.457  1.00 61.93 ? 347 LYS   B CB  1 
ATOM   5113 N  N   . LYS   B 1 314 ? 58.992  -16.289 38.089  1.00 62.07 ? 348 LYS   B N   1 
ATOM   5114 C  CA  . LYS   B 1 314 ? 59.897  -15.797 39.121  1.00 58.67 ? 348 LYS   B CA  1 
ATOM   5115 C  C   . LYS   B 1 314 ? 59.217  -14.902 40.154  1.00 61.93 ? 348 LYS   B C   1 
ATOM   5116 O  O   . LYS   B 1 314 ? 59.782  -14.698 41.235  1.00 55.59 ? 348 LYS   B O   1 
ATOM   5117 C  CB  . LYS   B 1 314 ? 61.060  -15.034 38.477  1.00 59.15 ? 348 LYS   B CB  1 
ATOM   5118 N  N   . ARG   B 1 315 ? 58.038  -14.345 39.856  1.00 61.26 ? 349 ARG   B N   1 
ATOM   5119 C  CA  . ARG   B 1 315 ? 57.395  -13.433 40.792  1.00 55.79 ? 349 ARG   B CA  1 
ATOM   5120 C  C   . ARG   B 1 315 ? 56.040  -13.895 41.310  1.00 48.81 ? 349 ARG   B C   1 
ATOM   5121 O  O   . ARG   B 1 315 ? 55.637  -13.444 42.383  1.00 61.72 ? 349 ARG   B O   1 
ATOM   5122 C  CB  . ARG   B 1 315 ? 57.258  -12.019 40.180  1.00 53.69 ? 349 ARG   B CB  1 
ATOM   5123 C  CG  . ARG   B 1 315 ? 57.135  -11.937 38.650  1.00 57.00 ? 349 ARG   B CG  1 
ATOM   5124 C  CD  . ARG   B 1 315 ? 57.446  -10.523 38.117  1.00 53.91 ? 349 ARG   B CD  1 
ATOM   5125 N  NE  . ARG   B 1 315 ? 56.287  -9.642  38.221  1.00 51.37 ? 349 ARG   B NE  1 
ATOM   5126 C  CZ  . ARG   B 1 315 ? 55.426  -9.396  37.240  1.00 48.62 ? 349 ARG   B CZ  1 
ATOM   5127 N  NH1 . ARG   B 1 315 ? 55.593  -9.932  36.035  1.00 48.08 ? 349 ARG   B NH1 1 
ATOM   5128 N  NH2 . ARG   B 1 315 ? 54.404  -8.593  37.468  1.00 42.62 ? 349 ARG   B NH2 1 
ATOM   5129 N  N   . VAL   B 1 316 ? 55.337  -14.784 40.616  1.00 48.24 ? 350 VAL   B N   1 
ATOM   5130 C  CA  . VAL   B 1 316 ? 54.017  -15.203 41.075  1.00 53.01 ? 350 VAL   B CA  1 
ATOM   5131 C  C   . VAL   B 1 316 ? 53.846  -16.717 40.985  1.00 60.31 ? 350 VAL   B C   1 
ATOM   5132 O  O   . VAL   B 1 316 ? 52.722  -17.228 41.070  1.00 61.76 ? 350 VAL   B O   1 
ATOM   5133 C  CB  . VAL   B 1 316 ? 52.907  -14.494 40.276  1.00 59.21 ? 350 VAL   B CB  1 
ATOM   5134 C  CG1 . VAL   B 1 316 ? 52.881  -12.998 40.581  1.00 52.27 ? 350 VAL   B CG1 1 
ATOM   5135 C  CG2 . VAL   B 1 316 ? 53.080  -14.748 38.776  1.00 55.10 ? 350 VAL   B CG2 1 
ATOM   5136 N  N   . GLY   B 1 317 ? 54.952  -17.448 40.826  1.00 60.52 ? 351 GLY   B N   1 
ATOM   5137 C  CA  . GLY   B 1 317 ? 54.872  -18.890 40.645  1.00 64.84 ? 351 GLY   B CA  1 
ATOM   5138 C  C   . GLY   B 1 317 ? 54.174  -19.624 41.773  1.00 65.27 ? 351 GLY   B C   1 
ATOM   5139 O  O   . GLY   B 1 317 ? 53.666  -20.732 41.561  1.00 67.48 ? 351 GLY   B O   1 
ATOM   5140 N  N   . ASP   B 1 318 ? 54.145  -19.035 42.970  1.00 62.51 ? 352 ASP   B N   1 
ATOM   5141 C  CA  . ASP   B 1 318 ? 53.461  -19.628 44.115  1.00 58.90 ? 352 ASP   B CA  1 
ATOM   5142 C  C   . ASP   B 1 318 ? 51.955  -19.451 44.029  1.00 63.34 ? 352 ASP   B C   1 
ATOM   5143 O  O   . ASP   B 1 318 ? 51.204  -20.231 44.630  1.00 59.24 ? 352 ASP   B O   1 
ATOM   5144 C  CB  . ASP   B 1 318 ? 53.958  -18.970 45.393  1.00 56.33 ? 352 ASP   B CB  1 
ATOM   5145 C  CG  . ASP   B 1 318 ? 53.794  -17.450 45.350  1.00 63.18 ? 352 ASP   B CG  1 
ATOM   5146 O  OD1 . ASP   B 1 318 ? 53.456  -16.849 46.392  1.00 59.12 ? 352 ASP   B OD1 1 
ATOM   5147 O  OD2 . ASP   B 1 318 ? 53.987  -16.857 44.258  1.00 59.93 ? 352 ASP   B OD2 1 
ATOM   5148 N  N   . VAL   B 1 319 ? 51.511  -18.426 43.305  1.00 61.33 ? 353 VAL   B N   1 
ATOM   5149 C  CA  . VAL   B 1 319 ? 50.106  -18.046 43.257  1.00 56.83 ? 353 VAL   B CA  1 
ATOM   5150 C  C   . VAL   B 1 319 ? 49.401  -18.683 42.064  1.00 55.92 ? 353 VAL   B C   1 
ATOM   5151 O  O   . VAL   B 1 319 ? 48.236  -19.081 42.163  1.00 56.60 ? 353 VAL   B O   1 
ATOM   5152 C  CB  . VAL   B 1 319 ? 50.009  -16.503 43.228  1.00 56.74 ? 353 VAL   B CB  1 
ATOM   5153 C  CG1 . VAL   B 1 319 ? 48.596  -16.029 43.512  1.00 51.01 ? 353 VAL   B CG1 1 
ATOM   5154 C  CG2 . VAL   B 1 319 ? 50.980  -15.881 44.216  1.00 52.16 ? 353 VAL   B CG2 1 
ATOM   5155 N  N   . LEU   B 1 320 ? 50.099  -18.801 40.936  1.00 57.54 ? 354 LEU   B N   1 
ATOM   5156 C  CA  . LEU   B 1 320 ? 49.538  -19.300 39.686  1.00 63.91 ? 354 LEU   B CA  1 
ATOM   5157 C  C   . LEU   B 1 320 ? 50.282  -20.556 39.246  1.00 65.89 ? 354 LEU   B C   1 
ATOM   5158 O  O   . LEU   B 1 320 ? 51.519  -20.590 39.263  1.00 64.93 ? 354 LEU   B O   1 
ATOM   5159 C  CB  . LEU   B 1 320 ? 49.628  -18.237 38.574  1.00 60.93 ? 354 LEU   B CB  1 
ATOM   5160 C  CG  . LEU   B 1 320 ? 48.886  -16.893 38.643  1.00 51.58 ? 354 LEU   B CG  1 
ATOM   5161 C  CD1 . LEU   B 1 320 ? 49.427  -15.963 37.560  1.00 50.22 ? 354 LEU   B CD1 1 
ATOM   5162 C  CD2 . LEU   B 1 320 ? 47.382  -17.050 38.481  1.00 45.04 ? 354 LEU   B CD2 1 
ATOM   5163 N  N   . SER   B 1 321 ? 49.538  -21.576 38.828  1.00 63.12 ? 355 SER   B N   1 
ATOM   5164 C  CA  . SER   B 1 321 ? 50.201  -22.743 38.276  1.00 62.44 ? 355 SER   B CA  1 
ATOM   5165 C  C   . SER   B 1 321 ? 50.842  -22.396 36.938  1.00 62.31 ? 355 SER   B C   1 
ATOM   5166 O  O   . SER   B 1 321 ? 50.578  -21.352 36.339  1.00 56.14 ? 355 SER   B O   1 
ATOM   5167 C  CB  . SER   B 1 321 ? 49.220  -23.886 38.082  1.00 60.30 ? 355 SER   B CB  1 
ATOM   5168 O  OG  . SER   B 1 321 ? 48.608  -23.763 36.815  1.00 61.08 ? 355 SER   B OG  1 
ATOM   5169 N  N   . ASP   B 1 322 ? 51.683  -23.309 36.455  1.00 66.44 ? 356 ASP   B N   1 
ATOM   5170 C  CA  . ASP   B 1 322 ? 52.384  -23.058 35.203  1.00 64.28 ? 356 ASP   B CA  1 
ATOM   5171 C  C   . ASP   B 1 322 ? 51.428  -23.041 34.018  1.00 63.19 ? 356 ASP   B C   1 
ATOM   5172 O  O   . ASP   B 1 322 ? 51.687  -22.349 33.026  1.00 58.78 ? 356 ASP   B O   1 
ATOM   5173 C  CB  . ASP   B 1 322 ? 53.482  -24.103 34.995  1.00 66.67 ? 356 ASP   B CB  1 
ATOM   5174 C  CG  . ASP   B 1 322 ? 54.786  -23.488 34.478  1.00 70.87 ? 356 ASP   B CG  1 
ATOM   5175 O  OD1 . ASP   B 1 322 ? 55.500  -24.150 33.699  1.00 65.96 ? 356 ASP   B OD1 1 
ATOM   5176 O  OD2 . ASP   B 1 322 ? 55.108  -22.346 34.857  1.00 68.21 ? 356 ASP   B OD2 1 
ATOM   5177 N  N   . ASP   B 1 323 ? 50.320  -23.783 34.102  1.00 66.92 ? 357 ASP   B N   1 
ATOM   5178 C  CA  . ASP   B 1 323 ? 49.320  -23.731 33.038  1.00 66.27 ? 357 ASP   B CA  1 
ATOM   5179 C  C   . ASP   B 1 323 ? 48.560  -22.407 33.060  1.00 65.13 ? 357 ASP   B C   1 
ATOM   5180 O  O   . ASP   B 1 323 ? 48.349  -21.791 32.009  1.00 61.83 ? 357 ASP   B O   1 
ATOM   5181 C  CB  . ASP   B 1 323 ? 48.351  -24.910 33.158  1.00 60.27 ? 357 ASP   B CB  1 
ATOM   5182 N  N   . GLN   B 1 324 ? 48.133  -21.958 34.248  1.00 65.85 ? 358 GLN   B N   1 
ATOM   5183 C  CA  . GLN   B 1 324 ? 47.430  -20.682 34.346  1.00 63.06 ? 358 GLN   B CA  1 
ATOM   5184 C  C   . GLN   B 1 324 ? 48.299  -19.533 33.864  1.00 60.26 ? 358 GLN   B C   1 
ATOM   5185 O  O   . GLN   B 1 324 ? 47.790  -18.567 33.285  1.00 59.55 ? 358 GLN   B O   1 
ATOM   5186 C  CB  . GLN   B 1 324 ? 46.973  -20.431 35.783  1.00 59.01 ? 358 GLN   B CB  1 
ATOM   5187 C  CG  . GLN   B 1 324 ? 45.680  -21.132 36.139  1.00 68.48 ? 358 GLN   B CG  1 
ATOM   5188 C  CD  . GLN   B 1 324 ? 45.892  -22.376 36.983  1.00 72.23 ? 358 GLN   B CD  1 
ATOM   5189 O  OE1 . GLN   B 1 324 ? 46.582  -22.334 38.004  1.00 71.88 ? 358 GLN   B OE1 1 
ATOM   5190 N  NE2 . GLN   B 1 324 ? 45.288  -23.490 36.566  1.00 66.75 ? 358 GLN   B NE2 1 
ATOM   5191 N  N   . ILE   B 1 325 ? 49.608  -19.620 34.088  1.00 63.01 ? 359 ILE   B N   1 
ATOM   5192 C  CA  . ILE   B 1 325 ? 50.522  -18.629 33.530  1.00 58.78 ? 359 ILE   B CA  1 
ATOM   5193 C  C   . ILE   B 1 325 ? 50.500  -18.686 32.008  1.00 54.96 ? 359 ILE   B C   1 
ATOM   5194 O  O   . ILE   B 1 325 ? 50.467  -17.649 31.334  1.00 56.42 ? 359 ILE   B O   1 
ATOM   5195 C  CB  . ILE   B 1 325 ? 51.938  -18.835 34.104  1.00 57.16 ? 359 ILE   B CB  1 
ATOM   5196 C  CG1 . ILE   B 1 325 ? 52.038  -18.159 35.475  1.00 49.33 ? 359 ILE   B CG1 1 
ATOM   5197 C  CG2 . ILE   B 1 325 ? 53.006  -18.331 33.137  1.00 55.29 ? 359 ILE   B CG2 1 
ATOM   5198 C  CD1 . ILE   B 1 325 ? 53.404  -18.189 36.062  1.00 55.92 ? 359 ILE   B CD1 1 
ATOM   5199 N  N   . LYS   B 1 326 ? 50.480  -19.896 31.444  1.00 55.05 ? 360 LYS   B N   1 
ATOM   5200 C  CA  . LYS   B 1 326 ? 50.390  -20.052 29.998  1.00 56.14 ? 360 LYS   B CA  1 
ATOM   5201 C  C   . LYS   B 1 326 ? 49.031  -19.635 29.453  1.00 52.84 ? 360 LYS   B C   1 
ATOM   5202 O  O   . LYS   B 1 326 ? 48.896  -19.474 28.235  1.00 54.52 ? 360 LYS   B O   1 
ATOM   5203 C  CB  . LYS   B 1 326 ? 50.684  -21.505 29.592  1.00 54.45 ? 360 LYS   B CB  1 
ATOM   5204 N  N   . GLU   B 1 327 ? 48.019  -19.477 30.312  1.00 52.09 ? 361 GLU   B N   1 
ATOM   5205 C  CA  . GLU   B 1 327 ? 46.717  -19.003 29.851  1.00 57.61 ? 361 GLU   B CA  1 
ATOM   5206 C  C   . GLU   B 1 327 ? 46.567  -17.493 30.004  1.00 54.50 ? 361 GLU   B C   1 
ATOM   5207 O  O   . GLU   B 1 327 ? 45.865  -16.862 29.203  1.00 51.32 ? 361 GLU   B O   1 
ATOM   5208 C  CB  . GLU   B 1 327 ? 45.583  -19.725 30.589  1.00 60.48 ? 361 GLU   B CB  1 
ATOM   5209 C  CG  . GLU   B 1 327 ? 44.280  -19.787 29.787  1.00 58.02 ? 361 GLU   B CG  1 
ATOM   5210 C  CD  . GLU   B 1 327 ? 43.204  -20.646 30.443  1.00 64.01 ? 361 GLU   B CD  1 
ATOM   5211 O  OE1 . GLU   B 1 327 ? 42.010  -20.441 30.129  1.00 65.22 ? 361 GLU   B OE1 1 
ATOM   5212 O  OE2 . GLU   B 1 327 ? 43.547  -21.523 31.268  1.00 61.20 ? 361 GLU   B OE2 1 
ATOM   5213 N  N   . CYS   B 1 328 ? 47.209  -16.899 31.012  1.00 49.37 ? 362 CYS   B N   1 
ATOM   5214 C  CA  . CYS   B 1 328 ? 47.454  -15.466 30.977  1.00 40.74 ? 362 CYS   B CA  1 
ATOM   5215 C  C   . CYS   B 1 328 ? 48.096  -15.073 29.651  1.00 46.73 ? 362 CYS   B C   1 
ATOM   5216 O  O   . CYS   B 1 328 ? 47.657  -14.126 28.986  1.00 43.33 ? 362 CYS   B O   1 
ATOM   5217 C  CB  . CYS   B 1 328 ? 48.346  -15.062 32.149  1.00 43.82 ? 362 CYS   B CB  1 
ATOM   5218 S  SG  . CYS   B 1 328 ? 47.526  -15.077 33.760  1.00 52.59 ? 362 CYS   B SG  1 
ATOM   5219 N  N   . GLU   B 1 329 ? 49.128  -15.817 29.234  1.00 40.57 ? 363 GLU   B N   1 
ATOM   5220 C  CA  . GLU   B 1 329 ? 49.870  -15.434 28.041  1.00 42.47 ? 363 GLU   B CA  1 
ATOM   5221 C  C   . GLU   B 1 329 ? 49.046  -15.618 26.773  1.00 46.60 ? 363 GLU   B C   1 
ATOM   5222 O  O   . GLU   B 1 329 ? 49.248  -14.894 25.788  1.00 38.24 ? 363 GLU   B O   1 
ATOM   5223 C  CB  . GLU   B 1 329 ? 51.170  -16.225 27.946  1.00 46.95 ? 363 GLU   B CB  1 
ATOM   5224 C  CG  . GLU   B 1 329 ? 52.051  -15.789 26.774  1.00 50.93 ? 363 GLU   B CG  1 
ATOM   5225 C  CD  . GLU   B 1 329 ? 53.104  -16.823 26.396  1.00 58.55 ? 363 GLU   B CD  1 
ATOM   5226 O  OE1 . GLU   B 1 329 ? 53.474  -17.659 27.258  1.00 56.43 ? 363 GLU   B OE1 1 
ATOM   5227 O  OE2 . GLU   B 1 329 ? 53.559  -16.792 25.230  1.00 57.84 ? 363 GLU   B OE2 1 
ATOM   5228 N  N   . GLU   B 1 330 ? 48.124  -16.581 26.765  1.00 46.39 ? 364 GLU   B N   1 
ATOM   5229 C  CA  . GLU   B 1 330 ? 47.218  -16.680 25.629  1.00 49.49 ? 364 GLU   B CA  1 
ATOM   5230 C  C   . GLU   B 1 330 ? 46.341  -15.437 25.533  1.00 41.24 ? 364 GLU   B C   1 
ATOM   5231 O  O   . GLU   B 1 330 ? 46.113  -14.909 24.438  1.00 35.24 ? 364 GLU   B O   1 
ATOM   5232 C  CB  . GLU   B 1 330 ? 46.358  -17.944 25.739  1.00 55.38 ? 364 GLU   B CB  1 
ATOM   5233 C  CG  . GLU   B 1 330 ? 47.100  -19.260 25.532  1.00 59.18 ? 364 GLU   B CG  1 
ATOM   5234 C  CD  . GLU   B 1 330 ? 46.162  -20.456 25.548  1.00 72.70 ? 364 GLU   B CD  1 
ATOM   5235 O  OE1 . GLU   B 1 330 ? 44.976  -20.281 25.184  1.00 76.14 ? 364 GLU   B OE1 1 
ATOM   5236 O  OE2 . GLU   B 1 330 ? 46.603  -21.562 25.938  1.00 69.01 ? 364 GLU   B OE2 1 
ATOM   5237 N  N   . LEU   B 1 331 ? 45.884  -14.932 26.681  1.00 43.19 ? 365 LEU   B N   1 
ATOM   5238 C  CA  . LEU   B 1 331 ? 44.901  -13.863 26.739  1.00 40.86 ? 365 LEU   B CA  1 
ATOM   5239 C  C   . LEU   B 1 331 ? 45.512  -12.472 26.822  1.00 43.01 ? 365 LEU   B C   1 
ATOM   5240 O  O   . LEU   B 1 331 ? 44.801  -11.490 26.581  1.00 45.73 ? 365 LEU   B O   1 
ATOM   5241 C  CB  . LEU   B 1 331 ? 43.972  -14.099 27.931  1.00 37.30 ? 365 LEU   B CB  1 
ATOM   5242 C  CG  . LEU   B 1 331 ? 43.229  -15.426 27.773  1.00 33.06 ? 365 LEU   B CG  1 
ATOM   5243 C  CD1 . LEU   B 1 331 ? 42.463  -15.808 29.023  1.00 31.23 ? 365 LEU   B CD1 1 
ATOM   5244 C  CD2 . LEU   B 1 331 ? 42.297  -15.342 26.577  1.00 30.26 ? 365 LEU   B CD2 1 
ATOM   5245 N  N   . GLY   B 1 332 ? 46.800  -12.357 27.142  1.00 39.31 ? 366 GLY   B N   1 
ATOM   5246 C  CA  . GLY   B 1 332 ? 47.410  -11.050 27.285  1.00 34.35 ? 366 GLY   B CA  1 
ATOM   5247 C  C   . GLY   B 1 332 ? 47.199  -10.420 28.642  1.00 36.78 ? 366 GLY   B C   1 
ATOM   5248 O  O   . GLY   B 1 332 ? 47.142  -9.189  28.750  1.00 42.28 ? 366 GLY   B O   1 
ATOM   5249 N  N   . ILE   B 1 333 ? 47.084  -11.230 29.684  1.00 35.81 ? 367 ILE   B N   1 
ATOM   5250 C  CA  . ILE   B 1 333 ? 46.853  -10.741 31.038  1.00 37.05 ? 367 ILE   B CA  1 
ATOM   5251 C  C   . ILE   B 1 333 ? 48.167  -10.278 31.662  1.00 38.27 ? 367 ILE   B C   1 
ATOM   5252 O  O   . ILE   B 1 333 ? 49.228  -10.879 31.454  1.00 41.32 ? 367 ILE   B O   1 
ATOM   5253 C  CB  . ILE   B 1 333 ? 46.166  -11.835 31.879  1.00 31.97 ? 367 ILE   B CB  1 
ATOM   5254 C  CG1 . ILE   B 1 333 ? 44.832  -12.210 31.222  1.00 35.57 ? 367 ILE   B CG1 1 
ATOM   5255 C  CG2 . ILE   B 1 333 ? 45.984  -11.408 33.323  1.00 22.59 ? 367 ILE   B CG2 1 
ATOM   5256 C  CD1 . ILE   B 1 333 ? 43.837  -12.923 32.133  1.00 37.67 ? 367 ILE   B CD1 1 
ATOM   5257 N  N   . LEU   B 1 334 ? 48.098  -9.175  32.403  1.00 37.49 ? 368 LEU   B N   1 
ATOM   5258 C  CA  . LEU   B 1 334 ? 49.189  -8.668  33.217  1.00 32.79 ? 368 LEU   B CA  1 
ATOM   5259 C  C   . LEU   B 1 334 ? 48.945  -9.031  34.678  1.00 34.42 ? 368 LEU   B C   1 
ATOM   5260 O  O   . LEU   B 1 334 ? 47.804  -9.101  35.138  1.00 30.88 ? 368 LEU   B O   1 
ATOM   5261 C  CB  . LEU   B 1 334 ? 49.308  -7.151  33.086  1.00 32.48 ? 368 LEU   B CB  1 
ATOM   5262 C  CG  . LEU   B 1 334 ? 49.156  -6.475  31.721  1.00 41.40 ? 368 LEU   B CG  1 
ATOM   5263 C  CD1 . LEU   B 1 334 ? 49.294  -4.960  31.898  1.00 40.12 ? 368 LEU   B CD1 1 
ATOM   5264 C  CD2 . LEU   B 1 334 ? 50.167  -6.990  30.712  1.00 35.90 ? 368 LEU   B CD2 1 
ATOM   5265 N  N   . VAL   B 1 335 ? 50.029  -9.242  35.414  1.00 28.36 ? 369 VAL   B N   1 
ATOM   5266 C  CA  . VAL   B 1 335 ? 49.951  -9.714  36.786  1.00 34.89 ? 369 VAL   B CA  1 
ATOM   5267 C  C   . VAL   B 1 335 ? 50.872  -8.851  37.624  1.00 38.59 ? 369 VAL   B C   1 
ATOM   5268 O  O   . VAL   B 1 335 ? 52.012  -8.591  37.226  1.00 41.51 ? 369 VAL   B O   1 
ATOM   5269 C  CB  . VAL   B 1 335 ? 50.356  -11.201 36.914  1.00 44.12 ? 369 VAL   B CB  1 
ATOM   5270 C  CG1 . VAL   B 1 335 ? 50.154  -11.710 38.351  1.00 38.18 ? 369 VAL   B CG1 1 
ATOM   5271 C  CG2 . VAL   B 1 335 ? 49.606  -12.072 35.900  1.00 37.80 ? 369 VAL   B CG2 1 
ATOM   5272 N  N   . ASP   B 1 336 ? 50.379  -8.417  38.777  1.00 35.41 ? 370 ASP   B N   1 
ATOM   5273 C  CA  . ASP   B 1 336 ? 51.163  -7.675  39.749  1.00 40.86 ? 370 ASP   B CA  1 
ATOM   5274 C  C   . ASP   B 1 336 ? 50.785  -8.203  41.125  1.00 46.60 ? 370 ASP   B C   1 
ATOM   5275 O  O   . ASP   B 1 336 ? 49.724  -8.814  41.314  1.00 37.50 ? 370 ASP   B O   1 
ATOM   5276 C  CB  . ASP   B 1 336 ? 50.929  -6.147  39.652  1.00 41.87 ? 370 ASP   B CB  1 
ATOM   5277 C  CG  . ASP   B 1 336 ? 51.985  -5.326  40.406  1.00 49.63 ? 370 ASP   B CG  1 
ATOM   5278 O  OD1 . ASP   B 1 336 ? 53.151  -5.781  40.472  1.00 52.42 ? 370 ASP   B OD1 1 
ATOM   5279 O  OD2 . ASP   B 1 336 ? 51.652  -4.225  40.922  1.00 44.40 ? 370 ASP   B OD2 1 
ATOM   5280 N  N   . ARG   B 1 337 ? 51.672  -7.970  42.087  1.00 49.47 ? 371 ARG   B N   1 
ATOM   5281 C  CA  . ARG   B 1 337 ? 51.503  -8.547  43.407  1.00 52.44 ? 371 ARG   B CA  1 
ATOM   5282 C  C   . ARG   B 1 337 ? 51.725  -7.482  44.479  1.00 59.06 ? 371 ARG   B C   1 
ATOM   5283 O  O   . ARG   B 1 337 ? 52.511  -6.542  44.309  1.00 56.87 ? 371 ARG   B O   1 
ATOM   5284 C  CB  . ARG   B 1 337 ? 52.431  -9.755  43.587  1.00 50.89 ? 371 ARG   B CB  1 
ATOM   5285 C  CG  . ARG   B 1 337 ? 52.495  -10.271 44.993  1.00 59.93 ? 371 ARG   B CG  1 
ATOM   5286 C  CD  . ARG   B 1 337 ? 53.350  -11.493 45.088  1.00 57.04 ? 371 ARG   B CD  1 
ATOM   5287 N  NE  . ARG   B 1 337 ? 52.761  -12.423 46.041  1.00 56.46 ? 371 ARG   B NE  1 
ATOM   5288 C  CZ  . ARG   B 1 337 ? 53.062  -13.712 46.104  1.00 60.25 ? 371 ARG   B CZ  1 
ATOM   5289 N  NH1 . ARG   B 1 337 ? 53.953  -14.218 45.259  1.00 66.05 ? 371 ARG   B NH1 1 
ATOM   5290 N  NH2 . ARG   B 1 337 ? 52.476  -14.494 47.007  1.00 58.38 ? 371 ARG   B NH2 1 
ATOM   5291 N  N   . ASP   B 1 338 ? 50.985  -7.636  45.571  1.00 58.63 ? 372 ASP   B N   1 
ATOM   5292 C  CA  . ASP   B 1 338 ? 50.872  -6.709  46.679  1.00 57.16 ? 372 ASP   B CA  1 
ATOM   5293 C  C   . ASP   B 1 338 ? 51.695  -7.202  47.856  1.00 59.69 ? 372 ASP   B C   1 
ATOM   5294 O  O   . ASP   B 1 338 ? 52.456  -8.175  47.762  1.00 55.27 ? 372 ASP   B O   1 
ATOM   5295 C  CB  . ASP   B 1 338 ? 49.407  -6.604  47.096  1.00 54.07 ? 372 ASP   B CB  1 
ATOM   5296 C  CG  . ASP   B 1 338 ? 48.992  -5.208  47.426  1.00 57.39 ? 372 ASP   B CG  1 
ATOM   5297 O  OD1 . ASP   B 1 338 ? 48.031  -5.059  48.210  1.00 60.39 ? 372 ASP   B OD1 1 
ATOM   5298 O  OD2 . ASP   B 1 338 ? 49.607  -4.265  46.888  1.00 61.90 ? 372 ASP   B OD2 1 
ATOM   5299 N  N   . ASP   B 1 339 ? 51.510  -6.541  48.996  1.00 58.49 ? 373 ASP   B N   1 
ATOM   5300 C  CA  . ASP   B 1 339 ? 51.858  -7.162  50.261  1.00 59.46 ? 373 ASP   B CA  1 
ATOM   5301 C  C   . ASP   B 1 339 ? 50.797  -8.179  50.678  1.00 63.88 ? 373 ASP   B C   1 
ATOM   5302 O  O   . ASP   B 1 339 ? 51.124  -9.176  51.332  1.00 55.44 ? 373 ASP   B O   1 
ATOM   5303 C  CB  . ASP   B 1 339 ? 52.074  -6.086  51.342  1.00 63.52 ? 373 ASP   B CB  1 
ATOM   5304 C  CG  . ASP   B 1 339 ? 51.029  -4.941  51.296  1.00 73.63 ? 373 ASP   B CG  1 
ATOM   5305 O  OD1 . ASP   B 1 339 ? 51.247  -3.922  50.596  1.00 66.76 ? 373 ASP   B OD1 1 
ATOM   5306 O  OD2 . ASP   B 1 339 ? 50.000  -5.042  51.995  1.00 77.46 ? 373 ASP   B OD2 1 
ATOM   5307 N  N   . GLN   B 1 340 ? 49.541  -7.978  50.264  1.00 66.87 ? 374 GLN   B N   1 
ATOM   5308 C  CA  . GLN   B 1 340 ? 48.422  -8.828  50.664  1.00 60.57 ? 374 GLN   B CA  1 
ATOM   5309 C  C   . GLN   B 1 340 ? 48.076  -9.870  49.612  1.00 58.04 ? 374 GLN   B C   1 
ATOM   5310 O  O   . GLN   B 1 340 ? 48.019  -11.066 49.919  1.00 57.26 ? 374 GLN   B O   1 
ATOM   5311 C  CB  . GLN   B 1 340 ? 47.159  -7.995  50.946  1.00 62.22 ? 374 GLN   B CB  1 
ATOM   5312 C  CG  . GLN   B 1 340 ? 47.346  -6.544  51.377  1.00 72.37 ? 374 GLN   B CG  1 
ATOM   5313 C  CD  . GLN   B 1 340 ? 46.087  -5.946  51.996  1.00 77.64 ? 374 GLN   B CD  1 
ATOM   5314 O  OE1 . GLN   B 1 340 ? 45.888  -6.002  53.222  1.00 76.62 ? 374 GLN   B OE1 1 
ATOM   5315 N  NE2 . GLN   B 1 340 ? 45.226  -5.371  51.148  1.00 66.93 ? 374 GLN   B NE2 1 
ATOM   5316 N  N   . GLY   B 1 341 ? 47.817  -9.435  48.380  1.00 54.36 ? 375 GLY   B N   1 
ATOM   5317 C  CA  . GLY   B 1 341 ? 47.275  -10.327 47.373  1.00 50.41 ? 375 GLY   B CA  1 
ATOM   5318 C  C   . GLY   B 1 341 ? 47.946  -10.229 46.020  1.00 48.52 ? 375 GLY   B C   1 
ATOM   5319 O  O   . GLY   B 1 341 ? 49.049  -9.690  45.896  1.00 46.76 ? 375 GLY   B O   1 
ATOM   5320 N  N   . THR   B 1 342 ? 47.286  -10.762 44.997  1.00 48.44 ? 376 THR   B N   1 
ATOM   5321 C  CA  . THR   B 1 342 ? 47.764  -10.698 43.623  1.00 50.35 ? 376 THR   B CA  1 
ATOM   5322 C  C   . THR   B 1 342 ? 46.664  -10.118 42.742  1.00 44.91 ? 376 THR   B C   1 
ATOM   5323 O  O   . THR   B 1 342 ? 45.477  -10.399 42.951  1.00 44.24 ? 376 THR   B O   1 
ATOM   5324 C  CB  . THR   B 1 342 ? 48.212  -12.099 43.124  1.00 49.34 ? 376 THR   B CB  1 
ATOM   5325 O  OG1 . THR   B 1 342 ? 49.545  -12.369 43.587  1.00 50.57 ? 376 THR   B OG1 1 
ATOM   5326 C  CG2 . THR   B 1 342 ? 48.179  -12.193 41.598  1.00 46.92 ? 376 THR   B CG2 1 
ATOM   5327 N  N   . LEU   B 1 343 ? 47.061  -9.300  41.767  1.00 36.09 ? 377 LEU   B N   1 
ATOM   5328 C  CA  . LEU   B 1 343 ? 46.136  -8.640  40.857  1.00 30.99 ? 377 LEU   B CA  1 
ATOM   5329 C  C   . LEU   B 1 343 ? 46.289  -9.213  39.451  1.00 32.78 ? 377 LEU   B C   1 
ATOM   5330 O  O   . LEU   B 1 343 ? 47.408  -9.319  38.932  1.00 32.76 ? 377 LEU   B O   1 
ATOM   5331 C  CB  . LEU   B 1 343 ? 46.390  -7.131  40.869  1.00 29.73 ? 377 LEU   B CB  1 
ATOM   5332 C  CG  . LEU   B 1 343 ? 45.731  -6.188  39.866  1.00 35.14 ? 377 LEU   B CG  1 
ATOM   5333 C  CD1 . LEU   B 1 343 ? 44.288  -5.926  40.250  1.00 35.32 ? 377 LEU   B CD1 1 
ATOM   5334 C  CD2 . LEU   B 1 343 ? 46.526  -4.881  39.738  1.00 32.16 ? 377 LEU   B CD2 1 
ATOM   5335 N  N   . LEU   B 1 344 ? 45.175  -9.597  38.840  1.00 28.93 ? 378 LEU   B N   1 
ATOM   5336 C  CA  . LEU   B 1 344 ? 45.146  -9.877  37.410  1.00 29.46 ? 378 LEU   B CA  1 
ATOM   5337 C  C   . LEU   B 1 344 ? 44.362  -8.762  36.725  1.00 34.60 ? 378 LEU   B C   1 
ATOM   5338 O  O   . LEU   B 1 344 ? 43.280  -8.378  37.199  1.00 33.23 ? 378 LEU   B O   1 
ATOM   5339 C  CB  . LEU   B 1 344 ? 44.535  -11.248 37.106  1.00 26.91 ? 378 LEU   B CB  1 
ATOM   5340 C  CG  . LEU   B 1 344 ? 45.073  -12.494 37.838  1.00 31.70 ? 378 LEU   B CG  1 
ATOM   5341 C  CD1 . LEU   B 1 344 ? 44.515  -13.801 37.252  1.00 38.17 ? 378 LEU   B CD1 1 
ATOM   5342 C  CD2 . LEU   B 1 344 ? 46.586  -12.547 37.835  1.00 33.35 ? 378 LEU   B CD2 1 
ATOM   5343 N  N   . GLN   B 1 345 ? 44.918  -8.234  35.624  1.00 32.06 ? 379 GLN   B N   1 
ATOM   5344 C  CA  . GLN   B 1 345 ? 44.386  -7.049  34.957  1.00 28.15 ? 379 GLN   B CA  1 
ATOM   5345 C  C   . GLN   B 1 345 ? 44.643  -7.103  33.457  1.00 32.81 ? 379 GLN   B C   1 
ATOM   5346 O  O   . GLN   B 1 345 ? 45.601  -7.723  32.984  1.00 29.16 ? 379 GLN   B O   1 
ATOM   5347 C  CB  . GLN   B 1 345 ? 45.011  -5.764  35.514  1.00 29.45 ? 379 GLN   B CB  1 
ATOM   5348 C  CG  . GLN   B 1 345 ? 46.506  -5.671  35.363  1.00 28.14 ? 379 GLN   B CG  1 
ATOM   5349 C  CD  . GLN   B 1 345 ? 47.065  -4.457  36.057  1.00 32.48 ? 379 GLN   B CD  1 
ATOM   5350 O  OE1 . GLN   B 1 345 ? 48.252  -4.415  36.396  1.00 37.44 ? 379 GLN   B OE1 1 
ATOM   5351 N  NE2 . GLN   B 1 345 ? 46.216  -3.450  36.274  1.00 31.00 ? 379 GLN   B NE2 1 
ATOM   5352 N  N   . ILE   B 1 346 ? 43.785  -6.404  32.714  1.00 34.68 ? 380 ILE   B N   1 
ATOM   5353 C  CA  . ILE   B 1 346 ? 44.028  -6.128  31.300  1.00 30.98 ? 380 ILE   B CA  1 
ATOM   5354 C  C   . ILE   B 1 346 ? 43.265  -4.858  30.926  1.00 27.98 ? 380 ILE   B C   1 
ATOM   5355 O  O   . ILE   B 1 346 ? 42.301  -4.475  31.590  1.00 28.96 ? 380 ILE   B O   1 
ATOM   5356 C  CB  . ILE   B 1 346 ? 43.623  -7.339  30.421  1.00 25.86 ? 380 ILE   B CB  1 
ATOM   5357 C  CG1 . ILE   B 1 346 ? 44.201  -7.188  29.010  1.00 23.54 ? 380 ILE   B CG1 1 
ATOM   5358 C  CG2 . ILE   B 1 346 ? 42.124  -7.473  30.410  1.00 30.15 ? 380 ILE   B CG2 1 
ATOM   5359 C  CD1 . ILE   B 1 346 ? 43.968  -8.355  28.084  1.00 29.18 ? 380 ILE   B CD1 1 
ATOM   5360 N  N   . PHE   B 1 347 ? 43.700  -4.195  29.858  1.00 26.25 ? 381 PHE   B N   1 
ATOM   5361 C  CA  . PHE   B 1 347 ? 43.140  -2.910  29.460  1.00 25.30 ? 381 PHE   B CA  1 
ATOM   5362 C  C   . PHE   B 1 347 ? 42.653  -2.949  28.015  1.00 24.71 ? 381 PHE   B C   1 
ATOM   5363 O  O   . PHE   B 1 347 ? 43.367  -3.416  27.121  1.00 20.74 ? 381 PHE   B O   1 
ATOM   5364 C  CB  . PHE   B 1 347 ? 44.172  -1.801  29.637  1.00 21.28 ? 381 PHE   B CB  1 
ATOM   5365 C  CG  . PHE   B 1 347 ? 44.718  -1.715  31.016  1.00 27.15 ? 381 PHE   B CG  1 
ATOM   5366 C  CD1 . PHE   B 1 347 ? 45.849  -2.421  31.371  1.00 33.14 ? 381 PHE   B CD1 1 
ATOM   5367 C  CD2 . PHE   B 1 347 ? 44.097  -0.939  31.969  1.00 30.36 ? 381 PHE   B CD2 1 
ATOM   5368 C  CE1 . PHE   B 1 347 ? 46.356  -2.358  32.635  1.00 26.45 ? 381 PHE   B CE1 1 
ATOM   5369 C  CE2 . PHE   B 1 347 ? 44.606  -0.862  33.239  1.00 32.92 ? 381 PHE   B CE2 1 
ATOM   5370 C  CZ  . PHE   B 1 347 ? 45.733  -1.585  33.574  1.00 32.15 ? 381 PHE   B CZ  1 
ATOM   5371 N  N   . THR   B 1 348 ? 41.442  -2.444  27.795  1.00 24.87 ? 382 THR   B N   1 
ATOM   5372 C  CA  . THR   B 1 348 ? 40.922  -2.272  26.447  1.00 27.34 ? 382 THR   B CA  1 
ATOM   5373 C  C   . THR   B 1 348 ? 41.585  -1.081  25.759  1.00 26.68 ? 382 THR   B C   1 
ATOM   5374 O  O   . THR   B 1 348 ? 42.144  -0.190  26.396  1.00 24.74 ? 382 THR   B O   1 
ATOM   5375 C  CB  . THR   B 1 348 ? 39.422  -1.997  26.460  1.00 26.66 ? 382 THR   B CB  1 
ATOM   5376 O  OG1 . THR   B 1 348 ? 39.222  -0.621  26.835  1.00 26.82 ? 382 THR   B OG1 1 
ATOM   5377 C  CG2 . THR   B 1 348 ? 38.693  -2.905  27.431  1.00 20.53 ? 382 THR   B CG2 1 
ATOM   5378 N  N   . LYS   B 1 349 ? 41.474  -1.051  24.441  1.00 25.87 ? 383 LYS   B N   1 
ATOM   5379 C  CA  . LYS   B 1 349 ? 41.745  0.188   23.722  1.00 29.47 ? 383 LYS   B CA  1 
ATOM   5380 C  C   . LYS   B 1 349 ? 40.628  1.201   24.039  1.00 27.04 ? 383 LYS   B C   1 
ATOM   5381 O  O   . LYS   B 1 349 ? 39.711  0.868   24.809  1.00 26.34 ? 383 LYS   B O   1 
ATOM   5382 C  CB  . LYS   B 1 349 ? 41.885  -0.124  22.227  1.00 27.74 ? 383 LYS   B CB  1 
ATOM   5383 C  CG  . LYS   B 1 349 ? 43.028  -1.079  21.906  1.00 24.13 ? 383 LYS   B CG  1 
ATOM   5384 C  CD  . LYS   B 1 349 ? 43.537  -0.857  20.487  1.00 25.51 ? 383 LYS   B CD  1 
ATOM   5385 C  CE  . LYS   B 1 349 ? 44.710  -1.766  20.136  1.00 33.68 ? 383 LYS   B CE  1 
ATOM   5386 N  NZ  . LYS   B 1 349 ? 45.314  -1.463  18.791  1.00 31.33 ? 383 LYS   B NZ  1 
ATOM   5387 N  N   . PRO   B 1 350 ? 40.666  2.444   23.532  1.00 26.87 ? 384 PRO   B N   1 
ATOM   5388 C  CA  . PRO   B 1 350 ? 39.594  3.398   23.881  1.00 27.15 ? 384 PRO   B CA  1 
ATOM   5389 C  C   . PRO   B 1 350 ? 38.203  2.936   23.434  1.00 23.00 ? 384 PRO   B C   1 
ATOM   5390 O  O   . PRO   B 1 350 ? 38.021  2.338   22.370  1.00 22.60 ? 384 PRO   B O   1 
ATOM   5391 C  CB  . PRO   B 1 350 ? 40.018  4.695   23.163  1.00 23.87 ? 384 PRO   B CB  1 
ATOM   5392 C  CG  . PRO   B 1 350 ? 41.489  4.597   23.019  1.00 18.45 ? 384 PRO   B CG  1 
ATOM   5393 C  CD  . PRO   B 1 350 ? 41.761  3.117   22.795  1.00 27.40 ? 384 PRO   B CD  1 
ATOM   5394 N  N   . LEU   B 1 351 ? 37.210  3.250   24.260  1.00 22.82 ? 385 LEU   B N   1 
ATOM   5395 C  CA  . LEU   B 1 351 ? 35.836  2.844   24.024  1.00 23.42 ? 385 LEU   B CA  1 
ATOM   5396 C  C   . LEU   B 1 351 ? 35.139  3.681   22.965  1.00 28.99 ? 385 LEU   B C   1 
ATOM   5397 O  O   . LEU   B 1 351 ? 34.041  3.308   22.535  1.00 30.40 ? 385 LEU   B O   1 
ATOM   5398 C  CB  . LEU   B 1 351 ? 35.019  2.945   25.316  1.00 24.30 ? 385 LEU   B CB  1 
ATOM   5399 C  CG  . LEU   B 1 351 ? 35.711  2.748   26.657  1.00 21.07 ? 385 LEU   B CG  1 
ATOM   5400 C  CD1 . LEU   B 1 351 ? 34.717  2.948   27.769  1.00 18.89 ? 385 LEU   B CD1 1 
ATOM   5401 C  CD2 . LEU   B 1 351 ? 36.285  1.367   26.691  1.00 23.88 ? 385 LEU   B CD2 1 
ATOM   5402 N  N   . GLY   B 1 352 ? 35.719  4.816   22.571  1.00 31.05 ? 386 GLY   B N   1 
ATOM   5403 C  CA  . GLY   B 1 352 ? 35.077  5.751   21.664  1.00 22.30 ? 386 GLY   B CA  1 
ATOM   5404 C  C   . GLY   B 1 352 ? 36.025  6.297   20.619  1.00 22.53 ? 386 GLY   B C   1 
ATOM   5405 O  O   . GLY   B 1 352 ? 37.094  5.724   20.387  1.00 26.04 ? 386 GLY   B O   1 
ATOM   5406 N  N   . ASP   B 1 353 ? 35.645  7.405   19.971  1.00 24.97 ? 387 ASP   B N   1 
ATOM   5407 C  CA  . ASP   B 1 353 ? 36.486  7.948   18.907  1.00 22.75 ? 387 ASP   B CA  1 
ATOM   5408 C  C   . ASP   B 1 353 ? 37.743  8.599   19.453  1.00 21.34 ? 387 ASP   B C   1 
ATOM   5409 O  O   . ASP   B 1 353 ? 38.781  8.577   18.785  1.00 25.98 ? 387 ASP   B O   1 
ATOM   5410 C  CB  . ASP   B 1 353 ? 35.703  8.948   18.073  1.00 19.28 ? 387 ASP   B CB  1 
ATOM   5411 C  CG  . ASP   B 1 353 ? 34.561  8.305   17.318  1.00 23.15 ? 387 ASP   B CG  1 
ATOM   5412 O  OD1 . ASP   B 1 353 ? 34.718  7.173   16.825  1.00 26.75 ? 387 ASP   B OD1 1 
ATOM   5413 O  OD2 . ASP   B 1 353 ? 33.495  8.927   17.204  1.00 27.36 ? 387 ASP   B OD2 1 
ATOM   5414 N  N   . ARG   B 1 354 ? 37.673  9.171   20.680  1.00 21.78 ? 388 ARG   B N   1 
ATOM   5415 C  CA  . ARG   B 1 354 ? 38.765  9.953   21.253  1.00 19.89 ? 388 ARG   B CA  1 
ATOM   5416 C  C   . ARG   B 1 354 ? 39.640  9.071   22.126  1.00 18.84 ? 388 ARG   B C   1 
ATOM   5417 O  O   . ARG   B 1 354 ? 39.113  8.315   22.939  1.00 21.27 ? 388 ARG   B O   1 
ATOM   5418 C  CB  . ARG   B 1 354 ? 38.222  11.105  22.080  1.00 21.93 ? 388 ARG   B CB  1 
ATOM   5419 C  CG  . ARG   B 1 354 ? 37.259  12.010  21.323  1.00 18.74 ? 388 ARG   B CG  1 
ATOM   5420 C  CD  . ARG   B 1 354 ? 36.999  13.256  22.101  1.00 20.00 ? 388 ARG   B CD  1 
ATOM   5421 N  NE  . ARG   B 1 354 ? 36.005  14.131  21.484  1.00 31.06 ? 388 ARG   B NE  1 
ATOM   5422 C  CZ  . ARG   B 1 354 ? 35.852  15.414  21.815  1.00 30.97 ? 388 ARG   B CZ  1 
ATOM   5423 N  NH1 . ARG   B 1 354 ? 34.919  16.152  21.226  1.00 31.31 ? 388 ARG   B NH1 1 
ATOM   5424 N  NH2 . ARG   B 1 354 ? 36.637  15.957  22.743  1.00 27.54 ? 388 ARG   B NH2 1 
ATOM   5425 N  N   . PRO   B 1 355 ? 40.976  9.148   22.007  1.00 19.34 ? 389 PRO   B N   1 
ATOM   5426 C  CA  . PRO   B 1 355 ? 41.839  8.332   22.871  1.00 17.09 ? 389 PRO   B CA  1 
ATOM   5427 C  C   . PRO   B 1 355 ? 41.761  8.792   24.316  1.00 18.03 ? 389 PRO   B C   1 
ATOM   5428 O  O   . PRO   B 1 355 ? 42.713  9.364   24.850  1.00 24.40 ? 389 PRO   B O   1 
ATOM   5429 C  CB  . PRO   B 1 355 ? 43.234  8.552   22.274  1.00 13.22 ? 389 PRO   B CB  1 
ATOM   5430 C  CG  . PRO   B 1 355 ? 43.162  9.890   21.675  1.00 15.78 ? 389 PRO   B CG  1 
ATOM   5431 C  CD  . PRO   B 1 355 ? 41.756  10.113  21.213  1.00 17.70 ? 389 PRO   B CD  1 
ATOM   5432 N  N   . THR   B 1 356 ? 40.624  8.579   24.964  1.00 19.01 ? 390 THR   B N   1 
ATOM   5433 C  CA  . THR   B 1 356 ? 40.472  9.136   26.302  1.00 22.01 ? 390 THR   B CA  1 
ATOM   5434 C  C   . THR   B 1 356 ? 40.097  8.062   27.313  1.00 21.33 ? 390 THR   B C   1 
ATOM   5435 O  O   . THR   B 1 356 ? 40.960  7.594   28.053  1.00 22.82 ? 390 THR   B O   1 
ATOM   5436 C  CB  . THR   B 1 356 ? 39.437  10.277  26.315  1.00 19.01 ? 390 THR   B CB  1 
ATOM   5437 O  OG1 . THR   B 1 356 ? 38.211  9.844   25.702  1.00 21.43 ? 390 THR   B OG1 1 
ATOM   5438 C  CG2 . THR   B 1 356 ? 39.970  11.466  25.573  1.00 19.00 ? 390 THR   B CG2 1 
ATOM   5439 N  N   . ILE   B 1 357 ? 38.837  7.689   27.360  1.00 17.30 ? 391 ILE   B N   1 
ATOM   5440 C  CA  . ILE   B 1 357 ? 38.340  6.734   28.337  1.00 20.96 ? 391 ILE   B CA  1 
ATOM   5441 C  C   . ILE   B 1 357 ? 38.531  5.309   27.826  1.00 26.89 ? 391 ILE   B C   1 
ATOM   5442 O  O   . ILE   B 1 357 ? 38.419  5.019   26.629  1.00 25.03 ? 391 ILE   B O   1 
ATOM   5443 C  CB  . ILE   B 1 357 ? 36.861  7.007   28.673  1.00 22.95 ? 391 ILE   B CB  1 
ATOM   5444 C  CG1 . ILE   B 1 357 ? 36.307  5.909   29.609  1.00 24.16 ? 391 ILE   B CG1 1 
ATOM   5445 C  CG2 . ILE   B 1 357 ? 36.059  7.106   27.415  1.00 18.21 ? 391 ILE   B CG2 1 
ATOM   5446 C  CD1 . ILE   B 1 357 ? 35.000  6.270   30.326  1.00 26.25 ? 391 ILE   B CD1 1 
ATOM   5447 N  N   . PHE   B 1 358 ? 38.822  4.397   28.754  1.00 28.17 ? 392 PHE   B N   1 
ATOM   5448 C  CA  . PHE   B 1 358 ? 38.925  2.987   28.422  1.00 24.59 ? 392 PHE   B CA  1 
ATOM   5449 C  C   . PHE   B 1 358 ? 38.525  2.155   29.637  1.00 25.30 ? 392 PHE   B C   1 
ATOM   5450 O  O   . PHE   B 1 358 ? 38.299  2.674   30.735  1.00 23.06 ? 392 PHE   B O   1 
ATOM   5451 C  CB  . PHE   B 1 358 ? 40.333  2.642   27.940  1.00 23.17 ? 392 PHE   B CB  1 
ATOM   5452 C  CG  . PHE   B 1 358 ? 41.405  3.005   28.913  1.00 22.47 ? 392 PHE   B CG  1 
ATOM   5453 C  CD1 . PHE   B 1 358 ? 42.020  4.233   28.850  1.00 20.15 ? 392 PHE   B CD1 1 
ATOM   5454 C  CD2 . PHE   B 1 358 ? 41.798  2.106   29.899  1.00 25.68 ? 392 PHE   B CD2 1 
ATOM   5455 C  CE1 . PHE   B 1 358 ? 43.016  4.564   29.741  1.00 26.23 ? 392 PHE   B CE1 1 
ATOM   5456 C  CE2 . PHE   B 1 358 ? 42.794  2.426   30.800  1.00 24.94 ? 392 PHE   B CE2 1 
ATOM   5457 C  CZ  . PHE   B 1 358 ? 43.410  3.653   30.731  1.00 26.57 ? 392 PHE   B CZ  1 
ATOM   5458 N  N   . ILE   B 1 359 ? 38.431  0.846   29.419  1.00 25.13 ? 393 ILE   B N   1 
ATOM   5459 C  CA  . ILE   B 1 359 ? 37.996  -0.092  30.444  1.00 23.50 ? 393 ILE   B CA  1 
ATOM   5460 C  C   . ILE   B 1 359 ? 39.152  -1.019  30.778  1.00 26.50 ? 393 ILE   B C   1 
ATOM   5461 O  O   . ILE   B 1 359 ? 40.027  -1.299  29.947  1.00 23.99 ? 393 ILE   B O   1 
ATOM   5462 C  CB  . ILE   B 1 359 ? 36.731  -0.876  30.015  1.00 18.44 ? 393 ILE   B CB  1 
ATOM   5463 C  CG1 . ILE   B 1 359 ? 35.485  -0.093  30.415  1.00 17.21 ? 393 ILE   B CG1 1 
ATOM   5464 C  CG2 . ILE   B 1 359 ? 36.679  -2.270  30.636  1.00 19.39 ? 393 ILE   B CG2 1 
ATOM   5465 C  CD1 . ILE   B 1 359 ? 34.230  -0.502  29.696  1.00 14.40 ? 393 ILE   B CD1 1 
ATOM   5466 N  N   . GLU   B 1 360 ? 39.176  -1.437  32.043  1.00 24.47 ? 394 GLU   B N   1 
ATOM   5467 C  CA  . GLU   B 1 360 ? 40.142  -2.393  32.554  1.00 26.99 ? 394 GLU   B CA  1 
ATOM   5468 C  C   . GLU   B 1 360 ? 39.378  -3.504  33.261  1.00 28.50 ? 394 GLU   B C   1 
ATOM   5469 O  O   . GLU   B 1 360 ? 38.508  -3.231  34.094  1.00 27.11 ? 394 GLU   B O   1 
ATOM   5470 C  CB  . GLU   B 1 360 ? 41.135  -1.699  33.494  1.00 27.36 ? 394 GLU   B CB  1 
ATOM   5471 C  CG  . GLU   B 1 360 ? 41.911  -2.623  34.393  1.00 29.44 ? 394 GLU   B CG  1 
ATOM   5472 C  CD  . GLU   B 1 360 ? 42.489  -1.919  35.613  1.00 32.66 ? 394 GLU   B CD  1 
ATOM   5473 O  OE1 . GLU   B 1 360 ? 42.041  -0.788  35.940  1.00 32.21 ? 394 GLU   B OE1 1 
ATOM   5474 O  OE2 . GLU   B 1 360 ? 43.387  -2.507  36.257  1.00 28.49 ? 394 GLU   B OE2 1 
ATOM   5475 N  N   . ILE   B 1 361 ? 39.698  -4.752  32.917  1.00 27.51 ? 395 ILE   B N   1 
ATOM   5476 C  CA  . ILE   B 1 361 ? 39.069  -5.937  33.490  1.00 25.13 ? 395 ILE   B CA  1 
ATOM   5477 C  C   . ILE   B 1 361 ? 40.017  -6.540  34.520  1.00 30.85 ? 395 ILE   B C   1 
ATOM   5478 O  O   . ILE   B 1 361 ? 41.220  -6.711  34.263  1.00 31.91 ? 395 ILE   B O   1 
ATOM   5479 C  CB  . ILE   B 1 361 ? 38.705  -6.952  32.394  1.00 23.14 ? 395 ILE   B CB  1 
ATOM   5480 C  CG1 . ILE   B 1 361 ? 37.874  -6.266  31.302  1.00 23.52 ? 395 ILE   B CG1 1 
ATOM   5481 C  CG2 . ILE   B 1 361 ? 37.949  -8.122  32.980  1.00 21.17 ? 395 ILE   B CG2 1 
ATOM   5482 C  CD1 . ILE   B 1 361 ? 36.494  -5.828  31.718  1.00 22.23 ? 395 ILE   B CD1 1 
ATOM   5483 N  N   . ILE   B 1 362 ? 39.468  -6.884  35.682  1.00 31.63 ? 396 ILE   B N   1 
ATOM   5484 C  CA  . ILE   B 1 362 ? 40.234  -7.140  36.897  1.00 31.66 ? 396 ILE   B CA  1 
ATOM   5485 C  C   . ILE   B 1 362 ? 39.719  -8.388  37.591  1.00 32.48 ? 396 ILE   B C   1 
ATOM   5486 O  O   . ILE   B 1 362 ? 38.505  -8.587  37.716  1.00 28.92 ? 396 ILE   B O   1 
ATOM   5487 C  CB  . ILE   B 1 362 ? 40.111  -5.951  37.866  1.00 32.57 ? 396 ILE   B CB  1 
ATOM   5488 C  CG1 . ILE   B 1 362 ? 40.731  -4.748  37.254  1.00 40.21 ? 396 ILE   B CG1 1 
ATOM   5489 C  CG2 . ILE   B 1 362 ? 40.965  -6.142  39.070  1.00 34.01 ? 396 ILE   B CG2 1 
ATOM   5490 C  CD1 . ILE   B 1 362 ? 42.023  -5.063  36.797  1.00 43.49 ? 396 ILE   B CD1 1 
ATOM   5491 N  N   . GLN   B 1 363 ? 40.645  -9.202  38.090  1.00 28.68 ? 397 GLN   B N   1 
ATOM   5492 C  CA  . GLN   B 1 363 ? 40.338  -10.160 39.139  1.00 31.02 ? 397 GLN   B CA  1 
ATOM   5493 C  C   . GLN   B 1 363 ? 41.398  -10.025 40.222  1.00 32.78 ? 397 GLN   B C   1 
ATOM   5494 O  O   . GLN   B 1 363 ? 42.588  -9.892  39.918  1.00 30.72 ? 397 GLN   B O   1 
ATOM   5495 C  CB  . GLN   B 1 363 ? 40.259  -11.607 38.605  1.00 36.43 ? 397 GLN   B CB  1 
ATOM   5496 C  CG  . GLN   B 1 363 ? 39.542  -12.568 39.562  1.00 41.59 ? 397 GLN   B CG  1 
ATOM   5497 C  CD  . GLN   B 1 363 ? 39.162  -13.904 38.934  1.00 51.97 ? 397 GLN   B CD  1 
ATOM   5498 O  OE1 . GLN   B 1 363 ? 39.489  -14.182 37.779  1.00 54.38 ? 397 GLN   B OE1 1 
ATOM   5499 N  NE2 . GLN   B 1 363 ? 38.448  -14.733 39.695  1.00 54.27 ? 397 GLN   B NE2 1 
ATOM   5500 N  N   . ARG   B 1 364 ? 40.961  -10.017 41.478  1.00 37.77 ? 398 ARG   B N   1 
ATOM   5501 C  CA  . ARG   B 1 364 ? 41.853  -10.001 42.628  1.00 38.46 ? 398 ARG   B CA  1 
ATOM   5502 C  C   . ARG   B 1 364 ? 41.856  -11.362 43.319  1.00 43.72 ? 398 ARG   B C   1 
ATOM   5503 O  O   . ARG   B 1 364 ? 40.872  -12.111 43.273  1.00 36.25 ? 398 ARG   B O   1 
ATOM   5504 C  CB  . ARG   B 1 364 ? 41.451  -8.914  43.623  1.00 41.49 ? 398 ARG   B CB  1 
ATOM   5505 C  CG  . ARG   B 1 364 ? 41.411  -7.517  43.025  1.00 45.82 ? 398 ARG   B CG  1 
ATOM   5506 C  CD  . ARG   B 1 364 ? 41.286  -6.453  44.103  1.00 36.68 ? 398 ARG   B CD  1 
ATOM   5507 N  NE  . ARG   B 1 364 ? 41.097  -5.121  43.547  1.00 37.78 ? 398 ARG   B NE  1 
ATOM   5508 C  CZ  . ARG   B 1 364 ? 42.073  -4.254  43.288  1.00 41.79 ? 398 ARG   B CZ  1 
ATOM   5509 N  NH1 . ARG   B 1 364 ? 43.344  -4.576  43.512  1.00 39.69 ? 398 ARG   B NH1 1 
ATOM   5510 N  NH2 . ARG   B 1 364 ? 41.769  -3.059  42.793  1.00 37.88 ? 398 ARG   B NH2 1 
ATOM   5511 N  N   . VAL   B 1 365 ? 42.982  -11.662 43.969  1.00 45.37 ? 399 VAL   B N   1 
ATOM   5512 C  CA  . VAL   B 1 365 ? 43.274  -12.978 44.532  1.00 46.17 ? 399 VAL   B CA  1 
ATOM   5513 C  C   . VAL   B 1 365 ? 43.837  -12.793 45.938  1.00 49.83 ? 399 VAL   B C   1 
ATOM   5514 O  O   . VAL   B 1 365 ? 44.851  -12.101 46.111  1.00 46.71 ? 399 VAL   B O   1 
ATOM   5515 C  CB  . VAL   B 1 365 ? 44.276  -13.751 43.657  1.00 44.95 ? 399 VAL   B CB  1 
ATOM   5516 C  CG1 . VAL   B 1 365 ? 44.515  -15.134 44.204  1.00 40.03 ? 399 VAL   B CG1 1 
ATOM   5517 C  CG2 . VAL   B 1 365 ? 43.796  -13.812 42.214  1.00 46.89 ? 399 VAL   B CG2 1 
ATOM   5518 N  N   . GLY   B 1 366 ? 43.200  -13.424 46.928  1.00 47.18 ? 400 GLY   B N   1 
ATOM   5519 C  CA  . GLY   B 1 366 ? 43.641  -13.369 48.319  1.00 50.42 ? 400 GLY   B CA  1 
ATOM   5520 C  C   . GLY   B 1 366 ? 42.813  -12.443 49.196  1.00 50.63 ? 400 GLY   B C   1 
ATOM   5521 O  O   . GLY   B 1 366 ? 41.666  -12.105 48.900  1.00 55.26 ? 400 GLY   B O   1 
ATOM   5522 N  N   . CYS   B 1 367 ? 43.447  -11.998 50.276  1.00 47.34 ? 401 CYS   B N   1 
ATOM   5523 C  CA  . CYS   B 1 367 ? 42.840  -11.078 51.229  1.00 59.87 ? 401 CYS   B CA  1 
ATOM   5524 C  C   . CYS   B 1 367 ? 41.399  -11.426 51.577  1.00 64.82 ? 401 CYS   B C   1 
ATOM   5525 O  O   . CYS   B 1 367 ? 40.486  -10.640 51.326  1.00 59.19 ? 401 CYS   B O   1 
ATOM   5526 C  CB  . CYS   B 1 367 ? 42.915  -9.642  50.702  1.00 57.81 ? 401 CYS   B CB  1 
ATOM   5527 S  SG  . CYS   B 1 367 ? 44.397  -9.279  49.731  1.00 66.83 ? 401 CYS   B SG  1 
ATOM   5528 N  N   . MET   B 1 368 ? 41.197  -12.604 52.155  1.00 62.62 ? 402 MET   B N   1 
ATOM   5529 C  CA  . MET   B 1 368 ? 39.853  -13.018 52.552  1.00 59.12 ? 402 MET   B CA  1 
ATOM   5530 C  C   . MET   B 1 368 ? 39.700  -13.163 54.058  1.00 58.65 ? 402 MET   B C   1 
ATOM   5531 O  O   . MET   B 1 368 ? 40.676  -13.247 54.794  1.00 61.42 ? 402 MET   B O   1 
ATOM   5532 C  CB  . MET   B 1 368 ? 39.463  -14.327 51.879  1.00 57.54 ? 402 MET   B CB  1 
ATOM   5533 C  CG  . MET   B 1 368 ? 39.563  -14.281 50.379  1.00 65.20 ? 402 MET   B CG  1 
ATOM   5534 S  SD  . MET   B 1 368 ? 38.038  -13.706 49.573  1.00 85.04 ? 402 MET   B SD  1 
ATOM   5535 C  CE  . MET   B 1 368 ? 36.773  -14.637 50.471  1.00 76.18 ? 402 MET   B CE  1 
ATOM   5536 N  N   . TYR   B 1 377 ? 34.596  -12.101 53.465  1.00 65.65 ? 411 TYR   B N   1 
ATOM   5537 C  CA  . TYR   B 1 377 ? 34.615  -11.283 52.268  1.00 73.65 ? 411 TYR   B CA  1 
ATOM   5538 C  C   . TYR   B 1 377 ? 36.038  -11.037 51.796  1.00 71.59 ? 411 TYR   B C   1 
ATOM   5539 O  O   . TYR   B 1 377 ? 36.991  -11.354 52.479  1.00 68.67 ? 411 TYR   B O   1 
ATOM   5540 C  CB  . TYR   B 1 377 ? 33.937  -9.944  52.546  1.00 67.06 ? 411 TYR   B CB  1 
ATOM   5541 C  CG  . TYR   B 1 377 ? 34.602  -9.143  53.630  1.00 66.33 ? 411 TYR   B CG  1 
ATOM   5542 C  CD1 . TYR   B 1 377 ? 35.570  -8.225  53.335  1.00 68.77 ? 411 TYR   B CD1 1 
ATOM   5543 C  CD2 . TYR   B 1 377 ? 34.268  -9.316  54.941  1.00 69.83 ? 411 TYR   B CD2 1 
ATOM   5544 C  CE1 . TYR   B 1 377 ? 36.201  -7.503  54.323  1.00 68.79 ? 411 TYR   B CE1 1 
ATOM   5545 C  CE2 . TYR   B 1 377 ? 34.880  -8.592  55.933  1.00 67.79 ? 411 TYR   B CE2 1 
ATOM   5546 C  CZ  . TYR   B 1 377 ? 35.844  -7.686  55.619  1.00 61.71 ? 411 TYR   B CZ  1 
ATOM   5547 O  OH  . TYR   B 1 377 ? 36.450  -6.969  56.599  1.00 55.13 ? 411 TYR   B OH  1 
ATOM   5548 N  N   . GLN   B 1 378 ? 36.173  -10.470 50.607  1.00 69.23 ? 412 GLN   B N   1 
ATOM   5549 C  CA  . GLN   B 1 378 ? 37.479  -10.130 50.094  1.00 65.11 ? 412 GLN   B CA  1 
ATOM   5550 C  C   . GLN   B 1 378 ? 37.607  -8.636  50.209  1.00 66.14 ? 412 GLN   B C   1 
ATOM   5551 O  O   . GLN   B 1 378 ? 36.735  -7.907  49.775  1.00 63.42 ? 412 GLN   B O   1 
ATOM   5552 C  CB  . GLN   B 1 378 ? 37.645  -10.538 48.646  1.00 60.96 ? 412 GLN   B CB  1 
ATOM   5553 C  CG  . GLN   B 1 378 ? 38.750  -9.780  47.938  1.00 60.66 ? 412 GLN   B CG  1 
ATOM   5554 C  CD  . GLN   B 1 378 ? 39.044  -10.342 46.574  1.00 58.46 ? 412 GLN   B CD  1 
ATOM   5555 O  OE1 . GLN   B 1 378 ? 40.002  -11.062 46.401  1.00 55.48 ? 412 GLN   B OE1 1 
ATOM   5556 N  NE2 . GLN   B 1 378 ? 38.215  -10.016 45.606  1.00 47.94 ? 412 GLN   B NE2 1 
ATOM   5557 N  N   . SER   B 1 379 ? 38.715  -8.197  50.791  1.00 65.39 ? 413 SER   B N   1 
ATOM   5558 C  CA  . SER   B 1 379 ? 39.025  -6.795  50.990  1.00 57.31 ? 413 SER   B CA  1 
ATOM   5559 C  C   . SER   B 1 379 ? 39.231  -6.069  49.697  1.00 57.00 ? 413 SER   B C   1 
ATOM   5560 O  O   . SER   B 1 379 ? 39.608  -6.643  48.697  1.00 62.81 ? 413 SER   B O   1 
ATOM   5561 C  CB  . SER   B 1 379 ? 40.290  -6.614  51.817  1.00 47.34 ? 413 SER   B CB  1 
ATOM   5562 O  OG  . SER   B 1 379 ? 40.571  -7.730  52.595  1.00 59.93 ? 413 SER   B OG  1 
ATOM   5563 N  N   . GLY   B 1 380 ? 39.028  -4.774  49.745  1.00 51.02 ? 414 GLY   B N   1 
ATOM   5564 C  CA  . GLY   B 1 380 ? 39.182  -3.948  48.589  1.00 47.56 ? 414 GLY   B CA  1 
ATOM   5565 C  C   . GLY   B 1 380 ? 40.572  -3.459  48.432  1.00 47.37 ? 414 GLY   B C   1 
ATOM   5566 O  O   . GLY   B 1 380 ? 41.133  -2.962  49.363  1.00 48.48 ? 414 GLY   B O   1 
ATOM   5567 N  N   . GLY   B 1 381 ? 41.120  -3.627  47.245  1.00 44.29 ? 415 GLY   B N   1 
ATOM   5568 C  CA  . GLY   B 1 381 ? 42.455  -3.186  46.966  1.00 42.39 ? 415 GLY   B CA  1 
ATOM   5569 C  C   . GLY   B 1 381 ? 43.474  -4.268  46.976  1.00 44.75 ? 415 GLY   B C   1 
ATOM   5570 O  O   . GLY   B 1 381 ? 44.591  -3.993  46.690  1.00 46.53 ? 415 GLY   B O   1 
ATOM   5571 N  N   . CYS   B 1 382 ? 43.084  -5.495  47.301  1.00 52.08 ? 416 CYS   B N   1 
ATOM   5572 C  CA  . CYS   B 1 382 ? 43.992  -6.638  47.352  1.00 47.84 ? 416 CYS   B CA  1 
ATOM   5573 C  C   . CYS   B 1 382 ? 44.719  -6.759  46.072  1.00 43.18 ? 416 CYS   B C   1 
ATOM   5574 O  O   . CYS   B 1 382 ? 44.146  -7.109  45.087  1.00 39.94 ? 416 CYS   B O   1 
ATOM   5575 C  CB  . CYS   B 1 382 ? 43.255  -7.968  47.615  1.00 55.16 ? 416 CYS   B CB  1 
ATOM   5576 S  SG  . CYS   B 1 382 ? 44.289  -9.458  47.785  1.00 59.60 ? 416 CYS   B SG  1 
ATOM   5577 N  N   . GLY   B 1 383 ? 46.003  -6.493  46.105  1.00 43.51 ? 417 GLY   B N   1 
ATOM   5578 C  CA  . GLY   B 1 383 ? 46.825  -6.577  44.925  1.00 46.57 ? 417 GLY   B CA  1 
ATOM   5579 C  C   . GLY   B 1 383 ? 47.281  -5.246  44.376  1.00 47.44 ? 417 GLY   B C   1 
ATOM   5580 O  O   . GLY   B 1 383 ? 48.156  -5.195  43.536  1.00 46.11 ? 417 GLY   B O   1 
ATOM   5581 N  N   . GLY   B 1 384 ? 46.674  -4.172  44.853  1.00 37.50 ? 418 GLY   B N   1 
ATOM   5582 C  CA  . GLY   B 1 384 ? 47.025  -2.861  44.402  1.00 32.28 ? 418 GLY   B CA  1 
ATOM   5583 C  C   . GLY   B 1 384 ? 46.292  -2.491  43.149  1.00 40.59 ? 418 GLY   B C   1 
ATOM   5584 O  O   . GLY   B 1 384 ? 45.199  -2.950  42.914  1.00 38.73 ? 418 GLY   B O   1 
ATOM   5585 N  N   . PHE   B 1 385 ? 46.963  -1.721  42.309  1.00 38.12 ? 419 PHE   B N   1 
ATOM   5586 C  CA  . PHE   B 1 385 ? 46.367  -1.196  41.089  1.00 33.67 ? 419 PHE   B CA  1 
ATOM   5587 C  C   . PHE   B 1 385 ? 47.265  -1.410  39.880  1.00 38.73 ? 419 PHE   B C   1 
ATOM   5588 O  O   . PHE   B 1 385 ? 46.953  -0.909  38.791  1.00 36.34 ? 419 PHE   B O   1 
ATOM   5589 C  CB  . PHE   B 1 385 ? 46.041  0.296   41.254  1.00 31.63 ? 419 PHE   B CB  1 
ATOM   5590 C  CG  . PHE   B 1 385 ? 45.026  0.570   42.318  1.00 34.40 ? 419 PHE   B CG  1 
ATOM   5591 C  CD1 . PHE   B 1 385 ? 45.411  0.728   43.642  1.00 33.70 ? 419 PHE   B CD1 1 
ATOM   5592 C  CD2 . PHE   B 1 385 ? 43.676  0.636   42.000  1.00 35.20 ? 419 PHE   B CD2 1 
ATOM   5593 C  CE1 . PHE   B 1 385 ? 44.470  0.952   44.623  1.00 39.23 ? 419 PHE   B CE1 1 
ATOM   5594 C  CE2 . PHE   B 1 385 ? 42.725  0.864   42.970  1.00 33.78 ? 419 PHE   B CE2 1 
ATOM   5595 C  CZ  . PHE   B 1 385 ? 43.118  1.020   44.287  1.00 42.64 ? 419 PHE   B CZ  1 
ATOM   5596 N  N   . GLY   B 1 386 ? 48.369  -2.134  40.043  1.00 40.34 ? 420 GLY   B N   1 
ATOM   5597 C  CA  . GLY   B 1 386 ? 49.206  -2.526  38.935  1.00 35.56 ? 420 GLY   B CA  1 
ATOM   5598 C  C   . GLY   B 1 386 ? 50.425  -1.671  38.708  1.00 34.12 ? 420 GLY   B C   1 
ATOM   5599 O  O   . GLY   B 1 386 ? 51.175  -1.939  37.768  1.00 38.41 ? 420 GLY   B O   1 
ATOM   5600 N  N   . LYS   B 1 387 ? 50.655  -0.655  39.536  1.00 41.57 ? 421 LYS   B N   1 
ATOM   5601 C  CA  . LYS   B 1 387 ? 51.727  0.290   39.237  1.00 42.49 ? 421 LYS   B CA  1 
ATOM   5602 C  C   . LYS   B 1 387 ? 53.051  -0.430  39.004  1.00 41.56 ? 421 LYS   B C   1 
ATOM   5603 O  O   . LYS   B 1 387 ? 53.831  -0.027  38.135  1.00 43.44 ? 421 LYS   B O   1 
ATOM   5604 C  CB  . LYS   B 1 387 ? 51.842  1.341   40.356  1.00 45.18 ? 421 LYS   B CB  1 
ATOM   5605 C  CG  . LYS   B 1 387 ? 50.822  2.517   40.270  1.00 41.15 ? 421 LYS   B CG  1 
ATOM   5606 C  CD  . LYS   B 1 387 ? 50.804  3.378   41.554  1.00 37.42 ? 421 LYS   B CD  1 
ATOM   5607 C  CE  . LYS   B 1 387 ? 51.520  4.719   41.382  1.00 51.34 ? 421 LYS   B CE  1 
ATOM   5608 N  NZ  . LYS   B 1 387 ? 51.763  5.415   42.697  1.00 55.69 ? 421 LYS   B NZ  1 
ATOM   5609 N  N   . GLY   B 1 388 ? 53.295  -1.534  39.709  1.00 43.29 ? 422 GLY   B N   1 
ATOM   5610 C  CA  . GLY   B 1 388 ? 54.519  -2.277  39.479  1.00 40.19 ? 422 GLY   B CA  1 
ATOM   5611 C  C   . GLY   B 1 388 ? 54.696  -2.731  38.048  1.00 44.08 ? 422 GLY   B C   1 
ATOM   5612 O  O   . GLY   B 1 388 ? 55.820  -3.029  37.633  1.00 45.04 ? 422 GLY   B O   1 
ATOM   5613 N  N   . ASN   B 1 389 ? 53.612  -2.760  37.272  1.00 47.74 ? 423 ASN   B N   1 
ATOM   5614 C  CA  . ASN   B 1 389 ? 53.628  -3.282  35.912  1.00 44.67 ? 423 ASN   B CA  1 
ATOM   5615 C  C   . ASN   B 1 389 ? 54.073  -2.267  34.869  1.00 47.63 ? 423 ASN   B C   1 
ATOM   5616 O  O   . ASN   B 1 389 ? 54.259  -2.652  33.709  1.00 45.58 ? 423 ASN   B O   1 
ATOM   5617 C  CB  . ASN   B 1 389 ? 52.245  -3.792  35.539  1.00 46.77 ? 423 ASN   B CB  1 
ATOM   5618 C  CG  . ASN   B 1 389 ? 52.151  -5.279  35.581  1.00 45.18 ? 423 ASN   B CG  1 
ATOM   5619 O  OD1 . ASN   B 1 389 ? 53.107  -5.978  35.246  1.00 45.52 ? 423 ASN   B OD1 1 
ATOM   5620 N  ND2 . ASN   B 1 389 ? 50.990  -5.786  35.986  1.00 39.38 ? 423 ASN   B ND2 1 
ATOM   5621 N  N   . PHE   B 1 390 ? 54.216  -0.989  35.233  1.00 47.72 ? 424 PHE   B N   1 
ATOM   5622 C  CA  . PHE   B 1 390 ? 54.897  -0.050  34.346  1.00 49.74 ? 424 PHE   B CA  1 
ATOM   5623 C  C   . PHE   B 1 390 ? 56.334  -0.504  34.127  1.00 47.35 ? 424 PHE   B C   1 
ATOM   5624 O  O   . PHE   B 1 390 ? 56.738  -0.832  33.006  1.00 41.59 ? 424 PHE   B O   1 
ATOM   5625 C  CB  . PHE   B 1 390 ? 54.851  1.386   34.917  1.00 45.99 ? 424 PHE   B CB  1 
ATOM   5626 C  CG  . PHE   B 1 390 ? 53.507  2.051   34.795  1.00 40.08 ? 424 PHE   B CG  1 
ATOM   5627 C  CD1 . PHE   B 1 390 ? 52.632  2.074   35.866  1.00 38.39 ? 424 PHE   B CD1 1 
ATOM   5628 C  CD2 . PHE   B 1 390 ? 53.111  2.641   33.603  1.00 40.20 ? 424 PHE   B CD2 1 
ATOM   5629 C  CE1 . PHE   B 1 390 ? 51.376  2.676   35.754  1.00 39.43 ? 424 PHE   B CE1 1 
ATOM   5630 C  CE2 . PHE   B 1 390 ? 51.862  3.241   33.483  1.00 42.10 ? 424 PHE   B CE2 1 
ATOM   5631 C  CZ  . PHE   B 1 390 ? 50.992  3.258   34.564  1.00 36.26 ? 424 PHE   B CZ  1 
ATOM   5632 N  N   . SER   B 1 391 ? 57.113  -0.549  35.209  1.00 48.84 ? 425 SER   B N   1 
ATOM   5633 C  CA  . SER   B 1 391 ? 58.507  -0.952  35.109  1.00 44.79 ? 425 SER   B CA  1 
ATOM   5634 C  C   . SER   B 1 391 ? 58.625  -2.324  34.456  1.00 56.03 ? 425 SER   B C   1 
ATOM   5635 O  O   . SER   B 1 391 ? 59.397  -2.507  33.508  1.00 60.01 ? 425 SER   B O   1 
ATOM   5636 C  CB  . SER   B 1 391 ? 59.136  -0.944  36.504  1.00 46.33 ? 425 SER   B CB  1 
ATOM   5637 O  OG  . SER   B 1 391 ? 60.545  -1.080  36.453  1.00 62.06 ? 425 SER   B OG  1 
ATOM   5638 N  N   . GLU   B 1 392 ? 57.902  -3.297  34.965  1.00 54.89 ? 426 GLU   B N   1 
ATOM   5639 C  CA  . GLU   B 1 392 ? 57.971  -4.635  34.462  1.00 49.65 ? 426 GLU   B CA  1 
ATOM   5640 C  C   . GLU   B 1 392 ? 57.907  -4.752  32.966  1.00 54.45 ? 426 GLU   B C   1 
ATOM   5641 O  O   . GLU   B 1 392 ? 58.699  -5.436  32.367  1.00 56.04 ? 426 GLU   B O   1 
ATOM   5642 C  CB  . GLU   B 1 392 ? 56.862  -5.465  35.070  1.00 49.48 ? 426 GLU   B CB  1 
ATOM   5643 C  CG  . GLU   B 1 392 ? 56.890  -6.903  34.661  1.00 46.60 ? 426 GLU   B CG  1 
ATOM   5644 C  CD  . GLU   B 1 392 ? 58.109  -7.599  35.161  1.00 56.54 ? 426 GLU   B CD  1 
ATOM   5645 O  OE1 . GLU   B 1 392 ? 58.813  -7.052  36.021  1.00 52.10 ? 426 GLU   B OE1 1 
ATOM   5646 O  OE2 . GLU   B 1 392 ? 58.365  -8.697  34.679  1.00 61.70 ? 426 GLU   B OE2 1 
ATOM   5647 N  N   . LEU   B 1 393 ? 56.950  -4.103  32.352  1.00 51.69 ? 427 LEU   B N   1 
ATOM   5648 C  CA  . LEU   B 1 393 ? 56.796  -4.199  30.903  1.00 50.40 ? 427 LEU   B CA  1 
ATOM   5649 C  C   . LEU   B 1 393 ? 58.024  -3.672  30.173  1.00 52.07 ? 427 LEU   B C   1 
ATOM   5650 O  O   . LEU   B 1 393 ? 58.612  -4.384  29.349  1.00 54.13 ? 427 LEU   B O   1 
ATOM   5651 C  CB  . LEU   B 1 393 ? 55.540  -3.455  30.468  1.00 47.25 ? 427 LEU   B CB  1 
ATOM   5652 C  CG  . LEU   B 1 393 ? 54.331  -4.378  30.472  1.00 46.78 ? 427 LEU   B CG  1 
ATOM   5653 C  CD1 . LEU   B 1 393 ? 53.055  -3.622  30.787  1.00 45.71 ? 427 LEU   B CD1 1 
ATOM   5654 C  CD2 . LEU   B 1 393 ? 54.228  -5.068  29.115  1.00 54.69 ? 427 LEU   B CD2 1 
ATOM   5655 N  N   . PHE   B 1 394 ? 58.416  -2.421  30.457  1.00 51.84 ? 428 PHE   B N   1 
ATOM   5656 C  CA  . PHE   B 1 394 ? 59.635  -1.836  29.900  1.00 55.18 ? 428 PHE   B CA  1 
ATOM   5657 C  C   . PHE   B 1 394 ? 60.786  -2.838  29.880  1.00 57.67 ? 428 PHE   B C   1 
ATOM   5658 O  O   . PHE   B 1 394 ? 61.397  -3.081  28.835  1.00 59.65 ? 428 PHE   B O   1 
ATOM   5659 C  CB  . PHE   B 1 394 ? 60.027  -0.591  30.703  1.00 50.47 ? 428 PHE   B CB  1 
ATOM   5660 N  N   . LYS   B 1 395 ? 61.080  -3.442  31.034  1.00 58.18 ? 429 LYS   B N   1 
ATOM   5661 C  CA  . LYS   B 1 395 ? 62.121  -4.461  31.099  1.00 55.61 ? 429 LYS   B CA  1 
ATOM   5662 C  C   . LYS   B 1 395 ? 61.830  -5.605  30.138  1.00 54.43 ? 429 LYS   B C   1 
ATOM   5663 O  O   . LYS   B 1 395 ? 62.697  -6.006  29.354  1.00 56.08 ? 429 LYS   B O   1 
ATOM   5664 C  CB  . LYS   B 1 395 ? 62.253  -4.986  32.529  1.00 58.53 ? 429 LYS   B CB  1 
ATOM   5665 N  N   . SER   B 1 396 ? 60.608  -6.140  30.178  1.00 51.30 ? 430 SER   B N   1 
ATOM   5666 C  CA  . SER   B 1 396 ? 60.299  -7.319  29.378  1.00 51.95 ? 430 SER   B CA  1 
ATOM   5667 C  C   . SER   B 1 396 ? 60.361  -7.021  27.886  1.00 56.59 ? 430 SER   B C   1 
ATOM   5668 O  O   . SER   B 1 396 ? 60.651  -7.924  27.090  1.00 53.64 ? 430 SER   B O   1 
ATOM   5669 C  CB  . SER   B 1 396 ? 58.927  -7.869  29.763  1.00 51.31 ? 430 SER   B CB  1 
ATOM   5670 O  OG  . SER   B 1 396 ? 58.959  -8.489  31.047  1.00 53.66 ? 430 SER   B OG  1 
ATOM   5671 N  N   . ILE   B 1 397 ? 60.115  -5.764  27.497  1.00 56.65 ? 431 ILE   B N   1 
ATOM   5672 C  CA  . ILE   B 1 397 ? 60.114  -5.379  26.088  1.00 48.65 ? 431 ILE   B CA  1 
ATOM   5673 C  C   . ILE   B 1 397 ? 61.528  -5.132  25.583  1.00 58.45 ? 431 ILE   B C   1 
ATOM   5674 O  O   . ILE   B 1 397 ? 61.804  -5.332  24.393  1.00 60.01 ? 431 ILE   B O   1 
ATOM   5675 C  CB  . ILE   B 1 397 ? 59.227  -4.142  25.869  1.00 50.59 ? 431 ILE   B CB  1 
ATOM   5676 N  N   . GLU   B 1 398 ? 62.439  -4.692  26.460  1.00 56.25 ? 432 GLU   B N   1 
ATOM   5677 C  CA  . GLU   B 1 398 ? 63.841  -4.527  26.083  1.00 56.19 ? 432 GLU   B CA  1 
ATOM   5678 C  C   . GLU   B 1 398 ? 64.609  -5.850  26.110  1.00 59.78 ? 432 GLU   B C   1 
ATOM   5679 O  O   . GLU   B 1 398 ? 65.529  -6.042  25.306  1.00 59.61 ? 432 GLU   B O   1 
ATOM   5680 C  CB  . GLU   B 1 398 ? 64.512  -3.501  27.000  1.00 50.60 ? 432 GLU   B CB  1 
ATOM   5681 N  N   . GLU   B 1 399 ? 64.266  -6.763  27.025  1.00 57.94 ? 433 GLU   B N   1 
ATOM   5682 C  CA  . GLU   B 1 399 ? 64.844  -8.103  26.981  1.00 58.00 ? 433 GLU   B CA  1 
ATOM   5683 C  C   . GLU   B 1 399 ? 64.424  -8.828  25.710  1.00 61.39 ? 433 GLU   B C   1 
ATOM   5684 O  O   . GLU   B 1 399 ? 65.219  -9.555  25.102  1.00 65.15 ? 433 GLU   B O   1 
ATOM   5685 C  CB  . GLU   B 1 399 ? 64.425  -8.905  28.218  1.00 57.10 ? 433 GLU   B CB  1 
ATOM   5686 N  N   . TYR   B 1 400 ? 63.177  -8.627  25.286  1.00 56.37 ? 434 TYR   B N   1 
ATOM   5687 C  CA  . TYR   B 1 400 ? 62.694  -9.282  24.078  1.00 59.62 ? 434 TYR   B CA  1 
ATOM   5688 C  C   . TYR   B 1 400 ? 63.344  -8.696  22.830  1.00 64.67 ? 434 TYR   B C   1 
ATOM   5689 O  O   . TYR   B 1 400 ? 63.708  -9.436  21.909  1.00 67.42 ? 434 TYR   B O   1 
ATOM   5690 C  CB  . TYR   B 1 400 ? 61.172  -9.168  24.000  1.00 56.14 ? 434 TYR   B CB  1 
ATOM   5691 C  CG  . TYR   B 1 400 ? 60.569  -9.958  22.873  1.00 57.42 ? 434 TYR   B CG  1 
ATOM   5692 C  CD1 . TYR   B 1 400 ? 60.892  -11.300 22.698  1.00 67.39 ? 434 TYR   B CD1 1 
ATOM   5693 C  CD2 . TYR   B 1 400 ? 59.668  -9.378  21.990  1.00 59.13 ? 434 TYR   B CD2 1 
ATOM   5694 C  CE1 . TYR   B 1 400 ? 60.346  -12.044 21.667  1.00 63.83 ? 434 TYR   B CE1 1 
ATOM   5695 C  CE2 . TYR   B 1 400 ? 59.109  -10.118 20.955  1.00 57.24 ? 434 TYR   B CE2 1 
ATOM   5696 C  CZ  . TYR   B 1 400 ? 59.455  -11.448 20.802  1.00 59.23 ? 434 TYR   B CZ  1 
ATOM   5697 O  OH  . TYR   B 1 400 ? 58.913  -12.198 19.789  1.00 63.65 ? 434 TYR   B OH  1 
ATOM   5698 N  N   . GLU   B 1 401 ? 63.503  -7.368  22.783  1.00 67.03 ? 435 GLU   B N   1 
ATOM   5699 C  CA  . GLU   B 1 401 ? 64.054  -6.712  21.601  1.00 64.96 ? 435 GLU   B CA  1 
ATOM   5700 C  C   . GLU   B 1 401 ? 65.531  -7.025  21.394  1.00 68.45 ? 435 GLU   B C   1 
ATOM   5701 O  O   . GLU   B 1 401 ? 66.048  -6.793  20.298  1.00 64.00 ? 435 GLU   B O   1 
ATOM   5702 C  CB  . GLU   B 1 401 ? 63.850  -5.196  21.689  1.00 58.83 ? 435 GLU   B CB  1 
ATOM   5703 N  N   . LYS   B 1 402 ? 66.218  -7.547  22.409  1.00 71.37 ? 436 LYS   B N   1 
ATOM   5704 C  CA  . LYS   B 1 402 ? 67.607  -7.959  22.275  1.00 72.19 ? 436 LYS   B CA  1 
ATOM   5705 C  C   . LYS   B 1 402 ? 67.769  -9.474  22.120  1.00 77.07 ? 436 LYS   B C   1 
ATOM   5706 O  O   . LYS   B 1 402 ? 68.891  -9.942  21.903  1.00 81.75 ? 436 LYS   B O   1 
ATOM   5707 C  CB  . LYS   B 1 402 ? 68.425  -7.451  23.475  1.00 65.22 ? 436 LYS   B CB  1 
ATOM   5708 N  N   . THR   B 1 403 ? 66.690  -10.252 22.209  1.00 72.77 ? 437 THR   B N   1 
ATOM   5709 C  CA  . THR   B 1 403 ? 66.794  -11.687 21.938  1.00 77.28 ? 437 THR   B CA  1 
ATOM   5710 C  C   . THR   B 1 403 ? 65.478  -12.312 21.471  1.00 74.30 ? 437 THR   B C   1 
ATOM   5711 O  O   . THR   B 1 403 ? 64.403  -11.998 21.980  1.00 68.93 ? 437 THR   B O   1 
ATOM   5712 C  CB  . THR   B 1 403 ? 67.305  -12.466 23.171  1.00 67.48 ? 437 THR   B CB  1 
ATOM   5713 O  OG1 . THR   B 1 403 ? 67.677  -13.788 22.766  1.00 76.27 ? 437 THR   B OG1 1 
ATOM   5714 C  CG2 . THR   B 1 403 ? 66.247  -12.546 24.274  1.00 60.06 ? 437 THR   B CG2 1 
HETATM 5715 CO CO  . CO    C 2 .   ? 11.045  1.351   0.570   1.00 31.00 ? 501 CO    A CO  1 
HETATM 5716 C  C13 . A1LWU D 3 .   ? 8.351   2.223   1.369   1.00 33.84 ? 502 A1LWU A C13 1 
HETATM 5717 C  C17 . A1LWU D 3 .   ? 8.213   4.414   -1.746  1.00 31.37 ? 502 A1LWU A C17 1 
HETATM 5718 C  C20 . A1LWU D 3 .   ? 6.614   4.084   0.689   1.00 33.86 ? 502 A1LWU A C20 1 
HETATM 5719 C  C24 . A1LWU D 3 .   ? 5.271   1.589   8.294   1.00 36.62 ? 502 A1LWU A C24 1 
HETATM 5720 C  C26 . A1LWU D 3 .   ? 3.710   -1.756  3.939   1.00 50.92 ? 502 A1LWU A C26 1 
HETATM 5721 C  C28 . A1LWU D 3 .   ? 7.803   1.296   8.788   1.00 29.23 ? 502 A1LWU A C28 1 
HETATM 5722 C  C01 . A1LWU D 3 .   ? 7.414   1.627   2.341   1.00 31.03 ? 502 A1LWU A C01 1 
HETATM 5723 C  C02 . A1LWU D 3 .   ? 6.611   0.512   1.706   1.00 34.32 ? 502 A1LWU A C02 1 
HETATM 5724 C  C03 . A1LWU D 3 .   ? 5.636   -0.198  2.595   1.00 33.13 ? 502 A1LWU A C03 1 
HETATM 5725 C  C04 . A1LWU D 3 .   ? 5.500   0.190   4.023   1.00 33.93 ? 502 A1LWU A C04 1 
HETATM 5726 C  C05 . A1LWU D 3 .   ? 6.273   1.302   4.756   1.00 42.55 ? 502 A1LWU A C05 1 
HETATM 5727 C  C06 . A1LWU D 3 .   ? 7.291   2.030   3.808   1.00 30.73 ? 502 A1LWU A C06 1 
HETATM 5728 N  N07 . A1LWU D 3 .   ? 4.339   -0.785  4.736   1.00 36.95 ? 502 A1LWU A N07 1 
HETATM 5729 C  C08 . A1LWU D 3 .   ? 3.907   -0.724  6.288   1.00 46.25 ? 502 A1LWU A C08 1 
HETATM 5730 C  C09 . A1LWU D 3 .   ? 4.550   0.274   7.093   1.00 52.39 ? 502 A1LWU A C09 1 
HETATM 5731 N  N10 . A1LWU D 3 .   ? 5.344   1.052   6.965   1.00 44.09 ? 502 A1LWU A N10 1 
HETATM 5732 C  C11 . A1LWU D 3 .   ? 6.101   1.593   6.005   1.00 41.69 ? 502 A1LWU A C11 1 
HETATM 5733 C  C12 . A1LWU D 3 .   ? 8.199   3.147   4.212   1.00 28.62 ? 502 A1LWU A C12 1 
HETATM 5734 C  C14 . A1LWU D 3 .   ? 7.992   3.466   0.611   1.00 34.30 ? 502 A1LWU A C14 1 
HETATM 5735 O  O15 . A1LWU D 3 .   ? 9.366   1.645   1.216   1.00 31.26 ? 502 A1LWU A O15 1 
HETATM 5736 C  C16 . A1LWU D 3 .   ? 8.845   3.671   -0.598  1.00 31.22 ? 502 A1LWU A C16 1 
HETATM 5737 C  C18 . A1LWU D 3 .   ? 6.705   4.270   -1.843  1.00 32.66 ? 502 A1LWU A C18 1 
HETATM 5738 C  C19 . A1LWU D 3 .   ? 5.982   4.628   -0.558  1.00 32.11 ? 502 A1LWU A C19 1 
HETATM 5739 O  O21 . A1LWU D 3 .   ? 9.819   2.706   -0.824  1.00 30.78 ? 502 A1LWU A O21 1 
HETATM 5740 O  O22 . A1LWU D 3 .   ? 6.045   4.165   1.675   1.00 36.45 ? 502 A1LWU A O22 1 
HETATM 5741 O  O23 . A1LWU D 3 .   ? 6.765   2.451   6.352   1.00 39.15 ? 502 A1LWU A O23 1 
HETATM 5742 O  O25 . A1LWU D 3 .   ? 3.099   -1.466  6.651   1.00 50.25 ? 502 A1LWU A O25 1 
HETATM 5743 C  C27 . A1LWU D 3 .   ? 6.443   1.715   9.182   1.00 28.98 ? 502 A1LWU A C27 1 
HETATM 5744 C  C29 . A1LWU D 3 .   ? 8.888   1.465   9.793   1.00 29.71 ? 502 A1LWU A C29 1 
HETATM 5745 C  C30 . A1LWU D 3 .   ? 8.644   2.078   11.132  1.00 22.66 ? 502 A1LWU A C30 1 
HETATM 5746 C  C31 . A1LWU D 3 .   ? 7.268   2.487   11.509  1.00 24.17 ? 502 A1LWU A C31 1 
HETATM 5747 C  C32 . A1LWU D 3 .   ? 6.169   2.309   10.519  1.00 29.48 ? 502 A1LWU A C32 1 
HETATM 5748 C  C33 . A1LWU D 3 .   ? 9.776   2.231   12.104  1.00 24.98 ? 502 A1LWU A C33 1 
HETATM 5749 N  N34 . A1LWU D 3 .   ? 10.614  2.342   12.852  1.00 26.87 ? 502 A1LWU A N34 1 
HETATM 5750 CO CO  . CO    E 2 .   ? 43.061  0.621   37.362  1.00 31.75 ? 501 CO    B CO  1 
HETATM 5751 C  C13 . A1LWU F 3 .   ? 45.860  1.852   36.519  1.00 35.47 ? 502 A1LWU B C13 1 
HETATM 5752 C  C17 . A1LWU F 3 .   ? 45.763  3.797   39.784  1.00 38.16 ? 502 A1LWU B C17 1 
HETATM 5753 C  C20 . A1LWU F 3 .   ? 47.353  3.868   37.342  1.00 37.24 ? 502 A1LWU B C20 1 
HETATM 5754 C  C24 . A1LWU F 3 .   ? 48.894  2.044   29.491  1.00 38.09 ? 502 A1LWU B C24 1 
HETATM 5755 C  C26 . A1LWU F 3 .   ? 50.631  -1.701  33.515  1.00 55.29 ? 502 A1LWU B C26 1 
HETATM 5756 C  C28 . A1LWU F 3 .   ? 47.684  3.033   27.485  1.00 36.85 ? 502 A1LWU B C28 1 
HETATM 5757 C  C01 . A1LWU F 3 .   ? 46.808  1.395   35.467  1.00 30.15 ? 502 A1LWU B C01 1 
HETATM 5758 C  C02 . A1LWU F 3 .   ? 47.658  0.257   35.962  1.00 36.84 ? 502 A1LWU B C02 1 
HETATM 5759 C  C03 . A1LWU F 3 .   ? 48.659  -0.328  35.004  1.00 38.60 ? 502 A1LWU B C03 1 
HETATM 5760 C  C04 . A1LWU F 3 .   ? 48.782  0.207   33.617  1.00 38.42 ? 502 A1LWU B C04 1 
HETATM 5761 C  C05 . A1LWU F 3 .   ? 47.957  1.360   33.020  1.00 39.57 ? 502 A1LWU B C05 1 
HETATM 5762 C  C06 . A1LWU F 3 .   ? 46.926  1.938   34.051  1.00 30.69 ? 502 A1LWU B C06 1 
HETATM 5763 N  N07 . A1LWU F 3 .   ? 49.977  -0.662  32.791  1.00 42.39 ? 502 A1LWU B N07 1 
HETATM 5764 C  C08 . A1LWU F 3 .   ? 50.391  -0.406  31.241  1.00 39.66 ? 502 A1LWU B C08 1 
HETATM 5765 C  C09 . A1LWU F 3 .   ? 49.715  0.642   30.569  1.00 55.57 ? 502 A1LWU B C09 1 
HETATM 5766 N  N10 . A1LWU F 3 .   ? 48.887  1.377   30.787  1.00 50.62 ? 502 A1LWU B N10 1 
HETATM 5767 C  C11 . A1LWU F 3 .   ? 48.104  1.784   31.807  1.00 41.11 ? 502 A1LWU B C11 1 
HETATM 5768 C  C12 . A1LWU F 3 .   ? 45.973  3.070   33.776  1.00 36.73 ? 502 A1LWU B C12 1 
HETATM 5769 C  C14 . A1LWU F 3 .   ? 46.017  3.162   37.279  1.00 38.46 ? 502 A1LWU B C14 1 
HETATM 5770 O  O15 . A1LWU F 3 .   ? 44.943  1.140   36.795  1.00 31.53 ? 502 A1LWU B O15 1 
HETATM 5771 C  C16 . A1LWU F 3 .   ? 45.197  3.136   38.547  1.00 35.43 ? 502 A1LWU B C16 1 
HETATM 5772 C  C18 . A1LWU F 3 .   ? 47.283  3.714   39.752  1.00 38.55 ? 502 A1LWU B C18 1 
HETATM 5773 C  C19 . A1LWU F 3 .   ? 47.831  4.519   38.578  1.00 35.79 ? 502 A1LWU B C19 1 
HETATM 5774 O  O21 . A1LWU F 3 .   ? 44.172  2.184   38.652  1.00 32.62 ? 502 A1LWU B O21 1 
HETATM 5775 O  O22 . A1LWU F 3 .   ? 48.061  3.920   36.444  1.00 42.50 ? 502 A1LWU B O22 1 
HETATM 5776 O  O23 . A1LWU F 3 .   ? 47.404  2.641   31.553  1.00 35.78 ? 502 A1LWU B O23 1 
HETATM 5777 O  O25 . A1LWU F 3 .   ? 51.220  -1.022  30.747  1.00 43.73 ? 502 A1LWU B O25 1 
HETATM 5778 C  C27 . A1LWU F 3 .   ? 47.623  2.210   28.723  1.00 26.06 ? 502 A1LWU B C27 1 
HETATM 5779 C  C29 . A1LWU F 3 .   ? 46.472  3.280   26.644  1.00 26.57 ? 502 A1LWU B C29 1 
HETATM 5780 C  C30 . A1LWU F 3 .   ? 45.177  2.694   27.058  1.00 21.73 ? 502 A1LWU B C30 1 
HETATM 5781 C  C31 . A1LWU F 3 .   ? 45.113  1.863   28.297  1.00 23.05 ? 502 A1LWU B C31 1 
HETATM 5782 C  C32 . A1LWU F 3 .   ? 46.326  1.617   29.139  1.00 31.08 ? 502 A1LWU B C32 1 
HETATM 5783 C  C33 . A1LWU F 3 .   ? 43.927  2.934   26.224  1.00 25.06 ? 502 A1LWU B C33 1 
HETATM 5784 N  N34 . A1LWU F 3 .   ? 42.996  3.103   25.626  1.00 26.28 ? 502 A1LWU B N34 1 
HETATM 5785 O  O   . HOH   G 4 .   ? 39.801  12.361  0.848   1.00 44.37 ? 601 HOH   A O   1 
HETATM 5786 O  O   . HOH   G 4 .   ? 9.853   3.958   -15.477 1.00 62.83 ? 602 HOH   A O   1 
HETATM 5787 O  O   . HOH   G 4 .   ? -0.656  -8.677  -3.266  1.00 37.97 ? 603 HOH   A O   1 
HETATM 5788 O  O   . HOH   G 4 .   ? 43.550  13.144  5.971   1.00 28.18 ? 604 HOH   A O   1 
HETATM 5789 O  O   . HOH   G 4 .   ? -3.007  -9.614  3.073   1.00 58.14 ? 605 HOH   A O   1 
HETATM 5790 O  O   . HOH   G 4 .   ? 12.335  -22.163 1.679   1.00 45.18 ? 606 HOH   A O   1 
HETATM 5791 O  O   . HOH   G 4 .   ? 37.607  3.905   17.551  1.00 24.24 ? 607 HOH   A O   1 
HETATM 5792 O  O   . HOH   G 4 .   ? 39.646  18.681  15.180  1.00 28.12 ? 608 HOH   A O   1 
HETATM 5793 O  O   . HOH   G 4 .   ? 17.724  12.622  20.053  1.00 22.39 ? 609 HOH   A O   1 
HETATM 5794 O  O   . HOH   G 4 .   ? 20.683  -7.097  24.474  1.00 35.36 ? 610 HOH   A O   1 
HETATM 5795 O  O   . HOH   G 4 .   ? 44.810  16.157  3.983   1.00 32.16 ? 611 HOH   A O   1 
HETATM 5796 O  O   . HOH   G 4 .   ? 41.175  1.818   -4.230  1.00 41.79 ? 612 HOH   A O   1 
HETATM 5797 O  O   . HOH   G 4 .   ? 33.592  8.583   -12.203 1.00 55.25 ? 613 HOH   A O   1 
HETATM 5798 O  O   . HOH   G 4 .   ? 43.032  10.320  6.875   1.00 22.13 ? 614 HOH   A O   1 
HETATM 5799 O  O   . HOH   G 4 .   ? 17.303  10.679  13.898  1.00 19.57 ? 615 HOH   A O   1 
HETATM 5800 O  O   . HOH   G 4 .   ? -3.163  11.741  8.388   1.00 35.06 ? 616 HOH   A O   1 
HETATM 5801 O  O   . HOH   G 4 .   ? 15.494  22.448  -9.469  1.00 31.91 ? 617 HOH   A O   1 
HETATM 5802 O  O   . HOH   G 4 .   ? 17.669  -19.957 2.638   1.00 39.26 ? 618 HOH   A O   1 
HETATM 5803 O  O   . HOH   G 4 .   ? 12.549  11.982  19.634  1.00 18.46 ? 619 HOH   A O   1 
HETATM 5804 O  O   . HOH   G 4 .   ? -5.691  11.669  8.691   1.00 40.58 ? 620 HOH   A O   1 
HETATM 5805 O  O   . HOH   G 4 .   ? 35.184  22.504  10.695  1.00 33.45 ? 621 HOH   A O   1 
HETATM 5806 O  O   . HOH   G 4 .   ? 17.691  9.007   16.471  1.00 19.34 ? 622 HOH   A O   1 
HETATM 5807 O  O   . HOH   G 4 .   ? 20.203  -5.670  21.159  1.00 26.22 ? 623 HOH   A O   1 
HETATM 5808 O  O   . HOH   G 4 .   ? 20.676  -7.365  13.954  1.00 17.26 ? 624 HOH   A O   1 
HETATM 5809 O  O   . HOH   G 4 .   ? 0.661   5.782   -5.138  1.00 31.40 ? 625 HOH   A O   1 
HETATM 5810 O  O   . HOH   G 4 .   ? 20.588  -19.799 5.945   1.00 34.31 ? 626 HOH   A O   1 
HETATM 5811 O  O   . HOH   G 4 .   ? 26.830  2.066   -1.604  1.00 25.39 ? 627 HOH   A O   1 
HETATM 5812 O  O   . HOH   G 4 .   ? 16.866  -12.266 18.850  1.00 42.07 ? 628 HOH   A O   1 
HETATM 5813 O  O   . HOH   G 4 .   ? 33.112  10.476  21.289  1.00 27.63 ? 629 HOH   A O   1 
HETATM 5814 O  O   . HOH   G 4 .   ? 13.756  -10.465 15.749  1.00 24.96 ? 630 HOH   A O   1 
HETATM 5815 O  O   . HOH   G 4 .   ? 14.325  6.282   22.475  1.00 26.40 ? 631 HOH   A O   1 
HETATM 5816 O  O   . HOH   G 4 .   ? 20.698  20.078  2.660   1.00 22.54 ? 632 HOH   A O   1 
HETATM 5817 O  O   . HOH   G 4 .   ? 24.952  0.473   -3.354  1.00 29.07 ? 633 HOH   A O   1 
HETATM 5818 O  O   . HOH   G 4 .   ? 16.619  -1.084  -8.126  1.00 34.72 ? 634 HOH   A O   1 
HETATM 5819 O  O   . HOH   G 4 .   ? 6.205   -27.599 10.115  1.00 48.00 ? 635 HOH   A O   1 
HETATM 5820 O  O   . HOH   G 4 .   ? 11.100  -26.135 5.559   1.00 38.65 ? 636 HOH   A O   1 
HETATM 5821 O  O   . HOH   G 4 .   ? 48.550  24.020  9.207   1.00 42.04 ? 637 HOH   A O   1 
HETATM 5822 O  O   . HOH   G 4 .   ? 31.876  15.090  19.461  1.00 35.16 ? 638 HOH   A O   1 
HETATM 5823 O  O   . HOH   G 4 .   ? 25.107  8.801   -23.350 1.00 37.41 ? 639 HOH   A O   1 
HETATM 5824 O  O   . HOH   G 4 .   ? 28.000  15.240  16.017  1.00 22.13 ? 640 HOH   A O   1 
HETATM 5825 O  O   . HOH   G 4 .   ? 14.272  -8.363  19.057  1.00 38.71 ? 641 HOH   A O   1 
HETATM 5826 O  O   . HOH   G 4 .   ? 4.691   0.530   -5.232  1.00 34.05 ? 642 HOH   A O   1 
HETATM 5827 O  O   . HOH   G 4 .   ? 30.245  16.414  4.789   1.00 24.54 ? 643 HOH   A O   1 
HETATM 5828 O  O   . HOH   G 4 .   ? 7.371   -13.117 13.890  1.00 32.96 ? 644 HOH   A O   1 
HETATM 5829 O  O   . HOH   G 4 .   ? 6.232   -9.456  16.223  1.00 26.73 ? 645 HOH   A O   1 
HETATM 5830 O  O   . HOH   G 4 .   ? -9.375  -13.345 17.145  1.00 46.73 ? 646 HOH   A O   1 
HETATM 5831 O  O   . HOH   G 4 .   ? 26.081  8.790   18.214  1.00 27.63 ? 647 HOH   A O   1 
HETATM 5832 O  O   . HOH   G 4 .   ? 27.773  -15.635 10.634  1.00 24.94 ? 648 HOH   A O   1 
HETATM 5833 O  O   . HOH   G 4 .   ? 29.477  -14.529 13.063  1.00 32.01 ? 649 HOH   A O   1 
HETATM 5834 O  O   . HOH   H 4 .   ? 35.656  10.600  25.551  1.00 21.57 ? 601 HOH   B O   1 
HETATM 5835 O  O   . HOH   H 4 .   ? 56.236  -0.041  37.282  1.00 45.90 ? 602 HOH   B O   1 
HETATM 5836 O  O   . HOH   H 4 .   ? 37.798  -20.259 33.712  1.00 48.74 ? 603 HOH   B O   1 
HETATM 5837 O  O   . HOH   H 4 .   ? 29.301  -18.489 35.719  1.00 34.80 ? 604 HOH   B O   1 
HETATM 5838 O  O   . HOH   H 4 .   ? 34.578  9.439   30.471  1.00 25.66 ? 605 HOH   B O   1 
HETATM 5839 O  O   . HOH   H 4 .   ? 29.570  -9.436  31.632  1.00 20.54 ? 606 HOH   B O   1 
HETATM 5840 O  O   . HOH   H 4 .   ? 10.679  7.616   32.004  1.00 31.04 ? 607 HOH   B O   1 
HETATM 5841 O  O   . HOH   H 4 .   ? 62.570  13.477  27.115  1.00 62.63 ? 608 HOH   B O   1 
HETATM 5842 O  O   . HOH   H 4 .   ? 47.589  6.156   47.486  1.00 35.99 ? 609 HOH   B O   1 
HETATM 5843 O  O   . HOH   H 4 .   ? 15.691  2.792   20.911  1.00 31.21 ? 610 HOH   B O   1 
HETATM 5844 O  O   . HOH   H 4 .   ? 35.135  16.250  32.461  1.00 29.38 ? 611 HOH   B O   1 
HETATM 5845 O  O   . HOH   H 4 .   ? 40.893  -8.781  20.969  1.00 30.13 ? 612 HOH   B O   1 
HETATM 5846 O  O   . HOH   H 4 .   ? 37.442  6.651   24.220  1.00 24.17 ? 613 HOH   B O   1 
HETATM 5847 O  O   . HOH   H 4 .   ? 43.849  22.692  38.571  1.00 37.64 ? 614 HOH   B O   1 
HETATM 5848 O  O   . HOH   H 4 .   ? 26.386  -17.304 33.150  1.00 39.04 ? 615 HOH   B O   1 
HETATM 5849 O  O   . HOH   H 4 .   ? 34.475  11.928  31.695  1.00 22.71 ? 616 HOH   B O   1 
HETATM 5850 O  O   . HOH   H 4 .   ? 27.427  -0.224  39.315  1.00 26.05 ? 617 HOH   B O   1 
HETATM 5851 O  O   . HOH   H 4 .   ? 34.005  -7.163  23.057  1.00 23.66 ? 618 HOH   B O   1 
HETATM 5852 O  O   . HOH   H 4 .   ? 28.751  -2.148  41.222  1.00 24.87 ? 619 HOH   B O   1 
HETATM 5853 O  O   . HOH   H 4 .   ? 9.162   9.825   33.064  1.00 31.86 ? 620 HOH   B O   1 
HETATM 5854 O  O   . HOH   H 4 .   ? 40.341  13.289  19.850  1.00 20.46 ? 621 HOH   B O   1 
HETATM 5855 O  O   . HOH   H 4 .   ? 34.299  -4.696  15.728  1.00 27.10 ? 622 HOH   B O   1 
HETATM 5856 O  O   . HOH   H 4 .   ? 36.996  -12.627 55.082  1.00 54.53 ? 623 HOH   B O   1 
HETATM 5857 O  O   . HOH   H 4 .   ? 44.449  8.009   26.790  1.00 35.91 ? 624 HOH   B O   1 
HETATM 5858 O  O   . HOH   H 4 .   ? 49.599  -0.044  42.923  1.00 37.04 ? 625 HOH   B O   1 
HETATM 5859 O  O   . HOH   H 4 .   ? 35.147  9.503   22.630  1.00 17.44 ? 626 HOH   B O   1 
HETATM 5860 O  O   . HOH   H 4 .   ? 27.136  8.622   20.813  1.00 20.22 ? 627 HOH   B O   1 
HETATM 5861 O  O   . HOH   H 4 .   ? 44.967  7.846   29.337  1.00 27.63 ? 628 HOH   B O   1 
# 
